2LOS | pdb_00002los

Backbone structure of human membrane protein TMEM14C


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
12D 1H-15N HSQC15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
23D HNCO13C,15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
33D HNCA13C,15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
43D HNCACB13C,15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
53D HN(CO)CA13C,15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
63D 1H-15N NOESY15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
73D 13C-15N HSQC-NOESY-HSQC13C,15N-TMEM14C, 20 mM MES-BisTris, 2 % LMPG, 0.5 mM DSS95% H2O/5% D2O406.0ambient310
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX700
NMR Refinement
MethodDetailsSoftware
torsion angle dynamicsTopSpin
NMR Ensemble Information
Conformer Selection Criteriatarget function
Conformers Calculated Total Number200
Conformers Submitted Total Number20
Representative Model1 (fewest violations)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1collectionTopSpinBruker Biospin
2processingTopSpinBruker Biospin
3processingNMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
4chemical shift assignmentSparkyGoddard
5chemical shift assignmentCARAKeller and Wuthrich
6data analysisCARAKeller and Wuthrich
7structure solutionCYANAGuntert, Mumenthaler and Wuthrich
8structure visualizationMOLMOLKoradi, Billeter and Wuthrich
9structure analysisMOLMOLKoradi, Billeter and Wuthrich
10refinementCYANAGuntert, Mumenthaler and Wuthrich