BMRB Entry 27614

Name: NMR resonance assignments of the TPR domain of human AIPL1
Published: 2019-09-17

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27614

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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:

NMR resonance assignments of the TPR domain of human AIPL1

Deposition date:

2018-09-16

Original release date:

2019-09-17

Authors:

Yu, Liping; Yadav, Ravi; Artemyev, Nikolai

Citation:

Citation: Yu, Liping; Yadav, Ravi; Artemyev, Nikolai. "NMR resonance assignments of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1)" Biomol. NMR Assign. 13, 79-83 (2019).
PubMed: 30341566

Assembly members:

Assembly members:
AIPL1-TPR, polymer, 155 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AIPL1-TPR: MGHHHHHHGNHEKMKAVPVL HGEGNRLFKLGRYEEASSKY QEAIICLRNLQTKEKPWEVQ WLKLEKMINTLILNYCQCLL KKEEYYEVLEHTSDILRHHP GIVKAYYVRARAHAEVWNEA EAKADLQKVLELEPSMQKAV RRELRLLENRMAEKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	404
15N chemical shifts	129
1H chemical shifts	257

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AIPL1-TPR	1

Entities:

Entity 1, AIPL1-TPR 155 residues - Formula weight is not available

1

MET

GLY

HIS

GLY

ASN

2

HIS

GLU

LYS

MET

LYS

ALA

VAL

PRO

VAL

LEU

3

HIS

GLY

GLU

GLY

ASN

ARG

LEU

PHE

LYS

LEU

4

GLY

ARG

TYR

GLU

ALA

SER

LYS

TYR

5

GLN

GLU

ALA

ILE

CYS

LEU

ARG

ASN

LEU

6

GLN

THR

LYS

GLU

LYS

PRO

TRP

GLU

VAL

GLN

7

TRP

LEU

LYS

LEU

GLU

LYS

MET

ILE

ASN

THR

8

LEU

ILE

LEU

ASN

TYR

CYS

GLN

CYS

LEU

9

LYS

GLU

TYR

GLU

VAL

LEU

GLU

10

HIS

THR

SER

ASP

ILE

LEU

ARG

HIS

PRO

11

GLY

ILE

VAL

LYS

ALA

TYR

VAL

ARG

ALA

12

ARG

ALA

HIS

ALA

GLU

VAL

TRP

ASN

GLU

ALA

13

GLU

ALA

LYS

ALA

ASP

LEU

GLN

LYS

VAL

LEU

14

GLU

LEU

GLU

PRO

SER

MET

GLN

LYS

ALA

VAL

15

ARG

GLU

LEU

ARG

LEU

GLU

ASN

ARG

16

MET

ALA

GLU

LYS

GLN

Samples:

sample_1: AIPL1-TPR, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 700 mM; DTT 6.0 mM

sample_conditions_1: ionic strength: 1.62 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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