[English] 日本語
Yorodumi
- PDB-5jlj: Crystal Structure of KPT8602 in complex with CRM1-Ran-RanBP1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5jlj
TitleCrystal Structure of KPT8602 in complex with CRM1-Ran-RanBP1
Components
  • Exportin-1
  • GTP-binding nuclear protein Ran
  • Ran-specific GTPase-activating protein 1
KeywordsPROTEIN TRANSPORT / HEAT repeat / Exportin-1 / Nuclear Transport / Transport receptor-Inhibitor complex
Function / homology
Function and homology information


tRNA re-export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / Regulation of HSF1-mediated heat shock response / Transcriptional and post-translational regulation of MITF-M expression and activity / manchette / nuclear export signal receptor activity / cellular response to mineralocorticoid stimulus ...tRNA re-export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / Regulation of HSF1-mediated heat shock response / Transcriptional and post-translational regulation of MITF-M expression and activity / manchette / nuclear export signal receptor activity / cellular response to mineralocorticoid stimulus / Regulation of cholesterol biosynthesis by SREBP (SREBF) / tRNA export from nucleus / importin-alpha family protein binding / SUMOylation of SUMOylation proteins / protein localization to kinetochore / spindle pole body / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / U4 snRNA binding / nuclear export / SUMOylation of RNA binding proteins / protein localization to nucleolus / NEP/NS2 Interacts with the Cellular Export Machinery / RNA export from nucleus / tRNA processing in the nucleus / GTP metabolic process / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of chromatin organization proteins / nuclear import signal receptor activity / MicroRNA (miRNA) biogenesis / DNA metabolic process / MAPK6/MAPK4 signaling / dynein intermediate chain binding / mitotic sister chromatid segregation / U5 snRNA binding / viral process / spermatid development / ribosomal large subunit export from nucleus / U2 snRNA binding / U6 snRNA binding / positive regulation of protein binding / sperm flagellum / nuclear pore / mRNA export from nucleus / U1 snRNA binding / ribosomal subunit export from nucleus / ribosomal small subunit export from nucleus / centriole / GTPase activator activity / protein export from nucleus / mitotic spindle organization / male germ cell nucleus / hippocampus development / Transcriptional regulation by small RNAs / G1/S transition of mitotic cell cycle / recycling endosome / kinetochore / positive regulation of protein import into nucleus / small GTPase binding / protein import into nucleus / GDP binding / melanosome / nuclear envelope / mitotic cell cycle / G protein activity / actin cytoskeleton organization / midbody / ubiquitin-dependent protein catabolic process / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cadherin binding / protein heterodimerization activity / protein domain specific binding / cell division / GTPase activity / chromatin binding / chromatin / GTP binding / protein-containing complex binding / nucleolus / perinuclear region of cytoplasm / magnesium ion binding / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
Ran-specific GTPase-activating protein 1, Ran-binding domain / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1, C-terminal / CRM1 C terminal ...Ran-specific GTPase-activating protein 1, Ran-binding domain / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1, C-terminal / CRM1 C terminal / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / Ran binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / Ran GTPase / Small GTPase Ran-type domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta N-terminal domain profile. / Importin-beta, N-terminal domain / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Armadillo-like helical / Small GTP-binding protein domain / PH-like domain superfamily / Armadillo-type fold / Roll / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-6L8 / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Exportin-1 / Ran-specific GTPase-activating protein 1 / GTP-binding nuclear protein Ran
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.5 Å
AuthorsFung, H.Y. / Chook, Y.M.
Funding support Hong Kong, United States, 6items
OrganizationGrant numberCountry
Croucher FoundationPredoc Scholarship Hong Kong
Cancer Prevention and Research Institute of Texas (CPRIT)RP120352, RP150053 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM069909 United States
University of Texas Southwestern Medical CenterEndowed Scholars Program United States
Welch FoundationI-1532 United States
Leukemia & Lymphoma SocietyScholar Award United States
CitationJournal: Leukemia / Year: 2016
Title: Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies.
Authors: Hing, Z.A. / Fung, H.Y. / Ranganathan, P. / Mitchell, S. / El-Gamal, D. / Woyach, J.A. / Williams, K. / Goettl, V.M. / Smith, J. / Yu, X. / Meng, X. / Sun, Q. / Cagatay, T. / Lehman, A.M. / ...Authors: Hing, Z.A. / Fung, H.Y. / Ranganathan, P. / Mitchell, S. / El-Gamal, D. / Woyach, J.A. / Williams, K. / Goettl, V.M. / Smith, J. / Yu, X. / Meng, X. / Sun, Q. / Cagatay, T. / Lehman, A.M. / Lucas, D.M. / Baloglu, E. / Shacham, S. / Kauffman, M.G. / Byrd, J.C. / Chook, Y.M. / Garzon, R. / Lapalombella, R.
History
DepositionApr 27, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 29, 2016Provider: repository / Type: Initial release
Revision 1.1Dec 14, 2016Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Sep 27, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Apr 24, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Sep 27, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: GTP-binding nuclear protein Ran
B: Ran-specific GTPase-activating protein 1
C: Exportin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)162,22512
Polymers160,7523
Non-polymers1,4739
Water3,333185
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10730 Å2
ΔGint-50 kcal/mol
Surface area57180 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.929, 105.929, 305.135
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212

