BMRB Entry 15456

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15456
MolProbity Validation Chart

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Title:
NMR Solution Structure of homodimer protein SO_2176 from Shewanella oneidensis. Northeast Structural Genomics Consortium Target SoR77.
Deposition date:
2007-09-03
Original release date:
2007-09-17
Authors:
Ramelot, Theresa; John, Cort; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Cort, John; Montelione, Gaetano; Kennedy, Michael. "NMR Solution Structure of homodimer protein SO_2176 from Shewanella oneidensis. Northeast Structural Genomics Consortium Target SoR77."  .

Assembly members:

Assembly members:
protein, polymer, 80 residues, 8930 Da.

Natural source:

Natural source:   Common Name: Shewanella oneidensis   Taxonomy ID: 70863   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Shewanella oneidensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein: MAIQSKYSNTQVESLIAEIL VVLEKHKAPTDLSLMALGNC VTHLLERKVPSESRQAVAEQ FAKALAQSVKSNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts86
1H chemical shifts556

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1proteinA1
2proteinB1

Entities:

Entity 1, proteinA 80 residues - 8930 Da.

homodimer, 8 non-native C-terminal His-tag (LEHHHHHH)

1   METALAILEGLNSERLYSTYRSERASNTHR
2   GLNVALGLUSERLEUILEALAGLUILELEU
3   VALVALLEUGLULYSHISLYSALAPROTHR
4   ASPLEUSERLEUMETALALEUGLYASNCYS
5   VALTHRHISLEULEUGLUARGLYSVALPRO
6   SERGLUSERARGGLNALAVALALAGLUGLN
7   PHEALALYSALALEUALAGLNSERVALLYS
8   SERASNLEUGLUHISHISHISHISHISHIS

Samples:

sample_NC: protein, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_NC50: protein, [U-100% 13C; U-100% 15N], 0.5 ± 0.05 mM; protein 0.5 ± 0.05 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_NC5: protein, [U-5% 13C; U-100% 15N], 1 ± 0.1 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_NC_in_D2O: protein, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
3D 1H-15N NOESYsample_NCisotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_NCisotropicsample_conditions_1
4D 1H-13C NOESYsample_NC_in_D2Oisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D H(CCO)NHsample_NC50isotropicsample_conditions_1
3D C(CO)NHsample_NC50isotropicsample_conditions_1
3D HBHA(CO)NHsample_NC50isotropicsample_conditions_1
3D HCCH-COSYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
2D 1H-15N HSQC (15 min)sample_NC_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQCsample_NC50isotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5isotropicsample_conditions_1
3D CCH-TOCSYsample_NC50isotropicsample_conditions_1
3D 1H-13C NOESYsample_NC_in_D2Oisotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_NCisotropicsample_conditions_1
2D 1H-15N HSQC (30 min)sample_NC_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC (1 hr)sample_NC_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC (24 hr)sample_NC_in_D2Oisotropicsample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.1, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAN55220 ABI39291 ABI43282 ABK48656 ABN62028
REF NP_717776 WP_006081998 WP_011072212 WP_023268262 WP_055648424
SP Q8EF26
AlphaFold Q8EF26

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