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- PDB-6mzf: Structural Basis of Tubulin Recruitment and Assembly by Microtubu... -

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Basic information

Entry
Database: PDB / ID: 6mzf
TitleStructural Basis of Tubulin Recruitment and Assembly by Microtubule Polymerases with Tumor Overexpressed Gene (TOG) Domain Arrays
Components
  • Designed ankyrin repeat protein (DARPIN) D1
  • Protein Stu2p/Alp14p
  • Tubulin alpha-1A chain
  • Tubulin beta chain
KeywordsCELL CYCLE / Microtubule / Tubulin / Tubulin polymerization / Heat repeats / Microtubule polymerase / TOG arrays / and Wheel-like assembly.
Function / homology
Function and homology information


supramolecular complex / microtubule plus end polymerase / establishment or maintenance of microtubule cytoskeleton polarity / microtubule plus-end binding / motile cilium / spindle organization / microtubule polymerization / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration ...supramolecular complex / microtubule plus end polymerase / establishment or maintenance of microtubule cytoskeleton polarity / microtubule plus-end binding / motile cilium / spindle organization / microtubule polymerization / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / mitotic cell cycle / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cytoskeleton / hydrolase activity / GTPase activity / GTP binding / metal ion binding / cytoplasm
Similarity search - Function
XMAP215 family / : / XMAP215/Dis1/CLASP, TOG domain / TOG domain / TOG / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin ...XMAP215 family / : / XMAP215/Dis1/CLASP, TOG domain / TOG domain / TOG / 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 / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Protein Stu2p/Alp14p / Tubulin alpha-1A chain / Tubulin beta chain
Similarity search - Component
Biological speciesLachancea kluyveri NRRL Y-12651 (fungus)
Escherichia coli (E. coli)
Sus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.4 Å
AuthorsNithianantham, S. / Al-Bassam, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM110283 United States
CitationJournal: Elife / Year: 2018
Title: Structural basis of tubulin recruitment and assembly by microtubule polymerases with Tumor Overexpressed Gene (TOG) domain arrays.
Authors: Nithianantham, S. / Cook, B.D. / Beans, M. / Guo, F. / Chang, F. / Al-Bassam, J.
History
DepositionNov 5, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 28, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Mar 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_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_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.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_label_asym_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

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Assembly

Deposited unit
A: Tubulin alpha-1A chain
B: Tubulin beta chain
C: Tubulin alpha-1A chain
D: Tubulin beta chain
E: Protein Stu2p/Alp14p
F: Designed ankyrin repeat protein (DARPIN) D1
G: Designed ankyrin repeat protein (DARPIN) D1
H: Tubulin alpha-1A chain
I: Tubulin beta chain
J: Tubulin alpha-1A chain
K: Tubulin beta chain
L: Protein Stu2p/Alp14p
M: Designed ankyrin repeat protein (DARPIN) D1
N: Designed ankyrin repeat protein (DARPIN) D1
O: Tubulin alpha-1A chain
P: Tubulin beta chain
Q: Tubulin alpha-1A chain
R: Tubulin beta chain
S: Protein Stu2p/Alp14p
T: Designed ankyrin repeat protein (DARPIN) D1
U: Designed ankyrin repeat protein (DARPIN) D1
V: Tubulin alpha-1A chain
W: Tubulin beta chain
X: Tubulin alpha-1A chain
Y: Tubulin beta chain
Z: Protein Stu2p/Alp14p
a: Designed ankyrin repeat protein (DARPIN) D1
b: Designed ankyrin repeat protein (DARPIN) D1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,205,29760
Polymers1,197,17728
Non-polymers8,12032
Water00
1
A: Tubulin alpha-1A chain
B: Tubulin beta chain
C: Tubulin alpha-1A chain
D: Tubulin beta chain
E: Protein Stu2p/Alp14p
F: Designed ankyrin repeat protein (DARPIN) D1
G: Designed ankyrin repeat protein (DARPIN) D1
H: Tubulin alpha-1A chain
I: Tubulin beta chain
J: Tubulin alpha-1A chain
K: Tubulin beta chain
L: Protein Stu2p/Alp14p
M: Designed ankyrin repeat protein (DARPIN) D1
N: Designed ankyrin repeat protein (DARPIN) D1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)602,64830
Polymers598,58814
Non-polymers4,06016
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
O: Tubulin alpha-1A chain
P: Tubulin beta chain
Q: Tubulin alpha-1A chain
R: Tubulin beta chain
S: Protein Stu2p/Alp14p
T: Designed ankyrin repeat protein (DARPIN) D1
U: Designed ankyrin repeat protein (DARPIN) D1
V: Tubulin alpha-1A chain
W: Tubulin beta chain
X: Tubulin alpha-1A chain
Y: Tubulin beta chain
Z: Protein Stu2p/Alp14p
a: Designed ankyrin repeat protein (DARPIN) D1
b: Designed ankyrin repeat protein (DARPIN) D1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)602,64830
Polymers598,58814
Non-polymers4,06016
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)218.800, 107.650, 282.740
Angle α, β, γ (deg.)90.000, 90.380, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain C
31chain H
41chain J
51chain O
61chain Q
71chain V
81chain X
12chain B
22chain D
32chain I
42chain K
52chain P
62chain R
72chain W
82chain Y
13chain E
23(chain L and (resid 14 through 262 or resid 300 through 543))
33(chain S and (resid 14 through 262 or resid 300 through 543))
43(chain Z and (resid 14 through 262 or resid 300 through 543))
14(chain F and (resid 13 through 149 or (resid 150...
24(chain G and (resid 13 through 149 or (resid 150...
34(chain M and (resid 13 through 149 or (resid 150...
44(chain N and (resid 13 through 149 or (resid 150...
54(chain T and (resid 13 through 149 or (resid 150...
64(chain U and (resid 13 through 149 or (resid 150...
74chain a
84(chain b and (resid 13 through 149 or (resid 150...

