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- PDB-6o61: Tubulin-RB3_SLD-TTL in complex with compound ABI-231 -

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Basic information

Entry
Database: PDB / ID: 6o61
TitleTubulin-RB3_SLD-TTL in complex with compound ABI-231
Components
  • Stathmin-4
  • Tubulin Tyrosine Ligase
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE / Microtubule Inhibitor / Colchicine / Cancer
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Resolution of Sister Chromatid Cohesion / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Mitotic Prometaphase / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle ...tubulin-tyrosine ligase activity / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Resolution of Sister Chromatid Cohesion / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Mitotic Prometaphase / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / EML4 and NUDC in mitotic spindle formation / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / Aggrephagy / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / microtubule depolymerization / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / COPI-mediated anterograde transport / regulation of microtubule polymerization or depolymerization / microtubule-based process / tubulin binding / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / microtubule cytoskeleton / growth cone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / neuron projection / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Helix non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Chem-KUM / Tubulin beta chain / Tubulin tyrosine ligase / Tubulin beta chain / Tubulin alpha-1B chain / Stathmin-4
Similarity search - Component
Biological speciesHomo sapiens (human)
Gallus gallus (chicken)
Sus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.599 Å
AuthorsKumar, G. / Wang, Y. / Li, W. / White, S.W.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)R01CA148706 United States
CitationJournal: J.Med.Chem. / Year: 2019
Title: Structure-Guided Design, Synthesis, and Biological Evaluation of (2-(1H-Indol-3-yl)-1H-imidazol-4-yl)(3,4,5-trimethoxyphenyl) Methanone (ABI-231) Analogues Targeting the Colchicine Binding Site in Tubulin.
Authors: Wang, Q. / Arnst, K.E. / Wang, Y. / Kumar, G. / Ma, D. / White, S.W. / Miller, D.D. / Li, W. / Li, W.
History
DepositionMar 5, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 10, 2019Provider: repository / Type: Initial release
Revision 1.1Jul 31, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Aug 7, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Mar 13, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tubulin alpha-1B chain
B: Tubulin beta-2B chain
C: Tubulin alpha-1B chain
D: Tubulin beta-2B chain
E: Stathmin-4
F: Tubulin Tyrosine Ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,04120
Polymers261,3056
Non-polymers3,73614
Water4,216234
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)105.257, 157.092, 184.039
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain B and (resid 2 through 21 or (resid 22...
21(chain D and (resid 2 through 32 or (resid 33...
12(chain A and (resid 1 through 72 or (resid 73...
22(chain C and (resid 1 through 87 or (resid 88...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ARGARGTRPTRP(chain B and (resid 2 through 21 or (resid 22...BB2 - 212 - 21
121GLUGLUGLUGLU(chain B and (resid 2 through 21 or (resid 22...BB2222
131ARGARGALAALA(chain B and (resid 2 through 21 or (resid 22...BB2 - 4282 - 428
141ARGARGALAALA(chain B and (resid 2 through 21 or (resid 22...BB2 - 4282 - 428
151ARGARGALAALA(chain B and (resid 2 through 21 or (resid 22...BB2 - 4282 - 428
161ARGARGALAALA(chain B and (resid 2 through 21 or (resid 22...BB2 - 4282 - 428
211ARGARGPROPRO(chain D and (resid 2 through 32 or (resid 33...DD2 - 322 - 32
221THRTHRTHRTHR(chain D and (resid 2 through 32 or (resid 33...DD3333
231METMETASPASP(chain D and (resid 2 through 32 or (resid 33...DD1 - 4311 - 431
241METMETASPASP(chain D and (resid 2 through 32 or (resid 33...DD1 - 4311 - 431
251METMETASPASP(chain D and (resid 2 through 32 or (resid 33...DD1 - 4311 - 431
112METMETPROPRO(chain A and (resid 1 through 72 or (resid 73...AA1 - 721 - 72
122THRTHRTHRTHR(chain A and (resid 1 through 72 or (resid 73...AA7373
132METMETVALVAL(chain A and (resid 1 through 72 or (resid 73...AA1 - 4371 - 437
142METMETVALVAL(chain A and (resid 1 through 72 or (resid 73...AA1 - 4371 - 437
152METMETVALVAL(chain A and (resid 1 through 72 or (resid 73...AA1 - 4371 - 437
162METMETVALVAL(chain A and (resid 1 through 72 or (resid 73...AA1 - 4371 - 437
212METMETPHEPHE(chain C and (resid 1 through 87 or (resid 88...CC1 - 871 - 87
222HISHISHISHIS(chain C and (resid 1 through 87 or (resid 88...CC8888
232METMETMGMG(chain C and (resid 1 through 87 or (resid 88...CC - P1 - 5021

NCS ensembles :
ID
1
2

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Components

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Protein , 4 types, 6 molecules ACBDEF

#1: Protein Tubulin alpha-1B chain / Alpha-tubulin ubiquitous / Tubulin K-alpha-1 / Tubulin alpha-ubiquitous chain


Mass: 50041.273 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q2XVP4
#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A0A287AGU7, UniProt: P02554*PLUS
#3: Protein Stathmin-4 / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: STMN4 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H169
#4: Protein Tubulin Tyrosine Ligase


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 8 types, 248 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#9: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#10: Chemical ChemComp-KUM / [2-(1H-indol-3-yl)-1H-imidazol-5-yl](3,4,5-trimethoxyphenyl)methanone


Mass: 377.393 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H19N3O4 / Feature type: SUBJECT OF INVESTIGATION
#11: Chemical ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H18N5O12P3 / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 234 / 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: 2.91 Å3/Da / Density % sol: 57.75 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 6% PEG 4000, 5% Glycerol, 0.1 M MES, 30 mM CaCl2, 30 mM MgCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97853 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 20, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97853 Å / Relative weight: 1
ReflectionResolution: 2.599→50 Å / Num. obs: 93639 / % possible obs: 99.2 % / Redundancy: 6.8 % / Biso Wilson estimate: 42.09 Å2 / Rmerge(I) obs: 0.107 / Rpim(I) all: 0.044 / Rrim(I) all: 0.116 / Χ2: 1.038 / Net I/σ(I): 4.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.6-2.666.90.89461880.7080.3610.9651.10799.5
2.66-2.736.90.80961310.7460.3260.8741.15199.1
2.73-2.86.90.65662160.8080.2660.7091.12299.7
2.8-2.886.90.51662040.8740.2090.5571.10999.6
2.88-2.986.80.42462140.9050.1730.4591.1199.8
2.98-3.086.80.32862150.9410.1350.3551.12799.8
3.08-3.216.40.25362530.9550.1080.2761.12299.6
3.21-3.356.70.20159830.9720.0830.2171.16396.3
3.35-3.537.10.1662460.9830.0640.1721.18499.9
3.53-3.757.10.12862820.9880.0510.1381.165100
3.75-4.0470.10163110.9910.0410.1091.097100
4.04-4.456.80.07962930.9940.0320.0850.921100
4.45-5.096.50.06961600.9940.0290.0750.84597.1
5.09-6.4170.06864050.9950.0270.0730.703100
6.41-506.50.04865380.9970.020.0530.64298

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIX(1.13_2998: ???)refinement
PDB_EXTRACT3.24data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.599→48.163 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.81
RfactorNum. reflection% reflection
Rfree0.2435 4620 4.99 %
Rwork0.2042 --
obs0.2061 92580 98.03 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 159.1 Å2 / Biso mean: 55.0797 Å2 / Biso min: 10.9 Å2
Refinement stepCycle: final / Resolution: 2.599→48.163 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16688 0 236 234 17158
Biso mean--55.85 40.72 -
Num. residues----2162
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11B2655X-RAY DIFFRACTION8.364TORSIONAL
12D2655X-RAY DIFFRACTION8.364TORSIONAL
21A2519X-RAY DIFFRACTION8.364TORSIONAL
22C2519X-RAY DIFFRACTION8.364TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5995-2.6290.33641430.29392499264283
2.629-2.65990.29671400.28362689282992
2.6599-2.69240.29611400.27712842298295
2.6924-2.72640.33861530.27622837299097
2.7264-2.76230.28661490.26942957310699
2.7623-2.80020.31741540.27542928308299
2.8002-2.84020.31761520.268829693121100
2.8402-2.88250.3311480.25692932308099
2.8825-2.92760.27171490.255529573106100
2.9276-2.97560.34741620.253429463108100
2.9756-3.02690.29381540.234829573111100
3.0269-3.08190.24591760.228829363112100
3.0819-3.14120.30011670.230529673134100
3.1412-3.20530.24861600.234129643124100
3.2053-3.2750.28121210.23772773289493
3.275-3.35110.27251400.23152949308999
3.3511-3.43490.27441630.219329583121100
3.4349-3.52770.26271620.204429723134100
3.5277-3.63150.20791620.192729803142100
3.6315-3.74870.24311580.191629803138100
3.7487-3.88260.23651350.176930073142100
3.8826-4.0380.21771620.171430003162100
4.038-4.22170.18681610.168629853146100
4.2217-4.44410.23071520.164229853137100
4.4441-4.72230.20691800.15822955313599
4.7223-5.08660.21571640.16452862302695
5.0866-5.59770.23111360.189830623198100
5.5977-6.40610.2291660.208230213187100
6.4061-8.06490.23841360.19763096323299
8.0649-48.17160.17821750.18112995317094
Refinement TLS params.Method: refined / Origin x: 17.204 Å / Origin y: -44.146 Å / Origin z: -25.806 Å
111213212223313233
T0.0683 Å2-0.0217 Å2-0.0079 Å2-0.2744 Å2-0.032 Å2--0.368 Å2
L0.2105 °20.0463 °20.1855 °2-0.8027 °20.7134 °2--1.2384 °2
S-0.0647 Å °-0.0171 Å °-0.0143 Å °-0.0404 Å °0.1241 Å °-0.0083 Å °-0.052 Å °0.1007 Å °-0.0392 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )A1 - 437
2X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )A501 - 502
3X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )A503
4X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )C1 - 440
5X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )C501 - 502
6X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )C503
7X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )B2 - 428
8X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )B501 - 502
9X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )B505
10X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )E6 - 141
11X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )D1 - 431
12X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )D501
13X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )D502
14X-RAY DIFFRACTION1( CHAIN A AND ( RESID 1:437 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN C AND ( RESID 1:440 OR RESID 501:502 OR RESID 503:503 ) ) OR ( CHAIN B AND ( RESID 2:428 OR RESID 501:502 OR RESID 505:505 ) ) OR ( CHAIN E AND RESID 6:141 ) OR ( CHAIN D AND ( RESID 1:431 OR RESID 501:501 OR RESID 502:502 ) ) OR ( CHAIN F AND RESID 1:380 )F1 - 380

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