BMRB Entry 6590

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6590

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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:

1H, 13C, and 15N Chemical Shifts Assignments for Human Sulfiredoxin (srx)

Deposition date:

2005-04-12

Original release date:

2005-10-26

Authors:

Gruschus, James; Lee, Duck-Yeon; Rhee, Sue-Goo; Ferretti, James

Citation:

Citation: Lee, Duck-Yeon; Rhee, Sue-Goo; Ferretti, James; Gruschus, James. "1H, 15N, and 13C Chemical Shift Assignments of the Human Sulfiredoxin (hSrx)" J. Biomol. NMR 32, 339-339 (2005).

Assembly members:

Assembly members:
sulfiredoxin, polymer, 121 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: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
sulfiredoxin: GAPEGPGPSGGAQGGSIHSG RIAAVHNVPLSVLIRPLPSV LDPAKVQSLVDTIREDPDSV PPIDVLWIKGAQGGDYFYSF GGCHRYAAYQQLQRETIPAK LVQSTLSDLRVYLGASTPDL Q

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	401
15N chemical shifts	118
1H chemical shifts	820

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	srx monomer	1

Entities:

Entity 1, srx monomer 121 residues - Formula weight is not available

residues 17-137 of full length protein

1

GLY

ALA

PRO

GLU

GLY

PRO

GLY

PRO

SER

GLY

2

GLY

ALA

GLN

GLY

SER

ILE

HIS

SER

GLY

3

ARG

ILE

ALA

VAL

HIS

ASN

VAL

PRO

LEU

4

SER

VAL

LEU

ILE

ARG

PRO

LEU

PRO

SER

VAL

5

LEU

ASP

PRO

ALA

LYS

VAL

GLN

SER

LEU

VAL

6

ASP

THR

ILE

ARG

GLU

ASP

PRO

ASP

SER

VAL

7

PRO

ILE

ASP

VAL

LEU

TRP

ILE

LYS

GLY

8

ALA

GLN

GLY

ASP

TYR

PHE

TYR

SER

PHE

9

GLY

CYS

HIS

ARG

TYR

ALA

TYR

GLN

10

GLN

LEU

GLN

ARG

GLU

THR

ILE

PRO

ALA

LYS

11

LEU

VAL

GLN

SER

THR

LEU

SER

ASP

LEU

ARG

12

VAL

TYR

LEU

GLY

ALA

SER

THR

PRO

ASP

LEU

13

GLN

Samples:

sample_1: sulfiredoxin, [U-15N], 0.7 ± 0.1 mM; sodium phosphate 50 ± 1 mM; NaCl 100 ± 1 mM; DTT 2 ± .1 mM

sample_2: sulfiredoxin, [U-15N; U-13C], 0.7 ± 0.1 mM; sodium phosphate 50 ± 1 mM; NaCl 100 ± 1 mM; DTT 2 ± .1 mM

conditions_1: pH: 7.3; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N_HSQC	sample_1	isotropic	conditions_1
15N_edited_1H_NOESY_HSQC	sample_1	isotropic	conditions_1
1H13C_CT_HSQC	sample_2	isotropic	conditions_1
1H13C_HMQC	sample_2	isotropic	conditions_1
HNCACB	not available	isotropic	conditions_1
CBCA(CO)NH	not available	isotropic	conditions_1
13C_edited_1H_NOESY_shortCT_HSQC	sample_2	isotropic	conditions_1
13C_edited_1H_NOESY_HMQC	not available	isotropic	conditions_1

Software:

xwinnmr v3.1, Bruker -

NMRPipe v2.3 rev 2004.184.22.03, NIH -

NMR spectrometers:

Bruker Avance 800 MHz

PDB	1XW3 1XW4 1YZS 2B6F 2RII 3CYI 3HY2
DBJ	BAG34990
EMBL	CAD38799 CAL38018 CAL38719
GB	AAH17001 AAH32604 AAH47707 EFB29583
REF	NP_542763 XP_002830202 XP_002925451 XP_003273506 XP_003476813
SP	Q9BYN0
AlphaFold	Q9BYN0