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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
401	1995-07-31	Chemical Shifts: 1 set	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi
402	1995-07-31	Chemical Shifts: 1 set	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi
417	1995-07-31	Chemical Shifts: 1 set	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi