英语翻译

英语翻译
CDR-H3 resides in the center of the P5a/P5c helical interface at
the three-helix junction (Fig.5A).Residues Gly-98,Ser-100,and
Thr100a interact with the wide and shallowminor groove of P5c via
direct H bonds,and Tyr-102 contacts P5a by H bonding to U131 in
the minor groove.Several CDR-H3 residues form a pocket (Fig.
5B) that encloses U130,the bulged uridine in P5a,and they use a
variety of molecular strategies to interact with U130.Arg-94,
Ala-96,Asp-101,and Gly100c form direct H bonds to the uracil
base and sugar ring,whereas the side chains of Ala-96 and Met-99
embrace the nucleotide with nonpolar contacts.Tyr100b stacks
perpendicularly with the base,and Arg-94 forms an N-O bridgetype
of ion pair with the adjacent phosphate (36).Interestingly,
although Arg-95 was selected from the library,it makes no interaction
with the RNA in the structure; instead,its side chain points
away from theRNAand makes hydrogen bonding interactions with
the backbone carbonyl groups of Tyr100b and Met-99,possibly
stabilizing the CDR-H3 loop conformation.
CDR-L2 loop residues (defined as residues 50–56) (37) and the
flanking framework residues interact extensively with RNA,mainly
in the P5a minor groove.Residues Ser-56,Gly-57,and Ser-60 form
direct H bonds to the 3\2 strand of P5a,across from U130 near the
hinge region (Fig.5A).A possible long-range ion pair between
Arg-61 and the phosphate moiety of C197 may stabilize this
interaction.Direct H bonding between Ser-50 and the U167
phosphate links CDR-L2 to P5c,making L2 another CDR that
binds both helical stems.Tyr-49 and Tyr-55 stack perpendicularly
with U130 from the nonpolar side to seal the U130-binding pocket
generated by CDR-H3 (Fig.5B).Three water molecules organized
by the four tyrosine residues surrounding U130 interact with the
sugar–phosphate moiety,which may further strengthen the RNAFab
interaction at the nonpolar interface of the U130 binding
pocket (Fig.5C).
我需要大致了解一下它的意思,不用太准确,大概意思说一下就行