BMRB Entry 31107

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31107
MolProbity Validation Chart

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

Title:
Solution NMR structure of KaiB variant from Thermosynechococcus elongatus vestitus (KaiBTV-4)
Deposition date:
2023-09-23
Original release date:
2023-10-18
Authors:
Ojoawo, A.; Wayment-Steele, K.; Kern, D.
Citation:

Citation: Wayment-Steele, Hannah; Ojoawo, Adedolapo; Otten, Renee; Apitz, Julia; Pitsawong, Warintra; Homberger, M.; Ovchinnikov, Sergey; Colwell, Lucy; Kern, D.. "Predicting multiple conformations via sequence clustering and AlphaFold2"  Nature 625, 832-839 (2024).
PubMed: 37956700

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, 9920.542 Da.

Natural source:

Natural source:   Common Name: Thermosynechococcus vestitus BP-1   Taxonomy ID: 197221   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermosynechococcus vestitus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MYVFRLYVRGETHAAEVALK NLHDLLSSALKVPYTLKVVD VTKQPDLAEKDQVQATPTLV RVYPQPVRRLVGQLDHRYRL QHLLSP

Data sets:
Data typeCount
13C chemical shifts267
15N chemical shifts78
1H chemical shifts573

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 86 residues - 9920.542 Da.

1   METTYRVALPHEARGLEUTYRVALARGGLY
2   GLUTHRHISALAALAGLUVALALALEULYS
3   ASNLEUHISASPLEULEUSERSERALALEU
4   LYSVALPROTYRTHRLEULYSVALVALASP
5   VALTHRLYSGLNPROASPLEUALAGLULYS
6   ASPGLNVALGLNALATHRPROTHRLEUVAL
7   ARGVALTYRPROGLNPROVALARGARGLEU
8   VALGLYGLNLEUASPHISARGTYRARGLEU
9   GLNHISLEULEUSERPRO

Samples:

sample_1: MOPS 100 mM; sodium chloride 50 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HDH AROMATICsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HD AROMATICsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY, NMRFAM-SPARKY - chemical shift assignment

PINE Server, PINE Server - chemical shift assignment

TopSpin, Bruker Biospin - collection

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

PONDEROSA-C/S, PONDEROSA-C/S - structure calculation

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

AUDANA, AUDANA - structure calculation

TALOS-N, TALOS-N - structure calculation

NMR spectrometers:

  • Bruker AVANCE III HD 750 MHz
  • Bruker AVANCE NEO 800 MHz
  • Bruker AVANCE III HD 600 MHz
  • Varian Uniform NMR System 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks