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- PDB-7mni: Crystal structure of the N-terminal domain of NUP88 in complex wi... -

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Basic information

Entry
Database: PDB / ID: 7mni
TitleCrystal structure of the N-terminal domain of NUP88 in complex with NUP98 C-terminal Autoproteolytic Domain
Components
  • Nuclear pore complex protein Nup88Nuclear pore
  • Nuclear pore complex protein Nup98Nuclear pore
KeywordsTRANSPORT PROTEIN / nuclear pore complex component / nucleocytoplasmic transport
Function / homology
Function and homology information


transporter activity / nuclear pore organization / nuclear pore outer ring / nuclear pore complex assembly / Nuclear Pore Complex (NPC) Disassembly / nuclear inclusion body / nuclear pore nuclear basket / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) ...transporter activity / nuclear pore organization / nuclear pore outer ring / nuclear pore complex assembly / Nuclear Pore Complex (NPC) Disassembly / nuclear inclusion body / nuclear pore nuclear basket / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / Transport of Mature mRNA Derived from an Intronless Transcript / structural constituent of nuclear pore / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / Nuclear import of Rev protein / positive regulation of mRNA splicing, via spliceosome / Transport of Mature mRNA derived from an Intron-Containing Transcript / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / Viral Messenger RNA Synthesis / nuclear localization sequence binding / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / SUMOylation of DNA replication proteins / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / ribosomal large subunit export from nucleus / Regulation of HSF1-mediated heat shock response / mRNA transport / ribosomal small subunit export from nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / mRNA export from nucleus / SUMOylation of DNA damage response and repair proteins / nuclear pore / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / serine-type peptidase activity / SUMOylation of chromatin organization proteins / nuclear periphery / HCMV Late Events / RHO GTPases Activate Formins / promoter-specific chromatin binding / Transcriptional regulation by small RNAs / ISG15 antiviral mechanism / HCMV Early Events / protein import into nucleus / Separation of Sister Chromatids / nuclear envelope / snRNP Assembly / nuclear membrane / transcription coactivator activity / nuclear body / ribonucleoprotein complex / mRNA binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / nucleoplasm / cytosol
Similarity search - Function
Nucleoporin Nup88 / Nuclear pore component / Nucleoporin NUP88/NUP82 / Nuclear pore complex protein NUP98-NUP96 / Nuclear pore complex protein NUP96, C-terminal domain / Nuclear protein 96 / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain superfamily / Nucleoporin autopeptidase / NUP C-terminal domain profile. / Nucleoporin peptidase S59-like
Similarity search - Domain/homology
Nuclear pore complex protein Nup98-Nup96 / Nuclear pore complex protein Nup88
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsBley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. ...Bley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. / Brown, B. / Tang, A.W. / Rundlet, E.J. / Correia, A.R. / Chen, S. / Regmi, S.G. / Stevens, T.A. / Jette, C.A. / Dasso, M. / Patke, A. / Palazzo, A.F. / Kossiakoff, A.A. / Hoelz, A.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM117360 United States
Howard Hughes Medical Institute (HHMI)55108534 United States
Heritage Medical Research Institute United States
CitationJournal: Science / Year: 2022
Title: Architecture of the cytoplasmic face of the nuclear pore.
Authors: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / ...Authors: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / Emily J Rundlet / Ana R Correia / Shane Chen / Saroj G Regmi / Taylor A Stevens / Claudia A Jette / Mary Dasso / Alina Patke / Alexander F Palazzo / Anthony A Kossiakoff / André Hoelz /
Abstract: INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are ...INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are generated by the circumscribed fusion of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) are the sole bidirectional gateways for nucleocytoplasmic transport. The ~110-MDa human NPC is an ~1000-protein assembly that comprises multiple copies of ~34 different proteins, collectively termed nucleoporins. The symmetric core of the NPC is composed of an inner ring encircling the central transport channel and outer rings formed by Y‑shaped coat nucleoporin complexes (CNCs) anchored atop both sides of the nuclear envelope. The outer rings are decorated with compartment‑specific asymmetric nuclear basket and cytoplasmic filament nucleoporins, which establish transport directionality and provide docking sites for transport factors and the small guanosine triphosphatase Ran. The cytoplasmic filament nucleoporins also play an essential role in the irreversible remodeling of messenger ribonucleoprotein particles (mRNPs) as they exit the central transport channel. Unsurprisingly, the NPC's cytoplasmic face represents a hotspot for disease‑associated mutations and is commonly targeted by viral virulence factors. RATIONALE Previous studies established a near-atomic composite structure of the human NPC's symmetric core by combining (i) biochemical reconstitution to elucidate the interaction network between symmetric nucleoporins, (ii) crystal and single-particle cryo-electron microscopy structure determination of nucleoporins and nucleoporin complexes to reveal their three-dimensional shape and the molecular details of their interactions, (iii) quantitative docking in cryo-electron tomography (cryo-ET) maps of the intact human NPC to uncover nucleoporin stoichiometry and positioning, and (iv) cell‑based assays to validate the physiological relevance of the biochemical and structural findings. In this work, we extended our approach to the cytoplasmic filament nucleoporins to reveal the near-atomic architecture of the cytoplasmic face of the human NPC. RESULTS Using biochemical reconstitution, we elucidated the protein-protein and protein-RNA interaction networks of the human and cytoplasmic filament nucleoporins, establishing an evolutionarily conserved heterohexameric cytoplasmic filament nucleoporin complex (CFNC) held together by a central heterotrimeric coiled‑coil hub that tethers two separate mRNP‑remodeling complexes. Further biochemical analysis and determination of a series of crystal structures revealed that the metazoan‑specific cytoplasmic filament nucleoporin NUP358 is composed of 16 distinct domains, including an N‑terminal S‑shaped α‑helical solenoid followed by a coiled‑coil oligomerization element, numerous Ran‑interacting domains, an E3 ligase domain, and a C‑terminal prolyl‑isomerase domain. Physiologically validated quantitative docking into cryo-ET maps of the intact human NPC revealed that pentameric NUP358 bundles, conjoined by the oligomerization element, are anchored through their N‑terminal domains to the central stalk regions of the CNC, projecting flexibly attached domains as far as ~600 Å into the cytoplasm. Using cell‑based assays, we demonstrated that NUP358 is dispensable for the architectural integrity of the assembled interphase NPC and RNA export but is required for efficient translation. After NUP358 assignment, the remaining 4-shaped cryo‑ET density matched the dimensions of the CFNC coiled‑coil hub, in close proximity to an outer-ring NUP93. Whereas the N-terminal NUP93 assembly sensor motif anchors the properly assembled related coiled‑coil channel nucleoporin heterotrimer to the inner ring, biochemical reconstitution confirmed that the NUP93 assembly sensor is reused in anchoring the CFNC to the cytoplasmic face of the human NPC. By contrast, two CFNCs are anchored by a divergent mechanism that involves assembly sensors located in unstructured portions of two CNC nucleoporins. Whereas unassigned cryo‑ET density occupies the NUP358 and CFNC binding sites on the nuclear face, docking of the nuclear basket component ELYS established that the equivalent position on the cytoplasmic face is unoccupied, suggesting that mechanisms other than steric competition promote asymmetric distribution of nucleoporins. CONCLUSION We have substantially advanced the biochemical and structural characterization of the asymmetric nucleoporins' architecture and attachment at the cytoplasmic and nuclear faces of the NPC. Our near‑atomic composite structure of the human NPC's cytoplasmic face provides a biochemical and structural framework for elucidating the molecular basis of mRNP remodeling, viral virulence factor interference with NPC function, and the underlying mechanisms of nucleoporin diseases at the cytoplasmic face of the NPC. [Figure: see text].
History
DepositionMay 1, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 15, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 22, 2022Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Nuclear pore complex protein Nup88
B: Nuclear pore complex protein Nup98
C: Nuclear pore complex protein Nup88
D: Nuclear pore complex protein Nup98


Theoretical massNumber of molelcules
Total (without water)143,7934
Polymers143,7934
Non-polymers00
Water7,512417
1
A: Nuclear pore complex protein Nup88
B: Nuclear pore complex protein Nup98


Theoretical massNumber of molelcules
Total (without water)71,8972
Polymers71,8972
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2390 Å2
ΔGint-2 kcal/mol
Surface area26340 Å2
MethodPISA
2
C: Nuclear pore complex protein Nup88
D: Nuclear pore complex protein Nup98


Theoretical massNumber of molelcules
Total (without water)71,8972
Polymers71,8972
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2430 Å2
ΔGint-3 kcal/mol
Surface area26670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.748, 72.085, 73.042
Angle α, β, γ (deg.)92.530, 103.690, 100.390
Int Tables number1
Space group name H-MP1

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Components

#1: Protein Nuclear pore complex protein Nup88 / Nuclear pore / 88 kDa nucleoporin / Nucleoporin Nup88


Mass: 54634.992 Da / Num. of mol.: 2 / Fragment: N-terminal domain of NUP88 (UNP residues 1-493)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NUP88 / Production host: Escherichia coli (E. coli) / References: UniProt: Q99567
#2: Protein Nuclear pore complex protein Nup98 / Nuclear pore


Mass: 17261.568 Da / Num. of mol.: 2
Fragment: NUP98 C-terminal Autoproteolytic Domain (UNP residues 715-863)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NUP98, ADAR2 / Production host: Escherichia coli (E. coli)
References: UniProt: P52948-2, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 417 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.08 Å3/Da / Density % sol: 40.93 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8.3
Details: 20% w/v PEG4000, 0.22 M sodium chloride, 0.1 M Tris

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.00003 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 7, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00003 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. obs: 76633 / % possible obs: 97.8 % / Redundancy: 6 % / CC1/2: 0.996 / Rmerge(I) obs: 0.131 / Rpim(I) all: 0.056 / Rrim(I) all: 0.143 / Net I/σ(I): 7.5 / Num. measured all: 456229 / Scaling rejects: 251
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2-2.043.60.9841618244720.5130.6041.1571.396.6
10-2070.07837765410.9950.0310.0842386.4

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Processing

Software
NameVersionClassification
Aimless0.7.4data scaling
PHENIX1.17.1refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entries 5CWW & 1KO6

5cww

1ko6


Resolution: 2→20 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 23.23 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2084 3639 4.76 %
Rwork0.1752 72850 -
obs0.1767 76489 97.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 191.54 Å2 / Biso mean: 61.7063 Å2 / Biso min: 21.4 Å2
Refinement stepCycle: final / Resolution: 2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8852 0 0 418 9270
Biso mean---49.12 -
Num. residues----1121
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 26

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2-2.030.35251410.2962761290296
2.03-2.050.29851460.28712758290496
2.05-2.080.311340.27992762289696
2.08-2.110.30791490.27382733288296
2.11-2.150.30721540.25682728288296
2.15-2.180.31881610.24882783294497
2.18-2.220.24651290.24492771290097
2.22-2.260.27281350.23362726286197
2.26-2.30.26061630.232808297197
2.3-2.350.26341480.22692772292098
2.35-2.40.26191520.2252797294997
2.4-2.460.26461350.22082780291598
2.46-2.520.23251230.21632850297398
2.52-2.590.22791270.20852815294298
2.59-2.660.26231490.20842792294198
2.66-2.750.25681490.20262796294598
2.75-2.850.2341300.2012863299398
2.85-2.960.26151300.20082812294298
2.96-3.090.25221600.19332770293098
3.09-3.260.21491370.17342858299599
3.26-3.460.1621300.15772866299699
3.46-3.730.16221430.14542825296899
3.73-4.10.17141160.13522842295899
4.1-4.680.1451390.1132850298999
4.68-5.880.15111360.12762873300999
5.88-200.20181230.17352859298299
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)
15.15530.76910.99463.49471.3642.92550.0622-0.15260.30090.2771-0.18560.59690.1162-0.36120.11630.2933-0.03740.02970.2852-0.05580.4523-45.5489-6.1972-35.4936
23.5361.84321.19722.25340.86971.47660.00640.0583-0.1553-0.03450.0409-0.16710.220.0336-0.05340.30060.02960.00880.21950.0070.337-27.9147-9.2881-38.7434
31.43950.52380.23331.7267-0.15172.831-0.0419-0.0732-0.0810.0467-0.0875-0.3712-0.02340.4330.16170.2480.0324-0.050.33390.02520.4239-11.97394.2565-30.5227
44.47750.22211.04044.5657-0.23872.79250.0064-0.128-0.19150.1466-0.01080.2089-0.1734-0.21570.03470.3770.0464-0.03660.2784-0.05310.3295-25.58312.995-21.9112
52.68161.50390.57224.38571.16572.15250.0667-0.05480.19580.2916-0.15380.2891-0.0417-0.14180.09290.37220.0570.02180.3281-0.03050.3836-35.349712.9218-25.345
64.0497-0.2864-0.02645.7271-1.22954.4140.07690.8184-0.4217-0.4713-0.6871-1.27930.66690.91550.51210.63910.11140.05360.76370.1680.68456.9463-20.8554.709
74.0052-0.0189-0.08588.9705-3.74866.54610.0820.4835-0.2162-0.242-0.3423-0.30970.24270.08940.17770.4143-0.0603-0.11510.57770.19850.5598-2.024-16.67955.2267
85.6509-1.07350.33155.5104-0.02613.9480.02941.6859-0.2935-1.1472-0.24640.29490.43970.54120.28510.92630.0937-0.06111.00590.00470.444-3.3855-17.8629-7.2293
91.1907-0.21581.27984.602-2.3292.79730.2162-0.2115-0.2106-0.0008-0.5195-0.41910.09020.25990.26070.4383-0.0173-0.10960.47250.07690.57-9.0696-3.9099-3.8524
102.0109-0.2566-0.12348.3375-2.51682.92360.176-0.3341-0.00120.53740.15670.9531-0.3506-0.409-0.28720.5780.0157-0.18790.58320.08730.6357-14.4806-0.3265-0.0393
113.48340.9475-0.26663.64311.14182.43090.0566-0.01270.43130.1333-0.04190.1018-0.08080.0256-0.02520.2658-0.020.01930.2520.00440.3446-15.44-29.073628.4259
122.57021.43190.71223.17380.9791.6577-0.11420.19560.0175-0.21210.1467-0.30470.0040.11130.00570.2567-0.00680.05840.31470.00120.2865-10.4921-41.060419.4719
131.45470.20260.2071.5238-0.41692.4236-0.03540.2325-0.1441-0.45210.0668-0.12310.1044-0.094-0.03240.3812-0.06350.04460.3286-0.06770.1969-21.2942-54.75678.7499
143.54211.36390.40822.98691.16923.7973-0.0340.07050.0385-0.21110.23540.23330.1331-0.3239-0.14070.2963-0.0691-0.02810.44560.01890.2963-38.8605-50.96813.5648
153.55061.71220.69973.13080.61881.7795-0.02170.11750.1401-0.04910.03890.1860.0618-0.2112-0.03940.27870.03090.04260.4019-0.00280.3266-35.7839-41.272825.3875
162.1198-0.4647-0.1823.6869-3.36484.7896-0.06720.39560.0415-0.2654-0.1847-0.51520.52450.39860.14170.40.05180.01050.3850.02340.423-31.6477-40.0783-34.5224
173.8090.5647-0.87144.1398-2.45015.49970.1219-0.08360.4180.354-0.072-0.1458-0.4291-0.1182-0.08120.31760.0270.00730.2444-0.03050.2785-34.7231-33.8028-29.3016
185.99871.6653-1.47195.44-1.09734.60970.3917-0.61-0.25030.7283-0.5564-0.68570.21870.69270.16760.50330.0144-0.08880.4850.05460.438-26.8116-39.5073-19.4202
192.16560.918-0.3564.3185-3.75735.0570.1063-0.2518-0.03680.1858-0.0147-0.347-0.2023-0.3469-0.06630.3897-0.02160.03180.395-0.05240.2793-36.9335-40.2465-12.5649
202.88450.4906-1.04824.2921-1.99334.21580.3417-0.78570.28420.55330.24460.7576-0.4964-0.7996-0.51260.53170.00760.07680.82920.04470.3614-44.1524-38.2649-8.1924
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 13 through 98 )A13 - 98
2X-RAY DIFFRACTION2chain 'A' and (resid 99 through 203 )A99 - 203
3X-RAY DIFFRACTION3chain 'A' and (resid 204 through 303 )A204 - 303
4X-RAY DIFFRACTION4chain 'A' and (resid 304 through 404 )A304 - 404
5X-RAY DIFFRACTION5chain 'A' and (resid 405 through 493 )A405 - 493
6X-RAY DIFFRACTION6chain 'B' and (resid 714 through 741 )B714 - 741
7X-RAY DIFFRACTION7chain 'B' and (resid 742 through 766 )B742 - 766
8X-RAY DIFFRACTION8chain 'B' and (resid 767 through 791 )B767 - 791
9X-RAY DIFFRACTION9chain 'B' and (resid 792 through 821 )B792 - 821
10X-RAY DIFFRACTION10chain 'B' and (resid 822 through 863 )B822 - 863
11X-RAY DIFFRACTION11chain 'C' and (resid 12 through 108 )C12 - 108
12X-RAY DIFFRACTION12chain 'C' and (resid 109 through 187 )C109 - 187
13X-RAY DIFFRACTION13chain 'C' and (resid 188 through 290 )C188 - 290
14X-RAY DIFFRACTION14chain 'C' and (resid 291 through 372 )C291 - 372
15X-RAY DIFFRACTION15chain 'C' and (resid 373 through 493 )C373 - 493
16X-RAY DIFFRACTION16chain 'D' and (resid 714 through 738 )D714 - 738
17X-RAY DIFFRACTION17chain 'D' and (resid 739 through 768 )D739 - 768
18X-RAY DIFFRACTION18chain 'D' and (resid 769 through 789 )D769 - 789
19X-RAY DIFFRACTION19chain 'D' and (resid 790 through 821 )D790 - 821
20X-RAY DIFFRACTION20chain 'D' and (resid 822 through 863 )D822 - 863

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  • 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

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