[English] 日本語
Yorodumi
- PDB-4a0l: Structure of DDB1-DDB2-CUL4B-RBX1 bound to a 12 bp abasic site co... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4a0l
TitleStructure of DDB1-DDB2-CUL4B-RBX1 bound to a 12 bp abasic site containing DNA-duplex
Components
  • (DNA DAMAGE-BINDING PROTEIN ...) x 2
  • 12 BP DNA DUPLEX
  • 12 BP THF CONTAINING DNA DUPLEX
  • CULLIN-4B
  • E3 UBIQUITIN-PROTEIN LIGASE RBX1
KeywordsLIGASE/DNA-BINDING PROTEIN/DNA / LIGASE-DNA-BINDING PROTEIN-DNA COMPLEX
Function / homology
Function and homology information


Dual Incision in GG-NER / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Neddylation / Prolactin receptor signaling / Regulation of BACH1 activity / Recognition of DNA damage by PCNA-containing replication complex / Formation of TC-NER Pre-Incision Complex / DNA Damage Recognition in GG-NER / Dual Incision in GG-NER ...Dual Incision in GG-NER / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Neddylation / Prolactin receptor signaling / Regulation of BACH1 activity / Recognition of DNA damage by PCNA-containing replication complex / Formation of TC-NER Pre-Incision Complex / DNA Damage Recognition in GG-NER / Dual Incision in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Formation of Incision Complex in GG-NER / Regulation of RAS by GAPs / Regulation of RUNX2 expression and activity / Degradation of GLI1 by the proteasome / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of DVL / Orc1 removal from chromatin / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Hedgehog 'on' state / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Degradation of beta-catenin by the destruction complex / eukaryotic initiation factor 4E binding / Interleukin-1 signaling / anaphase-promoting complex / GLI3 is processed to GLI3R by the proteasome / Neddylation / cullin-RING-type E3 NEDD8 transferase / cullin-RING ubiquitin ligase complex / Cul7-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / KEAP1-NFE2L2 pathway / positive regulation by virus of viral protein levels in host cell / astrocyte differentiation / positive regulation of protein autoubiquitination / spindle assembly involved in female meiosis / RNA polymerase II transcription initiation surveillance / protein neddylation / Antigen processing: Ubiquitination & Proteasome degradation / epigenetic programming in the zygotic pronuclei / UV-damage excision repair / NEDD8 ligase activity / negative regulation of response to oxidative stress / Cul5-RING ubiquitin ligase complex / biological process involved in interaction with symbiont / SCF ubiquitin ligase complex / regulation of mitotic cell cycle phase transition / Cul2-RING ubiquitin ligase complex / negative regulation of type I interferon production / WD40-repeat domain binding / ubiquitin-ubiquitin ligase activity / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / Cul3-RING ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / negative regulation of reproductive process / negative regulation of developmental process / cullin family protein binding / viral release from host cell / site of DNA damage / protein monoubiquitination / ubiquitin ligase complex / positive regulation of G1/S transition of mitotic cell cycle / ectopic germ cell programmed cell death / positive regulation of viral genome replication / protein K48-linked ubiquitination / response to UV / proteasomal protein catabolic process / transcription-coupled nucleotide-excision repair / positive regulation of TORC1 signaling / positive regulation of gluconeogenesis / negative regulation of insulin receptor signaling pathway / T cell activation / nucleotide-excision repair / cellular response to amino acid stimulus / protein catabolic process / Recognition of DNA damage by PCNA-containing replication complex / G1/S transition of mitotic cell cycle / regulation of circadian rhythm / DNA Damage Recognition in GG-NER / RING-type E3 ubiquitin transferase / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Formation of Incision Complex in GG-NER / Wnt signaling pathway / protein polyubiquitination / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / ubiquitin-protein transferase activity / positive regulation of protein catabolic process / cellular response to UV / ubiquitin protein ligase activity / rhythmic process / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / ribosome biogenesis / site of double-strand break
Similarity search - Function
DNA damage-binding protein 2 / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Cullin protein neddylation domain / : / Cullin, conserved site / Cullin family signature. / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin ...DNA damage-binding protein 2 / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Cullin protein neddylation domain / : / Cullin, conserved site / Cullin family signature. / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Cullin / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin alpha solenoid domain / Cullin family profile. / RSE1/DDB1/CPSF1 second beta-propeller / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / : / CPSF A subunit region / RSE1/DDB1/CPSF1 first beta-propeller / Zinc finger RING-type profile. / Zinc finger, RING-type / WD domain, G-beta repeat / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / Winged helix-like DNA-binding domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
DNA / DNA (> 10) / E3 ubiquitin-protein ligase RBX1 / Cullin-4B / DNA damage-binding protein 1 / DNA damage-binding protein 2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
DANIO RERIO (zebrafish)
MUS MUSCULUS (house mouse)
SYNTHETIC CONSTRUCT (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 7.4 Å
AuthorsFischer, E.S. / Scrima, A. / Gut, H. / Thoma, N.H.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2011
Title: The Molecular Basis of Crl4(Ddb2/Csa) Ubiquitin Ligase Architecture, Targeting, and Activation.
Authors: Fischer, E.S. / Scrima, A. / Bohm, K. / Matsumoto, S. / Lingaraju, G.M. / Faty, M. / Yasuda, T. / Cavadini, S. / Wakasugi, M. / Hanaoka, F. / Iwai, S. / Gut, H. / Sugasawa, K. / Thoma, N.H.
History
DepositionSep 9, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 14, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 7, 2012Group: Database references
Revision 1.2Mar 27, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Source and taxonomy
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / entity_src_gen / pdbx_database_proc / pdbx_database_status / pdbx_seq_map_depositor_info / struct_biol / struct_conn
Item: _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_host_org_cell_line ..._entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain / _pdbx_database_status.recvd_author_approval / _pdbx_seq_map_depositor_info.one_letter_code_mod / _struct_conn.pdbx_leaving_atom_flag
Revision 1.3Apr 3, 2019Group: Data collection / Category: pdbx_seq_map_depositor_info / Item: _pdbx_seq_map_depositor_info.one_letter_code_mod
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DNA DAMAGE-BINDING PROTEIN 1
B: DNA DAMAGE-BINDING PROTEIN 2
C: DNA DAMAGE-BINDING PROTEIN 1
D: DNA DAMAGE-BINDING PROTEIN 2
E: CULLIN-4B
F: E3 UBIQUITIN-PROTEIN LIGASE RBX1
H: CULLIN-4B
I: E3 UBIQUITIN-PROTEIN LIGASE RBX1
R: 12 BP THF CONTAINING DNA DUPLEX
S: 12 BP DNA DUPLEX
T: 12 BP THF CONTAINING DNA DUPLEX
U: 12 BP DNA DUPLEX


