BMRB Entry 34464

Name: NMR structure of the apo-form of Pseudomonas fluorescens CopC
Published: 2021-01-06

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PDB ID: 6tpb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34464
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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 structure of the apo-form of Pseudomonas fluorescens CopC

Deposition date:

2019-12-13

Original release date:

2021-01-06

Authors:

Persson, K.; Mayzel, M.; Karlsson, B.; Peciulyte, A.; Olsson, L.; Wittung Stafshede, P.; Salomon Johansen, K.; Horvath, I.

Citation:

Citation: Persson, K.; Mayzel, M.; Karlsson, B.; Peciulyte, A.; Olsson, L.; Wittung Stafshede, P.; Salomon Johansen, K.; Horvath, I.. "NMR structure of Pseudomonas fluorescens CopC" .

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, 10110.294 Da.

Natural source:

Natural source: Common Name: Pseudomonas fluorescens Taxonomy ID: 294 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas fluorescens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HAHLKSATPAADSTVAAPAD LRLTFSEGVEATFTKVSLSK DGTEVAIKGLETPDADKKTL VVTPAAPLAAGNYKVVWNAV SVDTHKSNGEYSFKVGQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	400
15N chemical shifts	90
1H chemical shifts	595

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 97 residues - 10110.294 Da.

1

HIS

ALA

HIS

LEU

LYS

SER

ALA

THR

PRO

ALA

2

ALA

ASP

SER

THR

VAL

ALA

PRO

ALA

ASP

3

LEU

ARG

LEU

THR

PHE

SER

GLU

GLY

VAL

GLU

4

ALA

THR

PHE

THR

LYS

VAL

SER

LEU

SER

LYS

5

ASP

GLY

THR

GLU

VAL

ALA

ILE

LYS

GLY

LEU

6

GLU

THR

PRO

ASP

ALA

ASP

LYS

THR

LEU

7

VAL

THR

PRO

ALA

PRO

LEU

ALA

8

GLY

ASN

TYR

LYS

VAL

TRP

ASN

ALA

VAL

9

SER

VAL

ASP

THR

HIS

LYS

SER

ASN

GLY

GLU

10

TYR

SER

PHE

LYS

VAL

GLY

GLN

Samples:

sample_1: CopC, [U-100% 13C; U-100% 15N], 0.7 mM

sample_conditions_1: ionic strength: 150 mM; pH: 5.6; pressure: 1 bar; 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation

WHAT IF, Vriend - refinement

CcpNmr Analysis, CCPN - data analysis

NMR spectrometers:

Bruker AVANCE III 800 MHz

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