BMRB Entry 51870

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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/BMR51870
MolProbity Validation Chart

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Title:
AtGRP2 CSD
Deposition date:
2023-03-07
Original release date:
2023-05-23
Authors:
Pougy, Karina; Almeida, Fabio; Pinheiro, Anderson
Citation:

Citation: Pougy, Karina; Sachetto-Martins, Gilberto; Almeida, Fabio; Pinheiro, Anderson. "1H, 15N, and 13C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2"  Biomol. NMR Assignments 17, 143-149 (2023).
PubMed: 37145295

Assembly members:

Assembly members:
entity_1, polymer, 92 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMSGDNGGGERRKGSVKWF DTQKGFGFITPDDGGDDLFV HQSSIRSEGFRSLAAEEAVE FEVEIDNNNRPKAIDVSGPD GAPVQGNSGGGS

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts92
1H chemical shifts542

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AtGRP2 CSD1

Entities:

Entity 1, AtGRP2 CSD 92 residues - Formula weight is not available

1   GLYHISMETSERGLYASPASNGLYGLYGLY
2   GLUARGARGLYSGLYSERVALLYSTRPPHE
3   ASPTHRGLNLYSGLYPHEGLYPHEILETHR
4   PROASPASPGLYGLYASPASPLEUPHEVAL
5   HISGLNSERSERILEARGSERGLUGLYPHE
6   ARGSERLEUALAALAGLUGLUALAVALGLU
7   PHEGLUVALGLUILEASPASNASNASNARG
8   PROLYSALAILEASPVALSERGLYPROASP
9   GLYALAPROVALGLNGLYASNSERGLYGLY
10   GLYSER

Samples:

sample_1: AtGRP2-CSD, [U-100% 13C; U-100% 15N], 1.3 mM; sodium phosphate 20 mM; sodium chloride 50 mM; PMSF 250 uM; sodium azide 3 mM; D2O, [U-100% 2H], 5%

sample_2: AtGRP2-CSD, [U-100% 15N], 1.3 mM; sodium phosphate 20 mM; sodium chloride 50 mM; PMSF 250 uM; sodium azide 3 mM; D2O, [U-100% 2H], 5%

sample_3: AtGRP2-CSD 1.3 mM; sodium phosphate 20 mM; sodium chloride 50 mM; PMSF 250 uM; sodium azide 3 mM; D2O, [U-100% 2H], 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.1 - collection

NMRPipe - processing

CARA v1.9.1.7 - chemical shift assignment

CcpNMR v2.5.2 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 900 MHz

Related Database Links:

Uniprot Q41188
AlphaFold C0Z2E8

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