[English] 日本語
Yorodumi
- PDB-5ntu: Crystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5ntu
TitleCrystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution
ComponentsGrowth/differentiation factor 8
KeywordsSIGNALING PROTEIN / growth factor / signalling protein / TGFbeta family / cystine knot
Function / homology
Function and homology information


negative regulation of muscle hypertrophy / negative regulation of skeletal muscle tissue growth / negative regulation of myoblast proliferation / skeletal muscle satellite cell differentiation / myoblast migration involved in skeletal muscle regeneration / negative regulation of skeletal muscle satellite cell proliferation / negative regulation of satellite cell differentiation / skeletal muscle atrophy / ovulation cycle process / FOXO-mediated transcription of cell cycle genes ...negative regulation of muscle hypertrophy / negative regulation of skeletal muscle tissue growth / negative regulation of myoblast proliferation / skeletal muscle satellite cell differentiation / myoblast migration involved in skeletal muscle regeneration / negative regulation of skeletal muscle satellite cell proliferation / negative regulation of satellite cell differentiation / skeletal muscle atrophy / ovulation cycle process / FOXO-mediated transcription of cell cycle genes / response to gravity / negative regulation of myoblast differentiation / response to muscle activity / muscle organ development / muscle cell cellular homeostasis / positive regulation of macrophage chemotaxis / response to testosterone / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of lamellipodium assembly / response to electrical stimulus / negative regulation of insulin receptor signaling pathway / cellular response to dexamethasone stimulus / transforming growth factor beta receptor signaling pathway / cytokine activity / growth factor activity / response to estrogen / heparin binding / cellular response to hypoxia / response to ethanol / signaling receptor binding / positive regulation of DNA-templated transcription / protein homodimerization activity / extracellular space / identical protein binding
Similarity search - Function
TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Cystine-knot cytokine
Similarity search - Domain/homology
Growth/differentiation factor 8
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.58 Å
AuthorsCotton, T.R. / Fischer, G. / Hyvonen, M.
CitationJournal: EMBO J. / Year: 2018
Title: Structure of the human myostatin precursor and determinants of growth factor latency.
Authors: Cotton, T.R. / Fischer, G. / Wang, X. / McCoy, J.C. / Czepnik, M. / Thompson, T.B. / Hyvonen, M.
History
DepositionApr 28, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 17, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2018Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Feb 21, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Growth/differentiation factor 8
B: Growth/differentiation factor 8
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,13725
Polymers75,7632
Non-polymers1,37423
Water54030
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, SEC-MALLS confirms disulphide linked dimer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10380 Å2
ΔGint6 kcal/mol
Surface area30520 Å2
MethodPISA
Unit cell
Length a, b, c (Å)168.157, 36.301, 120.448
Angle α, β, γ (deg.)90.000, 104.390, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-510-

HOH

-
Components

#1: Protein Growth/differentiation factor 8 / GDF-8 / Myostatin


Mass: 37881.328 Da / Num. of mol.: 2 / Fragment: Pro-Myostatin Precursor / Mutation: G319A, K320A, K217A, Q218A, E220A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MSTN, GDF8 / Plasmid: pHAT2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O14793
#2: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#3: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 21 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 30 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.35 Å3/Da / Density % sol: 47.66 %
Crystal growTemperature: 292 K / Method: vapor diffusion / pH: 7
Details: 10% PEG6000, 0.1M HEPES: cryo-protection: 70% ethylene glycol

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 16, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.575→76.264 Å / Num. obs: 22474 / % possible obs: 97.7 % / Redundancy: 4 % / Biso Wilson estimate: 95.66 Å2 / CC1/2: 0.997 / Rpim(I) all: 0.034 / Rrim(I) all: 0.071 / Net I/σ(I): 11.7 / Num. measured all: 90386
Reflection shell
Resolution (Å)Redundancy (%)CC1/2Rpim(I) allRrim(I) allDiffraction-ID% possible all
2.575-2.624.20.5830.4931.037199.6
6.989-76.2643.60.9970.0220.046199.1

-
Processing

Software
NameVersionClassification
Aimlessdata scaling
BUSTER2.10.3refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.58→28.27 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.917 / Rfactor Rfree error: 0 / SU R Cruickshank DPI: 0.576 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.554 / SU Rfree Blow DPI: 0.297 / SU Rfree Cruickshank DPI: 0.303
RfactorNum. reflection% reflectionSelection details
Rfree0.26 1118 5.01 %RANDOM
Rwork0.215 ---
obs0.217 22310 97.7 %-
Displacement parametersBiso max: 201.34 Å2 / Biso mean: 100.2 Å2 / Biso min: 46.99 Å2
Baniso -1Baniso -2Baniso -3
1--2.6578 Å20 Å20.5284 Å2
2---2.5218 Å20 Å2
3---5.1796 Å2
Refine analyzeLuzzati coordinate error obs: 0.36 Å
Refinement stepCycle: final / Resolution: 2.58→28.27 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4399 0 86 30 4515
Biso mean--91.21 76.07 -
Num. residues----581
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d1488SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes98HARMONIC2
X-RAY DIFFRACTIONt_gen_planes651HARMONIC5
X-RAY DIFFRACTIONt_it4579HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion634SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact4752SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d4579HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg6207HARMONIC60.55
X-RAY DIFFRACTIONt_omega_torsion3.34
X-RAY DIFFRACTIONt_other_torsion20.72
LS refinement shellResolution: 2.58→2.71 Å / Total num. of bins used: 11
RfactorNum. reflection% reflection
Rfree0.264 137 4.6 %
Rwork0.215 2843 -
all-2980 -
obs--99.87 %
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)
10.8039-4.5203-1.46354.7513-4.434-0.80390.0343-0.1657-0.04530.1974-0.11350.10090.1302-0.250.07930.35650.1638-0.00550.2738-0.2799-0.1498-35.7648-13.4213.3769
2-0.4374-0.32971.41261.2073-5.55671.95830.02260.38770.3302-0.12350.02470.5099-0.2486-0.2902-0.04730.14340.4040.12450.5495-0.02230.0863-31.2581-7.8145-2.3201
35.32415.698-1.0480.98383.25058.91080.0062-0.0927-0.0776-0.0252-0.02660.02260.0769-0.25950.02040.1411-0.06850.03490.2651-0.012-0.0855-22.3817-19.5425-10.6306
41.65212.5634-2.90246.0308-0.6240.45690.0348-0.09740.07680.1358-0.0542-0.2156-0.01660.05270.01940.3512-0.16310.14670.1788-0.29410.0061-19.1176-26.9599.4713
59.7542-1.02984.36024.78880.72892.50880.05820.0825-0.273-0.3469-0.2212-0.01620.38310.00410.163-0.16180.11510.133-0.11340.0185-0.1488-3.1595-29.393842.3165
63.2469-4.6174.477811.3265-1.29118.85860.1446-0.4378-0.8089-0.2793-0.11210.60660.5725-0.0767-0.0324-0.1550.10430.06220.00170.1098-0.06314.9426-34.909139.1793
76.8548-1.51051.20152.4963-0.40451.49110.1012-0.66340.36840.3725-0.1495-0.52090.11180.96670.0483-0.2651-0.0579-0.01180.41830.0810.095518.996-25.363855.1843
8-0.99342.97472.24021.53432.26694.4948-0.06170.0312-0.1751-0.0180.1206-0.27620.23750.1667-0.05890.18340.43230.20.14060.14490.461519.3769-47.002145.0487
91.65263.48973.22424.1886-3.23395.37550.1683-0.49720.49330.1341-0.436-0.1552-0.35470.7120.2677-0.4248-0.0210.04240.47690.00670.203122.5977-23.763152.2465
105.93632.4061.568702.59517.6214-0.0336-0.2736-0.4132-0.2517-0.2906-0.71270.95550.38060.3242-0.28080.17080.1197-0.00780.1855-0.0511.3894-33.586441.7498
