BMRB Entry 15263

Name: 1H, 13C, and 15N Chemical Shift Assignments for NAB2 N-terminal domain
Published: 2008-02-21

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15263

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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:

1H, 13C, and 15N Chemical Shift Assignments for NAB2 N-terminal domain

Deposition date:

2007-05-22

Original release date:

2008-02-21

Authors:

Grant, Richard; Marshall, Neil; Yang, Ji-Chun; Fasken, Milo; Kelly, Seth; Harreman, Michelle; Neuhaus, David; Corbett, Anita; Stewart, Murray

Citation:

Citation: Grant, Richard; Marshall, Neil; Yang, Ji-Chun; Fasken, Milo; Kelly, Seth; Harreman, Michelle; Neuhaus, David; Corbett, Anita; Stewart, Murray. "Structure of the N-Terminal Mlp1-Binding Domain of the Saccharomyces cerevisiae mRNA-Binding Protein, Nab2" J. Mol. Biol. 376, 1048-1059 (2008).
PubMed: 18190927

Assembly members:

Assembly members:
NAB2_NTD, polymer, 105 residues, 11462.986 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NAB2_NTD: MSQEQYTENLKVIVAEKLAG IPNFNEDIKYVAEYIVLLIV NGGTVESVVDELASLFDSVS RDTLANVVQTAFFALEALQQ GESAENIVSKIRMMNAQSLG QSDIA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	339
15N chemical shifts	111
1H chemical shifts	712

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NAB2 NTD polypeptide	1

Entities:

Entity 1, NAB2 NTD polypeptide 105 residues - 11462.986 Da.

1

MET

SER

GLN

GLU

GLN

TYR

THR

GLU

ASN

LEU

2

LYS

VAL

ILE

VAL

ALA

GLU

LYS

LEU

ALA

GLY

3

ILE

PRO

ASN

PHE

ASN

GLU

ASP

ILE

LYS

TYR

4

VAL

ALA

GLU

TYR

ILE

VAL

LEU

ILE

VAL

5

ASN

GLY

THR

VAL

GLU

SER

VAL

ASP

6

GLU

LEU

ALA

SER

LEU

PHE

ASP

SER

VAL

SER

7

ARG

ASP

THR

LEU

ALA

ASN

VAL

GLN

THR

8

ALA

PHE

ALA

LEU

GLU

ALA

LEU

GLN

9

GLY

GLU

SER

ALA

GLU

ASN

ILE

VAL

SER

LYS

10

ILE

ARG

MET

ASN

ALA

GLN

SER

LEU

GLY

11

GLN

SER

ASP

ILE

ALA

Samples:

sample_1: NAB2_NTD, [U-98% 13C; U-98% 15N], 2 mM; D2O, [U-2H], 10%; H2O 90%; sodium phosphate 25 mM; sodium chloride 10 mM

sample_conditions_1: ionic strength: 160 mM; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC CT	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY 15N filtered in F2	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHAHB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	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
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR, Brunger - structure solution

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DMX 600 MHz
Bruker DRX 500 MHz

PDB	2JPS 2V75 3LCN
DBJ	GAA23273
EMBL	CAA96830 CAY79645
GB	AAA34819 AAA34820 AAU09727 AHY79261 AJP38679
REF	NP_011393
SP	P32505
TPG	DAA07987
AlphaFold	P32505