FMO DATABASE

FMODB ID: J2K39

Calculation Name: 3E7K-A-Xray540

Preferred Name: Transient receptor potential cation channel subfamily M member 7

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3E7K

Chain ID: A

ChEMBL ID: CHEMBL3721309

UniProt ID: Q925B3

Base Structure: X-ray

Registration Date: 2025-07-08

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-210203.431145
FMO2-HF: Nuclear repulsion	189009.232539
FMO2-HF: Total energy	-21194.198606
FMO2-MP2: Total energy	-21256.214746

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-13.564	-9.726	4.278	-3.394	-4.724	0.021

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.153 / q_NPA : 0.032

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].
4	A	4	SER	0	0.069	0.034	2.540	-0.608	1.158	0.338	-0.891	-1.212	0.003
5	A	4	SER	0	0.021	0.092	3.124	1.732	2.384	0.200	-0.406	-0.447	-0.002
6	A	5	ARG	0	0.128	-0.074	2.372	-8.291	-8.558	2.602	-0.609	-1.726	0.013
7	A	5	ARG	1	0.793	1.022	2.648	-3.289	-2.168	1.114	-1.161	-1.074	0.005
8	A	6	VAL	0	0.054	-0.065	3.806	-2.416	-1.893	0.025	-0.311	-0.238	0.002
9	A	6	VAL	0	-0.090	0.067	4.643	-0.280	-0.237	-0.001	-0.016	-0.027	0.000
10	A	7	THR	0	-0.026	-0.089	5.739	-0.653	-0.653	0.000	0.000	0.000	0.000
11	A	7	THR	0	-0.031	0.044	6.970	-0.241	-0.241	0.000	0.000	0.000	0.000
12	A	8	PHE	0	0.124	-0.069	7.088	-0.712	-0.712	0.000	0.000	0.000	0.000
13	A	8	PHE	0	-0.083	0.089	7.631	0.153	0.153	0.000	0.000	0.000	0.000
14	A	9	GLU	0	0.103	-0.090	8.204	-0.396	-0.396	0.000	0.000	0.000	0.000
15	A	9	GLU	-1	-0.922	-0.816	7.395	2.104	2.104	0.000	0.000	0.000	0.000
16	A	10	ARG	0	0.091	-0.087	9.838	-0.238	-0.238	0.000	0.000	0.000	0.000
17	A	10	ARG	1	0.843	1.055	9.373	-0.139	-0.139	0.000	0.000	0.000	0.000
18	A	11	VAL	0	0.101	-0.079	11.763	-0.227	-0.227	0.000	0.000	0.000	0.000
19	A	11	VAL	0	-0.065	0.103	12.258	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	12	GLU	0	0.068	-0.105	12.988	-0.170	-0.170	0.000	0.000	0.000	0.000
21	A	12	GLU	-1	-0.970	-0.865	13.460	0.888	0.888	0.000	0.000	0.000	0.000
22	A	13	GLN	0	0.158	-0.094	14.116	-0.118	-0.118	0.000	0.000	0.000	0.000
23	A	13	GLN	0	-0.166	0.106	13.706	0.061	0.061	0.000	0.000	0.000	0.000
24	A	14	MET	0	0.014	-0.148	15.774	-0.090	-0.090	0.000	0.000	0.000	0.000
25	A	14	MET	0	-0.099	0.083	15.904	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	15	SER	0	0.104	-0.043	17.533	-0.084	-0.084	0.000	0.000	0.000	0.000
27	A	15	SER	0	-0.041	0.099	18.199	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	16	ILE	0	0.045	-0.131	18.814	-0.055	-0.055	0.000	0.000	0.000	0.000
29	A	16	ILE	0	-0.093	0.124	17.904	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	17	GLN	0	0.124	-0.103	20.152	-0.040	-0.040	0.000	0.000	0.000	0.000
31	A	17	GLN	0	-0.114	0.087	18.811	0.025	0.025	0.000	0.000	0.000	0.000
32	A	18	ILE	0	0.061	-0.116	21.752	-0.045	-0.045	0.000	0.000	0.000	0.000
33	A	18	ILE	0	-0.087	0.108	20.780	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	19	LYS	0	0.105	-0.087	23.464	-0.033	-0.033	0.000	0.000	0.000	0.000
35	A	19	LYS	1	0.844	1.063	24.299	-0.277	-0.277	0.000	0.000	0.000	0.000
36	A	20	GLU	0	0.074	-0.062	24.780	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	20	GLU	-1	-0.907	-0.856	25.211	0.197	0.197	0.000	0.000	0.000	0.000
38	A	21	VAL	0	-0.013	-0.120	26.065	-0.022	-0.022	0.000	0.000	0.000	0.000
39	A	21	VAL	0	-0.065	0.099	25.879	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	22	GLY	0	0.035	-0.096	27.849	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	23	ASP	0	0.091	-0.047	29.418	-0.019	-0.019	0.000	0.000	0.000	0.000
42	A	23	ASP	-1	-0.969	-0.807	29.154	0.226	0.226	0.000	0.000	0.000	0.000
43	A	24	ARG	0	0.061	-0.095	30.709	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	24	ARG	1	0.823	1.034	28.948	-0.151	-0.151	0.000	0.000	0.000	0.000
45	A	25	VAL	0	0.148	-0.104	32.219	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	25	VAL	0	-0.107	0.136	31.977	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	26	ASN	0	0.062	-0.105	33.829	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	26	ASN	0	-0.092	0.066	33.450	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	27	TYR	0	0.055	-0.108	35.293	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	27	TYR	0	-0.086	0.119	35.690	0.001	0.001	0.000	0.000	0.000	0.000
51	A	28	ILE	0	0.095	-0.106	36.745	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	28	ILE	0	-0.067	0.115	35.175	0.000	0.000	0.000	0.000	0.000	0.000
53	A	29	LYS	0	0.139	-0.047	38.291	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	29	LYS	1	0.845	1.026	37.117	-0.126	-0.126	0.000	0.000	0.000	0.000
55	A	30	ARG	0	0.051	-0.107	39.912	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	30	ARG	1	0.874	1.072	36.760	-0.129	-0.129	0.000	0.000	0.000	0.000
57	A	31	SER	0	0.021	-0.071	41.324	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	31	SER	0	-0.004	0.061	40.710	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	32	LEU	0	0.109	-0.108	42.686	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	32	LEU	0	-0.109	0.128	42.883	0.001	0.001	0.000	0.000	0.000	0.000
61	A	33	GLN	0	0.149	-0.044	44.419	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	33	GLN	0	-0.118	0.080	44.892	0.002	0.002	0.000	0.000	0.000	0.000
63	A	34	SER	0	0.032	-0.129	45.951	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	34	SER	0	-0.050	0.063	45.679	0.000	0.000	0.000	0.000	0.000	0.000
65	A	35	LEU	0	0.047	-0.093	47.160	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	35	LEU	0	-0.118	0.104	47.032	0.000	0.000	0.000	0.000	0.000	0.000
67	A	36	ASP	0	0.097	-0.122	48.601	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	36	ASP	-1	-0.996	-0.839	48.701	0.064	0.064	0.000	0.000	0.000	0.000
69	A	37	SER	0	0.062	-0.055	50.446	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	37	SER	0	-0.077	0.041	51.533	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	38	GLN	0	0.056	-0.096	52.076	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	38	GLN	0	-0.107	0.080	51.817	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	39	ILE	0	0.032	-0.125	53.053	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	39	ILE	0	-0.077	0.120	51.374	0.000	0.000	0.000	0.000	0.000	0.000
75	A	40	GLY	0	0.039	-0.076	54.756	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	41	HIS	0	0.109	0.040	56.701	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	41	HIS	0	-0.112	0.061	55.899	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	42	LEU	0	0.149	-0.091	57.853	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	42	LEU	0	-0.121	0.099	57.000	0.000	0.000	0.000	0.000	0.000	0.000
80	A	43	GLN	0	0.036	-0.122	58.921	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	43	GLN	0	-0.066	0.086	56.739	0.001	0.001	0.000	0.000	0.000	0.000
82	A	44	ASP	0	0.153	-0.084	60.611	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	44	ASP	-1	-1.026	-0.837	61.266	0.046	0.046	0.000	0.000	0.000	0.000
84	A	45	LEU	0	0.120	-0.137	62.550	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	45	LEU	0	-0.134	0.130	62.824	0.000	0.000	0.000	0.000	0.000	0.000
86	A	46	SER	0	0.082	-0.077	63.289	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	46	SER	0	-0.074	0.059	63.092	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	47	ALA	0	0.094	-0.101	64.753	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	47	ALA	0	-0.069	0.123	65.328	0.000	0.000	0.000	0.000	0.000	0.000
90	A	48	LEU	0	0.124	-0.122	66.685	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	48	LEU	0	-0.152	0.138	67.543	0.000	0.000	0.000	0.000	0.000	0.000
92	A	49	THR	0	0.075	-0.114	68.196	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	49	THR	0	-0.123	0.046	67.439	0.000	0.000	0.000	0.000	0.000	0.000
94	A	50	VAL	0	0.069	-0.131	69.053	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	50	VAL	0	-0.128	0.101	68.271	0.000	0.000	0.000	0.000	0.000	0.000
96	A	51	ASP	0	0.054	-0.130	70.726	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	51	ASP	-1	-0.993	-0.827	71.437	0.029	0.029	0.000	0.000	0.000	0.000
98	A	52	THR	0	0.022	-0.065	72.776	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	52	THR	0	-0.028	0.057	73.311	0.000	0.000	0.000	0.000	0.000	0.000
100	A	53	LEU	0	0.013	-0.121	73.866	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	53	LEU	0	-0.058	0.101	72.448	0.000	0.000	0.000	0.000	0.000	0.000
102	A	54	LYS	0	0.019	-0.083	75.488	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	54	LYS	1	0.835	1.046	72.379	-0.026	-0.026	0.000	0.000	0.000	0.000
104	A	55	THR	0	-0.138	-0.166	77.148	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	55	THR	0	0.052	0.044	76.654	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)