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
111ARGARGMGMGchain AAA - DA2 - 6012
211ARGARGMGMGchain CCC - HA2 - 6012
311ARGARGMGMGchain HHH - LA2 - 6012
411ARGARGMGMGchain JJJ - PA2 - 6012
511ARGARGMGMGchain OOO - TA2 - 6012
611ARGARGMGMGchain QQQ - XA2 - 6012
711ARGARGMGMGchain VVV - BB2 - 6012
811ARGARGMGMGchain XXX - FB2 - 6012
112METMETMGMGchain BBB - FA1 - 6011
212METMETMGMGchain DDD - JA1 - 6011
312METMETMGMGchain III - NA1 - 6011
412METMETMGMGchain KKK - RA1 - 6011
512METMETMGMGchain PPP - VA1 - 6011
612METMETMGMGchain RRR - ZA1 - 6011
712METMETMGMGchain WWW - DB1 - 6011
812METMETMGMGchain YYY - HB1 - 6011
113LEULEUVALVALchain EEE14 - 54314 - 543
213LEULEUGLUGLU(chain L and (resid 14 through 262 or resid 300 through 543))LL14 - 26214 - 262
223ASPASPVALVAL(chain L and (resid 14 through 262 or resid 300 through 543))LL300 - 543300 - 543
313LEULEUGLUGLU(chain S and (resid 14 through 262 or resid 300 through 543))SS14 - 26214 - 262
323ASPASPVALVAL(chain S and (resid 14 through 262 or resid 300 through 543))SS300 - 543300 - 543
413LEULEUGLUGLU(chain Z and (resid 14 through 262 or resid 300 through 543))ZZ14 - 26214 - 262
423ASPASPVALVAL(chain Z and (resid 14 through 262 or resid 300 through 543))ZZ300 - 543300 - 543
114ASPASPALAALA(chain F and (resid 13 through 149 or (resid 150...FF13 - 14913 - 149
124PHEPHEPHEPHE(chain F and (resid 13 through 149 or (resid 150...FF150150
134ASPASPLYSLYS(chain F and (resid 13 through 149 or (resid 150...FF13 - 16713 - 167
144ASPASPLYSLYS(chain F and (resid 13 through 149 or (resid 150...FF13 - 16713 - 167
154ASPASPLYSLYS(chain F and (resid 13 through 149 or (resid 150...FF13 - 16713 - 167
164ASPASPLYSLYS(chain F and (resid 13 through 149 or (resid 150...FF13 - 16713 - 167
214ASPASPALAALA(chain G and (resid 13 through 149 or (resid 150...GG13 - 14913 - 149
224PHEPHEPHEPHE(chain G and (resid 13 through 149 or (resid 150...GG150150
234ASPASPLYSLYS(chain G and (resid 13 through 149 or (resid 150...GG13 - 16713 - 167
244ASPASPLYSLYS(chain G and (resid 13 through 149 or (resid 150...GG13 - 16713 - 167
254ASPASPLYSLYS(chain G and (resid 13 through 149 or (resid 150...GG13 - 16713 - 167
264ASPASPLYSLYS(chain G and (resid 13 through 149 or (resid 150...GG13 - 16713 - 167
314ASPASPALAALA(chain M and (resid 13 through 149 or (resid 150...MM13 - 14913 - 149
324PHEPHEPHEPHE(chain M and (resid 13 through 149 or (resid 150...MM150150
334ASPASPLYSLYS(chain M and (resid 13 through 149 or (resid 150...MM13 - 16713 - 167
344ASPASPLYSLYS(chain M and (resid 13 through 149 or (resid 150...MM13 - 16713 - 167
354ASPASPLYSLYS(chain M and (resid 13 through 149 or (resid 150...MM13 - 16713 - 167
364ASPASPLYSLYS(chain M and (resid 13 through 149 or (resid 150...MM13 - 16713 - 167
414ASPASPALAALA(chain N and (resid 13 through 149 or (resid 150...NN13 - 14913 - 149
424PHEPHEPHEPHE(chain N and (resid 13 through 149 or (resid 150...NN150150
434ASPASPLYSLYS(chain N and (resid 13 through 149 or (resid 150...NN13 - 16713 - 167
444ASPASPLYSLYS(chain N and (resid 13 through 149 or (resid 150...NN13 - 16713 - 167
454ASPASPLYSLYS(chain N and (resid 13 through 149 or (resid 150...NN13 - 16713 - 167
464ASPASPLYSLYS(chain N and (resid 13 through 149 or (resid 150...NN13 - 16713 - 167
514ASPASPALAALA(chain T and (resid 13 through 149 or (resid 150...TT13 - 14913 - 149
524PHEPHEPHEPHE(chain T and (resid 13 through 149 or (resid 150...TT150150
534ASPASPLYSLYS(chain T and (resid 13 through 149 or (resid 150...TT13 - 16713 - 167
544ASPASPLYSLYS(chain T and (resid 13 through 149 or (resid 150...TT13 - 16713 - 167
554ASPASPLYSLYS(chain T and (resid 13 through 149 or (resid 150...TT13 - 16713 - 167
564ASPASPLYSLYS(chain T and (resid 13 through 149 or (resid 150...TT13 - 16713 - 167
614ASPASPALAALA(chain U and (resid 13 through 149 or (resid 150...UU13 - 14913 - 149
624PHEPHEPHEPHE(chain U and (resid 13 through 149 or (resid 150...UU150150
634ASPASPLYSLYS(chain U and (resid 13 through 149 or (resid 150...UU13 - 16713 - 167
644ASPASPLYSLYS(chain U and (resid 13 through 149 or (resid 150...UU13 - 16713 - 167
654ASPASPLYSLYS(chain U and (resid 13 through 149 or (resid 150...UU13 - 16713 - 167
664ASPASPLYSLYS(chain U and (resid 13 through 149 or (resid 150...UU13 - 16713 - 167
714ASPASPLYSLYSchain aaAA13 - 16713 - 167
814ASPASPALAALA(chain b and (resid 13 through 149 or (resid 150...bBA13 - 14913 - 149
824PHEPHEPHEPHE(chain b and (resid 13 through 149 or (resid 150...bBA150150
834ASPASPLYSLYS(chain b and (resid 13 through 149 or (resid 150...bBA13 - 16713 - 167
844ASPASPLYSLYS(chain b and (resid 13 through 149 or (resid 150...bBA13 - 16713 - 167
854ASPASPLYSLYS(chain b and (resid 13 through 149 or (resid 150...bBA13 - 16713 - 167
864ASPASPLYSLYS(chain b and (resid 13 through 149 or (resid 150...bBA13 - 16713 - 167

