BMRB Entry 31153

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31153
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
4F-Trp labeled Oscillatoria Agardhii Agglutinin (OAA)
Deposition date:
2024-03-21
Original release date:
2024-10-30
Authors:
Runge, B.; Zadorozhnyi, R.; Quinn, C.; Russell, R.; Lu, M.; Antolinez, S.; Struppe, J.; Schwieters, C.; Byeon, I.; Hadden-Perilla, J.; Gronenborn, A.; Polenova, T.
Citation:

Citation: Runge, B.; Zadorozhnyi, R.; Quinn, C.; Russell, R.; Lu, M.; Antolinez, S.; Struppe, J.; Schwieters, C.; Byeon, I.; Hadden-Perilla, J.; Gronenborn, A.; Polenova, T.. "Integrating 19F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy"  J. Am. Chem. Soc. 146, 30483-30494 (2024).
PubMed: 39440810

Assembly members:

Assembly members:
entity_1, polymer, 133 residues, 14169.901 Da.

Natural source:

Natural source:   Common Name: Oscillatoria agardhii   Taxonomy ID: 1160   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Oscillatoria agardhii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21   Vector: pET-26b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MALYNVENQXGGSSAPXNEG GQXEIGSRSDQNVVAINVES GDDGQTLNGTMTYAGEGPIG FRATLLGNNSYEVENQXGGD SAPXHSGGNXILGSRENQNV VAINVESGDDGQTLNGTMTY AGEGPIGFKGTLT

Data sets:
Data typeCount
13C chemical shifts504
15N chemical shifts132
19F chemical shifts6
1H chemical shifts37

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 133 residues - 14169.901 Da.

1   METALALEUTYRASNVALGLUASNGLN4FW
2   GLYGLYSERSERALAPRO4FWASNGLUGLY
3   GLYGLN4FWGLUILEGLYSERARGSERASP
4   GLNASNVALVALALAILEASNVALGLUSER
5   GLYASPASPGLYGLNTHRLEUASNGLYTHR
6   METTHRTYRALAGLYGLUGLYPROILEGLY
7   PHEARGALATHRLEULEUGLYASNASNSER
8   TYRGLUVALGLUASNGLN4FWGLYGLYASP
9   SERALAPRO4FWHISSERGLYGLYASN4FW
10   ILELEUGLYSERARGGLUASNGLNASNVAL
11   VALALAILEASNVALGLUSERGLYASPASP
12   GLYGLNTHRLEUASNGLYTHRMETTHRTYR
13   ALAGLYGLUGLYPROILEGLYPHELYSGLY
14   THRLEUTHR

Samples:

sample_1: NaH2PO4 1.2 mM; K2HPO4 0.8 mM; Li2SO4 0.2 mM; CAPS 0.1 mM; OAA, [U-100% 19F]-4F-Trp, U-100% 13C, U-100% 15N], 30 mg/mL

sample_conditions_1: ionic strength: 2.3 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D CORD 25 mssample_1isotropicsample_conditions_1
2D CORD 50 mssample_1isotropicsample_conditions_1
2D CORD 100 mssample_1isotropicsample_conditions_1
2D CORD 250 mssample_1isotropicsample_conditions_1
2D CORD 500 mssample_1isotropicsample_conditions_1
2D NCACX 50 mssample_1isotropicsample_conditions_1
2D NCOCX 25 mssample_1isotropicsample_conditions_1
3D NCACX 50 mssample_1isotropicsample_conditions_1
3D NCOCX 25 mssample_1isotropicsample_conditions_1
2D hCH HETCORsample_1isotropicsample_conditions_1
2D hNH HETCORsample_1isotropicsample_conditions_1
2D 19F-19F RFDRsample_1isotropicsample_conditions_1
2D hCF HETCORsample_1isotropicsample_conditions_1
3D hCHF HETCORsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

CcpNmr Analysis, CCPN - data analysis, peak picking

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL. - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III 850 MHz
  • Bruker AVANCE III HD 600 MHz
  • Bruker AVANCE III 500 MHz