BMRB Entry 11065

Title:
Solution structure of the 4.1R FERM alpha lobe domain
Deposition date:
2009-01-09
Original release date:
2009-04-23
Authors:
Kusunoki, Hideki; Kohno, Toshiyuki
Citation:

Citation: Kusunoki, Hideki; Kohno, Toshiyuki. "Solution structure and glycophorin C binding studies of the 4.1R FERM alpha-lobe domain"  Proteins 76, 255-260 (2009).
PubMed: 19338061

Assembly members:

Assembly members:
4.1R FERM alpha-lobe domain, polymer, 109 residues, 12420.137 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: pET15b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts489
15N chemical shifts109
1H chemical shifts777

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
14.1R FERM alpha-lobe domain1

Entities:

Entity 1, 4.1R FERM alpha-lobe domain 109 residues - 12420.137 Da.

Residues 79-82 represent vector-derived amino acid residues

1   GLYSERHISMETASPPROALAGLNLEUTHR
2   GLUASPILETHRARGTYRTYRLEUCYSLEU
3   GLNLEUARGGLNASPILEVALALAGLYARG
4   LEUPROCYSSERPHEALATHRLEUALALEU
5   LEUGLYSERTYRTHRILEGLNSERGLULEU
6   GLYASPTYRASPPROGLULEUHISGLYVAL
7   ASPTYRVALSERASPPHELYSLEUALAPRO
8   ASNGLNTHRLYSGLULEUGLUGLULYSVAL
9   METGLULEUHISLYSSERTYRARGSERMET
10   THRPROALAGLNALAASPLEUGLUPHELEU
11   GLUASNALALYSLYSLEUSERMETTYR

Samples:

sample_1: 4.1R FERM alpha-lobe domain0.12 – 0.8 mM; NaCl 45 mM; D2O 100%

sample_2: 4.1R FERM alpha-lobe domain, [U-98% 15N], 0.12 – 0.8 mM; NaCl 45 mM; H2O 90%; D2O 10%

sample_3: 4.1R FERM alpha-lobe domain, [U-98% 13C; U-98% 15N], 0.12 – 0.8 mM; NaCl 45 mM; H2O 90%; D2O 10%

sample_4: 4.1R FERM alpha-lobe domain, [U-98% 13C; U-98% 15N], 0.12 – 0.8 mM; NaCl 45 mM; D2O 100%

sample_5: 4.1R FERM alpha-lobe domain, [U-10% 13C; U-98% 15N], 0.48 mM; NaCl 45 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 45 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY No1sample_3isotropicsample_conditions_1
3D 1H-13C NOESY No2sample_4isotropicsample_conditions_1
2D 1H-15N HSQC No1sample_2isotropicsample_conditions_1
2D 1H-15N HSQC No2sample_3isotropicsample_conditions_1
2D 1H-13C HSQC No1sample_3isotropicsample_conditions_1
2D 1H-13C HSQC No2sample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSY No1sample_3isotropicsample_conditions_1
3D HCCH-TOCSY No2sample_4isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
3D HNHBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - NOE collection

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAD90280 BAD92886 BAE27807 BAE28045 BAG84710
EMBL CDR98361 CDR98362
GB AAA35793 AAA35794 AAA35795 AAA35797 AAA37122
REF NP_001003362 NP_001122078 NP_001122079 NP_001159477 NP_001159478
SP P11171 P48193 Q6Q7P4 Q9N179
TPG DAA32059
AlphaFold P48193 Q6Q7P4 Q9N179 P11171

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