BMRB Entry 17039

Title:
Solution NMR Structure of putative cell surface protein MA_4588 (272-376 domain) from Methanosarcina acetivorans, Northeast Structural Genomics Consortium Target MvR254A
Deposition date:
2010-06-30
Original release date:
2012-08-02
Authors:
Cort, John; Lee, D.; Ciccosanti, C.; Janjua, H.; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Ramelot, T.; Kennedy, M.
Citation:

Citation: Cort, John; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; KENNEDY, M.. "Northeast Structural Genomics Consortium Target MvR254A"  To be published ., .-..

Assembly members:

Assembly members:
MvR254A, polymer, 114 residues, 12299.430 Da.

Natural source:

Natural source:   Common Name: Methanosarcina acetivorans   Taxonomy ID: 2214   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanosarcina acetivorans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Data typeCount
13C chemical shifts458
15N chemical shifts119
1H chemical shifts736

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MvR254A1

Entities:

Entity 1, MvR254A 114 residues - 12299.430 Da.

Residue 2 corresponds with residue 272 of the predicted protein

1   METILEPROASPLEUVALPROVALSERLEU
2   THRPROVALTHRVALVALPROASNTHRVAL
3   ASNTHRMETTHRALATHRILEGLUASNGLN
4   GLYASNLYSASPSERTHRSERPHEASNVAL
5   SERLEULEUVALASPGLYILEVALVALASP
6   THRGLNTHRVALTHRSERLEUGLUSERGLU
7   ASNSERTHRASNVALASPPHEHISTRPTHR
8   LEUASPGLYTHRALAASNSERTYRTHRLEU
9   THRVALASNVALASPPROGLUASNALAVAL
10   ASNGLUGLYASNGLUSERASNASNTHRLEU
11   THRALALEUVALGLYTHRLEUGLUHISHIS
12   HISHISHISHIS

Samples:

sample_1: MvR254A, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; H2O 95%; D2O 5%

sample_2: MvR254A, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; D2O 100%

sample_3: MvR254A, [5% biosynthetically-directed 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aliph NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D 1H-13C-13C-1H HMQC-NOESY-HMQCsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks