BMRB Entry 51135

Name: Chemical shift assignments for D64Y mutant of holo Acyl Carrier Protein from Homo sapiens
Published: 2022-09-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51135

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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 shift assignments for D64Y mutant of holo Acyl Carrier Protein from Homo sapiens

Deposition date:

2021-10-13

Original release date:

2022-09-16

Authors:

Tang, Jingxuan; Tonelli, Marco; Lee, Yeongjoon; Lee, Woonghee; Frederick, Ronnie; Markley, John

Citation:

Citation: Tang, Jingxuan; Tonelli, Marco; Lee, Yeongjoon; Lee, Woonghee; Frederick, Ronnie; Markley, John. "Chemical shift assignments for D64Y mutant of holo Acyl Carrier Protein from Homo sapiens" .

Assembly members:

Assembly members:
entity_1, polymer, 88 residues, Formula weight is not available
entity_PNS, non-polymer, 358.348 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pE-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SDMPPLTLEGIQDRVLYVLK LYDKIDPEKLSVNSHFMKDL GLDSLDQVEIIMAMEDEFGF EIPYIDAEKLMCPQEIVDYI ADKKDVYE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	317
15N chemical shifts	81
1H chemical shifts	605

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	cofactor	2

Entities:

Entity 1, protein 88 residues - Formula weight is not available

1

SER

ASP

MET

PRO

LEU

THR

LEU

GLU

GLY

2

ILE

GLN

ASP

ARG

VAL

LEU

TYR

VAL

LEU

LYS

3

LEU

TYR

ASP

LYS

ILE

ASP

PRO

GLU

LYS

LEU

4

SER

VAL

ASN

SER

HIS

PHE

MET

LYS

ASP

LEU

5

GLY

LEU

ASP

SER

LEU

ASP

GLN

VAL

GLU

ILE

6

ILE

MET

ALA

MET

GLU

ASP

GLU

PHE

GLY

PHE

7

GLU

ILE

PRO

TYR

ILE

ASP

ALA

GLU

LYS

LEU

8

MET

CYS

PRO

GLN

GLU

ILE

VAL

ASP

TYR

ILE

9

ALA

ASP

LYS

ASP

VAL

TYR

GLU

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

1

PNS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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
3D H(C)CH TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_2	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 51135

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: