PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8590002-8	1995	The structure of the Abl SH(32) dual domain was characterized by NMR spectroscopy using the 1H and 15N resonance assignment of Abl SH3 and Abl SH2.	Hydrogen	92-94	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	21-24	
34508625-11	2021	Molecular docking analysis shows that ABL1 interacts with Cofilin1 mainly through hydrogen bonds and ionic interaction between amino acid residues.	Hydrogen	82-90	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	38-42	
1281542-2	1992	Assignments of nearly all 1H and 15N resonances of the SH2 domain from the c-Abl protein-tyrosine kinase have been obtained from homonuclear and heteronuclear NMR experiments.	Hydrogen	26-28	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	75-80	
35470777-4	2022	According to the data obtained, these compounds exhibit close modes of binding to the Abl kinase active site that are mainly provided by hydrogen bonds and multiple van der Waals contacts.	Hydrogen	137-145	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	86-89	
32424388-3	2020	As an example, the crystal structure of the kinase inhibitor dasatinib bound to the Abl1 kinase shows a hydrogen bond between the drug and residue Thr315 and very few contacts between the drug and residues Val299 and Phe317, yet mutations in those residues lead to drug resistance.	Hydrogen	104-112	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	84-88	
35172577-4	2022	The developed 2D-QSAR model showed five information rich molecular descriptors while the 3D-pharmacophore model of BCR-ABL showed five different chemical features (hydrogen bond acceptor, donor, hydrophobic group, positive ion group, and aromatic rings) and the HDAC model showed four different chemical features (hydrogen bond acceptor, donor, positive ion group, and aromatic rings) for potent BCR-ABL and HDAC inhibition.	Hydrogen	164-172	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	119-122	
35172577-4	2022	The developed 2D-QSAR model showed five information rich molecular descriptors while the 3D-pharmacophore model of BCR-ABL showed five different chemical features (hydrogen bond acceptor, donor, hydrophobic group, positive ion group, and aromatic rings) and the HDAC model showed four different chemical features (hydrogen bond acceptor, donor, positive ion group, and aromatic rings) for potent BCR-ABL and HDAC inhibition.	Hydrogen	314-322	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	119-122	
20808434-3	2010	To understand this, comprehensive analysis of hydrophobic interactions, hydrogen bonding and binding affinity have been analyzed at the interface of c-Src and c-Abl kinases and 4-amino substituted 1H-pyrazolo [3, 4-d] pyrimidine compounds.	Hydrogen	72-80	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	159-164	
20072125-2	2010	Here, using solution NMR, X-ray crystallography, mutagenesis and hydrogen exchange mass spectrometry, we show that GNF-2 binds to the myristate-binding site of Abl, leading to changes in the structural dynamics of the ATP-binding site.	Hydrogen	65-73	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	160-163	
28338290-6	2017	Further, the conformational transition, hydrogen bond interactions, and the binding energies were investigated during 10-ns molecular dynamics simulation of the Abl-hit complex.	Hydrogen	40-48	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	161-164	
27966954-1	2017	The discovery of a novel potent type II ABL/c-KIT dual kinase inhibitor compound 34 (CHMFL-ABL/KIT-155), which utilized a hydrogen bond formed by NH on the kinase backbone and carbonyl oxygen of 34 as a unique hinge binding, is described.	Hydrogen	122-130	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	40-43	
23679864-7	2013	The results of molecular dynamics simulations indicated that the dynamic stabilities of the hydrogen bonds between the inhibitors and Met318 should also be considered in designing the potent common inhibitors of the wild-type and T315I mutant of ABL.	Hydrogen	92-100	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	246-249	
19164531-4	2009	Hydrogen exchange mass spectrometry (HX MS) was used to compare the conformations of wild-type Abl with a nonmyristoylated form and with 3 clinically relevant imatinib resistance mutants (T315I, Y253H and E255V).	Hydrogen	0-8	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	95-98