BMRB Entry 52087

Name: C-terminal domain of AtBCCP1
Published: 2024-02-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52087

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

C-terminal domain of AtBCCP1

Deposition date:

2023-08-20

Original release date:

2024-02-19

Authors:

Shivaiah, Kiran-Kumar; Subedi, Ganesh; Barb, Adam; Nikolau, Basil

Citation:

Citation: Shivaiah, Kiran-Kumar; Subedi, Ganesh; Barb, Adam; Nikolau, Basil. "Solution Structure of C-terminal domain of the BCCP1 subunit of the Arabidopsis plastidic acetyl-CoA carboxylase" .

Assembly members:

Assembly members:
entity_1, polymer, 92 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: pET30f

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSENLYFQGSDPKSSLPTVK SPMAGTFYRSPAPGEPPFIK VGDKVQKGQVLCIVEAMKLM NEIESDHTGTVVDIVAEDGK PVSLDTPLFVVQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	344
15N chemical shifts	79
1H chemical shifts	564

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of AtBCCP1	1

Entities:

Entity 1, C-terminal domain of AtBCCP1 92 residues - Formula weight is not available

1

SER

GLU

ASN

LEU

TYR

PHE

GLN

GLY

SER

2

ASP

PRO

LYS

SER

LEU

PRO

THR

VAL

LYS

3

SER

PRO

MET

ALA

GLY

THR

PHE

TYR

ARG

SER

4

PRO

ALA

PRO

GLY

GLU

PRO

PHE

ILE

LYS

5

VAL

GLY

ASP

LYS

VAL

GLN

LYS

GLY

GLN

VAL

6

LEU

CYS

ILE

VAL

GLU

ALA

MET

LYS

LEU

MET

7

ASN

GLU

ILE

GLU

SER

ASP

HIS

THR

GLY

THR

8

VAL

ASP

ILE

VAL

ALA

GLU

ASP

GLY

LYS

9

PRO

VAL

SER

LEU

ASP

THR

PRO

LEU

PHE

VAL

10

VAL

GLN

Samples:

sample_1: entity_1 mM; sodium chloride 150 mM; DTT 2 mM; Phosphate buffer 20 mM; ammonium chloride, [U-100% 15N], 0.01%; Glucose, [U-100% 13C], 0.02%

sample_conditions_1: ionic strength: 20 mM; pH: 7.2; pressure: 1 atm; temperature: 303 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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - data analysis

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker Avance 700 MHz

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