BMRB Entry 51029

Name: AMOTL1 178-384
Published: 2022-05-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51029

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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:

AMOTL1 178-384

Deposition date:

2021-07-24

Original release date:

2022-05-06

Authors:

Vogel, Amber; Nyarko, Afua

Citation:

Citation: Vogel, Amber; Crawford, Alexandra; Nyarko, Afua. "Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex" Protein Sci. 31, e4295-e4295 (2022).
PubMed: 35481651

Assembly members:

Assembly members:
entity_1, polymer, 207 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 Host organism: Escherichia coli Vector: pET24c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STQPQQNNEELPTYEEAKAQ SQFFRGQQQQQQQQGAVGHG YYMAGGTSQKSRTEGRPTVN RANSGQAHKDEALKELKQGH VRSLSERIMQLSLERNGAKQ HLPGSGNGKGFKVGGGPSPA QPAGKVLDPRGPPPEYPFKT KQMMSPVSKTQEHGLFYGDQ HPGMLHEMVKPYPAPQPVRT DVAVLRYQPPPEYGVTSRPC QLPFPST

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	506
15N chemical shifts	154
1H chemical shifts	154

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AMOTL1	1

Entities:

Entity 1, AMOTL1 207 residues - Formula weight is not available

Residues 178-384

1

SER

THR

GLN

PRO

GLN

ASN

GLU

2

LEU

PRO

THR

TYR

GLU

ALA

LYS

ALA

GLN

3

SER

GLN

PHE

ARG

GLY

GLN

4

GLN

GLY

ALA

VAL

GLY

HIS

GLY

5

TYR

MET

ALA

GLY

THR

SER

GLN

LYS

6

SER

ARG

THR

GLU

GLY

ARG

PRO

THR

VAL

ASN

7

ARG

ALA

ASN

SER

GLY

GLN

ALA

HIS

LYS

ASP

8

GLU

ALA

LEU

LYS

GLU

LEU

LYS

GLN

GLY

HIS

9

VAL

ARG

SER

LEU

SER

GLU

ARG

ILE

MET

GLN

10

LEU

SER

LEU

GLU

ARG

ASN

GLY

ALA

LYS

GLN

11

HIS

LEU

PRO

GLY

SER

GLY

ASN

GLY

LYS

GLY

12

PHE

LYS

VAL

GLY

PRO

SER

PRO

ALA

13

GLN

PRO

ALA

GLY

LYS

VAL

LEU

ASP

PRO

ARG

14

GLY

PRO

GLU

TYR

PRO

PHE

LYS

THR

15

LYS

GLN

MET

SER

PRO

VAL

SER

LYS

THR

16

GLN

GLU

HIS

GLY

LEU

PHE

TYR

GLY

ASP

GLN

17

HIS

PRO

GLY

MET

LEU

HIS

GLU

MET

VAL

LYS

18

PRO

TYR

PRO

ALA

PRO

GLN

PRO

VAL

ARG

THR

19

ASP

VAL

ALA

VAL

LEU

ARG

TYR

GLN

PRO

20

PRO

GLU

TYR

GLY

VAL

THR

SER

ARG

PRO

CYS

21

GLN

LEU

PRO

PHE

PRO

SER

THR

Samples:

sample_1: AMOTL1, [U-100% 13C; U-100% 15N], 200 uM; D2O, [U-100% 2H], 10%; DSS 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; arginine 50 mM; glutamate 50 mM; sodium azide 1 mM; TCEP 2 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 283.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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