BMRB Entry 51033

Name: Chemical shift assignments of ANAC046(172-338)
Published: 2021-11-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51033

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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:

Chemical shift assignments of ANAC046(172-338)

Deposition date:

2021-07-28

Original release date:

2021-11-03

Authors:

Brakti, Inna; Newcombe, Estella; Skriver, Karen; Kragelund, Birthe

Citation:

Citation: Newcombe, Estella; Fernandes, Catarina; Lundsgaard, Jeppe; Brakti, Inna; Lindorff-Larsen, Kresten; Langkilde, Annette; Skriver, Karen; Kragelund, Birthe. "Insight into calcium-binding motifs of intrinsically disordered proteins" Biomolecules 11, 1173-1173 (2021).
PubMed: 34439840

Assembly members:

Assembly members:
entity_1, polymer, 167 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: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NAPSTTITTTKQLSRIDSLD NIDHLLDFSSLPPLIDPGFL GQPGPSFSGARQQHDLKPVL HHPTTAPVDNTYLPTQALNF PYHSVHNSGSDFGYGAGSGN NNKGMIKLEHSLVSVSQETG LSSDVNTTATPEISSYPMMM NPAMMDGSKSACDGLDDLIF WEDLYTS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	372
15N chemical shifts	146
1H chemical shifts	167

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ANAC046(172-338) monomer	1

Entities:

Entity 1, ANAC046(172-338) monomer 167 residues - Formula weight is not available

1

ASN

ALA

PRO

SER

THR

ILE

THR

2

LYS

GLN

LEU

SER

ARG

ILE

ASP

SER

LEU

ASP

3

ASN

ILE

ASP

HIS

LEU

ASP

PHE

SER

4

LEU

PRO

LEU

ILE

ASP

PRO

GLY

PHE

LEU

5

GLY

GLN

PRO

GLY

PRO

SER

PHE

SER

GLY

ALA

6

ARG

GLN

HIS

ASP

LEU

LYS

PRO

VAL

LEU

7

HIS

PRO

THR

ALA

PRO

VAL

ASP

ASN

8

THR

TYR

LEU

PRO

THR

GLN

ALA

LEU

ASN

PHE

9

PRO

TYR

HIS

SER

VAL

HIS

ASN

SER

GLY

SER

10

ASP

PHE

GLY

TYR

GLY

ALA

GLY

SER

GLY

ASN

11

ASN

LYS

GLY

MET

ILE

LYS

LEU

GLU

HIS

12

SER

LEU

VAL

SER

VAL

SER

GLN

GLU

THR

GLY

13

LEU

SER

ASP

VAL

ASN

THR

ALA

THR

14

PRO

GLU

ILE

SER

TYR

PRO

MET

15

ASN

PRO

ALA

MET

ASP

GLY

SER

LYS

SER

16

ALA

CYS

ASP

GLY

LEU

ASP

LEU

ILE

PHE

17

TRP

GLU

ASP

LEU

TYR

THR

SER

Samples:

sample_1: ANAC046(172-338) monomer, [U-13C; U-15N], 80 uM; HEPES 20 mM; sodium chloride 100 mM; TCEP 1 mM; D2O 10 % v/v; DSS 250 uM; sodium azide 1 % v/v

sample_2: ANAC046(172-338) monomer, [U-13C; U-15N], 500 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; D2O 10 % v/v; DSS 250 uM; sodium azide 1 % v/v

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

NMRPipe - processing

qMDD - processing

CcpNMR - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 750 MHz

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