Theoretical massNumber of molelcules
Total (without water)548,73612
Polymers548,73612
Non-polymers00
Water00
1
A: DNA DAMAGE-BINDING PROTEIN 1
B: DNA DAMAGE-BINDING PROTEIN 2
E: CULLIN-4B
F: E3 UBIQUITIN-PROTEIN LIGASE RBX1
R: 12 BP THF CONTAINING DNA DUPLEX
S: 12 BP DNA DUPLEX


Theoretical massNumber of molelcules
Total (without water)274,3686
Polymers274,3686
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11320 Å2
ΔGint-79.9 kcal/mol
Surface area123470 Å2
MethodPISA
2
C: DNA DAMAGE-BINDING PROTEIN 1
D: DNA DAMAGE-BINDING PROTEIN 2
H: CULLIN-4B
I: E3 UBIQUITIN-PROTEIN LIGASE RBX1
T: 12 BP THF CONTAINING DNA DUPLEX
U: 12 BP DNA DUPLEX


Theoretical massNumber of molelcules
Total (without water)274,3686
Polymers274,3686
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13260 Å2
ΔGint-74.5 kcal/mol
Surface area121070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)130.800, 155.840, 255.390
Angle α, β, γ (deg.)90.00, 94.17, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

-
DNA DAMAGE-BINDING PROTEIN ... , 2 types, 4 molecules ACBD

#1: Protein DNA DAMAGE-BINDING PROTEIN 1 / DDB P127 SUBUNIT / DNA DAMAGE-BINDING PROTEIN A / DDBA / DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1 / ...DDB P127 SUBUNIT / DNA DAMAGE-BINDING PROTEIN A / DDBA / DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1 / HBV X-ASSOCIATED PROTEIN 1 / XAP-1 / UV-DAMAGED DNA-BINDING FACTOR / UV-DAMAGED DNA-BINDING PROTEIN 1 / UV-DDB 1 / XPE-BINDING FACTOR / XPE-BF / XERODERMA PIGMENTOSUM GROUP E-COMPLEMENTING PROTEIN / XPCE


Mass: 127425.812 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PFASTBAC DERIVED / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q16531
#2: Protein DNA DAMAGE-BINDING PROTEIN 2 / DAMAGE-SPECIFIC DNA-BINDING PROTEIN 2


Mass: 43418.102 Da / Num. of mol.: 2 / Fragment: RESIDUES 60-423
Source method: isolated from a genetically manipulated source
Details: VARIANT WITH GLN AT POSITION 180 AND ARG AT POSITION 214 SIMILAR TO PDB ENTRY 3EI2
Source: (gene. exp.) DANIO RERIO (zebrafish) / Plasmid: PFASTBAC DERIVED / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q2YDS1

-
Protein , 2 types, 4 molecules EHFI

#3: Protein CULLIN-4B / CULLIN HOMOLOG 4B / CUL-4B


Mass: 84992.195 Da / Num. of mol.: 2 / Fragment: RESIDUES 193-913
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PFASTBAC DERIVED / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q13620
#4: Protein E3 UBIQUITIN-PROTEIN LIGASE RBX1 / RING FINGER PROTEIN 75 / RING-BOX PROTEIN 1 / RBX1


Mass: 11330.942 Da / Num. of mol.: 2 / Fragment: RESIDUES 12-108
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PFASTBAC DERIVED / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: P62878

