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Biological Magnetic Resonance Data Bank


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BMRB Entry 16072

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16072
MolProbity Validation Chart

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Title: Solution NMR structure of SSP0047 from Staphylococcus saprophyticus. Northeast Structural Genomics Consortium Target SyR6.

Deposition date: 2008-12-19 Original release date: 2009-02-17

Authors: Ramelot, Theresa; Ding, Keyang; Chen, Chen; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Ding, Keyang; Chen, Chen; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of SSP0047 from Staphylococcus saprophyticus. Northeast Structural Genomics Consortium Target SyR6."  Not known ., .-..

Assembly members:
SSP0047, polymer, 120 residues, 13320 Da.

Natural source:   Common Name: Staphylococcus saprophyticus   Taxonomy ID: 29385   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus saprophyticus

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

Entity Sequences (FASTA):
SSP0047: MTLELQLKHYITNLFNLPRD EKWECESIEEVADDILPDQY VRLGPLSNKILQTNTYYSDT LHKSNIYPFILYYQKQLIAI GFIDENHDMDFLYLHNTVMP LLDQRYLLTGGQLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts547
15N chemical shifts120
1H chemical shifts858

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SSP00471

Entities:

Entity 1, SSP0047 120 residues - 13320 Da.

1   METTHRLEUGLULEUGLNLEULYSHISTYR
2   ILETHRASNLEUPHEASNLEUPROARGASP
3   GLULYSTRPGLUCYSGLUSERILEGLUGLU
4   VALALAASPASPILELEUPROASPGLNTYR
5   VALARGLEUGLYPROLEUSERASNLYSILE
6   LEUGLNTHRASNTHRTYRTYRSERASPTHR
7   LEUHISLYSSERASNILETYRPROPHEILE
8   LEUTYRTYRGLNLYSGLNLEUILEALAILE
9   GLYPHEILEASPGLUASNHISASPMETASP
10   PHELEUTYRLEUHISASNTHRVALMETPRO
11   LEULEUASPGLNARGTYRLEULEUTHRGLY
12   GLYGLNLEUGLUHISHISHISHISHISHIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.3 ± 0.05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.3 ± 0.05 mM; D2O 100%

NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-5% 13C; U-100% 15N], 0.3 ± 0.05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
4D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
3D CBCACOCAHANC_sample_in_D2Oisotropicsample_conditions_1

Software:

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

VNMR v6.1C, Varian - collection

TOPSPIN v2.1, 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 validation

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

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

SWS Q4A134_STAS1
UNP Q4A134
PDB
DBJ BAE17192
REF WP_011302049 WP_053041968

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