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- PDB-2noj: Crystal structure of Ehp / C3d complex -

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Basic information

Entry
Database: PDB / ID: 2noj
TitleCrystal structure of Ehp / C3d complex
Components
  • Complement C3
  • Efb homologous protein
KeywordsIMMUNE SYSTEM / PROTEIN-PROTEIN COMPLEX
Function / homology
Function and homology information


oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement binding / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / positive regulation of G protein-coupled receptor signaling pathway ...oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement binding / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of lipid storage / positive regulation of phagocytosis, engulfment / complement receptor mediated signaling pathway / Activation of C3 and C5 / positive regulation of type IIa hypersensitivity / positive regulation of glucose transmembrane transport / complement-dependent cytotoxicity / complement activation, alternative pathway / complement activation / neuron remodeling / endopeptidase inhibitor activity / amyloid-beta clearance / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / Peptide ligand-binding receptors / fatty acid metabolic process / complement activation, classical pathway / Regulation of Complement cascade / Post-translational protein phosphorylation / response to bacterium / positive regulation of receptor-mediated endocytosis / positive regulation of angiogenesis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / G alpha (i) signalling events / secretory granule lumen / blood microparticle / inflammatory response / positive regulation of protein phosphorylation / immune response / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / signaling receptor binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Extracellular fibrinogen binding protein, C-terminal / Efb, C-terminal domain superfamily / Extracellular fibrinogen binding protein C terminal / Sbi, C3 binding domain IV / Sbi, C3 binding domain IV / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Complement C3-like, NTR domain ...Extracellular fibrinogen binding protein, C-terminal / Efb, C-terminal domain superfamily / Extracellular fibrinogen binding protein C terminal / Sbi, C3 binding domain IV / Sbi, C3 binding domain IV / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Complement C3-like, NTR domain / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / : / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system domain / Anaphylatoxin domain signature. / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Glycosyltransferase - #20 / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor binding domain / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin / Macroglobulin domain / Alpha-2-macroglobulin, bait region domain / Alpha-macroglobulin-like, TED domain / Alpha-2-macroglobulin family / MG2 domain / A-macroglobulin TED domain / Alpha-2-macroglobulin bait region domain / Alpha-2-Macroglobulin / Alpha-2-macroglobulin family / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Arc Repressor Mutant, subunit A / Immunoglobulin-like fold / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Fibrinogen-binding protein / Complement C3 / Fibrinogen-binding protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Staphylococcus aureus subsp. aureus Mu50 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsHammel, M. / Geisbrecht, B.V.
CitationJournal: J.Biol.Chem. / Year: 2007
Title: Characterization of Ehp, a Secreted Complement Inhibitory Protein from Staphylococcus aureus.
Authors: Hammel, M. / Sfyroera, G. / Pyrpassopoulos, S. / Ricklin, D. / Ramyar, K.X. / Pop, M. / Jin, Z. / Lambris, J.D. / Geisbrecht, B.V.
History
DepositionOct 25, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 14, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jan 22, 2020Group: Database references / Derived calculations
Category: pdbx_struct_assembly / pdbx_struct_assembly_gen / struct_ref_seq_dif
Item: _struct_ref_seq_dif.details
Revision 1.3Oct 20, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Aug 30, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Complement C3
B: Efb homologous protein
C: Complement C3
D: Efb homologous protein
E: Complement C3
F: Efb homologous protein
G: Complement C3
H: Efb homologous protein


Theoretical massNumber of molelcules
Total (without water)170,9608
Polymers170,9608
Non-polymers00
Water1,27971
1
A: Complement C3
B: Efb homologous protein


Theoretical massNumber of molelcules
Total (without water)42,7402
Polymers42,7402
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Complement C3
D: Efb homologous protein


Theoretical massNumber of molelcules
Total (without water)42,7402
Polymers42,7402
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Complement C3
F: Efb homologous protein


Theoretical massNumber of molelcules
Total (without water)42,7402
Polymers42,7402
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
G: Complement C3
H: Efb homologous protein


Theoretical massNumber of molelcules
Total (without water)42,7402
Polymers42,7402
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)67.894, 91.025, 122.595
Angle α, β, γ (deg.)90.00, 89.93, 90.00
Int Tables number4
Space group name H-MP1211
DetailsThe biological assembly is a tetramer in the asymmetric unit

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Components

#1: Protein
Complement C3


Mass: 33143.879 Da / Num. of mol.: 4 / Fragment: Residues 996-1287 / Mutation: C1010A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: C3 / Plasmid: pT7- / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P01024
#2: Protein
Efb homologous protein


Mass: 9596.170 Da / Num. of mol.: 4 / Fragment: Residues 30-109 / Mutation: N63E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus subsp. aureus Mu50 (bacteria)
Species: Staphylococcus aureus / Strain: Mu50 / ATCC 700699 / Gene: SAV1155 / Plasmid: pT7HMT / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q99UV2, UniProt: A0A0H3JUX1*PLUS
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 71 / 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: 2.22 Å3/Da / Density % sol: 44.51 %
Crystal growTemperature: 293 K / pH: 8.2
Details: 0.2M LiSO4, 25% PEG 3350, 0.1M Tris-HCl pH 8.2, additive: CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 0.9184 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 16, 2006 / Details: MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 2.699→50 Å / Num. obs: 33242 / % possible obs: 80.8 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.189

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
DENZOdata reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2GOX
Resolution: 2.7→50 Å / Cor.coef. Fo:Fc: 0.891 / Cor.coef. Fo:Fc free: 0.891 / SU B: 31.446 / SU ML: 0.308 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.466 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.284 1655 5 %RANDOM
Rwork0.291 ---
obs0.29 31582 80.6 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 48.51 Å2
Baniso -1Baniso -2Baniso -3
1-1.04 Å20 Å2-0.33 Å2
2---2.81 Å20 Å2
3---1.77 Å2
Refine analyzeLuzzati coordinate error obs: 0.4829 Å
Refinement stepCycle: LAST / Resolution: 2.7→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9697 0 0 71 9768
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0229882
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3371.93213494
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg1.11251322
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.74724.457368
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.184151363
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.4811533
X-RAY DIFFRACTIONr_chiral_restr0.0940.21611
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.027484
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2950.25707
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3320.27138
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1670.2439
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2870.2125
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.230.27
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.881.56676
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it3.196210436
X-RAY DIFFRACTIONr_scbond_it2.29333206
X-RAY DIFFRACTIONr_scangle_it3.4814.53058
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.7→2.77 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.357 123 -
Rwork0.334 2087 -
obs--73.3 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.3120.42570.17411.24840.32260.108-0.0341-0.01870.0789-0.0359-0.02370.09610.10070.03540.05780.0842-0.018-0.00870.09070.02440.114430.98052.49155.6254
20.71170.79521.00371.24790.45032.66970.0152-0.0551-0.0551-0.39570.1753-0.06810.05870.0296-0.19040.14070.006-0.01680.0026-0.01550.071233.6484-11.905145.6855
30.342-0.250.52450.2057-0.21182.0904-0.4651-0.2304-0.2177-0.8530.26720.0609-0.4312-0.03430.19790.3532-0.1206-0.08430.0137-0.0459-0.082927.9195-7.682633.7678
41.1486-0.71561.13460.4476-0.75382.3655-0.061-0.2637-0.1495-0.237-0.2670.3384-0.27180.34620.3280.2104-0.0849-0.22570.0197-0.02930.077520.61963.355939.0698
51.2935-1.44671.54991.618-1.73341.85710.39730.02370.7217-0.3507-0.1466-0.56060.0899-0.0451-0.25070.0702-0.04120.05110.0682-0.00070.16647.74119.076749.3375
61.5595-3.15140.2866.4867-0.16951.46160.21050.1072-0.0895-0.5746-0.0896-0.0678-0.2563-0.0139-0.1210.1133-0.0069-0.02630.01360.03990.145939.464316.447949.9148
70.5353-0.7163-0.78691.46921.24851.2316-0.2825-0.2378-0.1678-0.07390.33290.10990.12160.0011-0.05040.05460.01010.00850.0705-0.05890.130144.619115.707758.0551
80.9841-0.07660.61890.4696-0.19390.4351-0.025-0.10760.0276-0.1007-0.0927-0.05960.0211-0.07070.11760.07190.01330.01980.0702-0.02290.127636.797439.97095.7878
90.9660.35160.50051.1637-0.98161.56690.122-0.0238-0.1430.13830.01670.0711-0.00660.0128-0.13870.09570.0471-0.04730.05190.05820.108234.618325.135315.7439
100.71160.75210.24471.37890.96560.94-0.12870.0417-0.31030.60730.1727-0.1303-0.101-0.0637-0.0440.27670.0446-0.10130.13730.1918-0.115639.875629.439527.4675
110.02660.08590.29562.57121.60843.4758-0.20130.3693-0.43610.4109-0.3214-0.1564-0.6646-0.05110.52270.1358-0.0457-0.12940.10130.10350.053347.480240.869421.9919
127.78811.9714-12.5531.5046-16.657130.4393-0.8242-0.68390.5102-0.14140.27690.6456-0.59-0.58660.5473-0.03180.16740.18670.0246-0.04170.085116.154452.834614.0057
