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- PDB-8z4v: LH2 complex from Ectothiorhodospira haloalkaliphila at near-atomi... -

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基本情報

登録情報
データベース: PDB / ID: 8z4v
タイトルLH2 complex from Ectothiorhodospira haloalkaliphila at near-atomic resolution
要素
  • Light-harvesting protein B-800/850 alpha chain
  • Light-harvesting protein B:800-850 subunit beta
キーワードPHOTOSYNTHESIS / Light-harvesing / purple sulfur bacteria / cryo-EM
機能・相同性
機能・相同性情報


plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / : / metal ion binding / plasma membrane
類似検索 - 分子機能
Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain / Antenna complex, beta domain superfamily / Antenna complex alpha/beta subunit / Light-harvesting complex
類似検索 - ドメイン・相同性
: / BACTERIOCHLOROPHYLL A / Antenna complex alpha/beta subunit domain-containing protein / Light-harvesting protein B:800-850 subunit beta
類似検索 - 構成要素
生物種Ectothiorhodospira haloalkaliphila ATCC 51935 (紅色硫黄細菌)
手法電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 1.7 Å
データ登録者Burtseva, A.D. / Baymukhametov, T.N. / Popov, V.O. / Ashikhmin, A.A. / Boyko, K.M.
資金援助 ロシア, 1件
組織認可番号
Russian Science Foundation23-74-00062 ロシア
引用ジャーナル: Structure / : 2025
タイトル: Near-atomic cryo-EM structure of the light-harvesting complex LH2 from the sulfur purple bacterium Ectothiorhodospira haloalkaliphila.
著者: Anna D Burtseva / Timur N Baymukhametov / Maxim A Bolshakov / Zoya К Makhneva / Andrey V Mardanov / Andrey M Tsedilin / Huawei Zhang / Vladimir O Popov / Aleksandr A Ashikhmin / Konstantin M Boyko /
要旨: Bacteria with the simplest system for solar energy absorption and conversion use various types of light-harvesting complexes for these purposes. Light-harvesting complex 2 (LH2), an important ...Bacteria with the simplest system for solar energy absorption and conversion use various types of light-harvesting complexes for these purposes. Light-harvesting complex 2 (LH2), an important component of the bacterial photosynthetic apparatus, has been structurally well characterized among purple non-sulfur bacteria. In contrast, so far only one high-resolution LH2 structure from sulfur bacteria is known. Here, we report the near-atomic resolution cryoelectron microscopy (cryo-EM) structure of the LH2 complex from the purple sulfur bacterium Ectothiorhodospira haloalkaliphila, which allowed us to determine the predominant polypeptide composition of this complex and the identification of the most probable type of its carotenoid. Comparison of our structure with the only known LH2 complex from a sulfur bacterium revealed severe differences in the overall ring-like organization. Expanding the architectural universe of bacterial light-harvesting complexes, our results demonstrate that, as observed for non-sulfur bacteria, the LH2 complexes of sulfur bacteria may also exhibit various types of spatial organization.
履歴
登録2024年4月17日登録サイト: PDBJ / 処理サイト: PDBJ
改定 1.02025年1月1日Provider: repository / タイプ: Initial release
改定 1.12025年2月19日Group: Data collection / Database references / カテゴリ: citation / em_admin
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _em_admin.last_update

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構造の表示

構造ビューア分子:
MolmilJmol/JSmol

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集合体

登録構造単位
A: Light-harvesting protein B:800-850 subunit beta
C: Light-harvesting protein B-800/850 alpha chain
D: Light-harvesting protein B:800-850 subunit beta
E: Light-harvesting protein B-800/850 alpha chain
G: Light-harvesting protein B:800-850 subunit beta
H: Light-harvesting protein B-800/850 alpha chain
J: Light-harvesting protein B:800-850 subunit beta
K: Light-harvesting protein B-800/850 alpha chain
M: Light-harvesting protein B:800-850 subunit beta
N: Light-harvesting protein B-800/850 alpha chain
P: Light-harvesting protein B:800-850 subunit beta
Q: Light-harvesting protein B-800/850 alpha chain
S: Light-harvesting protein B:800-850 subunit beta
T: Light-harvesting protein B-800/850 alpha chain
V: Light-harvesting protein B:800-850 subunit beta
W: Light-harvesting protein B-800/850 alpha chain
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)133,00448
ポリマ-106,59316
非ポリマー26,41132
1,58588
1


  • 登録構造と同一
  • 登録者が定義した集合体
  • 根拠: gel filtration, not applicable
タイプ名称対称操作
identity operation1_5551
非結晶学的対称性 (NCS)NCSドメイン:
IDEns-ID詳細
11A
21D
32A
42G
53A
63J
74A
84M
95A
105P
116A
126S
137A
147V
158C
168E
179C
189H
1910C
2010K
2111C
2211N
2312C
2412Q
2513C
2613T
2714C
2814W
2915D
3015G
3116D
3216J
3317D
3417M
3518D
3618P
3719D
3819S
3920D
4020V
4121E
4221H
4322E
4422K
4523E
4623N
4724E
4824Q
4925E
5025T
5126E
5226W
5327G
5427J
5528G
5628M
5729G
5829P
5930G
6030S
6131G
6231V
6332H
6432K
6533H
6633N
6734H
6834Q
6935H
7035T
7136H
7236W
7337J
7437M
7538J
7638P
7739J
7839S
7940J
8040V
8141K
8241N
8342K
8442Q
8543K
8643T
8744K
8844W
8945M
9045P
9146M
9246S
9347M
9447V
9548N
9648Q
9749N
9849T
9950N
10050W
10151P
10251S
10352P
10452V
10553Q
10653T
10754Q
10854W
10955S
11055V
11156T
11256W

NCSドメイン領域:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNTYRTYRAA4 - 464 - 46
21ASNASNTYRTYRDC4 - 464 - 46
32ASNASNTYRTYRAA4 - 464 - 46
42ASNASNTYRTYRGE4 - 464 - 46
53ASNASNTYRTYRAA4 - 464 - 46
63ASNASNTYRTYRJG4 - 464 - 46
74ASNASNTYRTYRAA4 - 464 - 46
84ASNASNTYRTYRMI4 - 464 - 46
95ASNASNTYRTYRAA4 - 464 - 46
105ASNASNTYRTYRPK4 - 464 - 46
116ASNASNTYRTYRAA4 - 464 - 46
126ASNASNTYRTYRSM4 - 464 - 46
137ASNASNTYRTYRAA4 - 464 - 46
147ASNASNTYRTYRVO4 - 464 - 46
158GLUGLUPHEPHECB3 - 573 - 57
168GLUGLUPHEPHEED3 - 573 - 57
179GLUGLUPHEPHECB3 - 573 - 57
189GLUGLUPHEPHEHF3 - 573 - 57
1910GLUGLUPHEPHECB3 - 573 - 57
2010GLUGLUPHEPHEKH3 - 573 - 57
2111GLUGLUPHEPHECB3 - 573 - 57
2211GLUGLUPHEPHENJ3 - 573 - 57
2312GLUGLUPHEPHECB3 - 573 - 57
2412GLUGLUPHEPHEQL3 - 573 - 57
2513GLUGLUPHEPHECB3 - 573 - 57
2613GLUGLUPHEPHETN3 - 573 - 57
2714GLUGLUPHEPHECB3 - 573 - 57
2814GLUGLUPHEPHEWP3 - 573 - 57
2915ASNASNTYRTYRDC4 - 464 - 46
3015ASNASNTYRTYRGE4 - 464 - 46
3116ASNASNTYRTYRDC4 - 464 - 46
3216ASNASNTYRTYRJG4 - 464 - 46
3317ASNASNTYRTYRDC4 - 464 - 46
3417ASNASNTYRTYRMI4 - 464 - 46
3518ASNASNTYRTYRDC4 - 464 - 46
3618ASNASNTYRTYRPK4 - 464 - 46
3719ASNASNTYRTYRDC4 - 464 - 46
3819ASNASNTYRTYRSM4 - 464 - 46
3920ASNASNTYRTYRDC4 - 464 - 46
4020ASNASNTYRTYRVO4 - 464 - 46
4121GLUGLUPHEPHEED3 - 573 - 57
4221GLUGLUPHEPHEHF3 - 573 - 57
4322GLUGLUPHEPHEED3 - 573 - 57
4422GLUGLUPHEPHEKH3 - 573 - 57
4523GLUGLUPHEPHEED3 - 573 - 57
4623GLUGLUPHEPHENJ3 - 573 - 57
4724GLUGLUPHEPHEED3 - 573 - 57
4824GLUGLUPHEPHEQL3 - 573 - 57
4925GLUGLUPHEPHEED3 - 573 - 57
5025GLUGLUPHEPHETN3 - 573 - 57
5126GLUGLUPHEPHEED3 - 573 - 57
5226GLUGLUPHEPHEWP3 - 573 - 57
5327ASNASNTYRTYRGE4 - 464 - 46
5427ASNASNTYRTYRJG4 - 464 - 46
5528ASNASNTYRTYRGE4 - 464 - 46
5628ASNASNTYRTYRMI4 - 464 - 46
5729ASNASNTYRTYRGE4 - 464 - 46
5829ASNASNTYRTYRPK4 - 464 - 46
5930ASNASNTYRTYRGE4 - 464 - 46
6030ASNASNTYRTYRSM4 - 464 - 46
6131ASNASNTYRTYRGE4 - 464 - 46
6231ASNASNTYRTYRVO4 - 464 - 46
6332GLUGLUPHEPHEHF3 - 573 - 57
6432GLUGLUPHEPHEKH3 - 573 - 57
6533GLUGLUPHEPHEHF3 - 573 - 57
6633GLUGLUPHEPHENJ3 - 573 - 57
6734GLUGLUPHEPHEHF3 - 573 - 57
6834GLUGLUPHEPHEQL3 - 573 - 57
6935GLUGLUPHEPHEHF3 - 573 - 57
7035GLUGLUPHEPHETN3 - 573 - 57
7136GLUGLUPHEPHEHF3 - 573 - 57
7236GLUGLUPHEPHEWP3 - 573 - 57
7337ASNASNTYRTYRJG4 - 464 - 46
7437ASNASNTYRTYRMI4 - 464 - 46
7538ASNASNTYRTYRJG4 - 464 - 46
7638ASNASNTYRTYRPK4 - 464 - 46
7739ASNASNTYRTYRJG4 - 464 - 46
7839ASNASNTYRTYRSM4 - 464 - 46
7940ASNASNTYRTYRJG4 - 464 - 46
8040ASNASNTYRTYRVO4 - 464 - 46
8141GLUGLUPHEPHEKH3 - 573 - 57
8241GLUGLUPHEPHENJ3 - 573 - 57
8342GLUGLUPHEPHEKH3 - 573 - 57
8442GLUGLUPHEPHEQL3 - 573 - 57
8543GLUGLUPHEPHEKH3 - 573 - 57
8643GLUGLUPHEPHETN3 - 573 - 57
8744GLUGLUPHEPHEKH3 - 573 - 57
8844GLUGLUPHEPHEWP3 - 573 - 57
8945ASNASNTYRTYRMI4 - 464 - 46
9045ASNASNTYRTYRPK4 - 464 - 46
9146ASNASNTYRTYRMI4 - 464 - 46
9246ASNASNTYRTYRSM4 - 464 - 46
9347ASNASNTYRTYRMI4 - 464 - 46
9447ASNASNTYRTYRVO4 - 464 - 46
9548GLUGLUPHEPHENJ3 - 573 - 57
9648GLUGLUPHEPHEQL3 - 573 - 57
9749GLUGLUPHEPHENJ3 - 573 - 57
9849GLUGLUPHEPHETN3 - 573 - 57
9950GLUGLUPHEPHENJ3 - 573 - 57
10050GLUGLUPHEPHEWP3 - 573 - 57
10151ASNASNTYRTYRPK4 - 464 - 46
10251ASNASNTYRTYRSM4 - 464 - 46
10352ASNASNTYRTYRPK4 - 464 - 46
10452ASNASNTYRTYRVO4 - 464 - 46
10553GLUGLUPHEPHEQL3 - 573 - 57
10653GLUGLUPHEPHETN3 - 573 - 57
10754GLUGLUPHEPHEQL3 - 573 - 57
10854GLUGLUPHEPHEWP3 - 573 - 57
10955ASNASNTYRTYRSM4 - 464 - 46
11055ASNASNTYRTYRVO4 - 464 - 46
11156GLUGLUPHEPHETN3 - 573 - 57
11256GLUGLUPHEPHEWP3 - 573 - 57

