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- PDB-8sph: Crystal structure of chimeric omicron RBD (strain XBB.1) complexe... -

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Basic information

Entry
Database: PDB / ID: 8sph
TitleCrystal structure of chimeric omicron RBD (strain XBB.1) complexed with human ACE2
Components
  • Angiotensin-converting enzyme 2
  • Spike protein S1
KeywordsHYDROLASE/VIRAL PROTEIN / SARS2 / CELL INVASION / HYDROLASE-VIRAL PROTEIN complex
Function / homology
Function and homology information


positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / angiotensin-mediated drinking behavior / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / regulation of systemic arterial blood pressure by renin-angiotensin / positive regulation of gap junction assembly / tryptophan transport / regulation of cardiac conduction / regulation of vasoconstriction ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / angiotensin-mediated drinking behavior / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / regulation of systemic arterial blood pressure by renin-angiotensin / positive regulation of gap junction assembly / tryptophan transport / regulation of cardiac conduction / regulation of vasoconstriction / peptidyl-dipeptidase activity / maternal process involved in female pregnancy / Metabolism of Angiotensinogen to Angiotensins / carboxypeptidase activity / angiotensin maturation / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / metallocarboxypeptidase activity / viral life cycle / positive regulation of cardiac muscle contraction / regulation of cytokine production / regulation of transmembrane transporter activity / blood vessel diameter maintenance / negative regulation of smooth muscle cell proliferation / brush border membrane / negative regulation of ERK1 and ERK2 cascade / metallopeptidase activity / positive regulation of reactive oxygen species metabolic process / endocytic vesicle membrane / regulation of cell population proliferation / virus receptor activity / regulation of inflammatory response / endopeptidase activity / Potential therapeutics for SARS / Induction of Cell-Cell Fusion / entry receptor-mediated virion attachment to host cell / membrane fusion / Attachment and Entry / receptor-mediated virion attachment to host cell / cilium / apical plasma membrane / membrane raft / endoplasmic reticulum lumen / symbiont entry into host cell / cell surface / extracellular space / extracellular exosome / extracellular region / zinc ion binding / identical protein binding / membrane / plasma membrane
Similarity search - Function
Collectrin domain / Renal amino acid transporter / Collectrin-like domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Peptidase family M2 domain profile. / Neutral zinc metallopeptidases, zinc-binding region signature.
Similarity search - Domain/homology
Angiotensin-converting enzyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Severe acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.71 Å
AuthorsZhang, W. / Shi, K. / Aihara, H. / Li, F.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI089728 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI110700 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM118047 United States
CitationJournal: J.Virol. / Year: 2023
Title: Structural evolution of SARS-CoV-2 omicron in human receptor recognition.
Authors: Zhang, W. / Shi, K. / Geng, Q. / Herbst, M. / Wang, M. / Huang, L. / Bu, F. / Liu, B. / Aihara, H. / Li, F.
History
DepositionMay 3, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 2, 2023Provider: repository / Type: Initial release
Revision 1.1Aug 30, 2023Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Sep 13, 2023Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Angiotensin-converting enzyme 2
B: Angiotensin-converting enzyme 2
E: Spike protein S1
F: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)192,47924
Polymers186,8564
Non-polymers5,62320
Water52229
1
A: Angiotensin-converting enzyme 2
E: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,25911
Polymers93,4282
Non-polymers2,8309
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Angiotensin-converting enzyme 2
F: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,22113
Polymers93,4282
Non-polymers2,79211
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)79.740, 116.369, 111.658
Angle α, β, γ (deg.)90.000, 92.810, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 19 through 614 or resid 703 through 705))
d_2ens_1(chain "B" and (resid 19 through 614 or resid 703 through 705))
d_1ens_2chain "C"
d_2ens_2chain "L"
d_1ens_3chain "D"
d_2ens_3chain "G"
d_3ens_3chain "H"
d_4ens_3chain "I"
d_5ens_3chain "K"
d_6ens_3chain "M"
d_1ens_4(chain "E" and (resid 334 through 459 or resid 461...
d_2ens_4(chain "F" and (resid 334 through 459 or resid 461...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1SERSERALAALAAA19 - 6141 - 596
d_12ens_1ZNZNZNZNAN701
d_13ens_1CLCLCLCLAO702
d_14ens_1EDOEDOEDOEDOAP703
d_21ens_1SERSERALAALABB19 - 6141 - 596
d_22ens_1ZNZNZNZNBR701
d_23ens_1CLCLCLCLBS702
d_24ens_1EDOEDOEDOEDOBT703
d_11ens_2NAGNAGNAGNAGCE1
d_12ens_2NAGNAGNAGNAGCE2
d_13ens_2BMABMABMABMACE3
d_21ens_2NAGNAGNAGNAGLL1
d_22ens_2NAGNAGNAGNAGLL2
d_23ens_2BMABMABMABMALL3
d_11ens_3NAGNAGNAGNAGDF1
d_12ens_3NAGNAGNAGNAGDF2
d_21ens_3NAGNAGNAGNAGGG1
d_22ens_3NAGNAGNAGNAGGG2
d_31ens_3NAGNAGNAGNAGHH1
d_32ens_3NAGNAGNAGNAGHH2
d_41ens_3NAGNAGNAGNAGII1
d_42ens_3NAGNAGNAGNAGII2
d_51ens_3NAGNAGNAGNAGKK1
d_52ens_3NAGNAGNAGNAGKK2
d_61ens_3NAGNAGNAGNAGMM1
d_62ens_3NAGNAGNAGNAGMM2
d_11ens_4ASNASNSERSEREC334 - 45916 - 141
d_12ens_4LEULEUGLYGLYEC461 - 476143 - 158
d_13ens_4PROPROVALVALEC479 - 483161 - 165
d_14ens_4GLYGLYGLYGLYEC485167
d_15ens_4ASNASNTYRTYREC487 - 489169 - 171
d_16ens_4PROPROPHEPHEEC491 - 497173 - 179
d_17ens_4PROPROTHRTHREC499 - 500181 - 182
d_18ens_4GLYGLYGLYGLYEC502 - 504184 - 186
d_19ens_4GLNGLNGLUGLUEC506 - 516188 - 198
d_110ens_4ALAALAALAALAEC520202
d_111ens_4THRTHRPROPROEC523 - 527205 - 209
d_21ens_4ASNASNSERSERFD334 - 45916 - 141
d_22ens_4LEULEUGLYGLYFD461 - 476143 - 158
d_23ens_4PROPROVALVALFD479 - 483161 - 165
d_24ens_4GLYGLYGLYGLYFD485167
d_25ens_4ASNASNTYRTYRFD487 - 489169 - 171
d_26ens_4PROPROPHEPHEFD491 - 497173 - 179
d_27ens_4PROPROTHRTHRFD499 - 500181 - 182
d_28ens_4GLYGLYGLYGLYFD502 - 504184 - 186
d_29ens_4GLNGLNGLUGLUFD506 - 516188 - 198
d_210ens_4ALAALAPROPROFD522 - 527204 - 209

NCS ensembles :
ID
ens_1
ens_2
ens_3
ens_4

NCS oper:
IDCodeMatrixVector
1given(-0.95720318766, 0.231839256445, 0.173241498218), (0.186832411449, 0.0378357992746, 0.98166292704), (0.221033272532, 0.972018009846, -0.0795316350233)11.0324050946, -23.1147401301, 1.30545449196
2given(0.888945927155, -0.0212048772485, 0.457521028779), (-0.297756435641, 0.73227295508, 0.612468304725), (-0.348017590976, -0.680681035757, 0.644637172316)-31.540416836, -13.5461874846, 45.2392596059
3given(-0.984611600054, 0.0551743409785, 0.165818542803), (0.000980937822346, -0.94709240138, 0.320959531732), (0.174754212541, 0.316183135772, 0.932464042123)24.8329231975, 7.00058808858, 21.7929841239
4given(-0.146584189252, -0.834833986066, 0.530627261994), (0.919147509198, 0.0833211294134, 0.385000578867), (-0.36562403066, 0.544159723889, 0.755122018684)0.233061262875, -14.2878156782, 13.1505721479
5given(0.662014484985, 0.729761072781, 0.170837929989), (-0.659437316515, 0.458808593175, 0.595514147957), (0.35620113315, -0.506895898072, 0.78496961805)-14.1681282261, -12.376341257, -47.4621687542
6given(0.887451073633, 0.446455931069, 0.114488835787), (-0.442771304582, 0.894805615994, -0.0572405575104), (-0.128000639629, 0.00010582303643, 0.991774079645)-5.07768255959, 24.35698226, -35.814845024
7given(-0.876753013136, -0.242564678582, 0.415290898842), (0.480790870522, -0.420489247443, 0.769434163271), (-0.0120121929799, 0.874271793831, 0.48528809766)26.8349502972, 30.9074547729, -46.4883159741
8given(-0.981340788967, 0.183884373736, 0.0561853451054), (0.0640179222108, 0.0369347243251, 0.997265025846), (0.181306264494, 0.982253716325, -0.0480174470431)17.7300327859, -22.971433695, -0.0297421247164

