BMRB Entry 17827

Name: 1H, 13C, and 15N Chemical Shift Assignments for Kindle-2 N-terminus
Published: 2011-12-01

Click here to enlarge.

PDB ID: 2lgx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17827
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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:

1H, 13C, and 15N Chemical Shift Assignments for Kindle-2 N-terminus

Deposition date:

2011-08-03

Original release date:

2011-12-01

Authors:

Perera, H.; Ma, Yan-Qing; Yang, Jun; Hirbawi, Jamila; Plow, Edward; Qin, Jun

Citation:

Citation: Perera, H.; Ma, Yan-Qing; Yang, Jun; Hirbawi, Jamila; Plow, Edward; Qin, Jun. "Membrane Binding of the N-Terminal Ubiquitin-Like Domain of kindlin-2 Is Crucial for Its Regulation of Integrin Activation" Structure 19, 1664-1671 (2011).
PubMed: 22078565

Assembly members:

Assembly members:
entity, polymer, 112 residues, 10895.647 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGST-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMPDEFMALDGIRMPDGCY ADGTWELSVHVTDVNRDVTL RVTGEVHIGGVMLKLVEKLD VKKDWSDHALWWEKKRTWLL KTHWTLDKYGIQADAKLQFT PQHKLLRLQLPN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	398
15N chemical shifts	103
1H chemical shifts	581

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	k2-n	1

Entities:

Entity 1, k2-n 112 residues - 10895.647 Da.

Residues 1-7 represent a non-native cloning artifacts

1

GLY

ALA

MET

PRO

ASP

GLU

PHE

MET

ALA

LEU

2

ASP

GLY

ILE

ARG

MET

PRO

ASP

GLY

CYS

TYR

3

ALA

ASP

GLY

THR

TRP

GLU

LEU

SER

VAL

HIS

4

VAL

THR

ASP

VAL

ASN

ARG

ASP

VAL

THR

LEU

5

ARG

VAL

THR

GLY

GLU

VAL

HIS

ILE

GLY

6

VAL

MET

LEU

LYS

LEU

VAL

GLU

LYS

LEU

ASP

7

VAL

LYS

ASP

TRP

SER

ASP

HIS

ALA

LEU

8

TRP

GLU

LYS

ARG

THR

TRP

LEU

9

LYS

THR

HIS

TRP

THR

LEU

ASP

LYS

TYR

GLY

10

ILE

GLN

ALA

ASP

ALA

LYS

LEU

GLN

PHE

THR

11

PRO

GLN

HIS

LYS

LEU

ARG

LEU

GLN

LEU

12

PRO

ASN

Samples:

sample_1: k2-n, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_2: k2-n 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_3: k2-n, [U-100% 15N], 0.1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; 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	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 13C-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP, Garrett - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRView, Johnson, One Moon Scientific - data analysis

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - data analysis

PASA, Xu, Wang, Yang, Vaynberg, Xu, and Qin - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 900 MHz

PDB	2LGX
DBJ	BAC37692 BAE26194 BAE38850 BAF84427
EMBL	CAA80852 CAD61925
GB	AAH17327 AAH33436 AAH83876 AAI08179 AAI51293
REF	NP_001011915 NP_001094734 NP_001128471 NP_001128472 NP_001253248
SP	Q8CIB5 Q96AC1
TPG	DAA25234
AlphaFold	Q8CIB5 Q96AC1