分子量: 2123.481 Da / 分子数: 1 / 断片: N-TERMINAL FUSION PEPTIDE (RESIDUES 519-541) / 変異: C-TERMINUS HAS BEEN AMIDATED / 由来タイプ: 合成 詳細: The sequence of this peptide occurs naturally in human immunodeficiency virus glycoprotein 41. 参照: UniProt: P03377
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実験情報
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実験
実験
手法: 赤外分光
NMR実験
タイプ: 13-C isotope enhanced FTIR
NMR実験の詳細
Text: The coordinates in this entry were generated from 13-C induced spectral shifts which give residue-specific secondary structure information.
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試料調製
結晶
解説: This structure was determined by means of 13C-enhanced Fourier Transform Infrared Spectroscopy (FTIR). Data set consists of 17 conformers derived from simulated annealing with constraints from FTIR.
詳細
内容: THIS STRUCTURE WAS DETERMINED USING 13-C ISOTOPE ENHANCED FTIR SPECTROSCOPY ON A FAMILY OF SELECTIVELY LABELED CHEMICALLY SYNTHESIZED PEPTIDES. 13-C CARBONYL LABELS INCLUDED RESIDUES ...内容: THIS STRUCTURE WAS DETERMINED USING 13-C ISOTOPE ENHANCED FTIR SPECTROSCOPY ON A FAMILY OF SELECTIVELY LABELED CHEMICALLY SYNTHESIZED PEPTIDES. 13-C CARBONYL LABELS INCLUDED RESIDUES 519,521,523,524,525,526,527,528,529,530,531,532,533,534,538,539. 溶媒系: 70% hexafluoroisopropanol (HFIP), 29.9% water, 0.1% formic acid (v/v)
試料状態
イオン強度: 0 / pH: 7.0 / 圧: 1 atm / 温度: 298
結晶化
*PLUS
手法: 赤外分光
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データ収集
NMRスペクトロメーター
タイプ: Mattson FTIR Research Series / 製造業者: Mattson FTIR / モデル: Research Series / 磁場強度: 0 MHz
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解析
NMR software
名称
バージョン
開発者
分類
Winfirst
FTIRcurvefittingsoftware
Kauppineetal.
データ解析
DISCOVER
2.9.7
MolecularSimulations, Inc. (SanDiego, CA)
精密化
精密化
手法: molecular dynamics, simulated annealing / ソフトェア番号: 1 詳細: Molecular dynamics (simulated annealing) was used to generate an ensemble of conformers consistent with the FTIR data.