BMRB Entry 6128

Name: Structure of At3g01050.1, a ubiquitin-fold protein from Arabidopsis thaliana
Published: 2004-05-15

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PDB ID: 1se9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR6128
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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:

Structure of At3g01050.1, a ubiquitin-fold protein from Arabidopsis thaliana

Deposition date:

2004-03-03

Original release date:

2004-05-15

Authors:

Lytle, B.; Peterson, F.; Volkman, B.; Markley, J.

Citation:

Citation: Vinarov, D.; Lytle, B.; Peterson, F.; Tyler, E.; Volkman, B.; Markley, J.. "Cell-free protein production and labeling protocol for NMR-based structural proteomics" Nat. Methods 1, 149-153 (2004).
PubMed: 15782178

Assembly members:

Assembly members:
At3g01050.1, polymer, 126 residues, 12821 Da.

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: cell free synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
At3g01050.1: MGHHHHHHLEAEVHNQLEIK FRLTDGSDIGPKAFPDATTV SALKETVISEWPREKENGPK TVKEVKLISAGKVLENSKTV KDYRSPVSNLAGAVTTMHVI IQAPVTEKEKKPKGDPKMNK CVCSVM

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
15N chemical shifts	116
1H chemical shifts	669
13C chemical shifts	502

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	At3g01050.1	1

Entities:

Entity 1, At3g01050.1 126 residues - 12821 Da.

1

MET

GLY

HIS

LEU

GLU

2

ALA

GLU

VAL

HIS

ASN

GLN

LEU

GLU

ILE

LYS

3

PHE

ARG

LEU

THR

ASP

GLY

SER

ASP

ILE

GLY

4

PRO

LYS

ALA

PHE

PRO

ASP

ALA

THR

VAL

5

SER

ALA

LEU

LYS

GLU

THR

VAL

ILE

SER

GLU

6

TRP

PRO

ARG

GLU

LYS

GLU

ASN

GLY

PRO

LYS

7

THR

VAL

LYS

GLU

VAL

LYS

LEU

ILE

SER

ALA

8

GLY

LYS

VAL

LEU

GLU

ASN

SER

LYS

THR

VAL

9

LYS

ASP

TYR

ARG

SER

PRO

VAL

SER

ASN

LEU

10

ALA

GLY

ALA

VAL

THR

MET

HIS

VAL

ILE

11

ILE

GLN

ALA

PRO

VAL

THR

GLU

LYS

GLU

LYS

12

LYS

PRO

LYS

GLY

ASP

PRO

LYS

MET

ASN

LYS

13

CYS

VAL

CYS

SER

VAL

MET

Samples:

sample_1: At3g01050.1, [U-13C; U-15N], 0.5 mM; KCl 50 mM; phosphate buffer 10 mM; DTT 1 mM; H20 90%; D20 10%

sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 60 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	sample_1	not available	sample_cond_1
HNCA	sample_1	not available	sample_cond_1
HNCO	sample_1	not available	sample_cond_1
HN(CO)CA	sample_1	not available	sample_cond_1
HNCACB	sample_1	not available	sample_cond_1
HN(CA)CO	sample_1	not available	sample_cond_1
C(CO)NH	sample_1	not available	sample_cond_1
HCCH-TOCSY	sample_1	not available	sample_cond_1
3D 15N-NOESY	sample_1	not available	sample_cond_1
3D 13C-NOESY	sample_1	not available	sample_cond_1
3D 13C-NOESY-aromatic	sample_1	not available	sample_cond_1
diffusion	sample_1	not available	sample_cond_1
N15 hetNOE	sample_1	not available	sample_cond_1

Software:

XWINNMR v3.1 - collection

NMRPipe v2.1 - processing

XEASY v1.3.1 - analysis

SPSCAN v1.1.0 - peak picking

GARANT v2.1 - automated backbone assignments

TALOS - generation of torsion angle restraints

CYANA v1.0.6 - refinement (torsion angle dynamics)

XPLOR-NIH v2.0.6 - refinement (cartesian MD in explicit solvent)

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1SE9
GB	AAF26169 AAR20718 AAS92335 AEE73600
REF	NP_186754
SP	Q9MAB9
AlphaFold	Q9MAB9