1D7Q
HUMAN TRANSLATION INITIATION FACTOR EIF1A
SOLUTION NMR
NMR Experiment | ||||||||
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Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
1 | 3D_13C-SEPARATED_NOESY | 0.8MM U-13C,15N EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA | 500mM | 7.5 | 1 atm | 298 | ||
2 | 3D_15N-SEPARATED_NOESY | 0.5MM U-15N EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA | 500mM | 7.5 | 1 atm | 298 | ||
3 | 2D NOESY | 1.2MM EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA | 500mM | 7.5 | 1 atm | 298 |
NMR Spectrometer Information | |||
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Spectrometer | Manufacturer | Model | Field Strength |
1 | Varian | INOVA | 750 |
2 | Varian | INOVA | 500 |
3 | Varian | UNITY | 500 |
NMR Refinement | ||
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Method | Details | Software |
STRUCTURES WERE CALCULATED USING SIMULATED ANNEALING/MOLECULAR DYNAMICS FROM AN EXTENDED CONFORMATION WITH RANDOM PHI/PSI ANGLES. | 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. | VNMR |
NMR Ensemble Information | |
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Conformer Selection Criteria | structures with the least restraint violations |
Conformers Calculated Total Number | 50 |
Conformers Submitted Total Number | 20 |
Representative Model | 8 (lowest energy) |
Additional NMR Experimental Information | |
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Details | 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. |
Computation: NMR Software | ||||
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# | Classification | Version | Software Name | Author |
1 | collection | VNMR | 6.1 | VARIAN |
2 | processing | Felix | 98 | BIOSYM |
3 | data analysis | XEASY | 1.2 | C. BARTELS, T. XIA, M. BILLETER, P. GUNTERT, AND K. WUTHRICH |
4 | structure solution | X-PLOR | 3.851 | A.T. BRUNGER |
5 | data analysis | TALOS | 1.0 | G. CORNILESCU, F. DELAGLIO, AND A. BAX |
6 | refinement | X-PLOR | 3.851 | A.T. BRUNGER |