BMRB Entry 25033

Name: Solution structure of the Chlamydomonas reinhardtii NAB1 cold shock domain, CSD1
Published: 2015-05-04

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PDB ID: 2mqh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25033
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the Chlamydomonas reinhardtii NAB1 cold shock domain, CSD1

Deposition date:

2014-06-20

Original release date:

2015-05-04

Authors:

Sawyer, Anne; Mobli, Mehdi

Citation:

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).
PubMed: 25919092

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE-80L

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	265
15N chemical shifts	71
1H chemical shifts	428

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

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

MET

ARG

GLY

SER

HIS

2

GLY

SER

GLY

GLU

GLN

LEU

ARG

GLN

GLY

3

THR

VAL

LYS

TRP

PHE

ASN

ALA

THR

LYS

GLY

4

PHE

GLY

PHE

ILE

THR

PRO

GLY

5

GLU

ASP

LEU

PHE

VAL

HIS

GLN

THR

ASN

ILE

6

ASN

SER

GLU

GLY

PHE

ARG

SER

LEU

ARG

GLU

7

GLY

GLU

VAL

GLU

PHE

GLU

VAL

GLU

ALA

8

GLY

PRO

ASP

GLY

ARG

SER

LYS

ALA

VAL

ASN

9

VAL

THR

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:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	Sample_conditions_2
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_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

PDB	2MQH
GB	AAN77901 ABA01136 EDP08495
REF	XP_001696518