BMRB Entry 11085

Title:
Solution structure of the CH domain of human NEDD9 interacting protein with calponin homology and LIM domains
Deposition date:
2009-12-28
Original release date:
2011-01-04
Authors:
Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation:

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the CH domain of human NEDD9 interacting protein with calponin homology and LIM domains"  .

Assembly members:

Assembly members:
CH domain, polymer, 116 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040315-92

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts112
1H chemical shifts740

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CH domain1

Entities:

Entity 1, CH domain 116 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLNGLU
2   GLULEULEUARGTRPCYSGLNGLUGLNTHR
3   ALAGLYTYRPROGLYVALHISVALSERASP
4   LEUSERSERSERTRPALAASPGLYLEUALA
5   LEUCYSALALEUVALTYRARGLEUGLNPRO
6   GLYLEULEUGLUPROSERGLULEUGLNGLY
7   LEUGLYALALEUGLUALATHRALATRPALA
8   LEULYSVALALAGLUASNGLULEUGLYILE
9   THRPROVALVALSERALAGLNALAVALVAL
10   ALAGLYSERASPPROLEUGLYLEUILEALA
11   TYRLEUSERHISPHEHISSERALAPHELYS
12   SERGLYPROSERSERGLY

Samples:

sample_1: CH domain, [U-100% 13C; U-100% 15N], 1.22 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 1 mM; sodium azide 0.02%; D2O 10%; H2O 90%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N-separated NOESYsample_1isotropiccondition_1
3D 1H-13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9295, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB13949 BAB15124 BAB86289 BAD18727 BAH12301
EMBL CAB59266
GB AAH09972 AAH42144 AAH52983 AIC63549 EAW48341
REF NP_001152763 NP_001273542 NP_073602 XP_011905848 XP_011905849
SP Q8TDZ2
AlphaFold Q8TDZ2

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