[English] 日本語
Yorodumi
- PDB-5lgp: Crystal structure of mouse CARM1 in complex with ligand P1C3s -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5lgp
TitleCrystal structure of mouse CARM1 in complex with ligand P1C3s
Components
  • Histone-arginine methyltransferase CARM1
  • Polyadenylate-binding protein 1
KeywordsTRANSFERASE / PROTEIN ARGININE METHYLTRANSFERASE / CATALYTIC DOMAIN / CHROMATIN REGULATOR / MRNA PROCESSING / MRNA SPLICING / NUCLEUS / S-ADENOSYL-L-METHIONINE / TRANSCRIPTION / TRANSCRIPTION REGULATION
Function / homology
Function and homology information


histone H3R26 methyltransferase activity / mCRD-mediated mRNA stability complex / negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of growth plate cartilage chondrocyte proliferation / translation activator activity / histone H3R17 methyltransferase activity / endochondral bone morphogenesis / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / histone H3R2 methyltransferase activity ...histone H3R26 methyltransferase activity / mCRD-mediated mRNA stability complex / negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of growth plate cartilage chondrocyte proliferation / translation activator activity / histone H3R17 methyltransferase activity / endochondral bone morphogenesis / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / histone H3R2 methyltransferase activity / RMTs methylate histone arginines / Regulation of lipid metabolism by PPARalpha / type I protein arginine methyltransferase / negative regulation of dendrite development / protein-arginine omega-N asymmetric methyltransferase activity / Cytoprotection by HMOX1 / protein methyltransferase activity / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / Estrogen-dependent gene expression / Deadenylation of mRNA / regulation of intracellular estrogen receptor signaling pathway / replication fork reversal / positive regulation of cytoplasmic translation / protein-arginine N-methyltransferase activity / M-decay: degradation of maternal mRNAs by maternally stored factors / poly(A) binding / regulatory ncRNA-mediated gene silencing / mRNA stabilization / poly(U) RNA binding / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / Translation initiation complex formation / histone methyltransferase activity / cell leading edge / nuclear replication fork / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of fat cell differentiation / positive regulation of viral genome replication / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / nuclear receptor-mediated steroid hormone signaling pathway / response to cAMP / protein localization to chromatin / estrogen receptor signaling pathway / catalytic step 2 spliceosome / nuclear receptor coactivator activity / mRNA 3'-UTR binding / AUF1 (hnRNP D0) binds and destabilizes mRNA / lysine-acetylated histone binding / mRNA splicing, via spliceosome / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / cytoplasmic stress granule / RNA polymerase II transcription regulator complex / lamellipodium / methylation / cell population proliferation / transcription coactivator activity / transcription cis-regulatory region binding / chromatin remodeling / ribonucleoprotein complex / focal adhesion / mRNA binding / positive regulation of cell population proliferation / regulation of DNA-templated transcription / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / RNA binding / extracellular exosome / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
: / PABP, RNA recognition motif 2 / Polyadenylate binding protein, human types 1, 2, 3, 4 / Poly(A)-binding protein C-terminal (PABC) domain profile. / C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein. / Polyadenylate-binding protein/Hyperplastic disc protein / PABC (PABP) domain / Poly-adenylate binding protein, unique domain / Histone-arginine methyltransferase CARM1, N-terminal / Coactivator-associated arginine methyltransferase 1 N terminal ...: / PABP, RNA recognition motif 2 / Polyadenylate binding protein, human types 1, 2, 3, 4 / Poly(A)-binding protein C-terminal (PABC) domain profile. / C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein. / Polyadenylate-binding protein/Hyperplastic disc protein / PABC (PABP) domain / Poly-adenylate binding protein, unique domain / Histone-arginine methyltransferase CARM1, N-terminal / Coactivator-associated arginine methyltransferase 1 N terminal / Ribosomal protein L11 methyltransferase (PrmA) / Hnrnp arginine n-methyltransferase1 / Hnrnp arginine n-methyltransferase1 / RNA recognition motif domain, eukaryote / RNA recognition motif / Arginine methyltransferase oligomerization subdomain / Protein arginine N-methyltransferase / SAM-dependent methyltransferase PRMT-type domain profile. / Vaccinia Virus protein VP39 / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / Distorted Sandwich / RNA-binding domain superfamily / PH-like domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-8ZB / L-PROLINAMIDE / Polyadenylate-binding protein 1 / Histone-arginine methyltransferase CARM1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.04 Å
AuthorsMarechal, N. / Troffer-Charlier, N. / Cura, V. / Bonnefond, L. / Cavarelli, J.
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017
Title: Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
Authors: van Haren, M.J. / Marechal, N. / Troffer-Charlier, N. / Cianciulli, A. / Sbardella, G. / Cavarelli, J. / Martin, N.I.
History
DepositionJul 8, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 22, 2017Provider: repository / Type: Initial release
Revision 1.1Apr 5, 2017Group: Non-polymer description
Revision 1.2Apr 12, 2017Group: Database references
Revision 1.3Jan 10, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Histone-arginine methyltransferase CARM1
B: Histone-arginine methyltransferase CARM1
C: Histone-arginine methyltransferase CARM1
D: Histone-arginine methyltransferase CARM1
E: Polyadenylate-binding protein 1
F: Polyadenylate-binding protein 1
G: Polyadenylate-binding protein 1
H: Polyadenylate-binding protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)170,48421
Polymers168,6008
Non-polymers1,88413
Water13,601755
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22160 Å2
ΔGint-108 kcal/mol
Surface area48240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)74.794, 98.714, 207.253
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11D-728-

HOH

-
Components

-
Protein / Protein/peptide , 2 types, 8 molecules ABCDEFGH

#1: Protein
Histone-arginine methyltransferase CARM1 / Coactivator-associated arginine methyltransferase 1 / Protein arginine N-methyltransferase 4


Mass: 40850.457 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Carm1, Prmt4 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q9WVG6, type I protein arginine methyltransferase
#2: Protein/peptide
Polyadenylate-binding protein 1 / Poly(A)-binding protein 1


Mass: 1299.521 Da / Num. of mol.: 4 / Source method: obtained synthetically
Details: URG is a modified ARG residue ARP is an acetylated PRO residue
Source: (synth.) Homo sapiens (human) / References: UniProt: P11940

-
Non-polymers , 4 types, 768 molecules

#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-8ZB / (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-propyl-oxolane-3,4-diol


Mass: 279.295 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C12H17N5O3
Details: URG is a modified ARG residue ARP is an acetylated PRO residue
#5: Chemical
ChemComp-LPD / L-PROLINAMIDE


Type: L-peptide linking / Mass: 114.146 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C5H10N2O
Details: URG is a modified ARG residue ARP is an acetylated PRO residue
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 755 / 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: 2.23 Å3/Da / Density % sol: 44.95 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 / Details: 100 mM Tris-HCl pH 8.5 16% PEG 3350 200 mM A.S.

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97857 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 7, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 2.04→48 Å / Num. obs: 98498 / % possible obs: 100 % / Redundancy: 6.6 % / Biso Wilson estimate: 31.63 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.148 / Net I/σ(I): 9.7
Reflection shellResolution: 2.04→2.07 Å / Redundancy: 6.4 % / Rmerge(I) obs: 2.331 / Mean I/σ(I) obs: 0.8 / CC1/2: 0.313 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX(dev_2386: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5IH3

5ih3


Resolution: 2.04→48 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 22.65
RfactorNum. reflection% reflectionSelection details
Rfree0.2193 4879 4.96 %Random selection
Rwork0.1873 ---
obs0.1889 98404 99.93 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.04→48 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11449 0 20 755 12224
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00611766
X-RAY DIFFRACTIONf_angle_d0.69115944
X-RAY DIFFRACTIONf_dihedral_angle_d12.8976959
X-RAY DIFFRACTIONf_chiral_restr0.0481739
X-RAY DIFFRACTIONf_plane_restr0.0042094
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.04-2.06320.33821850.33183075X-RAY DIFFRACTION100
2.0632-2.08750.31651370.31293084X-RAY DIFFRACTION100
2.0875-2.11290.31561500.29283107X-RAY DIFFRACTION100
2.1129-2.13970.33381520.28693130X-RAY DIFFRACTION100
2.1397-2.16780.31721690.2853019X-RAY DIFFRACTION100
2.1678-2.19750.29451670.28343094X-RAY DIFFRACTION100
2.1975-2.22890.3171830.27093046X-RAY DIFFRACTION100
2.2289-2.26220.29981580.25853107X-RAY DIFFRACTION100
2.2622-2.29750.26651650.25083077X-RAY DIFFRACTION100
2.2975-2.33520.2631540.23613089X-RAY DIFFRACTION100
2.3352-2.37550.27651410.23793086X-RAY DIFFRACTION100
2.3755-2.41860.28481690.22473104X-RAY DIFFRACTION100
2.4186-2.46520.20941640.21513092X-RAY DIFFRACTION100
2.4652-2.51550.25661480.21573083X-RAY DIFFRACTION100
2.5155-2.57020.23881640.20143099X-RAY DIFFRACTION100
2.5702-2.630.23911580.20193102X-RAY DIFFRACTION100
2.63-2.69570.2561720.20063107X-RAY DIFFRACTION100
2.6957-2.76860.24441400.19913126X-RAY DIFFRACTION100
2.7686-2.85010.22091670.19813075X-RAY DIFFRACTION100
2.8501-2.9420.23031500.18933145X-RAY DIFFRACTION100
2.942-3.04720.21951650.18643100X-RAY DIFFRACTION100
3.0472-3.16920.22651740.19383098X-RAY DIFFRACTION100
3.1692-3.31340.21551610.18023140X-RAY DIFFRACTION100
3.3134-3.4880.19681440.17073137X-RAY DIFFRACTION100
3.488-3.70650.20851680.15243158X-RAY DIFFRACTION100
3.7065-3.99250.16211780.14463141X-RAY DIFFRACTION100
3.9925-4.3940.15731750.13013159X-RAY DIFFRACTION100
4.394-5.02930.15391480.12673195X-RAY DIFFRACTION100
5.0293-6.33410.21721770.15873207X-RAY DIFFRACTION100
6.3341-48.02750.19541960.18253343X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.6096-0.32240.04211.23660.05971.7988-0.0091-0.18680.26290.1108-0.05520.0461-0.28660.03720.05870.3051-0.03430.03250.22-0.06260.317354.971340.0985133.7905
21.75970.64320.69170.12830.22290.59480.0841-0.0696-0.09870.059-0.03590.06550.00720.0207-0.04360.23110.00150.01150.1488-0.0180.321447.861511.9278119.2948
30.4197-0.04140.0141.8125-0.02441.5196-0.0148-0.0191-0.0522-0.20050.0113-0.09410.05860.13550.00020.2182-0.03510.05160.2273-0.01060.320960.305919.4203119.3978
41.1420.0024-0.2541.08540.58891.81460.0850.04010.0539-0.0936-0.0250.0377-0.2069-0.1463-0.07080.240.06080.01430.17290.03650.291418.971719.7937114.9256
53.07521.4777-0.55930.6968-0.37930.25520.295-0.41550.08990.2723-0.14110.053-0.07940.0775-0.13310.379-0.01410.03530.3824-0.01520.289238.098128.8555148.4087
62.48920.36750.51490.76180.51861.82860.0655-0.25290.03330.0734-0.0990.13850.0741-0.22330.02390.28610.00160.05030.29090.00330.323117.02121.7172137.5239
