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 15777

Title: Solution Structure of IG-Like Domain 23 from Human Filamin A   PubMed: 19293932

Authors: Heikkinen, Outi; Kupiainen, Olga; Ylanne, Jari; Kilpelainen, Ilkka

Citation: Nakamura, Fumihiko; Heikkinen, Outi; Pentikainen, Olli; Osborn, Teresia; Kasza, Karen; Weitz, David; Kupiainen, Olga; Permi, Perttu; Kilpelainen, Ilkka; Ylanne, Jari; Hartwig, John; Stossel, Thomas. "Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations"  PLoS ONE 4, 4928-4928 (2009).

Assembly members:
FLNA23, polymer, 99 residues, 9989.371 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):
FLNA23: GAMGDPGLVSAYGAGLEGGV TGNPAEFVVNTSNAGAGALS VTIDGPSKVKMDCQECPEGY RVTYTPMAPGSYLISIKYGG PYHIGGSPFKAKVTGPRLV

Data sets:
Data typeCount
13C chemical shifts374
15N chemical shifts92
1H chemical shifts627

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FLNA231

Entities:

Entity 1, FLNA23 99 residues - 9989.371 Da.

1   GLYALAMETGLYASPPROGLYLEUVALSER
2   ALATYRGLYALAGLYLEUGLUGLYGLYVAL
3   THRGLYASNPROALAGLUPHEVALVALASN
4   THRSERASNALAGLYALAGLYALALEUSER
5   VALTHRILEASPGLYPROSERLYSVALLYS
6   METASPCYSGLNGLUCYSPROGLUGLYTYR
7   ARGVALTHRTYRTHRPROMETALAPROGLY
8   SERTYRLEUILESERILELYSTYRGLYGLY
9   PROTYRHISILEGLYGLYSERPROPHELYS
10   ALALYSVALTHRGLYPROARGLEUVAL

Samples:

sample_1: FLNA23, [U-13C; U-15N], 1 ± 0.2 mM; Sodium phosphate 20 mM; Sodium chloride 150 mM; DTT 1 mM; Sodium azide 2 mM

sample_conditions_1: ionic strength: 150 mM; 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 HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
iHNCAsample_1isotropicsample_conditions_1
iHNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection, data analysis, processing

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

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