[日本語] English
万見
- PDB-6par: Structure of a bacterial Atm1-family ABC exporter with MgAMPPNP bound -

+
データを開く


IDまたはキーワード:

読み込み中...

-
基本情報

登録情報
データベース: PDB / ID: 6par
タイトルStructure of a bacterial Atm1-family ABC exporter with MgAMPPNP bound
要素ATM1-type heavy metal exporter
キーワードTRANSPORT PROTEIN (運搬体タンパク質) / ABC transporter / ABC exporter / ATPase (ATPアーゼ) / membrane protein (膜タンパク質)
機能・相同性
機能・相同性情報


トランスロカーゼ / response to mercury ion / ABC-type transporter activity / monoatomic ion transport / ATP hydrolysis activity / ATP binding / 細胞膜
類似検索 - 分子機能
Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. ...Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
類似検索 - ドメイン・相同性
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / ATM1-type heavy metal exporter
類似検索 - 構成要素
生物種Novosphingobium aromaticivorans (バクテリア)
手法X線回折 / シンクロトロン / 分子置換 / 解像度: 3.35 Å
データ登録者Fan, C. / Kaiser, J.T. / Rees, D.C.
資金援助 米国, 1件
組織認可番号国
Howard Hughes Medical Institute (HHMI) 米国
引用ジャーナル: Proc Natl Acad Sci U S A / 年: 2020
タイトル: A structural framework for unidirectional transport by a bacterial ABC exporter.
著者: Chengcheng Fan / Jens T Kaiser / Douglas C Rees /
要旨: The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) mediates iron homeostasis in eukaryotes, while the prokaryotic homolog from (Atm1) can export glutathione derivatives and confer ...The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) mediates iron homeostasis in eukaryotes, while the prokaryotic homolog from (Atm1) can export glutathione derivatives and confer protection against heavy-metal toxicity. To establish the structural framework underlying the Atm1 transport mechanism, we determined eight structures by X-ray crystallography and single-particle cryo-electron microscopy in distinct conformational states, stabilized by individual disulfide crosslinks and nucleotides. As Atm1 progresses through the transport cycle, conformational changes in transmembrane helix 6 (TM6) alter the glutathione-binding site and the associated substrate-binding cavity. Significantly, kinking of TM6 in the post-ATP hydrolysis state stabilized by MgADPVO eliminates this cavity, precluding uptake of glutathione derivatives. The presence of this cavity during the transition from the inward-facing to outward-facing conformational states, and its absence in the reverse direction, thereby provide an elegant and conceptually simple mechanism for enforcing the export directionality of transport by Atm1. One of the disulfide crosslinked Atm1 variants characterized in this work retains significant glutathione transport activity, suggesting that ATP hydrolysis and substrate transport by Atm1 may involve a limited set of conformational states with minimal separation of the nucleotide-binding domains in the inward-facing conformation.
履歴
登録2019年6月11日登録サイト: RCSB / 処理サイト: RCSB
改定 1.02020年6月24日Provider: repository / タイプ: Initial release
改定 1.12020年8月19日Group: Database references / Derived calculations / カテゴリ: citation / struct_conn
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_label_asym_id
改定 1.22020年8月26日Group: Database references / カテゴリ: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
改定 1.32023年10月11日Group: Data collection / Database references / Refinement description
カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
構造の表示

構造ビューア分子:
MolmilJmol/JSmol

ダウンロードとリンク

-
集合体

登録構造単位
A: ATM1-type heavy metal exporter
B: ATM1-type heavy metal exporter
C: ATM1-type heavy metal exporter
D: ATM1-type heavy metal exporter
E: ATM1-type heavy metal exporter
F: ATM1-type heavy metal exporter
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)409,81318
ポリマ－406,6306
非ポリマー3,18312
水0
1
A: ATM1-type heavy metal exporter
B: ATM1-type heavy metal exporter
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)136,6046
ポリマ－135,5432
非ポリマー1,0614
水0
タイプ名称対称操作数
identity operation1_555x,y,z1
Buried area16760 Å2
ΔGint-96 kcal/mol
Surface area47440 Å2
手法PISA
2
C: ATM1-type heavy metal exporter
D: ATM1-type heavy metal exporter
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)136,6046
ポリマ－135,5432
非ポリマー1,0614
水0
タイプ名称対称操作数
identity operation1_555x,y,z1
Buried area16600 Å2
ΔGint-100 kcal/mol
Surface area48370 Å2
手法PISA
3
E: ATM1-type heavy metal exporter
F: ATM1-type heavy metal exporter
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)136,6046
ポリマ－135,5432
非ポリマー1,0614
水0
タイプ名称対称操作数
identity operation1_555x,y,z1
Buried area16960 Å2
ΔGint-98 kcal/mol
Surface area47760 Å2
手法PISA
単位格子
Length a, b, c (Å)169.648, 92.498, 237.691
Angle α, β, γ (deg.)90.000, 110.340, 90.000
Int Tables number4
Space group name H-MP1211
非結晶学的対称性 (NCS)NCSドメイン:
IDEns-ID詳細
11(chain A and (resid 38 through 53 or resid 55...
21(chain B and (resid 38 through 53 or resid 55...
31(chain C and (resid 38 through 53 or resid 55...
41(chain D and (resid 38 through 53 or resid 55...
51(chain E and (resid 38 through 53 or resid 55...
61(chain F and (resid 38 through 53 or resid 55...

NCSドメイン領域:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 38 through 53 or resid 55...A38 - 53
121(chain A and (resid 38 through 53 or resid 55...A55 - 56
131(chain A and (resid 38 through 53 or resid 55...A62 - 68
141(chain A and (resid 38 through 53 or resid 55...A75 - 106
151(chain A and (resid 38 through 53 or resid 55...A22 - 702
161(chain A and (resid 38 through 53 or resid 55...A22 - 702
171(chain A and (resid 38 through 53 or resid 55...A124 - 144
181(chain A and (resid 38 through 53 or resid 55...A22 - 702
191(chain A and (resid 38 through 53 or resid 55...A22 - 702
1101(chain A and (resid 38 through 53 or resid 55...A323 - 333
1111(chain A and (resid 38 through 53 or resid 55...A335 - 336
1121(chain A and (resid 38 through 53 or resid 55...A3
1131(chain A and (resid 38 through 53 or resid 55...A473 - 495
1141(chain A and (resid 38 through 53 or resid 55...A497 - 540
1151(chain A and (resid 38 through 53 or resid 55...A497 - 540
1161(chain A and (resid 38 through 53 or resid 55...A542 - 569
1171(chain A and (resid 38 through 53 or resid 55...A571
1181(chain A and (resid 38 through 53 or resid 55...A573 - 598
1191(chain A and (resid 38 through 53 or resid 55...A701 - 702
211(chain B and (resid 38 through 53 or resid 55...B38 - 53
221(chain B and (resid 38 through 53 or resid 55...B55 - 56
231(chain B and (resid 38 through 53 or resid 55...B62 - 68
241(chain B and (resid 38 through 53 or resid 55...B17 - 702
251(chain B and (resid 38 through 53 or resid 55...B17 - 702
261(chain B and (resid 38 through 53 or resid 55...B17 - 702
271(chain B and (resid 38 through 53 or resid 55...B124 - 144
281(chain B and (resid 38 through 53 or resid 55...B17 - 702
291(chain B and (resid 38 through 53 or resid 55...B17 - 702
2101(chain B and (resid 38 through 53 or resid 55...B323 - 333
2111(chain B and (resid 38 through 53 or resid 55...B335 - 336
2121(chain B and (resid 38 through 53 or resid 55...B3
2131(chain B and (resid 38 through 53 or resid 55...B473 - 495
2141(chain B and (resid 38 through 53 or resid 55...B497 - 540
2151(chain B and (resid 38 through 53 or resid 55...B497 - 540
2161(chain B and (resid 38 through 53 or resid 55...B542 - 569
2171(chain B and (resid 38 through 53 or resid 55...B571
2181(chain B and (resid 38 through 53 or resid 55...B573 - 598
2191(chain B and (resid 38 through 53 or resid 55...B701 - 702
311(chain C and (resid 38 through 53 or resid 55...C38 - 53
321(chain C and (resid 38 through 53 or resid 55...C55 - 56
331(chain C and (resid 38 through 53 or resid 55...C62 - 68
341(chain C and (resid 38 through 53 or resid 55...C26 - 702
351(chain C and (resid 38 through 53 or resid 55...C26 - 702
361(chain C and (resid 38 through 53 or resid 55...C26 - 702
371(chain C and (resid 38 through 53 or resid 55...C124 - 144
381(chain C and (resid 38 through 53 or resid 55...C26 - 702
391(chain C and (resid 38 through 53 or resid 55...C26 - 702
3101(chain C and (resid 38 through 53 or resid 55...C323 - 333
3111(chain C and (resid 38 through 53 or resid 55...C335 - 336
3121(chain C and (resid 38 through 53 or resid 55...C3
3131(chain C and (resid 38 through 53 or resid 55...C473 - 495
3141(chain C and (resid 38 through 53 or resid 55...C497 - 540
3151(chain C and (resid 38 through 53 or resid 55...C497 - 540
3161(chain C and (resid 38 through 53 or resid 55...C542 - 569
3171(chain C and (resid 38 through 53 or resid 55...C571
3181(chain C and (resid 38 through 53 or resid 55...C573 - 702
411(chain D and (resid 38 through 53 or resid 55...D38 - 53
421(chain D and (resid 38 through 53 or resid 55...D55 - 56
431(chain D and (resid 38 through 53 or resid 55...D62 - 68
441(chain D and (resid 38 through 53 or resid 55...D75 - 106
451(chain D and (resid 38 through 53 or resid 55...D108 - 122
461(chain D and (resid 38 through 53 or resid 55...D124 - 144
471(chain D and (resid 38 through 53 or resid 55...D146 - 204
481(chain D and (resid 38 through 53 or resid 55...D206 - 312
491(chain D and (resid 38 through 53 or resid 55...D314 - 3121
4101(chain D and (resid 38 through 53 or resid 55...D323 - 333
4111(chain D and (resid 38 through 53 or resid 55...D335333
4121(chain D and (resid 38 through 53 or resid 55...D335 - 336
4131(chain D and (resid 38 through 53 or resid 55...D338 - 339
4141(chain D and (resid 38 through 53 or resid 55...D343
4151(chain D and (resid 38 through 53 or resid 55...D345 - 471
4161(chain D and (resid 38 through 53 or resid 55...D473 - 495
4171(chain D and (resid 38 through 53 or resid 55...D571
4181(chain D and (resid 38 through 53 or resid 55...D571
4191(chain D and (resid 38 through 53 or resid 55...D573 - 598
4201(chain D and (resid 38 through 53 or resid 55...D701 - 702
511(chain E and (resid 38 through 53 or resid 55...E38 - 53
521(chain E and (resid 38 through 53 or resid 55...E55 - 56
531(chain E and (resid 38 through 53 or resid 55...E62 - 68
541(chain E and (resid 38 through 53 or resid 55...E124 - 144
551(chain E and (resid 38 through 53 or resid 55...E34 - 702
561(chain E and (resid 38 through 53 or resid 55...E146 - 204
571(chain E and (resid 38 through 53 or resid 55...E34 - 702
581(chain E and (resid 38 through 53 or resid 55...E314 - 316
591(chain E and (resid 38 through 53 or resid 55...E34 - 702
5101(chain E and (resid 38 through 53 or resid 55...E323 - 3
5111(chain E and (resid 38 through 53 or resid 55...E343 - 38
5121(chain E and (resid 38 through 53 or resid 55...E343
5131(chain E and (resid 38 through 53 or resid 55...E345 - 471
5141(chain E and (resid 38 through 53 or resid 55...E34 - 702
5151(chain E and (resid 38 through 53 or resid 55...E542 - 569
5161(chain E and (resid 38 through 53 or resid 55...E34 - 702
5171(chain E and (resid 38 through 53 or resid 55...E571
5181(chain E and (resid 38 through 53 or resid 55...E571
5191(chain E and (resid 38 through 53 or resid 55...E573 - 702
611(chain F and (resid 38 through 53 or resid 55...F38 - 53
621(chain F and (resid 38 through 53 or resid 55...F55 - 56
631(chain F and (resid 38 through 53 or resid 55...F62 - 68
641(chain F and (resid 38 through 53 or resid 55...F22 - 702
651(chain F and (resid 38 through 53 or resid 55...F22 - 702
661(chain F and (resid 38 through 53 or resid 55...F22 - 702
671(chain F and (resid 38 through 53 or resid 55...F124 - 144
681(chain F and (resid 38 through 53 or resid 55...F22 - 702
691(chain F and (resid 38 through 53 or resid 55...F22 - 702
6101(chain F and (resid 38 through 53 or resid 55...F323 - 333
6111(chain F and (resid 38 through 53 or resid 55...F335 - 336
6121(chain F and (resid 38 through 53 or resid 55...F3
6131(chain F and (resid 38 through 53 or resid 55...F473 - 495
6141(chain F and (resid 38 through 53 or resid 55...F497 - 540
6151(chain F and (resid 38 through 53 or resid 55...F497 - 540
6161(chain F and (resid 38 through 53 or resid 55...F542 - 569
6171(chain F and (resid 38 through 53 or resid 55...F571
6181(chain F and (resid 38 through 53 or resid 55...F573 - 598
6191(chain F and (resid 38 through 53 or resid 55...F701 - 702

