ALA A 80 - ASP A 81 OMEGA = 0.57 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION

ALA C 80 - ASP C 81 OMEGA = 0.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION

GLY B 47 - HIS B 47 OMEGA = 0.02 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION

GLY D 47 - HIS D 47 OMEGA = 0.02 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION

NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction.

Conserved Waters in Legume Lectin Crystal Structures: The Importance of Bound Waters for the Sequence-Structure Relationship within the Legume Lectin Family

Crystal Structure Determination and Refinement at 2.3 Angstroms Resolution of the Lentil Lectin

Two Crystal Forms of the Lentil Lectin Diffract to High Resolution

EACH MONOMER HAS A BOUND CALCIUM, MANGANESE, AND SUCROSE MOLECULE. THE CALCIUM AND MANGANESE IONS ARE ESSENTIAL FOR STABILIZING AN UNUSUAL ALA-ASP CIS PEPTIDE BOND THAT IS AN ESSENTIAL FEATURE OF THE CARBOHYDRATE RECOGNITION SITE OF THIS LECTIN. THESE SITES ARE PRESENTED ON *SITE* RECORDS BELOW.

THE ELECTRON DENSITY OF ONE BOUND SUCROSE MOLECULE WAS CLEARLY VISIBLE IN EACH SUGAR BINDING SITE. THE GLUCOSE MOIETY IS DIRECTLY BOUND IN THE BINDING SITE, WHILE THE CONTACT WITH THE FRUCTOSE MOIETY IS MEDIATED BY WATER MOLECULES. BOTH CARBOHYDRATE BINDING SITES INTERACT WITH EACH OTHER THROUGH CRYSTAL CONTACTS.

oligosaccharide with reducing-end-to-reducing-end glycosidic bond

THE LENTIL LECTIN MOLECULE NORMALLY EXISTS AS A DIMER. THE TWO MONOMERS IN THIS ENTRY ARE RELATED BY A PSEUDO TWO-FOLD AXIS. EACH MONOMER CONSISTS OF TWO SEPARATE POLYPEPTIDE CHAINS, ALPHA AND BETA. THE ALPHA CHAIN CONSISTS OF 181 RESIDUES AND THE BETA CHAIN CONSISTS OF 52 RESIDUES. THE ALPHA AND BETA CHAINS OF MONOMER 1 HAVE BEEN ASSIGNED CHAIN IDENTIFIERS *A* AND *B*, RESPECTIVELY, IN THIS ENTRY. THE ALPHA AND BETA CHAINS OF MONOMER 2 HAVE BEEN ASSIGNED CHAIN IDENTIFIERS *C* AND *D*, RESPECTIVELY, IN THIS ENTRY. THIS NUMBERING SCHEME IS THE SAME AS THAT USED FOR PEA LECTIN BY EINSPAHR ET AL. (ENTRY 2LTN). THE MONOMERS ARE RELATED BY A NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS PARALLEL TO THE CRYSTALLOGRAPHIC B-AXIS. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAINS *C* AND *D* WHEN APPLIED TO CHAINS *A* AND *B*, RESPECTIVELY. THE RMS BETWEEN THE BACKBONE COORDINATES IS 0.12 ANGSTROMS.