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Biological Magnetic Resonance Data Bank


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BMRB Entry 17175

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17175
MolProbity Validation Chart

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Title: Solution NMR structure of hepothetical homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae, Northeast Structural Genomics Consortium Target SpR104.

Deposition date: 2010-09-10 Original release date: 2015-05-07

Authors: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of hepothetical homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae, Northeast Structural Genomics Consortium Target SpR104."  Not known ., .-..

Assembly members:
SP_0782, polymer, 82 residues, 9574.8 Da.

Natural source:   Common Name: S. pneumoniae   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

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

Entity Sequences (FASTA):
SP_0782: MKKMAEFTFEIEEHLLTLSE NEKGWTKEINRVSFNGAPAK FDIRAWSPDHTKMGKGITLS NEEFQTMVDAFKGNLEHHHH HH

Data typeCount
13C chemical shifts358
15N chemical shifts92
1H chemical shifts555

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SP_0782, chain 11
2SP_0782, chain 21

Entities:

Entity 1, SP_0782, chain 1 82 residues - 9574.8 Da.

homodimer protein SP_0782 (7-79) from Chromobacterium violaceum, preceded by non-native N-terminal Met and followed by 8 non-native C-terminal residues (LEHHHHHH)

1   METLYSLYSMETALAGLUPHETHRPHEGLU
2   ILEGLUGLUHISLEULEUTHRLEUSERGLU
3   ASNGLULYSGLYTRPTHRLYSGLUILEASN
4   ARGVALSERPHEASNGLYALAPROALALYS
5   PHEASPILEARGALATRPSERPROASPHIS
6   THRLYSMETGLYLYSGLYILETHRLEUSER
7   ASNGLUGLUPHEGLNTHRMETVALASPALA
8   PHELYSGLYASNLEUGLUHISHISHISHIS
9   HISHIS

Samples:

NC_sample: homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae, [U-100% 13C; U-100% 15N], 1.2 ± 0.12 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC5_sample: homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae, [U-5% 13C; U-100% 15N], 1.2 ± 0.12 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC_sample_in_D2O: homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae, [U-100% 13C; U-100% 15N], 1.2 ± 0.12 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; D2O 100%

mixed_sample: homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae, [U-100% 13C; U-100% 15N], 1.2 ± 0.12 mM; homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae 1.2 ± 0.12 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliNC_sampleisotropicsample_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 HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC NOESYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC_swN150ppmNC_sampleisotropicsample_conditions_1
3D edited/filtered 13C NOESYmixed_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aroNC_sampleisotropicsample_conditions_1

Software:

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

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

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

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, A., Assadi, A., Markley, J. L. & Eghbalnia, H. - autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB
EMBL CAR68548 CBW32364 CBW34324 CBW36334 CCM08389
GB AAK74919 AAK99494 ABJ55343 ACA35659 ACB89982
REF NP_358284 WP_000807422 WP_000807423 WP_000807425 WP_000807426

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts