FMO DATABASE

FMODB ID: Y9GR2

Calculation Name: 1RHF-A-Xray547

Preferred Name: Tyrosine-protein kinase receptor TYRO3

Target Type: SINGLE PROTEIN

Ligand Name: 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid | acetate ion

Ligand 3-letter code: EPE | ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1RHF

Chain ID: A

ChEMBL ID: CHEMBL5314

UniProt ID: Q06418

Base Structure: X-ray

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	174
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1492835.603734
FMO2-HF: Nuclear repulsion	1425851.536972
FMO2-HF: Total energy	-66984.066762
FMO2-MP2: Total energy	-67178.687661

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)

Summations of interaction energy for fragment #1(A:7:GLY)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-124.744	-121.83	3.21	-3.164	-2.96	-0.033

Interaction energy analysis for fragmet #1(A:7:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.847 / q_NPA : 0.916

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	9	PRO	0	0.011	0.026	3.593	5.949	7.275	-0.008	-0.552	-0.765	-0.003
82	A	89	GLN	0	0.020	0.007	2.246	-24.398	-22.818	3.219	-2.605	-2.195	-0.030
83	A	90	PRO	0	0.000	-0.007	4.773	3.139	3.147	-0.001	-0.007	0.000	0.000
4	A	10	VAL	0	0.042	0.023	6.136	2.618	2.618	0.000	0.000	0.000	0.000
5	A	11	LYS	1	0.926	0.953	9.344	30.049	30.049	0.000	0.000	0.000	0.000
6	A	12	LEU	0	0.026	0.027	12.441	1.018	1.018	0.000	0.000	0.000	0.000
7	A	13	THR	0	0.006	-0.002	15.724	0.088	0.088	0.000	0.000	0.000	0.000
8	A	14	VAL	0	-0.010	0.001	18.617	0.447	0.447	0.000	0.000	0.000	0.000
9	A	15	SER	0	-0.018	-0.013	21.809	-0.080	-0.080	0.000	0.000	0.000	0.000
10	A	16	GLN	0	-0.030	-0.046	25.259	0.052	0.052	0.000	0.000	0.000	0.000
11	A	17	GLY	0	0.011	0.017	26.754	0.314	0.314	0.000	0.000	0.000	0.000
12	A	18	GLN	0	-0.069	-0.023	25.670	0.282	0.282	0.000	0.000	0.000	0.000
13	A	19	PRO	0	-0.013	0.010	25.924	-0.310	-0.310	0.000	0.000	0.000	0.000
14	A	20	VAL	0	-0.023	-0.018	20.028	-0.230	-0.230	0.000	0.000	0.000	0.000
15	A	21	LYS	1	0.888	0.941	20.879	12.373	12.373	0.000	0.000	0.000	0.000
16	A	22	LEU	0	-0.012	0.013	15.289	-0.558	-0.558	0.000	0.000	0.000	0.000
17	A	23	ASN	0	-0.044	-0.038	15.390	0.277	0.277	0.000	0.000	0.000	0.000
18	A	24	CYS	0	-0.004	0.011	11.115	0.870	0.870	0.000	0.000	0.000	0.000
19	A	25	SER	0	0.044	0.017	12.849	1.801	1.801	0.000	0.000	0.000	0.000
20	A	26	VAL	0	0.004	-0.011	12.947	-1.781	-1.781	0.000	0.000	0.000	0.000
21	A	27	GLU	-1	-0.900	-0.955	14.715	-16.628	-16.628	0.000	0.000	0.000	0.000
22	A	28	GLY	0	0.027	0.011	16.011	-0.821	-0.821	0.000	0.000	0.000	0.000
23	A	29	MET	0	0.018	0.017	18.536	0.061	0.061	0.000	0.000	0.000	0.000
24	A	30	GLU	-1	-0.955	-0.976	20.576	-11.458	-11.458	0.000	0.000	0.000	0.000
25	A	31	GLU	-1	-0.956	-0.977	23.948	-10.916	-10.916	0.000	0.000	0.000	0.000
26	A	32	PRO	0	-0.022	-0.007	18.916	-0.090	-0.090	0.000	0.000	0.000	0.000
27	A	33	ASP	-1	-0.872	-0.939	20.913	-13.175	-13.175	0.000	0.000	0.000	0.000
28	A	34	ILE	0	-0.062	-0.033	16.341	-0.875	-0.875	0.000	0.000	0.000	0.000
29	A	35	GLN	0	-0.011	-0.005	17.426	0.357	0.357	0.000	0.000	0.000	0.000
30	A	36	TRP	0	-0.031	-0.018	13.396	-1.767	-1.767	0.000	0.000	0.000	0.000
31	A	37	VAL	0	-0.027	-0.001	13.371	0.935	0.935	0.000	0.000	0.000	0.000
32	A	38	LYS	1	0.888	0.948	14.228	14.877	14.877	0.000	0.000	0.000	0.000
33	A	39	ASP	-1	-0.888	-0.953	12.730	-19.965	-19.965	0.000	0.000	0.000	0.000
34	A	40	GLY	0	-0.011	-0.001	13.528	0.286	0.286	0.000	0.000	0.000	0.000
35	A	41	ALA	0	-0.024	0.001	14.410	0.687	0.687	0.000	0.000	0.000	0.000
36	A	42	VAL	0	0.054	0.025	17.234	-0.639	-0.639	0.000	0.000	0.000	0.000
37	A	43	VAL	0	-0.029	-0.015	17.679	0.656	0.656	0.000	0.000	0.000	0.000
38	A	44	GLN	0	-0.007	-0.007	20.339	0.666	0.666	0.000	0.000	0.000	0.000
39	A	45	ASN	0	-0.062	-0.041	24.046	0.008	0.008	0.000	0.000	0.000	0.000
40	A	46	LEU	0	0.022	0.017	21.265	0.141	0.141	0.000	0.000	0.000	0.000
41	A	47	ASP	-1	-0.924	-0.960	24.612	-10.982	-10.982	0.000	0.000	0.000	0.000
42	A	48	GLN	0	-0.004	0.002	21.009	-0.894	-0.894	0.000	0.000	0.000	0.000
43	A	49	LEU	0	-0.045	-0.016	22.246	0.602	0.602	0.000	0.000	0.000	0.000
44	A	50	TYR	0	0.044	0.004	18.252	-0.983	-0.983	0.000	0.000	0.000	0.000
45	A	51	ILE	0	-0.022	-0.007	22.053	0.692	0.692	0.000	0.000	0.000	0.000
46	A	52	PRO	0	0.054	0.048	22.214	-0.639	-0.639	0.000	0.000	0.000	0.000
47	A	53	VAL	0	-0.051	-0.030	21.035	0.463	0.463	0.000	0.000	0.000	0.000
48	A	54	SER	0	-0.097	-0.063	23.404	0.397	0.397	0.000	0.000	0.000	0.000
49	A	55	GLU	-1	-0.879	-0.938	24.076	-11.225	-11.225	0.000	0.000	0.000	0.000
50	A	56	GLN	0	-0.060	-0.024	21.126	-0.314	-0.314	0.000	0.000	0.000	0.000
51	A	57	HIS	0	-0.001	0.015	17.199	-0.542	-0.542	0.000	0.000	0.000	0.000
52	A	58	TRP	0	0.038	0.008	18.745	0.923	0.923	0.000	0.000	0.000	0.000
53	A	59	ILE	0	-0.032	-0.010	17.518	-1.082	-1.082	0.000	0.000	0.000	0.000
54	A	60	GLY	0	0.044	0.012	17.125	0.904	0.904	0.000	0.000	0.000	0.000
55	A	61	PHE	0	-0.036	-0.042	17.504	-0.504	-0.504	0.000	0.000	0.000	0.000
56	A	62	LEU	0	0.027	0.024	18.000	0.494	0.494	0.000	0.000	0.000	0.000
57	A	63	SER	0	-0.032	-0.023	20.351	-0.033	-0.033	0.000	0.000	0.000	0.000
58	A	64	LEU	0	0.034	0.023	19.761	0.257	0.257	0.000	0.000	0.000	0.000
59	A	65	LYS	1	0.958	0.960	24.034	10.255	10.255	0.000	0.000	0.000	0.000
60	A	66	SER	0	0.011	-0.006	26.939	0.372	0.372	0.000	0.000	0.000	0.000
61	A	67	VAL	0	-0.052	-0.002	21.937	0.045	0.045	0.000	0.000	0.000	0.000
62	A	68	GLU	-1	-0.762	-0.888	24.793	-10.702	-10.702	0.000	0.000	0.000	0.000
63	A	69	ARG	1	0.870	0.922	23.184	11.805	11.805	0.000	0.000	0.000	0.000
64	A	70	SER	0	-0.011	0.002	21.953	-0.393	-0.393	0.000	0.000	0.000	0.000
65	A	71	ASP	-1	-0.861	-0.929	21.021	-13.381	-13.381	0.000	0.000	0.000	0.000
66	A	72	ALA	0	-0.018	0.009	17.989	-0.813	-0.813	0.000	0.000	0.000	0.000
67	A	73	GLY	0	0.025	0.011	15.039	0.500	0.500	0.000	0.000	0.000	0.000
68	A	74	ARG	1	0.837	0.915	8.733	26.715	26.715	0.000	0.000	0.000	0.000
69	A	75	TYR	0	0.015	-0.020	11.677	0.709	0.709	0.000	0.000	0.000	0.000
70	A	76	TRP	0	-0.068	-0.040	9.232	-3.163	-3.163	0.000	0.000	0.000	0.000
71	A	78	GLN	0	0.006	0.008	11.584	-2.968	-2.968	0.000	0.000	0.000	0.000
72	A	79	VAL	0	0.057	0.027	13.938	0.924	0.924	0.000	0.000	0.000	0.000
73	A	80	GLU	-1	-0.960	-0.973	16.363	-14.650	-14.650	0.000	0.000	0.000	0.000
74	A	81	ASP	-1	-0.954	-0.984	19.089	-14.554	-14.554	0.000	0.000	0.000	0.000
75	A	82	GLY	0	0.015	0.018	16.354	-1.044	-1.044	0.000	0.000	0.000	0.000
76	A	83	GLY	0	-0.007	0.001	17.079	0.235	0.235	0.000	0.000	0.000	0.000
77	A	84	GLU	-1	-0.999	-1.004	14.869	-21.222	-21.222	0.000	0.000	0.000	0.000
78	A	85	THR	0	-0.038	-0.025	14.228	0.151	0.151	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.958	-0.963	11.416	-25.122	-25.122	0.000	0.000	0.000	0.000
80	A	87	ILE	0	-0.004	-0.016	9.761	1.400	1.400	0.000	0.000	0.000	0.000
81	A	88	SER	0	-0.050	-0.005	8.393	-2.656	-2.656	0.000	0.000	0.000	0.000
84	A	91	VAL	0	0.028	0.014	7.725	-1.765	-1.765	0.000	0.000	0.000	0.000
85	A	92	TRP	0	-0.045	-0.037	6.897	1.584	1.584	0.000	0.000	0.000	0.000
86	A	93	LEU	0	0.016	0.024	11.665	0.493	0.493	0.000	0.000	0.000	0.000
87	A	94	THR	0	-0.017	-0.016	15.167	0.152	0.152	0.000	0.000	0.000	0.000
88	A	95	VAL	0	0.022	0.005	17.433	0.324	0.324	0.000	0.000	0.000	0.000
89	A	96	GLU	-1	-0.883	-0.944	21.210	-13.378	-13.378	0.000	0.000	0.000	0.000
90	A	97	GLY	0	0.017	-0.007	23.566	0.326	0.326	0.000	0.000	0.000	0.000
91	A	98	VAL	0	0.004	0.022	27.249	-0.151	-0.151	0.000	0.000	0.000	0.000
92	A	99	PRO	0	-0.052	-0.021	28.621	-0.259	-0.259	0.000	0.000	0.000	0.000
93	A	100	PHE	0	0.018	0.004	27.303	0.268	0.268	0.000	0.000	0.000	0.000
94	A	101	PHE	0	0.024	-0.014	29.047	-0.191	-0.191	0.000	0.000	0.000	0.000
95	A	102	THR	0	-0.007	0.004	26.537	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	103	VAL	0	-0.052	-0.019	29.688	0.151	0.151	0.000	0.000	0.000	0.000
97	A	104	GLU	-1	-0.736	-0.876	33.176	-8.538	-8.538	0.000	0.000	0.000	0.000
98	A	105	PRO	0	-0.026	0.007	36.333	0.081	0.081	0.000	0.000	0.000	0.000
99	A	106	LYS	1	0.906	0.944	36.742	8.405	8.405	0.000	0.000	0.000	0.000
100	A	107	ASP	-1	-0.739	-0.835	42.143	-6.984	-6.984	0.000	0.000	0.000	0.000
101	A	108	LEU	0	-0.063	-0.028	45.042	-0.030	-0.030	0.000	0.000	0.000	0.000
102	A	109	ALA	0	0.034	0.027	48.310	0.083	0.083	0.000	0.000	0.000	0.000
103	A	110	VAL	0	-0.025	-0.013	50.898	-0.028	-0.028	0.000	0.000	0.000	0.000
104	A	111	PRO	0	0.043	0.018	53.559	0.082	0.082	0.000	0.000	0.000	0.000
105	A	112	PRO	0	0.020	0.011	56.351	-0.074	-0.074	0.000	0.000	0.000	0.000
106	A	113	ASN	0	-0.098	-0.067	57.338	0.020	0.020	0.000	0.000	0.000	0.000
107	A	114	ALA	0	0.022	0.033	54.520	0.011	0.011	0.000	0.000	0.000	0.000
108	A	115	PRO	0	-0.006	-0.004	51.286	-0.068	-0.068	0.000	0.000	0.000	0.000
109	A	116	PHE	0	-0.023	-0.017	47.041	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	117	GLN	0	-0.033	-0.028	41.261	-0.147	-0.147	0.000	0.000	0.000	0.000
111	A	118	LEU	0	-0.028	0.006	42.386	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	119	SER	0	0.001	-0.016	37.311	-0.024	-0.024	0.000	0.000	0.000	0.000
113	A	120	CYS	0	-0.073	-0.020	35.846	0.147	0.147	0.000	0.000	0.000	0.000
114	A	121	GLU	-1	-0.880	-0.946	29.810	-10.387	-10.387	0.000	0.000	0.000	0.000
115	A	122	ALA	0	-0.012	0.002	30.061	0.048	0.048	0.000	0.000	0.000	0.000
116	A	123	VAL	0	0.017	0.013	24.734	-0.119	-0.119	0.000	0.000	0.000	0.000
117	A	124	GLY	0	0.049	0.046	24.968	0.273	0.273	0.000	0.000	0.000	0.000
118	A	125	PRO	0	-0.038	-0.005	19.919	-0.107	-0.107	0.000	0.000	0.000	0.000
119	A	126	PRO	0	0.051	0.009	22.910	0.234	0.234	0.000	0.000	0.000	0.000
120	A	127	GLU	-1	-0.805	-0.901	22.878	-11.925	-11.925	0.000	0.000	0.000	0.000
121	A	128	PRO	0	-0.056	-0.032	25.079	-0.178	-0.178	0.000	0.000	0.000	0.000
122	A	129	VAL	0	-0.006	0.006	27.351	0.312	0.312	0.000	0.000	0.000	0.000
123	A	130	THR	0	-0.086	-0.034	29.634	0.193	0.193	0.000	0.000	0.000	0.000
124	A	131	ILE	0	0.000	-0.018	32.826	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	132	VAL	0	-0.016	-0.007	35.996	0.149	0.149	0.000	0.000	0.000	0.000
126	A	133	TRP	0	0.001	-0.005	39.181	0.038	0.038	0.000	0.000	0.000	0.000
127	A	134	TRP	0	-0.018	-0.029	42.152	0.280	0.280	0.000	0.000	0.000	0.000
128	A	135	ARG	1	0.929	0.969	45.322	6.127	6.127	0.000	0.000	0.000	0.000
129	A	136	GLY	0	-0.004	-0.003	48.510	0.140	0.140	0.000	0.000	0.000	0.000
130	A	137	THR	0	0.008	-0.003	48.397	-0.116	-0.116	0.000	0.000	0.000	0.000
131	A	138	THR	0	-0.020	0.001	49.815	0.027	0.027	0.000	0.000	0.000	0.000
132	A	139	LYS	1	0.942	0.985	43.220	7.214	7.214	0.000	0.000	0.000	0.000
133	A	140	ILE	0	-0.052	-0.029	45.898	0.137	0.137	0.000	0.000	0.000	0.000
134	A	141	GLY	0	0.022	0.016	43.120	0.030	0.030	0.000	0.000	0.000	0.000
135	A	142	GLY	0	0.022	0.020	40.177	-0.099	-0.099	0.000	0.000	0.000	0.000
136	A	143	PRO	0	-0.023	-0.034	37.607	0.208	0.208	0.000	0.000	0.000	0.000
137	A	144	ALA	0	-0.026	0.003	37.019	0.083	0.083	0.000	0.000	0.000	0.000
