- PDB-3oqq: Crystal structure of a Putative lipoprotein (BACOVA_00967) from B... -
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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: 3oqq
タイトル
Crystal structure of a Putative lipoprotein (BACOVA_00967) from Bacteroides ovatus at 2.08 A resolution
要素
Putative lipoprotein
キーワード
Structural Genomics / Unknown Function / EXTRACELLULAR PROTEIN / JOINT CENTER FOR STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI-2
機能・相同性
LruC domain / Domain of unknown function DUF4841 / Domain of unknown function DUF4842 / Domain of unknown function (DUF4841) / Domain of unknown function (DUF4842) / metal ion binding / ACETATE ION / TRIETHYLENE GLYCOL / Uncharacterized protein
ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
THE CONSTRUCT (RESIDUES 23-456) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 23-456) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
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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: 2
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試料調製
結晶
ID
マシュー密度 (Å3/Da)
溶媒含有率 (%)
解説
1
2.48
50.5
THREE-WAVELENGTH MAD PHASES WERE OBTAINED FROM TWO CRYSTALS. THE PEAK DATA WERE FROM ONE CRYSTAL DIFFRACTING TO 2.08 A. THE INFLECTION AND REMOTE DATA WERE FROM ANOTHER CRYSTAL DIFFRACTING TO 2.6 A. THE PEAK DATA (FROM THE HIGHER RESOLUTION CRYSTAL) WERE USED FOR REFINEMENT.
2
結晶化
温度 (K)
Crystal-ID
手法
pH
詳細
277
1
蒸気拡散法, シッティングドロップ法
8
0.2M Ca(OAc)2, 20.0% PEG-1000, 0.1M Imidazole pH 8.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K, VAPOR DIFFUSION, SITTING DROP
277
2
蒸気拡散法, シッティングドロップ法
8
0.2M Ca(OAc)2, 20.0% PEG-1000, 0.1M Imidazole pH 8.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K, VAPOR DIFFUSION, SITTING DROP
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データ収集
回折
ID
平均測定温度 (K)
Crystal-ID
1
100
1
2
100
2
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
BL9-2
1
0.97903
シンクロトロン
SSRL
BL9-2
2
0.97918,0.91837
検出器
タイプ
ID
検出器
日付
詳細
MARMOSAIC 325 mm CCD
1
CCD
2010年7月22日
Flatcollimatingmirror, toroidfocusingmirror
MARMOSAIC 325 mm CCD
2
CCD
2010年7月22日
Flatcollimatingmirror, toroidfocusingmirror
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
1
Doublecrystalmonochromator
MAD
M
x-ray
1
2
Doublecrystalmonochromator
MAD
M
x-ray
2
放射波長
ID
波長 (Å)
相対比
1
0.97903
1
2
0.97918
1
3
0.91837
1
反射
解像度: 2.08→44.623 Å / Num. obs: 28606 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / 冗長度: 3.8 % / Biso Wilson estimate: 27.02 Å2 / Rmerge(I) obs: 0.109 / Net I/σ(I): 9.31
反射 シェル
Diffraction-ID: 1,2
解像度 (Å)
冗長度 (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
2.08-2.15
3.7
0.567
2.1
10236
2722
99.9
2.15-2.24
3.8
0.441
2.7
11288
2995
99.5
2.24-2.34
3.8
0.382
3.2
10326
2772
99.5
2.34-2.47
3.8
0.324
3.8
11427
3016
99.5
2.47-2.62
3.8
0.264
4.6
10395
2749
100
2.62-2.82
3.8
0.197
6.1
10711
2821
99.6
2.82-3.1
3.8
0.13
9
10811
2847
99.6
3.1-3.55
3.7
0.071
14.9
10893
2884
99.4
3.55-4.47
3.8
0.048
21.2
10788
2874
99.2
4.47-44.6
3.8
0.046
25
10884
2921
99.3
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位相決定
位相決定
手法: 多波長異常分散
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解析
ソフトウェア
名称
バージョン
分類
NB
SHELX
位相決定
BUSTER-TNT
BUSTER2.8.0
精密化
XSCALE
dataprocessing
PDB_EXTRACT
3.1
データ抽出
XDS
データ削減
XSCALE
データスケーリング
SHELXD
位相決定
autoSHARP
位相決定
BUSTER
2.8.0
精密化
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.08→25.75 Å / Cor.coef. Fo:Fc: 0.9493 / Cor.coef. Fo:Fc free: 0.9287 / Occupancy max: 1 / Occupancy min: 0.5 / 交差検証法: THROUGHOUT / σ(F): 0 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. CALCIUM (CA), ACETATE, POLYETHYLENE GLYCOL FRAGMENTS (PGE) MODELED ARE PRESENT PROTEIN/CRYSTALLIZATION/CRYO BUFFER. 4. RAMACHANDRAN OUTLIERS (A66 AND A210) ARE SUPPORTED BY DENSITY. 5. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT.
Rfactor
反射数
%反射
Selection details
Rfree
0.2039
1449
5.07 %
RANDOM
Rwork
0.161
-
-
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obs
0.1633
28586
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原子変位パラメータ
Biso mean: 31.81 Å2
Baniso -1
Baniso -2
Baniso -3
1-
5.1771 Å2
0 Å2
-3.8575 Å2
2-
-
-3.7928 Å2
0 Å2
3-
-
-
-1.3843 Å2
精密化ステップ
サイクル: LAST / 解像度: 2.08→25.75 Å
タンパク質
核酸
リガンド
溶媒
全体
原子数
3223
0
25
301
3549
拘束条件
Refine-ID
タイプ
Dev ideal
数
Restraint function
Weight
X-RAY DIFFRACTION
t_bond_d
0.01
3328
HARMONIC
2
X-RAY DIFFRACTION
t_angle_deg
1.08
4517
HARMONIC
2
X-RAY DIFFRACTION
t_dihedral_angle_d
1539
SINUSOIDAL
2
X-RAY DIFFRACTION
t_incorr_chiral_ct
X-RAY DIFFRACTION
t_pseud_angle
X-RAY DIFFRACTION
t_trig_c_planes
95
HARMONIC
2
X-RAY DIFFRACTION
t_gen_planes
478
HARMONIC
5
X-RAY DIFFRACTION
t_it
3328
HARMONIC
20
X-RAY DIFFRACTION
t_nbd
0
SEMIHARMONIC
5
X-RAY DIFFRACTION
t_omega_torsion
3.93
X-RAY DIFFRACTION
t_other_torsion
2.91
X-RAY DIFFRACTION
t_improper_torsion
X-RAY DIFFRACTION
t_chiral_improper_torsion
431
SEMIHARMONIC
5
X-RAY DIFFRACTION
t_sum_occupancies
X-RAY DIFFRACTION
t_utility_distance
X-RAY DIFFRACTION
t_utility_angle
X-RAY DIFFRACTION
t_utility_torsion
X-RAY DIFFRACTION
t_ideal_dist_contact
4072
SEMIHARMONIC
4
LS精密化 シェル
解像度: 2.08→2.16 Å / Total num. of bins used: 14
Rfactor
反射数
%反射
Rfree
0.2556
130
4.32 %
Rwork
0.1848
2881
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all
0.1876
3011
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精密化 TLS
手法: refined / Origin x: 11.7092 Å / Origin y: -0.349 Å / Origin z: 25.9619 Å