BMRB Entry 16186

Title:
Solution NMR structure of PSPTO_3016 from Pseudomonas syringae. Northeast Structural Genomics Consortium target PsR293.
Deposition date:
2009-02-24
Original release date:
2009-03-05
Authors:
Feldmann, Erik; Ramelot, Theresa; Zhao, Li; Hamilton, Keith; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Feldmann, Erik; Ramelot, Theresa; Zhao, Li; Hamilton, Keith; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of PSPTO_3016 from Pseudomonas syringae. Northeast Structural Genomics Consortium target PsR293."  .

Assembly members:

Assembly members:
PSPTO_3016, polymer, 125 residues, 14802 Da.

Natural source:

Natural source:   Common Name: Pseudomonas syringae   Taxonomy ID: 317   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas syringae

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts561
15N chemical shifts124
1H chemical shifts884

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PSPTO_30161

Entities:

Entity 1, PSPTO_3016 125 residues - 14802 Da.

full length followed by 8 non-native C-terminal residues (LEHHHHHH)

1   METASNARGGLNGLNPHEILEASPTYRALA
2   GLNLYSLYSTYRASPTHRLYSPROASPHIS
3   PROTRPGLULYSPHEPROASPTYRALAVAL
4   PHEARGHISSERASPASNASPLYSTRPTYR
5   ALALEULEUMETASPILEPROALAGLULYS
6   ILEGLYILEASNGLYASPLYSARGVALASP
7   VALILEASPLEULYSVALGLNPROGLULEU
8   VALGLYSERLEUARGLYSLYSPROGLYILE
9   TYRPROALATYRHISMETASNLYSGLUHIS
10   TRPILETHRVALLEULEUASNGLYPROLEU
11   GLYALALYSGLUILEHISSERLEUILEGLU
12   ASPSERPHEGLNLEUTHRARGLEUGLUHIS
13   HISHISHISHISHIS

Samples:

NC_sample: entity, [U-100% 13C; U-100% 15N], 1.1 ± 0.1 mM; ammonium acetate 20 ± 0.1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.2 mM; sodium azide 0.02 ± 0.001 %; DSS 50 ± 2.5 uM; H2O 90%; D2O 10%

NC5_sample: entity, [U-5% 13C; U-100% 15N], 1.1 ± 0.1 mM; ammonium acetate 20 ± 0.1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.2 mM; sodium azide 0.02 ± 0.001 %; DSS 50 ± 2.5 uM; H2O 90%; D2O 10%

NC_sample_in_D2O: entity, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; ammonium acetate 20 ± 0.1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.2 mM; sodium azide 0.02 ± 0.001 %; DSS 50 ± 2.5 uM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
2D 1H-15N HSQC (swN)NC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY (aliph)NC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
4D CC NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(C)CH-TOCSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D H(C)CH COSYNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC (NH2 only)NC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY (arom)NC_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.3, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure solution

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB
GB AAO56506 EEB58193 EGH95472 KGK93803 KKI26969
REF NP_792811 WP_007246459 WP_011104332 WP_044389995 WP_057415793

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