138	A	145	PRO	0	0.023	0.007	31.878	-0.096	-0.096	0.000	0.000	0.000	0.000
139	A	146	SER	0	0.027	0.027	29.776	0.397	0.397	0.000	0.000	0.000	0.000
140	A	147	PRO	0	0.017	0.008	30.089	-0.264	-0.264	0.000	0.000	0.000	0.000
141	A	148	SER	0	0.016	0.002	32.485	0.276	0.276	0.000	0.000	0.000	0.000
142	A	149	VAL	0	-0.005	-0.020	36.211	0.030	0.030	0.000	0.000	0.000	0.000
143	A	150	LEU	0	-0.012	0.009	39.597	0.086	0.086	0.000	0.000	0.000	0.000
144	A	151	ASN	0	0.017	0.013	43.233	0.009	0.009	0.000	0.000	0.000	0.000
145	A	152	VAL	0	-0.031	-0.014	46.041	0.068	0.068	0.000	0.000	0.000	0.000
146	A	153	THR	0	0.016	-0.003	49.334	0.006	0.006	0.000	0.000	0.000	0.000
147	A	154	GLY	0	0.082	0.046	52.890	0.078	0.078	0.000	0.000	0.000	0.000
148	A	155	VAL	0	-0.049	-0.025	52.451	-0.040	-0.040	0.000	0.000	0.000	0.000
149	A	156	THR	0	0.044	0.018	55.357	0.016	0.016	0.000	0.000	0.000	0.000
150	A	157	GLN	0	0.002	0.010	56.899	0.161	0.161	0.000	0.000	0.000	0.000
151	A	158	SER	0	0.035	0.007	54.307	-0.092	-0.092	0.000	0.000	0.000	0.000
152	A	159	THR	0	-0.073	-0.031	50.817	0.080	0.080	0.000	0.000	0.000	0.000
153	A	160	MET	0	0.008	0.012	48.164	-0.077	-0.077	0.000	0.000	0.000	0.000
154	A	161	PHE	0	0.019	-0.014	44.963	0.087	0.087	0.000	0.000	0.000	0.000
155	A	162	SER	0	-0.004	0.011	41.713	-0.086	-0.086	0.000	0.000	0.000	0.000
156	A	164	GLU	-1	-0.862	-0.918	37.911	-7.872	-7.872	0.000	0.000	0.000	0.000
157	A	165	ALA	0	0.009	0.004	32.720	-0.017	-0.017	0.000	0.000	0.000	0.000
158	A	166	HIS	0	-0.068	-0.043	33.675	0.095	0.095	0.000	0.000	0.000	0.000
159	A	167	ASN	0	0.050	-0.003	27.074	0.119	0.119	0.000	0.000	0.000	0.000
160	A	168	LEU	0	0.004	-0.003	26.821	0.228	0.228	0.000	0.000	0.000	0.000
161	A	169	LYS	1	0.849	0.930	25.339	12.278	12.278	0.000	0.000	0.000	0.000
162	A	170	GLY	0	0.003	0.013	29.973	0.216	0.216	0.000	0.000	0.000	0.000
163	A	171	LEU	0	-0.016	-0.006	33.395	-0.102	-0.102	0.000	0.000	0.000	0.000
164	A	172	ALA	0	0.049	0.023	33.179	-0.031	-0.031	0.000	0.000	0.000	0.000
165	A	173	SER	0	-0.004	0.003	35.185	0.040	0.040	0.000	0.000	0.000	0.000
166	A	174	SER	0	-0.017	-0.009	36.484	-0.148	-0.148	0.000	0.000	0.000	0.000
167	A	175	ARG	1	0.778	0.851	37.488	7.737	7.737	0.000	0.000	0.000	0.000
168	A	176	THR	0	-0.040	-0.021	39.869	0.048	0.048	0.000	0.000	0.000	0.000
169	A	177	ALA	0	-0.022	0.001	42.744	0.011	0.011	0.000	0.000	0.000	0.000
170	A	178	THR	0	-0.029	-0.037	44.492	0.168	0.168	0.000	0.000	0.000	0.000
171	A	179	VAL	0	0.001	0.009	48.032	-0.048	-0.048	0.000	0.000	0.000	0.000
172	A	180	HIS	0	0.000	-0.017	50.089	0.109	0.109	0.000	0.000	0.000	0.000
173	A	181	LEU	0	-0.016	-0.010	53.466	-0.040	-0.040	0.000	0.000	0.000	0.000
174	A	182	GLN	-1	-0.939	-0.958	54.607	-5.392	-5.392	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)