BMRB Entry 4801

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4801

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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:

Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, of the isolated c domain of Paracoccus pantotrophus in the oxidized state

Deposition date:

2000-08-04

Original release date:

2001-03-12

Authors:

Steensma, Elles; Gordon, Euan; Oster, Linda; Ferguson, Stuart; Hajdu, Janos

Citation:

Citation: Steensma, Elles; Gordon, Euan; Oster, Linda; Ferguson, Stuart; Hajdu, Janos. "Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase" J. Biol. Chem. 276, 5846-5855 (2001).

Assembly members:

Assembly members:
isolated oxidized c domain monomer, polymer, 133 residues, 14855 Da.
HEME C, non-polymer, 618.503 Da.

Natural source:

Natural source: Common Name: Paracoccus pantotrophus Taxonomy ID: 82367 Superkingdom: Eubacteria Kingdom: not available Genus/species: Paracoccus pantotrophus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
isolated oxidized c domain monomer: QEQVAPPKDPAAALEDHKTR TDNRYEPSLDNLAQQDVAAP GAPEGVSALSDAQYNEANKI YFERCAGCHGVLRKGATGKA LTPDLTRDLGFDYLQSFITY GSPAGMPNWGTSGELSAEQV DLMANYLLLDPAA

Data sets:

assigned_chemical_shifts
heteronucl_T1_relaxation
- T1_c_domain
- T1_heme

Data type	Count
1H chemical shifts	32
T1 relaxation values	8

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	isolated oxidized c domain monomer	1
2	oxidized heme	2

Entities:

Entity 1, isolated oxidized c domain monomer 133 residues - 14855 Da.

1

GLN

GLU

GLN

VAL

ALA

PRO

LYS

ASP

PRO

2

ALA

LEU

GLU

ASP

HIS

LYS

THR

ARG

3

THR

ASP

ASN

ARG

TYR

GLU

PRO

SER

LEU

ASP

4

ASN

LEU

ALA

GLN

ASP

VAL

ALA

PRO

5

GLY

ALA

PRO

GLU

GLY

VAL

SER

ALA

LEU

SER

6

ASP

ALA

GLN

TYR

ASN

GLU

ALA

ASN

LYS

ILE

7

TYR

PHE

GLU

ARG

CYS

ALA

GLY

CYS

HIS

GLY

8

VAL

LEU

ARG

LYS

GLY

ALA

THR

GLY

LYS

ALA

9

LEU

THR

PRO

ASP

LEU

THR

ARG

ASP

LEU

GLY

10

PHE

ASP

TYR

LEU

GLN

SER

PHE

ILE

THR

TYR

11

GLY

SER

PRO

ALA

GLY

MET

PRO

ASN

TRP

GLY

12

THR

SER

GLY

GLU

LEU

SER

ALA

GLU

GLN

VAL

13

ASP

LEU

MET

ALA

ASN

TYR

LEU

ASP

14

PRO

ALA

Entity 2, oxidized heme - C34 H34 Fe N4 O4 - 618.503 Da.

1

HEC

Samples:

sample_1: isolated oxidized c domain monomer1 – 2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; ferricyanide mM

Cond_1: pH*: 6.7; temperature: 278 K

Cond_2: pH*: 6.7; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-1H NOESY	not available	not available	not available
1H-1H cl-TOCSY	not available	not available	not available
1H-1H DQF-COSY	not available	not available	not available
1D NOESY	not available	not available	not available
1H-1H DEFT-NOESY	not available	not available	not available
1H-1H DEFT-TOCSY	not available	not available	not available

Software:

XEASY -

NMR spectrometers:

Bruker DMX 500.13 MHz
Bruker DMX 500.03 MHz

SWISS-PROT	P72181
GenBank	AAB17878
EMBL	CAC03621
PDB	1QKS 1HJ5 1HJ4 1HJ3 1HCM 1H9Y 1H9X 1GQ1 1E2R 1DY7 1AOQ 1AOM 1AOF
BMRB	4800