FMO DATABASE

FMODB ID: 6G28Z

Calculation Name: 1Q1H-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1Q1H

Chain ID: A

ChEMBL ID:

UniProt ID: Q980M5

Base Structure: X-ray

Registration Date: 2025-07-10

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	OptHSide
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	171
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-636883.616951
FMO2-HF: Nuclear repulsion	601041.535686
FMO2-HF: Total energy	-35842.081265
FMO2-MP2: Total energy	-35947.337727

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:1:MET)

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

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.
-3.913	-0.874	0.44	-1.493	-1.986	0.004

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.206 / q_NPA : 0.066

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	2	VAL	0	-0.064	0.096	3.551	-0.514	0.221	0.017	-0.362	-0.390	0.001
5	A	3	ASN	0	0.094	-0.051	3.826	-1.108	0.282	-0.011	-0.737	-0.642	0.002
6	A	3	ASN	0	-0.088	0.046	5.912	0.116	0.116	0.000	0.000	0.000	0.000
7	A	4	ALA	0	0.123	-0.097	3.581	0.663	0.751	0.012	0.088	-0.188	0.000
8	A	4	ALA	0	-0.061	0.101	2.621	-0.245	-0.036	0.416	-0.332	-0.293	0.002
9	A	5	GLU	0	0.043	-0.128	4.634	0.158	0.219	-0.001	-0.010	-0.050	0.000
10	A	5	GLU	-1	-0.876	-0.768	5.850	-1.430	-1.430	0.000	0.000	0.000	0.000
11	A	6	ASP	0	0.088	-0.150	6.966	0.286	0.286	0.000	0.000	0.000	0.000
12	A	6	ASP	-1	-0.978	-0.819	8.593	-0.854	-0.854	0.000	0.000	0.000	0.000
13	A	7	LEU	0	0.068	-0.116	7.645	0.187	0.187	0.000	0.000	0.000	0.000
14	A	7	LEU	0	-0.069	0.113	6.645	0.011	0.011	0.000	0.000	0.000	0.000
15	A	8	PHE	0	0.079	-0.095	8.686	0.190	0.190	0.000	0.000	0.000	0.000
16	A	8	PHE	0	-0.045	0.113	8.251	-0.047	-0.047	0.000	0.000	0.000	0.000
17	A	9	ILE	0	0.058	-0.118	9.888	0.115	0.115	0.000	0.000	0.000	0.000
18	A	9	ILE	0	-0.075	0.104	11.320	0.015	0.015	0.000	0.000	0.000	0.000
19	A	10	ASN	0	0.071	-0.070	11.924	0.082	0.082	0.000	0.000	0.000	0.000
20	A	10	ASN	0	-0.108	0.043	12.207	0.027	0.027	0.000	0.000	0.000	0.000
21	A	11	LEU	0	0.059	-0.103	12.521	0.066	0.066	0.000	0.000	0.000	0.000
22	A	11	LEU	0	-0.077	0.089	10.931	0.005	0.005	0.000	0.000	0.000	0.000
23	A	12	ALA	0	0.178	-0.029	14.104	0.054	0.054	0.000	0.000	0.000	0.000
24	A	12	ALA	0	-0.087	0.074	14.857	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	13	LYS	0	0.118	-0.065	16.049	0.039	0.039	0.000	0.000	0.000	0.000
26	A	13	LYS	1	0.794	0.985	16.913	0.307	0.307	0.000	0.000	0.000	0.000
27	A	14	SER	0	0.025	-0.049	17.590	0.023	0.023	0.000	0.000	0.000	0.000
28	A	14	SER	0	-0.072	0.040	17.741	0.005	0.005	0.000	0.000	0.000	0.000
29	A	15	LEU	0	-0.087	-0.127	19.118	0.027	0.027	0.000	0.000	0.000	0.000
30	A	15	LEU	0	-0.076	0.088	17.116	0.000	0.000	0.000	0.000	0.000	0.000
31	A	16	LEU	0	0.054	-0.066	20.082	0.025	0.025	0.000	0.000	0.000	0.000
32	A	16	LEU	0	-0.131	0.038	19.658	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	17	GLY	0	0.024	-0.108	21.908	0.005	0.005	0.000	0.000	0.000	0.000
34	A	18	ASP	0	0.065	-0.017	21.176	-0.021	-0.021	0.000	0.000	0.000	0.000
35	A	18	ASP	-1	-0.899	-0.805	21.289	-0.244	-0.244	0.000	0.000	0.000	0.000
36	A	19	ASP	0	0.088	-0.115	21.733	-0.020	-0.020	0.000	0.000	0.000	0.000
37	A	19	ASP	-1	-0.941	-0.855	25.175	-0.180	-0.180	0.000	0.000	0.000	0.000
38	A	20	VAL	0	0.059	-0.108	21.241	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	20	VAL	0	-0.110	0.094	19.233	0.001	0.001	0.000	0.000	0.000	0.000
40	A	21	ILE	0	0.154	-0.084	17.396	-0.022	-0.022	0.000	0.000	0.000	0.000
41	A	21	ILE	0	-0.112	0.144	16.186	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	22	ASP	0	0.086	-0.155	17.129	-0.061	-0.061	0.000	0.000	0.000	0.000
43	A	22	ASP	-1	-1.005	-0.845	21.115	-0.259	-0.259	0.000	0.000	0.000	0.000
44	A	23	VAL	0	0.047	-0.077	18.765	-0.016	-0.016	0.000	0.000	0.000	0.000
45	A	23	VAL	0	-0.124	0.066	18.946	0.006	0.006	0.000	0.000	0.000	0.000
46	A	24	LEU	0	0.122	-0.103	15.284	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	24	LEU	0	-0.113	0.098	12.892	0.008	0.008	0.000	0.000	0.000	0.000
48	A	25	ARG	0	-0.004	-0.125	14.051	-0.103	-0.103	0.000	0.000	0.000	0.000
49	A	25	ARG	1	0.703	0.935	10.804	0.759	0.759	0.000	0.000	0.000	0.000
50	A	26	ILE	0	0.204	-0.013	14.301	-0.069	-0.069	0.000	0.000	0.000	0.000
51	A	26	ILE	0	-0.076	0.088	18.367	0.008	0.008	0.000	0.000	0.000	0.000
52	A	27	LEU	0	0.078	-0.085	15.082	0.014	0.014	0.000	0.000	0.000	0.000
53	A	27	LEU	0	-0.130	0.054	14.432	0.006	0.006	0.000	0.000	0.000	0.000
54	A	28	LEU	0	0.062	-0.103	10.930	0.015	0.015	0.000	0.000	0.000	0.000
55	A	28	LEU	0	-0.095	0.075	8.608	-0.044	-0.044	0.000	0.000	0.000	0.000
56	A	29	ASP	0	0.032	-0.073	10.822	-0.144	-0.144	0.000	0.000	0.000	0.000
57	A	29	ASP	-1	-0.969	-0.849	14.074	-0.524	-0.524	0.000	0.000	0.000	0.000
58	A	30	LYS	0	0.115	-0.089	13.385	0.005	0.005	0.000	0.000	0.000	0.000
59	A	30	LYS	1	0.729	0.970	16.346	0.275	0.275	0.000	0.000	0.000	0.000
60	A	31	GLY	0	0.014	-0.076	11.917	0.035	0.035	0.000	0.000	0.000	0.000
61	A	32	THR	0	-0.064	-0.024	12.811	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	32	THR	0	-0.020	0.043	14.959	0.034	0.034	0.000	0.000	0.000	0.000
63	A	33	GLU	0	0.078	-0.087	15.619	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	33	GLU	-1	-0.930	-0.815	17.865	-0.235	-0.235	0.000	0.000	0.000	0.000
65	A	34	MET	0	0.075	-0.076	18.095	0.024	0.024	0.000	0.000	0.000	0.000
66	A	34	MET	0	-0.079	0.118	17.990	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	35	THR	0	0.009	-0.102	20.333	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	35	THR	0	-0.010	0.106	24.318	0.002	0.002	0.000	0.000	0.000	0.000
69	A	36	ASP	0	0.156	-0.039	23.588	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	36	ASP	-1	-0.881	-0.824	25.670	-0.163	-0.163	0.000	0.000	0.000	0.000
71	A	37	GLU	0	0.065	-0.112	25.174	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	37	GLU	-1	-1.001	-0.886	27.522	-0.134	-0.134	0.000	0.000	0.000	0.000
73	A	38	GLU	0	0.092	-0.069	23.661	0.009	0.009	0.000	0.000	0.000	0.000
74	A	38	GLU	-1	-0.894	-0.821	22.444	-0.230	-0.230	0.000	0.000	0.000	0.000
75	A	39	ILE	0	0.100	-0.074	21.923	0.005	0.005	0.000	0.000	0.000	0.000
76	A	39	ILE	0	-0.083	0.091	19.783	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	40	ALA	0	0.100	-0.086	22.629	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	40	ALA	0	-0.092	0.072	26.763	0.003	0.003	0.000	0.000	0.000	0.000
79	A	41	ASN	0	0.038	-0.059	26.159	0.009	0.009	0.000	0.000	0.000	0.000
80	A	41	ASN	0	-0.159	0.021	27.081	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	42	GLN	0	-0.037	-0.117	24.033	0.016	0.016	0.000	0.000	0.000	0.000
82	A	42	GLN	0	-0.087	0.063	22.329	-0.016	-0.016	0.000	0.000	0.000	0.000
