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- PDB-4adf: CRYSTAL STRUCTURE OF THE HUMAN COLONY-STIMULATING FACTOR 1 (hCSF-... -

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Basic information

Entry
Database: PDB / ID: 4adf
TitleCRYSTAL STRUCTURE OF THE HUMAN COLONY-STIMULATING FACTOR 1 (hCSF-1) CYTOKINE IN COMPLEX WITH THE VIRAL RECEPTOR BARF1
Components
  • MACROPHAGE COLONY-STIMULATING FACTOR 1
  • SECRETED PROTEIN BARF1
KeywordsIMMUNE SYSTEM/RECEPTOR / IMMUNE SYSTEM-RECEPTOR COMPLEX / RTKIII / EXTRACELLULAR / CYTOKINE RECEPTOR-CYTOKINE COMPLEX / FOUR-HELIX BUNDLE / GLYCOPROTEIN / IMMUNOGLOBULIN DOMAIN / ONCOGENE / CYTOKINE/SIGNALING
Function / homology
Function and homology information


regulation of macrophage derived foam cell differentiation / mammary gland fat development / positive regulation of macrophage colony-stimulating factor signaling pathway / monocyte homeostasis / macrophage homeostasis / macrophage colony-stimulating factor receptor binding / positive regulation of macrophage migration / osteoclast proliferation / positive regulation of odontogenesis of dentin-containing tooth / developmental process involved in reproduction ...regulation of macrophage derived foam cell differentiation / mammary gland fat development / positive regulation of macrophage colony-stimulating factor signaling pathway / monocyte homeostasis / macrophage homeostasis / macrophage colony-stimulating factor receptor binding / positive regulation of macrophage migration / osteoclast proliferation / positive regulation of odontogenesis of dentin-containing tooth / developmental process involved in reproduction / CSF1-CSF1R complex / monocyte activation / macrophage colony-stimulating factor signaling pathway / positive regulation of microglial cell migration / mammary duct terminal end bud growth / microglial cell proliferation / positive regulation of mononuclear cell proliferation / positive regulation of macrophage differentiation / myeloid leukocyte migration / neutrophil homeostasis / positive regulation of monocyte differentiation / positive regulation of multicellular organism growth / positive regulation of osteoclast differentiation / branching involved in mammary gland duct morphogenesis / positive regulation of macrophage derived foam cell differentiation / positive regulation of Ras protein signal transduction / Other interleukin signaling / positive regulation of cell-matrix adhesion / positive regulation of macrophage chemotaxis / Interleukin-10 signaling / positive regulation of protein metabolic process / macrophage differentiation / monocyte differentiation / regulation of ossification / Transcriptional and post-translational regulation of MITF-M expression and activity / homeostasis of number of cells within a tissue / cell surface receptor protein tyrosine kinase signaling pathway / osteoclast differentiation / response to ischemia / cytokine activity / Post-translational protein phosphorylation / growth factor activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Signaling by CSF1 (M-CSF) in myeloid cells / Ras protein signal transduction / nuclear body / positive regulation of cell migration / endoplasmic reticulum lumen / inflammatory response / innate immune response / positive regulation of cell population proliferation / positive regulation of gene expression / perinuclear region of cytoplasm / protein homodimerization activity / extracellular space / extracellular region / identical protein binding / membrane / plasma membrane
Similarity search - Function
: / BARF1 second Ig-like domain / Macrophage colony stimulating factor-1 / Macrophage colony stimulating factor-1 (CSF-1) / Four-helical cytokine-like, core / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Secreted protein BARF1 / Macrophage colony-stimulating factor 1 / Secreted protein BARF1
Similarity search - Component
Biological speciesHUMAN HERPESVIRUS 4 (Epstein-Barr virus)
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.4 Å
AuthorsElegheert, J. / Bracke, N. / Savvides, S.N.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2012
Title: Allosteric Competitive Inactivation of Hematopoietic Csf-1 Signaling by the Viral Decoy Receptor Barf1.
Authors: Elegheert, J. / Bracke, N. / Pouliot, P. / Gutsche, I. / Shkumatov, A.V. / Tarbouriech, N. / Verstraete, K. / Bekaert, A. / Burmeister, W.P. / Svergun, D.I. / Lambrecht, B.N. / Vergauwen, B. / Savvides, S.N.
History
DepositionDec 23, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 22, 2012Provider: repository / Type: Initial release
Revision 1.1Sep 26, 2012Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 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

