BMRB Entry 10336

Name: Solution structure of the DUF1000 domain of a thioredoxin-like protein 1
Published: 2010-12-09

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PDB ID: 1wwy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10336
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the DUF1000 domain of a thioredoxin-like protein 1

Deposition date:

2009-12-09

Original release date:

2010-12-09

Authors:

Goroncy, A.; Kigawa, T.; Koshiba, S.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Goroncy, Alexander; Koshiba, Seizo; Tochio, Naoya; Tomizawa, Tadashi; Inoue, Makoto; Tanaka, Akiko; Sugano, Sumio; Kigawa, Takanori; Yokoyama, Shigeyuki. "Solution structure of the C-terminal DUF1000 domain of the human thioredoxin-like 1 protein" Proteins 78, 2176-2180 (2010).
PubMed: 20455272

Assembly members:

Assembly members:
DUF1000 domain, polymer, 171 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: Cell free synthesis Vector: P040621-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DUF1000 domain: GSSGSSGGYMDLMPFINKAG CECLNESDEHGFDNCLRKDT TFLESDCDEQLLITVAFNQP VKLYSMKFQGPDNGQGPKYV KIFINLPRSMDFEEAERSEP TQALELTEDDIKEDGIVPLR YVKFQNVNSVTIFVQSNQGE EETTRISYFTFIGTPVQATN MNDFKSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	752
15N chemical shifts	183
1H chemical shifts	1172

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DUF1000 domain	1

Entities:

Entity 1, DUF1000 domain 171 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

TYR

MET

2

ASP

LEU

MET

PRO

PHE

ILE

ASN

LYS

ALA

GLY

3

CYS

GLU

CYS

LEU

ASN

GLU

SER

ASP

GLU

HIS

4

GLY

PHE

ASP

ASN

CYS

LEU

ARG

LYS

ASP

THR

5

THR

PHE

LEU

GLU

SER

ASP

CYS

ASP

GLU

GLN

6

LEU

ILE

THR

VAL

ALA

PHE

ASN

GLN

PRO

7

VAL

LYS

LEU

TYR

SER

MET

LYS

PHE

GLN

GLY

8

PRO

ASP

ASN

GLY

GLN

GLY

PRO

LYS

TYR

VAL

9

LYS

ILE

PHE

ILE

ASN

LEU

PRO

ARG

SER

MET

10

ASP

PHE

GLU

ALA

GLU

ARG

SER

GLU

PRO

11

THR

GLN

ALA

LEU

GLU

LEU

THR

GLU

ASP

12

ILE

LYS

GLU

ASP

GLY

ILE

VAL

PRO

LEU

ARG

13

TYR

VAL

LYS

PHE

GLN

ASN

VAL

ASN

SER

VAL

14

THR

ILE

PHE

VAL

GLN

SER

ASN

GLN

GLY

GLU

15

GLU

THR

ARG

ILE

SER

TYR

PHE

THR

16

PHE

ILE

GLY

THR

PRO

VAL

GLN

ALA

THR

ASN

17

MET

ASN

ASP

PHE

LYS

SER

GLY

PRO

SER

18

GLY

Samples:

sample_1: DUF1000 domain, [U-13C; U-15N], 1.02 mM; Tris-d11-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1
CBCACONH	sample_1	isotropic	condition_1
CCCONNH	sample_1	isotropic	condition_1
CCH TOCSY	sample_1	isotropic	condition_1
HBHACONH	sample_1	isotropic	condition_1
HCCCONNH	sample_1	isotropic	condition_1
HCCH COSY	sample_1	isotropic	condition_1
HCCH TOCSY	sample_1	isotropic	condition_1
3D HNCA	sample_1	isotropic	condition_1
3D HNCACB	sample_1	isotropic	condition_1
3D HNCACO	sample_1	isotropic	condition_1
3D HNCO	sample_1	isotropic	condition_1
3D HNCOCA	sample_1	isotropic	condition_1
C13 HSQC	sample_1	isotropic	condition_1
N15 HSQC	sample_1	isotropic	condition_1
3D 1H-13C NOESY-HSQC	sample_1	isotropic	condition_1
3D 1H-15N NOESY-HSQC	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v20020425, FRANK DELAGLIO - processing

NMRView v5.0.4, BRUCE A. JOHNSON - data analysis

Kujira v0.896, NAOHIRO KOBAYASHI - data analysis

CYANA v2, PETER GUENTERT - refinement

NMR spectrometers:

Bruker AVANCE 900 MHz

PDB	1WWY
DBJ	BAC26626 BAD92500 BAE25774 BAE29469 BAE29934
GB	AAC05830 AAC39599 AAC39898 AAC40183 AAF66676
REF	NP_001071354 NP_001131150 NP_001231205 NP_001248637 NP_004777
SP	O43396 Q8CDN6 Q920J4
TPG	DAA15792
AlphaFold	O43396 Q8CDN6 Q920J4