BMRB Entry 10090

Name: Solution structure of hypothetical protein F20O9.120 from Arabidopsis thaliana
Published: 2008-08-14

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PDB ID: 1wjj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10090
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 hypothetical protein F20O9.120 from Arabidopsis thaliana

Deposition date:

2007-01-24

Original release date:

2008-08-14

Authors:

Sato, M.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Sato, M.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of hypothetical protein F20O9.120 from Arabidopsis thaliana" .

Assembly members:

Assembly members:
residues 14-145, polymer, 145 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: cell free synthesis Vector: P020715-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
residues 14-145: GSSGSSGSTVKRKPVFVKVE QLKPGTTGHTLTVKVIEANI VVPVTRKTRPASSLSRPSQP SRIVECLIGDETGCILFTAR NDQVDLMKPGATVILRNSRI DMFKGTMRLGVDKWGRIEAT GAASFTVKEDNNLSLVEYES GPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	569
15N chemical shifts	130
1H chemical shifts	952

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical protein F20O9.120	1

Entities:

Entity 1, hypothetical protein F20O9.120 145 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

SER

THR

VAL

2

LYS

ARG

LYS

PRO

VAL

PHE

VAL

LYS

VAL

GLU

3

GLN

LEU

LYS

PRO

GLY

THR

GLY

HIS

THR

4

LEU

THR

VAL

LYS

VAL

ILE

GLU

ALA

ASN

ILE

5

VAL

PRO

VAL

THR

ARG

LYS

THR

ARG

PRO

6

ALA

SER

LEU

SER

ARG

PRO

SER

GLN

PRO

7

SER

ARG

ILE

VAL

GLU

CYS

LEU

ILE

GLY

ASP

8

GLU

THR

GLY

CYS

ILE

LEU

PHE

THR

ALA

ARG

9

ASN

ASP

GLN

VAL

ASP

LEU

MET

LYS

PRO

GLY

10

ALA

THR

VAL

ILE

LEU

ARG

ASN

SER

ARG

ILE

11

ASP

MET

PHE

LYS

GLY

THR

MET

ARG

LEU

GLY

12

VAL

ASP

LYS

TRP

GLY

ARG

ILE

GLU

ALA

THR

13

GLY

ALA

SER

PHE

THR

VAL

LYS

GLU

ASP

14

ASN

LEU

SER

LEU

VAL

GLU

TYR

GLU

SER

15

GLY

PRO

SER

GLY

Samples:

sample_1: residues 14-145, [U-13C; U-15N], 0.8 mM; d-Tris HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	condition_1
3D 15N-separated NOESY	sample_1	not available	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WJJ
EMBL	CAA16883 CAB79646
GB	AAK93582 AAL08288 AAM14346 AAM65628 AEE85487
REF	NP_194573 XP_002869502
SP	O49453
AlphaFold	O49453