BMRB Entry 53128

Name: Backbone 1H, 15N, 13C Resonance Assignment of p47 (101-266)
Published: 2025-11-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53128

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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:

Backbone 1H, 15N, 13C Resonance Assignment of p47 (101-266)

Deposition date:

2025-05-07

Original release date:

2025-11-12

Authors:

Raseekan, Rajivan; Black, Megan; Huang, Rui

Citation:

Citation: Raseekan, Rajivan; Black, Megan; Huang, Rui. "1H, 13C, and 15N backbone resonance assignments of full-length and a SIM-SEP-containing fragment (101-266) of p47, a p97 adaptor protein" Biomol. NMR Assign. 20, 1-1 (2025).
PubMed: 41188554

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GRSGQQIVGPPRKKSPNELV DDLFKGAKEHGAVAVERVTK SPGETSKPRPFAGGGYRLGA APEEESAYVAGERRRHSGQD VHVVLKLWKTGFSLDNGDLR SYQDPSNAQFLESIRRGEVP AELRRLAHGGQVNLDMEDHR DEDFVKPKGAFKAFTGEGQK LGSTAPQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	434
15N chemical shifts	142
1H chemical shifts	142

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p47	1

Entities:

Entity 1, p47 167 residues - Formula weight is not available

1

GLY

ARG

SER

GLY

GLN

ILE

VAL

GLY

PRO

2

PRO

ARG

LYS

SER

PRO

ASN

GLU

LEU

VAL

3

ASP

LEU

PHE

LYS

GLY

ALA

LYS

GLU

HIS

4

GLY

ALA

VAL

ALA

VAL

GLU

ARG

VAL

THR

LYS

5

SER

PRO

GLY

GLU

THR

SER

LYS

PRO

ARG

PRO

6

PHE

ALA

GLY

TYR

ARG

LEU

GLY

ALA

7

ALA

PRO

GLU

SER

ALA

TYR

VAL

ALA

8

GLY

GLU

ARG

HIS

SER

GLY

GLN

ASP

9

VAL

HIS

VAL

LEU

LYS

LEU

TRP

LYS

THR

10

GLY

PHE

SER

LEU

ASP

ASN

GLY

ASP

LEU

ARG

11

SER

TYR

GLN

ASP

PRO

SER

ASN

ALA

GLN

PHE

12

LEU

GLU

SER

ILE

ARG

GLY

GLU

VAL

PRO

13

ALA

GLU

LEU

ARG

LEU

ALA

HIS

GLY

14

GLN

VAL

ASN

LEU

ASP

MET

GLU

ASP

HIS

ARG

15

ASP

GLU

ASP

PHE

VAL

LYS

PRO

LYS

GLY

ALA

16

PHE

LYS

ALA

PHE

THR

GLY

GLU

GLY

GLN

LYS

17

LEU

GLY

SER

THR

ALA

PRO

GLN

Samples:

sample_1: p47 (101-266), [U-13C; U-15N; U-2H], 480 uM; Bis-tris 25 mM; sodium chloride 25 mM; EDTA 1 mM

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	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:

CcpNMR v3.2.12 - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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