NCSアンサンブル:
ID詳細
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36
19Local NCS retraints between domains: 37 38
20Local NCS retraints between domains: 39 40
21Local NCS retraints between domains: 41 42
22Local NCS retraints between domains: 43 44
23Local NCS retraints between domains: 45 46
24Local NCS retraints between domains: 47 48
25Local NCS retraints between domains: 49 50
26Local NCS retraints between domains: 51 52
27Local NCS retraints between domains: 53 54
28Local NCS retraints between domains: 55 56
29Local NCS retraints between domains: 57 58
30Local NCS retraints between domains: 59 60
31Local NCS retraints between domains: 61 62
32Local NCS retraints between domains: 63 64
33Local NCS retraints between domains: 65 66
34Local NCS retraints between domains: 67 68
35Local NCS retraints between domains: 69 70
36Local NCS retraints between domains: 71 72
37Local NCS retraints between domains: 73 74
38Local NCS retraints between domains: 75 76
39Local NCS retraints between domains: 77 78
40Local NCS retraints between domains: 79 80
41Local NCS retraints between domains: 81 82
42Local NCS retraints between domains: 83 84
43Local NCS retraints between domains: 85 86
44Local NCS retraints between domains: 87 88
45Local NCS retraints between domains: 89 90
46Local NCS retraints between domains: 91 92
47Local NCS retraints between domains: 93 94
48Local NCS retraints between domains: 95 96
49Local NCS retraints between domains: 97 98
50Local NCS retraints between domains: 99 100
51Local NCS retraints between domains: 101 102
52Local NCS retraints between domains: 103 104
53Local NCS retraints between domains: 105 106
54Local NCS retraints between domains: 107 108
55Local NCS retraints between domains: 109 110
56Local NCS retraints between domains: 111 112

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要素

#1: タンパク質・ペプチド
Light-harvesting protein B:800-850 subunit beta


分子量: 5468.237 Da / 分子数: 8 / 由来タイプ: 天然
由来: (天然) Ectothiorhodospira haloalkaliphila ATCC 51935 (紅色硫黄細菌)
参照: UniProt: W8KQR0
#2: タンパク質
Light-harvesting protein B-800/850 alpha chain / Antenna complex alpha/beta subunit domain-containing protein


分子量: 7855.903 Da / 分子数: 8 / 由来タイプ: 天然
由来: (天然) Ectothiorhodospira haloalkaliphila ATCC 51935 (紅色硫黄細菌)
参照: UniProt: W8KE12
#3: 化合物...
ChemComp-BCL / BACTERIOCHLOROPHYLL A


分子量: 911.504 Da / 分子数: 24 / 由来タイプ: 合成 / : C55H74MgN4O6 / タイプ: SUBJECT OF INVESTIGATION
#4: 化合物
ChemComp-A1L0S / Anhydrorhodovibrin / (6~{E},8~{E},10~{E},12~{E},14~{E},16~{E},18~{E},20~{E},22~{E},24~{E},26~{E},28~{E})-31-methoxy-2,6,10,14,19,23,27,31-octamethyl-dotriaconta-2,6,8,10,12,14,16,18,20,22,24,26,28-tridecaene


分子量: 566.899 Da / 分子数: 8 / 由来タイプ: 合成 / : C41H58O / タイプ: SUBJECT OF INVESTIGATION
#5: 水 ChemComp-HOH / water


分子量: 18.015 Da / 分子数: 88 / 由来タイプ: 天然 / : H2O
研究の焦点であるリガンドがあるかY
Has protein modificationN

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実験情報

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実験

実験手法: 電子顕微鏡法
EM実験試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法

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試料調製

構成要素名称: LH2 complex from Ectothiorhodospira haloalkaliphila / タイプ: COMPLEX / Entity ID: #1-#2 / 由来: NATURAL
分子量実験値: NO
由来(天然)生物種: Ectothiorhodospira haloalkaliphila (紅色硫黄細菌)
緩衝液pH: 8
試料包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES
試料支持詳細: The grids were stored under low vacuum conditions and were not specifically pretreated.
グリッドの材料: COPPER / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: Quantifoil R0.6/1
急速凍結装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 278 K

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電子顕微鏡撮影

実験機器
モデル: Titan Krios / 画像提供: FEI Company
顕微鏡モデル: FEI TITAN KRIOS / 詳細: Preliminary grid screening was performed manually.
電子銃電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM
電子レンズモード: BRIGHT FIELD / 倍率(公称値): 105000 X / 最大 デフォーカス(公称値): 1500 nm / 最小 デフォーカス(公称値): 600 nm / Cs: 0.01 mm / C2レンズ絞り径: 100 µm / アライメント法: ZEMLIN TABLEAU
試料ホルダ凍結剤: NITROGEN
試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER
撮影平均露光時間: 2.5 sec. / 電子線照射量: 52.5 e/Å2
フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k)
撮影したグリッド数: 1 / 実像数: 7346
電子光学装置エネルギーフィルター名称: GIF Bioquantum / エネルギーフィルタースリット幅: 15 eV
球面収差補正装置: Microscope was modified with a Cs corrector (CEOS GmbH, Germany).
画像スキャン: 5760 / : 4092

