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- PDB-5uw8: Structure of E. coli MCE protein MlaD, core MCE domain -

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Basic information

Entry
Database: PDB / ID: 5uw8
TitleStructure of E. coli MCE protein MlaD, core MCE domain
ComponentsProbable phospholipid ABC transporter-binding protein MlaD
KeywordsTRANSPORT PROTEIN / MCE protein / bacterial lipid transport
Function/homologyProbable phospholipid ABC transporter-binding protein MlaD / Mce/MlaD / MlaD protein / phospholipid transport / integral component of membrane / plasma membrane / Probable phospholipid ABC transporter-binding protein MlaD
Function and homology information
Specimen sourceEscherichia coli o157:h7 / / bacteria / image: Escherichia coli
MethodX-ray diffraction (2.15 Å resolution / MAD) / X-ray crystallography
AuthorsBhabha, G. / Ekiert, D.C.
CitationJournal: Cell / Year: 2017
Title: Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.
Authors: Damian C Ekiert / Gira Bhabha / Georgia L Isom / Garrett Greenan / Sergey Ovchinnikov / Ian R Henderson / Jeffery S Cox / Ronald D Vale
Abstract: How phospholipids are trafficked between the bacterial inner and outer membranes through the hydrophilic space of the periplasm is not known. We report that members of the mammalian cell entry (MCE) ...How phospholipids are trafficked between the bacterial inner and outer membranes through the hydrophilic space of the periplasm is not known. We report that members of the mammalian cell entry (MCE) protein family form hexameric assemblies with a central channel capable of mediating lipid transport. The E. coli MCE protein, MlaD, forms a ring associated with an ABC transporter complex in the inner membrane. A soluble lipid-binding protein, MlaC, ferries lipids between MlaD and an outer membrane protein complex. In contrast, EM structures of two other E. coli MCE proteins show that YebT forms an elongated tube consisting of seven stacked MCE rings, and PqiB adopts a syringe-like architecture. Both YebT and PqiB create channels of sufficient length to span the periplasmic space. This work reveals diverse architectures of highly conserved protein-based channels implicated in the transport of lipids between the membranes of bacteria and some eukaryotic organelles.
Copyright: 2017 Elsevier Inc. All rights reserved.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Feb 20, 2017 / Release: Apr 12, 2017
RevisionDateData content typeGroupCategoryItemProviderType
1.0Apr 12, 2017Structure modelrepositoryInitial release
1.1Apr 19, 2017Structure modelDatabase references
1.2Sep 27, 2017Structure modelAuthor supporting evidencepdbx_audit_support_pdbx_audit_support.funding_organization

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Structure visualization

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Assembly

Deposited unit
A: Probable phospholipid ABC transporter-binding protein MlaD
B: Probable phospholipid ABC transporter-binding protein MlaD
C: Probable phospholipid ABC transporter-binding protein MlaD
D: Probable phospholipid ABC transporter-binding protein MlaD
E: Probable phospholipid ABC transporter-binding protein MlaD
F: Probable phospholipid ABC transporter-binding protein MlaD
G: Probable phospholipid ABC transporter-binding protein MlaD


Theoretical massNumber of molelcules
Total (without water)94,9497
Polyers94,9497
Non-polymers00
Water2,252125
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)139.660, 103.820, 77.210
Angle α, β, γ (deg.)90.00, 111.03, 90.00
Int Tables number5
Space group name H-MC 1 2 1
DetailsAS PER THE AUTHORS THERE IS SOME AMBIGUITY AS TO WHETHER THIS PROTEIN FORMS A HEPTAMER OR A TETRADECAMER.

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Components

#1: Protein/peptide
Probable phospholipid ABC transporter-binding protein MlaD


Mass: 13564.138 Da / Num. of mol.: 7 / Fragment: UNP residues 32-140
Source: (gene. exp.) Escherichia coli o157:h7 / / bacteria / image: Escherichia coli
Gene: mlaD, Z4556, ECs4072 / Production host: Escherichia coli / References: UniProt:P64605
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 125 / Formula: H2O / : Water

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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: 2.75 / Density percent sol: 55.29
Crystal growTemp: 295 K / Method: VAPOR DIFFUSION, SITTING DROP
Details: 0.1 M sodium acetate pH 4.5, and 40% 1,2 propanediol

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Data collection

DiffractionMean temperature: 100 kelvins
SourceSource: SYNCHROTRON / Type: ALS BEAMLINE 8.3.1 / Synchrotron site: ALS / Beamline: 8.3.1 / Wavelength: 1.116
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Collection date: Jan 16, 2015
RadiationDiffraction protocol: SINGLE WAVELENGTH / Monochromatic or laue m l: M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.116 Å / Relative weight: 1
ReflectionD resolution high: 2.15 Å / D resolution low: 50 Å / Number obs: 55590 / CC half: 0.46 / NetI over sigmaI: 15.4 / Redundancy: 7.6 / Percent possible obs: 99.3

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefineMethod to determine structure: MAD / Overall SU ML: 0.34 / Cross valid method: FREE R-VALUE / Sigma F: 0 / Overall phase error: 30.06
Solvent computationSolvent shrinkage radii: 0.9 Å / Solvent vdw probe radii: 1.11 Å
Least-squares processR factor R free: 0.2436 / R factor R work: 0.2039 / R factor obs: 0.2053 / Highest resolution: 2.15 Å / Lowest resolution: 42.12 Å / Number reflection R free: 1810 / Number reflection obs: 49929 / Percent reflection R free: 3.63 / Percent reflection obs: 89.29
Refine hist #LASTHighest resolution: 2.15 Å / Lowest resolution: 42.12 Å
Number of atoms included #LASTProtein: 5502 / Nucleic acid: 0 / Ligand: 0 / Solvent: 125 / Total: 5627
Refine LS restraints
Refine IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0045703
X-RAY DIFFRACTIONf_angle_d0.9397789
X-RAY DIFFRACTIONf_dihedral_angle_d10.8772114
X-RAY DIFFRACTIONf_chiral_restr0.034935
X-RAY DIFFRACTIONf_plane_restr0.0041016
Refine LS shell

Refine ID: X-RAY DIFFRACTION

Highest resolutionR factor R freeR factor R workLowest resolutionNumber reflection R freeNumber reflection R workPercent reflection obs
2.14990.40880.36902.2081113292871.00
2.20810.41750.34332.2730119314276.00
2.27300.35650.31532.3464124324179.00
2.34640.33430.29902.4303125332281.00
2.43030.29920.27642.5276130350084.00
2.52760.32310.25872.6426141363888.00
2.64260.26380.23902.7819139377692.00
2.78190.25980.21822.9561148394295.00
2.95610.22620.21263.1843149400997.00
3.18430.26780.20273.5046155411298.00
3.50460.22560.18914.0114152410699.00
4.01140.20330.15225.05261564173100.00
5.05260.20450.179242.12851594230100.00
Refine TLS

Method: refined / Refine ID: X-RAY DIFFRACTION

IDL11L12L13L22L23L33S11S12S13S21S22S23S31S32S33T11T12T13T22T23T33Origin xOrigin yOrigin z
10.7903-0.18060.92452.5936-0.01700.4946-0.08360.1816-0.0652-0.2456-0.0495-0.05880.33750.16790.00010.37180.00240.04720.4944-0.03750.452213.809150.124335.0690
22.8601-2.11031.50781.4759-1.10491.35170.42010.44340.03720.0140-0.33270.03150.0573-0.0521-0.00020.39540.05970.11670.4978-0.02640.332613.672554.035634.8424
32.3213-2.2600-0.10993.4887-1.25241.44840.0684-0.0180-0.3433-0.08210.1962-0.38370.32960.07510.19560.3257-0.02870.10650.4034-0.01410.391315.169447.682140.4038
41.36751.25621.30401.14770.98512.1222-1.0532-0.72211.6300-0.31160.18840.1547-0.6993-1.9450-0.08420.46140.1070-0.02990.5575-0.08320.49665.889155.685541.1567
50.25560.12540.30150.52580.42280.5016-0.71401.36130.9470-1.11271.20510.3817-2.31831.7493-0.03041.38250.25030.02421.22190.03800.88652.808763.784528.8647
63.1558-2.9710-0.41131.9680-0.11160.10301.0206-0.24540.7389-1.25460.36562.2412-1.2762-1.20345.19960.22860.11910.26730.47690.07350.29748.303157.163739.0198
71.10070.33670.00810.3278-0.07840.0348-0.3666-0.0662-1.38020.94960.4340-0.1364-0.15970.54080.00600.71170.08000.04700.62730.03390.528916.999454.471259.0403
80.58160.7845-0.53201.8925-0.31160.5153-0.0990-0.1488-0.81260.49500.02220.28760.2814-0.4847-0.00220.5308-0.00660.03050.6123-0.01070.556113.374747.777545.5107
92.5583-0.13991.74941.56860.57393.38210.64650.9241-1.4496-0.00190.22100.21580.8380-0.11831.31480.53140.1212-0.20650.7740-0.09420.7384-7.306538.898921.7359
100.9797-0.46561.39152.5653-1.66662.5600-0.04810.7850-1.4351-0.36770.8172-0.1653-0.1448-0.51630.51450.75750.0886-0.06920.8889-0.06260.6118-6.762339.073419.0647
111.9113-0.2839-0.08074.2060-2.29551.31081.47640.1788-1.14340.5695-1.4675-0.93650.6213-0.2735-0.13070.56840.1869-0.27990.7997-0.07881.1214-24.694133.651617.5130
129.2020-0.1001-1.63000.6002-1.00412.3866-0.16860.8994-0.1748-0.35800.6114-0.58130.1015-0.05450.39680.61330.0825-0.17740.5932-0.27521.0436-7.986234.793720.4304
134.6681-1.71242.16172.02681.67935.48200.6775-0.7398-1.03100.23230.3451-1.17550.9996-0.41992.57420.5436-0.0274-0.36920.57590.05261.1096-3.994035.391429.9229
140.0012-0.00100.04000.0353-0.06600.0754-0.11083.18221.2753-1.72281.03691.42441.10170.5068-0.00261.16480.0251-0.02010.89410.12471.4103-5.008755.670122.3207
150.63380.2726-0.83530.3351-0.36101.23710.3216-0.1327-0.00680.45370.78131.0533-1.3591-0.28400.10690.53570.0849-0.04920.53970.04680.4849-7.084743.689027.7527
161.85060.04311.98612.48941.03682.58561.1767-1.0866-1.37300.3226-0.05960.11281.0260-1.15450.17400.9513-0.1827-0.43120.74640.10901.0315-9.404731.230531.7196
171.9294-0.24931.65941.8519-0.89901.61110.30400.6377-0.6123-0.1798-0.0671-0.58080.70490.5331-0.06900.53930.0802-0.01960.5154-0.11720.5028-29.738643.66421.9768
183.1656-1.5269-1.09351.9720-0.86861.46830.0680-0.36870.10501.1930-0.2852-0.5256-1.00050.2240-0.14610.4610-0.0706-0.06500.5216-0.04210.5758-25.951354.753910.1648
190.96420.7966-0.29451.40400.80451.60120.23260.0994-0.3294-0.43150.26170.2249-0.7353-0.12690.04460.49370.00990.06330.45240.02520.6433-26.169651.62905.2392
203.95300.51710.30840.2396-0.17162.7094-0.07550.3212-0.5971-0.0061-0.07620.7947-0.6680-0.25600.00310.55390.0770-0.01610.3855-0.08020.2756-35.167454.10973.6669
