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 16806

Title: Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803. Northeast Structural Genomics Consortium Target Target SgR145.

Authors: Rossi, Paolo; Forouhar, F.; Lange, O.; Lee, H.; Lemak, A; Belote, R.; Ciccosanti, C.; Foote, Erica; Sahdev, Seema; Acton, T.; Xiao, R.; Everett, J.; Montelione, Gaetano

Citation: Rossi, Paolo; Forouhar, Farhad; Lange, Oliver; Lee, Hsiau; Acton, Thomas; Xiao, Rong; Montelione, Gaetano. "Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803. Northeast Structural Genomics Consortium Target Target SgR145."  To be published ., .-..

Assembly members:
SgR145, polymer, 202 residues, 22403.449 Da.

Natural source:   Common Name: Synechocystis sp. PCC 6803   Taxonomy ID: 1148   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis not available

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

Entity Sequences (FASTA):
SgR145: MWDERFSQSEYVYGTEPNDF LVSVANQIPQGKILCLAEGE GRNACFLASLGYEVTAVDQS SVGLAKAKQLAQEKGVKITT VQSNLADFDIVADAWEGIVS IFCHLPSSLRQQLYPKVYQG LKPGGVFILEGFAPEQLQYN TGGPKDLDLLPKLETLQSEL PSLNWLIANNLERNLDEGAY HQGKAALIQLLGQKLEHHHH HH

Data typeCount
13C chemical shifts567
15N chemical shifts159
1H chemical shifts423

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SgR1451

Entities:

Entity 1, SgR145 202 residues - 22403.449 Da.

1   METTRPASPGLUARGPHESERGLNSERGLU
2   TYRVALTYRGLYTHRGLUPROASNASPPHE
3   LEUVALSERVALALAASNGLNILEPROGLN
4   GLYLYSILELEUCYSLEUALAGLUGLYGLU
5   GLYARGASNALACYSPHELEUALASERLEU
6   GLYTYRGLUVALTHRALAVALASPGLNSER
7   SERVALGLYLEUALALYSALALYSGLNLEU
8   ALAGLNGLULYSGLYVALLYSILETHRTHR
9   VALGLNSERASNLEUALAASPPHEASPILE
10   VALALAASPALATRPGLUGLYILEVALSER
11   ILEPHECYSHISLEUPROSERSERLEUARG
12   GLNGLNLEUTYRPROLYSVALTYRGLNGLY
13   LEULYSPROGLYGLYVALPHEILELEUGLU
14   GLYPHEALAPROGLUGLNLEUGLNTYRASN
15   THRGLYGLYPROLYSASPLEUASPLEULEU
16   PROLYSLEUGLUTHRLEUGLNSERGLULEU
17   PROSERLEUASNTRPLEUILEALAASNASN
18   LEUGLUARGASNLEUASPGLUGLYALATYR
19   HISGLNGLYLYSALAALALEUILEGLNLEU
20   LEUGLYGLNLYSLEUGLUHISHISHISHIS
21   HISHIS

Samples:

sample: SgR145, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
2D 1H-15N HSQCsampleanisotropicsample_conditions_1
2D 1H-15N HSQCsampleanisotropicsample_conditions_1
3D HNCA(CO)sampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D 1H-13C NOESYsampleisotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
3D 1H-13C HSQC_NOESY_HSQCsampleisotropicsample_conditions_1
3D 1H-15N HSQC_NOESY_HSQCsampleisotropicsample_conditions_1
3D 1H-13C-15N HSQC_NOESY_HSQCsampleisotropicsample_conditions_1
3D 1H-15N-13C HSQC_NOESY_HSQCsampleisotropicsample_conditions_1
3D HCCH-TOCSYsampleisotropicsample_conditions_1
1D 15N T1sampleisotropicsample_conditions_1
1D 15N T2 CPMGsampleisotropicsample_conditions_1
2D- HET NOEsampleisotropicsample_conditions_1

Software:

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, 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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA18831 BAK51873 BAL30871 BAL34040 BAL37209
GB AGF53380 ALJ69250
REF WP_010874311