Table 3.

Averaged differences in deuterium incorporation percentages for twenty-four hRXRα-LBD peptic peptides relative to apo-hRXRα-LBD for three conditions.

Peptide Sequence	Secondary Structure	hRXRα-LBD	hRXRα-LBD:GRIP-1	hRXRα-LBD:9cRA	hRXRα-LBD:9cRA: GRIP-1
G219SHMTSSANEDMPVERILE237	H1	73%	−5	−3	−5
A241VEPKTET248	H1	100%	−1	0	1
A241VEPKTETYVE251	H1	100%	−8	−3	−11
A271ADKQLFT278	H3	99%	−14	−15	−30
A271ADKQLFTL279	H3	100%	−9	−28	−39
L279VEWAKRIPHFSELPLDDQ297	H3	30%	−2	−1	−2
L301RAGWNEL308	H4	37%	−11	−12	−20
L309IASFSHRSIAVKDGIL325	H5	57%	−5	−24	−27
L326ATGLHVHRNSAHSAGVGAIF346	Beta	65%	−5	−9	−12
D347RVLTEL353	H7	48%	−5	−31	−35
V354SKMRDMQM362	H7	69%	−8	−31	−38
D363KTEL367	H8	41%	−8	−6	−6
D363KTELGCL370	H8	20%	−4	0	−1
R371AIVLFNPDSKGLSNPAEVEA391	H8	50%	−4	1	−3
I373VLFNPDSKGLSNPAEVEA391	H8	53%	−4	0	−5
L392REKVYASL400	H9	3%	−1	−1	0
E401AYCKHKYPEQPGRF415	H9	40%	−2	1	−2
L419LRLPALRSIGLKC432	H10	86%	−6	−37	−47
L419LRLPALRSIGLKCLEHLFF438	H10	91%	−9	−26	−37
P423ALRSIGLKCLEHLFF438	H11	88%	−8	−25	−37
L433EHLFF438	H11	80%	−8	−1	−10
F439KLIGDTPIDTFL451	H11	88%	−1	−3	−5
F450LMEM454	H12	92%	−17	4	−14
L455EAPHQMT462	CTERM	84%	−3	−2	−6

Values reflect differences in percent deuterium incorporation for each peptic peptide averaged across five time points (15 s, 30 s, 120 s, 900 s, 3600 s) relative to apo-hRXRα-LBD (column 3). Negative values indicate an increased level of protection for that peptide under the indicated conditions and are color coded in increasing shades of blue. Differences <5% are considered insignificant (shown in grey). Peptides are listed from N- to C- terminus, holo structural element indicated in column 2. Observed hRXRα-LBD amino acid contacts with 9cRA are in red. Observed hRXRα-LBD amino acid contacts with GRIP1 are underlined.