BMRB Entry 15131

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15131

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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 assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein

Deposition date:

2007-02-13

Original release date:

2007-06-26

Authors:

Libich, David; Monette, Martine; Robertson, Valerie; Harauz, George

Citation:

Citation: Libich, David; Monette, Martine; Robertson, Valerie; Harauz, George. "NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein" Biomol. NMR Assignments 1, 61-63 (2007).
PubMed: 19636827

Assembly members:

Assembly members:
MBP, polymer, 176 residues, 19421.5 Da.

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: pET_22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MBP: ASQKRPSQRSKYLATASTMD HARHGFLPRHRDTGILDSIG RFFSGDRGAPKRGSGKDSHT RTTHYGSLPQKSQHGRTQDE NPVVHFFKNIVTPRTPPPSQ GKGRGLSLSRFSWGAEGQRP GFGYGGRASDYKSAHKGFKG AYDAQGTLSKIFKLGGRDSR SGSPMARRLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	401
15N chemical shifts	281
1H chemical shifts	571

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MBP	1

Entities:

Entity 1, MBP 176 residues - 19421.5 Da.

sequence includes a LEHHHHHH affinity tag (residues 169-176)

1

ALA

SER

GLN

LYS

ARG

PRO

SER

GLN

ARG

SER

2

LYS

TYR

LEU

ALA

THR

ALA

SER

THR

MET

ASP

3

HIS

ALA

ARG

HIS

GLY

PHE

LEU

PRO

ARG

HIS

4

ARG

ASP

THR

GLY

ILE

LEU

ASP

SER

ILE

GLY

5

ARG

PHE

SER

GLY

ASP

ARG

GLY

ALA

PRO

6

LYS

ARG

GLY

SER

GLY

LYS

ASP

SER

HIS

THR

7

ARG

THR

HIS

TYR

GLY

SER

LEU

PRO

GLN

8

LYS

SER

GLN

HIS

GLY

ARG

THR

GLN

ASP

GLU

9

ASN

PRO

VAL

HIS

PHE

LYS

ASN

ILE

10

VAL

THR

PRO

ARG

THR

PRO

SER

GLN

11

GLY

LYS

GLY

ARG

GLY

LEU

SER

LEU

SER

ARG

12

PHE

SER

TRP

GLY

ALA

GLU

GLY

GLN

ARG

PRO

13

GLY

PHE

GLY

TYR

GLY

ARG

ALA

SER

ASP

14

TYR

LYS

SER

ALA

HIS

LYS

GLY

PHE

LYS

GLY

15

ALA

TYR

ASP

ALA

GLN

GLY

THR

LEU

SER

LYS

16

ILE

PHE

LYS

LEU

GLY

ARG

ASP

SER

ARG

17

SER

GLY

SER

PRO

MET

ALA

ARG

LEU

GLU

18

HIS

Samples:

15N-MBP: MBP, [U-15N], 1.47 mM; potassium chloride 100 mM; D2O, [U-2H], 10%

15N_13C-MBP: MBP, [U-13C; U-15N], 2.0 mM; potassium chloride 100 mM; D2O, [U-2H], 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 277 K

sample_conditions_2: pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-MBP	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_13C-MBP	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C-MBP	isotropic	sample_conditions_1
3D HNCACB	15N_13C-MBP	isotropic	sample_conditions_1
3D H(CCO)NH	15N_13C-MBP	isotropic	sample_conditions_1
3D HBHA(CO)NH	15N_13C-MBP	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

CARA v1.5.3, Rochus Keller - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 600 MHz

GB	AAA37720 AAA39496 AAA39501 EDL09385
REF	NP_001020426 NP_001020463 NP_034907 XP_006526519 XP_013204950
SP	P04370
AlphaFold	P04370