[English] 日本語
Yorodumi
- PDB-5jjl: Rho transcription termination factor bound to rU8 and 5 ADP-BeF3 ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5jjl
TitleRho transcription termination factor bound to rU8 and 5 ADP-BeF3 molecules
Components
  • Transcription termination factor Rho
  • rU12: RNA (5'-R(P*UP*UP*UP*UP*UP*UP*U)-3')
KeywordsTRANSCRIPTION/RNA / protein-RNA complex / TRANSCRIPTION-RNA complex
Function / homology
Function and homology information


ATP-dependent activity, acting on RNA / helicase activity / DNA-templated transcription termination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ATP hydrolysis activity / RNA binding / ATP binding / membrane / identical protein binding / cytosol
Similarity search - Function
Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / Cold shock domain ...Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / Cold shock domain / Cold shock protein domain / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / BERYLLIUM TRIFLUORIDE ION / RNA / RNA (> 10) / Transcription termination factor Rho / Transcription termination factor Rho
Similarity search - Component
Biological speciesEscherichia coli O157:H7 (bacteria)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsThomsen, N.D. / Lawson, M.R. / Witkowsky, L.B. / Qu, S. / Berger, J.M.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM071747 United States
G. Harold and Leila Y. Mathers Foundation United States
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2016
Title: Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
Authors: Thomsen, N.D. / Lawson, M.R. / Witkowsky, L.B. / Qu, S. / Berger, J.M.
History
DepositionApr 24, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 16, 2016Provider: repository / Type: Initial release
Revision 1.1Dec 21, 2016Group: Structure summary
Revision 1.2Dec 28, 2016Group: Database references
Revision 1.3Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Sep 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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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.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
Revision 1.6Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Transcription termination factor Rho
B: Transcription termination factor Rho
C: Transcription termination factor Rho
D: Transcription termination factor Rho
E: Transcription termination factor Rho
F: Transcription termination factor Rho
G: rU12: RNA (5'-R(P*UP*UP*UP*UP*UP*UP*U)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)293,91422
Polymers291,3267
Non-polymers2,58815
Water28816
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26370 Å2
ΔGint-98 kcal/mol
Surface area92450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.091, 199.071, 111.666
Angle α, β, γ (deg.)90.000, 105.022, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb

-
Components

-
Protein / RNA chain , 2 types, 7 molecules ABCDEFG

#1: Protein
Transcription termination factor Rho / ATP-dependent helicase Rho


Mass: 47949.500 Da / Num. of mol.: 6 / Mutation: N-terminal MGH insertion
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli O157:H7 (bacteria) / Gene: rho, Z5293, ECs4716 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) pLysS
References: UniProt: P0AG32, UniProt: P0AG30*PLUS, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
#2: RNA chain rU12: RNA (5'-R(P*UP*UP*UP*UP*UP*UP*U)-3')


Mass: 3629.032 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

-
Non-polymers , 4 types, 31 molecules

#3: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: BeF3
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 16 / 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: 2.58 Å3/Da / Density % sol: 52.36 %
Crystal growTemperature: 291 K / Method: microbatch / pH: 7.5 / Details: 200 mM KOAc, 40% MPD, 0.5% ethyl acetate

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.116 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: May 4, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.116 Å / Relative weight: 1
ReflectionResolution: 3.2→49.52 Å / Num. obs: 46060 / % possible obs: 96.12 % / Biso Wilson estimate: 63.31 Å2
Reflection shellResolution: 3.2→3.31 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 1.8 / % possible all: 96.4

-
Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
HKL-2000data scaling
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5JJI
Resolution: 3.2→49.52 Å / SU ML: 0.410615569722 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 27.7612787883
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.266 2310 5.01519756839 %
Rwork0.232 43750 -
obs0.234 46060 96.1205367391 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 73.3330848993 Å2
Refinement stepCycle: LAST / Resolution: 3.2→49.52 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18888 165 160 16 19229
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0062515017640219504
X-RAY DIFFRACTIONf_angle_d0.57346508041626316
X-RAY DIFFRACTIONf_chiral_restr0.03976390524553028
X-RAY DIFFRACTIONf_plane_restr0.003098246677023363
X-RAY DIFFRACTIONf_dihedral_angle_d23.96311032647533
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.201-3.27060.3520257643241480.3269906712332731X-RAY DIFFRACTION95.5526053767
3.2706-3.34670.315374535721460.3044658948492695X-RAY DIFFRACTION96.9955616251
3.3467-3.43030.3229702701371470.2914386167452736X-RAY DIFFRACTION96.1
3.4303-3.52310.2806896377081400.2687840767022726X-RAY DIFFRACTION96.4658364187
3.5231-3.62670.3084591280131530.2650031985062751X-RAY DIFFRACTION95.9682749504
3.6267-3.74370.2987850911821360.2623419510752731X-RAY DIFFRACTION96.2726662189
3.7437-3.87750.3150374458381540.2496110848962729X-RAY DIFFRACTION96.7774420947
3.8775-4.03260.2826042385031370.2449265654182758X-RAY DIFFRACTION96.8551354968
4.0326-4.21610.3005418279581400.2213758308222731X-RAY DIFFRACTION96.6992253284
4.2161-4.43820.2154281062071570.2119639725422743X-RAY DIFFRACTION96.6988996332
4.4382-4.71610.266704983281370.2001489530142763X-RAY DIFFRACTION97.0548862115
4.7161-5.07990.2281211140441480.199378844032750X-RAY DIFFRACTION96.4392678869
5.0799-5.59050.2686693112471440.2249179187562735X-RAY DIFFRACTION96.1268781302
5.5905-6.3980.2444626533741400.2366277442752746X-RAY DIFFRACTION95.373430271
6.398-8.05520.2382995476361440.228333633632674X-RAY DIFFRACTION94.1215764863
8.0552-49.52490.2208443947031390.1874504646852751X-RAY DIFFRACTION94.660989191
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)
10.0149209205424-0.0144257376644-0.01647351501980.01163542390730.01365658738730.01762993443440.08386449266090.339690942838-0.352273272668-0.316227084232-0.05646535469660.3052511176-0.0186437435846-0.1446493564713.11050801788E-71.1988247324-0.10426038727-0.0002789072245291.185140802870.03428758586961.3025821746144.611500012817.1756330619-20.6816066986
20.02615910917250.0108769063516-0.0164813177650.0103792113823-0.002434596107480.0120244189496-0.0673747676190.208539306364-0.945977626003-0.400136687016-0.0622917859255-0.1437611717350.8213999957940.0252298132446-4.9911655972E-71.274203756640.09635223267450.1511264354041.50057796398-0.291122729631.0271093235644.6710399051-44.4574502425-19.4303201714
30.22915173526-0.01644759018940.1217508717950.04148208476280.005043000058670.07711459044630.0888970491072-0.636221424287-0.6616073994060.574337696833-0.413675975634-0.2809811662440.4244735978560.146038635181-0.003772992880971.113239284790.0837870199279-0.1953395743410.8444591469450.375107499921.4893664755842.345561037-71.398698072135.3884897329
40.0556477854567-0.0002199269764830.007711188966410.1194458053240.02588723815140.0680174668441-0.0972582310975-0.162785448273-0.03517996223640.6774400835370.1802544196060.291225000253-0.144433634862-0.03067947328695.66881495723E-80.944786384350.222789453730.003861546761.12339652744-0.04464449015480.55114292624842.7661252773-39.189064525381.8481124703
50.04721830705660.03417010881380.02451403232420.04122787591570.006278411698630.0345972031158-0.09570449219390.52017056859-0.0717524808704-0.2620860371420.1336903394650.263017495570.3000199677910.02327237670924.37545477692E-71.07028369366-0.295023490013-0.2475908374471.60499035504-0.01354682950551.3171587217745.264117772444.323885447527.985370074
60.03794074916950.05050834816880.125216082160.07501034952710.1798783445630.446077470878-0.1314361292470.1533324338160.45780718618-0.7560048041070.129150435459-0.774914090673-0.1575669715170.3226636009850.1194921388150.61748076032-0.07781493320930.04103153161090.2614900740360.2559377587191.083153732346.314469515221.122633223-2.165510819
70.6695896981610.2029750933760.2511040685320.0832607983522-0.03435719355831.286375548440.2421554459840.836939803983-0.0189722506279-0.308094220433-0.0870257442829-0.1489925984980.2087603937380.5655966054451.240388017870.4496392454540.2651148266520.2093104925840.989047133042-0.01317559724990.24791949615645.7428345691-25.0984049925-15.0139417766
80.9398526370060.539387392786-0.7800011914811.209292408820.2275229675861.182717643030.2911761024970.117990364555-1.05486730360.0371071786897-0.171321606453-0.473103548710.5935721757510.4112317669570.07896664837080.4984649280760.281097272506-0.2469345189040.245407987507-0.1026085990211.1117364402944.270553392-58.514365175918.7141270596
91.33932774360.03850198718850.1661081932260.4513186961270.03299904159490.399016946793-0.0525300508999-0.0429793149525-0.6468201380430.2376277903050.118832350582-0.1462448693630.07878703688010.6747192131610.0002716565201720.5827606081280.080940795427-0.06372790945780.9170033889660.1589021209690.40416550907442.6433022528-45.781609517762.7578158302
100.1332505397270.07726410758090.01836846281850.07265592759460.009579184445930.00100382509762-0.246701346507-0.5684409407920.2235245329320.399442147148-0.24795288887-0.683065973116-0.2366249524350.185567567959-0.001932192090671.149633380520.0647931258297-0.2969790248341.32180088094-0.2376289376370.84449735769840.4447052153-2.8017810116274.8147480786
110.1163719192750.08745401952670.01635854523510.270188922929-0.145265572610.120958410367-0.0235377851031-0.505268742039-0.01583531391370.328025432481-0.251057291482-0.07257501395880.337452861636-0.02613747126334.73547196638E-81.098709618470.050178172165-0.2509442722560.87589285976-0.308431260341.0107518227944.021327216432.03365335344.8890289185
120.6215924219990.378522853561-0.01918359746521.93697456970.3878074859540.769896066802-0.1456012337670.1621867529960.5486073535510.133824117863-0.08955021340510.448884831906-0.33633628574-0.0949506903211-0.1146856615840.4509016527630.117208021442-0.007533426731090.01938211196260.08149005070460.95260258612717.728913225510.79788844239.80221259285
131.68074997729-0.0184626027641-0.2110413905841.37869652483-0.2319712469551.831312167020.1003114760510.5015772085250.108007499549-0.14540800079-0.03554669531670.198681559709-0.0217524946606-0.1224299452940.007632884824650.2960707294220.0660994426647-0.02437492330570.2932803954740.02561590993340.18936179581216.5408404142-18.8410149099-0.567418413927
141.23335420106-0.2481067056060.3972144111.233042813150.1407223076752.216813980710.195341193146-0.121562268044-0.6257345586950.08287389011380.008681968906520.2015638086120.148735386817-0.2342400975880.06297369733720.273142056355-0.0440190250826-0.08065784702010.06873661452250.06730895307450.37451463012515.0134057857-42.96858118919.8033140085
151.124420547560.0605731115730.4580748826611.000682598210.1199698332421.655856378870.10673170877-1.07151956381-0.3184775250850.531071148480.3315160972510.341708409984-0.0230458002387-0.7580561524030.2229475914710.2842303629-0.03862566922460.2722496285180.8014438574260.4325705348080.07653150195313.4200091656-37.461256173150.8754499141
161.690819633090.866455912839-0.5382552896161.32789855332-0.3799376432651.28350214638-0.332491873376-0.9983779512580.5436222044020.4516178608780.2564446419220.495169623689-0.657856703814-0.854115879402-0.1990766844090.8372154777270.5568751400750.1375740174561.3739960844-0.2539236722290.3505777611513.6954926108-7.9479535149461.7898709986
170.8484294688910.6041872552890.2502653925350.996879985153-0.6501264485072.1280723996-0.223353184598-0.3750429548270.08373226802480.2441495408040.02754229012120.102281779403-0.203196053185-0.388539285667-6.14563140335E-50.9846300625930.109322599532-0.04691802866750.613020811724-0.2872212696081.0515277337915.34027836317.838912815740.9569447355
180.156067003533-0.0403305043727-0.0992289059080.362084720201-0.09546534762150.189756808061-0.662040936235-0.1601239837821.00016110898-0.555998881160.1308168679510.367413789086-0.8514700076050.287620469244-0.001919513915870.9348088523880.00293366763132-0.02806603808150.619988795124-0.03388507501060.46907119854926.5894998516-13.131719611830.2988789502
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resseq 1:47
2X-RAY DIFFRACTION2chain B and resseq 1:47
3X-RAY DIFFRACTION3chain C and resseq 1:47
4X-RAY DIFFRACTION4chain D and resseq 1:47
5X-RAY DIFFRACTION5chain F and resseq 1:47
6X-RAY DIFFRACTION6chain A and resseq 48:124
7X-RAY DIFFRACTION7chain B and resseq 48:128
8X-RAY DIFFRACTION8chain C and resseq 48:128
9X-RAY DIFFRACTION9chain D and resseq 48:128
10X-RAY DIFFRACTION10chain E and resseq 49:128
11X-RAY DIFFRACTION11chain F and resseq 49:128
12X-RAY DIFFRACTION12chain A and resseq 130:416
13X-RAY DIFFRACTION13chain B and resseq 129:417
14X-RAY DIFFRACTION14chain C and resseq 129:417
15X-RAY DIFFRACTION15chain D and resseq 129:416
16X-RAY DIFFRACTION16chain E and resseq 129:405
17X-RAY DIFFRACTION17chain F and resseq 129:416
18X-RAY DIFFRACTION18chain G and resseq 1:9

+
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