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- PDB-6gff: Structure of GARP (LRRC32) in complex with latent TGF-beta1 and M... -

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基本情報

登録情報
データベース: PDB / ID: 6gff
タイトルStructure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab
要素
  • (Transforming growth factor beta- ...) x 2
  • Leucine-rich repeat-containing protein 32
  • MHG-8 Fab heavy chain
  • MHG-8 Fab light chain
キーワードIMMUNE SYSTEM / GARP / TGF-B1 / Activation / Treg
機能・相同性
機能・相同性情報


establishment of protein localization to extracellular region / cellular response to acetaldehyde / frontal suture morphogenesis / Influenza Virus Induced Apoptosis / adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains / positive regulation of microglia differentiation / regulation of interleukin-23 production / branch elongation involved in mammary gland duct branching / positive regulation of primary miRNA processing / columnar/cuboidal epithelial cell maturation ...establishment of protein localization to extracellular region / cellular response to acetaldehyde / frontal suture morphogenesis / Influenza Virus Induced Apoptosis / adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains / positive regulation of microglia differentiation / regulation of interleukin-23 production / branch elongation involved in mammary gland duct branching / positive regulation of primary miRNA processing / columnar/cuboidal epithelial cell maturation / negative regulation of skeletal muscle tissue development / embryonic liver development / regulation of branching involved in mammary gland duct morphogenesis / macrophage derived foam cell differentiation / response to laminar fluid shear stress / regulation of enamel mineralization / regulation of cartilage development / TGFBR2 MSI Frameshift Mutants in Cancer / regulation of striated muscle tissue development / regulatory T cell differentiation / regulation of blood vessel remodeling / tolerance induction to self antigen / regulation of protein import into nucleus / extracellular matrix assembly / negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of hyaluronan biosynthetic process / type III transforming growth factor beta receptor binding / positive regulation of cardiac muscle cell differentiation / myofibroblast differentiation / odontoblast differentiation / positive regulation of odontogenesis / connective tissue replacement involved in inflammatory response wound healing / positive regulation of exit from mitosis / Langerhans cell differentiation / TGFBR2 Kinase Domain Mutants in Cancer / positive regulation of smooth muscle cell differentiation / negative regulation of macrophage cytokine production / secondary palate development / positive regulation of isotype switching to IgA isotypes / positive regulation of mesenchymal stem cell proliferation / SMAD2/3 Phosphorylation Motif Mutants in Cancer / TGFBR1 KD Mutants in Cancer / membrane protein intracellular domain proteolysis / positive regulation of receptor signaling pathway via STAT / retina vasculature development in camera-type eye / positive regulation of extracellular matrix assembly / heart valve morphogenesis / TGFBR3 regulates TGF-beta signaling / mammary gland branching involved in thelarche / bronchiole development / hyaluronan catabolic process / positive regulation of vasculature development / lens fiber cell differentiation / negative regulation of extracellular matrix disassembly / ATP biosynthetic process / positive regulation of branching involved in ureteric bud morphogenesis / type II transforming growth factor beta receptor binding / receptor catabolic process / TGFBR1 LBD Mutants in Cancer / positive regulation of chemotaxis / receptor ligand inhibitor activity / type I transforming growth factor beta receptor binding / germ cell migration / negative regulation of biomineral tissue development / positive regulation of mononuclear cell migration / phospholipid homeostasis / response to salt / endoderm development / negative regulation of cell-cell adhesion mediated by cadherin / negative regulation of myoblast differentiation / positive regulation of vascular permeability / response to cholesterol / oligodendrocyte development / negative regulation of interleukin-17 production / cell-cell junction organization / surfactant homeostasis / deubiquitinase activator activity / phosphate-containing compound metabolic process / transforming growth factor beta binding / sprouting angiogenesis / negative regulation of release of sequestered calcium ion into cytosol / digestive tract development / aortic valve morphogenesis / negative regulation of ossification / positive regulation of chemokine (C-X-C motif) ligand 2 production / response to vitamin D / RUNX3 regulates CDKN1A transcription / positive regulation of fibroblast migration / face morphogenesis / neural tube development / positive regulation of regulatory T cell differentiation / ureteric bud development / Molecules associated with elastic fibres / positive regulation of peptidyl-tyrosine phosphorylation / negative regulation of phagocytosis / negative regulation of cytokine production / positive regulation of epidermal growth factor receptor signaling pathway / negative regulation of neuroblast proliferation / lung alveolus development / Syndecan interactions
類似検索 - 分子機能
Jelly Rolls - #970 / Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / Leucine rich repeat N-terminal domain / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family ...Jelly Rolls - #970 / Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / Leucine rich repeat N-terminal domain / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / Leucine rich repeat, ribonuclease inhibitor type / Leucine-rich repeats, bacterial type / Cystine-knot cytokine / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Jelly Rolls / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
類似検索 - ドメイン・相同性
Transforming growth factor beta-1 proprotein / Transforming growth factor beta activator LRRC32
類似検索 - 構成要素
生物種Homo sapiens (ヒト)
Mus musculus (ハツカネズミ)
手法X線回折 / シンクロトロン / 分子置換 / 解像度: 3.1 Å
データ登録者Merceron, R. / Lienart, S. / Vanderaa, C. / Colau, D. / Stockis, J. / Van Der Woning, B. / De Haard, H. / Saunders, M. / Coulie, P.G. / Savvides, S.N. / Lucas, S.
資金援助 ベルギー, 2件
組織認可番号
Walloon Excellence in Lifesciences & BIOtechnologyBF-2014-01 ベルギー
European Research CouncilTARG-SUP 682818 ベルギー
引用ジャーナル: Science / : 2018
タイトル: Structural basis of latent TGF-beta 1 presentation and activation by GARP on human regulatory T cells.
著者: Lienart, S. / Merceron, R. / Vanderaa, C. / Lambert, F. / Colau, D. / Stockis, J. / van der Woning, B. / De Haard, H. / Saunders, M. / Coulie, P.G. / Savvides, S.N. / Lucas, S.
履歴
登録2018年4月30日登録サイト: PDBE / 処理サイト: PDBE
改定 1.02018年11月7日Provider: repository / タイプ: Initial release
改定 1.12018年12月5日Group: Data collection / Database references
カテゴリ: citation / citation_author / pdbx_database_proc
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
改定 2.02020年7月29日Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
カテゴリ: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
解説: Carbohydrate remediation / Provider: repository / タイプ: Remediation
改定 2.12024年11月6日Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
カテゴリ: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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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: Transforming growth factor beta-1
B: Transforming growth factor beta-1
C: Transforming growth factor beta-1
D: Transforming growth factor beta-1
E: Transforming growth factor beta-1
F: Transforming growth factor beta-1
G: Transforming growth factor beta-1
H: Transforming growth factor beta-1
I: Leucine-rich repeat-containing protein 32
J: Leucine-rich repeat-containing protein 32
K: MHG-8 Fab light chain
L: MHG-8 Fab heavy chain
M: MHG-8 Fab light chain
N: MHG-8 Fab heavy chain
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)398,36121
ポリマ-394,25514
非ポリマー4,1067
00
1
A: Transforming growth factor beta-1
B: Transforming growth factor beta-1
C: Transforming growth factor beta-1
D: Transforming growth factor beta-1
I: Leucine-rich repeat-containing protein 32
K: MHG-8 Fab light chain
L: MHG-8 Fab heavy chain
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)199,31211
ポリマ-197,1287
非ポリマー2,1844
0
タイプ名称対称操作
identity operation1_555x,y,z1
2
E: Transforming growth factor beta-1
F: Transforming growth factor beta-1
G: Transforming growth factor beta-1
H: Transforming growth factor beta-1
J: Leucine-rich repeat-containing protein 32
M: MHG-8 Fab light chain
N: MHG-8 Fab heavy chain
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)199,04910
ポリマ-197,1287
非ポリマー1,9223
0
タイプ名称対称操作
identity operation1_555x,y,z1
単位格子
Length a, b, c (Å)103.860, 175.010, 145.770
Angle α, β, γ (deg.)90.00, 92.23, 90.00
Int Tables number4
Space group name H-MP1211