-
DNA chain , 2 types, 4 molecules RTSU

#5: DNA chain 12 BP THF CONTAINING DNA DUPLEX


Mass: 3498.283 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others)
#6: DNA chain 12 BP DNA DUPLEX


Mass: 3702.428 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others)

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 4.6 Å3/Da / Density % sol: 73 % / Description: NONE
Crystal growpH: 6.2 / Details: 100MM MES PH 6.2, 3.1% PEG 6000, 4% ETHYLENEGLYCOL

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.0015
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 17, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0015 Å / Relative weight: 1
ReflectionResolution: 7.4→30 Å / Num. obs: 13547 / % possible obs: 97.5 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 10.2
Reflection shellResolution: 7.4→7.59 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 2.3 / % possible all: 99.1

-
Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 3EI2, 4A0C

3ei2

4a0c


Resolution: 7.4→29.862 Å / SU ML: 2.21 / σ(F): 2 / Phase error: 34.97 / Stereochemistry target values: ML
Details: THE MOLECULAR REPLACEMENT SOLUTION HAS BEEN RIGID BODY REFINED TO OBTAIN THE OVERALL ASSEMBLY OF THE COMPLEX. NO REBUILDING HAS BEEN PERFORMED DUE TO LIMITED RESOLUTION. RBX1 RESIDUES 40-108 ...Details: THE MOLECULAR REPLACEMENT SOLUTION HAS BEEN RIGID BODY REFINED TO OBTAIN THE OVERALL ASSEMBLY OF THE COMPLEX. NO REBUILDING HAS BEEN PERFORMED DUE TO LIMITED RESOLUTION. RBX1 RESIDUES 40-108 AND CUL4B RESIDUES 208-209 HAVE BEEN REMOVED DUE TO UNCERTAINTY OF CONFORMATIONS. STEREOCHEMISTRY IS BASED ON THE SEARCH MODELS 3EI2 AND 4A0C.
RfactorNum. reflection% reflection
Rfree0.3199 1352 10 %
Rwork0.3178 --
obs0.318 13523 99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 143.782 Å2 / ksol: 0.313 e/Å3
Displacement parametersBiso mean: 344 Å2
Refinement stepCycle: LAST / Resolution: 7.4→29.862 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms34587 966 0 0 35553
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00836315
X-RAY DIFFRACTIONf_angle_d1.23349309
X-RAY DIFFRACTIONf_dihedral_angle_d18.54513521
X-RAY DIFFRACTIONf_chiral_restr0.0835617
X-RAY DIFFRACTIONf_plane_restr0.0066162
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
7.4001-7.66030.39251340.38471202X-RAY DIFFRACTION99
7.6603-7.96150.37981340.39381206X-RAY DIFFRACTION99
7.9615-8.31640.42031320.36611198X-RAY DIFFRACTION99
8.3164-8.74440.33541370.36151241X-RAY DIFFRACTION99
8.7444-9.27680.33671340.34821205X-RAY DIFFRACTION99
9.2768-9.96830.27981340.31061206X-RAY DIFFRACTION99
9.9683-10.92650.30091360.27061219X-RAY DIFFRACTION99
10.9265-12.40730.23791340.25571205X-RAY DIFFRACTION99
12.4073-15.27540.30221370.26621234X-RAY DIFFRACTION99
15.2754-29.86230.35971400.37051255X-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)
12.16092.75872.21584.06970.87253.06240.40510.1255-0.340.69880.14120.0398-0.1921-0.4892-0.41971.64320.09560.67292.3331-0.06111.64669.0148-1.741427.691
23.89641.0343-0.47680.62480.00954.6669-0.8249-1.3288-0.7139-0.1346-0.61490.972-0.39220.06081.10214.5984-0.8239-0.76513.73710.49633.193829.28362.088178.0278
32.16671.0471.73693.6670.97351.82660.10940.4382-0.57330.10550.07220.5298-0.1616-0.3858-0.07351.711-0.06950.82122.53060.09161.3205-40.783758.30922.5275
42.0569-1.31091.47495.76832.74933.55641.1303-1.1532-0.69230.70350.31160.53681.951-1.1286-1.29542.332-0.5710.08552.28010.46471.9873-12.355562.868469.1982
50.09150.8887-0.14221.4119-0.2719-0.0962-0.892-1.56180.23882.21090.5971-0.4475-1.3757-0.7753-0.25623.72930.43480.25043.7199-0.47772.1247-6.1137-53.088175.563
61.81390.4156-0.33791.0881-0.81660.11160.1779-0.99410.27291.1918-0.1075-0.0393-0.4284-0.2648-0.14884.4176-0.4538-0.41723.2456-0.10552.948-71.975931.482677.202
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A
2X-RAY DIFFRACTION2CHAIN B OR CHAIN R OR CHAIN S
3X-RAY DIFFRACTION3CHAIN C
4X-RAY DIFFRACTION4CHAIN D OR CHAIN T OR CHAIN U
5X-RAY DIFFRACTION5CHAIN E OR CHAIN F
6X-RAY DIFFRACTION6CHAIN H OR CHAIN I

+
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