THE MECHANISM OF IRON UPTAKE BY TRANSFERRINS: THE STRUCTURE OF AN 18KD NII-DOMAIN FRAGMENT AT 2.3 ANGSTROMS RESOLUTION
GLY 104 - THR 105 OMEGA ANGLE = 137.204 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
ALA 126 - GLY 127 OMEGA ANGLE = 217.267 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
ILE 141 - GLU 142 OMEGA ANGLE = 143.256 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
GLU 142 - SER 143 OMEGA ANGLE = 242.000 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
GLU 224 - LEU 225 OMEGA ANGLE = 211.241 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
The mechanism of iron uptake by transferrins: the structure of an 18 kDa NII-domain fragment from duck ovotransferrin at 2.3 A resolution.
New Perspectives on the Structure and Function of Transferrins
High-Resolution X-Ray Studies on Rabbit Serum Transferrin-Preliminary Structure Analysis of the N-Terminal Half-Molecule at 2.3 Angstroms Resolution
Molecular Structure of Serum Transferrin at 3.3 Angstroms Resolution
SYYAVAVVKKGTDFMIKDLRGKTSCHTGLGRSAGWNIPIGTLIHREDIEWEGIESGSVEQAVAKFFSASCVPGATIEQKL CRQCKGDAKTKCLRNAPYSGYSGAFQCLKDGKGDVAFVKHTTVQENAPEEKDEYELLCLDGSRQPVDSYKTCNWARVAA
THE SEQUENCE IS THAT DETERMINED BY THE AUTHORS.
OVOTRANSFERRIN (18 KDA FRAGMENT, DOMAIN II FROM N-TERMINAL LOBE)
APPKTTVRWCTISSAEEKKCNSLKDHMQQERVTLSCVQKATYLDCIKAISNNEADAISLDGGQVFEAGLAPYKLKPIAAE VYERSGGSTTSYYAVAVVKKGTDFMIKDLRGKTSCHTGLGRSAGWNIPIGTLIHREDIEWEGIESGISEQAVAKFFSASC VPGATIEQKLCRQCKGDAKTKCLRNGPYSGYSGAFQCLKDGKGDVAFVKHTTVQENAPEEKDEYELLCLDGSRQPVDSYK TCNWARVAAHAVVARDDSKIDDIWSFLGMQAYSLGVDTTSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPELMDSQLYL GFEYYSAIQSLRKDQLTVGPRENKIQWCAVGKDEKSKCDRWSVVSNGEVECTILDDNKDCIVKITKGEADAISLDGGFVY TAGVCGLVPVVGESYEDETQCSKDEEQPAYYFAVAVVKKSSAITWNNLQGKKSCHTAVGRTAGWNIPMGLIHNKTGSCDF DDYFSEGCAPGSPPNSRLCKLCQGSGENLLEKCVASSHEKYYGYTGALRCLVEQGDVAFIKHSTVGENVSGSNKDDWAKG LTRDDFELLCTNGKRAKTMDYKTCHLAKVPTHAVVARPEKANKIRELLEGQEKLFGLHGTEKERFMMFQSQTKDLLFKAL TKCLVKLRQGITYKEFLGDEYYASVASLNTCNPSDLLQVCTFLEDK