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- PDB-5vcp: Crystal structure of a peptide deformylase from Burkholderia xeno... -

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Basic information

Entry
Database: PDB / ID: 5vcp
TitleCrystal structure of a peptide deformylase from Burkholderia xenovorans in complex with actinonin
ComponentsPeptide deformylase
KeywordsHYDROLASE/HYDROLASE INHIBITOR / SSGCID / Burkholderia xenovorans / peptide deformylase / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / actinonin / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


peptide deformylase / peptide deformylase activity / translation / metal ion binding
Similarity search - Function
Peptide Deformylase / Peptide deformylase / Peptide deformylase / Peptide deformylase superfamily / Polypeptide deformylase / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
ACTINONIN / : / Peptide deformylase
Similarity search - Component
Biological speciesParaburkholderia xenovorans (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.95 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To be Published
Title: Crystal structure of a peptide deformylase from Burkholderia xenovorans in complex with actinonin
Authors: Conrady, D.G. / Abendroth, J. / Lorimer, D.D. / Edwards, T.E.
History
DepositionMar 31, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 3, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 4, 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 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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.ptnr1_symmetry / _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 / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Peptide deformylase
B: Peptide deformylase
C: Peptide deformylase
D: Peptide deformylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,60915
Polymers83,7714
Non-polymers1,83811
Water6,179343
1
A: Peptide deformylase
C: Peptide deformylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,7937
Polymers41,8862
Non-polymers9075
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3460 Å2
ΔGint-48 kcal/mol
Surface area14350 Å2
MethodPISA
2
B: Peptide deformylase
D: Peptide deformylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,8178
Polymers41,8862
Non-polymers9316
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3500 Å2
ΔGint-51 kcal/mol
Surface area14330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)63.110, 90.330, 140.210
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
Peptide deformylase / PDF / Polypeptide deformylase / BuxeA.00078.a


Mass: 20942.793 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Paraburkholderia xenovorans (strain LB400) (bacteria)
Strain: LB400 / Gene: def, Bxe_A1677 / Plasmid: AVA0421 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q13XB1, peptide deformylase
#2: Chemical
ChemComp-FE2 / FE (II) ION


Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe
#3: Chemical
ChemComp-BB2 / ACTINONIN / 2-[(FORMYL-HYDROXY-AMINO)-METHYL]-HEPTANOIC ACID [1-(2-HYDROXYMETHYL-PYRROLIDINE-1-CARBONYL)-2-METHYL-PROPYL]-AMIDE


Mass: 385.498 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C19H35N3O5 / Comment: antitumor, antibiotic*YM
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 343 / 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: 2.39 Å3/Da / Density % sol: 48.44 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 1:1 22 mg/mL BuxeA.00078.a.B1.PS37823 / Rigaku reagents Morpheus A8 (0.03 M magnesium chloride, 0.03 M calcium chloride, 0.1 M HEPES/MOPS, pH 7.5, 12.5% MPD, 12.5% PEG1000, 12.5% PEG3350), ...Details: 1:1 22 mg/mL BuxeA.00078.a.B1.PS37823 / Rigaku reagents Morpheus A8 (0.03 M magnesium chloride, 0.03 M calcium chloride, 0.1 M HEPES/MOPS, pH 7.5, 12.5% MPD, 12.5% PEG1000, 12.5% PEG3350), crystal id: wda5-2 270123a8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 24, 2016
RadiationMonochromator: diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.95→48.536 Å / Num. obs: 59117 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 6.138 % / Biso Wilson estimate: 34.02 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.04 / Rrim(I) all: 0.044 / Χ2: 1.024 / Net I/σ(I): 23.88 / Num. measured all: 362861 / Scaling rejects: 8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
1.95-26.2050.533.7943280.9440.578100
2-2.066.220.4054.7841970.960.44299.9
2.06-2.126.2220.3056.2941140.9760.332100
2.12-2.186.2190.2298.1239950.9840.25100
2.18-2.256.2150.1879.7538840.9870.20399.9
2.25-2.336.2090.14312.2737250.9920.15799.9
2.33-2.426.2270.12113.9836050.9950.13299.9
2.42-2.526.1910.10216.4534950.9960.11199.9
2.52-2.636.2140.08120.2233460.9970.08899.9
2.63-2.766.1890.06624.0331860.9980.07299.8
2.76-2.916.1590.05229.2330610.9980.05799.9
2.91-3.086.1620.04434.0128750.9990.04899.7
3.08-3.36.1230.03639.9827150.9990.0499.9
3.3-3.566.0690.034825620.9990.03399.9
3.56-3.96.0170.02652.3423480.9990.02999.7
3.9-4.366.0060.02456.421410.9990.02699.9
4.36-5.035.9240.02358.1419120.9990.02599.8
5.03-6.175.8760.02357.2316330.9990.02599.9
6.17-8.725.70.02257.5112840.9990.02499.8
8.72-48.5365.0930.02156.677110.9990.02393.4

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHASERphasing
PHENIX1.8.4_1496refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 5KOB
Resolution: 1.95→48.536 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 20.07
RfactorNum. reflection% reflection
Rfree0.1918 1926 3.26 %
Rwork0.1615 --
obs0.1625 59092 99.76 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 123.7 Å2 / Biso mean: 47.11 Å2 / Biso min: 21.27 Å2
Refinement stepCycle: final / Resolution: 1.95→48.536 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4934 0 115 348 5397
Biso mean--66.48 48.96 -
Num. residues----640
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0075198
X-RAY DIFFRACTIONf_angle_d1.0627065
X-RAY DIFFRACTIONf_chiral_restr0.047777
X-RAY DIFFRACTIONf_plane_restr0.006938
X-RAY DIFFRACTIONf_dihedral_angle_d13.4981927
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9499-1.99870.26241320.205540344166100
1.9987-2.05270.25031350.190240454180100
2.0527-2.11310.21051420.179340084150100
2.1131-2.18130.19681250.169240484173100
2.1813-2.25930.2521300.179940964226100
2.2593-2.34970.241340.17340254159100
2.3497-2.45670.24371330.182140384171100
2.4567-2.58620.23241560.177840504206100
2.5862-2.74820.20261370.182440864223100
2.7482-2.96040.26491280.177540424170100
2.9604-3.25820.1931530.176940964249100
3.2582-3.72950.17211350.149941364271100
3.7295-4.69820.14641450.127141524297100
4.6982-48.55070.16871410.16044310445199
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)
12.43921.4432-1.93147.9607-1.85635.00450.0567-0.150.30180.4228-0.07280.6536-0.5174-0.537-0.06730.30320.02810.01770.2749-0.0440.2835-22.09179.49631.2684
28.5725.1989-6.69814.3882-5.85547.98240.1294-0.7364-0.17990.467-0.38270.21070.17550.38310.40310.406-0.02940.05830.3419-0.01080.2392-20.1314-4.565913.1852
35.3497-1.1513.35028.549-5.82996.1907-0.2294-0.15930.51280.30530.36220.518-0.7757-2.2197-0.18560.26580.04360.07240.7153-0.03740.3754-32.52872.736211.0316
41.57790.2593-0.71617.52910.81773.3305-0.06030.0899-0.1294-0.4049-0.17330.62880.3801-0.79230.2060.2802-0.08530.01740.3766-0.050.2412-28.8834-4.36613.0933
52.5685-0.51540.23526.0205-0.74163.48910.06430.1587-0.2057-0.2986-0.21120.16260.4653-0.38260.16070.2794-0.06810.02280.32640.01140.2151-26.7058-4.2159-12.1789
62.27260.8711-0.53523.28742.23033.60250.0945-0.2452-0.02890.7521-0.05870.36321.3853-0.31570.18860.5349-0.14150.09770.34190.00520.3331-28.5835-13.49346.1264
72.21240.2904-0.37312.9503-1.32045.2166-0.052-0.0127-0.29650.01590.03680.31330.6651-0.7811-0.01520.3633-0.09160.05880.2744-0.00440.242-28.161-9.3323-2.2941
84.6735-0.68044.0184.7877-2.89334.72970.18380.3766-0.0915-0.09450.0234-0.17680.481.0574-0.10310.23350.0087-0.01010.2555-0.00170.2419-19.2363-0.1032-11.341
96.9213-0.4699-1.86092.33971.08534.86780.03120.13930.3512-0.33980.11760.3748-0.2852-0.5292-0.17450.27580.0087-0.0380.35420.03390.3177-29.33556.8501-19.229
102.61542.9434-0.21198.7843-2.30683.96110.0348-0.2933-0.23230.7199-0.30530.08380.5761-0.59410.32190.3598-0.05090.07820.32440.00330.3077-26.3001-5.6537-34.2287
117.1864-1.79663.16487.4759-4.80233.5694-0.3662-0.6348-0.0770.9776-0.2408-0.4851-0.40210.14890.81850.42810.02510.0190.36260.01110.2189-12.9839-3.8457-21.7005
128.29370.8883.43055.59020.70762.65680.2875-0.3084-0.7374-0.0404-0.25330.18881.6717-0.4824-0.04250.594-0.0320.03990.24890.05990.3635-19.5405-16.1889-24.8436
136.5529-0.54741.22864.6667-0.82176.97160.03170.198-0.4414-0.16-0.04410.09190.8951-0.03340.01550.30380.00250.04890.22480.03890.209-17.691-10.6096-31.3394
142.60312.05321.29494.37664.10684.0218-1.39160.6818-1.7110.1051.1050.3706-0.193-0.5236-0.00850.84810.10630.15030.6714-0.2051.0368-9.7164-22.8488-37.5664
151.9399-1.1294-2.56710.87621.50187.38590.2127-0.35290.05990.4536-0.4682-0.41250.22681.27870.30320.29390.14880.01090.460.12570.3385-5.5385-8.4978-31.1777
162.10081.02423.54974.62870.77216.72-0.34520.8255-0.2609-0.55830.0507-0.52120.64721.57520.11370.36310.18230.08380.59690.10610.3107-5.451-8.8231-48.9884
172.3647-0.34921.10730.724-1.1963.1155-0.0978-0.0468-0.30680.1164-0.0734-0.06060.66440.53790.11180.38740.16820.03470.37480.03750.2717-10.96-10.8163-37.8356
182.66770.00941.12831.32960.61924.8308-0.04130.0699-0.2442-0.0255-0.1012-0.15330.43010.75320.13260.27380.08740.05070.33280.05080.2334-10.2589-8.3083-40.2329
198.63570.591-0.10627.2777-0.51712.26130.10890.3604-0.7561-0.0804-0.04150.45670.8766-0.1197-0.0270.4030.0141-0.03810.325-0.05680.3115-22.7922-11.7483-55.0754
204.2324.4146-0.22065.6941-1.45138.1468-0.08190.21980.6937-0.14120.37240.5905-0.4269-1.1734-0.24240.31080.0534-0.05420.31930.07530.3785-27.503514.4087-26.2892
214.85650.5337-1.53964.2425-5.56987.5144-0.2381.19070.3627-1.86770.8961.20770.1495-0.9042-0.38480.8634-0.1176-0.0590.45940.09840.4192-18.828817.811-42.8941
225.9555-0.6707-1.1616.26274.82114.50080.0080.20780.92520.8736-0.02271.1585-2.5011-0.1471-0.03941.12880.00320.07370.28590.12350.6486-22.483628.2092-33.8738
232.84311.0505-2.7796.6664-1.99675.78210.2713-0.17870.40650.34830.05010.1404-1.1551-0.062-0.26770.4527-0.0798-0.02080.32990.03620.3163-19.614720.9067-30.5822
246.62855.21116.62996.45334.41867.4679-0.2688-1.58681.68341.7739-1.173-0.7721-2.7873-0.60061.13130.9842-0.2049-0.0750.654-0.04950.538-8.635630.1063-24.6209
254.24270.53641.14841.9198-1.09375.375-0.03120.57630.2273-0.5803-0.1269-0.0175-0.25430.54190.23650.4243-0.15390.02290.38730.00410.3308-8.446718.5639-35.3412
264.8918-3.2096-6.94134.54333.91612.1592-0.131-0.8801-0.06960.07850.2516-0.7530.48071.2376-0.19280.3090.038-0.00080.72310.09480.5423-2.905113.1043-19.0704
273.58791.1514-1.87451.9117-2.09364.5044-0.1320.18770.1974-0.22520.1017-0.1765-0.41790.40920.04320.3878-0.1452-0.0030.3130.00420.3251-11.212618.6162-26.8937
283.70960.4702-1.20623.3558-1.28793.5834-0.25380.14940.1828-0.24330.2547-0.3992-0.59710.7546-0.0250.3703-0.16180.01520.40870.01580.2937-8.009219.139-28.5251
293.63722.4813-1.10356.74732.95083.0984-0.381-0.4632-0.43270.14850.1964-0.1330.27521.13380.07620.22260.0327-0.00020.40150.08160.3133-14.46948.0443-20.0657
302.27970.00510.29879.25990.10463.0009-0.3268-0.52190.31050.7256-0.19770.0266-1.10741.20830.53040.4415-0.07540.00560.42180.0680.4007-16.966314.5599-7.2256
317.5533-0.35434.96393.7954-0.42026.37390.202-0.2855-0.522-0.3576-0.20140.51621.0545-0.7539-0.08790.3883-0.0754-0.06750.3292-0.07310.402-30.6294-9.4577-62.7091
323.5713-0.9384.26141.3956-1.76835.62890.81611.3377-0.4268-1.0218-0.54870.50890.76410.2921-0.35080.65090.2269-0.18360.7379-0.08850.445-32.145-0.6378-78.8731
336.0708-0.4477-0.70826.5697-2.9258.4139-0.01220.0448-0.5341-0.7297-0.29591.71850.3984-2.1537-0.29060.38080.0151-0.23760.9572-0.21640.9328-43.4005-4.1221-70.5444
343.93670.20250.10946.266-2.27014.26480.13610.21470.2386-0.0288-0.10190.7222-0.3429-0.7604-0.03520.29240.12-0.07380.4338-0.10320.3982-36.39873.7203-67.452
353.2463-1.20480.25158.3663-3.22678.9229-0.1214-0.09490.42570.4947-0.3738-0.1737-1.1663-0.36730.37890.30370.0646-0.09480.3247-0.04480.3193-29.25248.3492-54.2007
364.51862.09042.61688.85353.34056.9795-0.39220.43360.4894-0.84080.05980.9049-1.1229-0.5170.51610.6010.2434-0.14660.5760.01890.521-36.272912.0432-72.7341
371.8513-0.02770.16533.7056-1.45224.337-0.126-0.04540.26210.05840.01280.2978-0.8464-0.65970.08050.32760.1154-0.05880.3195-0.03290.3093-30.40347.8658-61.5788
388.7531-0.0659-1.01799.3338-0.3557.6314-0.1813-0.31920.1920.69580.16550.6208-0.4503-0.8221-0.01090.34860.06690.01830.421-0.01720.2966-30.33160.1937-43.3081
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 14 )A2 - 14
2X-RAY DIFFRACTION2chain 'A' and (resid 15 through 25 )A15 - 25
3X-RAY DIFFRACTION3chain 'A' and (resid 26 through 41 )A26 - 41
4X-RAY DIFFRACTION4chain 'A' and (resid 42 through 87 )A42 - 87
5X-RAY DIFFRACTION5chain 'A' and (resid 88 through 112 )A88 - 112
6X-RAY DIFFRACTION6chain 'A' and (resid 113 through 125 )A113 - 125
7X-RAY DIFFRACTION7chain 'A' and (resid 126 through 147 )A126 - 147
8X-RAY DIFFRACTION8chain 'A' and (resid 148 through 157 )A148 - 157
9X-RAY DIFFRACTION9chain 'A' and (resid 158 through 169 )A158 - 169
10X-RAY DIFFRACTION10chain 'B' and (resid 2 through 14 )B2 - 14
11X-RAY DIFFRACTION11chain 'B' and (resid 15 through 25 )B15 - 25
12X-RAY DIFFRACTION12chain 'B' and (resid 26 through 41 )B26 - 41
13X-RAY DIFFRACTION13chain 'B' and (resid 42 through 61 )B42 - 61
14X-RAY DIFFRACTION14chain 'B' and (resid 62 through 77 )B62 - 77
15X-RAY DIFFRACTION15chain 'B' and (resid 78 through 87 )B78 - 87
16X-RAY DIFFRACTION16chain 'B' and (resid 88 through 97 )B88 - 97
17X-RAY DIFFRACTION17chain 'B' and (resid 98 through 125 )B98 - 125
18X-RAY DIFFRACTION18chain 'B' and (resid 126 through 157 )B126 - 157
19X-RAY DIFFRACTION19chain 'B' and (resid 158 through 169 )B158 - 169
20X-RAY DIFFRACTION20chain 'C' and (resid 2 through 14 )C2 - 14
21X-RAY DIFFRACTION21chain 'C' and (resid 15 through 25 )C15 - 25
22X-RAY DIFFRACTION22chain 'C' and (resid 26 through 41 )C26 - 41
23X-RAY DIFFRACTION23chain 'C' and (resid 42 through 61 )C42 - 61
24X-RAY DIFFRACTION24chain 'C' and (resid 62 through 77 )C62 - 77
25X-RAY DIFFRACTION25chain 'C' and (resid 78 through 87 )C78 - 87
26X-RAY DIFFRACTION26chain 'C' and (resid 88 through 97 )C88 - 97
27X-RAY DIFFRACTION27chain 'C' and (resid 98 through 125 )C98 - 125
28X-RAY DIFFRACTION28chain 'C' and (resid 126 through 147 )C126 - 147
29X-RAY DIFFRACTION29chain 'C' and (resid 148 through 157 )C148 - 157
30X-RAY DIFFRACTION30chain 'C' and (resid 158 through 170 )C158 - 170
31X-RAY DIFFRACTION31chain 'D' and (resid 1 through 14 )D1 - 14
32X-RAY DIFFRACTION32chain 'D' and (resid 15 through 25 )D15 - 25
33X-RAY DIFFRACTION33chain 'D' and (resid 26 through 41 )D26 - 41
34X-RAY DIFFRACTION34chain 'D' and (resid 42 through 87 )D42 - 87
35X-RAY DIFFRACTION35chain 'D' and (resid 88 through 112 )D88 - 112
36X-RAY DIFFRACTION36chain 'D' and (resid 113 through 125 )D113 - 125
37X-RAY DIFFRACTION37chain 'D' and (resid 126 through 157 )D126 - 157
38X-RAY DIFFRACTION38chain 'D' and (resid 158 through 169 )D158 - 169

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