BMRB Entry 17455

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human TrJ disease-related mutant form of PMP22
Published: 2011-08-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17455

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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, 13C, and 15N Chemical Shift Assignments for human TrJ disease-related mutant form of PMP22

Deposition date:

2011-02-10

Original release date:

2011-08-17

Authors:

Sakakura, Masayoshi; Hadziselimovic, Arina; Wang, Zhen; Schey, Kevin; Sanders, Charles

Citation:

Citation: Sakakura, Masayoshi; Hadziselimovic, Arina; Wang, Zhen; Schey, Kevin; Sanders, Charles. "Structural basis for the trembler-j phenotype of charcot-marie-tooth disease." Structure 19, 1160-1169 (2011).
PubMed: 21827951

Assembly members:

Assembly members:
TrJ-PMP22, polymer, 173 residues, 19260.56 Da.

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: pAH13.1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TrJ-PMP22: GSGWSHPQFEKGSMLLLLLS IIVLHVAVPVLLFVSTIVSQ WIVGNGHATDLWQNCSTSSS GNVHHCFSSSPNEWLQSVQA TMILSIIFSILSLFLFFCQL FTLTKGGRFYITGIFQILAG LCVMSAAAIYTVRHPEWHLN SDYSYGFAYILAWVAFPLAL LSGVIYVILRKRE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	82
15N chemical shifts	74
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	membrane protein	1

Entities:

Entity 1, membrane protein 173 residues - 19260.56 Da.

Residues 1-13 represent a non-native tag

1

GLY

SER

GLY

TRP

SER

HIS

PRO

GLN

PHE

GLU

2

LYS

GLY

SER

MET

LEU

SER

3

ILE

VAL

LEU

HIS

VAL

ALA

VAL

PRO

VAL

4

LEU

PHE

VAL

SER

THR

ILE

VAL

SER

GLN

5

TRP

ILE

VAL

GLY

ASN

GLY

HIS

ALA

THR

ASP

6

LEU

TRP

GLN

ASN

CYS

SER

THR

SER

7

GLY

ASN

VAL

HIS

CYS

PHE

SER

8

PRO

ASN

GLU

TRP

LEU

GLN

SER

VAL

GLN

ALA

9

THR

MET

ILE

LEU

SER

ILE

PHE

SER

ILE

10

LEU

SER

LEU

PHE

LEU

PHE

CYS

GLN

LEU

11

PHE

THR

LEU

THR

LYS

GLY

ARG

PHE

TYR

12

ILE

THR

GLY

ILE

PHE

GLN

ILE

LEU

ALA

GLY

13

LEU

CYS

VAL

MET

SER

ALA

ILE

TYR

14

THR

VAL

ARG

HIS

PRO

GLU

TRP

HIS

LEU

ASN

15

SER

ASP

TYR

SER

TYR

GLY

PHE

ALA

TYR

ILE

16

LEU

ALA

TRP

VAL

ALA

PHE

PRO

LEU

ALA

LEU

17

LEU

SER

GLY

VAL

ILE

TYR

VAL

ILE

LEU

ARG

18

LYS

ARG

GLU

Samples:

sample_1: TrJ-PMP22, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%; sodium acetate 10 mM; EDTA 1 mM; DTT 10 mM; tetradecylphosphocholine 216 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 5; pressure: 1 atm; temperature: 318 K

Experiments:

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

Software:

TOPSPIN v1.3 and 2.1, Bruker Biospin - collection (v1.3), processing (v2.1)

SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking

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