BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27439

Title: Sph15   PubMed: 30284185

Deposition date: 2018-03-30 Original release date: 2018-10-04

Authors: Coulthard, Rachel; Rajasekar, Karthik; Hyde, Eva; Smith, Lorna

Citation: Coulthard, Rachel; Rajasekar, Karthik; Hyde, Eva; Smith, Lorna. "1H, 13C and 15N NMR assignments of self-incompatibility protein homologue 15 from Arabidopsis thaliana"  Biomol. NMR Assignments 13, 67-70 (2019).

Assembly members:
Sph15, polymer, 115 residues, Formula weight is not available

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
Sph15: AMGCKEIEIVIKNTLGPSRI LQYHCRSGNTNVGVQYLNFK GTRIIKFKDDGTERSRWNCL FRQGINMKFFTEVEAYRPDL KHPLCGKRYELSARMDAIYF KMDERPPQPLNKWRS

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts105
1H chemical shifts598

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sph151

Entities:

Entity 1, Sph15 115 residues - Formula weight is not available

1   ALAMETGLYCYSLYSGLUILEGLUILEVAL
2   ILELYSASNTHRLEUGLYPROSERARGILE
3   LEUGLNTYRHISCYSARGSERGLYASNTHR
4   ASNVALGLYVALGLNTYRLEUASNPHELYS
5   GLYTHRARGILEILELYSPHELYSASPASP
6   GLYTHRGLUARGSERARGTRPASNCYSLEU
7   PHEARGGLNGLYILEASNMETLYSPHEPHE
8   THRGLUVALGLUALATYRARGPROASPLEU
9   LYSHISPROLEUCYSGLYLYSARGTYRGLU
10   LEUSERALAARGMETASPALAILETYRPHE
11   LYSMETASPGLUARGPROPROGLNPROLEU
12   ASNLYSTRPARGSER

Samples:

sample_1: Sph15, [U-99% 13C; U-99% 15N], 0.3 mM; sodium chloride 50 mM

sample_2: Sph15, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

CCPN vV2, CCPN - chemical shift assignment

ARIA v2.3, Linge, O'Donoghue and Nilges - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Varian INOVA 800 MHz
  • Bruker Avance 600 MHz

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