83	A	43	LEU	0	0.126	-0.091	23.537	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	43	LEU	0	-0.093	0.112	21.460	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	44	ASN	0	0.067	-0.069	24.867	0.005	0.005	0.000	0.000	0.000	0.000
86	A	44	ASN	0	-0.128	0.053	28.349	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	45	ILE	0	0.075	-0.124	28.015	0.003	0.003	0.000	0.000	0.000	0.000
88	A	45	ILE	0	0.008	0.133	24.586	0.001	0.001	0.000	0.000	0.000	0.000
89	A	46	LYS	0	0.080	-0.064	29.209	0.000	0.000	0.000	0.000	0.000	0.000
90	A	46	LYS	1	0.828	1.030	31.792	0.110	0.110	0.000	0.000	0.000	0.000
91	A	47	VAL	0	0.189	-0.096	28.466	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	47	VAL	0	-0.030	0.144	28.191	0.002	0.002	0.000	0.000	0.000	0.000
93	A	48	ASN	0	0.067	-0.038	28.758	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	48	ASN	0	-0.135	0.032	32.388	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	49	ASP	0	0.108	-0.102	29.107	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	49	ASP	-1	-0.931	-0.828	28.049	-0.170	-0.170	0.000	0.000	0.000	0.000
97	A	50	VAL	0	0.121	-0.100	25.325	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	50	VAL	0	-0.090	0.140	23.811	0.000	0.000	0.000	0.000	0.000	0.000
99	A	51	ARG	0	0.117	-0.084	24.545	-0.022	-0.022	0.000	0.000	0.000	0.000
100	A	51	ARG	1	0.749	0.973	26.906	0.149	0.149	0.000	0.000	0.000	0.000
101	A	52	LYS	0	0.019	-0.091	26.082	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	52	LYS	1	0.865	1.039	28.138	0.134	0.134	0.000	0.000	0.000	0.000
103	A	53	LYS	0	0.118	-0.050	23.401	0.006	0.006	0.000	0.000	0.000	0.000
104	A	53	LYS	1	0.780	1.045	22.359	0.201	0.201	0.000	0.000	0.000	0.000
105	A	54	LEU	0	0.071	-0.093	21.093	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	54	LEU	0	-0.100	0.083	19.936	0.001	0.001	0.000	0.000	0.000	0.000
107	A	55	ASN	0	0.135	-0.056	21.656	-0.019	-0.019	0.000	0.000	0.000	0.000
108	A	55	ASN	0	-0.115	0.035	25.766	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	56	LEU	0	0.112	-0.048	23.678	0.006	0.006	0.000	0.000	0.000	0.000
110	A	56	LEU	0	-0.073	0.083	23.630	0.002	0.002	0.000	0.000	0.000	0.000
111	A	57	LEU	0	0.118	-0.087	19.014	0.011	0.011	0.000	0.000	0.000	0.000
112	A	57	LEU	0	-0.099	0.062	16.691	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	58	GLU	0	0.027	-0.067	19.343	-0.021	-0.021	0.000	0.000	0.000	0.000
114	A	58	GLU	-1	-1.009	-0.870	20.973	-0.202	-0.202	0.000	0.000	0.000	0.000
115	A	59	GLU	0	0.091	-0.123	20.441	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	59	GLU	-1	-1.017	-0.838	23.420	-0.170	-0.170	0.000	0.000	0.000	0.000
117	A	60	GLN	0	0.038	-0.107	19.450	0.018	0.018	0.000	0.000	0.000	0.000
118	A	60	GLN	0	-0.173	0.050	18.787	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	61	GLY	0	-0.007	-0.103	17.094	0.002	0.002	0.000	0.000	0.000	0.000
120	A	62	PHE	0	0.016	-0.047	14.044	-0.047	-0.047	0.000	0.000	0.000	0.000
121	A	62	PHE	0	-0.093	0.112	13.092	0.004	0.004	0.000	0.000	0.000	0.000
122	A	63	VAL	0	0.042	-0.138	14.236	-0.091	-0.091	0.000	0.000	0.000	0.000
123	A	63	VAL	0	-0.068	0.079	15.822	0.004	0.004	0.000	0.000	0.000	0.000
124	A	64	SER	0	0.075	-0.053	16.290	0.039	0.039	0.000	0.000	0.000	0.000
125	A	64	SER	0	-0.031	0.056	16.507	0.018	0.018	0.000	0.000	0.000	0.000
126	A	65	TYR	0	0.023	-0.071	18.313	-0.024	-0.024	0.000	0.000	0.000	0.000
127	A	65	TYR	0	-0.113	0.059	21.820	0.013	0.013	0.000	0.000	0.000	0.000
