PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21523511-1	2011	PURPOSE: Several poorly water-soluble drugs have previously been shown to bind to intestinal (I-FABP) and liver fatty acid binding protein (L-FABP) in vitro.	Water	24-29	fatty acid binding protein 2	Rattus norvegicus	94-100	
17901544-5	2007	FABP increases this rate by increasing the solubility of fatty acids in water.	Water	72-77	fatty acid binding protein 2	Rattus norvegicus	0-4	
11170215-1	2001	Multiple molecular dynamics (MD) simulations of fully solvated rat intestinal fatty acid binding protein (I-FABP) were conducted to investigate the dynamics of internal water molecules.	Water	169-174	fatty acid binding protein 2	Rattus norvegicus	106-112	
11812142-11	2002	Solvent inside apo-FABP, for example, shows characteristics of a water droplet, while solvent in holo-FABP benefits from interactions with the ligand headgroup and slightly stronger interactions with protein residues.	Water	65-70	fatty acid binding protein 2	Rattus norvegicus	19-23	
11170215-2	2001	Although the long time average of the number of internal water molecules in I-FABP is 22 as shown by the X-ray crystal structure, MD simulations predict large variations in the instantaneous number of internal water molecules on the nanosecond time scale.	Water	57-62	fatty acid binding protein 2	Rattus norvegicus	76-82	
11170215-5	2001	Exchange of internal water in I-FABP appears to occur almost exclusively through the interface of beta-strands EF with the rest of the protein, which has significant implications for the pathways of the fatty acid entry and exit from the binding cavity.	Water	21-26	fatty acid binding protein 2	Rattus norvegicus	30-36	
10452609-8	1999	In holo I-FABP the fatty acid chain interactions with the hydrophilic side chains are mediated by water molecules.	Water	98-103	fatty acid binding protein 2	Rattus norvegicus	8-14	
10752611-1	2000	A single water molecule (w135), buried within the structure of rat intestinal fatty acid binding protein (I-FABP), is investigated by NMR, molecular dynamics simulations, and analysis of known crystal structures.	Water	9-14	fatty acid binding protein 2	Rattus norvegicus	67-104	
10752611-1	2000	A single water molecule (w135), buried within the structure of rat intestinal fatty acid binding protein (I-FABP), is investigated by NMR, molecular dynamics simulations, and analysis of known crystal structures.	Water	9-14	fatty acid binding protein 2	Rattus norvegicus	106-112	
10752611-8	2000	Computer simulations suggest that escape of w135 from the I-FABP matrix is primarily determined by conformational fluctuations of the protein backbone and interactions with external water molecules.	Water	182-187	fatty acid binding protein 2	Rattus norvegicus	58-64	
10452609-11	1999	The MD simulation predicts significant structural perturbations of the cavity on the subnanosecond time scale, which are capable of facilitating exchange of I-FABP internal water.	Water	173-178	fatty acid binding protein 2	Rattus norvegicus	157-163	
1429693-8	1992	The variation of these Kd values with FA molecular species is highly correlated with the solubility of the FA in water, suggesting that all these FA bind with a similar conformation in the I-FABP binding site.	Water	113-118	fatty acid binding protein 2	Rattus norvegicus	189-195	
26012957-3	2015	We use magnetic relaxation dispersion (MRD) to directly monitor internal-water dynamics in apo and palmitate-bound rat intestinal fatty acid-binding protein (rIFABP).	Water	73-78	fatty acid binding protein 2	Rattus norvegicus	158-164	
31198147-14	2019	Serum I-FABP level in the EHS+water and EHS+ORS III groups were notably lower than that in the EHS group [mug/L: 24.19 (20.00, 28.36), 0.31 (0.31, 5.58) vs. 36.90 (29.10, 45.00), both P < 0.01], additionally, I-FABP level was much lower in the EHS+ORS III group (P < 0.01).	Water	30-35	fatty acid binding protein 2	Rattus norvegicus	6-12	
26012957-4	2015	Specifically, we record the water (2)H and (17)O MRD profiles of the apo and holo forms of rIFABP in solution or immobilized by covalent cross-links.	Water	28-33	fatty acid binding protein 2	Rattus norvegicus	91-97