BMRB Entry 30659

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30659
MolProbity Validation Chart

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Title:
Solution structure of paxillin LIM4 in complex with kindlin-2 F0
Deposition date:
2019-08-26
Original release date:
2019-10-16
Authors:
Zhu, L.; Qin, J.
Citation:

Citation: Zhu, Liang; Liu, Huan; Lu, Fan; Yang, Jun; Byzova, Tatiana; Qin, Jun. "Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion"  Structure 27, 1686-1697 (2019).
PubMed: 31590942

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, 13002.017 Da.
entity_2, polymer, 72 residues, 8309.760 Da.
entity_ZN, non-polymer, 65.409 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 BL21(DE3)   Vector: pGST-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMDPEFMALDGIRMPDGCY ADGTWELSVHVTDLNRDVTL RVTGEVHIGGVMLKLVEKLD VKKDWSDHALWWEKKRTWLL KTHWTLDKYGIQADAKLQFT PQHKLLRLQLPN
entity_2: GAMDPEFYHERRGSLCSGCQ KPITGRCITAMAKKFHPEHF VCAFCLKQLNKGTFKEQNDK PYCQNCFLKLFC

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts150
1H chemical shifts985

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3, 13
4entity_3, 23

Entities:

Entity 1, entity_1 112 residues - 13002.017 Da.

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

Entity 2, entity_2 72 residues - 8309.760 Da.

1   GLYALAMETASPPROGLUPHETYRHISGLU
2   ARGARGGLYSERLEUCYSSERGLYCYSGLN
3   LYSPROILETHRGLYARGCYSILETHRALA
4   METALALYSLYSPHEHISPROGLUHISPHE
5   VALCYSALAPHECYSLEULYSGLNLEUASN
6   LYSGLYTHRPHELYSGLUGLNASNASPLYS
7   PROTYRCYSGLNASNCYSPHELEULYSLEU
8   PHECYS

Entity 3, entity_3, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: paxillin LIM4, [U-15N; U-13C], 0.55 mM; kindlin-2 F0 0.89 mM; NaCl 50 mM

sample_2: paxillin LIM4 0.85 mM; kindlin-2 F0, U-15N, U-13C, 0.54 mM; NaCl 50 mM

sample_3: paxillin LIM4, U-15N, U-13C, 0.55 mM; kindlin-2 F0 0.89 mM; NaCl 50 mM

sample_4: paxillin LIM4 0.85 mM; kindlin-2 F0, U-15N, U-13C, 0.54 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 Pa; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.8; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N/13C-edited NOESYsample_1isotropicsample_conditions_1
3D 15N/13C-edited NOESYsample_2isotropicsample_conditions_1
3D 15N/13C-filtered NOESYsample_3isotropicsample_conditions_2
3D 15N/13C-filtered NOESYsample_4isotropicsample_conditions_2

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

PIPP, Garrett - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks