BMRB Entry 36070

Name: NMR solution structure of the aromatic mutant H43W H67F cytochrome b5
Published: 2018-02-12

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PDB ID: 5xe4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36070
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of the aromatic mutant H43W H67F cytochrome b5 PubMed: 28738155

Deposition date: 2017-03-31 Original release date: 2018-02-12

Authors: Swati, B.; Siddhartha, P.

Citation: Balakrishnan, Swati; Sarma, Siddhartha. "Engineering Aromatic-Aromatic Interactions To Nucleate Folding in Intrinsically Disordered Regions of Proteins" Biochemistry 56, 4346-4359 (2017).

Assembly members:
Cytochrome b5, polymer, 98 residues, 11314.472 Da.

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Cytochrome b5: AEQSDKDVKYYTLEEIQKHK DSKSTWVILHHKVYDLTKFL EEWPGGEEVLREQAGGDATE NFEDVGFSTDARELSKKYII GELHPDDRSKIAKPSETL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	196
15N chemical shifts	83
1H chemical shifts	636

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 98 residues - 11314.472 Da.

1

ALA

GLU

GLN

SER

ASP

LYS

ASP

VAL

LYS

TYR

2

TYR

THR

LEU

GLU

ILE

GLN

LYS

HIS

LYS

3

ASP

SER

LYS

SER

THR

TRP

VAL

ILE

LEU

HIS

4

HIS

LYS

VAL

TYR

ASP

LEU

THR

LYS

PHE

LEU

5

GLU

TRP

PRO

GLY

GLU

VAL

LEU

6

ARG

GLU

GLN

ALA

GLY

ASP

ALA

THR

GLU

7

ASN

PHE

GLU

ASP

VAL

GLY

PHE

SER

THR

ASP

8

ALA

ARG

GLU

LEU

SER

LYS

TYR

ILE

9

GLY

GLU

LEU

HIS

PRO

ASP

ARG

SER

LYS

10

ILE

ALA

LYS

PRO

SER

GLU

THR

LEU

Samples:

sample_1: WF cytochrome b5, [U-99% 15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%; potassium phosphate 20 mM; sodium chloride 20 mM; Proline+Arginine+Glutamate 20 mM

sample_2: WF cytochrome b5, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%; potassium phosphate 20 mM; sodium chloride 20 mM; Proline+Arginine+Glutamate 20 mM

sample_conditions_1: ionic strength: 60 mM; pH: 7 .; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D NOESY-HSQC	sample_1	isotropic	sample_conditions_1
2D NOE	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Varian Uniform NMR System 600 MHz
Bruker Avance 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts