BMRB Entry 17038

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17038
MolProbity Validation Chart

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Title:
Solution NMR Structure of protein STY4237 (residues 36-120) from Salmonella enterica, Northeast Structural Genomics Consortium Target SlR115
Deposition date:
2010-06-30
Original release date:
2010-08-24
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 SlR115"  To be published ., .-..

Assembly members:

Assembly members:
SlR115, polymer, 97 residues, 11129.551 Da.

Natural source:

Natural source:   Common Name: Salmonella enterica   Taxonomy ID: 28901   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella enterica

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SlR115: MAPLQQKQVVVSNKREKPVN DRRSRQQEVSPAGTSMRYEA SFKPLNGGLEKTFRLQAQQY HALTVGDQGTLSYKGTRFVG FVSRTPDNELEHHHHHH

Data typeCount
13C chemical shifts390
15N chemical shifts96
1H chemical shifts582

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1SlR1151

Entities:

Entity 1, SlR115 97 residues - 11129.551 Da.

residue 2 of the structure corresponds to residue 36 of the sequence.

1   METALAPROLEUGLNGLNLYSGLNVALVAL
2   VALSERASNLYSARGGLULYSPROVALASN
3   ASPARGARGSERARGGLNGLNGLUVALSER
4   PROALAGLYTHRSERMETARGTYRGLUALA
5   SERPHELYSPROLEUASNGLYGLYLEUGLU
6   LYSTHRPHEARGLEUGLNALAGLNGLNTYR
7   HISALALEUTHRVALGLYASPGLNGLYTHR
8   LEUSERTYRLYSGLYTHRARGPHEVALGLY
9   PHEVALSERARGTHRPROASPASNGLULEU
10   GLUHISHISHISHISHISHIS

Samples:

sample_1: SlR115, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; DTT 10 mM; H2O 95%; D2O 5%

sample_2: SlR115, [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: SlR115, [5% 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
HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
4D 1H-13C-13C-1H HMQC NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinemen, rgeometry optimization, 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
DBJ BAJ38571 BAP09540
EMBL CAD08056 CAR34973 CAR39639 CAR61453 CBG26565
GB AAL22434 AAO71419 AAV79236 AAX67409 ACF62437
PIR AD0991
REF NP_458347 NP_462475 WP_000042846 WP_000042847 WP_000042849

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