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. 2016 Feb 2;5:e13571. doi: 10.7554/eLife.13571

Table 4.

NMR-derived dissociation constant (KD) values determined by monitoring chemical shift perturbations of individual N130 nitrogen backbone resonances while titrating the rpL5 peptide.

DOI: http://dx.doi.org/10.7554/eLife.13571.018

Residue Structural context KD (μM)
Met5 N-terminus 385 ± 108
Asp6 N-terminus 116 ± 25
Met7 N-terminus 142 ± 30
Ser10 N-terminus 56 ± 13
Leu12 N-terminus 10 ± 5
Arg13 N-terminus 58 ± 13
Gln15 Core 36 ± 10
Tyr17 Core 19 ± 9
Leu18 Core 205 ± 51
Val33 Core 1041 ± 649
Asp36 A1 tract 329 ± 93
Glu37 A1 tract 1549 ± 1168
Glu39 A1 tract 115 ± 37
His40 Core 123 ± 23
Leu42 Core 24 ± 9
Ser43 Core 166 ± 38
Ala64 Core 1227 ± 562
Asn66 Core 1530 ± 958
Tyr67 Core 245 ± 58
Glu68 Core 147 ± 29
Val74 Core 53 ± 14
Phe92 Core 14 ± 6
Glu93 Core 329 ± 78
Ile94 Core 73 ± 17
Thr95 Core 34 ± 9
Leu116 Core 101 ± 24
Val117 Core 61 ± 17
Ala118 Core 35 ± 9
Glu120 A2 tract 68 ± 16
Glu121 A2 tract 101 ± 18
Asp122 A2 tract 279 ± 76
Ala123 A2 tract 182 ± 50
Glu124 A2 tract 614 ± 410
Glu126 A2 tract 576 ± 471
Asp127 A2 tract 2162 ± 1612
Glu130 A2 tract 4258 ± 1986