71.05940.1025-0.29310.8529-0.56792.57750.1222-0.17570.1111-0.01720.0168-0.1605-0.17780.1422-0.15260.2991-0.02690.03190.2432-0.01860.323924.472830.1291141.5206
81.91950.0478-0.01671.427-0.36471.521-0.05850.02250.2068-0.03760.0480.0132-0.2527-0.16720.00730.42890.04710.02940.4346-0.00070.315723.205241.8111175.2808
90.47880.07630.25370.09850.05950.57470.1134-0.0679-0.0478-0.0793-0.05320.1061-0.0799-0.15-0.0730.29920.01220.03270.4196-0.01260.283326.062921.0705191.0909
100.8012-0.0647-0.07181.63-0.60860.926-0.0420.0228-0.08920.12810.05110.1636-0.0093-0.1951-0.01320.29870.04140.06660.4816-0.03250.288716.215220.161191.065
111.10250.1069-0.64081.533-0.35881.43140.0865-0.1636-0.01240.1016-0.0864-0.1933-0.13160.1925-0.0080.2917-0.0789-0.00580.4444-0.04250.293357.27218.0544196.2038
122.0039-1.3556-0.14590.92510.20470.18610.18580.38530.0485-0.2237-0.1466-0.07460.0391-0.0056-0.05350.419-0.02050.05470.5037-0.02630.295239.972227.7197164.1251
131.5501-0.17770.20731.24880.34142.4987-0.06440.1877-0.1235-0.06690.0859-0.17540.05860.709-0.03830.35890.00380.04270.5742-0.01060.34563.779623.1656175.9871
140.2830.21660.0610.7584-0.47841.75540.03010.1154-0.0621-0.1539-0.0478-0.1459-0.00510.27350.0470.344-0.00210.0470.4819-0.0470.332158.549317.412170.6024
151.43770.4482-1.26290.9231-0.84662.34810.3956-0.28060.05170.16-0.14260.1726-0.39570.3346-0.26080.43630.00520.02720.59030.02050.355550.625927.308167.7259
160.1660.0011-0.39520.9785-0.41321.18420.0921-0.0666-0.00910.45310.14840.0521-0.41150.5545-0.13280.39480.0187-0.02610.3101-0.0320.365932.910821.3887128.2453
170.8364-0.33850.1350.4916-0.42252.6152-0.01230.0955-0.4256-0.1941-0.09961.13650.4519-0.52290.16040.3251-0.04910.00380.3045-0.08120.554145.96625.3481129.7123
180.44490.55680.18321.50770.38260.1217-0.05470.1144-0.21820.6304-0.0745-1.13750.63920.51740.0760.69020.12990.01320.47710.03240.607730.9726.1395182.3173
190.23270.21140.12260.69790.50461.4207-0.07760.13140.1129-0.402-0.08920.2064-0.5225-1.31090.20790.54420.01530.00210.7709-0.05790.45543.33720.9162182.986
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 136 through 282 )
2X-RAY DIFFRACTION2chain 'A' and (resid 283 through 349 )
3X-RAY DIFFRACTION3chain 'A' and (resid 350 through 478 )
4X-RAY DIFFRACTION4chain 'B' and (resid 135 through 293)
5X-RAY DIFFRACTION5chain 'B' and (resid 294 through 336 )
6X-RAY DIFFRACTION6chain 'B' and (resid 337 through 365 )
7X-RAY DIFFRACTION7chain 'B' and (resid 446 through 477 )
8X-RAY DIFFRACTION8chain 'C' and (resid 136 through 257)
9X-RAY DIFFRACTION9chain 'C' and (resid 258 through 336 )
10X-RAY DIFFRACTION10chain 'C' and (resid 337 through 478 )
11X-RAY DIFFRACTION11chain 'D' and (resid 136 through 293)
12X-RAY DIFFRACTION12chain 'D' and (resid 294 through 344 )
13X-RAY DIFFRACTION13chain 'D' and (resid 345 through 372 )
14X-RAY DIFFRACTION14chain 'D' and (resid 373 through 430 )
15X-RAY DIFFRACTION15chain 'D' and (resid 458 through 477 )
16X-RAY DIFFRACTION16chain 'F' and (resid -8 through 4 )
17X-RAY DIFFRACTION17chain 'E' and (resid -6 through 4)
18X-RAY DIFFRACTION18chain 'G' and (resid -6 through 4 )
19X-RAY DIFFRACTION19chain 'H' and (resid -8 through 4 )

+
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