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- PDB-5y9c: Crystal structure of HPV58 pentamer in complex with the Fab fragm... -

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基本情報

登録情報
データベース: PDB / ID: 5y9c
タイトルCrystal structure of HPV58 pentamer in complex with the Fab fragment of antibody A12A3
要素
  • Major capsid protein L1
  • heavy chain of Fab fragment of antibody A12A3
  • light chain of Fab fragment of antibody A12A3
キーワードSTRUCTURAL PROTEIN/IMMUNE SYSTEM / capsid protein / STRUCTURAL PROTEIN-IMMUNE SYSTEM complex
機能・相同性
機能・相同性情報


T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity
類似検索 - 分子機能
Major capsid L1 (late) superfamily, Papillomavirus / Major capsid L1 (late) protein, Papillomavirus / Major capsid L1 (late) superfamily, Papillomavirus / L1 (late) protein / Polyomavirus Vp1; Chain A / Double-stranded DNA virus, group I, capsid / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
類似検索 - ドメイン・相同性
Major capsid protein L1
類似検索 - 構成要素
生物種Human papillomavirus type 58 (パピローマウイルス)
Mus musculus (ハツカネズミ)
手法X線回折 / シンクロトロン / 解像度: 3.443 Å
データ登録者Li, S.W. / Li, Z.H.
資金援助 中国, 4件
組織認可番号
National Natural Science Foundation of China31670935 中国
National Natural Science Foundation of China81671645 中国
National Natural Science Foundation of China81571996 中国
Natural Science Foundation of Fujian Province2015YZ0002 中国
引用ジャーナル: mBio / : 2017
タイトル: Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human Papillomavirus.
著者: Zhihai Li / Daning Wang / Ying Gu / Shuo Song / Maozhou He / Jingjie Shi / Xinlin Liu / Shuangping Wei / Jinjin Li / Hai Yu / Qingbing Zheng / Xiaodong Yan / Timothy S Baker / Jun Zhang / ...著者: Zhihai Li / Daning Wang / Ying Gu / Shuo Song / Maozhou He / Jingjie Shi / Xinlin Liu / Shuangping Wei / Jinjin Li / Hai Yu / Qingbing Zheng / Xiaodong Yan / Timothy S Baker / Jun Zhang / Jason S McLellan / Shaowei Li / Ningshao Xia /
要旨: Persistent, high-risk human papillomavirus (HPV) infection is the primary cause of cervical cancer. Neutralizing antibodies elicited by L1-only virus-like particles (VLPs) can block HPV infection; ...Persistent, high-risk human papillomavirus (HPV) infection is the primary cause of cervical cancer. Neutralizing antibodies elicited by L1-only virus-like particles (VLPs) can block HPV infection; however, the lack of high-resolution structures has limited our understanding of the mode of virus infection and the requirement for type specificity at the molecular level. Here, we describe two antibodies, A12A3 and 28F10, that specifically bind to and neutralize HPV58 and HPV59, respectively, through two distinct binding stoichiometries. We show that the epitopes of A12A3 are clustered in the DE loops of two adjacent HPV58 L1 monomers, whereas 28F10 recognizes the HPV59 FG loop of a single monomer. Via structure-based mutagenesis and analysis of antibody binding, we further identified the residues HPV58 D154, S168, and N170 and HPV59 M267, Q270, E273, Y276, K278, and R283, which play critical roles in virus infection. By substituting these strategic epitope residues into other HPV genotypes, we could then redirect the type-specific binding of the antibodies to these genotypes, thus highlighting the importance of these specific residues, HPV58 R161, S168, and N308 and HPV59 Q270, E273, and D281. Overall, our findings provide molecular insights into potential structural determinants of HPV required for infectivity and type specificity. High-risk human papillomaviruses (HPVs) are considered the major causative pathogens of cancers that affect epithelial mucosa, such as cervical cancer. However, because of the lack of high-resolution structural information on the sites of neutralization, we have yet to determine the precise mode of HPV infection and how different types of HPV cause infection. Our crystal structures in this study have uncovered discrete binding stoichiometries for two different antibodies. We show that one A12A3 Fab binds to the center of one HPV58 pentamer, whereas five 28F10 Fabs bind along the top fringe of one HPV59 pentamer. Furthermore, through targeted epitope analysis, we show that 6 to 7 discontinuous residues of the L1 major capsid protein of HPV are determinants, at least in part, for virus infection and type specificity. This knowledge will help us to unravel the process of HPV infection and can potentially be used to drive the development of therapeutics that target neutralization-sensitive sites.
履歴
登録2017年8月24日登録サイト: PDBJ / 処理サイト: PDBJ
改定 1.02017年10月25日Provider: repository / タイプ: Initial release
改定 1.12024年11月6日Group: Data collection / Database references / Structure summary
カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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