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要素

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Transforming growth factor beta- ... , 2種, 8分子 ACEGBDFH

#1: タンパク質
Transforming growth factor beta-1 / TGF-beta-1


分子量: 28531.488 Da / 分子数: 4 / 断片: LAP / 由来タイプ: 組換発現
詳細: Mature protein expected to start at Leucine30. Obtained after cleavage of Pro-TGF-b1 by Furin after Arginine278.
由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: TGFB1, TGFB / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P01137
#2: タンパク質
Transforming growth factor beta-1 / TGF-beta-1


分子量: 12809.812 Da / 分子数: 4 / 断片: Mature / 由来タイプ: 組換発現
詳細: Obtained after cleavage of Pro-TGF-b1 by Furin after Arginine278.
由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: TGFB1, TGFB / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P01137

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タンパク質 , 1種, 2分子 IJ

#3: タンパク質 Leucine-rich repeat-containing protein 32 / Garpin / Glycoprotein A repetitions predominant / GARP


分子量: 67235.578 Da / 分子数: 2 / 由来タイプ: 組換発現 / 詳細: Mature protein expected to start at Histidine20. / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: LRRC32, D11S833E, GARP / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q14392

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抗体 , 2種, 4分子 KMLN

#4: 抗体 MHG-8 Fab light chain


分子量: 23376.770 Da / 分子数: 2 / 由来タイプ: 天然
詳細: Mature protein expected to start at Aspartic acid21.
由来: (天然) Mus musculus (ハツカネズミ)
#5: 抗体 MHG-8 Fab heavy chain


分子量: 23832.617 Da / 分子数: 2 / 由来タイプ: 天然 / 詳細: Mature protein expected to start at Glutamine20. / 由来: (天然) Mus musculus (ハツカネズミ)

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, 3種, 7分子

#6: 多糖
beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


タイプ: oligosaccharide / 分子量: 586.542 Da / 分子数: 5 / 由来タイプ: 組換発現
記述子タイププログラム
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#7: 多糖 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


タイプ: oligosaccharide / 分子量: 424.401 Da / 分子数: 1 / 由来タイプ: 組換発現
記述子タイププログラム
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#8: 多糖 alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


タイプ: oligosaccharide / 分子量: 748.682 Da / 分子数: 1 / 由来タイプ: 組換発現
記述子タイププログラム
DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE

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詳細

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: 3.3 Å3/Da / 溶媒含有率: 62.67 %
結晶化温度: 277 K / 手法: 蒸気拡散法, ハンギングドロップ法 / 詳細: 15% (w/v) PEG4000, 0.1 M HEPES pH 6.75

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データ収集

回折平均測定温度: 100 K
放射光源由来: シンクロトロン / サイト: SLS / ビームライン: X06SA / 波長: 1.00001 Å
検出器タイプ: DECTRIS PILATUS3 6M / 検出器: PIXEL / 日付: 2014年10月27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: 1.00001 Å / 相対比: 1
反射解像度: 3.1→50 Å / Num. obs: 84967 / % possible obs: 90.1 % / 冗長度: 2.3 % / Biso Wilson estimate: 77.7 Å2 / Net I/σ(I): 8.15
反射 シェル解像度: 3.1→3.18 Å / 冗長度: 2.2 % / Num. unique obs: 6320 / % possible all: 90.6

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解析

ソフトウェア
名称分類
PHENIX精密化
BUSTER精密化
XDSデータ削減
XSCALEデータスケーリング
PHASER位相決定
精密化構造決定の手法: 分子置換 / 解像度: 3.1→29.921 Å / SU ML: 0.48 / 交差検証法: FREE R-VALUE / σ(F): 1.36 / 位相誤差: 29.07
Rfactor反射数%反射
Rfree0.2684 4244 5 %
Rwork0.233 --
obs0.2348 84892 90.11 %
溶媒の処理減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å
精密化ステップサイクル: LAST / 解像度: 3.1→29.921 Å
タンパク質核酸リガンド溶媒全体
原子数21395 0 273 0 21668
拘束条件
Refine-IDタイプDev ideal
X-RAY DIFFRACTIONf_bond_d0.00222185
X-RAY DIFFRACTIONf_angle_d0.54830416
X-RAY DIFFRACTIONf_dihedral_angle_d8.7313321
X-RAY DIFFRACTIONf_chiral_restr0.0413608
X-RAY DIFFRACTIONf_plane_restr0.0033925
LS精密化 シェル
解像度 (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0999-3.13510.37641430.33682706X-RAY DIFFRACTION90
3.1351-3.17190.39681420.33442698X-RAY DIFFRACTION91
3.1719-3.21060.4081370.33542621X-RAY DIFFRACTION88
3.2106-3.25120.34271310.32522485X-RAY DIFFRACTION83
3.2512-3.29390.40561300.32132453X-RAY DIFFRACTION83
3.2939-3.3390.36721480.3212821X-RAY DIFFRACTION95
3.339-3.38660.33911490.30372817X-RAY DIFFRACTION94
3.3866-3.43710.34721460.28342796X-RAY DIFFRACTION94
3.4371-3.49070.30661470.26722797X-RAY DIFFRACTION94
3.4907-3.54790.3141450.26692770X-RAY DIFFRACTION93
3.5479-3.60890.29591460.26442770X-RAY DIFFRACTION93
3.6089-3.67440.29371460.25032777X-RAY DIFFRACTION93
3.6744-3.7450.34071460.24812773X-RAY DIFFRACTION93
3.745-3.82130.27221460.24292772X-RAY DIFFRACTION93
3.8213-3.90420.24651440.21672741X-RAY DIFFRACTION93
3.9042-3.99480.23661460.20642774X-RAY DIFFRACTION92
3.9948-4.09450.23231440.20432726X-RAY DIFFRACTION93
4.0945-4.20490.23891430.20222723X-RAY DIFFRACTION91
4.2049-4.32830.21271420.19462687X-RAY DIFFRACTION90
4.3283-4.46750.23441400.18682669X-RAY DIFFRACTION90
4.4675-4.62670.20361370.18712608X-RAY DIFFRACTION88
4.6267-4.81120.19971250.17812366X-RAY DIFFRACTION80
4.8112-5.02920.20221420.18752689X-RAY DIFFRACTION90
5.0292-5.29290.23891440.19942742X-RAY DIFFRACTION92
5.2929-5.62250.2691430.20862724X-RAY DIFFRACTION91
5.6225-6.05330.26271430.23822720X-RAY DIFFRACTION90
6.0533-6.65640.29581420.25412692X-RAY DIFFRACTION90
6.6564-7.60580.3111390.25472649X-RAY DIFFRACTION88
7.6058-9.53080.25111290.23222442X-RAY DIFFRACTION81
9.5308-29.92260.26961390.24462640X-RAY DIFFRACTION86
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)
10.9450.60.08634.39151.33052.39540.19810.2013-0.7466-0.76340.12290.56630.9794-0.4536-0.29011.2979-0.0617-0.4880.8509-0.01091.11086.283529.044313.504
23.5815-0.53390.40173.16061.00262.2338-0.03060.2515-0.3654-0.48180.1562-0.11090.33970.5727-0.19120.4975-0.0413-0.06170.4640.01230.513224.835648.065129.2051
33.27510.47490.12476.41860.20763.1649-0.0376-0.239-1.07630.53120.13710.18351.19960.2266-0.03910.83680.0937-0.1150.69550.12120.776818.004934.394346.895
43.88272.1244.33534.09414.48499.6043-0.07130.2495-0.2485-0.5374-0.15430.84250.5474-0.85810.32050.72-0.1771-0.22260.69320.02050.66795.134349.333820.5
51.6462-2.33230.27615.6571-0.60362.1535-0.3024-0.30680.1290.84670.422-0.56040.27860.6382-0.14020.74610.1028-0.16090.8176-0.18320.519848.642129.5933-5.1536
63.7058-0.06661.25744.36811.96116.94690.2434-0.0152-0.03810.16050.05310.42340.3453-0.4241-0.30050.41610.0691-0.05960.30910.03530.494824.847440.1507-26.8089
74.0928-3.3141.4725.897-2.05871.2470.41870.434-0.4763-0.8014-0.3319-0.0150.60790.2518-0.10030.75350.0761-0.10020.6112-0.13440.387939.990123.5913-37.4498
85.7553-1.35966.76322.1029-1.6979.5065-0.0915-0.15490.38390.3064-0.0263-0.11-0.2620.44420.08490.53790.0262-0.01230.4784-0.08130.403840.295951.8687-16.9264
93.542-0.148-2.40870.65470.00052.88980.08570.23840.2826-0.0280.0844-0.0494-0.3792-0.0395-0.18620.5993-0.0775-0.13760.31420.02630.451632.794678.205226.5735
101.60790.3354-0.72681.1131-1.09534.01930.14520.00730.24060.11460.1770.4092-0.4622-0.5667-0.31780.55570.1773-0.06440.46390.04960.62098.929664.6117-34.3796
113.31010.9753-1.01561.2392-0.54991.52740.0260.69740.6460.20760.35770.9094-0.1008-1.3033-0.38620.61240.1940.06591.66360.08821.0345-31.098665.711860.3335
129.45440.8371-1.5050.78650.30460.8475-0.05910.3277-0.51370.0314-0.08170.53480.3745-1.52040.1120.66-0.1781-0.08311.69110.06470.8441-25.079452.180651.6456
138.8672.5765-3.37086.4742-1.564.498-0.77851.25082.2658-0.50740.397-0.2016-1.38631.19360.23830.9376-0.4348-0.24941.26260.41011.10354.841377.3454-51.7978
142.17971.1051-1.10256.50170.16423.57160.2963-0.1036-0.00290.1957-0.3015-0.68820.18521.8446-0.0180.6083-0.0309-0.12881.43230.12590.616257.263458.1868-44.8236
精密化 TLSグループ
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'A' and resid 30 through 266)
2X-RAY DIFFRACTION2(chain 'B' and resid 279 through 390)
3X-RAY DIFFRACTION3(chain 'C' and resid 32 through 274)
4X-RAY DIFFRACTION4(chain 'D' and resid 280 through 390)
5X-RAY DIFFRACTION5(chain 'E' and resid 30 through 269)
6X-RAY DIFFRACTION6(chain 'F' and resid 279 through 390)
7X-RAY DIFFRACTION7(chain 'G' and resid 32 through 270)
8X-RAY DIFFRACTION8(chain 'H' and resid 282 through 390)
9X-RAY DIFFRACTION9(chain 'I' and resid 20 through 591)
10X-RAY DIFFRACTION10(chain 'J' and resid 20 through 546)
11X-RAY DIFFRACTION11(chain 'K' and resid 21 through 232)
12X-RAY DIFFRACTION12(chain 'L' and resid 20 through 240)
13X-RAY DIFFRACTION13(chain 'M' and resid 21 through 124)
14X-RAY DIFFRACTION14(chain 'N' and resid 20 through 137)

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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