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解析

EMソフトウェア
ID名称バージョンカテゴリ
1Warp1.0.9粒子像選択
2SerialEM4.0.4画像取得
4Warp1.0.9CTF補正
7Coot0.9.8.92モデルフィッティング
9cryoSPARC4.4.1初期オイラー角割当
10cryoSPARC4.4.1最終オイラー角割当
12cryoSPARC4.4.13次元再構成
19Servalcat1.6.0モデル精密化
CTF補正タイプ: NONE
粒子像の選択選択した粒子像数: 1589688
対称性点対称性: C8 (8回回転対称)
3次元再構成解像度: 1.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 324434 / 対称性のタイプ: POINT
原子モデル構築プロトコル: AB INITIO MODEL / 空間: REAL
精密化解像度: 1.7→93.8 Å / Cor.coef. Fo:Fc: 0.892 / WRfactor Rwork: 0.239 / SU B: 1.442 / SU ML: 0.042 / Average fsc overall: 0.8484 / Average fsc work: 0.8484 / ESU R: 0.073 / 詳細: Hydrogens have been added in their riding positions
Rfactor反射数%反射
Rwork0.2387 281392 -
all0.239 --
Rfree--0 %
obs--100 %
溶媒の処理溶媒モデル: BABINET MODEL
原子変位パラメータBiso mean: 31.95 Å2
拘束条件
Refine-IDタイプDev idealDev ideal target
ELECTRON MICROSCOPYr_bond_refined_d0.0130.0148368
ELECTRON MICROSCOPYr_bond_other_d0.0250.0187912
ELECTRON MICROSCOPYr_angle_refined_deg4.1221.94711768
ELECTRON MICROSCOPYr_angle_other_deg1.4151.83817880
ELECTRON MICROSCOPYr_dihedral_angle_1_deg5.4125760
ELECTRON MICROSCOPYr_dihedral_angle_2_deg26.48317.143448
ELECTRON MICROSCOPYr_dihedral_angle_3_deg11.57215872
ELECTRON MICROSCOPYr_dihedral_angle_4_deg5.163158
ELECTRON MICROSCOPYr_chiral_restr0.090.21000
ELECTRON MICROSCOPYr_gen_planes_refined0.0120.029472
ELECTRON MICROSCOPYr_gen_planes_other0.0060.021992
ELECTRON MICROSCOPYr_nbd_refined0.2160.23696
ELECTRON MICROSCOPYr_symmetry_nbd_other0.1550.215634
ELECTRON MICROSCOPYr_nbtor_refined0.1830.27952
ELECTRON MICROSCOPYr_symmetry_nbtor_other0.0740.26858
ELECTRON MICROSCOPYr_xyhbond_nbd_refined0.1090.2288
ELECTRON MICROSCOPYr_mcbond_it2.2573.2513104
ELECTRON MICROSCOPYr_mcbond_other2.2583.253103
ELECTRON MICROSCOPYr_mcangle_it3.4364.8643848
ELECTRON MICROSCOPYr_mcangle_other3.4354.8653849
ELECTRON MICROSCOPYr_scbond_it2.6333.4875264
ELECTRON MICROSCOPYr_scbond_other2.6333.4875265
ELECTRON MICROSCOPYr_scangle_it4.0245.0627920
ELECTRON MICROSCOPYr_scangle_other4.0245.0637921
ELECTRON MICROSCOPYr_lrange_it6.65459.15431282
ELECTRON MICROSCOPYr_lrange_other6.65459.15531279
ELECTRON MICROSCOPYr_ncsr_local_group_100.052750
ELECTRON MICROSCOPYr_ncsr_local_group_200.052750
ELECTRON MICROSCOPYr_ncsr_local_group_300.052750
ELECTRON MICROSCOPYr_ncsr_local_group_400.052750
ELECTRON MICROSCOPYr_ncsr_local_group_500.052750
ELECTRON MICROSCOPYr_ncsr_local_group_600.052750
ELECTRON MICROSCOPYr_ncsr_local_group_700.052750
ELECTRON MICROSCOPYr_ncsr_local_group_800.053306
ELECTRON MICROSCOPYr_ncsr_local_group_900.053306
ELECTRON MICROSCOPYr_ncsr_local_group_100.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_110.0330.053304
ELECTRON MICROSCOPYr_ncsr_local_group_120.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_130.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_1400.053306
ELECTRON MICROSCOPYr_ncsr_local_group_1500.052750
ELECTRON MICROSCOPYr_ncsr_local_group_1600.052750
ELECTRON MICROSCOPYr_ncsr_local_group_1700.052750
ELECTRON MICROSCOPYr_ncsr_local_group_1800.052750
ELECTRON MICROSCOPYr_ncsr_local_group_1900.052750
ELECTRON MICROSCOPYr_ncsr_local_group_2000.052750
ELECTRON MICROSCOPYr_ncsr_local_group_2100.053306
ELECTRON MICROSCOPYr_ncsr_local_group_220.0310.053306
ELECTRON MICROSCOPYr_ncsr_local_group_230.0320.053304
ELECTRON MICROSCOPYr_ncsr_local_group_240.0310.053306
ELECTRON MICROSCOPYr_ncsr_local_group_250.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_2600.053308
ELECTRON MICROSCOPYr_ncsr_local_group_2700.052750
ELECTRON MICROSCOPYr_ncsr_local_group_2800.052750
ELECTRON MICROSCOPYr_ncsr_local_group_2900.052750
ELECTRON MICROSCOPYr_ncsr_local_group_3000.052750
ELECTRON MICROSCOPYr_ncsr_local_group_3100.052750
ELECTRON MICROSCOPYr_ncsr_local_group_320.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_330.0330.053304
ELECTRON MICROSCOPYr_ncsr_local_group_340.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_350.0310.053304
ELECTRON MICROSCOPYr_ncsr_local_group_3600.053306
ELECTRON MICROSCOPYr_ncsr_local_group_3700.052750
ELECTRON MICROSCOPYr_ncsr_local_group_3800.052750
ELECTRON MICROSCOPYr_ncsr_local_group_3900.052750
ELECTRON MICROSCOPYr_ncsr_local_group_4000.052750
ELECTRON MICROSCOPYr_ncsr_local_group_410.0020.053306
ELECTRON MICROSCOPYr_ncsr_local_group_4200.053308
ELECTRON MICROSCOPYr_ncsr_local_group_430.0010.053306
ELECTRON MICROSCOPYr_ncsr_local_group_440.0310.053306
ELECTRON MICROSCOPYr_ncsr_local_group_4500.052750
ELECTRON MICROSCOPYr_ncsr_local_group_4600.052750
ELECTRON MICROSCOPYr_ncsr_local_group_4700.052750
ELECTRON MICROSCOPYr_ncsr_local_group_480.0020.053306
ELECTRON MICROSCOPYr_ncsr_local_group_490.0020.053306
ELECTRON MICROSCOPYr_ncsr_local_group_500.0320.053304
ELECTRON MICROSCOPYr_ncsr_local_group_5100.052750
ELECTRON MICROSCOPYr_ncsr_local_group_5200.052750
ELECTRON MICROSCOPYr_ncsr_local_group_530.0010.053306
ELECTRON MICROSCOPYr_ncsr_local_group_540.0310.053306
ELECTRON MICROSCOPYr_ncsr_local_group_5500.052750
ELECTRON MICROSCOPYr_ncsr_local_group_560.0310.053304
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDタイプRms dev position (Å)Weight position
11AELECTRON MICROSCOPYLocal ncs0.000460.05006
12DELECTRON MICROSCOPYLocal ncs0.000460.05006
23AELECTRON MICROSCOPYLocal ncs0.000110.05006
24GELECTRON MICROSCOPYLocal ncs0.000110.05006
35AELECTRON MICROSCOPYLocal ncs0.000460.05006
36JELECTRON MICROSCOPYLocal ncs0.000460.05006
47AELECTRON MICROSCOPYLocal ncs0.000110.05006
48MELECTRON MICROSCOPYLocal ncs0.000110.05006
59AELECTRON MICROSCOPYLocal ncs0.000460.05006
510PELECTRON MICROSCOPYLocal ncs0.000460.05006
611AELECTRON MICROSCOPYLocal ncs0.000110.05006
612SELECTRON MICROSCOPYLocal ncs0.000110.05006
713AELECTRON MICROSCOPYLocal ncs0.000460.05006
714VELECTRON MICROSCOPYLocal ncs0.000460.05006
815CELECTRON MICROSCOPYLocal ncs0.000210.05009
816EELECTRON MICROSCOPYLocal ncs0.000210.05009
917CELECTRON MICROSCOPYLocal ncs7.0E-50.05009
918HELECTRON MICROSCOPYLocal ncs7.0E-50.05009
1019CELECTRON MICROSCOPYLocal ncs0.031240.05009
1020KELECTRON MICROSCOPYLocal ncs0.031240.05009
1121CELECTRON MICROSCOPYLocal ncs0.03250.05009
1122NELECTRON MICROSCOPYLocal ncs0.03250.05009
1223CELECTRON MICROSCOPYLocal ncs0.031260.05009
1224QELECTRON MICROSCOPYLocal ncs0.031260.05009
1325CELECTRON MICROSCOPYLocal ncs0.030730.05009
1326TELECTRON MICROSCOPYLocal ncs0.030730.05009
1427CELECTRON MICROSCOPYLocal ncs0.000210.05009
1428WELECTRON MICROSCOPYLocal ncs0.000210.05009
1529DELECTRON MICROSCOPYLocal ncs0.000460.05006
1530GELECTRON MICROSCOPYLocal ncs0.000460.05006
1631DELECTRON MICROSCOPYLocal ncs5.0E-50.05006
1632JELECTRON MICROSCOPYLocal ncs5.0E-50.05006
1733DELECTRON MICROSCOPYLocal ncs0.000450.05006
1734MELECTRON MICROSCOPYLocal ncs0.000450.05006
1835DELECTRON MICROSCOPYLocal ncs3.0E-50.05006
1836PELECTRON MICROSCOPYLocal ncs3.0E-50.05006
1937DELECTRON MICROSCOPYLocal ncs0.000460.05006
1938SELECTRON MICROSCOPYLocal ncs0.000460.05006
2039DELECTRON MICROSCOPYLocal ncs5.0E-50.05006
2040VELECTRON MICROSCOPYLocal ncs5.0E-50.05006
2141EELECTRON MICROSCOPYLocal ncs0.000210.05009
2142HELECTRON MICROSCOPYLocal ncs0.000210.05009
2243EELECTRON MICROSCOPYLocal ncs0.031210.05009
2244KELECTRON MICROSCOPYLocal ncs0.031210.05009
2345EELECTRON MICROSCOPYLocal ncs0.032480.05009
2346NELECTRON MICROSCOPYLocal ncs0.032480.05009
2447EELECTRON MICROSCOPYLocal ncs0.031230.05009
2448QELECTRON MICROSCOPYLocal ncs0.031230.05009
2549EELECTRON MICROSCOPYLocal ncs0.030720.05009
2550TELECTRON MICROSCOPYLocal ncs0.030720.05009
2651EELECTRON MICROSCOPYLocal ncs7.0E-50.05009
2652WELECTRON MICROSCOPYLocal ncs7.0E-50.05009
2753GELECTRON MICROSCOPYLocal ncs0.000450.05006
2754JELECTRON MICROSCOPYLocal ncs0.000450.05006
2855GELECTRON MICROSCOPYLocal ncs5.0E-50.05006
2856MELECTRON MICROSCOPYLocal ncs5.0E-50.05006
2957GELECTRON MICROSCOPYLocal ncs0.000450.05006
2958PELECTRON MICROSCOPYLocal ncs0.000450.05006
3059GELECTRON MICROSCOPYLocal ncs4.0E-50.05006
3060SELECTRON MICROSCOPYLocal ncs4.0E-50.05006
3161GELECTRON MICROSCOPYLocal ncs0.000450.05006
3162VELECTRON MICROSCOPYLocal ncs0.000450.05006
3263HELECTRON MICROSCOPYLocal ncs0.031240.05009
3264KELECTRON MICROSCOPYLocal ncs0.031240.05009
3365HELECTRON MICROSCOPYLocal ncs0.032510.05009
3366NELECTRON MICROSCOPYLocal ncs0.032510.05009
3467HELECTRON MICROSCOPYLocal ncs0.031270.05009
3468QELECTRON MICROSCOPYLocal ncs0.031270.05009
3569HELECTRON MICROSCOPYLocal ncs0.030740.05009
3570TELECTRON MICROSCOPYLocal ncs0.030740.05009
3671HELECTRON MICROSCOPYLocal ncs0.000210.05009
3672WELECTRON MICROSCOPYLocal ncs0.000210.05009
3773JELECTRON MICROSCOPYLocal ncs0.000440.05006
3774MELECTRON MICROSCOPYLocal ncs0.000440.05006
3875JELECTRON MICROSCOPYLocal ncs5.0E-50.05006
3876PELECTRON MICROSCOPYLocal ncs5.0E-50.05006
3977JELECTRON MICROSCOPYLocal ncs0.000450.05006
3978SELECTRON MICROSCOPYLocal ncs0.000450.05006
4079JELECTRON MICROSCOPYLocal ncs4.0E-50.05006
4080VELECTRON MICROSCOPYLocal ncs4.0E-50.05006
4181KELECTRON MICROSCOPYLocal ncs0.001790.05009
4182NELECTRON MICROSCOPYLocal ncs0.001790.05009
4283KELECTRON MICROSCOPYLocal ncs7.0E-50.05009
4284QELECTRON MICROSCOPYLocal ncs7.0E-50.05009
4385KELECTRON MICROSCOPYLocal ncs0.000750.05009
4386TELECTRON MICROSCOPYLocal ncs0.000750.05009
4487KELECTRON MICROSCOPYLocal ncs0.031210.05009
4488WELECTRON MICROSCOPYLocal ncs0.031210.05009
4589MELECTRON MICROSCOPYLocal ncs0.000440.05006
4590PELECTRON MICROSCOPYLocal ncs0.000440.05006
4691MELECTRON MICROSCOPYLocal ncs5.0E-50.05006
4692SELECTRON MICROSCOPYLocal ncs5.0E-50.05006
4793MELECTRON MICROSCOPYLocal ncs0.000450.05006
4794VELECTRON MICROSCOPYLocal ncs0.000450.05006
4895NELECTRON MICROSCOPYLocal ncs0.001780.05009
4896QELECTRON MICROSCOPYLocal ncs0.001780.05009
4997NELECTRON MICROSCOPYLocal ncs0.002460.05009
4998TELECTRON MICROSCOPYLocal ncs0.002460.05009
5099NELECTRON MICROSCOPYLocal ncs0.032480.05009
50100WELECTRON MICROSCOPYLocal ncs0.032480.05009
51101PELECTRON MICROSCOPYLocal ncs0.000450.05006
51102SELECTRON MICROSCOPYLocal ncs0.000450.05006
52103PELECTRON MICROSCOPYLocal ncs5.0E-50.05006
52104VELECTRON MICROSCOPYLocal ncs5.0E-50.05006
53105QELECTRON MICROSCOPYLocal ncs0.000760.05009
53106TELECTRON MICROSCOPYLocal ncs0.000760.05009
54107QELECTRON MICROSCOPYLocal ncs0.031240.05009
54108WELECTRON MICROSCOPYLocal ncs0.031240.05009
55109SELECTRON MICROSCOPYLocal ncs0.000450.05006
55110VELECTRON MICROSCOPYLocal ncs0.000450.05006
56111TELECTRON MICROSCOPYLocal ncs0.030720.05009
56112WELECTRON MICROSCOPYLocal ncs0.030720.05009
LS精密化 シェル

Refine-ID: ELECTRON MICROSCOPY / Num. reflection Rfree: _ / Total num. of bins used: 20 / % reflection obs: 100 %

解像度 (Å)Rfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc workWRfactor Rwork
1.7-1.7441.035208391.035208390.4641.035
1.744-1.7920.779203980.779203980.5640.779
1.792-1.8440.643196330.643196330.6810.643
1.844-1.9010.595190610.595190610.7540.595
1.901-1.9630.515186470.515186470.8310.515
1.963-2.0320.335179220.335179220.9010.335
2.032-2.1080.245173390.245173390.9290.245
2.108-2.1950.212166230.212166230.9490.212
2.195-2.2920.203160820.203160820.9610.203
2.292-2.4040.195153250.195153250.9660.195
2.404-2.5340.182145160.182145160.9670.182
2.534-2.6870.19137640.19137640.9640.19
2.687-2.8730.178128990.178128990.9680.178
2.873-3.1030.163121260.163121260.9710.163
3.103-3.3980.165110000.165110000.9720.165
3.398-3.7990.154100090.154100090.9750.154
3.799-4.3850.16188120.16188120.9710.161
4.385-5.3680.19674340.19674340.9590.196
5.368-7.5790.29157740.29157740.9210.291
7.579-93.80.4631890.4631890.9490.46

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万見について

-
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