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- PDB-2vz8: Crystal Structure of Mammalian Fatty Acid Synthase -

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Basic information

Entry
Database: PDB / ID: 2vz8
TitleCrystal Structure of Mammalian Fatty Acid Synthase
ComponentsFATTY ACID SYNTHASE
KeywordsTRANSFERASE / PHOSPHOPANTETHEINE / FATTY ACID SYNTHASE / MULTIENZYME / MEGASYNTHASE / FATTY ACID SYNTHESIS
Function / homology
Function and homology information


fatty acyl-[ACP] hydrolase activity / fatty-acid synthase system / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / : / (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity / [acyl-carrier-protein] S-acetyltransferase / [acyl-carrier-protein] S-acetyltransferase activity / oleoyl-[acyl-carrier-protein] hydrolase / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity ...fatty acyl-[ACP] hydrolase activity / fatty-acid synthase system / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / : / (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity / [acyl-carrier-protein] S-acetyltransferase / [acyl-carrier-protein] S-acetyltransferase activity / oleoyl-[acyl-carrier-protein] hydrolase / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / 3-hydroxyacyl-[acyl-carrier-protein] dehydratase / (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity / fatty acid synthase activity / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / phosphopantetheine binding / small molecule binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / nucleotide binding
Similarity search - Function
Alpha-Beta Plaits - #3290 / Polyketide synthase dehydratase / : / Fatty acid synthase, pseudo-KR domain / Malonyl-Coenzyme A Acyl Carrier Protein, domain 2 / Malonyl-Coenzyme A Acyl Carrier Protein; domain 2 / Zinc-binding dehydrogenase / Methyltransferase type 12 / Methyltransferase domain / : ...Alpha-Beta Plaits - #3290 / Polyketide synthase dehydratase / : / Fatty acid synthase, pseudo-KR domain / Malonyl-Coenzyme A Acyl Carrier Protein, domain 2 / Malonyl-Coenzyme A Acyl Carrier Protein; domain 2 / Zinc-binding dehydrogenase / Methyltransferase type 12 / Methyltransferase domain / : / Polyketide synthase dehydratase domain / Thioesterase / Thioesterase domain / Polyketide synthase dehydratase N-terminal domain / PKS_DH / Polyketide synthase, dehydratase domain / Polyketide synthase, dehydratase domain superfamily / Polyketide synthase, ketoreductase domain / KR domain / Thiol Ester Dehydrase; Chain A / Polyketide synthase, C-terminal extension / Ketoacyl-synthetase C-terminal extension / Malonyl-CoA ACP transacylase, ACP-binding / Quinone Oxidoreductase; Chain A, domain 1 / Medium-chain alcohol dehydrogenases, catalytic domain / PKS_KR / Acyl transferase domain superfamily / Acyl transferase / Acyl transferase domain / Acyl transferase domain in polyketide synthase (PKS) enzymes. / Acyl transferase/acyl hydrolase/lysophospholipase / Zinc-binding dehydrogenase / Thiolase/Chalcone synthase / Peroxisomal Thiolase; Chain A, domain 1 / Polyketide synthase, enoylreductase domain / Enoylreductase / Ketosynthase family 3 (KS3) domain profile. / Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / Beta-ketoacyl synthase / Beta-ketoacyl synthase, active site / Ketosynthase family 3 (KS3) active site signature. / Polyketide synthase, beta-ketoacyl synthase domain / Beta-ketoacyl synthase, N-terminal / Beta-ketoacyl synthase, C-terminal / Beta-ketoacyl synthase, N-terminal domain / Beta-ketoacyl synthase, C-terminal domain / GroES-like superfamily / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Thiolase-like / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Alpha/Beta hydrolase fold / NAD(P)-binding Rossmann-like Domain / Alpha-Beta Plaits / NAD(P)-binding domain superfamily / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Roll / Alpha-Beta Complex / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesSUS SCROFA (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.219 Å
AuthorsMaier, T. / Leibundgut, M. / Ban, N.
Citation
Journal: Science / Year: 2008
Title: The Crystal Structure of a Mammalian Fatty Acid Synthase.
Authors: Maier, T. / Leibundgut, M. / Ban, N.
#1: Journal: Science / Year: 2006
Title: Architecture of Mammalian Fatty Acid Synthase at 4. 5 A Resolution.
Authors: Maier, T. / Jenni, S. / Ban, N.
History
DepositionJul 31, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 9, 2008Provider: repository / Type: Initial release
Revision 1.1May 7, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: FATTY ACID SYNTHASE
B: FATTY ACID SYNTHASE


Theoretical massNumber of molelcules
Total (without water)545,0642
Polymers545,0642
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10830 Å2
ΔGint-53 kcal/mol
Surface area152180 Å2
MethodPISA
Unit cell
Length a, b, c (Å)96.320, 244.700, 135.250
Angle α, β, γ (deg.)90.00, 101.65, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25
16
26
17
27
18
28
19
29
110
210
111
211
112
212
113
213
114
214
115
215
116
216
117
217
118
218
119
219
120
220
121
221
122
222
123
223
124
224
125
225
126
226

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 1:116 OR RESSEQ 118:120 OR RESSEQ...
211CHAIN B AND (RESSEQ 1:116 OR RESSEQ 118:120 OR RESSEQ...
112CHAIN A AND (RESSEQ 474:479 OR RESSEQ 485:489))
212CHAIN B AND (RESSEQ 474:479 OR RESSEQ 485:489))
113CHAIN A AND (RESSEQ 490:499 OR RESSEQ 500:503 OR RESSEQ...
213CHAIN B AND (RESSEQ 490:499 OR RESSEQ 500:503 OR RESSEQ...
114CHAIN A AND RESSEQ 626:633)
214CHAIN B AND RESSEQ 626:633)
115CHAIN A AND RESSEQ 637:642)
215CHAIN B AND RESSEQ 637:642)
116CHAIN A AND RESSEQ 648:652)
216CHAIN B AND RESSEQ 648:652)
117CHAIN A AND RESSEQ 683:702)
217CHAIN B AND RESSEQ 683:702)
118CHAIN A AND (RESSEQ 706:722 OR RESSEQ 724:732 OR RESSEQ 734:750 OR RESSEQ 752:755))
218CHAIN B AND (RESSEQ 706:722 OR RESSEQ 724:732 OR RESSEQ 734:750 OR RESSEQ 752:755))
119CHAIN A AND RESSEQ 756:817)
219CHAIN B AND RESSEQ 756:817)
1110CHAIN A AND RESSEQ 822:843)
2110CHAIN B AND RESSEQ 822:843)
1111CHAIN A AND RESSEQ 859:970)
2111CHAIN B AND RESSEQ 859:970)
1112CHAIN A AND (RESSEQ 985:1052 OR RESSEQ 1054:1105))
2112CHAIN B AND (RESSEQ 985:1052 OR RESSEQ 1054:1105))
1113CHAIN A AND RESSEQ 1105:1111)
2113CHAIN B AND RESSEQ 1105:1111)
1114CHAIN A AND RESSEQ 1113:1135)
2114CHAIN B AND RESSEQ 1113:1135)
1115CHAIN A AND (RESSEQ 1216:1275 OR RESSEQ 1277:1281 OR RESSEQ 1283:1289 OR RESSEQ 1294:1300))
2115CHAIN B AND (RESSEQ 1216:1275 OR RESSEQ 1277:1281 OR RESSEQ 1283:1289 OR RESSEQ 1294:1300))
1116CHAIN A AND RESSEQ 1312:1320)
2116CHAIN B AND RESSEQ 1312:1320)
1117CHAIN A AND RESSEQ 1327:1349)
2117CHAIN B AND RESSEQ 1327:1349)
1118CHAIN A AND RESSEQ 1376:1385)
2118CHAIN B AND RESSEQ 1376:1385)
1119CHAIN A AND RESSEQ 1387:1406)
2119CHAIN B AND RESSEQ 1387:1406)
1120CHAIN A AND RESSEQ 1414:1433)
2120CHAIN B AND RESSEQ 1414:1433)
1121CHAIN A AND RESSEQ 1438:1470)
2121CHAIN B AND RESSEQ 1438:1470)
1122CHAIN A AND RESSEQ 1471:1482)
2122CHAIN B AND RESSEQ 1471:1482)
1123CHAIN A AND RESSEQ 1492:1512)
2123CHAIN B AND RESSEQ 1492:1512)
1124CHAIN A AND RESSEQ 1513:1526)
2124CHAIN B AND RESSEQ 1513:1526)
1125CHAIN A AND (RESSEQ 1563:1594 OR RESSEQ 1696:1798 OR RESSEQ...
2125CHAIN B AND (RESSEQ 1563:1594 OR RESSEQ 1696:1798 OR RESSEQ...
1126CHAIN A AND (RESSEQ 1872:1974 OR RESSEQ 1991:2071 OR RESSEQ 2076:2110))
2126CHAIN B AND (RESSEQ 1872:1974 OR RESSEQ 1991:2071 OR RESSEQ 2076:2110))

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26

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Components

#1: Protein FATTY ACID SYNTHASE /


Mass: 272532.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: LACTATING MAMMARY GLAND / Source: (natural) SUS SCROFA (pig) / Organ: MAMMARY GLAND / References: UniProt: A5YV76, fatty-acid synthase system
Sequence detailsSEQUENCE CONTAINS A SINGLE X BASED ON TRANSLATION FROM NUCLEIC ACID SEQUENCE CONTAINING A K. THIS ...SEQUENCE CONTAINS A SINGLE X BASED ON TRANSLATION FROM NUCLEIC ACID SEQUENCE CONTAINING A K. THIS POSITION WAS ASSIGNED BASED ON FURTHER EST SEQUENCES.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 16

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Sample preparation

CrystalDensity Matthews: 3.2 Å3/Da / Density % sol: 57.03 % / Description: NONE
Crystal growpH: 7 / Details: pH 7.0

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Data collection

DiffractionMean temperature: 10 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD / Date: Dec 8, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→30 Å / Num. obs: 96975 / % possible obs: 98.5 % / Redundancy: 7 % / Biso Wilson estimate: 94.87 Å2 / Rmerge(I) obs: 0.17 / Net I/σ(I): 9.9
Reflection shellResolution: 3.2→3.4 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.99 / Mean I/σ(I) obs: 1.4 / % possible all: 93.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2CF2
Resolution: 3.219→29.496 Å / SU ML: 0.48 / σ(F): 0.84 / Phase error: 28.62 / Stereochemistry target values: ML
Details: UNBIASED ELECTRON DENSITY MAPS FOR THE LINKERS (RESIDUES 852-857) IN THE REGION OF THE CENTRAL CONNECTION ARE NOT CONTIGUOUS FOR ONE OR TWO AMINO ACIDS SUCH THAT THE POSSIBILITY OF ...Details: UNBIASED ELECTRON DENSITY MAPS FOR THE LINKERS (RESIDUES 852-857) IN THE REGION OF THE CENTRAL CONNECTION ARE NOT CONTIGUOUS FOR ONE OR TWO AMINO ACIDS SUCH THAT THE POSSIBILITY OF ALTERNATIVE CONNECTIVITY OR MULTIPLE CONFORMATIONS FOR THIS REGION CAN NOT BE EXCLUDED.
RfactorNum. reflection% reflection
Rfree0.2588 9286 5 %
Rwork0.2175 --
obs0.2196 185581 94.79 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 71.89 Å2 / ksol: 0.288 e/Å3
Displacement parametersBiso mean: 143.83 Å2
Baniso -1Baniso -2Baniso -3
1--10.6551 Å20 Å20.4366 Å2
2---7.3604 Å20 Å2
3---18.0155 Å2
Refinement stepCycle: LAST / Resolution: 3.219→29.496 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms30281 0 0 0 30281
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00930938
X-RAY DIFFRACTIONf_angle_d1.23142039
X-RAY DIFFRACTIONf_dihedral_angle_d18.78911220
X-RAY DIFFRACTIONf_chiral_restr0.0754761
X-RAY DIFFRACTIONf_plane_restr0.0065483
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3329X-RAY DIFFRACTIONPOSITIONAL
12B3329X-RAY DIFFRACTIONPOSITIONAL0.035
21A65X-RAY DIFFRACTIONPOSITIONAL
22B65X-RAY DIFFRACTIONPOSITIONAL0.036
31A785X-RAY DIFFRACTIONPOSITIONAL
32B785X-RAY DIFFRACTIONPOSITIONAL0.037
41A73X-RAY DIFFRACTIONPOSITIONAL
42B73X-RAY DIFFRACTIONPOSITIONAL0.048
51A37X-RAY DIFFRACTIONPOSITIONAL
52B37X-RAY DIFFRACTIONPOSITIONAL0.046
61A35X-RAY DIFFRACTIONPOSITIONAL
62B35X-RAY DIFFRACTIONPOSITIONAL0.031
71A168X-RAY DIFFRACTIONPOSITIONAL
72B168X-RAY DIFFRACTIONPOSITIONAL0.034
81A373X-RAY DIFFRACTIONPOSITIONAL
82B373X-RAY DIFFRACTIONPOSITIONAL0.034
91A476X-RAY DIFFRACTIONPOSITIONAL
92B476X-RAY DIFFRACTIONPOSITIONAL0.033
101A178X-RAY DIFFRACTIONPOSITIONAL
102B178X-RAY DIFFRACTIONPOSITIONAL0.03
111A884X-RAY DIFFRACTIONPOSITIONAL
112B884X-RAY DIFFRACTIONPOSITIONAL0.035
121A949X-RAY DIFFRACTIONPOSITIONAL
122B949X-RAY DIFFRACTIONPOSITIONAL0.039
131A64X-RAY DIFFRACTIONPOSITIONAL
132B64X-RAY DIFFRACTIONPOSITIONAL0.028
141A171X-RAY DIFFRACTIONPOSITIONAL
142B171X-RAY DIFFRACTIONPOSITIONAL0.087
151A589X-RAY DIFFRACTIONPOSITIONAL
152B589X-RAY DIFFRACTIONPOSITIONAL0.142
161A61X-RAY DIFFRACTIONPOSITIONAL
162B61X-RAY DIFFRACTIONPOSITIONAL0.131
171A68X-RAY DIFFRACTIONPOSITIONAL
172B68X-RAY DIFFRACTIONPOSITIONAL0.141
181A79X-RAY DIFFRACTIONPOSITIONAL
182B79X-RAY DIFFRACTIONPOSITIONAL0.192
191A165X-RAY DIFFRACTIONPOSITIONAL
192B165X-RAY DIFFRACTIONPOSITIONAL0.147
201A167X-RAY DIFFRACTIONPOSITIONAL
202B167X-RAY DIFFRACTIONPOSITIONAL0.139
211A245X-RAY DIFFRACTIONPOSITIONAL
212B245X-RAY DIFFRACTIONPOSITIONAL0.146
221A82X-RAY DIFFRACTIONPOSITIONAL
222B82X-RAY DIFFRACTIONPOSITIONAL0.193
231A167X-RAY DIFFRACTIONPOSITIONAL
232B167X-RAY DIFFRACTIONPOSITIONAL0.151
241A125X-RAY DIFFRACTIONPOSITIONAL
242B125X-RAY DIFFRACTIONPOSITIONAL0.165
251A1446X-RAY DIFFRACTIONPOSITIONAL
252B1446X-RAY DIFFRACTIONPOSITIONAL0.042
261A1649X-RAY DIFFRACTIONPOSITIONAL
262B1649X-RAY DIFFRACTIONPOSITIONAL0.038
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2188-3.25530.4271880.40133249X-RAY DIFFRACTION53
3.2553-3.29360.40751930.37864339X-RAY DIFFRACTION69
3.2936-3.33370.38283020.37625911X-RAY DIFFRACTION94
3.3337-3.37580.39063230.35025942X-RAY DIFFRACTION97
3.3758-3.42020.35822890.35656099X-RAY DIFFRACTION98
3.4202-3.4670.37343360.33586068X-RAY DIFFRACTION97
3.467-3.51640.3763020.31095978X-RAY DIFFRACTION98
3.5164-3.56880.29243150.29826230X-RAY DIFFRACTION98
3.5688-3.62450.34653300.3126044X-RAY DIFFRACTION98
3.6245-3.68380.35993140.30925979X-RAY DIFFRACTION97
3.6838-3.74720.31653360.28635987X-RAY DIFFRACTION97
3.7472-3.81520.32732910.26286125X-RAY DIFFRACTION98
3.8152-3.88840.29573150.25726070X-RAY DIFFRACTION98
3.8884-3.96760.27193080.24425965X-RAY DIFFRACTION96
3.9676-4.05370.25653420.22946045X-RAY DIFFRACTION98
4.0537-4.14770.26883060.22576091X-RAY DIFFRACTION98
4.1477-4.25110.24613370.20796030X-RAY DIFFRACTION98
4.2511-4.36570.25833400.20536081X-RAY DIFFRACTION98
4.3657-4.49380.24113410.18545984X-RAY DIFFRACTION97
4.4938-4.63830.2183270.17966020X-RAY DIFFRACTION97
4.6383-4.80340.2283420.17896007X-RAY DIFFRACTION97
4.8034-4.99480.22612990.17076037X-RAY DIFFRACTION97
4.9948-5.2210.24013540.18375946X-RAY DIFFRACTION97
5.221-5.49450.25533070.17956056X-RAY DIFFRACTION97
5.4945-5.83630.20892970.17966035X-RAY DIFFRACTION97
5.8363-6.28290.23723000.17556009X-RAY DIFFRACTION97
6.2829-6.90780.21983360.16866025X-RAY DIFFRACTION97
6.9078-7.89060.20143120.14596015X-RAY DIFFRACTION97
7.8906-9.8790.15423340.12495946X-RAY DIFFRACTION97
9.879-29.49760.20272700.16855982X-RAY DIFFRACTION96
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)
13.6050.40220.76332.0715-0.04052.6706-0.3173-0.06260.85360.0622-0.14350.1038-0.1507-0.28750.00050.82240.00450.09680.5831-0.0521.587634.941773.868350.658
20.252-0.1087-0.07360.18150.02550.0112-0.2753-0.3572-0.74580.3156-0.0320.39242.2991-1.38920.00291.2464-0.39790.26631.2248-0.30311.916917.748657.47758.3008
33.21381.3975-1.9511.91831.81442.4502-0.2183-0.90390.57410.74910.13490.42470.4222-0.91460.00050.8929-0.06350.21040.8066-0.14541.676826.197262.829658.7297
41.8075-1.06091.88551.92491.02111.078-0.397-1.0411-0.0218-0.1617-0.0535-0.7757-0.4102-0.058-0.00050.8310.1840.08060.85180.08981.758258.203562.104168.6618
52.1022-2.2903-0.71132.2238-2.24572.2086-0.40080.260.6173-0.28720.4664-0.0375-0.2449-0.3528-00.6558-0.1256-0.05380.63050.04720.726379.477840.205966.6238
61.4428-0.11350.35281.2729-0.61222.64440.0284-0.94770.92330.06410.0980.0465-0.2498-0.2502-0.0010.754-0.0948-0.06921.0076-0.35611.6575101.139451.197379.2453
72.4365-1.98490.71333.3095-0.29130.51520.0229-0.15110.9927-0.14370.0264-0.3571-0.115-0.013-0.00020.7648-0.02650.13120.74830.06191.151678.397953.789963.9912
84.0407-0.33962.70744.12630.05294.1520.17620.1374-1.3385-0.175-0.01470.02560.3663-0.0629-0.00060.8510.12330.05110.6549-0.17351.470752.5849117.75950.4163
92.75150.15312.47235.83740.89712.54510.45330.3978-1.01610.1630.1119-0.66590.18040.5152-0.00080.89610.060.13750.8295-0.12120.88866.7238125.124952.5095
100.78680.5564-0.48740.17880.21320.2035-1.0277-0.26360.16140.4692-0.6417-0.30530.40650.31410.00062.40860.0995-0.221.50870.3411.832673.0328115.016496.2184
110.5440.3389-1.37542.42150.06061.163-0.1541-0.493-0.78140.3763-0.344-0.47460.95370.40610.00023.02090.1285-0.2822.00680.71871.997177.135196.6776104.2604
120.66290.8083-0.47830.0623-0.33031.1986-0.19490.0568-1.1961.3680.5315-2.34160.86390.0623-0.00062.55230.6026-0.78652.30830.20972.712399.4821108.326896.3904
135.7704-0.4273.43620.028-0.16363.4306-0.0401-1.2069-0.35540.3157-0.1843-0.0650.3966-0.201-01.0764-0.0980.13051.2394-0.10780.418445.0256144.413580.3704
143.46570.47780.63052.1483-0.05784.9110.0417-0.5526-1.14310.54220.0022-0.52610.53830.7938-0.00021.15310.0289-0.20771.10980.15830.953282.9134133.979182.1113
150.93220.6314-0.83770.6082-1.24080.44640.11570.7222-1.62130.69560.5039-0.60661.41661.7732-0.0021.89750.149-0.25341.51060.33321.570678.8655120.087184.6607
163.1893-0.33780.22741.49180.66511.997-0.11291.18331.1209-0.5807-0.395-0.0186-0.350.34970.00031.28280.12230.01141.11160.67841.877239.094480.993826.0112
170.06710.0276-0.20950.05540.2358-0.1843-0.30990.78690.0342-0.7998-0.31770.02430.96661.14130.00211.5560.04390.05472.86491.30622.266356.422171.295810.9304
181.4369-0.6635-1.46061.4572-0.79480.6770.01541.28590.8241-1.0228-0.29050.1987-0.09141.28210.0011.48410.20180.24361.93260.58911.935947.949975.987413.3508
190.23550.33110.49410.06170.36390.1629-0.78551.5346-0.14840.2436-0.44440.0794-0.3273-0.6061-0.00021.95020.2488-0.08911.86110.2922.131515.910980.38454.307
200.9292-0.09480.46940.6274-0.66860.82220.251.0082-0.017-0.563-0.56710.4224-0.1043-0.2448-0.00062.00390.2832-0.30292.2893-0.26341.5361-4.190259.3617-4.5893
21-0.3527-0.3341-0.0928-0.22920.5019-0.3090.25850.7879-0.3371-1.2177-0.05070.8318-1.3770.2296-0.00163.21140.3588-0.37892.7566-0.08012.0259-29.149572.2681-9.3985
220.8734-0.33180.77810.3310.3482.4742-0.09090.53150.2351-0.4153-0.16230.08170.2829-0.4869-0.00031.73750.2222-0.09942.09680.07531.7549-3.809669.71844.4762
235.9404-2.15371.45145.1850.35793.73430.19830.0705-1.7797-0.22-0.25030.68240.49660.0171-0.00010.6952-0.172-0.14960.7502-0.2621.583819.6446121.954548.7298
243.579-1.35052.27214.09940.34063.23220.21240.0364-1.0434-0.1101-0.1290.7359-0.1235-0.47180.00050.8413-0.1168-0.04110.9822-0.0520.927.3123132.041151.5879