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Components

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Protein , 2 types, 4 molecules ABEF

#1: Protein Angiotensin-converting enzyme 2 / ACE-related carboxypeptidase / Angiotensin-converting enzyme homolog / ACEH / Metalloprotease MPROT15


Mass: 69153.664 Da / Num. of mol.: 2 / Fragment: UNP residues 19-615
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2, UNQ868/PRO1885 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q9BYF1, angiotensin-converting enzyme 2
#2: Protein Spike protein S1


Mass: 24274.527 Da / Num. of mol.: 2 / Fragment: receptor-binding domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Strain: omicron XBB1 / Production host: Spodoptera frugiperda (fall armyworm)

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Sugars , 4 types, 12 molecules

#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE
#4: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#5: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 789.734 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-1/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-GlcpNAc]{}}}}LINUCSPDB-CARE
#9: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 37 molecules

#6: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#7: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#8: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 29 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationY

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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: 2.77 Å3/Da / Density % sol: 55.58 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.2
Details: 100 mM Tris, pH 8.2, 24% PEG6000, 150 mM sodium chloride, 10% ethylene glycol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.979 Å
DetectorType: DECTRIS EIGER2 S 16M / Detector: PIXEL / Date: Mar 14, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.706→111.524 Å / Num. obs: 24963 / % possible obs: 85.5 % / Redundancy: 4.1 % / Biso Wilson estimate: 62.15 Å2 / CC1/2: 0.993 / Rmerge(I) obs: 0.152 / Rpim(I) all: 0.085 / Rrim(I) all: 0.174 / Rsym value: 0.152 / Net I/σ(I): 5.3
Reflection shellResolution: 2.706→3.035 Å / Rmerge(I) obs: 0.93 / Mean I/σ(I) obs: 1.7 / Num. unique obs: 1248 / CC1/2: 0.549 / Rpim(I) all: 0.525 / Rrim(I) all: 1.071 / Rsym value: 0.93

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
autoPROCdata reduction
autoPROCdata scaling
PHASESphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2AJF

2ajf


Resolution: 2.71→111.52 Å / SU ML: 0.4138 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 35.5949
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2829 1275 5.11 %
Rwork0.2188 23656 -
obs0.2221 24931 44.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 71.67 Å2
Refinement stepCycle: LAST / Resolution: 2.71→111.52 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12772 0 361 29 13162
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.003813483
X-RAY DIFFRACTIONf_angle_d0.623918313
X-RAY DIFFRACTIONf_chiral_restr0.04451994
X-RAY DIFFRACTIONf_plane_restr0.00382333
X-RAY DIFFRACTIONf_dihedral_angle_d14.34664910
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AAX-RAY DIFFRACTIONTorsion NCS1.72530255436
ens_2d_2ECX-RAY DIFFRACTIONTorsion NCS2.01268290022
ens_3d_2FDX-RAY DIFFRACTIONTorsion NCS2.68184430107
ens_3d_3FDX-RAY DIFFRACTIONTorsion NCS2.79516303687
ens_3d_4FDX-RAY DIFFRACTIONTorsion NCS1.44679910999
ens_3d_5FDX-RAY DIFFRACTIONTorsion NCS1.47797867489
ens_3d_6FDX-RAY DIFFRACTIONTorsion NCS3.16529570821
ens_4d_2CEX-RAY DIFFRACTIONTorsion NCS0.903005945104
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.71-2.820.351570.3841177X-RAY DIFFRACTION3.03
2.82-2.950.4654270.3504528X-RAY DIFFRACTION9.04
2.95-3.10.3222450.3277880X-RAY DIFFRACTION15.12
3.1-3.30.3625670.30561298X-RAY DIFFRACTION22.23
3.3-3.550.32921010.27931959X-RAY DIFFRACTION33.71
3.55-3.910.33331320.24052446X-RAY DIFFRACTION41.79
3.91-4.470.30572790.21284783X-RAY DIFFRACTION82.02
4.47-5.640.26413070.20855810X-RAY DIFFRACTION99.24
5.64-111.520.25483100.20265775X-RAY DIFFRACTION97.02
Refinement TLS params.

L11: 0 °2 / L12: 0 °2 / L13: 0 °2 / L22: 0 °2 / L23: 0 °2 / L33: 0 °2 / S11: 0 Å ° / S12: 0 Å ° / S13: 0 Å ° / S21: 0 Å ° / S22: 0 Å ° / S23: 0 Å ° / S31: 0 Å ° / S32: 0 Å ° / S33: 0 Å ° / T11: 0 Å2 / T12: 0 Å2 / T13: 0 Å2 / T22: 0 Å2 / T23: 0 Å2 / T33: 0 Å2 / Method: refined / Refine-ID: X-RAY DIFFRACTION

IDOrigin x (Å)Origin y (Å)Origin z (Å)
119.274112907-17.598307965959.316712251
239.09592646010.81190832084243.2461892707
320.003295304512.13721447663.2486084422
426.53488504785.2227319635842.3908276821
52.3667614642541.9992836426-15.5616717763
6-6.1360663518832.337432957-17.4741951245
7-24.362097049537.55807766064.53064802497
8-13.776578755920.26654471289.44695181865
93.4900551805736.150796818211.6534010243
10-20.274978193123.93412803013.86582690235
11-1.4040855300817.121838781811.0474268482
12-12.00402614-6.0424675294383.1044403676
13-21.3429751497-2.2261822457384.0914519486
14-13.03190319556.7997980385574.5448050173
15-27.07083438484.7937237696375.9939648611
16-10.4632427438-6.4621013532672.0356586628
17-10.7513234443-6.1924185787869.4516056845
18-4.56874455608-18.595251574370.5781214706
191.72337049291-34.024505858762.6833955571
204.56645864691-11.189655845869.8768697189
21-13.2771304714-3.6802824127975.5568570892
22-32.6803409356-2.7085648072380.6705647601
2343.589509258364.2736800885-8.38128286391
2436.387277625957.7957012396-12.3890714897
2536.111672985551.08951820080.305329613995
2649.218449587150.9393489408-3.64016371795
2730.828295771948.0544786864-11.8459320169
2829.60960179838.9227425916-15.7194672297
2931.764090173848.334074543-9.49497783576
3022.802340633746.3071691274-22.5800564656
3113.382918423837.9283875064-36.2885194713
3227.309885154450.1064667338-11.7236955684
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 19 through 129 )AA19 - 1291 - 111
22chain 'A' and (resid 130 through 293 )AA130 - 293112 - 275
33chain 'A' and (resid 294 through 352 )AA294 - 352276 - 334
44chain 'A' and (resid 353 through 614 )AA353 - 614335 - 596
55chain 'B' and (resid 19 through 82 )BG19 - 821 - 64
66chain 'B' and (resid 83 through 129 )BG83 - 12965 - 111
77chain 'B' and (resid 130 through 194 )BG130 - 194112 - 176
88chain 'B' and (resid 195 through 293 )BG195 - 293177 - 275
99chain 'B' and (resid 294 through 433 )BG294 - 433276 - 415
1010chain 'B' and (resid 434 through 512 )BG434 - 512416 - 494
1111chain 'B' and (resid 513 through 614 )BG513 - 614495 - 596
1212chain 'E' and (resid 334 through 353 )EP334 - 3531 - 20
1313chain 'E' and (resid 354 through 367 )EP354 - 36721 - 34
1414chain 'E' and (resid 368 through 380 )EP368 - 38035 - 47
1515chain 'E' and (resid 381 through 393 )EP381 - 39348 - 60
1616chain 'E' and (resid 394 through 409 )EP394 - 40961 - 76
1717chain 'E' and (resid 410 through 442 )EP410 - 44277 - 109
1818chain 'E' and (resid 443 through 474 )EP443 - 474110 - 141
1919chain 'E' and (resid 475 through 487 )EP475 - 487142 - 154
2020chain 'E' and (resid 488 through 506 )EP488 - 506155 - 173
2121chain 'E' and (resid 507 through 516 )EP507 - 516174 - 183
2222chain 'E' and (resid 517 through 527 )EP517 - 527184 - 193
2323chain 'F' and (resid 331 through 342 )FR331 - 3421 - 12
2424chain 'F' and (resid 343 through 367 )FR343 - 36713 - 37
2525chain 'F' and (resid 368 through 380 )FR368 - 38038 - 50
2626chain 'F' and (resid 381 through 393 )FR381 - 39351 - 63
2727chain 'F' and (resid 394 through 409 )FR394 - 40964 - 79
2828chain 'F' and (resid 410 through 421 )FR410 - 42180 - 91
2929chain 'F' and (resid 422 through 442 )FR422 - 44292 - 112
3030chain 'F' and (resid 443 through 474 )FR443 - 474113 - 144
3131chain 'F' and (resid 475 through 487 )FR475 - 487145 - 157
3232chain 'F' and (resid 488 through 527 )FR488 - 527158 - 194

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