-
要素

#1: タンパク質
ATM1-type heavy metal exporter / ATP-binding cassette transporter Atm1 / NaAtm1


分子量: 67771.602 Da / 分子数: 6 / 由来タイプ: 組換発現
由来: (組換発現) Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199) (バクテリア)
株: ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199
遺伝子: atm1, Saro_2631 / 発現宿主: Escherichia coli BL21(DE3) (大腸菌) / 参照: UniProt: Q2G506
#2: 化合物
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP


分子量: 506.196 Da / 分子数: 6 / 由来タイプ: 合成 / 式: C10H17N6O12P3
コメント: AMP-PNP, エネルギー貯蔵分子類似体*YM
#3: 化合物
ChemComp-MG / MAGNESIUM ION / マグネシウムジカチオン


分子量: 24.305 Da / 分子数: 6 / 由来タイプ: 合成 / 式: Mg
研究の焦点であるリガンドがあるかN

-
実験情報

-
実験

実験手法: X線回折 / 使用した結晶の数: 1

-
試料調製

結晶マシュー密度: 4.3 Å3/Da / 溶媒含有率: 71.4 % / 解説: plates
結晶化温度: 296 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 7.1 / 詳細: ADA, PEG1500, PEG1000

-
データ収集

回折
ID平均測定温度 (K)Crystal-IDSerial crystal experiment
11001N
21001N
放射光源
由来サイトビームラインID波長 (Å)
シンクロトロンSSRL BL12-210.97946
シンクロトロンSSRL BL12-220.9793
検出器
タイプID検出器日付
DECTRIS PILATUS 6M1PIXEL2018年3月27日
DECTRIS PILATUS 6M2PIXEL2018年5月19日
放射
IDモノクロメータープロトコル単色(M)・ラウエ(L)散乱光タイプWavelength-ID
1Liquid nitrogen-cooled double crystal, non fixed exit slit Si(111)SINGLE WAVELENGTHMx-ray1
2Liquid nitrogen-cooled double crystal, non fixed exit slit Si(111)SINGLE WAVELENGTHMx-ray2
放射波長
ID波長 (Å)相対比
10.979461
20.97931
反射

Entry-ID: 6PAR

解像度 (Å)Num. obs% possible obs (%)冗長度 (%)Biso Wilson estimate (Å2)CC1/2Rmerge(I) obsRpim(I) allRrim(I) allDiffraction-IDNet I/σ(I)
3.35-39.6199850797.85791.20.9990.1740.0710.18919.43
3.6-39.857909498.17.194.990.9940.2110.0860.22827.5
反射 シェル
解像度 (Å)冗長度 (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allDiffraction-ID% possible all
3.35-3.476.41.7680.9790410.530.7541.927191.11
3.6-3.676.91.9421.143760.4660.7872.1295.8

-
解析

ソフトウェア
名称バージョン分類
PHENIX1.15.2_3472精密化
REFMAC精密化
PHASER位相決定
AutoSol位相決定
PDB_EXTRACTデータ抽出
Aimlessデータスケーリング
XDSデータ削減
Blu-Iceデータ収集
精密化構造決定の手法: 分子置換
開始モデル: 6PAN

6pan


解像度: 3.35→39.619 Å / SU ML: 0.5 / 交差検証法: FREE R-VALUE / σ(F): 1.33 / 位相誤差: 30.01
Rfactor反射数%反射
Rfree0.2816 4897 5 %
Rwork0.2538 --
obs0.2551 97915 97.92 %
溶媒の処理減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å
原子変位パラメータBiso max: 356.72 Å2 / Biso mean: 120.0215 Å2 / Biso min: 13.79 Å2
精密化ステップサイクル: final / 解像度: 3.35→39.619 Å
タンパク質核酸リガンド溶媒全体
原子数26783 0 192 0 26975
Biso mean--101.67 --
残基数----3452
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-ID数Refine-IDRmsタイプ
11A14693X-RAY DIFFRACTION11.717TORSIONAL
12B14693X-RAY DIFFRACTION11.717TORSIONAL
13C14693X-RAY DIFFRACTION11.717TORSIONAL
14D14693X-RAY DIFFRACTION11.717TORSIONAL
15E14693X-RAY DIFFRACTION11.717TORSIONAL
16F14693X-RAY DIFFRACTION11.717TORSIONAL
LS精密化 シェル

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

解像度 (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.3501-3.38820.39741300.37572763289387
3.3882-3.4280.36381410.34612951309294
3.428-3.46980.33831540.33732896305093
3.4698-3.51370.3641380.32183118325698
3.5137-3.55990.33511370.28893174331199
3.5599-3.60860.29581640.2763045320999
3.6086-3.66010.26751720.26753122329499
3.6601-3.71470.31141770.27883153333099
3.7147-3.77270.34841740.27613062323699
3.7727-3.83450.33311470.26273143329099
3.8345-3.90060.28551360.2663123325999
3.9006-3.97150.3411740.254331363310100
3.9715-4.04780.29311750.25783137331299
4.0478-4.13030.29051850.2430923277100
4.1303-4.220.26551670.2383130329799
4.22-4.31810.28291710.2323104327599
4.3181-4.42590.25441500.223069321997
4.4259-4.54540.25651720.22222971314395
4.5454-4.6790.25481690.23223095326498
4.679-4.82980.26471790.221331783357100
4.8298-5.00210.25551850.225231053290100
5.0021-5.20190.24731500.229531703320100
5.2019-5.43810.25741770.227331753352100
5.4381-5.7240.30131790.24563120329999
5.724-6.08150.29891580.25483168332699
6.0815-6.54910.28091960.25133090328698
6.5491-7.20460.25121520.24843083323596
7.2046-8.23890.23911720.214531843356100
8.2389-10.34950.22211640.196232363400100
10.3495-39.62190.31161520.31993225337797

+
万見について

-
お知らせ

-
2022年2月9日: EMDBエントリの付随情報ファイルのフォーマットが新しくなりました

EMDBエントリの付随情報ファイルのフォーマットが新しくなりました

  • EMDBのヘッダファイルのバージョン3が、公式のフォーマットとなりました。
  • これまでは公式だったバージョン1.9は、アーカイブから削除されます。

関連情報:EMDBヘッダ

外部リンク:wwPDBはEMDBデータモデルのバージョン3へ移行します

-
2020年8月12日: 新型コロナ情報

新型コロナ情報

URL: https://pdbj.org/emnavi/covid19.php

新ページ: EM Navigatorに新型コロナウイルスの特設ページを開設しました。

関連情報:Covid-19情報 / 2020年3月5日: 新型コロナウイルスの構造データ

+
2020年3月5日: 新型コロナウイルスの構造データ

新型コロナウイルスの構造データ

関連情報:万見生物種 / 2020年8月12日: 新型コロナ情報

外部リンク:COVID-19特集ページ - PDBj / 今月の分子2020年2月：コロナウイルスプロテーアーゼ

+
2019年1月31日: EMDBのIDの桁数の変更

EMDBのIDの桁数の変更

  • EMDBエントリに付与されているアクセスコード(EMDB-ID)は4桁の数字(例、EMD-1234)でしたが、間もなく枯渇します。これまでの4桁のID番号は4桁のまま変更されませんが、4桁の数字を使い切った後に発行されるIDは5桁以上の数字(例、EMD-12345)になります。5桁のIDは2019年の春頃から発行される見通しです。
  • EM Navigator/万見では、接頭語「EMD-」は省略されています。

関連情報:Q: 「EMD」とは何ですか？ / 万見/EM NavigatorにおけるID/アクセスコードの表記

外部リンク:EMDB Accession Codes are Changing Soon! / PDBjへお問い合わせ

+
2017年7月12日: PDB大規模アップデート

PDB大規模アップデート

  • 新バージョンのPDBx/mmCIF辞書形式に基づくデータがリリースされました。
  • 今回の更新はバージョン番号が4から5になる大規模なもので、全エントリデータの書き換えが行われる「Remediation」というアップデートに該当します。
  • このバージョンアップで、電子顕微鏡の実験手法に関する多くの項目の書式が改定されました(例：em_softwareなど)。
  • EM NavigatorとYorodumiでも、この改定に基づいた表示内容になります。

外部リンク:wwPDB Remediation / OneDepデータ基準に準拠した、より強化された内容のモデル構造ファイルが、PDBアーカイブで公開されました。

-
万見 (Yorodumi)

幾万の構造データを、幾万の視点から

  • 万見(Yorodumi)は、EMDB/PDB/SASBDBなどの構造データを閲覧するためのページです。
  • EM Navigatorの詳細ページの後継、Omokage検索のフロントエンドも兼ねています。

関連情報:EMDB / PDB / SASBDB / 3つのデータバンクの比較 / 万見検索 / 2016年8月31日: 新しいEM Navigatorと万見 / 万見文献 / Jmol/JSmol / 機能・相同性情報 / 新しいEM Navigatorと万見の変更点

他の情報も見る