BMRB Entry 30478

Name: NMR solution structure of wild type hFABP1 in the presence of GW7647
Published: 2019-01-02

Click here to enlarge.

PDB ID: 6do7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30478
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: NMR solution structure of wild type hFABP1 in the presence of GW7647 PubMed: 30598509

Deposition date: 2018-06-11 Original release date: 2019-01-02

Authors: Scanlon, M.; Mohanty, B.; Doak, B.; Patil, R.

Citation: Patil, Rahul; Mohanty, Biswaranjan; Liu, Bonan; Chandrashekaran, Indu; Headey, Stephen; Williams, Martin; Clements, Craig; Ilyichova, Olga; Doak, Bradley; Genissel, Patrick; Weaver, Richard; Vuillard, Laurent; Halls, Michelle; Porter, Christopher; Scanlon, Martin. "A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor alpha agonists" J. Biol. Chem. 294, 3720-3734 (2019).

Assembly members:
entity_1, polymer, 135 residues, 15225.457 Da.
entity_2VN, non-polymer, 502.752 Da.

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

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

Entity Sequences (FASTA):
entity_1: HHHHHHVAMSFSGKYQLQSQ ENFEAFMKAIGLPEELIQKG KDIKGVSEIVQNGKHFKFTI TAGSKVIQNEFTVGEECELE TMTGEKVKTVVQLEGDNKLV TTFKNIKSVTELNGDIITNT MTLGDIVFKRISKRI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	449
15N chemical shifts	145
1H chemical shifts	932

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 135 residues - 15225.457 Da.

1

HIS

VAL

ALA

MET

SER

2

PHE

SER

GLY

LYS

TYR

GLN

LEU

GLN

SER

GLN

3

GLU

ASN

PHE

GLU

ALA

PHE

MET

LYS

ALA

ILE

4

GLY

LEU

PRO

GLU

LEU

ILE

GLN

LYS

GLY

5

LYS

ASP

ILE

LYS

GLY

VAL

SER

GLU

ILE

VAL

6

GLN

ASN

GLY

LYS

HIS

PHE

LYS

PHE

THR

ILE

7

THR

ALA

GLY

SER

LYS

VAL

ILE

GLN

ASN

GLU

8

PHE

THR

VAL

GLY

GLU

CYS

GLU

LEU

GLU

9

THR

MET

THR

GLY

GLU

LYS

VAL

LYS

THR

VAL

10

VAL

GLN

LEU

GLU

GLY

ASP

ASN

LYS

LEU

VAL

11

THR

PHE

LYS

ASN

ILE

LYS

SER

VAL

THR

12

GLU

LEU

ASN

GLY

ASP

ILE

THR

ASN

THR

13

MET

THR

LEU

GLY

ASP

ILE

VAL

PHE

LYS

ARG

14

ILE

SER

LYS

ARG

ILE

Entity 2, entity_2 - C29 H46 N2 O3 S - 502.752 Da.

1

2VN

Samples:

sample_1: hFABP1 wild type, [U-15N13C], 0.5 mM; GW7647 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DMSO, D6, 1%

sample_2: hFABP1 wild type, [U-2H,15N13C], 1 mM; GW7647 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DMSO, D6, 1%

sample_conditions_1: ionic strength: 70 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 15N-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
3D 13Cali resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
3D 13Caro resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
2D F1-edited, F2-13C,15N-filtered [1H,1H] NOESY	sample_1	isotropic	sample_conditions_1
3D F1-13C,15N-filtered, F2-13Cali edited [1H,1H] NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D F1, F2-13C,15N-filtered [1H,1H] NOESY	sample_2	isotropic	sample_conditions_1
2D F1-edited, F2-13C,15N-filtered [1H,1H] NOESY	sample_2	isotropic	sample_conditions_1
3D F1-13C,15N-filtered, F2-15N edited [1H,1H] NOESY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Prime, Prime, Schrodinger, LLC, New York, NY, 2018 - refinement

OPALp, Koradi et al, 2000 - refinement

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts