BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17827

Title: 1H, 13C, and 15N Chemical Shift Assignments for Kindle-2 N-terminus   PubMed: 22078565

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: 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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts398
15N chemical shifts103
1H chemical shifts581

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1k2-n1

Entities:

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

Residues 1-7 represent a non-native cloning artifacts

1   GLYALAMETPROASPGLUPHEMETALALEU
2   ASPGLYILEARGMETPROASPGLYCYSTYR
3   ALAASPGLYTHRTRPGLULEUSERVALHIS
4   VALTHRASPVALASNARGASPVALTHRLEU
5   ARGVALTHRGLYGLUVALHISILEGLYGLY
6   VALMETLEULYSLEUVALGLULYSLEUASP
7   VALLYSLYSASPTRPSERASPHISALALEU
8   TRPTRPGLULYSLYSARGTHRTRPLEULEU
9   LYSTHRHISTRPTHRLEUASPLYSTYRGLY
10   ILEGLNALAASPALALYSLEUGLNPHETHR
11   PROGLNHISLYSLEULEUARGLEUGLNLEU
12   PROASN

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 13C-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_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

Related Database Links:

PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts