Backbone relaxation data of rat holo cellular retinol-binding protein type I
(CRBP-I)

The sequence is identical with SWISS-PROT entry P02696, except that it starts
with an additional N-terminal methionine residue that should be numbered as M0,
since it occurs only in the recombinantly-expressed protein.

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jun 9 12:03:01 2011

Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution.

The above molecular mass excludes MET 0.

Crystallographic Studies On A Family Of Cellular Lipophilic Transport Proteins. Refinement Of P2 Myelin Protein And The Structu

Solution Structure Of Cellular Retinol Binding Protein Type- I In The Ligand-Free State

Solution Structure Of Cellular Retinol Binding Protein Type- I In Complex With All-Trans-Retinol

Two Homologous Rat Cellular Retinol-Binding Proteins Differ In Local Structure And Flexibility

cellular retinol binding protein I [Mus musculus]

retinol-binding protein, partial [Homo sapiens]

cytosolic retinol-binding protein [Rattus norvegicus]

cellular retinol binding protein [Rattus norvegicus]

Retinol binding protein 1, cellular [Mus musculus]

retinol-binding protein 1 [Mus musculus]

retinol-binding protein 1 [Rattus norvegicus]

PREDICTED: retinol-binding protein 1 [Mesocricetus auratus]

PREDICTED: retinol-binding protein 1 [Microtus ochrogaster]

PREDICTED: retinol-binding protein 1 [Myotis lucifugus]

RecName: Full=Retinol-binding protein 1; AltName: Full=Cellular retinol-binding protein; Short=CRBP; AltName: Full=Cellular ret

TORSION ANGLE DYNAMICS COMBINED WITH SIMULATED ANNEALING FOLLOWED BY ENERGY MINIMIZATION

chemical shift assignments of the apo protein

chemical shift assignments of the holo protein