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- PDB-4cpi: streptavidin A86D mutant with love-hate ligand 4 -

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Basic information

Entry
Database: PDB / ID: 4cpi
Titlestreptavidin A86D mutant with love-hate ligand 4
ComponentsSTREPTAVIDIN
KeywordsBIOTIN BINDING PROTEIN / AVIDIN / BIOTIN / STRAIN / BIOTINYLATED / STERIC CLASH / STRAINED / HINDERED / FORCE / LIGAND SERIES / AFFINITY
Function / homology
Function and homology information


biotin binding / extracellular region
Similarity search - Function
Avidin-like / Avidin-like, conserved site / Avidin-like domain signature. / Avidin / Avidin/streptavidin / Avidin-like superfamily / Avidin family / Avidin-like domain profile. / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Chem-LH4 / DI(HYDROXYETHYL)ETHER / Streptavidin
Similarity search - Component
Biological speciesSTREPTOMYCES AVIDINII (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.54 Å
AuthorsFairhead, M. / Shen, D. / Chan, L.K.M. / Lowe, E.D. / Donohoe, T.J. / Howarth, M.
CitationJournal: Bioorg.Med.Chem. / Year: 2014
Title: Love-Hate Ligands for High Resolution Analysis of Strain in Ultra-Stable Protein/Small Molecule Interaction.
Authors: Fairhead, M. / Shen, D. / Chan, L.K.M. / Lowe, E.D. / Donohoe, T.J. / Howarth, M.
History
DepositionFeb 6, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 6, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 27, 2014Group: Database references
Revision 1.2Oct 1, 2014Group: Database references
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_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.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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: STREPTAVIDIN
B: STREPTAVIDIN
C: STREPTAVIDIN
D: STREPTAVIDIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,94614
Polymers53,3014
Non-polymers3,64410
Water5,603311
1
D: STREPTAVIDIN
hetero molecules

D: STREPTAVIDIN
hetero molecules

C: STREPTAVIDIN
hetero molecules

C: STREPTAVIDIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,94614
Polymers53,3014
Non-polymers3,64410
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_758-x+2,y,-z+31
crystal symmetry operation3_555x+1/2,y+1/2,z1
crystal symmetry operation4_658-x+3/2,y+1/2,-z+31
Buried area10480 Å2
ΔGint-61.5 kcal/mol
Surface area19530 Å2
MethodPISA
2
A: STREPTAVIDIN
B: STREPTAVIDIN
hetero molecules

A: STREPTAVIDIN
B: STREPTAVIDIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,94614
Polymers53,3014
Non-polymers3,64410
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_657-x+1,y,-z+21
Buried area10420 Å2
ΔGint-66.1 kcal/mol
Surface area19440 Å2
MethodPISA
3
C: STREPTAVIDIN
hetero molecules

C: STREPTAVIDIN
hetero molecules

D: STREPTAVIDIN
hetero molecules

D: STREPTAVIDIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,94614
Polymers53,3014
Non-polymers3,64410
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_658-x+1,y,-z+31
crystal symmetry operation4_648-x+3/2,y-1/2,-z+31
crystal symmetry operation3_445x-1/2,y-1/2,z1
Buried area3100 Å2
ΔGint-17.5 kcal/mol
Surface area11090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)81.260, 81.250, 90.690
Angle α, β, γ (deg.)90.00, 103.84, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11C-2029-

HOH

21D-2030-

HOH

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Components

#1: Protein
STREPTAVIDIN /


Mass: 13325.346 Da / Num. of mol.: 4 / Fragment: RESIDUES 37-163 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) STREPTOMYCES AVIDINII (bacteria) / Plasmid: PET21 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): RIPL / References: UniProt: P22629
#2: Chemical
ChemComp-LH4 / 5-[(3aS,4S,6aR)-2-oxo-hexahydro-1H-thieno[3,4- d]imidazolidin-4-yl]-N'-{2,6-bis[4-(morpholine-4- sulfonyl)phenyl]phenyl}pentanehydrazide


Mass: 784.965 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C36H44N6O8S3
#3: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 311 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsN-TERMINAL METHIONINE REMOVED IN MATURE PROTEIN, ALANINE 86 ASPARTATE MUTATION

