BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16298

Title: Solution NMR structure of the domain N-terminal to the integrase domain of SH1003 from Staphylococcus haemolyticus. Northeast Structural Genomics Consortium Target ShR105F (64-166).

Authors: Yang, Yunhuang; Ramelot, Theresa; Belote, Rachel; Foote, Erica; Janjua, Haleema; Nair, R.; Rost, Burkhard; Swapna, G.V.T; Acton, Thomas; Xiao, Rong; Everett, John; Montelio, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Belote, Rachel; Foote, Erica; Janjua, Haleema; Nair, R.; Rost, Burkhard; Swapna, G.V.T; Acton, Thomas; Xiao, Rong; Everett, John; Montelio, Gaetano; Kennedy, Michael. "Solution NMR structure of the domain N-terminal to the integrase domain of SH1003 from Staphylococcus haemolyticus. Northeast Structural Genomics Consortium Target ShR105F (64-166)."  Not known ., .-..

Assembly members:
SH1003, polymer, 111 residues, 13123.101 Da.

Natural source:   Common Name: Staphylococcus haemolyticus   Taxonomy ID: 1283   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus haemolyticus

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

Entity Sequences (FASTA):
SH1003: TFKQVADDWLKQYANDVKVS SVRAREKAIQHAIERFNTKP IQTIKKHDYQRFVDDISAQY SKNYVDSIVASTNMIFKYAY DTRLIKAMPSEGIKRPKKKV SVELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts511
15N chemical shifts116
1H chemical shifts803

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH10031

Entities:

Entity 1, SH1003 111 residues - 13123.101 Da.

residues 64-166 of SH1003 followed by 8 non-native C-terminal residues (LEHHHHHH)

1   THRPHELYSGLNVALALAASPASPTRPLEU
2   LYSGLNTYRALAASNASPVALLYSVALSER
3   SERVALARGALAARGGLULYSALAILEGLN
4   HISALAILEGLUARGPHEASNTHRLYSPRO
5   ILEGLNTHRILELYSLYSHISASPTYRGLN
6   ARGPHEVALASPASPILESERALAGLNTYR
7   SERLYSASNTYRVALASPSERILEVALALA
8   SERTHRASNMETILEPHELYSTYRALATYR
9   ASPTHRARGLEUILELYSALAMETPROSER
10   GLUGLYILELYSARGPROLYSLYSLYSVAL
11   SERVALGLULEUGLUHISHISHISHISHIS
12   HIS

Samples:

NC_sample: SH1003, [U-100% 13C; U-100% 15N], 0.84 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC5_sample: SH1003 0.79 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 200 ± 10 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: SH1003, [U-100% 13C; U-100% 15N], 0.84 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; 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 HSQC (ct)NC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY (aliph)NC_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-13C HSQC (no ct)NC5_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

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

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure solution

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

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB
DBJ BAE04312
GB AKC75758 KDP56009 KQC18344
REF WP_011275311 WP_016931052 WP_033079901 WP_048667935 WP_049383042