BMRB Entry 26819

Name: 1H, 13C and 15N backbone and side chain chemical shift assignments of CHIP-TPR
Published: 2016-10-13

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26819

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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 backbone and side chain chemical shift assignments of CHIP-TPR

Deposition date:

2016-06-17

Original release date:

2016-10-13

Authors:

Zhang, Huaqun; Page, Richard

Citation:

Citation: Zhang, Huaqun; McGlone, Cameron; Mannion, Matthew; Page, Richard. "1H, 15N and 13C resonance assignments for free and IEEVD peptide-bound forms of the tetratricopeptide repeat domain from the human E3 ubiquitin ligase CHIP" Biomol. NMR Assign. 11, 5-9 (2016).
PubMed: 27709416

Assembly members:

Assembly members:
CHIP-TPR, polymer, 139 residues, 15860 Da.
Hsp70p1, polymer, 8 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: pHis//2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CHIP-TPR: GAMGSEKSPSAQELKEQGNR LFVGRKYPEAAACYGRAITR NPLVAVYYTNRALCYLKMQQ HEQALADCRRALELDGQSVK AHFFLGQCQLEMESYDEAIA NLQRAYSLAKEQRLNFGDDI PSALRIAKKKRWNSIEERR
Hsp70p1: GPTIEEVD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	362
15N chemical shifts	121
1H chemical shifts	121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CHIP-TPR	1
2	Hsp70p1	2

Entities:

Entity 1, CHIP-TPR 139 residues - 15860 Da.

Residues 1-5 are from a non-native affinity tag after cleavage by TEV protease.

1

GLY

ALA

MET

GLY

SER

GLU

LYS

SER

PRO

SER

2

ALA

GLN

GLU

LEU

LYS

GLU

GLN

GLY

ASN

ARG

3

LEU

PHE

VAL

GLY

ARG

LYS

TYR

PRO

GLU

ALA

4

ALA

CYS

TYR

GLY

ARG

ALA

ILE

THR

ARG

5

ASN

PRO

LEU

VAL

ALA

VAL

TYR

THR

ASN

6

ARG

ALA

LEU

CYS

TYR

LEU

LYS

MET

GLN

7

HIS

GLU

GLN

ALA

LEU

ALA

ASP

CYS

ARG

8

ALA

LEU

GLU

LEU

ASP

GLY

GLN

SER

VAL

LYS

9

ALA

HIS

PHE

LEU

GLY

GLN

CYS

GLN

LEU

10

GLU

MET

GLU

SER

TYR

ASP

GLU

ALA

ILE

ALA

11

ASN

LEU

GLN

ARG

ALA

TYR

SER

LEU

ALA

LYS

12

GLU

GLN

ARG

LEU

ASN

PHE

GLY

ASP

ILE

13

PRO

SER

ALA

LEU

ARG

ILE

ALA

LYS

14

ARG

TRP

ASN

SER

ILE

GLU

ARG

Entity 2, Hsp70p1 8 residues - Formula weight is not available

1

GLY

PRO

THR

ILE

GLU

VAL

ASP

Samples:

sample_1: CHIP-TPR, [U-100% 15N], 0.4 – 0.5 mM; sodium chloride 150 mM; HEPES 20 mM; beta-mercaptoethanol 5 mM; Hsp70p11.5 – 2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

SPARKY v3.115, Goddard - chemical shift assignment

NMRDraw v8.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - refinement

NMRPipe v2012.090.12.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz

UNP	Q9UNE7 P0DMV8
AlphaFold	Q9HBT1 Q9UQM0