BMRB Entry 27254

Name: Molten globule of L94G mutant of horse cytochrome-c
Published: 2019-11-08

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27254

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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:

Molten globule of L94G mutant of horse cytochrome-c

Deposition date:

2017-09-15

Original release date:

2019-11-08

Authors:

Naiyer, Abdullah; Islam, Asimul; Hassan, Md.Imtaiyaz; Sundd, Monica; Ahmad, Faizan

Citation:

Citation: Naiyer, Abdullah; Islam, Asimul; Hassan, Md.Imtaiyaz; Ahmad, Faizan; Sundd, Monica. "Backbone and side chain 1H, 15N and 13C chemical shift assignments of the molten globule state of L94G mutant of horse cytochrome-c" Biomol. NMR Assign. 14, 37-44 (2020).
PubMed: 31686356

Assembly members:

Assembly members:
Cyt_c, polymer, 104 residues, Formula weight is not available
HEME C, non-polymer, 618.503 Da.

Natural source:

Natural source: Common Name: Horse Taxonomy ID: 9796 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Equus caballus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cyt_c: GDVEKGKKIFVQKCAQCHTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYIDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDGIAYLKK ATNE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	453
15N chemical shifts	99
1H chemical shifts	705

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	horse cytochrome c	1
2	HEME C	2

Entities:

Entity 1, horse cytochrome c 104 residues - Formula weight is not available

1

GLY

ASP

VAL

GLU

LYS

GLY

LYS

ILE

PHE

2

VAL

GLN

LYS

CYS

ALA

GLN

CYS

HIS

THR

VAL

3

GLU

LYS

GLY

LYS

HIS

LYS

THR

GLY

PRO

4

ASN

LEU

HIS

GLY

LEU

PHE

GLY

ARG

LYS

THR

5

GLY

GLN

ALA

PRO

GLY

PHE

THR

TYR

THR

ASP

6

ALA

ASN

LYS

ASN

LYS

GLY

ILE

THR

TRP

LYS

7

GLU

THR

LEU

MET

GLU

TYR

LEU

GLU

ASN

8

PRO

LYS

TYR

ILE

PRO

GLY

THR

LYS

MET

9

ILE

PHE

ALA

GLY

ILE

LYS

THR

GLU

10

ARG

GLU

ASP

GLY

ILE

ALA

TYR

LEU

LYS

11

ALA

THR

ASN

GLU

Entity 2, HEME C - C34 H34 Fe N4 O4 - 618.503 Da.

1

HEC

Samples:

sample_1: Cyt_c, [U-99% 13C; U-99% 15N], 2 mM; NaCl 0.1 M

sample_conditions_1: ionic strength: 30 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY_CARA, Goddard, Keller and Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 700 MHz

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