[English] 日本語
Yorodumi
- PDB-4lln: Crystal structure of S. aureus MepR-DNA complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4lln
TitleCrystal structure of S. aureus MepR-DNA complex
Components
  • MepR
  • Palindromized mepR operator sequence
KeywordsTRANSCRIPTION/DNA / multidrug resistance / winged helix-turn-helix / transcription repression / mepR operator / TRANSCRIPTION-DNA complex
Function / homology
Function and homology information


DNA-binding transcription factor activity
Similarity search - Function
MarR family / : / MarR-type HTH domain profile. / helix_turn_helix multiple antibiotic resistance protein / MarR-type HTH domain / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
DNA / DNA (> 10) / MarR family protein
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.842 Å
AuthorsBirukou, I. / Brennan, R.G.
CitationJournal: Nucleic Acids Res. / Year: 2014
Title: Structural mechanism of transcription regulation of the Staphylococcus aureus multidrug efflux operon mepRA by the MarR family repressor MepR.
Authors: Birukou, I. / Seo, S.M. / Schindler, B.D. / Kaatz, G.W. / Brennan, R.G.
History
DepositionJul 9, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 14, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software
Revision 1.2Sep 20, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: MepR
B: MepR
G: Palindromized mepR operator sequence
H: Palindromized mepR operator sequence
C: MepR
D: MepR
E: Palindromized mepR operator sequence
F: Palindromized mepR operator sequence
I: MepR
J: MepR
K: Palindromized mepR operator sequence
L: Palindromized mepR operator sequence


Theoretical massNumber of molelcules
Total (without water)141,76912
Polymers141,76912
Non-polymers00
Water0
1
A: MepR
B: MepR
G: Palindromized mepR operator sequence
H: Palindromized mepR operator sequence


Theoretical massNumber of molelcules
Total (without water)47,2564
Polymers47,2564
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10560 Å2
ΔGint-79 kcal/mol
Surface area19060 Å2
MethodPISA
2
C: MepR
D: MepR
E: Palindromized mepR operator sequence
F: Palindromized mepR operator sequence


Theoretical massNumber of molelcules
Total (without water)47,2564
Polymers47,2564
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9900 Å2
ΔGint-82 kcal/mol
Surface area20020 Å2
MethodPISA
3
I: MepR
J: MepR
K: Palindromized mepR operator sequence
L: Palindromized mepR operator sequence


Theoretical massNumber of molelcules
Total (without water)47,2564
Polymers47,2564
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10450 Å2
ΔGint-87 kcal/mol
Surface area19590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.343, 76.231, 109.410
Angle α, β, γ (deg.)90.61, 104.75, 106.27
Int Tables number1
Space group name H-MP1

-
Components

#1: Protein
MepR


Mass: 16262.288 Da / Num. of mol.: 6 / Fragment: MepR
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: mepR / Production host: Escherichia coli (E. coli) / References: UniProt: Q5Y812
#2: DNA chain
Palindromized mepR operator sequence


Mass: 7365.814 Da / Num. of mol.: 6 / Fragment: palindromized mepR operator / Source method: obtained synthetically
Details: this is a palindromized version of mepR operator sequence naturally occurring in S. aureus

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 4.15 Å3/Da / Density % sol: 70.38 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6
Details: 0.14M CaCl2, 0.7M Na Acetate, 14% 2-propanol, 30% glycerol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 18, 2012
RadiationMonochromator: Double-crystal, Si(111) liquid N2 cooled / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.84→50 Å / % possible obs: 91 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 2 / Redundancy: 7.3 % / Biso Wilson estimate: 70.91 Å2 / Rmerge(I) obs: 0.096 / Net I/σ(I): 31.73

-
Processing

Software
NameVersionClassificationNB
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.11data extraction
ADSCQuantumdata collection
DENZOdata reduction
SCALEPACKdata scaling
HKL-3000data scaling
PHENIX(Phaser)phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1z9c
Resolution: 2.842→44.835 Å / Occupancy max: 1 / Occupancy min: 0.22 / SU ML: 0.4 / σ(F): 1.97 / Phase error: 31.97 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2408 1997 4.18 %
Rwork0.2062 --
obs0.2076 47765 88.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 116.8066 Å2
Refinement stepCycle: LAST / Resolution: 2.842→44.835 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6345 2934 0 0 9279
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0039723
X-RAY DIFFRACTIONf_angle_d0.91513760
X-RAY DIFFRACTIONf_dihedral_angle_d25.2613737
X-RAY DIFFRACTIONf_chiral_restr0.0441589
X-RAY DIFFRACTIONf_plane_restr0.0031268
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8424-2.91340.5503780.41621782X-RAY DIFFRACTION48
2.9134-2.99220.41451100.37382525X-RAY DIFFRACTION69
2.9922-3.08020.37561180.30342699X-RAY DIFFRACTION74
3.0802-3.17960.30091300.24112964X-RAY DIFFRACTION81
3.1796-3.29320.25831370.21513202X-RAY DIFFRACTION87
3.2932-3.4250.25441540.21663492X-RAY DIFFRACTION95
3.425-3.58080.29941550.22453582X-RAY DIFFRACTION98
3.5808-3.76950.28851590.2173647X-RAY DIFFRACTION99
3.7695-4.00560.24821590.20623655X-RAY DIFFRACTION99
4.0056-4.31460.21431590.17583619X-RAY DIFFRACTION99
4.3146-4.74840.18771600.18123656X-RAY DIFFRACTION99
4.7484-5.43450.27361580.20213647X-RAY DIFFRACTION99
5.4345-6.84290.25151610.23123670X-RAY DIFFRACTION100
6.8429-44.84030.17781590.17133628X-RAY DIFFRACTION99
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)
10.07120.0271-0.01360.0085-0.00680.0044-0.0710.022-0.02180.07120.0810.0178-0.0841-0.0550.03410.3845-0.093-0.11940.4735-0.02960.0345-14.048557.088735.4798
20.3229-0.12940.33640.228-0.29010.4851-0.08690.20850.1551-0.0541-0.129-0.10960.03130.1983-0.01950.2302-0.0361-0.10870.1586-0.00320.2576-7.348175.893834.3277
30.1381-0.0641-0.05910.21190.15150.1055-0.12420.06160.09710.03510.25240.0616-0.21850.11940.00880.4057-0.0092-0.040.3020.05690.2405-10.823182.937936.8241
40.0254-0.0293-0.01140.03040.01430.0173-0.0027-0.0875-0.03970.03850.13930.003-0.0802-0.10790.02090.9470.157-0.27110.3088-0.10830.6772-3.456957.022743.1644
5-0.0017-0.00190.00320.0045-0.00650.0023-0.01180.0027-0.08320.14830.2795-0.10740.02030.10770.07510.56280.0955-0.17050.5046-0.24530.70951.993955.316427.7653
60.2931-0.21980.08110.2740.00740.1405-0.34050.15470.00740.32630.1135-0.11460.13160.0156-0.05010.4529-0.1209-0.03070.36630.01020.2374-10.41461.740223.3875
7-0.00320.0131-0.00470.08420.00060.0019-0.01-0.0855-0.15820.02820.02220.04420.0679-0.07820.08660.1881-0.2870.24160.26190.04990.1158-27.003449.823424.9607
80.1584-0.07520.1670.1086-0.0760.17150.0675-0.184-0.13430.09670.09590.17570.0733-0.30670.09020.3002-0.07080.1410.46580.05530.259-37.174553.061325.7236
90.00580.05980.02770.28890.01720.03740.12350.17520.08740.2330.115-0.22480.0303-0.06290.13260.273-0.0280.00180.4614-0.08550.3567-14.499149.083521.1143
100.21190.06120.18090.09730.13590.241-0.1646-0.0096-0.0427-0.09720.01930.0727-0.03380.1033-0.03580.6537-0.2680.02760.40450.06460.2176-9.874488.731212.3398
110.25660.1876-0.04460.1667-0.05560.03450.0231-0.11630.3363-0.06020.01450.2116-0.1727-0.0947-0.0240.3139-0.19030.06370.24390.11560.4999-24.462975.211724.6689
120.22410.0203-0.09060.01130.01940.05610.0516-0.28950.07880.0320.14290.13110.1188-0.0140.1970.1393-0.58690.62580.647-0.07930.4567-39.332856.154141.5207
