2LOR | pdb_00002lor

Backbone structure of human membrane protein TMEM141


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
12D 1H-15N HSQC15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
23D HNCA13C,15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
33D HNCACB13C,15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
43D HN(CO)CA13C,15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
53D 1H-15N NOESY15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
63D HNCA13C,15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
73D HN(CO)CA13C,15N-TMEM141, 20 mM MES-Bis-TRIS, 3 % LMPG95% H2O/5% D2O606.0ambient310
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
2processingNMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
3processingNMRDrawDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
4data analysisNMRDrawDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
5structure visualizationMOLMOLKoradi, Billeter and Wuthrich
6structure analysisMOLMOLKoradi, Billeter and Wuthrich
7chemical shift assignmentSparkyGoddard
8data analysisSparkyGoddard
9structure solutionCYANAGuntert, Mumenthaler and Wuthrich
10refinementCYANAGuntert, Mumenthaler and Wuthrich