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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: 2.7 Å3/Da / Density % sol: 54 % / Description: NONE
Crystal growMethod: vapor diffusion, sitting drop / pH: 8.5
Details: CONDITION A9 OF THE MORPHEUS SCREEN: 0.1 M BICINE/TRIZMA BASE PH 8.5, 10% W/V POLYETHYLENE GLYCOL 20,000, 20% V/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 550, 30 MM MAGNESIUM CHLORIDE AND 30 MM ...Details: CONDITION A9 OF THE MORPHEUS SCREEN: 0.1 M BICINE/TRIZMA BASE PH 8.5, 10% W/V POLYETHYLENE GLYCOL 20,000, 20% V/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 550, 30 MM MAGNESIUM CHLORIDE AND 30 MM CALCIUM CHLORIDE. SITTING DROP.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.98
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 13, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.54→39.45 Å / Num. obs: 84164 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 17.55 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 15.6
Reflection shellResolution: 1.54→1.6 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 2.34 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
xia2data reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3RY1
Resolution: 1.54→39.45 Å / SU ML: 0.16 / σ(F): 1.34 / Phase error: 17.95 / Stereochemistry target values: ML
Details: RESIDUES 46-48 ARE MODELLED STEREOCHEMICALLY DUE TO POOR DENSITY IN CHAINS A AND D. 46-48 ARE OMITTED FROM CHAINS B AND C. LH4 B1000 AND C1000 REPRESENT LH4 SHOWN WITHOUT THE AROMATIC ...Details: RESIDUES 46-48 ARE MODELLED STEREOCHEMICALLY DUE TO POOR DENSITY IN CHAINS A AND D. 46-48 ARE OMITTED FROM CHAINS B AND C. LH4 B1000 AND C1000 REPRESENT LH4 SHOWN WITHOUT THE AROMATIC HEADGROUP BECAUSE OF WEAK ELECTRON DENSITY
RfactorNum. reflection% reflection
Rfree0.1815 4202 5 %
Rwork0.1571 --
obs0.1583 84162 99.55 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 25.1 Å2
Refinement stepCycle: LAST / Resolution: 1.54→39.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3568 0 170 311 4049
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0084166
X-RAY DIFFRACTIONf_angle_d1.1695725
X-RAY DIFFRACTIONf_dihedral_angle_d12.4351468
X-RAY DIFFRACTIONf_chiral_restr0.048621
X-RAY DIFFRACTIONf_plane_restr0.006765
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.54-1.55750.30071300.26132681X-RAY DIFFRACTION100
1.5575-1.57580.26961380.25212607X-RAY DIFFRACTION99
1.5758-1.5950.27731650.23852698X-RAY DIFFRACTION100
1.595-1.61520.26521370.23432584X-RAY DIFFRACTION100
1.6152-1.63650.22821210.21842719X-RAY DIFFRACTION100
1.6365-1.65890.20981370.20652665X-RAY DIFFRACTION100
1.6589-1.68260.23111400.19642661X-RAY DIFFRACTION100
1.6826-1.70770.24611440.18862628X-RAY DIFFRACTION100
1.7077-1.73440.19791470.17952719X-RAY DIFFRACTION100
1.7344-1.76280.191210.16592645X-RAY DIFFRACTION100
1.7628-1.79320.2061190.16322673X-RAY DIFFRACTION100
1.7932-1.82580.1771500.15842640X-RAY DIFFRACTION100
1.8258-1.8610.16371570.15182674X-RAY DIFFRACTION100
1.861-1.8990.18661130.15562681X-RAY DIFFRACTION100
1.899-1.94020.20281300.15462669X-RAY DIFFRACTION100
1.9402-1.98540.17231510.14662659X-RAY DIFFRACTION100
