PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
20496919-5	2010	Sequential and side chain assignment of IFNAR2-EC and IFNalpha2 in their binary complex helped assign the intermolecular NOEs to the corresponding protons.	noes	121-125	interferon alpha and beta receptor subunit 2	Homo sapiens	40-46
20496919-5	2010	Sequential and side chain assignment of IFNAR2-EC and IFNalpha2 in their binary complex helped assign the intermolecular NOEs to the corresponding protons.	noes	121-125	interferon alpha 2	Homo sapiens	54-63
20496919-6	2010	A docking model of the IFNAR2-EC-IFNalpha2 complex was calculated on the basis of the intermolecular interactions found in this study as well as four double mutant cycle constraints, previously observed NOEs between a single pair of residues and the NMR mapping of the binding sites on IFNAR2-EC and IFNalpha2.	noes	203-207	interferon alpha and beta receptor subunit 2	Homo sapiens	23-29
20496919-6	2010	A docking model of the IFNAR2-EC-IFNalpha2 complex was calculated on the basis of the intermolecular interactions found in this study as well as four double mutant cycle constraints, previously observed NOEs between a single pair of residues and the NMR mapping of the binding sites on IFNAR2-EC and IFNalpha2.	noes	203-207	interferon alpha 2	Homo sapiens	33-42
16384999-5	2006	We have determined the NMR structure of the HDGF PWWP domain to high resolution using a combination of NOEs, J-couplings, and dipolar couplings.	noes	103-107	heparin binding growth factor	Homo sapiens	44-48
20164409-4	2010	Measurements on three beta-PGM-MgF-3 -sugar phosphate complexes show a remarkable relationship between NMR chemical shifts, primary isotope shifts, NOEs, cross hydrogen bond F...H-N scalar couplings, and the atomic positions determined from the high-resolution crystal structure of the beta-PGM-MgF--3 -G6P complex.	noes	148-152	signal transducer and activator of transcription 5A	Homo sapiens	31-34
19907790-1	2009	The solution structure of a 14 base-pair non-self complementary DNA duplex containing the consensus-binding site of the yeast transcription factor Mbp1 has been determined by NMR using a combination of scalar coupling analysis, time-dependent NOEs, residual dipolar couplings and 13C-edited NMR spectroscopy of a duplex prepared with one strand uniformly labeled with 13C-nucleotides.	noes	243-247	transcription factor MBP1	Saccharomyces cerevisiae S288C	147-151
16964534-12	2006	The method was applied to measure individual intermolecular NOEs between the anti-apoptotic protein Bcl-xL at 25 microM and a "first generation" small-molecule ligand, for which the spectrum is entirely broadened at stoichiometric concentrations.	noes	60-64	BCL2 like 1	Homo sapiens	100-106
18830565-2	2008	Unambiguous assignments of the bound inhibitor and intermolecular NOEs between the Grb2 SH2 domain and the inhibitor was accomplished using perdeuterated Grb2 SH2 protein.	noes	66-70	growth factor receptor bound protein 2	Homo sapiens	83-87
18830565-2	2008	Unambiguous assignments of the bound inhibitor and intermolecular NOEs between the Grb2 SH2 domain and the inhibitor was accomplished using perdeuterated Grb2 SH2 protein.	noes	66-70	growth factor receptor bound protein 2	Homo sapiens	154-158
16787334-6	2005	Additionally, the C-terminal of [Tyr3]octreotate, comprising Cys7 and Thr8, appears to form a turn-like structure manifested by characteristic side-chain NOEs between Lys5 and Thr8, which have not been detected for the other two compounds.	noes	154-158	aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase	Homo sapiens	167-171
11841216-9	2002	Two native-like contacts are implied by NOEs in reduced and unfolded BPTI, between residues Tyr23 and Ala25, and between Gly37 NH and the Tyr35 ring.	noes	40-44	spleen trypsin inhibitor I	Bos taurus	69-73
14752254-1	2004	We demonstrate improved accuracy in protein structure determination for large (>/=30 kDa), deuterated proteins (e.g. STAT4(NT)) via the combination of pseudocontact shifts for amide and methyl protons with the available NOEs in methyl-protonated proteins.	noes	223-227	signal transducer and activator of transcription 4	Homo sapiens	120-125
9889202-4	1999	Long-range NOEs indicate that beta1 and beta3 interact with each other.	noes	11-15	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	30-45
11045617-5	2000	The NMR studies have also allowed the DNase contact surface on Im9 to be investigated through changes in backbone chemical shifts and NOEs between the two proteins determined from comparisons of 1H-1H-13C NOESY-HSQC spectra with and without 13C decoupling.	noes	134-138	colicin E8	Escherichia coli	38-43
10441120-6	1999	In particular, the partially disordered residues Val86-Arg97 that contain the human cyclophilin A (CypA) packaging signal have (15)N heteronuclear NOEs and transversal relaxation rates consistent with a high degree of dynamic conformational averaging.	noes	147-151	peptidylprolyl isomerase A	Homo sapiens	84-97
10441120-6	1999	In particular, the partially disordered residues Val86-Arg97 that contain the human cyclophilin A (CypA) packaging signal have (15)N heteronuclear NOEs and transversal relaxation rates consistent with a high degree of dynamic conformational averaging.	noes	147-151	peptidylprolyl isomerase A	Homo sapiens	99-103
10320322-11	1999	Structure calculations based on the observed transferred NOEs show that the central portion of the Cdc42-bound CRIB peptide assumes a loop conformation in which the side chains of consensus residues Phe80, His82, Ile84, His85, and Val86 are brought into proximity.	noes	57-61	cell division cycle 42	Homo sapiens	99-104
9692951-4	1998	Transferred NOESY NMR showed a number of long-range NOEs, from the gp120-bound state, between residues 38, 40, 45, 48, and 49 of the peptide.	noes	52-56	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	67-72
9933923-7	1999	As illustrated by the study of the PMP1 fragment, paramagnetic relaxation data also allow us to supply the missing medium-range NOEs and therefore to complete a standard conformational analysis of peptides in micelles.	noes	128-132	peroxisomal biogenesis factor 19	Homo sapiens	35-39
8393341-8	1993	A comparison of the tail region of NPK with the related peptide homologue, neurokinin A, in the same solvent system, indicates that both show increasing order when trifluoroethanol is titrated into water solution, with the appearance of sequential NOEs between backbone amide protons.	noes	248-252	tachykinin precursor 1	Homo sapiens	35-38
9680059-3	1998	HMQC NOESY spectra of the labelled Leu-enkephalin in a DMSOd6/H2O) mixture at 275 K do show numerous NOEs, but these are not consistent with a single conformer and are only sufficient to describe the conformational state as a mixture of several conformers.	noes	101-105	prodynorphin	Homo sapiens	35-49
9199409-3	1997	The starting point for ARIA is an almost complete assignment of the proton chemical shifts, and a list of partially assigned NOEs, mostly sequential and secondary structure NOEs.	noes	125-129	endothelial cell surface expressed chemotaxis and apoptosis regulator	Homo sapiens	23-27
9199409-3	1997	The starting point for ARIA is an almost complete assignment of the proton chemical shifts, and a list of partially assigned NOEs, mostly sequential and secondary structure NOEs.	noes	173-177	endothelial cell surface expressed chemotaxis and apoptosis regulator	Homo sapiens	23-27
8845763-5	1996	The beta 1 strand is parallel to the beta 2 strand of the same subunit on the basis of cross stand NH(i)-NH(j) NOEs in a 2D 15N-edited 1H-NOESY spectrum of hexameric 4-OT containing two 15N-labeled subunits/hexamer.	noes	111-115	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	4-10
7756285-4	1995	Long-range NOEs indicate that the global folding pattern of human IL-3 is a four-helical bundle with an up-up-down-down arrangement of helices that is similar to that of other members of the cytokine family, such as granulocyte-macrophage colony stimulating factor (GM-CSF).	noes	11-15	interleukin 3	Homo sapiens	66-70
9729790-6	1998	From chemical shifts and on the basis of inter-residue NOEs, we have inferred the secondary structure and topology of monomeric beta-LG A.	noes	55-59	beta-lactoglobulin	Bos taurus	128-135
9923693-7	1998	H3 becomes much more ordered in a mixture of 50:50 H2O-dimethyl sulfoxide as indicated by the numerous NOEs, including several side chain to side chain and side chain to backbone connectivities.	noes	103-107	histatin 3	Homo sapiens	0-2
9135122-0	1997	Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts.	noes	134-138	growth factor receptor bound protein 2	Mus musculus	26-30
9007990-9	1997	The HLH region of E47 is structured, but highly dynamic as judged by the rapid exchange of backbone hydrogen atoms and the relatively weak intensities of many of the NOEs defining the dimerization helices.	noes	166-170	transcription factor 3	Homo sapiens	18-21
8111229-0	1993	Measurement of amide proton exchange rates and NOEs with water in 13C/15N-enriched calcineurin B.	noes	47-51	protein phosphatase 3 regulatory subunit B, alpha	Homo sapiens	83-96
8393341-8	1993	A comparison of the tail region of NPK with the related peptide homologue, neurokinin A, in the same solvent system, indicates that both show increasing order when trifluoroethanol is titrated into water solution, with the appearance of sequential NOEs between backbone amide protons.	noes	248-252	tachykinin precursor 1	Homo sapiens	75-87
2789994-7	1989	A wobble alignment of the O6alkG4.C9 base pair stablized by two hydrogen bonds, one between the amino group of C9 and N1 of O6alkG and the other between the amino group of O6alkG and N3 of C9, is tentatively proposed on the basis of the NOEs between the amino protons of C9 at the lesion site and the imino protons of flanking Watson-Crick base pairs.	noes	237-241	complement C9	Homo sapiens	111-130
1993196-8	1991	These structures can be differentiated on the basis of the observed NOEs from the imino proton of dT5 to the imino proton of dG4 but not dG6 and to the amino protons of dC15 but not dC13 that were not included in the constraints data set used in energy minimization.	noes	68-72	achaete	Drosophila melanogaster	98-101
1993197-6	1991	We detect a set of intra- and interstrand NOEs between protons (exchangeable and nonexchangeable) on adjacent residues in the d(G4-G5-G6).d(C13-epsilon A14-C15) trinucleotide segment which establish formation of right-handed helical conformations on both strands and stacking of the dG5(anti).epsilon dA14(syn) pair between stable dG4.dC15 and dG6.dC13 pairs.	noes	42-46	placenta associated 8	Homo sapiens	140-159
1993197-6	1991	We detect a set of intra- and interstrand NOEs between protons (exchangeable and nonexchangeable) on adjacent residues in the d(G4-G5-G6).d(C13-epsilon A14-C15) trinucleotide segment which establish formation of right-handed helical conformations on both strands and stacking of the dG5(anti).epsilon dA14(syn) pair between stable dG4.dC15 and dG6.dC13 pairs.	noes	42-46	synemin	Homo sapiens	306-309
1332764-3	1992	Measurement of transferred NOEs and molecular modeling indicate that the side chain of the Asp(P3) residue may form a hydrogen bond with thrombin and, by doing so, it is brought near a positively-charged thrombin residue Arg(221A), thereby partially neutralizing the negative charge of an Asp residue at this site of protein substrates.	noes	27-31	coagulation factor II, thrombin	Bos taurus	137-145
1332764-3	1992	Measurement of transferred NOEs and molecular modeling indicate that the side chain of the Asp(P3) residue may form a hydrogen bond with thrombin and, by doing so, it is brought near a positively-charged thrombin residue Arg(221A), thereby partially neutralizing the negative charge of an Asp residue at this site of protein substrates.	noes	27-31	coagulation factor II, thrombin	Bos taurus	204-212
2207078-12	1990	Since the repressor is a symmetric dimer, long-range intersubunit NOEs were distinguished from intrasubunit interactions by formation of heterodimers between two appropriate selectively deuterated proteins and comparison of the resulting NOESY spectrum with that of each selectively deuterated homodimer.	noes	66-70	repressor	Escherichia coli	10-19
2350549-4	1990	Hirudin fragments take on a well-defined structure when bound to thrombin as indicated by several long-range transferred NOEs between the backbone and side-chain protons of the peptides, but they are not structured when free in solution.	noes	121-125	coagulation factor II, thrombin	Bos taurus	65-73
2730873-6	1989	Complete sets of NOEs were obtained for VIP" in 25% methanol, pH 4, and in 50% methanol, pH 6.	noes	17-21	vasoactive intestinal peptide	Homo sapiens	40-43
2742826-5	1989	There is a chain reversal within residues Asp(7)-Arg(16) such that Phe(8) is brought close to the Arg(16)-Gly(17) peptide bond in the thrombin-peptide complex, as indicated by transferred NOEs between the aromatic ring protons of Phe(8) and the C alpha H protons of Gly(14) and the C gamma H protons of Val(15).	noes	188-192	coagulation factor II, thrombin	Homo sapiens	134-142
3266557-7	1988	The NMR data, combined with known disulfide linkages and a small number of critical long-range NOEs, provide the global folding pattern of C3a in solution.	noes	95-99	complement C3	Homo sapiens	139-142
2855784-9	1985	Difference NOE spectra of netropsin-poly(dA).poly(dT) complex in which AH2 was irradiated indicate that dominant NOEs were observed at the imino and pyrrole ring protons of netropsin.	noes	113-117	zinc finger RANBP2-type containing 3	Homo sapiens	71-74
6849902-5	1983	Differentially evolving NOEs are also generated between aromatic protons and the C-2" methylene protons on both the same residue and on the neighboring 5" residue.	noes	24-28	complement C2	Homo sapiens	81-84