BMRB Entry 25322

Name: pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements
Published: 2014-12-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25322

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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:

pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements

Deposition date:

2014-10-22

Original release date:

2014-12-09

Authors:

McIntosh, Lawrence; Platzer, Gerald; Okon, Mark

Citation:

Citation: Platzer, Gerald; Okon, Mark; McIntosh, Lawrence. "pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements" J. Biomol. NMR 60, 109-129 (2014).
PubMed: 25239571

Assembly members:

Assembly members:
ACE-GLY-LYS-GLY-NH2 peptide, polymer, 5 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ACE-GLY-LYS-GLY-NH2 peptide: XGKGX

Data sets:

pH_titration
- pH_titration_list_1
pH_param_list
- pH_parameter_list_1

Data type	Count
pKa values	11
pH NMR parameter values	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ACE-GLY-LYS-GLY-NH2 peptide	1

Entities:

Entity 1, ACE-GLY-LYS-GLY-NH2 peptide 5 residues - Formula weight is not available

1

ACE

GLY

LYS

GLY

NH2

Samples:

sample_1: blocked tripeptide, [U-13C; U-15N], 10 mM; NaCl 50 mM

sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 50 mM

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H-NMR	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
multiple-bond 13C HMBC	sample_1	isotropic	sample_conditions_1
multiple-bond 15N HMBC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3, Bruker Biospin - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz