BMRB Entry 6188

Name: Solution structure of Acyl Coenzyme A Binding Protein from yeast
Published: 2005-02-21

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PDB ID: 1st7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6188
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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:

Solution structure of Acyl Coenzyme A Binding Protein from yeast

Deposition date:

2004-04-22

Original release date:

2005-02-21

Authors:

Teilum, K.; Thormann, T.; Caterer, N.; Poulsen, H.; Jensen, P.; Knudsen, J.; Kragelund, B.; Poulsen, F.

Citation:

Citation: Teilum, K.; Thormann, T.; Caterer, N.; Poulsen, H.; Jensen, P.; Knudsen, J.; Kragelund, B.; Poulsen, F.. "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles" Proteins 59, 80-90 (2005).
PubMed: 15690348

Assembly members:

Assembly members:
Acyl-CoA-binding protein, polymer, 86 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Acyl-CoA-binding protein: VSQLFEEKAKAVNELPTKPS TDELLELYALYKQATVGDND KEKPGIFNMKDRYKWEAWEN LKGKSQEDAEKEYIALVDQL IAKYSS

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	249
1H chemical shifts	496
15N chemical shifts	88

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Acyl-CoA-binding protein	1

Entities:

Entity 1, Acyl-CoA-binding protein 86 residues - Formula weight is not available

1

VAL

SER

GLN

LEU

PHE

GLU

LYS

ALA

LYS

2

ALA

VAL

ASN

GLU

LEU

PRO

THR

LYS

PRO

SER

3

THR

ASP

GLU

LEU

GLU

LEU

TYR

ALA

LEU

4

TYR

LYS

GLN

ALA

THR

VAL

GLY

ASP

ASN

ASP

5

LYS

GLU

LYS

PRO

GLY

ILE

PHE

ASN

MET

LYS

6

ASP

ARG

TYR

LYS

TRP

GLU

ALA

TRP

GLU

ASN

7

LEU

LYS

GLY

LYS

SER

GLN

GLU

ASP

ALA

GLU

8

LYS

GLU

TYR

ILE

ALA

LEU

VAL

ASP

GLN

LEU

9

ILE

ALA

LYS

TYR

SER

Samples:

sample_1: Acyl-CoA-binding protein, [U-13C; U-15N], 2.5 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.75; temperature: 298 K; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	sample_cond_1
3D 15N-separated NOESY	sample_1	not available	sample_cond_1
HNHA	sample_1	not available	sample_cond_1

Software:

X-PLOR v3.8 - structure solution, refinement

NMR spectrometers:

Varian UNITY 750 MHz

PDB	1ST7
DBJ	GAA23421
EMBL	CAA69944 CAA69947 CAA97025 CAY79799
GB	AAA34384 AAB31936 AAZ22453 AHY79403 EDN61634
REF	NP_011551
SP	P31787
TPG	DAA08135
AlphaFold	P31787