1.9854-2.0350.15451570.14592644X-RAY DIFFRACTION100
2.035-2.090.17531200.14622667X-RAY DIFFRACTION100
2.09-2.15150.16471730.14732630X-RAY DIFFRACTION100
2.1515-2.2210.17721460.14432683X-RAY DIFFRACTION100
2.221-2.30040.16691330.152689X-RAY DIFFRACTION100
2.3004-2.39240.17951530.15882661X-RAY DIFFRACTION100
2.3924-2.50130.18171360.1592648X-RAY DIFFRACTION100
2.5013-2.63320.18911350.15592678X-RAY DIFFRACTION100
2.6332-2.79810.18451360.15142657X-RAY DIFFRACTION99
2.7981-3.01410.17811470.14942678X-RAY DIFFRACTION99
3.0141-3.31720.17061490.15282631X-RAY DIFFRACTION99
3.3172-3.79690.18461550.14542678X-RAY DIFFRACTION99
3.7969-4.78240.13541210.13322693X-RAY DIFFRACTION99
4.7824-39.46330.18811410.16342720X-RAY DIFFRACTION99
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)
13.8326-0.50941.49744.2117-0.943.17480.0271-0.1195-0.37250.0040.08220.14520.1739-0.1199-0.20010.1765-0.03270.00120.11050.02450.20794.5912-8.404490.2737
25.7582-0.41862.97014.1977-1.89837.0290.1476-0.2312-0.2974-0.0430.44070.80480.2911-0.5126-0.23430.1672-0.0164-0.00920.15210.02810.268-2.1488-3.294787.8387
37.8232-1.77813.74414.2389-0.97876.9309-0.145-0.2912-0.49440.09190.3250.36240.0503-0.5249-0.2080.1452-0.02710.0230.13710.05080.2542-1.7488-0.897691.5979
40.00820.15160.16223.30623.44773.5956-0.04321.2860.594-0.60560.17260.4068-0.3231-0.0171-0.00930.76730.2097-0.27230.79650.16350.5213.5961-6.5404103.7417
51.86080.2527-0.86931.90620.81315.22840.135-0.2016-0.09740.20020.12430.23390.374-0.4592-0.17490.1277-0.0229-0.00660.1480.04230.2108-1.20411.341693.6737
62.1226-0.3827-0.01162.64980.89764.11250.06110.2981-0.2284-0.33860.05390.16820.24-0.0396-0.09830.1754-0.0269-0.04620.1573-00.19414.21160.341978.4616
71.5064-0.1248-0.09052.39830.91183.8896-0.0218-0.2103-0.07090.29360.09460.18780.2083-0.2592-0.05940.1272-0.0020.01430.1350.04330.15514.53213.532296.7
82.9072.77190.45166.87634.98244.95360.01810.4564-1.1268-0.18660.0013-0.39911.28490.5757-0.20490.597-0.0131-0.07720.2011-0.06780.47697.5092-14.710879.4589
93.66852.00381.59947.87154.9026.35980.02880.0973-0.25810.01020.2592-0.22260.25140.1652-0.31110.10470.0017-0.00370.0660.02580.102611.82551.173889.7084
106.43372.6176-0.78758.8696.05798.5173-0.1596-0.35910.70580.21280.4445-0.4958-0.24360.424-0.17360.20920.0119-0.02860.1671-0.06180.231817.244517.4961101.565
112.55560.72510.32424.83451.83322.31970.06670.0182-0.50770.08120.0264-0.04580.3412-0.1937-0.07880.1569-0.0168-0.0270.11150.04260.169610.3746-6.339190.2281
125.55971.242-1.30017.1553-1.58823.8004-0.14680.13330.0704-0.12920.19610.1672-0.1606-0.1494-0.05880.11670.0377-0.01680.1160.01990.18190.697119.925285.6979
131.88350.48340.10252.4791.28065.17710.0625-0.08730.09870.12410.15630.2318-0.2795-0.152-0.15180.12490.03940.03070.11330.02910.20051.729314.533390.6836
141.82660.12150.56142.9181.573.9421-0.01160.18650.0601-0.21340.16540.1346-0.2082-0.0395-0.11880.1122-0.0073-0.00080.09060.04510.13634.342311.917179.557
152.6583-1.1081-0.70493.98311.30862.82440.05950.07560.2806-0.03730.059-0.1588-0.1827-0.0528-0.02670.0911-0.00760.00320.0770.03020.118412.492814.360384.2347
165.7932-1.8945-2.74617.1742.83494.95560.15860.02010.2818-0.105-0.1272-0.1744-0.22480.048-0.0350.1074-0.03130.00690.14040.02050.176921.5973-4.294131.9768
