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- PDB-3wip: Crystal structure of acetylcholine bound to Ls-AChBP -

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Basic information

Entry
Database: PDB / ID: 3wip
TitleCrystal structure of acetylcholine bound to Ls-AChBP
ComponentsAcetylcholine-binding protein
KeywordsACETYLCHOLINE-BINDING PROTEIN / Acetylcholine-binding protein-agonist complex / Lymnaea stagnalis / Agonist / Acetylcholine
Function / homology
Function and homology information


extracellular ligand-gated monoatomic ion channel activity / synaptic cleft / transmembrane signaling receptor activity / synapse / membrane
Similarity search - Function
Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Distorted Sandwich / Ig-like domain profile. / Immunoglobulin-like domain / Mainly Beta
Similarity search - Domain/homology
ACETYLCHOLINE / ACETATE ION / Acetylcholine-binding protein
Similarity search - Component
Biological speciesLymnaea stagnalis (great pond snail)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsOlsen, J.A. / Balle, T. / Gajhede, M. / Ahring, P.K. / Kastrup, J.S.
CitationJournal: Plos One / Year: 2014
Title: Molecular recognition of the neurotransmitter acetylcholine by an acetylcholine binding protein reveals determinants of binding to nicotinic acetylcholine receptors
Authors: Olsen, J.A. / Balle, T. / Gajhede, M. / Ahring, P.K. / Kastrup, J.S.
History
DepositionSep 24, 2013Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 23, 2014Provider: repository / Type: Initial release
Revision 1.1May 16, 2018Group: Data collection / Refinement description / Category: diffrn_source / software
Item: _diffrn_source.pdbx_synchrotron_site / _software.version
Revision 1.2Nov 8, 2023Group: 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_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Acetylcholine-binding protein
B: Acetylcholine-binding protein
C: Acetylcholine-binding protein
D: Acetylcholine-binding protein
E: Acetylcholine-binding protein
F: Acetylcholine-binding protein
G: Acetylcholine-binding protein
H: Acetylcholine-binding protein
I: Acetylcholine-binding protein
J: Acetylcholine-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)266,13643
Polymers260,87310
Non-polymers5,26333
Water7,332407
1
A: Acetylcholine-binding protein
B: Acetylcholine-binding protein
C: Acetylcholine-binding protein
D: Acetylcholine-binding protein
E: Acetylcholine-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)133,51723
Polymers130,4375
Non-polymers3,08118
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17490 Å2
ΔGint-120 kcal/mol
Surface area42080 Å2
MethodPISA
2
F: Acetylcholine-binding protein
G: Acetylcholine-binding protein
H: Acetylcholine-binding protein
I: Acetylcholine-binding protein
J: Acetylcholine-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,61920
Polymers130,4375
Non-polymers2,18315
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16740 Å2
ΔGint-123 kcal/mol
Surface area42600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)236.850, 73.150, 132.470
Angle α, β, γ (deg.)90.000, 101.450, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain F and (resseq 4:12 or resseq 16:21 or resseq...
21chain B and (resseq 4:12 or resseq 16:21 or resseq...
31chain C and (resseq 4:12 or resseq 16:21 or resseq...
41chain D and (resseq 4:12 or resseq 16:21 or resseq...
51chain A and (resseq 4:12 or resseq 16:21 or resseq...
61chain E and (resseq 4:12 or resseq 16:21 or resseq...
71chain G and (resseq 4:12 or resseq 16:21 or resseq...
81chain H and (resseq 4:12 or resseq 16:21 or resseq...
91chain I and (resseq 4:12 or resseq 16:21 or resseq...
101chain J and (resseq 4:12 or resseq 16:21 or resseq...
12chain C and (resseq 22:25 )
22chain B and (resseq 22:25 )
32chain E and (resseq 22:25 )
42chain D and (resseq 22:25 )
52chain A and (resseq 22:25 )
62chain F and (resseq 22:25 )
72chain G and (resseq 22:25 )
82chain H and (resseq 22:22 or resseq 25:25 )
92chain I and (resseq 22:25 )
102chain J and (resseq 22:25 )

