BMRB Entry 34744

Name: NMR structure of holo-acp
Published: 2023-03-14

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PDB ID: 8all
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34744
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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 holo-acp

Deposition date:

2022-08-01

Original release date:

2023-03-14

Authors:

Collin, S.; Weissman, K.; Chagot, B.; Gruez, A.

Citation:

Citation: Collin, S.; Weissman, K.; Chagot, B.; Gruez, A.. "NMR structure of holo-acp" .

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 8938.062 Da.
entity_PNS, non-polymer, 358.348 Da.

Natural source:

Natural source: Common Name: Streptomyces virginiae Taxonomy ID: 1961 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces virginiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMYGEAVTEQLSRLVAG FVPDAAGSVDPDRTLLEHGI DSINLMNLRFEITERFGRTL PLQLLSESTVPVLAAHLSAD RAH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	348
15N chemical shifts	90
1H chemical shifts	598

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 83 residues - 8938.062 Da.

1

GLY

PRO

GLY

SER

MET

TYR

GLY

GLU

ALA

VAL

2

THR

GLU

GLN

LEU

SER

ARG

LEU

VAL

ALA

GLY

3

PHE

VAL

PRO

ASP

ALA

GLY

SER

VAL

ASP

4

PRO

ASP

ARG

THR

LEU

GLU

HIS

GLY

ILE

5

ASP

SER

ILE

ASN

LEU

MET

ASN

LEU

ARG

PHE

6

GLU

ILE

THR

GLU

ARG

PHE

GLY

ARG

THR

LEU

7

PRO

LEU

GLN

LEU

SER

GLU

SER

THR

VAL

8

PRO

VAL

LEU

ALA

HIS

LEU

SER

ALA

ASP

9

ARG

ALA

HIS

Entity 2, unit_2 - C11 H23 N2 O7 P S - 358.348 Da.

1

PNS

Samples:

sample_1: Hybrid polyketide synthase-non ribosomal peptide synthetase ACP7, [U-100% 13C; U-100% 15N], 1.6 mM; sodium phosphate 100 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H(C12 N14)-1H(C12 N14) NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H(C12 N14) NOESY	sample_1	isotropic	sample_conditions_1
2D 1H(C12 N14) -1H(C12 N14) TOCSY	sample_1	isotropic	sample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz

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