- PDB-4h3w: Crystal structure of a putative secreted protein (BDI_1231) from ... -
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IDまたはキーワード:
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基本情報
登録情報
データベース: PDB / ID: 4h3w
タイトル
Crystal structure of a putative secreted protein (BDI_1231) from Parabacteroides distasonis ATCC 8503 at 2.00 A resolution
要素
hypothetical protein
キーワード
Structural Genomics / Unknown Function / two beta barrel domains / secreted protein / ORFan / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
機能・相同性
Jelly Rolls - #1260 / Protein of unknown function (DUF4621), C-terminal domain / Protein of unknown function DUF4621 / Protein of unknown function (DUF4621) / Hypothetical Protein Tm1070; Chain: A / Jelly Rolls / Sandwich / Mainly Beta / DUF4621 domain-containing protein
1. THE CONSTRUCT (RESIDUES 24-352) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG ...1. THE CONSTRUCT (RESIDUES 24-352) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. 2. THE PROTEIN WAS REDUCTIVELY METHYLATED PRIOR TO CRYSTALLIZATION.
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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: 2.58 Å3/Da / 溶媒含有率: 52.24 %
結晶化
温度: 277 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 8.5 詳細: 30.0% polyethylene glycol 4000, 0.2M magnesium chloride, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
モノクロメーター: single crystal Si(111) bent / プロトコル: SAD / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.97885 Å / 相対比: 1
反射
解像度: 1.87→48.317 Å / Num. obs: 53817 / % possible obs: 87.2 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 30.595 Å2 / Rmerge(I) obs: 0.059 / Net I/σ(I): 11.4
反射 シェル
Diffraction-ID: 1
解像度 (Å)
最高解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
1.87-1.94
0.57
1.8
13764
3971
61.5
1.94-2.01
0.421
2.5
18617
5095
91.8
2.01-2.11
0.271
3.9
22778
6262
93
2.11-2.22
0.215
4.8
20391
5569
92
2.22-2.36
0.155
6.8
20208
5563
90.1
2.36-2.54
0.116
9.1
21096
5706
93.5
2.54-2.79
0.088
12.2
19498
5339
88.1
2.79-3.19
0.057
18.5
20446
5572
90.5
3.19-4.02
0.04
24.5
19209
5284
85.3
4.02
0.038
28.4
19668
5456
87.7
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位相決定
位相決定
手法: 単波長異常分散
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解析
ソフトウェア
名称
バージョン
分類
NB
MolProbity
3beta29
モデル構築
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
XSCALE
March15, 2012
データスケーリング
REFMAC
5.7.0029
精密化
XDS
データ削減
SHELXD
位相決定
精密化
構造決定の手法: 単波長異常分散 / 解像度: 1.87→48.317 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.944 / Occupancy max: 1 / Occupancy min: 0.33 / SU B: 7.939 / SU ML: 0.116 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.169 / ESU R Free: 0.155 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED ...詳細: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3.SOLVENT WAS EXCLUDED FROM TLS REFINEMENT. 4. THE PROTEIN WAS SUBJECTED TO REDUCTIVE METHYLATION PRIOR TO CRYSTALLIZATION LYSINES HAVE BEEN MODELED AS N-DIMETHYL-LYSINE (MLY).5. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 6. THE NOMINAL RESOLUTION IS 2.00 ANGSTROMS WITH 7826 OBSERVED REFLECTIONS BETWEEN 2.00-1.87 (71.2% COMPLETE FOR THIS SHELL) INCLUDED IN THE REFINEMENT.
Rfactor
反射数
%反射
Selection details
Rfree
0.2382
2703
5.1 %
RANDOM
Rwork
0.1963
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obs
0.1984
53272
86.62 %
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溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: BABINET MODEL WITH MASK