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Assembly

Deposited unit
A: SECRETED PROTEIN BARF1
B: SECRETED PROTEIN BARF1
C: SECRETED PROTEIN BARF1
D: SECRETED PROTEIN BARF1
E: SECRETED PROTEIN BARF1
F: SECRETED PROTEIN BARF1
G: MACROPHAGE COLONY-STIMULATING FACTOR 1
H: MACROPHAGE COLONY-STIMULATING FACTOR 1
I: MACROPHAGE COLONY-STIMULATING FACTOR 1
J: MACROPHAGE COLONY-STIMULATING FACTOR 1
K: MACROPHAGE COLONY-STIMULATING FACTOR 1
L: MACROPHAGE COLONY-STIMULATING FACTOR 1
M: SECRETED PROTEIN BARF1
N: SECRETED PROTEIN BARF1
O: SECRETED PROTEIN BARF1
P: SECRETED PROTEIN BARF1
Q: SECRETED PROTEIN BARF1
R: SECRETED PROTEIN BARF1
S: MACROPHAGE COLONY-STIMULATING FACTOR 1
T: MACROPHAGE COLONY-STIMULATING FACTOR 1
U: MACROPHAGE COLONY-STIMULATING FACTOR 1
V: MACROPHAGE COLONY-STIMULATING FACTOR 1
W: MACROPHAGE COLONY-STIMULATING FACTOR 1
X: MACROPHAGE COLONY-STIMULATING FACTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)508,24636
Polymers495,37024
Non-polymers12,87612
Water00
1
A: SECRETED PROTEIN BARF1
B: SECRETED PROTEIN BARF1
C: SECRETED PROTEIN BARF1
D: SECRETED PROTEIN BARF1
E: SECRETED PROTEIN BARF1
F: SECRETED PROTEIN BARF1
G: MACROPHAGE COLONY-STIMULATING FACTOR 1
H: MACROPHAGE COLONY-STIMULATING FACTOR 1
I: MACROPHAGE COLONY-STIMULATING FACTOR 1
J: MACROPHAGE COLONY-STIMULATING FACTOR 1
K: MACROPHAGE COLONY-STIMULATING FACTOR 1
L: MACROPHAGE COLONY-STIMULATING FACTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)253,96118
Polymers247,68512
Non-polymers6,2766
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area35730 Å2
ΔGint-10.5 kcal/mol
Surface area93500 Å2
MethodPISA
2
M: SECRETED PROTEIN BARF1
N: SECRETED PROTEIN BARF1
O: SECRETED PROTEIN BARF1
P: SECRETED PROTEIN BARF1
Q: SECRETED PROTEIN BARF1
R: SECRETED PROTEIN BARF1
S: MACROPHAGE COLONY-STIMULATING FACTOR 1
T: MACROPHAGE COLONY-STIMULATING FACTOR 1
U: MACROPHAGE COLONY-STIMULATING FACTOR 1
V: MACROPHAGE COLONY-STIMULATING FACTOR 1
W: MACROPHAGE COLONY-STIMULATING FACTOR 1
X: MACROPHAGE COLONY-STIMULATING FACTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)254,28518
Polymers247,68512
Non-polymers6,6006
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area36350 Å2
ΔGint-1.5 kcal/mol
Surface area94650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)218.440, 218.440, 331.170
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.3802, 0.8789, 0.2882), (0.8876, -0.4342, 0.1534), (0.26, 0.1975, -0.9452)-11.9754, -26.4457, 146.5728
