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 30321

Title: Solution structure of the sorting nexin 25 phox-homology domain   PubMed: 30948714

Deposition date: 2017-08-01 Original release date: 2018-07-30

Authors: Chin, Y.; Mas, C.; Mobli, M.; Collins, B.

Citation: Chandra, Mintu; Chin, Yanni K-Y; Mas, Caroline; Feathers, J Ryan; Paul, Blessy; Datta, Sanchari; Chen, Kai-En; Jia, Xinying; Yang, Zhe; Norwood, Suzanne; Mohanty, Biswaranjan; Bugarcic, Andrea; Teasdale, Rohan; Henne, W Mike; Mobli, Mehdi; Collins, Brett. "Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities"  Nat. Commun. 10, 1528-1528 (2019).

Assembly members:
entity_1, polymer, 125 residues, 14245.309 Da.

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

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

Entity Sequences (FASTA):
entity_1: GSNLGMWKASITSGEVTEEN GEQLPCYFVMVSLQEVGGVE TKNWTVPRRLSEFQNLHRKL SECVPSLKKVQLPSLSKLPF KSIDQKFMEKSKNQLNKFLQ NLLSDERLCQSEALYAFLSP SPDYL

Data typeCount
13C chemical shifts535
15N chemical shifts131
1H chemical shifts886

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 14245.309 Da.

1   GLYSERASNLEUGLYMETTRPLYSALASER
2   ILETHRSERGLYGLUVALTHRGLUGLUASN
3   GLYGLUGLNLEUPROCYSTYRPHEVALMET
4   VALSERLEUGLNGLUVALGLYGLYVALGLU
5   THRLYSASNTRPTHRVALPROARGARGLEU
6   SERGLUPHEGLNASNLEUHISARGLYSLEU
7   SERGLUCYSVALPROSERLEULYSLYSVAL
8   GLNLEUPROSERLEUSERLYSLEUPROPHE
9   LYSSERILEASPGLNLYSPHEMETGLULYS
10   SERLYSASNGLNLEUASNLYSPHELEUGLN
11   ASNLEULEUSERASPGLUARGLEUCYSGLN
12   SERGLUALALEUTYRALAPHELEUSERPRO
13   SERPROASPTYRLEU

Samples:

sample_1: DTT 2 mM; HEPES 20 mM; NaCl 100 mM; SNX25, [U-99% 13C; U-99% 15N], 0.8 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D HBHA(CO)NHsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1anisotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

Rowland NMR ToolKit, Gregory P. Mullen - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceII 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts