BMRB Entry 15925

Title:
Filamin A Ig-like domains 18-19
Deposition date:
2008-08-19
Original release date:
2009-01-15
Authors:
Heikkinen, Outi; Kilpelainen, Ilkka; Koskela, Harri; Permi, Perttu; Heikkinen, Sami; Ylanne, Jari
Citation:

Citation: Heikkinen, Outi; Permi, Perttu; Koskela, Harri; Ylanne, Jari; Kilpelainen, Ilkka. "1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19"  Biomol. NMR Assignments 3, 53-56 (2009).
PubMed: 19636946

Assembly members:

Assembly members:
FLNa18-19, polymer, 191 residues, 20379.8945 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: pGEX-4T1-HTb

Data sets:
Data typeCount
13C chemical shifts761
15N chemical shifts175
1H chemical shifts1298

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FLNa18-191

Entities:

Entity 1, FLNa18-19 191 residues - 20379.8945 Da.

1   GLYALAMETGLYASPASPSERMETARGMET
2   SERHISLEULYSVALGLYSERALAALAASP
3   ILEPROILEASNILESERGLUTHRASPLEU
4   SERLEULEUTHRALATHRVALVALPROPRO
5   SERGLYARGGLUGLUPROCYSLEULEULYS
6   ARGLEUARGASNGLYHISVALGLYILESER
7   PHEVALPROLYSGLUTHRGLYGLUHISLEU
8   VALHISVALLYSLYSASNGLYGLNHISVAL
9   ALASERSERPROILEPROVALVALILESER
10   GLNSERGLUILEGLYASPALASERARGVAL
11   ARGVALSERGLYGLNGLYLEUHISGLUGLY
12   HISTHRPHEGLUPROALAGLUPHEILEILE
13   ASPTHRARGASPALAGLYTYRGLYGLYLEU
14   SERLEUSERILEGLUGLYPROSERLYSVAL
15   ASPILEASNTHRGLUASPLEUGLUASPGLY
16   THRCYSARGVALTHRTYRCYSPROTHRGLU
17   PROGLYASNTYRILEILEASNILELYSPHE
18   ALAASPGLNHISVALPROGLYSERPROPHE
19   SERVALLYSVALTHRGLYGLUGLYARGVAL
20   LYS

Samples:

sample_1: FLNa18-19, [U-13C; U-15N], 0.8 mM; sodium phosphate 50 mM; potassium chloride 100 mM; DTT 1 mM; sodium azide 2 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C-CT-HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C-CT-HSQC_aromaticssample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
HN(CA)COsample_1isotropicsample_conditions_1
HNCAHAsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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 600 MHz
  • Varian INOVA 800 MHz
  • Bruker DRX 750 MHz

Related Database Links:

PDB

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