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain F and (resseq 4:12 or resseq 16:21 or resseq...F4 - 12
121chain F and (resseq 4:12 or resseq 16:21 or resseq...F16 - 21
131chain F and (resseq 4:12 or resseq 16:21 or resseq...F26 - 52
141chain F and (resseq 4:12 or resseq 16:21 or resseq...F55 - 111
151chain F and (resseq 4:12 or resseq 16:21 or resseq...F115 - 119
161chain F and (resseq 4:12 or resseq 16:21 or resseq...F121 - 154
171chain F and (resseq 4:12 or resseq 16:21 or resseq...F164 - 184
181chain F and (resseq 4:12 or resseq 16:21 or resseq...F193 - 202
191chain F and (resseq 4:12 or resseq 16:21 or resseq...J300 - 301
211chain B and (resseq 4:12 or resseq 16:21 or resseq...B4 - 12
221chain B and (resseq 4:12 or resseq 16:21 or resseq...B16 - 21
231chain B and (resseq 4:12 or resseq 16:21 or resseq...B26 - 52
241chain B and (resseq 4:12 or resseq 16:21 or resseq...B55 - 111
251chain B and (resseq 4:12 or resseq 16:21 or resseq...B115 - 119
261chain B and (resseq 4:12 or resseq 16:21 or resseq...B121 - 154
271chain B and (resseq 4:12 or resseq 16:21 or resseq...B164 - 184
281chain B and (resseq 4:12 or resseq 16:21 or resseq...B193 - 202
291chain B and (resseq 4:12 or resseq 16:21 or resseq...A300 - 301
311chain C and (resseq 4:12 or resseq 16:21 or resseq...C4 - 12
321chain C and (resseq 4:12 or resseq 16:21 or resseq...C16 - 21
331chain C and (resseq 4:12 or resseq 16:21 or resseq...C26 - 52
341chain C and (resseq 4:12 or resseq 16:21 or resseq...C55 - 111
351chain C and (resseq 4:12 or resseq 16:21 or resseq...C115 - 119
361chain C and (resseq 4:12 or resseq 16:21 or resseq...C121 - 154
371chain C and (resseq 4:12 or resseq 16:21 or resseq...C164 - 184
381chain C and (resseq 4:12 or resseq 16:21 or resseq...C193 - 202
391chain C and (resseq 4:12 or resseq 16:21 or resseq...B300 - 301
411chain D and (resseq 4:12 or resseq 16:21 or resseq...D4 - 12
421chain D and (resseq 4:12 or resseq 16:21 or resseq...D16 - 21
431chain D and (resseq 4:12 or resseq 16:21 or resseq...D26 - 52
441chain D and (resseq 4:12 or resseq 16:21 or resseq...D55 - 111
451chain D and (resseq 4:12 or resseq 16:21 or resseq...D115 - 119
461chain D and (resseq 4:12 or resseq 16:21 or resseq...D121 - 154
471chain D and (resseq 4:12 or resseq 16:21 or resseq...D164 - 184
481chain D and (resseq 4:12 or resseq 16:21 or resseq...D193 - 202
491chain D and (resseq 4:12 or resseq 16:21 or resseq...C300 - 301
511chain A and (resseq 4:12 or resseq 16:21 or resseq...A4 - 12
521chain A and (resseq 4:12 or resseq 16:21 or resseq...A16 - 21
531chain A and (resseq 4:12 or resseq 16:21 or resseq...A26 - 52
541chain A and (resseq 4:12 or resseq 16:21 or resseq...A55 - 111
551chain A and (resseq 4:12 or resseq 16:21 or resseq...A115 - 119
561chain A and (resseq 4:12 or resseq 16:21 or resseq...A121 - 154
571chain A and (resseq 4:12 or resseq 16:21 or resseq...A164 - 184
581chain A and (resseq 4:12 or resseq 16:21 or resseq...A193 - 202
591chain A and (resseq 4:12 or resseq 16:21 or resseq...E300 - 301
611chain E and (resseq 4:12 or resseq 16:21 or resseq...E4 - 12
621chain E and (resseq 4:12 or resseq 16:21 or resseq...E16 - 21
631chain E and (resseq 4:12 or resseq 16:21 or resseq...E26 - 52
641chain E and (resseq 4:12 or resseq 16:21 or resseq...E55 - 111
651chain E and (resseq 4:12 or resseq 16:21 or resseq...E115 - 119
661chain E and (resseq 4:12 or resseq 16:21 or resseq...E121 - 154
671chain E and (resseq 4:12 or resseq 16:21 or resseq...E164 - 184
681chain E and (resseq 4:12 or resseq 16:21 or resseq...E193 - 202
691chain E and (resseq 4:12 or resseq 16:21 or resseq...D300 - 301
711chain G and (resseq 4:12 or resseq 16:21 or resseq...G4 - 12
721chain G and (resseq 4:12 or resseq 16:21 or resseq...G16 - 21
731chain G and (resseq 4:12 or resseq 16:21 or resseq...G26 - 52
741chain G and (resseq 4:12 or resseq 16:21 or resseq...G55 - 111
751chain G and (resseq 4:12 or resseq 16:21 or resseq...G115 - 119
761chain G and (resseq 4:12 or resseq 16:21 or resseq...G121 - 154
771chain G and (resseq 4:12 or resseq 16:21 or resseq...G164 - 184
781chain G and (resseq 4:12 or resseq 16:21 or resseq...G193 - 202
791chain G and (resseq 4:12 or resseq 16:21 or resseq...F300 - 301
811chain H and (resseq 4:12 or resseq 16:21 or resseq...H4 - 12
821chain H and (resseq 4:12 or resseq 16:21 or resseq...H16 - 21
831chain H and (resseq 4:12 or resseq 16:21 or resseq...H26 - 52
841chain H and (resseq 4:12 or resseq 16:21 or resseq...H55 - 111
851chain H and (resseq 4:12 or resseq 16:21 or resseq...H115 - 119
861chain H and (resseq 4:12 or resseq 16:21 or resseq...H121 - 154
871chain H and (resseq 4:12 or resseq 16:21 or resseq...H164 - 184
881chain H and (resseq 4:12 or resseq 16:21 or resseq...H193 - 202
891chain H and (resseq 4:12 or resseq 16:21 or resseq...G300 - 301
911chain I and (resseq 4:12 or resseq 16:21 or resseq...I4 - 12
921chain I and (resseq 4:12 or resseq 16:21 or resseq...I16 - 21
931chain I and (resseq 4:12 or resseq 16:21 or resseq...I26 - 52
941chain I and (resseq 4:12 or resseq 16:21 or resseq...I55 - 111
951chain I and (resseq 4:12 or resseq 16:21 or resseq...I115 - 119
961chain I and (resseq 4:12 or resseq 16:21 or resseq...I121 - 154
971chain I and (resseq 4:12 or resseq 16:21 or resseq...I164 - 184
981chain I and (resseq 4:12 or resseq 16:21 or resseq...I193 - 202
991chain I and (resseq 4:12 or resseq 16:21 or resseq...H300 - 301
1011chain J and (resseq 4:12 or resseq 16:21 or resseq...J4 - 12
1021chain J and (resseq 4:12 or resseq 16:21 or resseq...J16 - 21
1031chain J and (resseq 4:12 or resseq 16:21 or resseq...J26 - 52
1041chain J and (resseq 4:12 or resseq 16:21 or resseq...J55 - 111
1051chain J and (resseq 4:12 or resseq 16:21 or resseq...J115 - 119
1061chain J and (resseq 4:12 or resseq 16:21 or resseq...J121 - 154
1071chain J and (resseq 4:12 or resseq 16:21 or resseq...J164 - 184
1081chain J and (resseq 4:12 or resseq 16:21 or resseq...J193 - 202
1091chain J and (resseq 4:12 or resseq 16:21 or resseq...I300 - 301
112chain C and (resseq 22:25 )C22 - 25
212chain B and (resseq 22:25 )B22 - 25
312chain E and (resseq 22:25 )E22 - 25
412chain D and (resseq 22:25 )D22 - 25
512chain A and (resseq 22:25 )A22 - 25
612chain F and (resseq 22:25 )F22 - 25
712chain G and (resseq 22:25 )G22 - 25
812chain H and (resseq 22:22 or resseq 25:25 )H22
822chain H and (resseq 22:22 or resseq 25:25 )H25
912chain I and (resseq 22:25 )I22 - 25
1012chain J and (resseq 22:25 )J22 - 25

NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(-0.997966, 0.053132, -0.035219), (0.058609, 0.547514, -0.834741), (-0.025068, -0.835108, -0.549515)83.570801, 30.288, 62.3521
2given(-0.998237, 0.05883, 0.007828), (0.058766, 0.96137, 0.268912), (0.008294, 0.268898, -0.963133)82.311501, -10.7583, 59.387402
3given(-0.998813, 0.029651, 0.038633), (0.039853, 0.041721, 0.998334), (0.02799, 0.998689, -0.042853)81.657898, -20.9951, 19.252399
4given(-0.999309, 0.016993, -0.033046), (0.015433, -0.619182, -0.785096), (-0.033803, -0.785064, 0.618492)84.2062, 45.927399, 24.226999
5given(-0.999925, 0.008722, 0.008628), (-0.005159, -0.936992, 0.349314), (0.011131, 0.349243, 0.936966)83.186203, 14.5462, -2.70512
6given(0.999157, -0.01977, -0.035974), (-0.027816, 0.31839, -0.947552), (0.030187, 0.947754, 0.317572)1.30464, 40.744999, 8.43061
7given(0.998463, -0.053216, -0.015512), (-0.052146, -0.806848, -0.588453), (0.018799, 0.588357, -0.808382)1.18056, 44.930199, 49.674599
8given(0.998329, -0.049994, 0.028978), (-0.057543, -0.814268, 0.57763), (-0.005282, -0.578332, -0.815784)-0.43737, 7.88442, 66.487999
9given(0.99893, -0.01409, 0.04406), (-0.037783, 0.300998, 0.952876), (-0.026688, -0.953521, 0.300143)-1.60546, -19.792601, 36.486
10given(0.998472, -0.0268, -0.048321), (-0.036813, 0.329512, -0.943433), (0.041207, 0.943771, 0.328022)1.59302, 40.0564, 7.89473
11given(0.996295, -0.085762, -0.006405), (-0.063867, -0.787705, 0.612733), (-0.057594, -0.610054, -0.790264)0.472191, 7.30067, 66.6334
12given(0.999122, -0.041234, -0.00736), (0.020893, 0.338318, 0.9408), (-0.036303, -0.940128, 0.338882)1.40698, -21.363701, 34.492401
13given(0.999147, -0.020323, -0.03594), (-0.036619, -0.838293, -0.543989), (-0.019073, 0.544842, -0.838322)0.933353, 44.703201, 50.698898
14given(-0.996006, 0.028491, -0.084615), (0.0049, 0.963732, 0.266826), (0.089149, 0.265346, -0.960023)85.286301, -7.40639, 54.935001
15given(-0.992771, 0.089401, -0.080083), (0.119674, 0.686315, -0.717391), (-0.009173, -0.721789, -0.692053)82.5811, 25.2936, 60.040699
16given(-0.982874, -0.097759, 0.156211), (-0.095313, -0.455809, -0.88496), (0.157715, -0.884693, 0.438685)76.770897, 57.124001, 16.439199
17given(-0.999946, -0.01038, 0.000308), (0.009948, -0.948949, 0.315274), (-0.002981, 0.31526, 0.949001)83.569397, 15.7495, -3.01584
18given(-0.997971, 0.057035, 0.028288), (0.029798, 0.025793, 0.999223), (0.056261, 0.998039, -0.027441)81.0131, -20.364901, 16.8724

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Components

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Protein , 1 types, 10 molecules ABCDEFGHIJ

#1: Protein
Acetylcholine-binding protein / ACh-binding protein / AchBP


Mass: 26087.311 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lymnaea stagnalis (great pond snail) / Plasmid: PFASTBAC I / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf9 / References: UniProt: P58154

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Non-polymers , 6 types, 440 molecules

#2: Chemical
ChemComp-ACH / ACETYLCHOLINE / Acetylcholine


Mass: 146.207 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C7H16NO2 / Comment: neurotransmitter*YM
#3: Chemical
ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol


Mass: 238.278 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#4: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 407 / 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: 2.16 Å3/Da / Density % sol: 42.94 % / Mosaicity: 0.56 °
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 0.1M TRIS, 1.025M (NH4)2SO4, 0.1M NaCl, 1.5% PEG 400, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 101 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 21, 2012
RadiationMonochromator: Si[111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.6→129.834 Å / Num. obs: 68170 / % possible obs: 99.2 % / Redundancy: 3.3 % / Biso Wilson estimate: 34.95 Å2 / Rsym value: 0.101 / Net I/σ(I): 8.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) allRmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRpim(I) allRrim(I) allRsym valueNet I/σ(I) obs% possible all
2.6-2.743.20.3570.29623228099430.1980.3570.2963.899.9
2.74-2.913.30.2430.2013.33078194390.1340.2430.201599.8
2.91-3.113.30.1830.1524.32878888340.1010.1830.1526.399.7
3.11-3.363.30.1280.1065.82706382530.070.1280.1068.399.5
3.36-3.683.30.1110.0926.32483275640.0610.1110.0929.899.4
3.68-4.113.30.10.08362254968660.0550.10.08310.999.1
4.11-4.753.30.0930.0787.31987860410.050.0930.07812.198.8
4.75-5.813.30.1190.15.81675550800.0640.1190.111.998.4
5.81-8.223.30.0990.0836.91302339610.0530.0990.08311.597.9
8.22-48.293.20.0840.076.8689921890.0460.0840.0712.196.4

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Processing

Software
NameVersionClassificationNB
SCALA3.3.16data scaling
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.11data extraction
MxCuBEmarccddata collection
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3ZDG

3zdg


Resolution: 2.6→46.172 Å / Occupancy max: 1 / Occupancy min: 0.34 / SU ML: 0.32 / Cross valid method: Random / σ(F): 0 / Phase error: 23.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2389 3446 5.06 %R-free set generated in Scala
Rwork0.1787 64697 --
obs0.1818 68143 99.06 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 116.61 Å2 / Biso mean: 32.7157 Å2 / Biso min: 6.11 Å2
Refinement stepCycle: LAST / Resolution: 2.6→46.172 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16170 0 340 407 16917
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00917105
X-RAY DIFFRACTIONf_angle_d1.36823254
X-RAY DIFFRACTIONf_chiral_restr0.0712621
X-RAY DIFFRACTIONf_plane_restr0.0052973
X-RAY DIFFRACTIONf_dihedral_angle_d13.4546436
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11F1341X-RAY DIFFRACTIONPOSITIONAL0.051
12B1341X-RAY DIFFRACTIONPOSITIONAL0.051
13C1311X-RAY DIFFRACTIONPOSITIONAL0.045
14D1335X-RAY DIFFRACTIONPOSITIONAL0.048
15A1333X-RAY DIFFRACTIONPOSITIONAL0.048
16E1341X-RAY DIFFRACTIONPOSITIONAL0.047
17G1341X-RAY DIFFRACTIONPOSITIONAL0.056
18H1341X-RAY DIFFRACTIONPOSITIONAL0.044
19I1332X-RAY DIFFRACTIONPOSITIONAL0.059
110J1341X-RAY DIFFRACTIONPOSITIONAL0.056
21C39X-RAY DIFFRACTIONPOSITIONAL0.026
22B39X-RAY DIFFRACTIONPOSITIONAL0.026
23E39X-RAY DIFFRACTIONPOSITIONAL0.03
24D39X-RAY DIFFRACTIONPOSITIONAL0.03
25A39X-RAY DIFFRACTIONPOSITIONAL0.024
26F39X-RAY DIFFRACTIONPOSITIONAL0.035
27G39X-RAY DIFFRACTIONPOSITIONAL0.026
28H20X-RAY DIFFRACTIONPOSITIONAL0.075
29I39X-RAY DIFFRACTIONPOSITIONAL0.021
210J39X-RAY DIFFRACTIONPOSITIONAL0.025
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 25

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.6-2.63560.34031420.228326112753100
2.6356-2.67330.32781220.22525362658100
2.6733-2.71320.31211310.207126222753100
2.7132-2.75560.27641180.192626372755100
2.7556-2.80070.30411220.194325702692100
2.8007-2.8490.29071310.197425912722100
2.849-2.90080.27861500.197625932743100
2.9008-2.95660.27291490.199725632712100
2.9566-3.01690.26351170.193526122729100
3.0169-3.08250.25781460.199925832729100
3.0825-3.15420.28481350.18322593272899
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6.0299-7.59160.23961420.19822577271998
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