-
Components

-
Protein , 3 types, 3 molecules ABC

#1: Protein GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 26758.564 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Plasmid: pET15 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62826
#2: Protein Ran-specific GTPase-activating protein 1 / Chromosome stability protein 20 / Perinuclear array-localized protein / Ran-binding protein 1 / RANBP1


Mass: 16521.867 Da / Num. of mol.: 1 / Fragment: RanDB1, unp residues 62-201
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: YRB1, CST20, HTN1, SFO1, YDR002W, YD8119.08 / Plasmid: pGex4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P41920
#3: Protein Exportin-1 / Chromosome region maintenance protein 1 / Karyopherin-124


Mass: 117471.922 Da / Num. of mol.: 1 / Mutation: T539C,Y1022C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: CRM1, KAP124, XPO1, YGR218W, G8514 / Plasmid: pGex4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P30822

-
Non-polymers , 6 types, 194 molecules

#4: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-6L8 / (2R)-3-{3-[3,5-bis(trifluoromethyl)phenyl]-1H-1,2,4-triazol-1-yl}-2-(pyrimidin-5-yl)propanamide


Mass: 430.307 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H12F6N6O
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 185 / 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: 2.66 Å3/Da / Density % sol: 53.8 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.6
Details: 17% PEG3350, 100mM Bis-Tris pH6.6, 200mM Ammounium Nitrate

-
Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 21, 2014
RadiationMonochromator: ROSENBAUM-ROCK HIGH-RESOLUTION DOUBLE-CRYSTAL MONOCHROMATOR
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.5→50 Å / Num. obs: 60851 / % possible obs: 99.9 % / Redundancy: 6.4 % / Biso Wilson estimate: 36.73 Å2 / Rmerge(I) obs: 0.085 / Rpim(I) all: 0.036 / Rrim(I) all: 0.093 / Χ2: 0.903 / Net I/av σ(I): 20.457 / Net I/σ(I): 7.5 / Num. measured all: 388048
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
2.5-2.546.50.8771100
2.54-2.596.50.7761100
2.59-2.646.50.7511100
2.64-2.696.40.684199.8
2.69-2.756.50.534199.9
2.75-2.826.50.4311100
2.82-2.896.50.351100
2.89-2.966.60.291100
2.96-3.056.50.2461100
3.05-3.156.50.1831100
3.15-3.266.50.1521100
3.26-3.396.50.1151100
3.39-3.556.30.1121100
3.55-3.736.30.0891100
3.73-3.976.30.071199.9
3.97-4.276.40.051100
4.27-4.76.30.046199.9
4.7-5.386.20.0421100
5.38-6.7860.0331100
6.78-505.80.018199.4

-
Processing

Software
NameVersionClassification
HKL-2000data collection
HKL-2000data scaling
PHENIX1.10.1_2155refinement
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4HB2