130.14680.03410.09220.1076-0.00970.07860.0475-0.12160.3573-0.033-0.1170.04150.117-0.0788-0.07430.403-0.22690.14640.56940.03560.5515-38.791355.981240.9171
140.14770.04140.06250.21020.18370.1656-0.21140.03890.262-0.4601-0.0830.3857-0.136-0.0477-0.590.6321-0.4805-0.0940.08230.05910.365-21.891375.002324.3021
150.0017-0.00270.00030.00680.01040.015-0.05440.01730.055-0.0882-0.03830.10490.08020.42840.00010.7375-0.1702-0.04620.56650.09380.8203-12.543393.817317.7294
160.0360.0109-0.0410.0174-0.01220.05090.0164-0.0227-0.0482-0.0350.00170.2957-0.03840.0179-0.02540.4797-0.0178-0.18990.23660.04080.523-58.441844.70145.8119
170.2840.19660.03750.14670.02750.02010.30220.1447-0.2367-0.2-0.0866-0.2035-0.1612-0.01070.15840.3728-0.0105-0.04370.16630.04380.2159-41.21232.574410.6852
180.06090.00480.06270.05330.06530.06910.2190.0246-0.03050.1415-0.22540.19520.1470.01870.03180.38070.05880.0520.37690.14410.5749-46.250734.398417.3436
190.00580.00970.0050.00520.00310.0076-0.0279-0.1190.0580.0364-0.01250.05820.019-0.114300.6746-0.1307-0.02230.7280.03010.9523-68.564231.13168.7293
200.02760.0780.03980.08530.04810.04210.16870.0117-0.17350.0969-0.0038-0.02220.3056-0.11310.18080.35-0.0458-0.18210.435-0.0040.4107-58.718438.772-5.4296
210.0966-0.0530.00190.0681-0.00480.00440.01080.0110.01510.02020.14460.084-0.0783-0.0250.12660.18360.13290.04840.4026-0.08340.1306-54.78954.0427-9.2203
22-0.0013-0.0007-0.00170.0035-0.0003-0.00210.10370.052-0.0376-0.01330.15530.013-0.056-0.029-0.00010.95480.0801-0.06230.68820.12860.6853-57.650259.2735-19.0953
230.02090.03040.0320.03670.02010.037-0.00530.13540.1579-0.24310.08140.4175-0.0441-0.13460.03380.432-0.0903-0.240.44940.05420.6338-68.316238.1221-5.6261
240.101-0.0066-0.06250.0147-0.0190.08170.00820.165-0.1291-0.0723-0.1094-0.01180.160.0088-0.07091.09540.31160.13670.3744-0.30721.0525-33.864919.251-4.0629
250.04240.0563-0.01030.0747-0.07120.12510.0607-0.1316-0.14810.0841-0.4289-0.3719-0.39910.2661-0.28310.61190.0703-0.03590.359-0.03080.668-41.979148.5334-3.4447
260.01470.02150.02890.03190.04290.0612-0.09420.01490.0417-0.0101-0.12780.0304-0.1429-0.0583-0.08481.44160.3408-0.24570.33850.0360.8515-47.602673.6014-9.6033
270.0145-0.0101-0.01090.0090.00770.0076-0.21890.042-0.09150.0324-0.10620.00060.0453-0.0942-0.00481.09920.17310.27130.442-0.12921.4146-51.268773.8154-2.3605
280.4609-0.04880.18510.1696-0.0920.110.12370.29340.0874-0.2684-0.2923-0.1925-0.060.1648-0.36380.5080.3738-0.2492-0.0226-0.15120.5714-42.555747.0413-4.0986
290.0557-0.0026-0.04430.00320.01010.3085-0.010.185-0.02580.1262-0.1926-0.00230.11020.0219-0.1121.12510.5711-0.14030.4348-0.01671.1511-29.192620.8642-4.8439
300.0157-0.05330.07560.111-0.15530.24020.12230.02420.0476-0.0665-0.09-0.02810.05990.1445-0.0120.1984-0.08790.07310.4814-0.19740.1925-11.338108.125952.7912
310.0122-0.00010.00570.0696-0.00220.0304-0.1703-0.2525-0.12620.14170.1774-0.1301-0.28220.05570.03260.3035-0.0354-0.0650.5477-0.0620.30915.457594.861648.3001
320.16560.09150.10090.0704-0.02470.17550.1544-0.09190.0150.03120.06620.0160.03220.24740.1480.2563-0.02340.01790.3252-0.11630.32281.5484106.516444.4732
330.0507-0.0152-0.00890.04440.02240.00940.08010.18330.0108-0.01970.0006-0.0393-0.00230.0630.08890.3135-0.1230.10520.3658-0.43320.21310.1055110.20558.3385
340.07690.01940.02950.20520.0060.01840.0615-0.05720.05030.2134-0.03480.1411-0.209-0.07090.29750.7885-0.0408-0.13450.8348-0.36280.3827-15.9566108.984172.5597
350.00070.00030.00170.0040.00590.00550.06570.02520.0137-0.04530.05720.0441-0.0193-0.00470.00010.5991-0.00620.00480.6592-0.0280.6164-21.052104.799863.7423
360.0063-0.0113-0.01080.0546-0.01430.0392-0.1129-0.1505-0.0232-0.1274-0.03210.0014-0.04220.0947-0.03260.42050.017-0.02580.7322-0.25010.4573-18.015299.101174.4585
370.1348-0.00550.06740.10140.0360.44910.4082-0.1269-0.04930.02920.0908-0.0923-0.29530.1040.69310.7024-0.3398-0.08850.6763-0.510.4623-16.7377109.483374.4661
380.00730.0166-0.01960.0284-0.02840.030.1038-0.04210.08830.0363-0.05080.0803-0.18730.08360.06550.5502-0.0835-0.20120.4024-0.34210.8856-9.7318122.870353.2493
390.0159-0.02220.01140.0767-0.10690.1611-0.0676-0.12820.00080.1238-0.0041-0.0115-0.09950.3542-0.040.19060.1524-0.21471.05830.08550.716615.179190.673963.9787
400.0275-0.02090.07210.0309-0.06480.2012-0.2754-0.10940.0414-0.03420.17430.1661-0.0762-0.5099-0.06450.2636-0.0971-0.04931.0544-0.18710.5322-22.391491.703663.5228
410.1753-0.0139-0.0219-0.00710.03890.0985-0.2025-0.1073-0.1788-0.0612-0.03710.0889-0.0726-0.1982-0.3132-0.18340.0353-0.01030.9376-0.32950.6545-21.31291.256761.1264
420.0279-0.0550.00350.09910.03420.0144-0.2355-0.06140.04940.068-0.143-0.1944-0.06560.1006-0.68830.10550.1148-0.4631.4156-0.09830.849915.834190.24764.7795
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 27 )
2X-RAY DIFFRACTION2chain 'A' and (resid 28 through 60 )
3X-RAY DIFFRACTION3chain 'A' and (resid 61 through 105 )
4X-RAY DIFFRACTION4chain 'A' and (resid 106 through 120 )
5X-RAY DIFFRACTION5chain 'A' and (resid 121 through 139 )
6X-RAY DIFFRACTION6chain 'B' and (resid 2 through 27 )
7X-RAY DIFFRACTION7chain 'B' and (resid 28 through 60 )
8X-RAY DIFFRACTION8chain 'B' and (resid 61 through 88 )
9X-RAY DIFFRACTION9chain 'B' and (resid 89 through 139 )
10X-RAY DIFFRACTION10chain 'G' and (resid 1 through 5 )
11X-RAY DIFFRACTION11chain 'G' and (resid 6 through 14 )
12X-RAY DIFFRACTION12chain 'G' and (resid 15 through 24 )
13X-RAY DIFFRACTION13chain 'H' and (resid 1 through 10 )
14X-RAY DIFFRACTION14chain 'H' and (resid 11 through 19 )
15X-RAY DIFFRACTION15chain 'H' and (resid 20 through 24 )
16X-RAY DIFFRACTION16chain 'C' and (resid 2 through 27 )
17X-RAY DIFFRACTION17chain 'C' and (resid 28 through 80 )
18X-RAY DIFFRACTION18chain 'C' and (resid 81 through 117 )
19X-RAY DIFFRACTION19chain 'C' and (resid 118 through 139 )
20X-RAY DIFFRACTION20chain 'D' and (resid 0 through 46 )
21X-RAY DIFFRACTION21chain 'D' and (resid 47 through 73 )
22X-RAY DIFFRACTION22chain 'D' and (resid 74 through 94 )
23X-RAY DIFFRACTION23chain 'D' and (resid 95 through 139 )
24X-RAY DIFFRACTION24chain 'E' and (resid 1 through 7 )
25X-RAY DIFFRACTION25chain 'E' and (resid 8 through 19 )
26X-RAY DIFFRACTION26chain 'E' and (resid 20 through 24 )
27X-RAY DIFFRACTION27chain 'F' and (resid 1 through 5 )
28X-RAY DIFFRACTION28chain 'F' and (resid 6 through 17 )
29X-RAY DIFFRACTION29chain 'F' and (resid 18 through 24 )
30X-RAY DIFFRACTION30chain 'I' and (resid 2 through 27 )
31X-RAY DIFFRACTION31chain 'I' and (resid 28 through 80 )
32X-RAY DIFFRACTION32chain 'I' and (resid 81 through 138 )
33X-RAY DIFFRACTION33chain 'J' and (resid 0 through 27 )
34X-RAY DIFFRACTION34chain 'J' and (resid 28 through 49 )
35X-RAY DIFFRACTION35chain 'J' and (resid 50 through 60 )
36X-RAY DIFFRACTION36chain 'J' and (resid 61 through 81 )
37X-RAY DIFFRACTION37chain 'J' and (resid 82 through 116 )
38X-RAY DIFFRACTION38chain 'J' and (resid 117 through 139 )
39X-RAY DIFFRACTION39chain 'K' and (resid 1 through 10 )
40X-RAY DIFFRACTION40chain 'K' and (resid 11 through 24 )
41X-RAY DIFFRACTION41chain 'L' and (resid 1 through 14 )
42X-RAY DIFFRACTION42chain 'L' and (resid 15 through 24 )

+
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