212.0457-0.89021.74133.1894-3.41135.67810.1316-0.4001-0.43530.6115-0.0658-1.30830.35530.4930-0.03430.47180.0235-0.08350.4970-0.10870.4578-27.320146.348413.4794
220.18250.00240.03919.4847-9.42709.4577-0.03861.7043-0.6480-1.2980-0.71210.34143.33870.3639-0.69990.9628-0.1473-0.11220.6026-0.15620.7901-35.995936.855520.6985
230.2382-0.05840.40840.36990.39291.3603-0.3620-0.12780.7558-1.94550.5092-0.1529-1.2106-0.98030.03280.9175-0.3993-0.08121.2161-0.01421.0204-41.495031.864118.8387
241.6437-1.2586-0.55841.1575-0.40781.89590.1860-0.2302-0.31740.23140.0984-0.05640.4373-1.22140.25760.58830.0150-0.04670.5924-0.02690.3187-36.004246.050210.4972
253.03131.7949-0.04092.61041.94371.59620.26580.53930.4207-1.59090.44520.7887-0.5607-0.63611.17190.95080.0537-0.09050.44420.02470.3757-37.141977.3480-3.0249
260.10290.1438-0.67130.5815-0.30331.52680.21890.2193-0.12390.4220-0.3630-0.6891-0.0597-0.00630.00010.58610.07740.06140.44470.10140.4462-29.887177.87707.7076
270.9971-0.94650.82710.8261-0.3604-0.26650.10160.3747-0.0741-0.0942-0.6245-0.20590.12850.0906-0.00030.69060.06890.12170.48840.06990.4712-33.364085.05294.1580
284.67671.32060.88010.55170.11010.3730-0.44820.54490.2767-1.36190.30841.09520.10620.9931-0.32610.91010.0602-0.02160.51210.08620.3906-34.810779.98450.6284
291.2522-2.6902-0.20879.56691.74810.5666-0.0042-0.0315-1.5054-0.6403-0.56372.82880.8594-0.8913-1.22700.80720.1003-0.16310.4125-0.00060.3279-42.006869.0672-1.1737
306.77933.65711.07622.00180.57260.14731.1900-0.9627-0.87171.2927-0.9081-0.3177-0.01620.35630.07920.87930.02030.04910.46660.10090.4280-33.790774.715212.8918
310.9648-0.13390.02690.0884-0.03890.1077-0.24830.0653-0.36840.05080.0329-1.30620.6483-1.29860.00440.93590.0479-0.02040.88490.08081.0062-20.287371.755213.5005
320.2585-0.1772-0.37960.59740.28990.39440.0851-1.21770.09380.3398-0.5172-0.7188-0.3978-0.1430-0.00120.68120.01740.07090.51750.02360.5379-32.872973.27109.8669
33-0.0081-0.2245-0.10284.05601.71430.72230.7002-0.05560.6765-0.2440-0.64911.65051.8739-1.8823-0.60970.5673-0.1692-0.19301.1157-0.06130.9057-51.792268.61985.5886
340.83370.5692-0.62174.2608-1.26690.60710.44140.16060.29710.4865-0.25250.4213-0.3549-0.0007-0.02680.59360.0734-0.06660.48610.04610.5381-42.182279.18325.5071
352.7439-0.13291.25417.28586.27626.13631.08610.4152-0.4047-1.06740.3307-1.6144-0.61780.53401.32980.6680-0.0439-0.07020.56350.13370.5652-23.6467104.02786.3670
360.7677-0.32901.22461.2894-0.40091.36030.1395-0.1834-0.2625-0.1305-0.3010-0.62370.29030.3075-0.09780.4507-0.0132-0.00220.58880.16950.3951-17.907598.538314.9106
370.78930.32921.20721.88060.85740.9064-0.06210.2001-0.5113-0.41060.3482-0.7626-0.30000.29390.06680.4952-0.0119-0.03370.56270.12260.4748-16.8361108.374118.0622
380.39770.29020.36810.10170.38240.13860.16150.07620.3240-0.4044-0.62370.8494-1.2775-0.6545-0.64170.4725-0.01260.02050.51390.10070.4159-32.8900102.84749.8967
390.4096-0.58541.09642.3446-0.86053.23000.6214-2.5600-1.50430.1166-0.2003-0.39850.49850.47440.51100.6783-0.0919-0.08330.69800.29280.6668-23.348094.579520.7586
406.67563.50073.16666.12317.68951.9692-0.01251.01120.4360-0.95822.3401-0.0516-3.02402.38240.79621.07210.34660.24810.87500.03851.0594-14.503184.465616.4351
410.25230.12580.35361.82070.94351.12130.2744-0.8672-0.8445-0.1228-0.4025-0.36990.46150.6131-0.74030.59940.0495-0.07970.71890.23790.4590-23.362094.465317.4414