2given(-0.06, -0.6682, -0.7416), (-0.7113, 0.5498, -0.4379), (0.7003, 0.5013, -0.5082)-57.0679, -43.4434, 164.3233
3given(-0.4285, 0.3652, -0.8265), (0.3787, -0.7579, -0.5312), (-0.8203, -0.5406, 0.1865)-22.8723, -34.0066, -31.1434
4given(-0.8158, 0.0583, 0.5753), (0.1629, -0.9314, 0.3254), (0.5549, 0.3592, 0.7504)-150.4641, -109.7784, 69.7763
5given(-0.0273, -0.6964, 0.7171), (-0.7052, 0.5219, 0.48), (-0.7085, -0.4926, -0.5054)-146.3162, -101.0406, 20.3415
6given(0.8752, 0.0153, -0.4835), (-0.2001, 0.9214, -0.333), (0.4404, 0.3882, 0.8095)35.7667, -52.7992, 90.5062
7given(0.2791, 0.9262, -0.2535), (0.9385, -0.319, -0.1321), (-0.2032, -0.201, -0.9583)-19.1516, 41.8933, 62.3786
8given(-0.8066, 0.0239, -0.5906), (0.228, -0.9093, -0.3482), (-0.5453, -0.4155, 0.728)-131.0981, -31.6164, -16.8411
9given(-0.2574, -0.9046, -0.3397), (-0.9025, 0.3507, -0.2502), (0.3454, 0.2422, -0.9066)-93.2644, -132.6127, 121.197
10given(-0.4989, 0.2938, 0.8153), (0.4367, -0.7274, 0.5293), (0.7486, 0.6201, 0.2346)-131.1521, -30.7066, 138.3157
11given(0.3967, -0.3569, 0.8457), (-0.4965, 0.6915, 0.5247), (-0.7721, -0.628, 0.0971)-50.5125, -106.2829, -26.3359
12given(-0.0862, 0.7755, -0.6254), (0.7766, -0.3409, -0.5297), (-0.624, -0.5314, -0.5729)-86.6694, 75.9797, -32.302
13given(0.1699, -0.7196, -0.6733), (-0.6588, 0.4252, -0.6207), (0.7329, 0.549, -0.4018)-78.3533, -59.0174, 110.7804
14given(-0.9845, 0.0513, -0.1677), (-0.0382, -0.996, -0.0802), (-0.1711, -0.0726, 0.9826)-195.2462, -24.9015, -15.7065
15given(0.1582, -0.7434, 0.6498), (-0.7461, 0.3411, 0.5718), (-0.6468, -0.5753, -0.5007)-112.1727, -95.0428, -34.9037
16given(-0.1805, 0.7201, 0.6699), (0.7195, -0.3677, 0.5892), (0.6706, 0.5884, -0.4518)-129.0869, 40.4984, 106.9487
17given(0.452, 0.8759, 0.1689), (0.8779, -0.4703, 0.0896), (0.1579, 0.1078, -0.9816)1.5056, -27.0973, 130.5347
18given(-0.0865, -0.6303, -0.7715), (-0.6389, 0.6293, -0.4425), (0.7644, 0.4546, -0.4571)-53.4391, -36.6886, 160.4976
19given(-0.4621, 0.3147, -0.8291), (0.3308, -0.8062, -0.4905), (-0.8228, -0.5009, 0.2685)-26.2274, -43.223, -38.2439
20given(-0.1042, -0.6963, 0.7102), (-0.7456, 0.5272, 0.4075), (-0.6582, -0.4871, -0.5741)-149.265, -101.6087, 24.2202
21given(-0.8126, 0.0295, 0.5821), (0.2108, -0.9163, 0.3405), (0.5435, 0.3994, 0.7383)-151.4188, -107.7135, 71.3844

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Components

#1: Protein
SECRETED PROTEIN BARF1 / BARF1 / 33 KDA EARLY PROTEIN / P33


Mass: 23412.654 Da / Num. of mol.: 12 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HUMAN HERPESVIRUS 4 (Epstein-Barr virus)
Strain: B95-8 / Cell line (production host): HEK293T / Production host: HOMO SAPIENS (human) / References: UniProt: P0CW72, UniProt: P03228*PLUS
#2: Protein
MACROPHAGE COLONY-STIMULATING FACTOR 1 / HCSF-1 / CSF-1 / M-CSF / MCSF / LANIMOSTIM / PROCESSED MACROPHAGE COLONY-STIMULATING FACTOR 1


Mass: 17868.219 Da / Num. of mol.: 12 / Fragment: UNP RESIDUES 33-181
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS RIL / References: UniProt: P09603
#3: Polysaccharide
alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(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: 1072.964 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e6-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(6+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#4: Polysaccharide
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(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: 1235.105 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#5: Polysaccharide
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
Compound detailsENGINEERED RESIDUE IN CHAIN A, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN B, THR 169 TO SER ...ENGINEERED RESIDUE IN CHAIN A, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN B, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN C, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN D, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN E, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN F, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN M, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN N, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN O, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN P, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN Q, THR 169 TO SER ENGINEERED RESIDUE IN CHAIN R, THR 169 TO SER
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: 4.6 Å3/Da / Density % sol: 74.1 % / Description: NONE
Crystal growpH: 8.5
Details: 0.1 M TRIS HCL, PH 8.50, 1.0 M AMMONIUM PHOSPHATE MONOBASIC

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.9714
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 11, 2009
RadiationMonochromator: BARTELS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9714 Å / Relative weight: 1
ReflectionResolution: 4.4→75.85 Å / Num. obs: 58151 / % possible obs: 99.4 % / Observed criterion σ(I): 2 / Redundancy: 5.6 % / Biso Wilson estimate: 165.84 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 13.5
Reflection shellResolution: 4.4→4.51 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 2.8 / % possible all: 98.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2CH8, 3UF2

2ch8

3uf2


Resolution: 4.4→75.847 Å / SU ML: 0.45 / σ(F): 1.34 / Phase error: 27.5 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2763 2872 4.9 %
Rwork0.2376 --
obs0.2395 58094 99.12 %
Solvent computationShrinkage radii: 1.11 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 187.195 Å2 / ksol: 0.317 e/Å3
Displacement parametersBiso mean: 216.8 Å2
Baniso -1Baniso -2Baniso -3
1-19.4246 Å20 Å20 Å2
2--19.4246 Å20 Å2
3----38.8493 Å2
Refinement stepCycle: LAST / Resolution: 4.4→75.847 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms31549 0 864 0 32413
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00633275
X-RAY DIFFRACTIONf_angle_d1.29245139
X-RAY DIFFRACTIONf_dihedral_angle_d21.61712385
X-RAY DIFFRACTIONf_chiral_restr0.075276
X-RAY DIFFRACTIONf_plane_restr0.0055606
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.4-4.47220.40541340.34562565X-RAY DIFFRACTION97
4.4722-4.54930.35621370.32222604X-RAY DIFFRACTION99
4.5493-4.6320.34011360.30782564X-RAY DIFFRACTION99
4.632-4.7210.29951390.2832631X-RAY DIFFRACTION99
4.721-4.81740.28841370.28142563X-RAY DIFFRACTION99
4.8174-4.92210.3191380.26932614X-RAY DIFFRACTION100
4.9221-5.03660.31381380.24932627X-RAY DIFFRACTION99
5.0366-5.16250.29041390.23562628X-RAY DIFFRACTION100
5.1625-5.30210.28061360.22822605X-RAY DIFFRACTION99
5.3021-5.45810.31841390.22492618X-RAY DIFFRACTION99
5.4581-5.63420.30281360.23412594X-RAY DIFFRACTION99
5.6342-5.83550.30821380.22882637X-RAY DIFFRACTION99
5.8355-6.0690.26941390.22072638X-RAY DIFFRACTION100
6.069-6.34510.28781370.22332610X-RAY DIFFRACTION99
6.3451-6.67940.25551380.21952648X-RAY DIFFRACTION99
6.6794-7.09760.27311380.21032654X-RAY DIFFRACTION99
7.0976-7.64520.26061390.19392648X-RAY DIFFRACTION100
7.6452-8.41370.25061400.21012649X-RAY DIFFRACTION99
8.4137-9.6290.22681400.19732663X-RAY DIFFRACTION99
9.629-12.12360.22421410.19342676X-RAY DIFFRACTION98
12.1236-75.8580.28821130.29392786X-RAY DIFFRACTION97

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