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 25033

Title: Solution structure of the Chlamydomonas reinhardtii NAB1 cold shock domain, CSD1   PubMed: 25919092

Deposition date: 2014-06-20 Original release date: 2015-05-04

Authors: Sawyer, Anne; Mobli, Mehdi

Citation: Sawyer, Anne; Mobli, Mehdi; Landsberg, Michael; Ross, Ian; Hankamer, Ben. "Solution structure of the RNA-binding cold shock domain of the Chlamydomonas reinhardtii NAB1 protein and insights into RNA recognition"  Biochem. J. ., .-. (2015).

Assembly members:
NAB1_cold_shock_domain, polymer, 82 residues, 7736.490 Da.

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

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

Entity Sequences (FASTA):
NAB1_cold_shock_domain: MRGSHHHHHHGSGEQLRQQG TVKWFNATKGFGFITPGGGG EDLFVHQTNINSEGFRSLRE GEVVEFEVEAGPDGRSKAVN VT

Data sets:
Data typeCount
13C chemical shifts265
15N chemical shifts71
1H chemical shifts428

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 82 residues - 7736.490 Da.

Residues 1-12 are part of a non-native His tag, this is the cold shock domain of NAB1

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERGLYGLUGLNLEUARGGLNGLNGLY
3   THRVALLYSTRPPHEASNALATHRLYSGLY
4   PHEGLYPHEILETHRPROGLYGLYGLYGLY
5   GLUASPLEUPHEVALHISGLNTHRASNILE
6   ASNSERGLUGLYPHEARGSERLEUARGGLU
7   GLYGLUVALVALGLUPHEGLUVALGLUALA
8   GLYPROASPGLYARGSERLYSALAVALASN
9   VALTHR

Samples:

sample_1: NAB1 cold shock domain, [U-100% 13C; U-100% 15N], 267 uM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.3 M; pH: 7; pressure: 1 atm; temperature: 298 K

Sample_conditions_2: ionic strength: 0.3 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicSample_conditions_2
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CcpNmr v2.4.0, CCPN - chemical shift assignment, data analysis, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

TOPSPIN v3.1, Bruker Biospin - collection

Rowland_NMR_Toolkit v3, A. Stern, J. C. Hoch - processing

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
GB AAN77901 ABA01136 EDP08495
REF XP_001696518

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