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集合体

登録構造単位
A: Major capsid protein L1
B: Major capsid protein L1
C: Major capsid protein L1
D: Major capsid protein L1
E: Major capsid protein L1
H: heavy chain of Fab fragment of antibody A12A3
L: light chain of Fab fragment of antibody A12A3


分子量 (理論値)分子数
合計 (水以外)323,3577
ポリマ-323,3577
非ポリマー00
00
1


  • 登録構造と同一
  • 登録者が定義した集合体
タイプ名称対称操作
identity operation1_555x,y,z1
Buried area41670 Å2
ΔGint-241 kcal/mol
Surface area92810 Å2
単位格子
Length a, b, c (Å)121.571, 102.600, 138.032
Angle α, β, γ (deg.)90.00, 114.52, 90.00
Int Tables number4
Space group name H-MP1211

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要素

#1: タンパク質
Major capsid protein L1


分子量: 55250.492 Da / 分子数: 5 / 断片: UNP RESIDUES 36-524 / 由来タイプ: 組換発現
由来: (組換発現) Human papillomavirus type 58 (パピローマウイルス)
遺伝子: L1 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P26535
#2: 抗体 heavy chain of Fab fragment of antibody A12A3


分子量: 23374.998 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Mus musculus (ハツカネズミ)
#3: 抗体 light chain of Fab fragment of antibody A12A3


分子量: 23729.375 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Mus musculus (ハツカネズミ)
Has protein modificationY

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実験情報

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実験

実験手法: X線回折 / 使用した結晶の数: 1

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試料調製

結晶マシュー密度: 2.42 Å3/Da / 溶媒含有率: 49.2 %
結晶化温度: 293 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 8
詳細: 0.2 M lithium chloride, 0.1 M Tris pH 8.0, 14% (w/v) PEG 3350

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データ収集

回折平均測定温度: 80 K
放射光源由来: シンクロトロン / サイト: SSRF / ビームライン: BL17U1 / 波長: 0.9795 Å
検出器タイプ: ADSC QUANTUM 315r / 検出器: CCD / 日付: 2012年9月10日
放射プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長波長: 0.9795 Å / 相対比: 1
反射解像度: 3.45→50 Å / Num. obs: 41030 / % possible obs: 99.9 % / 冗長度: 6.2 % / Net I/σ(I): 10.4

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解析

ソフトウェア
名称バージョン分類
PHENIX(1.11.1_2575)精密化
HKL-2000データスケーリング
PHASER位相決定
精密化解像度: 3.443→47.861 Å / SU ML: 0.43 / 交差検証法: FREE R-VALUE / σ(F): 1.37 / 位相誤差: 26.58 / 立体化学のターゲット値: ML
Rfactor反射数%反射
Rfree0.2492 2024 4.94 %
Rwork0.2023 --
obs0.2046 40995 99.51 %
溶媒の処理減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å / 溶媒モデル: FLAT BULK SOLVENT MODEL
精密化ステップサイクル: LAST / 解像度: 3.443→47.861 Å
タンパク質核酸リガンド溶媒全体
原子数19789 0 0 0 19789
拘束条件
Refine-IDタイプDev ideal
X-RAY DIFFRACTIONf_bond_d0.00220307
X-RAY DIFFRACTIONf_angle_d0.50727566
X-RAY DIFFRACTIONf_dihedral_angle_d11.58912022
X-RAY DIFFRACTIONf_chiral_restr0.0422956
X-RAY DIFFRACTIONf_plane_restr0.0043585
LS精密化 シェル
解像度 (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.4425-3.52860.31491270.2872662X-RAY DIFFRACTION95
3.5286-3.62390.36011290.27022777X-RAY DIFFRACTION100
3.6239-3.73050.31371440.262767X-RAY DIFFRACTION100
3.7305-3.85090.27951440.24542781X-RAY DIFFRACTION100
3.8509-3.98850.28531380.23862780X-RAY DIFFRACTION100
3.9885-4.14810.27711530.23432774X-RAY DIFFRACTION100
4.1481-4.33670.25711690.20072772X-RAY DIFFRACTION100
4.3367-4.56520.23161600.19072760X-RAY DIFFRACTION100
4.5652-4.8510.19211480.16672794X-RAY DIFFRACTION100
4.851-5.22510.20171450.17022783X-RAY DIFFRACTION100
5.2251-5.75020.22221360.18352817X-RAY DIFFRACTION100
5.7502-6.58040.24961490.20732787X-RAY DIFFRACTION100
6.5804-8.28360.26331520.19482818X-RAY DIFFRACTION100
8.2836-47.86530.21691300.16092899X-RAY DIFFRACTION100
精密化 TLS

手法: 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)
10.1847-0.50670.02730.77550.0707-0.1190.215-0.1062-0.07970.2725-0.0816-0.0618-0.03050.087100.58220.0095-0.06340.45310.05630.536511.978-4.194164.5621
20.24060.11170.29220.08650.11670.25410.0365-0.1627-0.18830.7496-0.3861-0.2502-0.0749-0.2009-0.00170.7467-0.2510.04260.61280.06590.5927-2.2106-4.8779.4069
30.48370.19670.55170.52520.45270.4961-0.0159-0.0449-0.1817-0.006-0.01010.03250.13490.277-00.54470.04740.01970.449-0.00890.62313.5914-1.20541.923
40.42190.5951-0.27040.56120.60550.88030.0805-0.30580.14930.1397-0.22030.09660.30050.2997-0.00070.4884-0.04470.0330.60950.15490.67536.4067-3.563669.2207
50.40590.00140.4056-0.25210.1380.56970.0112-0.1582-0.13750.0514-0.0061-0.1098-0.3055-0.04830.01180.7223-0.11990.04240.4549-0.11180.509417.58836.823968.2463
60.5890.2090.33431.0786-0.10550.5615-0.2764-0.3264-0.29220.43770.04080.2977-0.73820.50810.37460.51-0.1446-0.06090.406-0.2340.37211.087336.615869.3663
70.1755-0.05650.07990.01110.003-0.0360.0768-0.21470.1545-0.3169-0.0754-0.1804-0.13360.496400.6072-0.02220.07330.7797-0.02690.675127.762817.925341.1908
80.06690.0968-0.12120.2173-0.00730.0464-0.49040.1891-0.1062-0.4559-0.09570.03110.3420.5868-0.00090.75060.1360.04770.93910.11110.762331.381510.482164.6555
9-0.08080.5695-0.76530.3833-0.51860.65180.0397-0.2602-0.17520.024-0.05980.1048-0.1110.4156-00.4430.0049-0.02370.6922-0.03230.560525.1515.354453.3459
100.0173-0.00990.05720.11050.08010.04320.033-0.04920.2893-0.06560.0932-0.19320.3619-0.467200.6834-0.06380.05750.5446-0.04190.74693.598329.032962.694
110.1024-0.4926-0.38050.64760.0087-0.09840.0345-0.04820.00270.1721-0.2176-0.0539-0.27340.382-0.03110.6752-0.19350.05820.6803-0.09510.493620.151340.171754.1637
120.2535-0.1919-0.39370.0410.02140.55440.2035-0.42240.00990.17980.00850.2686-0.66910.37860.01860.7725-0.07450.11270.63-0.18180.64299.310636.537978.9926
130.40730.02040.17740.0908-0.00890.25630.1216-0.0148-0.4493-0.4968-0.12410.20130.0103-0.1261-0.15650.6822-0.2968-0.03770.5125-0.1771.0245-13.1512-11.127831.7606
140.46890.12310.20050.03310.06680.2098-0.0043-0.2375-0.3526-0.12560.20990.44630.4401-0.26280.31740.7554-0.5053-0.0740.94720.04961.3738-29.7964-13.698743.4128
150.20.34170.16260.79930.26710.1657-0.08740.8086-0.2349-0.5574-0.413-0.18210.0311-0.3752-0.26640.4281-0.1897-0.17210.4797-0.34940.6284.88246.831619.1711
160.2162-0.1187-0.06180.24320.0286-0.009-0.01880.6317-0.548-0.1364-0.2692-0.03240.3397-0.383-0.46450.4535-0.4546-0.17210.6246-0.57560.5219-8.67413.298712.8567
170.3541-0.47380.12270.4785-0.10220.0352-0.10780.191-0.2417-0.13930.23910.12610.1945-0.092500.6609-0.1491-0.04020.8523-0.1590.6971-5.46856.685719.412
180.6766-0.49410.37450.480.10230.4206-0.02720.219-0.4102-0.2251-0.06970.09430.1818-0.3756-00.5472-0.1717-0.08050.6395-0.11020.5849-6.50768.250326.7183
190.1501-0.0967-0.23540.2589-0.49520.930.29090.33370.095-0.14-0.08890.01660.3451-0.33620.00010.599-0.14250.01920.6863-0.17940.9283-9.9167-11.007531.186
200.00770.02090.02190.1751-0.05260.07320.1502-0.0909-0.2688-0.09950.130.2024-0.0151-0.39260.00010.8137-0.15270.11230.8343-0.07121.05-17.3427-10.997445.3008
210.0421-0.3380.24730.0396-0.28550.43890.04430.15730.08540.03960.13110.15260.3592-0.2280.1880.5116-0.0463-0.23111.03670.04030.664-23.069126.00815.1368
220.0360.36450.12350.37530.24240.39820.12860.4772-0.0928-0.3234-0.05630.162-0.2562-0.2882-0.01840.5030.1058-0.19570.85570.05840.7163-10.113127.602519.1322
230.34360.00150.17370.4022-0.00790.2250.13730.2329-0.1853-0.2368-0.04190.0709-0.1577-0.048600.68610.0674-0.07560.8760.06040.5662-0.245237.420219.2565
240.1140.05730.03630.1806-0.2810.52210.0472-0.063-0.10230.2302-0.14640.08850.0078-1.1991-0.06560.6293-0.0033-0.15290.8347-0.01510.7222-19.785825.548231.8412