111.31674.88720.88667.1771-0.98240.36830.0821-0.46080.00360.4919-0.1856-0.4738-0.11170.63990.1034-0.13380.1355-0.10740.4858-0.01930.156720.7897-32.378356.7033
121.32731.35547.08170-4.70018.7699-0.0378-0.1708-0.1340.1988-0.3149-0.0820.49720.250.3528-0.2599-0.01530.02160.1733-0.0588-0.067910.7243-28.869461.468
132.1209-0.4635-3.4514.56136.505-1.80960.15780.0229-0.3797-0.0125-0.2834-0.48970.1857-0.03360.1256-0.3288-0.01040.0470.01540.0122-0.11796.9025-27.388849.7512
14-2.80256.13715.00050.0265.71383.71670.01790.3231-0.0665-0.44570.01360.22880.0407-0.3685-0.03150.11020.1363-0.10210.44520.04810.3001-10.5652-30.564127.3811
15-0.6018-4.35631.15691.65225.96020.6568-0.03090.2147-0.3458-0.33470.11430.29920.3913-0.3019-0.08340.2878-0.3266-0.03740.0491-0.22390.3537-38.8332-31.543423.0905
162.29830.17420.98331.35372.58.22180.17210.5310.1688-0.162-0.1920.08840.2067-0.54980.0199-0.1773-0.0084-0.14890.6411-0.1936-0.2033-35.391-18.27914.2656
171.6664-2.48820.35520-0.73432.8137-0.23230.4875-0.3326-0.16040.58610.01670.20820.1464-0.35380.0445-0.3158-0.21710.1332-0.1427-0.0678-35.1119-23.951520.0743
180.39562.1024-1.41393.8583-1.80047.4154-0.1427-0.18230.1792-0.22180.22290.66370.1059-0.9208-0.0802-0.10380.0407-0.0549-0.0929-0.09540.0482-31.898-26.835142.3751
192.99480.4547-3.103801.01496.97740.26551.0743-0.0744-0.2791-0.1227-0.3046-0.3491-0.3043-0.14280.11170.08590.08560.4391-0.1719-0.0141-24.5805-14.53134.2367
204.4624-1.8357-1.80540.2360.86367.6520.02860.6038-0.144-0.1524-0.11270.05620.02060.32780.0841-0.0138-0.0532-0.04160.0564-0.1938-0.0248-24.9344-19.621713.245
210.84552.27162.82475.2673-2.72561.83990.09810.01620.02550.0424-0.13080.86470.2025-0.77790.0328-0.16960.0123-0.03020.0127-0.02830.0192-29.8938-15.679742.5314
222.2336-3.2518-1.849400.26921.94710.37940.0034-0.5743-0.1444-0.14060.26320.20430.3014-0.23870.00570.02060.0235-0.08870.0339-0.0715-14.5939-28.516645.6696
233.45570.1943-1.60531.22270.9632-1.0512-0.0432-0.56380.44420.1338-0.1397-0.6014-0.14960.47980.1828-0.15080.02120.00050.0999-0.0353-0.03990.0962-23.058555.3643
24-1.16331.65332.117700.72011.1633-0.00970.23680.57670.12160.2001-0.1148-0.4844-0.0827-0.19030.0186-0.08160.06480.060.01850.177-1.214-12.492744.7694
251.38210.5178-2.74454.85384.01450.39760.15220.06690.22390.7887-0.46030.0737-0.09220.21390.30810.2152-0.00010.07720.4166-0.1066-0.0755-18.7533-9.30123.274
264.70260.64491.45564.39054.16853.34270.0332-0.32250.1041-0.0072-0.0485-0.1139-0.25710.06370.01530.43010.28620.1960.272-0.07640.2045-14.5593-0.6961-8.1513
271.14130.5633-0.84390-1.03540.23250.0327-0.0709-0.03510.07580.001-0.0383-0.0130.0125-0.0336-0.1511-0.0676-0.0660.50530.0089-0.1647-8.1701-11.9434-5.5959
281.8592-1.37360.47091.20580.64776.55380.009-0.0965-0.00440.04770.05940.0066-0.6673-0.5506-0.0685-0.1012-0.07460.1282-0.2128-0.0655-0.0822-14.3303-14.0733-27.3399
290.42741.1258-0.63752.20150.62261.38490.0027-0.0109-0.0171-0.0277-0.02460.0525-0.03150.00560.02190.5323-0.1383-0.01930.2136-0.30730.3893-6.57463.8018-19.5976
302.7311-0.7254-2.09621.99760.56088.2519-0.0916-0.31690.12240.06890.0866-0.03570.1141-0.20860.0049-0.0381-0.00920.1331-0.2424-0.07820.0889-10.2471-16.6197-27.3728
315.88841.3206-3.36080-1.30942.11480.0937-0.194-0.14970.0347-0.1539-0.3443-0.14060.53170.0602-0.03880.09550.14730.06920.21270.0137-10.1375-12.8981-16.0283
