BMRB Entry 30551

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30551
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 Structure of the Thioredoxin-like Domain of Arabidopsis NCP
Deposition date:
2018-12-17
Original release date:
2019-06-17
Authors:
Liu, J.; Chen, M.; Zhou, P.
Citation:

Citation: Yang, Emily; Yoo, Chan Yul; Liu, Jiangxin; Wang, He; Cao, Jun; Li, Fay-Wei; Pryer, Kathleen; Sun, Tai-Ping; Weigel, Detlef; Zhou, Pei; Chen, Meng. "NCP activates chloroplast transcription by controlling phytochrome-dependent dual nuclear and plastidial switches"  Nat. Commun. 10, 2630-2630 (2019).
PubMed: 31201314

Assembly members:

Assembly members:
entity_1, polymer, 146 residues, 16605.234 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SHMDNYIRPIKDLTTAEWEE AVFKDISPLMVLVHNRYKRP KENEKFREELEKAIQVIWNC GLPSPRCVAVDAVVETDLVS ALKVSVFPEIIFTKAGKILY REKGIRTADELSKIMAFFYY GAAKPPCLNGVVNSQEQIPL VDVSVN

Data sets:
Data typeCount
13C chemical shifts503
15N chemical shifts139
1H chemical shifts1058

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 146 residues - 16605.234 Da.

1   SERHISMETASPASNTYRILEARGPROILE
2   LYSASPLEUTHRTHRALAGLUTRPGLUGLU
3   ALAVALPHELYSASPILESERPROLEUMET
4   VALLEUVALHISASNARGTYRLYSARGPRO
5   LYSGLUASNGLULYSPHEARGGLUGLULEU
6   GLULYSALAILEGLNVALILETRPASNCYS
7   GLYLEUPROSERPROARGCYSVALALAVAL
8   ASPALAVALVALGLUTHRASPLEUVALSER
9   ALALEULYSVALSERVALPHEPROGLUILE
10   ILEPHETHRLYSALAGLYLYSILELEUTYR
11   ARGGLULYSGLYILEARGTHRALAASPGLU
12   LEUSERLYSILEMETALAPHEPHETYRTYR
13   GLYALAALALYSPROPROCYSLEUASNGLY
14   VALVALASNSERGLNGLUGLNILEPROLEU
15   VALASPVALSERVALASN

Samples:

sample_1: NCP Thioredoxin-like Domain, [U-99% 13C; U-99% 15N], 1.2 mM; HEPES 25 mM; KCl 50 mM; DTT 10 mM

sample_2: NCP Thioredoxin-like Domain, [U-99% 13C; U-99% 15N], 1.2 mM; HEPES 25 mM; KCl 50 mM; DTT 10 mM

sample_3: NCP Thioredoxin-like Domain, [U-99% 15N], 1.2 mM; HEPES 25 mM; KCl 50 mM; DTT 10 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
Triple-resonancesample_1isotropicsample_conditions_1
4D HCCH-TOCSYsample_1isotropicsample_conditions_1
4D HCCONHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
4D 13C-HMQC-NOESY-15N-HSQCsample_1isotropicsample_conditions_1
4D 13C-HMQC-NOESY-13C-HSQCsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

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