131.74631.7045-0.44261.82990.05351.531-0.0374-0.08220.11240.16550.03830.11310.0810.1198-0.00090.080.0093-0.03190.0315-0.03510.163226.016254.086110.7411
140.18250.3818-0.3590.799-0.75120.7062-0.6215-0.07710.154-0.31720.39330.05350.15130.06910.2282-0.0021-0.0280.0070.1205-0.03280.193624.652454.78822.2382
150.0333-0.12310.02391.42030.3580.2237-0.0326-0.011-0.0508-0.02790.03060.0888-0.0070.07080.00210.06490.0205-0.01190.07850.01590.1278-1.941-1.96576.565
162.62881.12760.11830.65770.55991.4946-0.0802-0.18680.40810.1897-0.03110.29570.1679-0.08890.11130.12060.0696-0.01560.0241-0.04480.1262-3.573211.698516.0308
170.4240.6295-0.51831.4462-0.0831.555-0.15370.15610.19880.96410.0250.26530.20020.15170.12870.30110.09070.16880.0938-0.0657-0.0677-8.79363.808626.6818
181.00431.3205-0.33942.4754-2.67576.8387-0.17390.16640.26970.3782-0.25080.21460.2031-0.14910.42470.17570.16080.10650.0605-0.05150.0077-12.2844-4.42216.307
193.02645.1794-0.381244.77446.26971.3823-1.3018-0.8552-0.28641.95521.9157-0.82041.41240.3448-0.6140.09750.1169-0.14670.0680.03850.107218.2319-15.786713.6471
201.24111.03680.93121.5679-0.70043.8129-0.1101-0.28630.0530.00520.07350.01760.12180.06290.03660.10590.04930.041-0.02410.02130.14437.7785-17.408310.8681
210.98092.11680.82624.56841.78310.6959-0.21510.40290.11310.03820.4150.19350.09580.1394-0.19990.05470.0188-0.0130.0627-0.00990.15859.8841-17.32062.4964
224.3309-3.89760.65794.2746-1.11160.45180.02410.1494-0.214-0.1548-0.09730.2262-0.38810.40240.0732-0.0140.0027-0.06610.1072-0.01270.174410.4111-40.271358.1189
231.056-0.3013-0.24120.5923-0.04380.0802-0.0849-0.0093-0.0536-0.0640.10240.10070.0208-0.0233-0.01750.0984-0.0015-0.00710.0404-0.0250.13961.9856-41.145254.679
240.8673-0.5099-0.71440.42110.43820.59120.06940.13390.2335-0.166-0.08-0.00750.0161-0.13060.01060.05880.0063-0.02690.12670.11390.110.2211-26.939141.5433
250.09660.3566-0.01041.6706-0.81651.7096-0.2167-0.49160.2571-0.65490.0395-0.08260.49190.1720.17720.2277-0.06180.15240.03570.08150.034613.8282-37.856337.5048
269.2563-16.953714.211331.052-26.029221.8188-0.5112-0.57440.0948-2.66962.7131-0.1251.9019-1.5448-2.2019-0.0237-0.1383-0.0708-0.0264-0.01390.2972-17.6989-53.575247.7128
272.4068-1.43691.20720.8837-0.97623.12930.0049-0.08560.3731-0.33110.4345-0.37530.5723-0.2349-0.43940.0928-0.02150.05350.0108-0.05780.1155-5.231-57.430250.1626
281.2712-2.20180.55983.8278-0.84071.4063-0.2884-0.04740.07660.06460.2124-0.2399-0.1396-0.13760.076-0.0052-0.02930.00930.09690.0160.1834-10.7463-53.132457.3727
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1001 - 109711 - 107
2X-RAY DIFFRACTION2AA1098 - 1156108 - 166
3X-RAY DIFFRACTION3AA1157 - 1228167 - 238
4X-RAY DIFFRACTION4AA1229 - 1286239 - 296
5X-RAY DIFFRACTION5BB52 - 6723 - 38
6X-RAY DIFFRACTION6BB68 - 8439 - 55
7X-RAY DIFFRACTION7BB85 - 10956 - 80
8X-RAY DIFFRACTION8CC1001 - 109811 - 108
9X-RAY DIFFRACTION9CC1099 - 1154109 - 164
10X-RAY DIFFRACTION10CC1155 - 1228165 - 238
11X-RAY DIFFRACTION11CC1229 - 1287239 - 297
12X-RAY DIFFRACTION12DD52 - 5923 - 30
13X-RAY DIFFRACTION13DD60 - 8731 - 58
14X-RAY DIFFRACTION14DD88 - 10959 - 80
15X-RAY DIFFRACTION15EE997 - 11117 - 121
16X-RAY DIFFRACTION16EE1112 - 1155122 - 165
17X-RAY DIFFRACTION17EE1156 - 1260166 - 270
18X-RAY DIFFRACTION18EE1261 - 1287271 - 297
19X-RAY DIFFRACTION19FF52 - 5923 - 30
20X-RAY DIFFRACTION20FF60 - 8631 - 57
21X-RAY DIFFRACTION21FF87 - 10958 - 80
22X-RAY DIFFRACTION22GG997 - 10197 - 29
23X-RAY DIFFRACTION23GG1020 - 109730 - 107
24X-RAY DIFFRACTION24GG1098 - 1193108 - 203
25X-RAY DIFFRACTION25GG1194 - 1286204 - 296
26X-RAY DIFFRACTION26HH52 - 6023 - 31
27X-RAY DIFFRACTION27HH61 - 8132 - 52
28X-RAY DIFFRACTION28HH82 - 10953 - 80

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