BMRB Entry 15787

Name: 1H and 15N chemical shift assignments for HINT1 protein
Published: 2009-01-28

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15787

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H and 15N chemical shift assignments for HINT1 protein

Deposition date:

2008-05-29

Original release date:

2009-01-28

Authors:

Shapiro, Michael; Bai, Guoyun; Feng, Bo

Citation:

Citation: Bai, Guoyun; Feng, Bo; Wang, Jia Bei; Varney, Kristen; Shapiro, Michael. "Backbone assignment of HINT1 protein, a mouse histidine triad nucleotide binding protein" Biomol. NMR Assignments 3, 57-59 (2009).
PubMed: 19636947

Assembly members:

Assembly members:
HINT1, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HINT1: MADEIAKAQVAQPGGDTIFG KIIRKEIPAKIIFEDDRCLA FHDISPQAPTHFLVIPKKHI SQISVADDDDESLLGHLMIV GKKCAADLGLKRGYRMVVNE GADGGQSVYHIHLHVLGGRQ MNWPPG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	347
15N chemical shifts	116
1H chemical shifts	116

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HINT1	1

Entities:

Entity 1, HINT1 126 residues - Formula weight is not available

1

MET

ALA

ASP

GLU

ILE

ALA

LYS

ALA

GLN

VAL

2

ALA

GLN

PRO

GLY

ASP

THR

ILE

PHE

GLY

3

LYS

ILE

ARG

LYS

GLU

ILE

PRO

ALA

LYS

4

ILE

PHE

GLU

ASP

ARG

CYS

LEU

ALA

5

PHE

HIS

ASP

ILE

SER

PRO

GLN

ALA

PRO

THR

6

HIS

PHE

LEU

VAL

ILE

PRO

LYS

HIS

ILE

7

SER

GLN

ILE

SER

VAL

ALA

ASP

8

GLU

SER

LEU

GLY

HIS

LEU

MET

ILE

VAL

9

GLY

LYS

CYS

ALA

ASP

LEU

GLY

LEU

10

LYS

ARG

GLY

TYR

ARG

MET

VAL

ASN

GLU

11

GLY

ALA

ASP

GLY

GLN

SER

VAL

TYR

HIS

12

ILE

HIS

LEU

HIS

VAL

LEU

GLY

ARG

GLN

13

MET

ASN

TRP

PRO

GLY

Samples:

sample_1: HINT1, [U-98% 13C; U-98% 15N], 0.2 mM; D2O, [U-99% 2H], 10%; H2O 90%; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DMX 600 MHz
Varian Unity 500 MHz

DBJ	BAB22484 BAB28235
GB	AAC71076 AAH70415 AAH80296 AAI68732 EDL33521
REF	NP_001103077 NP_032274 XP_005350115
SP	P62959 P70349
AlphaFold	P62959 P70349