Text: THE PROTEIN WAS ASSIGNED FROM THE TRIPLE RESONANCE EXPERIMENTS HNCA, HN(CO)CA, HNCO, HN(CA)CO, CBCA(CO)NH, HBHA(CBCACO)NH, H(CCCO)NH, (H)C(CCO)NH, AND HCCH- TOCSY. VAL AND LEU METHYL GROUPS ...Text: THE PROTEIN WAS ASSIGNED FROM THE TRIPLE RESONANCE EXPERIMENTS HNCA, HN(CO)CA, HNCO, HN(CA)CO, CBCA(CO)NH, HBHA(CBCACO)NH, H(CCCO)NH, (H)C(CCO)NH, AND HCCH- TOCSY. VAL AND LEU METHYL GROUPS WERE STEREOSPECIFICALLY ASSIGNED FROM ANALYSIS OF MULTIPLET COUPLINGS IN AN HSQC OF 10% 13C-LABELED PROTEIN. BACKBONE DIHEDRAL ANGLES WERE ESTIMATED USING THE PROGRAM TALOS AND BACKBONE HETERONUCLEAR CHEMICAL SHIFTS.
C. BARTELS, T. XIA, M. BILLETER, P. GUNTERT, ANDK. WUTHRICH
データ解析
X-PLOR
3.851
A.T. BRUNGER
構造決定
TALOS
1
G. CORNILESCU, F. DELAGLIO, ANDA. BAX
データ解析
X-PLOR
3.851
A.T. BRUNGER
精密化
精密化
手法: STRUCTURES WERE CALCULATED USING SIMULATED ANNEALING, MOLECULAR DYNAMICS FROM AN EXTENDED CONFORMATION WITH RANDOM PHI, PSI ANGLES. ソフトェア番号: 1 詳細: CALCULATIONS WERE RESTRAINED WITH THE FOLLOWING NMR DATA. NOE DISTANCE RESTRAINTS INTRA-RESIDUE 607 INTER-RESIDUE SEQUENTIAL (IJ=1) 266 INTER-RESIDUE MEDIUM (IJ 4) 342 HYDROGENS BONDS: ...詳細: CALCULATIONS WERE RESTRAINED WITH THE FOLLOWING NMR DATA. NOE DISTANCE RESTRAINTS INTRA-RESIDUE 607 INTER-RESIDUE SEQUENTIAL (IJ=1) 266 INTER-RESIDUE MEDIUM (IJ <= 4) 105 INTER-RESIDUE LONG (IJ > 4) 342 HYDROGENS BONDS: PROTEIN BACKBONE 40 DIHEDRAL ANGLES: PHI 65 PSI 65 NO NOE VIOLATIONS >0.3 A IN FINAL STRUCTURES. RMS DEVIATIONS OF THE ENSEMBLE SUPERPOSITION TO THE AVERAGE STRUCTURE ARE: BACKBONE 39-131 0.57 A SECONDARY STRUCTURE 0.23 A HEAVY ATOMS 39-131 1.17 A SECONDARY STRUCTURE 0.72 A BOND LENGTHS 0.0016 A BOND ANGLES 0.345 DEGREE IMPROPER ANGLES 0.259 DEGREE. NOTE THAT RESIDUES 1-38 AND 132-143 HAD NO LONG RANGE NOES AND ARE DISORDERED IN THE CALCULATED STRUCTURES.
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: structures with the least restraint violations 計算したコンフォーマーの数: 50 / 登録したコンフォーマーの数: 20