PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19153082-6	2009	The x-ray structures revealed surprising conformational changes of the binding cleft of HdmX, including an "open conformation" of Tyr(99) and unexpected "cross-talk" between the Trp and Leu pockets.	Leucine	186-189	MDM2 proto-oncogene	Homo sapiens	88-92	
7926727-5	1994	Rather, the hydrophobic amino acid residues Leu-22 and Trp-23 of human p53 are both required for trans-activation activity, binding to the adenovirus E1B 55-kD protein and the human mdm-2-p53 protein in vitro.	Leucine	44-47	MDM2 proto-oncogene	Homo sapiens	182-187	
7926727-6	1994	In addition, hydrophobic residues Leu-14 and Phe-19 are crucial for the interactions between p53 and human mdm-2 (hdm-2).	Leucine	34-37	MDM2 proto-oncogene	Homo sapiens	107-112	
7926727-6	1994	In addition, hydrophobic residues Leu-14 and Phe-19 are crucial for the interactions between p53 and human mdm-2 (hdm-2).	Leucine	34-37	MDM2 proto-oncogene	Homo sapiens	114-119	
34958576-4	2022	Hoping to create a novel class of membrane-permeable PPI inhibitors, the phenylalanine, tryptophan, and leucine residues that play a critical role in inhibiting the p53-HDM2 interaction were grafted into the framework of CADY2 a cell-penetrating peptide (CPP) having a helical propensity.	Leucine	104-111	MDM2 proto-oncogene	Homo sapiens	169-173	
31226791-10	2019	The resultant analog sequence Ac-Leu-Thr-Phe-Aib-Glu-Tyr-Trp-Gln-Leu-Cba-Aib-Ser-Ala-Ala-NH2 exhibited high-affinity target binding (Mdm2 Kd = 43 nM) and significant alpha-helicity in circular dichroism studies.	Leucine	33-36	MDM2 proto-oncogene	Homo sapiens	133-137	
34977581-3	2021	X-Ray crystallography reveals a novel binding mode utilizing a unique pharmacophore to occupy the Phe/Trp/Leu pockets on MDM2.	Leucine	106-109	MDM2 proto-oncogene	Homo sapiens	121-125	
18707164-2	2008	The result of the calculation, based on structures from nanosecond molecular dynamics simulation, revealed that (19)Phe, (22)Leu, and (23)Trp of p53 have the strongest binding interaction with MDM2 followed by (26)Leu and (27)Pro.	Leucine	125-128	MDM2 proto-oncogene	Homo sapiens	193-197	
18707164-2	2008	The result of the calculation, based on structures from nanosecond molecular dynamics simulation, revealed that (19)Phe, (22)Leu, and (23)Trp of p53 have the strongest binding interaction with MDM2 followed by (26)Leu and (27)Pro.	Leucine	214-217	MDM2 proto-oncogene	Homo sapiens	193-197	
18707164-3	2008	The specific residues of MDM2 that have dominant binding interactions with p53 are specifically identified to be (51)Lys, (54)Leu, (62)Met, (67)Tyr, (72)Gln, (94)Lys, (96)His, and (100)Tyr.	Leucine	126-129	MDM2 proto-oncogene	Homo sapiens	25-29	
11925449-5	2002	Mutation of conserved amino acids in the linker at Ser(261) and Leu(264), which bridges the S9-S10 beta-sheets, stimulated p53 activity from reporter templates and increased MDM2-dependent ubiquitination of p53.	Leucine	64-67	MDM2 proto-oncogene	Homo sapiens	174-178	
17002294-5	2006	Specificity for binding MDM2 via FXX phi phi motifs derives almost entirely from Trp23 of p53, with a 3.0 kcal mol(-1) loss of binding energy when Trp23 is changed to p65-derived Leu.	Leucine	179-182	MDM2 proto-oncogene	Homo sapiens	24-28	
15600307-2	2004	A retroinverso isomer of the natural N-terminal helical peptide was found to interact with MDM2 using the same hydrophobic residues, Phe, Trp, and Leu.	Leucine	147-150	MDM2 proto-oncogene	Homo sapiens	91-95