4hb2


Resolution: 2.5→50 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.45 / Phase error: 24.61
RfactorNum. reflection% reflection
Rfree0.232 2001 3.5 %
Rwork0.1964 --
obs0.1976 57196 93.63 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 118.52 Å2 / Biso mean: 46.6406 Å2 / Biso min: 17.37 Å2
Refinement stepCycle: final / Resolution: 2.5→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10868 0 94 185 11147
Biso mean--50.07 35.16 -
Num. residues----1345
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00811269
X-RAY DIFFRACTIONf_angle_d0.73215257
X-RAY DIFFRACTIONf_chiral_restr0.0441733
X-RAY DIFFRACTIONf_plane_restr0.0051938
X-RAY DIFFRACTIONf_dihedral_angle_d15.8546850
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5004-2.56290.3554770.26742080215751
2.5629-2.63220.27721040.24892961306572
2.6322-2.70970.27391280.27313706383489
2.7097-2.79710.29761490.24664077422698
2.7971-2.89710.25481510.245641374288100
2.8971-3.01310.28671520.243641704322100
3.0131-3.15020.31081510.243441564307100
3.1502-3.31620.28671530.231241944347100
3.3162-3.5240.24751520.226741714323100
3.524-3.7960.23581540.195342074361100
3.796-4.17780.21431530.172742214374100
4.1778-4.78190.18451530.142942674420100
4.7819-6.02310.19961580.164343094467100
6.0231-50.04520.16861660.15584539470599
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)
12.1910.321-0.08933.5070.65262.53810.01950.18920.0263-0.2010.3123-0.6496-0.33290.5223-0.36990.2234-0.08420.05790.3451-0.06080.37548.892449.068232.9384
22.8076-1.7558-3.37354.5280.11137.053-0.0518-0.1823-0.7053-0.16740.0826-0.32640.7071-0.2175-0.02210.2132-0.0332-0.04670.3763-0.1310.598411.124432.848934.973
31.2805-0.3079-1.37433.3726-1.92013.7283-0.09340.0871-0.0689-0.07690.2369-0.37340.25630.0609-0.150.14090.00020.00170.2572-0.06940.2671-0.402337.426738.3502
41.719-0.0103-2.21315.4939-1.89413.99080.03870.22820.1626-0.06110.12120.10820.04-0.2633-0.17960.1101-0.03110.00690.2372-0.03450.2293-5.859644.695337.2354
56.14580.10212.2978.10510.1824.59230.2135-0.32880.72940.5143-0.2001-0.1801-0.95150.23850.04840.39-0.15510.04980.3272-0.05410.32732.266658.723743.5265
62.16583.14633.46587.17634.78145.586-0.0605-0.0020.0187-0.51360.3562-0.3652-0.31420.9981-0.23990.5527-0.10060.08830.5749-0.05070.444110.399262.978211.5988
71.12030.06970.62391.2760.2990.39680.2248-0.3292-0.1691-0.47590.5576-0.5861-0.81530.7856-0.780.9301-0.1443-0.13670.5817-0.06920.85372.219681.743447.9232
86.7134-3.8451-0.32316.78982.44184.4811-0.0363-0.14-0.24430.13390.1020.005-0.46410.4572-0.06120.4584-0.16070.11910.34780.00440.34646.431663.438217.489
91.05941.02790.43663.75861.91242.5931-0.0081-0.06740.1965-0.4021-0.03660.0452-0.85180.53350.05650.5796-0.2030.11990.4249-0.02510.44677.051871.577716.758
101.42030.0174-0.23841.63080.50321.1179-0.0235-0.1495-0.1340.53820.2337-0.62630.2750.4614-0.16090.36440.1103-0.21530.4303-0.06050.52558.554125.931153.3956
112.3302-1.0091.21571.9236-0.52073.60440.03440.10380.14980.0163-0.0198-0.0918-0.2050.208-0.02360.1951-0.05660.01390.2302-0.05060.1434-23.427852.181150.4967
121.1252-0.5531-0.50791.32130.99672.95380.14080.14360.1115-0.3043-0.03920.0919-0.7726-0.4292-0.09610.3880.0972-0.00080.32090.0960.2324-27.782856.16359.0644
130.954-0.9181.12071.6708-1.73972.79640.12120.1012-0.3216-0.21790.04290.16180.1796-0.0333-0.15820.20620.00860.00850.2651-0.09280.3147-7.778815.821915.6416
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 66 )A9 - 66
2X-RAY DIFFRACTION2chain 'A' and (resid 67 through 80 )A67 - 80
3X-RAY DIFFRACTION3chain 'A' and (resid 81 through 109 )A81 - 109
4X-RAY DIFFRACTION4chain 'A' and (resid 110 through 158 )A110 - 158
5X-RAY DIFFRACTION5chain 'A' and (resid 159 through 179 )A159 - 179
6X-RAY DIFFRACTION6chain 'A' and (resid 180 through 216 )A180 - 216
7X-RAY DIFFRACTION7chain 'B' and (resid 65 through 82 )B65 - 82
8X-RAY DIFFRACTION8chain 'B' and (resid 83 through 106 )B83 - 106
9X-RAY DIFFRACTION9chain 'B' and (resid 107 through 200 )B107 - 200
10X-RAY DIFFRACTION10chain 'C' and (resid 0 through 268 )C0 - 268
11X-RAY DIFFRACTION11chain 'C' and (resid 269 through 520 )C269 - 520
12X-RAY DIFFRACTION12chain 'C' and (resid 521 through 826 )C521 - 826
13X-RAY DIFFRACTION13chain 'C' and (resid 827 through 1053 )C827 - 1053

+
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