BMRB Entry 26962

Name: Backbone resonance assignment of insect arylalkylamine N-acetyltransferase from bombyx mori reveals conformational heterogeneity
Published: 2017-03-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26962

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:

Backbone resonance assignment of insect arylalkylamine N-acetyltransferase from bombyx mori reveals conformational heterogeneity

Deposition date:

2016-11-29

Original release date:

2017-03-02

Authors:

Aboalroub, Adam; Zhang, Ziming; Keramisanou, Dimitra; Gelis, Ioannis

Citation:

Citation: Aboalroub, Adam; Zhang, ziming; Keramisanou, Dimitra; Gelis, Ioannis. "Backbone resonance assignment of an insect arylalkylamine N-acetyltransferase from Bombyx mori reveals conformational heterogeneity" J. Biomol. NMR 11, 105-109 (2017).
PubMed: 28236225

Assembly members:

Assembly members:
bmAANAT3, polymer, 216 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
bmAANAT3: GSHMADFVVVMPSMKDAVIQ HLRDSFFADEPLNKAVGLCE RGQPHAALERLCLATMTDGL SIAAMDGDKVLGVALNGILR HGDIEQSIEKIKQSTDEKFN KIFNILYTVSRDLNLFNTFE VDLIMECRIISVHENARGRG LAKELMKRSIDLARDNEFKL FKVDATGAFSQRICRSLSLE ELKSVRYDEYCDESGTPIFR VPPPDHALCVMILKLP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	601
15N chemical shifts	197
1H chemical shifts	197

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	bmAANAT3	1

Entities:

Entity 1, bmAANAT3 216 residues - Formula weight is not available

The three amino acids GSH remain after thrombin cleavage.

1

GLY

SER

HIS

MET

ALA

ASP

PHE

VAL

2

MET

PRO

SER

MET

LYS

ASP

ALA

VAL

ILE

GLN

3

HIS

LEU

ARG

ASP

SER

PHE

ALA

ASP

GLU

4

PRO

LEU

ASN

LYS

ALA

VAL

GLY

LEU

CYS

GLU

5

ARG

GLY

GLN

PRO

HIS

ALA

LEU

GLU

ARG

6

LEU

CYS

LEU

ALA

THR

MET

THR

ASP

GLY

LEU

7

SER

ILE

ALA

MET

ASP

GLY

ASP

LYS

VAL

8

LEU

GLY

VAL

ALA

LEU

ASN

GLY

ILE

LEU

ARG

9

HIS

GLY

ASP

ILE

GLU

GLN

SER

ILE

GLU

LYS

10

ILE

LYS

GLN

SER

THR

ASP

GLU

LYS

PHE

ASN

11

LYS

ILE

PHE

ASN

ILE

LEU

TYR

THR

VAL

SER

12

ARG

ASP

LEU

ASN

LEU

PHE

ASN

THR

PHE

GLU

13

VAL

ASP

LEU

ILE

MET

GLU

CYS

ARG

ILE

14

SER

VAL

HIS

GLU

ASN

ALA

ARG

GLY

ARG

GLY

15

LEU

ALA

LYS

GLU

LEU

MET

LYS

ARG

SER

ILE

16

ASP

LEU

ALA

ARG

ASP

ASN

GLU

PHE

LYS

LEU

17

PHE

LYS

VAL

ASP

ALA

THR

GLY

ALA

PHE

SER

18

GLN

ARG

ILE

CYS

ARG

SER

LEU

SER

LEU

GLU

19

GLU

LEU

LYS

SER

VAL

ARG

TYR

ASP

GLU

TYR

20

CYS

ASP

GLU

SER

GLY

THR

PRO

ILE

PHE

ARG

21

VAL

PRO

ASP

HIS

ALA

LEU

CYS

VAL

22

MET

ILE

LEU

LYS

LEU

PRO

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 26962

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: