FMO DATABASE

FMODB ID: N261Q

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	OptAll
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	-210630.037568
FMO2-HF: Nuclear repulsion	189434.729013
FMO2-HF: Total energy	-21195.308555
FMO2-MP2: Total energy	-21257.208652

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.
-12.866	-11.173	6.952	-3.23	-5.413	0.011

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 : 0.176 / q_NPA : 0.060

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	0.074	0.064	2.650	0.180	1.753	0.142	-0.742	-0.972	0.001
5	A	4	SER	0	0.000	0.077	2.344	-0.361	-0.335	2.115	-1.001	-1.141	-0.011
6	A	5	ARG	0	0.156	-0.064	2.356	-6.468	-7.881	2.697	0.366	-1.650	0.009
7	A	5	ARG	1	0.761	1.006	2.743	-3.701	-2.743	1.961	-1.561	-1.358	0.009
8	A	6	VAL	0	0.106	-0.070	4.037	-2.572	-2.067	0.038	-0.279	-0.263	0.003
9	A	6	VAL	0	-0.107	0.080	5.085	-0.266	-0.222	-0.001	-0.013	-0.029	0.000
10	A	7	THR	0	0.000	-0.107	6.084	-0.646	-0.646	0.000	0.000	0.000	0.000
11	A	7	THR	0	-0.066	0.044	6.735	-0.227	-0.227	0.000	0.000	0.000	0.000
12	A	8	PHE	0	0.111	-0.062	7.096	-0.662	-0.662	0.000	0.000	0.000	0.000
13	A	8	PHE	0	-0.087	0.087	7.399	0.107	0.107	0.000	0.000	0.000	0.000
14	A	9	GLU	0	0.123	-0.102	8.282	-0.467	-0.467	0.000	0.000	0.000	0.000
15	A	9	GLU	-1	-0.906	-0.797	7.280	3.228	3.228	0.000	0.000	0.000	0.000
16	A	10	ARG	0	0.089	-0.073	10.066	-0.253	-0.253	0.000	0.000	0.000	0.000
17	A	10	ARG	1	0.855	1.052	9.329	-0.331	-0.331	0.000	0.000	0.000	0.000
18	A	11	VAL	0	0.099	-0.076	11.644	-0.217	-0.217	0.000	0.000	0.000	0.000
19	A	11	VAL	0	-0.088	0.091	11.957	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	12	GLU	0	0.131	-0.107	12.968	-0.183	-0.183	0.000	0.000	0.000	0.000
21	A	12	GLU	-1	-0.944	-0.802	13.710	0.855	0.855	0.000	0.000	0.000	0.000
22	A	13	GLN	0	0.098	-0.086	14.246	-0.116	-0.116	0.000	0.000	0.000	0.000
23	A	13	GLN	0	-0.140	0.058	14.286	0.066	0.066	0.000	0.000	0.000	0.000
24	A	14	MET	0	0.034	-0.132	15.959	-0.092	-0.092	0.000	0.000	0.000	0.000
25	A	14	MET	0	-0.113	0.092	16.291	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	15	SER	0	0.019	-0.078	17.421	-0.093	-0.093	0.000	0.000	0.000	0.000
27	A	15	SER	0	-0.075	0.063	17.589	-0.023	-0.023	0.000	0.000	0.000	0.000
28	A	16	ILE	0	0.124	-0.099	18.945	-0.069	-0.069	0.000	0.000	0.000	0.000
29	A	16	ILE	0	-0.103	0.103	17.741	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	17	GLN	0	0.079	-0.091	20.193	-0.046	-0.046	0.000	0.000	0.000	0.000
31	A	17	GLN	0	-0.074	0.084	18.950	0.025	0.025	0.000	0.000	0.000	0.000
32	A	18	ILE	0	0.077	-0.091	21.819	-0.046	-0.046	0.000	0.000	0.000	0.000
33	A	18	ILE	0	-0.085	0.096	20.648	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	19	LYS	0	0.095	-0.091	23.504	-0.039	-0.039	0.000	0.000	0.000	0.000
35	A	19	LYS	1	0.827	1.041	24.354	-0.289	-0.289	0.000	0.000	0.000	0.000
36	A	20	GLU	0	0.112	-0.084	24.916	-0.027	-0.027	0.000	0.000	0.000	0.000
37	A	20	GLU	-1	-0.919	-0.792	25.094	0.242	0.242	0.000	0.000	0.000	0.000
38	A	21	VAL	0	0.015	-0.150	26.228	-0.023	-0.023	0.000	0.000	0.000	0.000
39	A	21	VAL	0	-0.084	0.121	26.000	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	22	GLY	0	0.036	-0.094	27.809	-0.022	-0.022	0.000	0.000	0.000	0.000
41	A	23	ASP	0	0.046	-0.025	29.481	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	23	ASP	-1	-0.903	-0.790	29.772	0.235	0.235	0.000	0.000	0.000	0.000
43	A	24	ARG	0	0.109	-0.087	30.795	-0.013	-0.013	0.000	0.000	0.000	0.000
44	A	24	ARG	1	0.765	0.996	28.891	-0.196	-0.196	0.000	0.000	0.000	0.000
45	A	25	VAL	0	0.089	-0.100	32.286	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	25	VAL	0	-0.084	0.113	32.277	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	26	ASN	0	0.065	-0.095	33.749	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	26	ASN	0	-0.105	0.072	32.810	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	27	TYR	0	0.090	-0.099	35.294	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	27	TYR	0	-0.072	0.102	35.758	0.001	0.001	0.000	0.000	0.000	0.000
51	A	28	ILE	0	0.121	-0.075	36.720	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	28	ILE	0	-0.086	0.102	35.321	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	29	LYS	0	0.113	-0.066	38.209	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	29	LYS	1	0.806	1.009	36.013	-0.139	-0.139	0.000	0.000	0.000	0.000
55	A	30	ARG	0	0.057	-0.076	39.801	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	30	ARG	1	0.872	1.051	35.729	-0.148	-0.148	0.000	0.000	0.000	0.000
57	A	31	SER	0	0.064	-0.059	41.217	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	31	SER	0	-0.059	0.051	40.550	0.000	0.000	0.000	0.000	0.000	0.000
59	A	32	LEU	0	0.111	-0.090	42.606	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	32	LEU	0	-0.115	0.107	42.955	0.001	0.001	0.000	0.000	0.000	0.000
61	A	33	GLN	0	0.131	-0.093	44.236	-0.006	-0.006	0.000	0.000	0.000	0.000
62	A	33	GLN	0	-0.152	0.067	44.879	0.003	0.003	0.000	0.000	0.000	0.000
63	A	34	SER	0	0.024	-0.090	45.871	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	34	SER	0	-0.088	0.048	45.449	0.001	0.001	0.000	0.000	0.000	0.000
65	A	35	LEU	0	0.108	-0.066	47.212	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	35	LEU	0	-0.106	0.085	47.398	0.000	0.000	0.000	0.000	0.000	0.000
67	A	36	ASP	0	0.064	-0.108	48.571	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	36	ASP	-1	-0.969	-0.846	48.785	0.070	0.070	0.000	0.000	0.000	0.000
69	A	37	SER	0	0.068	-0.058	50.399	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	37	SER	0	-0.023	0.071	51.424	0.001	0.001	0.000	0.000	0.000	0.000
71	A	38	GLN	0	0.058	-0.091	52.041	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	38	GLN	0	-0.100	0.069	51.219	0.000	0.000	0.000	0.000	0.000	0.000
73	A	39	ILE	0	0.073	-0.103	53.037	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	39	ILE	0	-0.116	0.099	51.026	0.000	0.000	0.000	0.000	0.000	0.000
75	A	40	GLY	0	0.019	-0.097	54.624	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	41	HIS	0	0.109	0.030	56.582	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	41	HIS	0	-0.103	0.070	55.652	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	42	LEU	0	0.125	-0.072	57.773	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	42	LEU	0	-0.106	0.085	57.145	0.000	0.000	0.000	0.000	0.000	0.000
80	A	43	GLN	0	0.049	-0.111	58.874	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	43	GLN	0	-0.099	0.084	56.133	0.000	0.000	0.000	0.000	0.000	0.000
82	A	44	ASP	0	0.119	-0.098	60.545	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	44	ASP	-1	-1.002	-0.839	61.061	0.049	0.049	0.000	0.000	0.000	0.000
84	A	45	LEU	0	0.125	-0.097	62.500	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	45	LEU	0	-0.111	0.102	62.667	0.000	0.000	0.000	0.000	0.000	0.000
86	A	46	SER	0	0.055	-0.062	63.252	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	46	SER	0	-0.073	0.052	62.894	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	47	ALA	0	0.093	-0.096	64.632	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	47	ALA	0	-0.062	0.110	64.937	0.000	0.000	0.000	0.000	0.000	0.000
90	A	48	LEU	0	0.085	-0.103	66.507	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	48	LEU	0	-0.070	0.119	67.681	0.000	0.000	0.000	0.000	0.000	0.000
92	A	49	THR	0	0.032	-0.072	68.005	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	49	THR	0	-0.072	0.042	67.410	0.000	0.000	0.000	0.000	0.000	0.000
94	A	50	VAL	0	0.093	-0.102	68.819	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	50	VAL	0	-0.124	0.091	67.748	0.000	0.000	0.000	0.000	0.000	0.000
96	A	51	ASP	0	0.040	-0.123	70.444	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	51	ASP	-1	-0.884	-0.786	71.130	0.032	0.032	0.000	0.000	0.000	0.000
98	A	52	THR	0	0.058	-0.082	72.526	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	52	THR	0	-0.068	0.054	72.406	0.000	0.000	0.000	0.000	0.000	0.000
100	A	53	LEU	0	0.019	-0.070	73.683	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	53	LEU	0	-0.067	0.089	71.792	0.000	0.000	0.000	0.000	0.000	0.000
102	A	54	LYS	0	0.000	-0.123	75.382	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	54	LYS	1	0.769	0.989	71.630	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	55	THR	0	-0.146	-0.171	77.443	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	55	THR	0	0.007	0.022	76.976	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)