172.3955-0.4021.22532.2728-0.54625.65070.08660.0780.2252-0.02180.0064-0.1574-0.15060.332-0.05630.1119-0.02450.02680.1166-0.01310.196915.5929-4.177132.4745
182.07820.19590.49482.0162-0.27822.79470.10380.0980.0432-0.112-0.003-0.1621-0.02930.1973-0.09640.07940.00620.0360.0998-0.00720.110914.638-10.473127.4582
198.61152.76683.69913.16210.86653.29210.06250.1631-0.2197-0.12750.0417-0.12880.03410.0738-0.0650.10580.01970.04990.1068-0.0220.078411.8397-16.6645125.1765
203.9196-1.39731.9384.3168-1.96044.1850.227-0.0255-0.3238-0.1053-0.12350.22120.2567-0.0186-0.11110.1224-0.0383-0.03070.14750.0110.225835.20010.9168131.1712
213.8143-1.94161.01728.9735-4.78739.27760.37770.1256-0.3536-0.2306-0.10560.22350.5082-0.0368-0.31090.115-0.0296-0.05170.1296-0.00030.266840.1352-2.0503128.5974
227.03291.1056-1.97460.1757-0.28321.5123-1.20030.62772.0612-1.37010.5951.2597-2.9016-0.76630.68880.75640.2759-0.07380.80110.32850.670734.14663.162116.313
231.9327-0.217-0.78262.64550.98276.72550.1322-0.1522-0.21510.0929-0.01480.1520.2031-0.2888-0.08160.1061-0.0346-0.0290.13080.03550.213741.83761.5697134.8356
243.06570.4115-1.00532.1358-0.37043.72020.15620.2126-0.2174-0.20540.00240.16810.0693-0.3507-0.06610.09640.0041-0.05460.10610.00520.177642.04464.6125.837
253.08051.6741-2.30124.4645-0.75447.15010.3258-0.08860.21070.1061-0.03230.28-0.2763-0.1791-0.28030.05730.0195-0.02040.07040.00130.108442.358111.9059130.6963
267.25251.7982-2.66333.1249-0.7093.0590.15850.22430.1089-0.1833-0.010.1177-0.0437-0.0469-0.10160.09640.0238-0.03460.0890.00830.082244.829113.3858124.924
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 16 THROUGH 27 )
2X-RAY DIFFRACTION2CHAIN A AND (RESID 28 THROUGH 37 )
3X-RAY DIFFRACTION3CHAIN A AND (RESID 38 THROUGH 44 )
4X-RAY DIFFRACTION4CHAIN A AND (RESID 45 THROUGH 49 )
5X-RAY DIFFRACTION5CHAIN A AND (RESID 50 THROUGH 60 )
6X-RAY DIFFRACTION6CHAIN A AND (RESID 61 THROUGH 78 )
7X-RAY DIFFRACTION7CHAIN A AND (RESID 79 THROUGH 97 )
8X-RAY DIFFRACTION8CHAIN A AND (RESID 98 THROUGH 102 )
9X-RAY DIFFRACTION9CHAIN A AND (RESID 103 THROUGH 112 )
10X-RAY DIFFRACTION10CHAIN A AND (RESID 113 THROUGH 122 )
11X-RAY DIFFRACTION11CHAIN A AND (RESID 123 THROUGH 134 )
12X-RAY DIFFRACTION12CHAIN B AND (RESID 15 THROUGH 49 )
13X-RAY DIFFRACTION13CHAIN B AND (RESID 50 THROUGH 78 )
14X-RAY DIFFRACTION14CHAIN B AND (RESID 79 THROUGH 97 )
15X-RAY DIFFRACTION15CHAIN B AND (RESID 98 THROUGH 135 )
16X-RAY DIFFRACTION16CHAIN C AND (RESID 15 THROUGH 37 )
17X-RAY DIFFRACTION17CHAIN C AND (RESID 38 THROUGH 78 )
18X-RAY DIFFRACTION18CHAIN C AND (RESID 79 THROUGH 112 )
19X-RAY DIFFRACTION19CHAIN C AND (RESID 113 THROUGH 134 )
20X-RAY DIFFRACTION20CHAIN D AND (RESID 16 THROUGH 37 )
21X-RAY DIFFRACTION21CHAIN D AND (RESID 38 THROUGH 44 )
22X-RAY DIFFRACTION22CHAIN D AND (RESID 45 THROUGH 49 )
23X-RAY DIFFRACTION23CHAIN D AND (RESID 50 THROUGH 78 )
24X-RAY DIFFRACTION24CHAIN D AND (RESID 79 THROUGH 102 )
25X-RAY DIFFRACTION25CHAIN D AND (RESID 103 THROUGH 112 )
26X-RAY DIFFRACTION26CHAIN D AND (RESID 113 THROUGH 135 )

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