BMRB Entry 15512

Name: 1H, 13C, and 15N NMR chemical shift assignments of the palladin Ig3 domain
Published: 2008-03-31

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PDB ID: 2lqr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15512
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N NMR chemical shift assignments of the palladin Ig3 domain

Deposition date:

2007-10-08

Original release date:

2008-03-31

Authors:

Dixon, Richard; Rachlin, Andrew; Otey, Carol; Campbell, Sharon

Citation:

Citation: Dixon, Richard; Campbell, Sharon. "1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin" Biomol. NMR Assignments 2, 51-53 (2008).
PubMed: 19636923

Assembly members:

Assembly members:
Palladin_Ig3_domain, polymer, 108 residues, 11975 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMAL-c2x

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Palladin_Ig3_domain: GGSNATAPFFEMKLKHYKIF EGMPVTFTCRVAGNPKPKIY WFKDGKQISPKSDHYTIQRD LDGTCSLHTTASTLDDDGNY TIMAANPQGRVSCTGRLMVQ AVNQRGRS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	455
15N chemical shifts	112
1H chemical shifts	701

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	molecule 1	1

Entities:

Entity 1, molecule 1 108 residues - 11975 Da.

Residues 1-3 are non-native amino acids resulting from the cloning and purification strategy

1

GLY

SER

ASN

ALA

THR

ALA

PRO

PHE

2

GLU

MET

LYS

LEU

LYS

HIS

TYR

LYS

ILE

PHE

3

GLU

GLY

MET

PRO

VAL

THR

PHE

THR

CYS

ARG

4

VAL

ALA

GLY

ASN

PRO

LYS

PRO

LYS

ILE

TYR

5

TRP

PHE

LYS

ASP

GLY

LYS

GLN

ILE

SER

PRO

6

LYS

SER

ASP

HIS

TYR

THR

ILE

GLN

ARG

ASP

7

LEU

ASP

GLY

THR

CYS

SER

LEU

HIS

THR

8

ALA

SER

THR

LEU

ASP

GLY

ASN

TYR

9

THR

ILE

MET

ALA

ASN

PRO

GLN

GLY

ARG

10

VAL

SER

CYS

THR

GLY

ARG

LEU

MET

VAL

GLN

11

ALA

VAL

ASN

GLN

ARG

GLY

ARG

SER

Samples:

sample_1: Palladin Ig3 domain, [U-98% 13C; U-98% 15N], 0.3-1.8 mM; D2O 10%; H2O 90%; TRIS 50 mM; sodium chloride 150 mM; DTT 2 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC (aliphatic)	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH TOCSY	sample_1	isotropic	sample_conditions_1
3D HC(CO)NH TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (aliphatic)	sample_1	isotropic	sample_conditions_1
HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC (aromatic)	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (aromatic)	sample_1	isotropic	sample_conditions_1

Software:

NMRView v5.2.2.01, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian INOVA 700 MHz
Varian INOVA 600 MHz

PDB	2DM2 2LQR
GB	EDL28653 EDL28654