BMRB Entry 16255

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16255
MolProbity Validation Chart

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Title:
Solution Structure Of Protein Nmul_A0922 From Nitrosospira multiformis. Northeast Structural Genomics Consortium Target Hr5524a.
Deposition date:
2009-04-13
Original release date:
2009-05-20
Authors:
Wu, Yibing; Mills, Jeffrey; Wang, Dongyan; Ciccosanti, Colleen; Sukumaran, Dinesh; Jiang, Mei; Garcia, Erwin; Nair, R.; Rost, B.; Swapna, G.V.T; Acton, T.B.; Xiao, R.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas
Citation:

Citation: Wu, Yibing; Mills, Jeffrey; Wang, Dongyan; Ciccosanti, Colleen; Sukumaran, Dinesh; Jiang, Mei; Garcia, Erwin; Nair, R.; Rost, B.; Swapna, G.V.T; Acton, T.B.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas. "Solution Structure Of Protein Nmul_A0922 From Nitrosospira multiformis. Northeast Structural Genomics Consortium Target Hr5524a."  .

Assembly members:

Assembly members:
Nmul_A0922, polymer, 106 residues, 12399.174 Da.

Natural source:

Natural source:   Common Name: Nitrosopira multiformis   Taxonomy ID: 323848   Superkingdom: Bacteria   Kingdom: Proteobacteria   Genus/species: Nitrosospira multiformis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21(DE3)+Magic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nmul_A0922: MTFSECAALYIKAHRSSWKN TKHADQWTNTIKTYCGPVIG PLSVQDVDTKLIMKVLDPIW EQKPETASRLRGRIESVLDW ATVRGYREGDNPARWRGYLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts353
15N chemical shifts107
1H chemical shifts723

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nmul_A09221

Entities:

Entity 1, Nmul_A0922 106 residues - 12399.174 Da.

1   METTHRPHESERGLUCYSALAALALEUTYR
2   ILELYSALAHISARGSERSERTRPLYSASN
3   THRLYSHISALAASPGLNTRPTHRASNTHR
4   ILELYSTHRTYRCYSGLYPROVALILEGLY
5   PROLEUSERVALGLNASPVALASPTHRLYS
6   LEUILEMETLYSVALLEUASPPROILETRP
7   GLUGLNLYSPROGLUTHRALASERARGLEU
8   ARGGLYARGILEGLUSERVALLEUASPTRP
9   ALATHRVALARGGLYTYRARGGLUGLYASP
10   ASNPROALAARGTRPARGGLYTYRLEUGLU
11   HISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.9 mM; H20 90.0%; D20 10.0%

sample_2: entity, [U-5% 13C; U-100% 15N], 1.0 mM; H20 90.0%; D20 10.0%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
(4,3) D GFT HNNCABCAsample_1isotropicsample_conditions_1
(4,3) D GFT CABCACONHNsample_1isotropicsample_conditions_1
(4,3) D GFT HABCABCONHNsample_1isotropicsample_conditions_1
(4,3) D GFT HCCHsample_1isotropicsample_conditions_1
3D 15N-13C RESOLVED SIMULTANEOUS NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

XEASY, Bartels et al. - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - refinement

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB ABB74225
REF WP_011380270

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