annotation_CSV/PMC4781976.csv

anno_start	anno_end	anno_text	entity_type	sentence	section
0	9	Structure	evidence	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
17	20	GAT	structure_element	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
45	60	adapter protein	protein_type	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
61	65	Tom1	protein	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
50	71	cell-surface receptor	protein_type	Cellular homeostasis requires correct delivery of cell-surface receptor proteins (cargo) to their target subcellular compartments.	ABSTRACT
4	20	adapter proteins	protein_type	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
21	25	Tom1	protein	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
30	36	Tollip	protein	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
64	77	ubiquitinated	ptm	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
15	19	Tom1	protein	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
69	72	GAT	structure_element	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
97	103	Tollip	protein	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
106	125	Tom1-binding domain	structure_element	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
127	130	TBD	structure_element	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
36	48	solution NMR	experimental_method	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
57	66	structure	evidence	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
74	78	Tom1	protein	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
79	82	GAT	structure_element	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
22	31	structure	evidence	The estimated protein structure exhibits a bundle of three helical elements.	ABSTRACT
3	10	compare	experimental_method	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
15	19	Tom1	protein	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
20	23	GAT	structure_element	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
24	33	structure	evidence	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
45	55	structures	evidence	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
77	83	Tollip	protein	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
84	88	TBD-	protein_state	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
93	108	ubiquitin-bound	protein_state	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
141	159	Circular dichroism	experimental_method	"Subject area	Biology	 	More specific subject area	Structural biology	 	Type of data	Table, text file, graph, figures	 	How data was acquired	Circular dichroism and NMR."	TABLE
164	167	NMR	experimental_method	"Subject area	Biology	 	More specific subject area	Structural biology	 	Type of data	Table, text file, graph, figures	 	How data was acquired	Circular dichroism and NMR."	TABLE
0	3	NMR	experimental_method	"NMR data was recorded using a Bruker 800 MHz	 	Data format	PDB format text file."	TABLE
12	22	CS-Rosetta	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
24	59	Protein Structure Validation Server	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
61	65	PSVS	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
68	75	NMRPipe	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
77	84	NMRDraw	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
131	136	human	species	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
137	141	Tom1	protein	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
142	145	GAT	structure_element	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
216	234	Solution structure	evidence	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
238	242	Tom1	protein	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
243	246	GAT	structure_element	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
267	270	NMR	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
271	285	chemical shift	evidence	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
5	8	GAT	structure_element	"Tom1 GAT structural data is publicly available in the RCSB Protein Data Bank (http://www.rscb.org/) under the accession number PDB: 2n9d	 	"	TABLE
4	8	Tom1	protein	The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.	TABLE
9	12	GAT	structure_element	The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.	TABLE
20	38	solution structure	evidence	The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.	TABLE
0	4	Tom1	protein	Tom1 GAT can adopt distinct conformations upon ligand binding.	TABLE
5	8	GAT	structure_element	Tom1 GAT can adopt distinct conformations upon ligand binding.	TABLE
33	37	Tom1	protein	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
38	41	GAT	structure_element	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
54	60	Tollip	protein	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
61	64	TBD	structure_element	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
16	41	far-UV circular dichroism	experimental_method	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
43	45	CD	experimental_method	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
47	55	spectrum	evidence	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
63	68	Tom 1	protein	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
69	72	GAT	structure_element	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
104	111	α-helix	structure_element	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
116	124	β-strand	structure_element	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
4	8	Tom1	protein	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
9	12	GAT	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
13	34	structural restraints	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
55	65	structures	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
85	111	root mean square deviation	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
113	117	RMSD	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
243	252	Q216-E240	residue_range	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
254	263	α-helix 1	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
266	275	P248-Q274	residue_range	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
277	286	α-helix 2	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
293	302	E278-T306	residue_range	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
304	313	α-helix 3	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
7	16	ubiquitin	chemical	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
74	78	Tom1	protein	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
79	82	GAT	structure_element	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
83	100	α-helices 1 and 2	structure_element	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
112	118	Tollip	protein	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
119	122	TBD	structure_element	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
15	24	far-UV CD	experimental_method	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
25	33	spectrum	evidence	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
41	45	His-	experimental_method	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
45	49	Tom1	protein	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
50	53	GAT	structure_element	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
40	62	backbone superposition	experimental_method	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
78	88	structures	evidence	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
97	101	Tom1	protein	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
102	105	GAT	structure_element	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
96	100	Tom1	protein	Helices are shown in orange, whereas loops are colored in green. (B) Ribbon illustration of the Tom1 GAT domain.	FIG
101	104	GAT	structure_element	Helices are shown in orange, whereas loops are colored in green. (B) Ribbon illustration of the Tom1 GAT domain.	FIG
21	44	superimposed structures	experimental_method	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
52	56	Tom1	protein	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
57	60	GAT	structure_element	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
75	79	free	protein_state	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
110	116	Tollip	protein	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
117	126	TBD-bound	protein_state	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
161	184	superimposed structures	experimental_method	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
192	196	Tom1	protein	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
197	200	GAT	structure_element	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
232	240	Ub-bound	protein_state	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
0	3	NMR	experimental_method	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
8	29	refinement statistics	evidence	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
38	42	Tom1	protein	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
43	46	GAT	structure_element	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
0	3	NMR	experimental_method	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
4	25	structural statistics	evidence	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
58	62	Tom1	protein	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
63	66	GAT	structure_element	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
73	77	PSVS	experimental_method	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
28	41	superimposing	experimental_method	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
51	58	215–309	residue_range	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
62	66	Tom1	protein	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
67	70	GAT	structure_element	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
102	112	structures	evidence	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE