BMRB Entry 36589

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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/BMR36589
MolProbity Validation Chart

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Title:
Solution structures of the N-terminal divergent caplonin homology (NN-CH) domains of human intraflagellar transport protein 54
Deposition date:
2023-08-08
Original release date:
2023-10-09
Authors:
Dang, W.; Kuwasako, K.; He, F.; Takahashi, M.; Tsuda, K.; Nagata, T.; Tanaka, A.; Kobayashi, N.; Kigawa, T.; Guentert, P.; Shirouzu, M.; Yokoyama, S.; Muto, Y.
Citation:

Citation: Kuwasako, K.; Dang, W.; He, F.; Takahashi, M.; Tsuda, K.; Nagat, T.; Tanaka, A.; Kobayashi, N.; KIgawa, T.; Guentert, P.; Shirouzu, M.; Yokoyama, S.; Muto, Y.. "1H, 13C, and 15N resonance assignments and solution structure of the N-terminal divergent calponin homology (NN-CH) domain of human intraflagellar transport protein 54"  Biomol. NMR Assign. 18, 71-78 (2024).
PubMed: 38551798

Assembly members:

Assembly members:
TRAF3-interacting protein 1, polymer, 140 residues, 15401.022 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Cell-free gateway cloning vector N-term 8xHis mcherry pCellFree_G05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TRAF3-interacting protein 1: GSSGSSGMNAAVVRRTQEAL GKVIRRPPLTEKLLSKPPFR YLHDIITEVIRMTGFMKGLY TDAEMKSDNVKDKDAKISFL QKAIDVVVMVSGEPLLAKPA RIVAGHEPERTNELLQIIGK CCLNKLSSDDAVRRVLAGEK

Data sets:
Data typeCount
13C chemical shifts615
15N chemical shifts134
1H chemical shifts1002
distance constraints10909
torsion angle constraints686

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 140 residues - 15401.022 Da.

1   GLYSERSERGLYSERSERGLYMETASNALA
2   ALAVALVALARGARGTHRGLNGLUALALEU
3   GLYLYSVALILEARGARGPROPROLEUTHR
4   GLULYSLEULEUSERLYSPROPROPHEARG
5   TYRLEUHISASPILEILETHRGLUVALILE
6   ARGMETTHRGLYPHEMETLYSGLYLEUTYR
7   THRASPALAGLUMETLYSSERASPASNVAL
8   LYSASPLYSASPALALYSILESERPHELEU
9   GLNLYSALAILEASPVALVALVALMETVAL
10   SERGLYGLUPROLEULEUALALYSPROALA
11   ARGILEVALALAGLYHISGLUPROGLUARG
12   THRASNGLULEULEUGLNILEILEGLYLYS
13   CYSCYSLEUASNLYSLEUSERSERASPASP
14   ALAVALARGARGVALLEUALAGLYGLULYS

Samples:

sample_1: NN-CH domain of human IFT54, [U-99% 13C; U-99% 15N], 0.8 mM; NaN3, None, 0.02%; d-DTT, [U-2H], 1 mM; NaCl 100 mM; d-Tris HCl, [U-2H], 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_13C,15N-SEPARATED_NOESY SPECTRAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

Amber v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure calculation

KUJIRA v0.863, N. Kobayashi, T. Kigawa, S. Yokoyama - chemical shift assignment

MagRO-NMRView v1.2.38, N. Kobayashi - peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TopSpin, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 600 MHz

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