FMO DATABASE

FMODB ID: QNGLY

Calculation Name: 3Q6C-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3Q6C

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-07-09

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-402933.280549
FMO2-HF: Nuclear repulsion	375960.570582
FMO2-HF: Total energy	-26972.709967
FMO2-MP2: Total energy	-27051.48633

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:38:LEU)

Summations of interaction energy for fragment #1(A:38:LEU)

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.
-16.212	-10.643	4.519	-4.892	-5.193	0.011

Interaction energy analysis for fragmet #1(A:38:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.083 / q_NPA : 0.012

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	39	LEU	0	-0.059	0.113	1.878	-0.163	-0.485	3.291	-1.236	-1.733	0.007
5	A	40	GLN	0	0.137	-0.091	3.833	-0.948	1.192	-0.022	-1.279	-0.838	0.003
6	A	40	GLN	0	-0.027	0.114	6.406	0.318	0.318	0.000	0.000	0.000	0.000
7	A	41	LYS	0	0.085	-0.080	7.025	-0.060	-0.060	0.000	0.000	0.000	0.000
8	A	41	LYS	1	0.858	1.068	9.167	0.293	0.293	0.000	0.000	0.000	0.000
9	A	42	ARG	0	0.124	-0.077	10.277	0.061	0.061	0.000	0.000	0.000	0.000
10	A	42	ARG	1	0.748	0.998	13.998	0.369	0.369	0.000	0.000	0.000	0.000
11	A	43	VAL	0	-0.021	-0.129	13.719	0.019	0.019	0.000	0.000	0.000	0.000
12	A	43	VAL	0	-0.065	0.086	12.468	0.014	0.014	0.000	0.000	0.000	0.000
13	A	44	ILE	0	0.170	-0.062	15.181	-0.037	-0.037	0.000	0.000	0.000	0.000
14	A	44	ILE	0	-0.121	0.086	18.951	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	45	VAL	0	0.061	-0.140	17.337	0.034	0.034	0.000	0.000	0.000	0.000
16	A	45	VAL	0	-0.142	0.120	16.737	0.004	0.004	0.000	0.000	0.000	0.000
17	A	46	SER	0	0.003	-0.087	18.290	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	46	SER	0	-0.068	0.038	18.880	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	47	ASN	0	0.115	-0.045	19.858	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	47	ASN	0	-0.044	0.077	21.198	0.010	0.010	0.000	0.000	0.000	0.000
21	A	48	LYS	0	0.098	-0.104	19.981	0.028	0.028	0.000	0.000	0.000	0.000
22	A	48	LYS	1	0.817	1.067	19.983	-0.107	-0.107	0.000	0.000	0.000	0.000
23	A	49	ARG	0	0.106	-0.080	21.715	-0.024	-0.024	0.000	0.000	0.000	0.000
24	A	49	ARG	1	0.786	1.040	22.504	-0.252	-0.252	0.000	0.000	0.000	0.000
25	A	50	GLU	0	0.095	-0.142	22.725	0.031	0.031	0.000	0.000	0.000	0.000
26	A	50	GLU	-1	-0.990	-0.800	25.027	0.139	0.139	0.000	0.000	0.000	0.000
27	A	51	LYS	0	0.106	-0.092	25.154	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	51	LYS	1	0.728	1.001	23.546	-0.275	-0.275	0.000	0.000	0.000	0.000
29	A	52	VAL	0	0.114	-0.123	26.445	0.017	0.017	0.000	0.000	0.000	0.000
30	A	52	VAL	0	-0.051	0.158	30.414	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	53	ILE	0	-0.024	-0.116	27.668	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	53	ILE	0	-0.133	0.033	24.883	0.009	0.009	0.000	0.000	0.000	0.000
33	A	54	ASN	0	0.050	-0.050	28.962	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	54	ASN	0	0.022	0.002	31.124	0.009	0.009	0.000	0.000	0.000	0.000
35	A	69	GLU	0	0.172	-0.009	27.246	0.010	0.010	0.000	0.000	0.000	0.000
36	A	69	GLU	-1	-1.048	-0.838	29.520	0.172	0.172	0.000	0.000	0.000	0.000
37	A	70	MET	0	0.108	-0.110	26.345	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	70	MET	0	-0.074	0.138	26.035	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	71	ARG	0	0.086	-0.123	22.542	0.022	0.022	0.000	0.000	0.000	0.000
40	A	71	ARG	1	0.810	1.045	19.308	-0.425	-0.425	0.000	0.000	0.000	0.000
41	A	72	TYR	0	0.003	-0.112	20.665	-0.024	-0.024	0.000	0.000	0.000	0.000
42	A	72	TYR	0	-0.034	0.119	19.792	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	73	GLU	0	0.062	-0.122	17.920	0.059	0.059	0.000	0.000	0.000	0.000
44	A	73	GLU	-1	-0.924	-0.824	18.481	0.349	0.349	0.000	0.000	0.000	0.000
45	A	74	ALA	0	0.102	-0.107	16.780	-0.052	-0.052	0.000	0.000	0.000	0.000
46	A	74	ALA	0	-0.030	0.129	15.792	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	75	SER	0	-0.050	-0.120	15.905	0.074	0.074	0.000	0.000	0.000	0.000
48	A	75	SER	0	-0.042	0.077	18.286	0.015	0.015	0.000	0.000	0.000	0.000
49	A	76	PHE	0	0.129	-0.086	13.973	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	76	PHE	0	-0.090	0.101	13.332	0.003	0.003	0.000	0.000	0.000	0.000
51	A	77	ARG	0	0.097	-0.114	15.416	0.045	0.045	0.000	0.000	0.000	0.000
52	A	77	ARG	1	0.842	1.071	18.472	-0.066	-0.066	0.000	0.000	0.000	0.000
53	A	78	PRO	0	-0.008	-0.099	14.430	-0.049	-0.049	0.000	0.000	0.000	0.000
54	A	79	GLU	0	0.056	0.039	16.509	0.034	0.034	0.000	0.000	0.000	0.000
55	A	79	GLU	-1	-0.914	-0.846	17.206	-0.297	-0.297	0.000	0.000	0.000	0.000
56	A	80	ASN	0	0.069	-0.073	19.141	0.035	0.035	0.000	0.000	0.000	0.000
57	A	80	ASN	0	-0.128	0.051	18.468	0.014	0.014	0.000	0.000	0.000	0.000
58	A	81	GLY	0	0.030	-0.104	18.113	-0.014	-0.014	0.000	0.000	0.000	0.000
59	A	82	GLY	0	0.010	0.023	19.232	0.009	0.009	0.000	0.000	0.000	0.000
60	A	83	DLE	0	-0.019	-0.025	16.631	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	84	GLU	0	0.034	-0.040	16.667	-0.023	-0.023	0.000	0.000	0.000	0.000
62	A	84	GLU	-1	-0.911	-0.798	18.224	0.158	0.158	0.000	0.000	0.000	0.000
63	A	85	VAL	0	0.056	-0.122	13.057	0.009	0.009	0.000	0.000	0.000	0.000
64	A	85	VAL	0	-0.068	0.125	11.098	0.011	0.011	0.000	0.000	0.000	0.000
65	A	86	VAL	0	0.094	-0.125	14.499	-0.036	-0.036	0.000	0.000	0.000	0.000
66	A	86	VAL	0	-0.069	0.122	16.507	0.000	0.000	0.000	0.000	0.000	0.000
67	A	87	PHE	0	0.027	-0.108	12.628	0.114	0.114	0.000	0.000	0.000	0.000
68	A	87	PHE	0	-0.083	0.119	8.582	-0.039	-0.039	0.000	0.000	0.000	0.000
69	A	88	ARG	0	0.203	-0.068	13.664	-0.112	-0.112	0.000	0.000	0.000	0.000
70	A	88	ARG	1	0.820	1.046	15.150	-0.509	-0.509	0.000	0.000	0.000	0.000
71	A	89	LEU	0	-0.069	-0.142	14.090	0.113	0.113	0.000	0.000	0.000	0.000
72	A	89	LEU	0	-0.048	0.121	13.397	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	90	ASP	0	0.071	-0.086	16.095	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	90	ASP	-1	-0.871	-0.814	17.770	0.290	0.290	0.000	0.000	0.000	0.000
75	A	91	ALA	0	0.158	-0.113	18.735	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	91	ALA	0	-0.079	0.115	22.983	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	92	PRO	0	-0.052	-0.108	19.640	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	93	GLN	0	0.173	0.034	16.173	-0.046	-0.046	0.000	0.000	0.000	0.000
79	A	93	GLN	0	-0.104	0.086	14.057	-0.042	-0.042	0.000	0.000	0.000	0.000
80	A	94	TYR	0	0.086	-0.087	17.362	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	94	TYR	0	-0.120	0.074	19.205	0.004	0.004	0.000	0.000	0.000	0.000
82	A	95	HIS	0	0.005	-0.134	19.149	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	95	HIS	0	-0.083	0.084	22.880	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	96	ALA	0	0.152	-0.095	18.938	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	96	ALA	0	-0.094	0.125	18.008	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	97	LEU	0	-0.039	-0.139	18.296	-0.037	-0.037	0.000	0.000	0.000	0.000
87	A	97	LEU	0	-0.067	0.112	15.010	0.005	0.005	0.000	0.000	0.000	0.000
88	A	98	SER	0	0.036	-0.106	19.122	0.019	0.019	0.000	0.000	0.000	0.000
89	A	98	SER	0	0.010	0.136	21.813	0.003	0.003	0.000	0.000	0.000	0.000
90	A	99	VAL	0	0.126	-0.126	21.186	-0.014	-0.014	0.000	0.000	0.000	0.000
91	A	99	VAL	0	-0.101	0.113	21.833	0.003	0.003	0.000	0.000	0.000	0.000
92	A	100	GLY	0	-0.046	-0.099	21.512	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	101	ASP	0	0.140	-0.013	20.240	-0.015	-0.015	0.000	0.000	0.000	0.000
94	A	101	ASP	-1	-0.968	-0.814	19.463	-0.076	-0.076	0.000	0.000	0.000	0.000
95	A	102	ARG	0	0.018	-0.105	17.999	0.027	0.027	0.000	0.000	0.000	0.000
96	A	102	ARG	1	0.869	1.066	18.804	0.124	0.124	0.000	0.000	0.000	0.000
97	A	103	GLY	0	0.023	-0.096	15.851	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	104	MET	0	0.105	-0.001	12.051	0.045	0.045	0.000	0.000	0.000	0.000
99	A	104	MET	0	-0.115	0.123	9.961	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	105	LEU	0	0.108	-0.112	9.742	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	105	LEU	0	-0.109	0.110	8.412	0.024	0.024	0.000	0.000	0.000	0.000
102	A	106	SER	0	0.004	-0.104	5.864	-0.254	-0.254	0.000	0.000	0.000	0.000
103	A	106	SER	0	-0.028	0.082	5.448	-0.209	-0.209	0.000	0.000	0.000	0.000
104	A	107	TYR	0	0.043	-0.118	4.251	0.168	0.253	-0.001	-0.022	-0.061	0.000
105	A	107	TYR	0	-0.079	0.105	5.706	-0.328	-0.328	0.000	0.000	0.000	0.000
106	A	108	LYS	0	0.104	-0.086	2.907	-1.131	0.787	0.683	-1.476	-1.124	-0.010
107	A	108	LYS	1	0.840	1.080	2.581	-11.232	-9.576	0.552	-0.845	-1.363	0.011
108	A	109	GLY	0	0.018	-0.094	3.794	-1.761	-1.724	0.017	-0.022	-0.032	0.000
109	A	110	THR	0	0.044	0.027	6.244	-0.334	-0.334	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.030	0.063	10.777	0.088	0.088	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.133	-0.089	7.748	-0.601	-0.601	0.000	0.000	0.000	0.000
112	A	111	ALA	0	-0.103	0.092	7.026	0.049	0.049	0.000	0.000	0.000	0.000
113	A	112	PHE	0	0.120	-0.086	6.719	0.602	0.602	0.000	0.000	0.000	0.000
114	A	112	PHE	0	-0.066	0.115	10.350	-0.021	-0.021	0.000	0.000	0.000	0.000
115	A	113	VAL	0	0.001	-0.117	5.949	0.085	0.085	0.000	0.000	0.000	0.000
116	A	113	VAL	0	-0.132	0.069	4.331	0.028	0.083	-0.001	-0.012	-0.042	0.000
117	A	114	ALA	0	0.175	-0.115	7.354	-0.143	-0.143	0.000	0.000	0.000	0.000
118	A	114	ALA	0	-0.066	0.123	8.765	-0.044	-0.044	0.000	0.000	0.000	0.000
119	A	115	PHE	0	0.087	-0.118	9.435	-0.039	-0.039	0.000	0.000	0.000	0.000
120	A	115	PHE	0	-0.088	0.111	12.379	0.015	0.015	0.000	0.000	0.000	0.000
121	A	116	THR	0	-0.025	-0.062	12.113	0.066	0.066	0.000	0.000	0.000	0.000
122	A	116	THR	0	-0.047	0.058	12.512	0.008	0.008	0.000	0.000	0.000	0.000
123	A	117	PRO	0	0.025	-0.077	14.213	-0.044	-0.044	0.000	0.000	0.000	0.000
124	A	118	ASP	0	0.116	0.012	17.370	-0.037	-0.037	0.000	0.000	0.000	0.000
125	A	118	ASP	-1	-0.903	-0.821	18.076	-0.309	-0.309	0.000	0.000	0.000	0.000
126	A	119	PRO	0	-0.048	-0.109	18.987	0.037	0.037	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:38:LEU)