424.9662-1.66732.12981.99674.07253.32430.05970.83231.1756-0.57620.8653-0.6355-1.3897-0.53703.74010.63050.21000.17730.51120.33870.6309-42.7971104.358219.1415
431.48570.27781.70250.85051.24594.0084-0.0753-0.85710.31060.5109-0.00190.0225-1.4119-0.1156-0.00800.5148-0.0616-0.03980.55560.04900.6562-27.6473106.388318.0516
443.8588-0.22520.39641.6961-0.11671.3508-0.36350.85070.4533-0.35970.0916-0.33270.17750.5725-0.13480.4620-0.0246-0.06960.61980.12940.54514.6573100.039131.2998
451.12971.9358-0.30604.49030.51590.8590-0.23150.1851-0.2397-0.22000.14360.06840.1196-0.0169-0.00030.4076-0.05500.10420.61960.03360.26181.3858100.424027.2734
460.1850-0.1623-0.19020.12170.14200.1606-0.19840.45250.57921.7076-0.2190-0.8374-1.49690.7905-0.09990.7400-0.0049-0.21090.62600.24420.780813.803698.170243.7055
475.23860.21281.21414.3623-0.50430.7584-1.44420.51801.73720.11190.4606-0.7300-1.04290.1534-0.28090.6759-0.1175-0.18400.66050.19780.8554-0.0288109.200229.8514
483.5233-2.68170.01801.98390.08337.8551-0.6923-0.6067-1.52250.33721.23791.76432.0477-1.87621.57940.5365-0.1167-0.01220.62710.13710.6795-5.508996.040432.7192
492.06091.1215-0.26702.6854-1.02523.8471-0.52820.4665-1.30760.26990.58250.25251.4297-0.0005-0.18080.5553-0.08170.00700.5677-0.02440.6458-5.397494.470528.4538
503.2876-2.8044-0.49852.81171.30451.2175-1.03680.57651.08141.9189-1.3785-1.1964-1.66301.7098-6.05562.13910.1342-0.73460.66600.01051.1851-11.4092117.025939.3565
514.66811.0130-4.84540.2575-0.88126.94190.4038-1.58292.48030.7360-0.91070.1333-1.36771.3004-0.58690.7193-0.0320-0.32560.52310.00751.13102.3300112.239035.8616
521.13600.6030-0.12061.30700.55310.36370.7268-1.4035-0.2790-1.9826-0.10740.17180.2276-2.05330.03850.72360.0495-0.04100.76070.21020.7215-2.964597.773640.1995
531.0108-0.91430.10233.16711.56961.4241-0.21750.2337-0.2273-0.4538-0.03290.2865-0.09660.0968-0.00100.3917-0.07090.02260.39370.05160.502417.420279.326737.1519
542.7119-0.19882.23461.70010.47451.9069-0.32390.01440.27900.42840.1153-0.4393-0.36840.1307-0.01050.3625-0.02380.13630.39630.01590.377020.476979.771444.0132
557.67692.77740.25251.07020.36830.6735-0.6618-0.3804-0.69610.45760.07182.13101.0824-0.8582-0.15100.5149-0.01950.06620.51130.04880.93407.632379.397743.0522
560.4896-0.30110.21360.74740.05260.28660.18390.0394-0.3682-0.0045-0.59061.0987-0.0548-0.8383-0.05240.43940.0336-0.02180.6128-0.06160.76736.371980.462737.1378
577.33042.9964-1.94295.96120.21747.14980.1288-1.5620-0.06430.3992-0.76321.1734-1.00952.1049-1.49710.8142-0.17320.49500.8259-0.06901.127717.238293.145857.0144
581.82610.3205-1.65571.1882-0.96411.9075-0.6069-1.4271-0.47530.36090.10410.51230.52070.1757-0.18740.4158-0.00180.12230.49070.04520.557518.792481.822749.7062
Refine TLS group
IDRefine IDRefine TLS IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 36 through 56 )
2X-RAY DIFFRACTION2chain 'A' and (resid 57 through 73 )
3X-RAY DIFFRACTION3chain 'A' and (resid 74 through 97 )
4X-RAY DIFFRACTION4chain 'A' and (resid 98 through 103 )
5X-RAY DIFFRACTION5chain 'A' and (resid 104 through 109 )
6X-RAY DIFFRACTION6chain 'A' and (resid 110 through 115 )
7X-RAY DIFFRACTION7chain 'A' and (resid 116 through 125 )
8X-RAY DIFFRACTION8chain 'A' and (resid 126 through 140 )
9X-RAY DIFFRACTION9chain 'B' and (resid 37 through 62 )
10X-RAY DIFFRACTION10chain 'B' and (resid 63 through 73 )
11X-RAY DIFFRACTION11chain 'B' and (resid 74 through 79 )
12X-RAY DIFFRACTION12chain 'B' and (resid 80 through 87 )
13X-RAY DIFFRACTION13chain 'B' and (resid 88 through 103 )
14X-RAY DIFFRACTION14chain 'B' and (resid 104 through 109 )
15X-RAY DIFFRACTION15chain 'B' and (resid 110 through 115 )
16X-RAY DIFFRACTION16chain 'B' and (resid 116 through 139 )
17X-RAY DIFFRACTION17chain 'C' and (resid 36 through 45 )
18X-RAY DIFFRACTION18chain 'C' and (resid 46 through 62 )
19X-RAY DIFFRACTION19chain 'C' and (resid 63 through 73 )
20X-RAY DIFFRACTION20chain 'C' and (resid 74 through 87 )
21X-RAY DIFFRACTION21chain 'C' and (resid 88 through 115 )
22X-RAY DIFFRACTION22chain 'C' and (resid 116 through 120 )
23X-RAY DIFFRACTION23chain 'C' and (resid 121 through 125 )
24X-RAY DIFFRACTION24chain 'C' and (resid 126 through 140 )
25X-RAY DIFFRACTION25chain 'D' and (resid 37 through 45 )
26X-RAY DIFFRACTION26chain 'D' and (resid 46 through 62 )
27X-RAY DIFFRACTION27chain 'D' and (resid 63 through 79 )
28X-RAY DIFFRACTION28chain 'D' and (resid 80 through 87 )
29X-RAY DIFFRACTION29chain 'D' and (resid 88 through 97 )
30X-RAY DIFFRACTION30chain 'D' and (resid 98 through 103 )
31X-RAY DIFFRACTION31chain 'D' and (resid 104 through 109 )
32X-RAY DIFFRACTION32chain 'D' and (resid 110 through 115 )
33X-RAY DIFFRACTION33chain 'D' and (resid 116 through 127 )
34X-RAY DIFFRACTION34chain 'D' and (resid 128 through 140 )
35X-RAY DIFFRACTION35chain 'E' and (resid 35 through 45 )
36X-RAY DIFFRACTION36chain 'E' and (resid 46 through 73 )
37X-RAY DIFFRACTION37chain 'E' and (resid 74 through 87 )
38X-RAY DIFFRACTION38chain 'E' and (resid 88 through 97 )
39X-RAY DIFFRACTION39chain 'E' and (resid 98 through 103 )
40X-RAY DIFFRACTION40chain 'E' and (resid 104 through 109 )
41X-RAY DIFFRACTION41chain 'E' and (resid 110 through 115 )
42X-RAY DIFFRACTION42chain 'E' and (resid 116 through 125 )
43X-RAY DIFFRACTION43chain 'E' and (resid 126 through 140 )
44X-RAY DIFFRACTION44chain 'F' and (resid 38 through 56 )
45X-RAY DIFFRACTION45chain 'F' and (resid 57 through 73 )
46X-RAY DIFFRACTION46chain 'F' and (resid 74 through 79 )
47X-RAY DIFFRACTION47chain 'F' and (resid 80 through 97 )
48X-RAY DIFFRACTION48chain 'F' and (resid 98 through 104 )
49X-RAY DIFFRACTION49chain 'F' and (resid 105 through 115 )
50X-RAY DIFFRACTION50chain 'F' and (resid 116 through 125 )
51X-RAY DIFFRACTION51chain 'F' and (resid 126 through 135 )
52X-RAY DIFFRACTION52chain 'F' and (resid 136 through 140 )
53X-RAY DIFFRACTION53chain 'G' and (resid 35 through 73 )
54X-RAY DIFFRACTION54chain 'G' and (resid 74 through 97 )
55X-RAY DIFFRACTION55chain 'G' and (resid 98 through 103 )
56X-RAY DIFFRACTION56chain 'G' and (resid 104 through 115 )
57X-RAY DIFFRACTION57chain 'G' and (resid 116 through 123 )
58X-RAY DIFFRACTION58chain 'G' and (resid 124 through 140 )

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Jul 12, 2017. Major update of PDB

Major update of PDB

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Yorodumi

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Related info.: Yorodumi (legacy version) / EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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