: / Protein of unknown function DUF903 / Bacterial protein of unknown function (DUF903) / SH3 type barrels. - #100 / LSM domain superfamily / SH3 type barrels. / Prokaryotic membrane lipoprotein lipid attachment site profile. / Roll / Mainly Beta 類似検索 - ドメイン・相同性
Text: STRUCTURE DETERMINED BY TRIPLE RESONANCE NMR SPECTROSCOPY. MONOMER IN SOLUTION BY NMR TC = 8.2 +/- 1.0 NS (1D T1/T1RHO +/- FIT STD). POSSIBLE CIS PEPTIDE RES. 20K-21P. COULD NOT BE ANAMBIGUOSLY ...Text: STRUCTURE DETERMINED BY TRIPLE RESONANCE NMR SPECTROSCOPY. MONOMER IN SOLUTION BY NMR TC = 8.2 +/- 1.0 NS (1D T1/T1RHO +/- FIT STD). POSSIBLE CIS PEPTIDE RES. 20K-21P. COULD NOT BE ANAMBIGUOSLY ESTABLISHED DUE TO SPECTRAL OVERLAP. COORDINATES REPORTED FROM RESIDUE 4 TO 53 SECTION BASED ON ORDER PARAMETER. MANUAL RESONANCE ASSIGNMENT. 13C AND 15N EDITED NOESY WERE WERE ASSIGNED USING AUTOSTRUCTURE. DIHEDRAL ANGLE RESTRAINTS DETERMINED BY HYPER AND TALOS. ASSIGNMENT STATS (EXCLUDING C-TERM TAG): BACKBONE 80.4%, SIDECHAIN 77.7%, AROMATIC (SC) 100%, VL METHYL STEREOSP. 80%. STRUCTURE QUALITY FACTOR PSVS 1.3: ORDERED RESIDUES RANGES B-STRAND (14-16, 6-9, 47-49, 22-24, 29-33, 39-43, 65, 50-51, 56-57) [S(PHI)+S(PSI)]>1.8. RMSD 0.6 BB, 1.1 ALL HEAVY ATOMS. RAMA: 84.1% MOST FAV, 13.6% ADDTL.ALL.,2.2% GEN. ALL.,0.1% DISALL. PROCHECK (PSI-PHI): 0.75/-2.64 (RAW/Z), PROCHECK (ALL): -0.6/-3.55 (RAW/Z), MOLPROBITY CLASH: 23.61/- 2.53 (RAW/Z). RPF SCORES ALL ASSIGNED RESIDUES (FIT OF NOESY PEAKLISTS TO STRUCTURE): RECALL: 0.925, PRECISION: 0.916, F-MEASURE: 0.921, DP-SCORE: 0.731. MONOMER BY LIGHT SCATTERING
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試料調製
詳細
内容: 1.17 mM [U-100% 13C; U-100% 15N] ER382A, 10 mM DTT, 5 mM CaCl2, 0.1 M NaCl, 20 mM MES, 0.02 % sodium azide
試料
濃度 (mg/ml)
構成要素
Isotopic labeling
Solution-ID
1.17mM
ER382A
[U-100% 13C; U-100% 15N]
1
10mM
DTT
1
5mM
CaCl2
1
0.1M
NaCl
1
20mM
MES
1
0.02 %
sodiumazide
1
試料状態
イオン強度: 0.1 / pH: 6.5 / 圧: AMBIENT / 温度: 293 K
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NMR測定
放射
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M
放射波長
相対比: 1
NMRスペクトロメーター
タイプ: Bruker AVANCE / 製造業者: Bruker / モデル: AVANCE / 磁場強度: 600 MHz
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解析
NMR software
名称
バージョン
開発者
分類
CNSSOLVE
1.1
BRUNGER, et. al.
精密化
X-PLOR
2.11.2
CLOREet. al.
精密化
PROCHECK NMR
3.51
LASKOWSKI, MACARTHUR
精密化
MolProbity
3.01
LOVELL, RICHARDSONET. AL.
精密化
QUEEN
1.1
NABUURS, VUISTER
精密化
PSVS
1.3
BHATTACHARYA, MONTELIONE
精密化
AutoStructure
2.1.1
構造決定
NMRPipe
構造決定
Sparky
構造決定
MOLMOL
構造決定
CNS
構造決定
PROCHECK
構造決定
XPLOR-NIH
構造決定
DIANA
構造決定
QUEEN
1.1
構造決定
精密化
手法: simulated annealing / ソフトェア番号: 1 詳細: NOESY ASSIGNMENT MADE WITH ITERATIVE METHOD USING CNS, HYPER (DIHEDRAL) AND DYANA FOLLOWED BY NIH- XPLOR FOR SIMMULATED ANNEALING MD. CONVERGED STRUCTURES WERE FURTHER MINIMIZED USING CNS IN ...詳細: NOESY ASSIGNMENT MADE WITH ITERATIVE METHOD USING CNS, HYPER (DIHEDRAL) AND DYANA FOLLOWED BY NIH- XPLOR FOR SIMMULATED ANNEALING MD. CONVERGED STRUCTURES WERE FURTHER MINIMIZED USING CNS IN EXPLICIT H2O SHELL (NILGES PROTOCOL). FULL LENGTH SEQUENCE WAS CARRIED THROUGH THE REFINEMENT PROTOCOL. COORDINATES FROM DISORDERED REGIONS, INCLUDING HEXHIS TAG, WERE NOT REPORTED. STRUCTURE IS BASED ON 439 CONSTRAINTS (216 LONG RANGE), 43 DIHEDRAL AND 20 H-BOND.
代表構造
選択基準: lowest energy
NMRアンサンブル
コンフォーマー選択の基準: target function / 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 20