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 19308

Title: Biochemical effect of S-67 phosphorylation on UVI31+ from C. reinhardtii   PubMed: 23979961

Deposition date: 2013-06-18 Original release date: 2014-02-13

Authors: Singh, Himanshu; Verma, Deepshikha; Chary, KVR

Citation: Singh, Himanshu; Rao, B.; Chary, Kandala. "(1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii."  Biomol. NMR Assignments ., .-. (2013).

Assembly members:
Phophorylated_UVI31+, polymer, 123 residues, 13360 Da.

Natural source:   Common Name: Chlamydomonas reinhardtii   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET and pQE-30

Entity Sequences (FASTA):
Phophorylated_UVI31+: MRGSHHHHHHGSHVISSIAS RGSMAEHQLGPIAGAIKSKV EAALSPTHFKLINDSHKHAG HYARDGSTASDAGETHFRLE VTSDAFKGLTLVKRHQLIYG LLSDEFKAGLHALSMTTKTP AEQ

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts106
1H chemical shifts106

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UVI31+1

Entities:

Entity 1, UVI31+ 123 residues - 13360 Da.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERHISVALILESERSERILEALASER
3   ARGGLYSERMETALAGLUHISGLNLEUGLY
4   PROILEALAGLYALAILELYSSERLYSVAL
5   GLUALAALALEUSERPROTHRHISPHELYS
6   LEUILEASNASPSERHISLYSHISALAGLY
7   HISTYRALAARGASPGLYSERTHRALASER
8   ASPALAGLYGLUTHRHISPHEARGLEUGLU
9   VALTHRSERASPALAPHELYSGLYLEUTHR
10   LEUVALLYSARGHISGLNLEUILETYRGLY
11   LEULEUSERASPGLUPHELYSALAGLYLEU
12   HISALALEUSERMETTHRTHRLYSTHRPRO
13   ALAGLUGLN

Samples:

sample_1: Phophorylated UVI31+, [U-99% 13C; U-99% 15N], 0.5 mM; phosphate buffer 50 mM; ATP 1.5 mM; MgCl2 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2, bruker - chemical shift assignment, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16864 18567 18969 19307
PDB
GB EDO96758
REF XP_001702905

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