128	A	66	ARG	0	0.072	-0.099	21.178	0.009	0.009	0.000	0.000	0.000	0.000
129	A	66	ARG	1	0.778	1.012	21.591	0.188	0.188	0.000	0.000	0.000	0.000
130	A	67	LYS	0	0.169	-0.099	23.457	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	67	LYS	1	0.771	1.044	27.757	0.123	0.123	0.000	0.000	0.000	0.000
132	A	68	THR	0	-0.078	-0.151	27.040	0.008	0.008	0.000	0.000	0.000	0.000
133	A	68	THR	0	0.017	0.106	25.925	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	69	ARG	0	0.112	-0.035	28.477	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	69	ARG	1	0.836	1.009	32.751	0.081	0.081	0.000	0.000	0.000	0.000
136	A	70	ASP	0	0.136	-0.095	31.167	0.003	0.003	0.000	0.000	0.000	0.000
137	A	70	ASP	-1	-0.978	-0.804	28.756	-0.115	-0.115	0.000	0.000	0.000	0.000
138	A	71	LYS	0	0.035	-0.085	32.211	0.001	0.001	0.000	0.000	0.000	0.000
139	A	71	LYS	1	0.799	0.989	35.949	0.056	0.056	0.000	0.000	0.000	0.000
140	A	72	ASP	0	0.068	-0.088	35.929	0.000	0.000	0.000	0.000	0.000	0.000
141	A	72	ASP	-1	-0.928	-0.857	37.342	-0.059	-0.059	0.000	0.000	0.000	0.000
142	A	73	SER	0	-0.033	-0.105	35.724	0.005	0.005	0.000	0.000	0.000	0.000
143	A	73	SER	0	-0.024	0.094	34.281	0.000	0.000	0.000	0.000	0.000	0.000
144	A	74	GLY	0	-0.013	-0.114	35.467	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	75	TRP	0	0.024	-0.030	35.134	0.001	0.001	0.000	0.000	0.000	0.000
146	A	75	TRP	0	-0.021	0.123	34.320	0.001	0.001	0.000	0.000	0.000	0.000
147	A	76	PHE	0	0.156	-0.026	32.251	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	76	PHE	0	-0.137	0.036	31.278	0.001	0.001	0.000	0.000	0.000	0.000
149	A	77	ILE	0	0.010	-0.135	28.711	0.002	0.002	0.000	0.000	0.000	0.000
150	A	77	ILE	0	0.001	0.156	26.827	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	78	TYR	0	0.063	-0.071	25.780	0.003	0.003	0.000	0.000	0.000	0.000
152	A	78	TYR	0	-0.062	0.076	25.096	0.010	0.010	0.000	0.000	0.000	0.000
153	A	79	TYR	0	0.052	-0.082	22.302	0.003	0.003	0.000	0.000	0.000	0.000
154	A	79	TYR	0	-0.070	0.105	21.360	0.001	0.001	0.000	0.000	0.000	0.000
155	A	80	TRP	0	0.105	-0.063	19.463	0.005	0.005	0.000	0.000	0.000	0.000
156	A	80	TRP	0	-0.081	0.084	19.156	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	81	LYS	0	0.157	-0.082	15.583	0.003	0.003	0.000	0.000	0.000	0.000
158	A	81	LYS	1	0.848	1.042	11.338	0.639	0.639	0.000	0.000	0.000	0.000
159	A	82	PRO	0	0.015	-0.070	11.044	0.049	0.049	0.000	0.000	0.000	0.000
160	A	83	ASN	0	0.066	0.010	11.501	-0.106	-0.106	0.000	0.000	0.000	0.000
161	A	83	ASN	0	-0.056	0.108	13.275	0.013	0.013	0.000	0.000	0.000	0.000
162	A	84	ILE	0	0.152	-0.061	7.813	0.199	0.199	0.000	0.000	0.000	0.000
163	A	84	ILE	0	-0.057	0.113	5.354	-0.024	-0.006	-0.001	-0.001	-0.016	0.000
164	A	85	ASP	0	0.097	-0.088	7.010	-0.133	-0.133	0.000	0.000	0.000	0.000
165	A	85	ASP	-1	-0.908	-0.843	7.690	-1.141	-1.141	0.000	0.000	0.000	0.000
166	A	86	GLN	0	0.036	-0.056	8.023	0.138	0.138	0.000	0.000	0.000	0.000
167	A	86	GLN	0	-0.067	0.075	12.155	-0.014	-0.014	0.000	0.000	0.000	0.000
168	A	87	ILE	0	0.029	-0.088	8.404	0.160	0.160	0.000	0.000	0.000	0.000
169	A	87	ILE	0	-0.087	0.100	6.309	-0.005	-0.005	0.000	0.000	0.000	0.000
170	A	88	ASN	0	-0.140	-0.168	5.723	0.344	0.344	0.000	0.000	0.000	0.000
171	A	88	ASN	0	-0.026	-0.041	3.649	-1.102	-0.564	0.008	-0.139	-0.407	-0.001

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