320.8303-4.2403-1.061.39642.94441.01110.01890.12740.0752-0.024-0.0739-0.0412-0.1198-0.10590.0550.2651-0.1151-0.04450.4363-0.45590.213-7.17880.4744-7.1903
3311.0936-0.9795-3.13698.1638-1.31252.131-0.06970.04970.3528-0.21630.07340.2169-0.4854-0.6147-0.00370.2928-0.00140.107-0.0354-0.04930.0212-17.3327-8.592-28.7666
341.1995-0.5064-0.53750.35070.39090.57570.0151-0.07540.03130.10920.00310.0593-0.0776-0.0569-0.0182-0.17620.11220.27450.3311-0.13530.0618-26.4823-12.743-20.2755
350.1229-0.22062.76214.32660.33382.52740.0227-0.6266-0.00020.43440.062-0.2274-0.16350.0941-0.0847-0.09140.03150.16760.3598-0.0424-0.1798-14.6635-10.4199-1.0928
368.5955-0.4587-2.14165.9179-1.44062.74680.01470.48520.5137-1.021-0.40720.7401-0.0374-0.41370.39250.06870.1388-0.1319-0.2695-0.08750.061-29.9366-2.549735.3995
377.8322-1.51093.39873.1187-0.51291.22840.1018-0.58850.3003-0.2103-0.0433-0.2726-0.1251-0.082-0.0585-0.110.05220.0325-0.1137-0.0452-0.1494-16.1652-16.450348.2635
381.1991-4.8385-0.94994.0992-0.94652.32810.09880.5556-0.5072-0.5395-0.32890.54570.0776-0.05580.23010.07090.0791-0.1124-0.1361-0.071-0.0277-25.542-12.058732.7926
3911.5907-2.0812-2.51382.14164.69095.1437-0.0139-0.5088-0.5196-0.00540.010.21290.46560.29370.0039-0.21050.04370.0456-0.0270.0133-0.0689-5.2759-26.520945.3732
401.3518-3.04-0.10593.90951.38614.69970.22250.35810.214-0.7529-0.29860.1224-0.47940.02110.07610.13290.1108-0.0209-0.0830.0297-0.1009-18.9634-14.964931.8623
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{A|47 - 62}A47 - 62
2X-RAY DIFFRACTION2{A|63 - 79}A63 - 79
3X-RAY DIFFRACTION3{A|80 - 92}A80 - 92
4X-RAY DIFFRACTION4{A|93 - 109}A93 - 109
5X-RAY DIFFRACTION5{A|110 - 136}A110 - 136
6X-RAY DIFFRACTION6{A|137 - 154}A137 - 154
7X-RAY DIFFRACTION7{A|155 - 174}A155 - 174
8X-RAY DIFFRACTION8{A|175 - 187}A175 - 187
9X-RAY DIFFRACTION9{A|188 - 200}A188 - 200
10X-RAY DIFFRACTION10{A|201 - 222}A201 - 222
11X-RAY DIFFRACTION11{A|223 - 235}A223 - 235
12X-RAY DIFFRACTION12{A|236 - 247}A236 - 247
13X-RAY DIFFRACTION13{A|248 - 255}A248 - 255
14X-RAY DIFFRACTION14{A|256 - 270}A256 - 270
15X-RAY DIFFRACTION15{A|271 - 283}A271 - 283
16X-RAY DIFFRACTION16{A|284 - 301}A284 - 301
17X-RAY DIFFRACTION17{A|302 - 315}A302 - 315
18X-RAY DIFFRACTION18{A|316 - 342}A316 - 342
19X-RAY DIFFRACTION19{A|343 - 358}A343 - 358
20X-RAY DIFFRACTION20{A|359 - 375}A359 - 375
21X-RAY DIFFRACTION21{B|42 - 58}B42 - 58
22X-RAY DIFFRACTION22{B|59 - 74}B59 - 74
23X-RAY DIFFRACTION23{B|75 - 87}B75 - 87
24X-RAY DIFFRACTION24{B|88 - 96}B88 - 96
25X-RAY DIFFRACTION25{B|107 - 125}B107 - 125
26X-RAY DIFFRACTION26{B|134 - 149}B134 - 149
27X-RAY DIFFRACTION27{B|150 - 155}B150 - 155
28X-RAY DIFFRACTION28{B|156 - 174}B156 - 174
29X-RAY DIFFRACTION29{B|175 - 187}B175 - 187
30X-RAY DIFFRACTION30{B|188 - 200}B188 - 200
31X-RAY DIFFRACTION31{B|201 - 211}B201 - 211
32X-RAY DIFFRACTION32{B|212 - 224}B212 - 224
33X-RAY DIFFRACTION33{B|225 - 244}B225 - 244
34X-RAY DIFFRACTION34{B|245 - 250}B245 - 250
35X-RAY DIFFRACTION35{B|251 - 268}B251 - 268
36X-RAY DIFFRACTION36{B|269 - 283}B269 - 283
37X-RAY DIFFRACTION37{B|284 - 303}B284 - 303
38X-RAY DIFFRACTION38{B|304 - 348}B304 - 348
39X-RAY DIFFRACTION39{B|349 - 361}B349 - 361
40X-RAY DIFFRACTION40{B|362 - 375}B362 - 375

+
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