BMRB Entry 25607

Name: 1H, 13C and 15N assignment of HA, HB, HN, CA, CB, C' and N of human Androgen Receptor-25Q
Published: 2017-02-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25607

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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 assignment of HA, HB, HN, CA, CB, C' and N of human Androgen Receptor-25Q

Deposition date:

2015-05-12

Original release date:

2017-02-08

Authors:

Eftekharzadeh, Bahareh; Piai, Alessandro; Chiesa, Giulio; Garcia, Jesus; Pierattelli, Roberta; Felli, Isabella; Salvatella, Xavier

Citation:

Citation: Eftekharzadeh, Bahareh; Piai, Alessandro; Chiesa, Giulio; Garcia, Jesus; Pierattelli, Roberta; Felli, Isabella; Salvatella, Xavier. "Sequence Context Influences the Structure and Aggregation Behavior of a PolyQ Tract" Biophys. J. 110, 2361-2366 (2016).
PubMed: 27276254

Assembly members:

Assembly members:
AR-25Q, polymer, 156 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: pDEST-HisMBP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AR-25Q: GMEVQLGLGRVYPRPPSKTY RGAFQNLFQSVREVIQNPGP RHPEAASAAPPGASLLLLQQ QQQQQQQQQQQQQQQQQQQQ QQQETSPRQQQQQQGEDGSP QAHRRGPTGYLVLDEEQQPS QPQSALECHPERGCVPEPGA AVAASKGLPQQLPAPP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	154
1H chemical shifts	554

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AR-25Q	1

Entities:

Entity 1, AR-25Q 156 residues - Formula weight is not available

1

GLY

MET

GLU

VAL

GLN

LEU

GLY

LEU

GLY

ARG

2

VAL

TYR

PRO

ARG

PRO

SER

LYS

THR

TYR

3

ARG

GLY

ALA

PHE

GLN

ASN

LEU

PHE

GLN

SER

4

VAL

ARG

GLU

VAL

ILE

GLN

ASN

PRO

GLY

PRO

5

ARG

HIS

PRO

GLU

ALA

SER

ALA

PRO

6

PRO

GLY

ALA

SER

LEU

GLN

7

GLN

8

GLN

9

GLN

GLU

THR

SER

PRO

ARG

GLN

10

GLN

GLY

GLU

ASP

GLY

SER

PRO

11

GLN

ALA

HIS

ARG

GLY

PRO

THR

GLY

TYR

12

LEU

VAL

LEU

ASP

GLU

GLN

PRO

SER

13

GLN

PRO

GLN

SER

ALA

LEU

GLU

CYS

HIS

PRO

14

GLU

ARG

GLY

CYS

VAL

PRO

GLU

PRO

GLY

ALA

15

ALA

VAL

ALA

SER

LYS

GLY

LEU

PRO

GLN

16

GLN

LEU

PRO

ALA

PRO

Samples:

sample_1: AR-25Q, [U-100% 13C; U-100% 15N], 0.4 mM; sodium phosphate 20 mM; TCEP 1 mM

sample_conditions_1: pH: 7.4; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D CON-IPAP	sample_1	isotropic	sample_conditions_1
4D HCBCACON-IPAP	sample_1	isotropic	sample_conditions_1
4D HCBCANCO-IPAP	sample_1	isotropic	sample_conditions_1
4D (HN)CON(CA)CON	sample_1	isotropic	sample_conditions_1
3D TROSY HNCO	sample_1	isotropic	sample_conditions_1
3D TROSY HN(CA)CO	sample_1	isotropic	sample_conditions_1
4D TROSY HN(COCA)NNH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 950 MHz

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