BMRB Entry 15099

Name: Solution structure of CM15 in DPC micelles
Published: 2007-09-12

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PDB ID: 2jmy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15099
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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 CM15 in DPC micelles

Deposition date:

2007-01-10

Original release date:

2007-09-12

Authors:

Respondek, Michal; Madl, Tobias; Goebl, Christoph; Golser, Regina; Zangger, Klaus

Citation:

Citation: Respondek, Michal; Madl, Tobias; Goebl, Christoph; Golser, Regina; Zangger, Klaus. "Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves" J. Am. Chem. Soc. 129, 5228-5234 (2007).
PubMed: 17397158

Assembly members:

Assembly members:
CM15, polymer, 15 residues, 1776.343 Da.

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 Host organism: not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CM15: KWKLFKKIGAVLKVL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	26
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CM15	1

Entities:

Entity 1, CM15 15 residues - 1776.343 Da.

1

LYS

TRP

LYS

LEU

PHE

LYS

ILE

GLY

ALA

2

VAL

LEU

LYS

VAL

LEU

Samples:

sample_1: CM15 1.7 mM; DPC, [U-2H], 100 mM; KPi 50 mM; Sodium azide 0.02%

sample_conditions_1: ionic strength: 0.15 M; pH: 5.0; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
HNCACO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHACANH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCOCA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY arom	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D CCCONH	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY RD1	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HBHACACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCCONH TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Bruker Avance 500 MHz