250.99620.7678-0.31790.2662-0.06930.1101-0.92990.31040.2046-0.25150.7181-0.69370.315-1.1170.00081.9187-0.3459-0.2822.024-0.35141.22744.3902150.85365.1874
262.3981.4213-0.651.025-0.60881.3524-0.61151.0989-0.8887-0.90810.2960.07370.2718-0.7733-0.00122.4893-0.6914-0.25733.0342-0.49021.1156-7.1162139.0661-7.5187
270.87540.3683-0.82050.4337-0.36130.6684-0.36571.4086-0.1098-1.85910.0191.9594-0.1069-0.88620.00182.2368-0.5134-0.69913.11450.17791.544-25.7282149.5348.0593
285.4036-0.71862.4332-0.2935-0.80792.158-0.24741.20170.6146-0.5629-0.1610.25460.0481-0.39870.00071.1170.0725-0.07091.21150.04880.738134.0498158.350837.8483
292.6154-0.7726-0.9632.4466-1.29785.3109-0.0141.1680.0303-0.72140.16170.56930.2174-0.7142-0.00140.8617-0.0537-0.27561.2717-0.07520.6168-6.5837157.089931.7675
302.4619-1.459-0.6093.83531.07561.7482-0.72120.8157-1.3642-0.61991.57862.33690.8154-0.31360.10761.386-0.2454-0.28182.0411-0.3120.652-3.2418147.836722.3872
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 1:315)
2X-RAY DIFFRACTION2CHAIN A AND RESID 316:325)
3X-RAY DIFFRACTION3CHAIN A AND RESID 326:419)
4X-RAY DIFFRACTION4CHAIN A AND RESID 420:488)
5X-RAY DIFFRACTION5CHAIN A AND RESID 489:611)
6X-RAY DIFFRACTION6CHAIN A AND RESID 612:672)
7X-RAY DIFFRACTION7CHAIN A AND RESID 673:851)
8X-RAY DIFFRACTION8CHAIN A AND RESID 858:981)
9X-RAY DIFFRACTION9CHAIN A AND RESID 982:1105)
10X-RAY DIFFRACTION10CHAIN A AND RESID 1106:1192)
11X-RAY DIFFRACTION11CHAIN A AND RESID 1193:1418)
12X-RAY DIFFRACTION12CHAIN A AND RESID 1419:1505)
13X-RAY DIFFRACTION13CHAIN A AND RESID 1506:1856)
14X-RAY DIFFRACTION14CHAIN A AND RESID 1857:2043)
15X-RAY DIFFRACTION15CHAIN A AND RESID 2044:2113)
16X-RAY DIFFRACTION16CHAIN B AND RESID 1:315)
17X-RAY DIFFRACTION17CHAIN B AND RESID 316:325)
18X-RAY DIFFRACTION18CHAIN B AND RESID 326:419)
19X-RAY DIFFRACTION19CHAIN B AND RESID 420:488)
20X-RAY DIFFRACTION20CHAIN B AND RESID 489:611)
21X-RAY DIFFRACTION21CHAIN B AND RESID 612:672)
22X-RAY DIFFRACTION22CHAIN B AND RESID 673:851)
23X-RAY DIFFRACTION23CHAIN B AND RESID 858:981)
24X-RAY DIFFRACTION24CHAIN B AND RESID 982:1105)
25X-RAY DIFFRACTION25CHAIN B AND RESID 1106:1192)
26X-RAY DIFFRACTION26CHAIN B AND RESID 1193:1418)
27X-RAY DIFFRACTION27CHAIN B AND RESID 1419:1505)
28X-RAY DIFFRACTION28CHAIN B AND RESID 1506:1856)
29X-RAY DIFFRACTION29CHAIN B AND RESID 1857:2043)
30X-RAY DIFFRACTION30CHAIN B AND RESID 2044:2113)

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