BMRB Entry 5843

Name: Solution Structure of At3g17210
Published: 2003-07-17

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PDB ID: 1q53
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR5843
MolProbity Validation Chart

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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 At3g17210

Deposition date:

2003-06-25

Original release date:

2003-07-17

Authors:

Volkman, B.

Citation:

Citation: Lytle, Betsy; Peterson, Francis; Kjer, Kelly; Frederick, Ronnie; Zhao, Qin; Thao, Sandy; Bingman, Craig; Johnson, Kenneth; Phillips, Georage; Volkman, Brian. "Letter to the Editor: Structure of the hypothetical protein At3g17210 from Arabidopsis thaliana" J. Biomol. NMR 28, 397-400 (2004).

Assembly members:

Assembly members:
expressed protein At3g17210.1, polymer, 112 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
expressed protein At3g17210.1: GSHMEEAKGPVKHVLLASFK DGVSPEKIEELIKGYANLVN LIEPMKAFHWGKDVSIENLH QGYTHIFESTFESKEAVAEY IAHPAHVEFATIFLGSLDKV LVIDYKPTSVSL

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	776
13C chemical shifts	493
15N chemical shifts	111

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical protein At3g17210, chain 1	1
2	hypothetical protein At3g17210, chain 2	1

Entities:

Entity 1, hypothetical protein At3g17210, chain 1 112 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLU

ALA

LYS

GLY

PRO

2

VAL

LYS

HIS

VAL

LEU

ALA

SER

PHE

LYS

3

ASP

GLY

VAL

SER

PRO

GLU

LYS

ILE

GLU

4

LEU

ILE

LYS

GLY

TYR

ALA

ASN

LEU

VAL

ASN

5

LEU

ILE

GLU

PRO

MET

LYS

ALA

PHE

HIS

TRP

6

GLY

LYS

ASP

VAL

SER

ILE

GLU

ASN

LEU

HIS

7

GLN

GLY

TYR

THR

HIS

ILE

PHE

GLU

SER

THR

8

PHE

GLU

SER

LYS

GLU

ALA

VAL

ALA

GLU

TYR

9

ILE

ALA

HIS

PRO

ALA

HIS

VAL

GLU

PHE

ALA

10

THR

ILE

PHE

LEU

GLY

SER

LEU

ASP

LYS

VAL

11

LEU

VAL

ILE

ASP

TYR

LYS

PRO

THR

SER

VAL

12

SER

LEU

Samples:

sample_1: expressed protein At3g17210.1, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 70 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	not available	sample_cond_1
3D 13C-separated NOESY	sample_1	not available	sample_cond_1
3D HNCO	sample_1	not available	sample_cond_1
3D HNCACO	sample_1	not available	sample_cond_1
3D HNCA	sample_1	not available	sample_cond_1
3D HNCOCA	sample_1	not available	sample_cond_1
3D HNCACB	sample_1	not available	sample_cond_1
3D CCONH	sample_1	not available	sample_cond_1
3D 15N-edited TOCSY-HSQC	sample_1	not available	sample_cond_1
HCCH-TOCSY	sample_1	not available	sample_cond_1
15N-1H HSQC	sample_1	not available	sample_cond_1
3D 13C-separated NOESY (arom)	sample_1	not available	sample_cond_1

Software:

XWINNMR v3.0 - collection

NMRPIPE v97.027.12.56 - processing

XEASY v1.4 - data analysis

CYANA v1.0.6 - structure solution, refinement

NMR spectrometers:

Bruker DMX 600 MHz

PDB	1Q4R 1Q53 2Q3P
DBJ	BAB02723 BAF02259
GB	AAK43839 AAL47379 AAM63750 AEE75921
REF	NP_566569
SP	Q9LUV2
AlphaFold	Q9LUV2