BMRB Entry 51154

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51154
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of paxillin LIM2/3
Deposition date:
2021-10-25
Original release date:
2024-05-09
Authors:
Prestel, Andreas; Michaelis, Marcus; Klishin, Nikolai; Moller, Heiko
Citation:

Citation: Baade, Timo; Michaelis, Marcus; Prestel, Andreas; Paone, Christoph; Klishin, Nikolai; Scheinost, Laura; Nedielkov, Ruslan; Hauck, Christof; Moller, Heiko. "A flexible loop in the paxillin LIM3 domain mediates direct binding to integrin b3"  .

Assembly members:

Assembly members:
entity_1, polymer, 127 residues, 14729.60 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   Vector: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SPRCYYCNGPILDKVVTALD RTWHPEHFFCAQCGAFFGPE GFHEKDGKAYCRKDYFDMFA PKCGGCARAILENYISALNT LWHPECFVCRECFTPFVNGS FFEHDGQPYCEVHYHERRGS PEYFKNG

Data sets:
Data typeCount
13C chemical shifts575
15N chemical shifts124
1H chemical shifts830

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Paxillin LIM2/31
2Zn, 12
3Zn, 22
4Zn, 32
5Zn, 42

Entities:

Entity 1, Paxillin LIM2/3 127 residues - 14729.60 Da.

Residues 121-127 constitute a non-native Nef-tag.

1   SERPROARGCYSTYRTYRCYSASNGLYPRO
2   ILELEUASPLYSVALVALTHRALALEUASP
3   ARGTHRTRPHISPROGLUHISPHEPHECYS
4   ALAGLNCYSGLYALAPHEPHEGLYPROGLU
5   GLYPHEHISGLULYSASPGLYLYSALATYR
6   CYSARGLYSASPTYRPHEASPMETPHEALA
7   PROLYSCYSGLYGLYCYSALAARGALAILE
8   LEUGLUASNTYRILESERALALEUASNTHR
9   LEUTRPHISPROGLUCYSPHEVALCYSARG
10   GLUCYSPHETHRPROPHEVALASNGLYSER
11   PHEPHEGLUHISASPGLYGLNPROTYRCYS
12   GLUVALHISTYRHISGLUARGARGGLYSER
13   PROGLUTYRPHELYSASNGLY

Entity 2, Zn, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Paxillin LIM2/3, [U-13C; U-15N], 500 uM; NaCl 150 mM; Na2HPO4 50 mM; NaN3 4 mM; DTT 1 mM

sample_2: Paxillin LIM2/3, [U-13C; U-15N], 500 uM; NaCl 150 mM; Na2HPO4 50 mM; NaN3 4 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1
NOESY-15N-HSQCsample_1isotropicsample_conditions_1
NOESY-13Cali-HSQCsample_1isotropicsample_conditions_1
1H-15N-NOE-HSQCsample_1isotropicsample_conditions_1
1H-13Cali-HSQCsample_1isotropicsample_conditions_1
1H-13Caro-HSQCsample_1isotropicsample_conditions_1
H(C)CH-TOCSYsample_1isotropicsample_conditions_1
(H)CCH-TOCSYsample_1isotropicsample_conditions_1
H(C)CH-COSYsample_1isotropicsample_conditions_1
NOESY-13Caro-HSQCsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4.2 - chemical shift assignment

ATNOS - data analysis

TALOS-N - data analysis

CYANA v3.0 - structure determination

PyMOL - data analysis

TOPSPIN v3.1 - processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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