250.01960.11-0.05170.16360.0884-0.0855-0.30380.43980.2749-0.06110.3605-0.17280.2585-0.22100.65120.0221-0.09861.0814-0.09480.7267-11.828316.661813.7781
260.50470.491-0.3480.2368-0.30770.3480.15640.2354-0.0324-0.4041-0.16010.39140.0438-0.9298-0.13430.64210.1307-0.23151.42430.03211.0085-34.724729.665821.2957
27-0.00120.0051-0.14690.43740.04970.29160.10660.04720.095-0.0656-0.0774-0.0709-0.22970.1897-00.94460.26760.02310.5230.06420.7178-4.07655.673837.7782
280.05340.01510.40590.4204-0.27320.8405-0.2985-0.3596-0.17330.13430.17820.1698-0.35130.229-0.00040.85320.13410.04040.5245-0.0080.69794.884345.376737.5662
290.72880.27150.55950.23920.30540.78290.11940.22770.03450.01040.24340.3435-0.7110.61740.08640.9681-0.00310.14990.4042-0.00040.627213.527947.446142.8863
300.12510.0585-0.3150.4184-0.14450.7793-0.0687-0.1753-0.2005-0.06350.05440.086-0.56120.37430.00090.6243-0.1318-0.00250.5252-0.03830.651520.023339.610242.3731
310.10970.10150.17440.1120.02390.2021-0.24050.00710.02590.51520.27230.1339-0.0351-0.35940.00580.83980.17460.04650.6626-0.13150.8664-8.311741.229345.8168
320.56470.09450.1034-0.1988-0.03630.26340.19910.280.1624-0.2551-0.11840.1265-0.937-0.1937-0.0030.87680.21480.12890.46070.00190.7334-6.819953.23837.0707
330.1979-0.09130.09530.4391-0.13280.17550.0445-0.04420.004-0.0386-0.1629-0.0713-0.05730.27800.95910.0240.04230.9451-0.08410.711238.393616.32696.5654
340.0595-0.0227-0.0531-0.0017-0.00030.0266-0.34280.0562-0.52440.0784-0.0388-0.08030.2260.0672-01.02970.10780.09261.1643-0.10061.346532.633112.1395.5967
350.28710.0547-0.36710.0457-0.09720.1528-0.27570.2267-0.1207-0.0140.11540.2820.38410.335101.08640.06870.04041.2139-0.12630.967338.224319.17314.6198
360.06810.08390.10120.05390.00410.0459-0.3816-0.59410.68840.26260.0651-0.2489-0.5340.140901.21130.1369-0.02261.4221-0.07751.604369.810512.1519-4.6088
370.00910.02710.00030.02620.07310.0590.2791-0.8457-0.49240.09420.04920.2927-0.144-0.151901.75440.02710.04591.80770.21041.780967.413213.0173-1.8514
380.0314-0.0243-0.02580.01560.03380.011-0.34790.48810.0125-0.3832-0.01420.54480.9501-0.0771-0.00011.64540.26890.07171.7784-0.08361.36264.801616.1437-6.5899
390.01770.0325-0.0246-0.02580.00110.0568-0.2185-0.42380.3230.331-0.0170.37680.03930.467-01.8291-0.0773-0.48861.64070.0752.05776.651419.4341-1.5599
400.01470.01590.0091-0.00540.0080.047-0.02730.1016-0.31510.97170.42890.76130.52110.232501.07240.066-0.05011.7670.31821.186670.23219.82124.9123
410.0653-0.03610.0753-0.0218-0.01650.0360.27490.2349-0.1926-0.6441-0.4371-0.3464-0.1875-0.5620.00010.8734-0.07780.04231.15930.0730.811441.597134.3826-13.305
420.05990.0135-0.06410.0238-0.04750.09380.30010.2640.0359-0.63860.1020.0866-0.1785-0.55820.00010.8808-0.04120.06651.1833-0.00210.72933.046132.9498-4.8848
430.0343-0.0105-0.03830.008-0.09380.2568-0.1414-0.38190.0418-0.2184-0.24350.26140.06780.41800.8596-0.1238-0.04791.1189-0.09790.911542.485636.43771.4331
440.02920.0345-0.05650.0588-0.04170.06430.37820.2032-0.1177-0.110.10980.46810.2181-0.49530.00021.3918-0.05570.14521.279-0.1110.752636.174139.5847-8.6487
45-0.01270.01210.00920.3701-0.06940.0260.37750.60430.34380.1837-0.0330.38190.12210.136601.0953-0.13490.06331.2038-0.11320.673741.50531.7284-5.1276
460.0564-0.03860.04010.00430.01470.05760.07250.37890.15260.3373-0.3190.29550.59080.1353-0.00021.1468-0.12880.33921.2846-0.08461.088661.186534.6896-14.2298
470.3941-0.01780.0610.11340.009-0.00570.2701-0.14050.40690.20.4774-0.82070.25130.27840.01671.37240.4089-0.21681.4236-0.28311.104773.156515.8821-16.5894
480.0797-0.09810.08280.0774-0.0313-0.03430.23190.2862-0.9787-0.2585-0.35980.7161-0.74330.4002-0.00031.24240.18180.0981.7132-0.3311.076369.705717.1187-14.5367
491.53371.10140.63990.75580.41650.2764-0.6174-0.17350.4409-0.2512-0.04820.4966-0.27840.5353-0.03630.97960.13280.17541.5101-0.21510.72375.333224.2976-22.8277
精密化 TLSグループ
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 20 through 83 )
2X-RAY DIFFRACTION2chain 'A' and (resid 84 through 110 )
3X-RAY DIFFRACTION3chain 'A' and (resid 111 through 355 )
4X-RAY DIFFRACTION4chain 'A' and (resid 356 through 473 )
5X-RAY DIFFRACTION5chain 'B' and (resid 20 through 83 )
6X-RAY DIFFRACTION6chain 'B' and (resid 84 through 126 )
7X-RAY DIFFRACTION7chain 'B' and (resid 127 through 161 )
8X-RAY DIFFRACTION8chain 'B' and (resid 162 through 187 )
9X-RAY DIFFRACTION9chain 'B' and (resid 188 through 296 )
10X-RAY DIFFRACTION10chain 'B' and (resid 297 through 324 )
11X-RAY DIFFRACTION11chain 'B' and (resid 325 through 381 )
12X-RAY DIFFRACTION12chain 'B' and (resid 382 through 473 )
13X-RAY DIFFRACTION13chain 'C' and (resid 20 through 83 )
14X-RAY DIFFRACTION14chain 'C' and (resid 84 through 110 )SOU 2137 O SER
15X-RAY DIFFRACTION15chain 'C' and (resid 111 through 172 )
16X-RAY DIFFRACTION16chain 'C' and (resid 173 through 209 )
17X-RAY DIFFRACTION17chain 'C' and (resid 210 through 272 )
18X-RAY DIFFRACTION18chain 'C' and (resid 273 through 338 )
19X-RAY DIFFRACTION19chain 'C' and (resid 339 through 442 )
20X-RAY DIFFRACTION20chain 'C' and (resid 443 through 473 )
21X-RAY DIFFRACTION21chain 'D' and (resid 20 through 83 )
22X-RAY DIFFRACTION22chain 'D' and (resid 84 through 146 )
23X-RAY DIFFRACTION23chain 'D' and (resid 147 through 296 )
24X-RAY DIFFRACTION24chain 'D' and (resid 297 through 324 )
25X-RAY DIFFRACTION25chain 'D' and (resid 325 through 381 )
26X-RAY DIFFRACTION26chain 'D' and (resid 382 through 473 )
27X-RAY DIFFRACTION27chain 'E' and (resid 20 through 83 )
28X-RAY DIFFRACTION28chain 'E' and (resid 84 through 146 )
29X-RAY DIFFRACTION29chain 'E' and (resid 147 through 209 )
30X-RAY DIFFRACTION30chain 'E' and (resid 210 through 296 )
31X-RAY DIFFRACTION31chain 'E' and (resid 297 through 324 )
32X-RAY DIFFRACTION32chain 'E' and (resid 325 through 473 )
33X-RAY DIFFRACTION33chain 'H' and (resid 1 through 60 )
34X-RAY DIFFRACTION34chain 'H' and (resid 61 through 77 )
35X-RAY DIFFRACTION35chain 'H' and (resid 78 through 113 )
36X-RAY DIFFRACTION36chain 'H' and (resid 114 through 141 )
37X-RAY DIFFRACTION37chain 'H' and (resid 142 through 160 )
38X-RAY DIFFRACTION38chain 'H' and (resid 161 through 179 )
39X-RAY DIFFRACTION39chain 'H' and (resid 180 through 199 )
40X-RAY DIFFRACTION40chain 'H' and (resid 200 through 216 )
41X-RAY DIFFRACTION41chain 'L' and (resid 1 through 25 )
42X-RAY DIFFRACTION42chain 'L' and (resid 26 through 38 )
43X-RAY DIFFRACTION43chain 'L' and (resid 39 through 61 )
44X-RAY DIFFRACTION44chain 'L' and (resid 62 through 75 )
45X-RAY DIFFRACTION45chain 'L' and (resid 76 through 101 )
46X-RAY DIFFRACTION46chain 'L' and (resid 102 through 112 )
47X-RAY DIFFRACTION47chain 'L' and (resid 113 through 157 )
48X-RAY DIFFRACTION48chain 'L' and (resid 158 through 188 )
49X-RAY DIFFRACTION49chain 'L' and (resid 193 through 209 )

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万見について

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お知らせ

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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

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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

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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

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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

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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。

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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