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 15791

Title: Solution NMR Structure of UPF0339 Protein SO3888 from Shewanella Oneidensis. Northeast Structural Genomics Consortium Target SoR190   PubMed: TBA

Authors: Tang, Yuefeng; Wang, Dongyan; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Tang, Yuefeng; Wang, Dongyan; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of UPF0339 Protein SO3888 from Shewanella Oneidensis."  Not known ., .-..

Assembly members:
SoR190, polymer, 118 residues, 13103.730 Da.

Natural source:   Common Name: Shewanella Oneidensis   Taxonomy ID: 70863   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Shewanella Oneidensis

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

Entity Sequences (FASTA):
SoR190: MSGWYELSKSSNDQFKFVLK AGNGEVILTSELYTGKSGAM NGIESVQTNSPIEARYAKEV AKNDKPYFNLKAANHQIIGT SQMYSSTAARDNGIKSVMEN GKTTTIKDLTLEHHHHHH

Data typeCount
13C chemical shifts471
15N chemical shifts124
1H chemical shifts758

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SoR1901

Entities:

Entity 1, SoR190 118 residues - 13103.730 Da.

Residue 111-118 represent a non-native affinity purification tag (LEHHHHHH)

1   METSERGLYTRPTYRGLULEUSERLYSSER
2   SERASNASPGLNPHELYSPHEVALLEULYS
3   ALAGLYASNGLYGLUVALILELEUTHRSER
4   GLULEUTYRTHRGLYLYSSERGLYALAMET
5   ASNGLYILEGLUSERVALGLNTHRASNSER
6   PROILEGLUALAARGTYRALALYSGLUVAL
7   ALALYSASNASPLYSPROTYRPHEASNLEU
8   LYSALAALAASNHISGLNILEILEGLYTHR
9   SERGLNMETTYRSERSERTHRALAALAARG
10   ASPASNGLYILELYSSERVALMETGLUASN
11   GLYLYSTHRTHRTHRILELYSASPLEUTHR
12   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: SoR190, [U-100% 13C; U-100% 15N], 1.3 mM; CaCl2 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; NaN3 0.02%

sample_2: SoR190, [U-5% 13C; U-100% 15N], 1.3 mM; CaCl2 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; 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 1H-15N NOESYsample_1isotropicsample_conditions_1
3D simutaneous NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY_aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC_high resolutionsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.110, Goddard - data analysis, peak picking

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - data analysis

PDBStat v5.0, Tejero and Montelione - PDBanalysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAN56863 ABI40290 ABK46978 ABN63039 ADV53245
REF NP_719419 WP_011073636 WP_011847750 WP_025007863
SP Q8EAL4