NCS ensembles :
ID
1
2
3
4

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Components

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Protein , 4 types, 28 molecules ACHJOQVXBDIKPRWYELSZFGMNTUab

#1: Protein
Tubulin alpha-1A chain / Alpha-tubulin 1 / Tubulin alpha-1 chain


Mass: 50121.266 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: Brain / References: UniProt: P02550
#2: Protein
Tubulin beta chain / Beta-tubulin


Mass: 49907.770 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: Brain / References: UniProt: P02554
#3: Protein
Protein Stu2p/Alp14p


Mass: 63099.242 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Protein was obtained from cDNA (Lachancea kluyveri NRRL Y-12651 chromosome)
Source: (gene. exp.) Lachancea kluyveri NRRL Y-12651 (fungus)
Gene: SKLU-Cont10078 / Plasmid: pLIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: A0A493R6X8*PLUS
#4: Protein
Designed ankyrin repeat protein (DARPIN) D1


Mass: 18068.439 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Details: Darpin was synthesized and inserted into bacterial expression vector.
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pET303 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21

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Non-polymers , 3 types, 32 molecules

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


Mass: 523.180 Da / Num. of mol.: 8 / 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.: 16 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM

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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: 2.78 Å3/Da / Density % sol: 55.78 % / Description: Cube-shaped crystals
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 50 mM PIPES, 100 mM MgCl2 [pH 7.0], and 10-15% PEG-8000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Nov 25, 2013
RadiationMonochromator: Cryo-Cooled double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
Reflection twinOperator: h,-k,-l / Fraction: 0.12
ReflectionResolution: 4.4→96.592 Å / Num. obs: 80099 / % possible obs: 95.4 % / Redundancy: 2.9 % / Biso Wilson estimate: 82.7 Å2 / Rpim(I) all: 0.112 / Rrim(I) all: 0.198 / Rsym value: 0.144 / Net I/av σ(I): 3.9 / Net I/σ(I): 4.9
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsRpim(I) allRrim(I) allRsym value% possible all
4.4-4.642.80.4781.4115670.3860.6750.47894.8
4.64-4.922.70.312.2106320.2580.4480.3192.3
4.92-5.2630.3152.2106720.2510.4420.31598.6
5.26-5.682.90.3162.2100270.2530.4450.31698.5
5.68-6.222.80.2512.985830.2070.3630.25192.6
6.22-6.962.90.1784.180630.140.2470.17895.6
6.96-8.0330.1076.373180.080.1420.10798.2
8.03-9.842.80.0599.558150.0410.0710.05991.3
9.84-13.9130.05210.748460.0340.060.05298.4
13.91-96.5922.80.0616.125760.0380.0690.06192.3

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALA3.3.21data scaling
PHENIXrefinement
PDB_EXTRACT3.24data extraction
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 4.4→96.592 Å / Cross valid method: THROUGHOUT / σ(F): 2.13 / Phase error: 29.13 / Details: The twin fractions were adjusted during refinement
RfactorNum. reflection% reflection
Rfree0.2515 3571 5.25 %
Rwork0.2247 --
obs0.2331 68039 80.63 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Bsol: 59.6 Å2 / ksol: 0.31 e/Å3
Displacement parametersBiso max: 432.2 Å2 / Biso mean: 108.3886 Å2 / Biso min: 22.29 Å2
Refinement stepCycle: final / Resolution: 4.4→96.592 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms77534 0 496 0 78030
Biso mean--78.51 --
Num. residues----9989
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONf_bond_d0.002
X-RAY DIFFRACTIONf_angle_d0.566
X-RAY DIFFRACTIONf_chiral_restr0.04
X-RAY DIFFRACTIONf_plane_restr0.005
X-RAY DIFFRACTIONf_dihedral_angle_d5.784
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A10344X-RAY DIFFRACTION4.695TORSIONAL
12C10344X-RAY DIFFRACTION4.695TORSIONAL
13H10344X-RAY DIFFRACTION4.695TORSIONAL
14J10344X-RAY DIFFRACTION4.695TORSIONAL
15O10344X-RAY DIFFRACTION4.695TORSIONAL
16Q10344X-RAY DIFFRACTION4.695TORSIONAL
17V10344X-RAY DIFFRACTION4.695TORSIONAL
18X10344X-RAY DIFFRACTION4.695TORSIONAL
21B10384X-RAY DIFFRACTION4.695TORSIONAL
22D10384X-RAY DIFFRACTION4.695TORSIONAL
23I10384X-RAY DIFFRACTION4.695TORSIONAL
24K10384X-RAY DIFFRACTION4.695TORSIONAL
25P10384X-RAY DIFFRACTION4.695TORSIONAL
26R10384X-RAY DIFFRACTION4.695TORSIONAL
27W10384X-RAY DIFFRACTION4.695TORSIONAL
28Y10384X-RAY DIFFRACTION4.695TORSIONAL
31E5936X-RAY DIFFRACTION4.695TORSIONAL
32L5936X-RAY DIFFRACTION4.695TORSIONAL
33S5936X-RAY DIFFRACTION4.695TORSIONAL
34Z5936X-RAY DIFFRACTION4.695TORSIONAL
41F3704X-RAY DIFFRACTION4.695TORSIONAL
42G3704X-RAY DIFFRACTION4.695TORSIONAL
43M3704X-RAY DIFFRACTION4.695TORSIONAL
44N3704X-RAY DIFFRACTION4.695TORSIONAL
45T3704X-RAY DIFFRACTION4.695TORSIONAL
46U3704X-RAY DIFFRACTION4.695TORSIONAL
47a3704X-RAY DIFFRACTION4.695TORSIONAL
48b3704X-RAY DIFFRACTION4.695TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)Rfactor Rfree error
4.403-4.47890.2673180.239184520
4.4789-4.56030.2986270.239141234
4.5603-4.6480.3045560.225181443
4.648-4.74290.2487770.2213207150
4.7429-4.8460.2496980.2171254961
4.846-4.95870.2451390.2144311274
4.9587-5.08270.24961540.223344682
5.0827-5.22010.27661800.2361375891
5.2201-5.37360.32551890.2381396194
5.3736-5.5470.3042130.2431387093
5.547-5.74520.30332310.2431383592
5.7452-5.97510.31762600.252375389
5.9751-6.24690.29621750.2541350583
6.2469-6.57610.28372240.25053650870
6.5761-6.98780.28722450.24823884920
6.9878-7.52680.26052480.2449388692
7.5268-8.28330.25452430.22423879910
8.2833-9.47970.22011860.2042356384
9.4797-11.9350.19432250.18753959920
11.935-72.94170.26942380.2689383887

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