BMRB Entry 5900

Title:
NMR structure of 16th module of Immune Adherence Receptor, Cr1 (Cd35)
Deposition date:
2003-08-07
Original release date:
2004-07-23
Authors:
O'Leary, J.; Bromek, K.; Black, G.; Uhrinova, S.; Schmitz, C.; Krych, M.; Atkinson, J.; Uhrin, D.; Barlow, P.
Citation:

Citation: O'Leary, J.; Bromek, K.; Black, G.; Uhrinova, S.; Schmitz, C.; Wang, X.; Krych, M.; Atkinson, J.; Uhrin, D.; Barlow, P.. "Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces."  Protein Sci. 13, 1238-1250 (2004).
PubMed: 15096630

Assembly members:

Assembly members:
complement receptor type 1, polymer, 68 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: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
complement receptor type 1: EAEAKSCKTPPDPVNGMVHV ITDIQVGSRITYSCTTGHRL IGHSSAECILSGNTAHWSTK PPICQRIP

Data typeCount
15N chemical shifts65
1H chemical shifts409

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Complement receptor type 11

Entities:

Entity 1, Complement receptor type 1 68 residues - Formula weight is not available

1   GLUALAGLUALALYSSERCYSLYSTHRPRO
2   PROASPPROVALASNGLYMETVALHISVAL
3   ILETHRASPILEGLNVALGLYSERARGILE
4   THRTYRSERCYSTHRTHRGLYHISARGLEU
5   ILEGLYHISSERSERALAGLUCYSILELEU
6   SERGLYASNTHRALAHISTRPSERTHRLYS
7   PROPROILECYSGLNARGILEPRO

Samples:

sample_1: complement receptor type 1, [U-15N], 1 mM; phosphate buffer 25 mM; D2O 10%; H2O 90%

sample_cond_1: ionic strength: 25 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
15N HSQCnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
2D RSCUBACOSYnot availablenot availablenot available
3D 15N HSQC-TOCSYnot availablenot availablenot available
3D 15N HSQC-NOESYnot availablenot availablenot available

Software:

VNMR - collection

AZARA v2.6 - processing

ANSIG v3.3 - data analysis

CNS v1.0 - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 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