FMO DATABASE

FMODB ID: ZN81N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-636721.062728
FMO2-HF: Nuclear repulsion	600877.99451
FMO2-HF: Total energy	-35843.068218
FMO2-MP2: Total energy	-35948.15551

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.
-4.628	-1.404	0.499	-1.442	-2.282	-0.002

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 : 0.187 / q_NPA : 0.049

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	-0.096	0.066	3.660	-0.471	0.222	0.021	-0.357	-0.356	0.002
5	A	3	ASN	0	0.151	-0.042	3.924	-1.779	-0.807	-0.007	-0.478	-0.487	0.002
6	A	3	ASN	0	-0.071	0.053	5.973	0.239	0.239	0.000	0.000	0.000	0.000
7	A	4	ALA	0	0.091	-0.097	3.760	0.763	1.080	0.008	-0.117	-0.208	0.000
8	A	4	ALA	0	-0.070	0.112	3.261	-0.154	-0.072	0.097	-0.042	-0.138	0.000
9	A	5	GLU	0	0.073	-0.103	4.909	0.208	0.277	-0.002	-0.006	-0.060	0.000
10	A	5	GLU	-1	-0.892	-0.781	5.946	-1.426	-1.426	0.000	0.000	0.000	0.000
11	A	6	ASP	0	0.089	-0.140	7.006	0.261	0.261	0.000	0.000	0.000	0.000
12	A	6	ASP	-1	-1.003	-0.835	9.588	-0.716	-0.716	0.000	0.000	0.000	0.000
13	A	7	LEU	0	0.095	-0.107	8.292	0.221	0.221	0.000	0.000	0.000	0.000
14	A	7	LEU	0	-0.120	0.098	7.431	0.009	0.009	0.000	0.000	0.000	0.000
15	A	8	PHE	0	0.086	-0.090	8.653	0.248	0.248	0.000	0.000	0.000	0.000
16	A	8	PHE	0	-0.079	0.104	8.488	-0.057	-0.057	0.000	0.000	0.000	0.000
17	A	9	ILE	0	0.089	-0.086	10.244	0.134	0.134	0.000	0.000	0.000	0.000
18	A	9	ILE	0	-0.069	0.100	11.501	0.027	0.027	0.000	0.000	0.000	0.000
19	A	10	ASN	0	0.077	-0.072	12.495	0.100	0.100	0.000	0.000	0.000	0.000
20	A	10	ASN	0	-0.126	0.041	12.833	0.037	0.037	0.000	0.000	0.000	0.000
21	A	11	LEU	0	0.061	-0.105	12.973	0.094	0.094	0.000	0.000	0.000	0.000
22	A	11	LEU	0	-0.100	0.081	11.037	0.002	0.002	0.000	0.000	0.000	0.000
23	A	12	ALA	0	0.166	-0.058	14.409	0.066	0.066	0.000	0.000	0.000	0.000
24	A	12	ALA	0	-0.089	0.090	15.166	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	13	LYS	0	0.056	-0.122	16.388	0.044	0.044	0.000	0.000	0.000	0.000
26	A	13	LYS	1	0.744	0.972	17.497	0.325	0.325	0.000	0.000	0.000	0.000
27	A	14	SER	0	-0.002	-0.060	17.728	0.038	0.038	0.000	0.000	0.000	0.000
28	A	14	SER	0	-0.081	0.047	17.879	0.006	0.006	0.000	0.000	0.000	0.000
29	A	15	LEU	0	-0.050	-0.128	19.453	0.034	0.034	0.000	0.000	0.000	0.000
30	A	15	LEU	0	-0.035	0.112	17.460	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	16	LEU	0	0.020	-0.125	20.665	0.028	0.028	0.000	0.000	0.000	0.000
32	A	16	LEU	0	-0.068	0.105	19.716	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	17	GLY	0	0.038	-0.075	22.012	0.001	0.001	0.000	0.000	0.000	0.000
34	A	18	ASP	0	0.178	0.027	21.553	-0.027	-0.027	0.000	0.000	0.000	0.000
35	A	18	ASP	-1	-0.915	-0.796	20.735	-0.294	-0.294	0.000	0.000	0.000	0.000
36	A	19	ASP	0	0.099	-0.112	21.868	-0.024	-0.024	0.000	0.000	0.000	0.000
37	A	19	ASP	-1	-0.987	-0.881	25.370	-0.202	-0.202	0.000	0.000	0.000	0.000
38	A	20	VAL	0	0.016	-0.131	21.426	0.008	0.008	0.000	0.000	0.000	0.000
39	A	20	VAL	0	-0.061	0.116	19.494	0.001	0.001	0.000	0.000	0.000	0.000
40	A	21	ILE	0	0.060	-0.097	17.684	-0.035	-0.035	0.000	0.000	0.000	0.000
41	A	21	ILE	0	-0.097	0.112	16.540	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	22	ASP	0	0.118	-0.119	17.389	-0.065	-0.065	0.000	0.000	0.000	0.000
43	A	22	ASP	-1	-1.001	-0.852	21.451	-0.272	-0.272	0.000	0.000	0.000	0.000
44	A	23	VAL	0	0.059	-0.085	18.888	-0.016	-0.016	0.000	0.000	0.000	0.000
45	A	23	VAL	0	-0.112	0.068	19.176	0.006	0.006	0.000	0.000	0.000	0.000
46	A	24	LEU	0	0.121	-0.088	15.550	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	24	LEU	0	-0.106	0.093	13.099	0.004	0.004	0.000	0.000	0.000	0.000
48	A	25	ARG	0	0.019	-0.129	14.067	-0.125	-0.125	0.000	0.000	0.000	0.000
49	A	25	ARG	1	0.673	0.931	10.850	0.777	0.777	0.000	0.000	0.000	0.000
50	A	26	ILE	0	0.119	-0.042	14.352	-0.077	-0.077	0.000	0.000	0.000	0.000
51	A	26	ILE	0	-0.075	0.091	18.140	0.009	0.009	0.000	0.000	0.000	0.000
52	A	27	LEU	0	0.135	-0.102	15.169	0.026	0.026	0.000	0.000	0.000	0.000
53	A	27	LEU	0	-0.120	0.070	14.490	0.004	0.004	0.000	0.000	0.000	0.000
54	A	28	LEU	0	0.050	-0.100	11.025	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	28	LEU	0	-0.074	0.084	8.629	-0.058	-0.058	0.000	0.000	0.000	0.000
56	A	29	ASP	0	0.068	-0.087	11.198	-0.109	-0.109	0.000	0.000	0.000	0.000
57	A	29	ASP	-1	-0.934	-0.808	13.955	-0.540	-0.540	0.000	0.000	0.000	0.000
58	A	30	LYS	0	0.072	-0.098	13.494	0.047	0.047	0.000	0.000	0.000	0.000
59	A	30	LYS	1	0.734	0.980	15.854	0.326	0.326	0.000	0.000	0.000	0.000
60	A	31	GLY	0	0.013	-0.081	11.272	0.045	0.045	0.000	0.000	0.000	0.000
61	A	32	THR	0	-0.052	-0.017	12.107	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	32	THR	0	-0.043	0.044	14.349	0.042	0.042	0.000	0.000	0.000	0.000
63	A	33	GLU	0	0.088	-0.071	14.986	-0.024	-0.024	0.000	0.000	0.000	0.000
64	A	33	GLU	-1	-0.930	-0.832	17.155	-0.316	-0.316	0.000	0.000	0.000	0.000
65	A	34	MET	0	0.046	-0.081	17.638	0.032	0.032	0.000	0.000	0.000	0.000
66	A	34	MET	0	-0.061	0.121	17.954	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	35	THR	0	0.023	-0.070	20.284	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	35	THR	0	-0.026	0.090	24.644	0.001	0.001	0.000	0.000	0.000	0.000
69	A	36	ASP	0	0.113	-0.076	23.527	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	36	ASP	-1	-0.827	-0.801	25.458	-0.197	-0.197	0.000	0.000	0.000	0.000
71	A	37	GLU	0	0.075	-0.146	25.075	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	37	GLU	-1	-0.970	-0.853	27.611	-0.158	-0.158	0.000	0.000	0.000	0.000
73	A	38	GLU	0	0.027	-0.119	23.527	0.017	0.017	0.000	0.000	0.000	0.000
74	A	38	GLU	-1	-0.867	-0.793	22.324	-0.269	-0.269	0.000	0.000	0.000	0.000
75	A	39	ILE	0	0.118	-0.050	22.145	0.010	0.010	0.000	0.000	0.000	0.000
76	A	39	ILE	0	-0.078	0.089	19.834	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	40	ALA	0	0.061	-0.091	22.909	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	40	ALA	0	-0.096	0.084	27.303	0.003	0.003	0.000	0.000	0.000	0.000
79	A	41	ASN	0	0.081	-0.065	26.530	0.010	0.010	0.000	0.000	0.000	0.000
80	A	41	ASN	0	-0.146	0.037	26.994	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	42	GLN	0	0.005	-0.118	23.572	0.020	0.020	0.000	0.000	0.000	0.000
82	A	42	GLN	0	-0.095	0.072	21.856	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	43	LEU	0	0.090	-0.092	23.653	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	43	LEU	0	-0.055	0.108	21.261	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	44	ASN	0	-0.003	-0.068	24.727	0.002	0.002	0.000	0.000	0.000	0.000
86	A	44	ASN	0	-0.121	0.052	28.469	0.000	0.000	0.000	0.000	0.000	0.000
87	A	45	ILE	0	0.095	-0.108	27.774	0.013	0.013	0.000	0.000	0.000	0.000
88	A	45	ILE	0	-0.036	0.125	24.378	0.001	0.001	0.000	0.000	0.000	0.000
89	A	46	LYS	0	0.098	-0.095	28.876	0.000	0.000	0.000	0.000	0.000	0.000
90	A	46	LYS	1	0.849	1.043	31.581	0.125	0.125	0.000	0.000	0.000	0.000
91	A	47	VAL	0	0.153	-0.088	28.458	-0.010	-0.010	0.000	0.000	0.000	0.000
92	A	47	VAL	0	-0.026	0.131	28.353	0.003	0.003	0.000	0.000	0.000	0.000
93	A	48	ASN	0	0.073	-0.050	28.525	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	48	ASN	0	-0.111	0.045	32.290	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	49	ASP	0	0.069	-0.094	28.900	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	49	ASP	-1	-0.928	-0.837	27.941	-0.196	-0.196	0.000	0.000	0.000	0.000
97	A	50	VAL	0	0.136	-0.095	24.867	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	50	VAL	0	-0.103	0.123	23.441	0.000	0.000	0.000	0.000	0.000	0.000
99	A	51	ARG	0	0.141	-0.054	24.361	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	51	ARG	1	0.705	0.966	26.739	0.184	0.184	0.000	0.000	0.000	0.000
101	A	52	LYS	0	0.040	-0.102	25.613	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	52	LYS	1	0.871	1.035	27.830	0.164	0.164	0.000	0.000	0.000	0.000
103	A	53	LYS	0	0.120	-0.051	23.506	0.001	0.001	0.000	0.000	0.000	0.000
104	A	53	LYS	1	0.773	1.039	22.497	0.230	0.230	0.000	0.000	0.000	0.000
105	A	54	LEU	0	0.087	-0.094	20.907	-0.028	-0.028	0.000	0.000	0.000	0.000
106	A	54	LEU	0	-0.113	0.077	19.825	0.001	0.001	0.000	0.000	0.000	0.000
107	A	55	ASN	0	0.120	-0.050	21.401	-0.030	-0.030	0.000	0.000	0.000	0.000
108	A	55	ASN	0	-0.169	0.015	25.298	0.014	0.014	0.000	0.000	0.000	0.000
109	A	56	LEU	0	0.115	-0.073	23.339	0.001	0.001	0.000	0.000	0.000	0.000
110	A	56	LEU	0	-0.081	0.089	23.351	0.003	0.003	0.000	0.000	0.000	0.000
111	A	57	LEU	0	0.119	-0.097	18.706	0.009	0.009	0.000	0.000	0.000	0.000
112	A	57	LEU	0	-0.108	0.084	16.560	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	58	GLU	0	0.061	-0.093	18.657	-0.045	-0.045	0.000	0.000	0.000	0.000
114	A	58	GLU	-1	-0.976	-0.850	21.219	-0.258	-0.258	0.000	0.000	0.000	0.000
115	A	59	GLU	0	0.071	-0.110	20.456	-0.012	-0.012	0.000	0.000	0.000	0.000
116	A	59	GLU	-1	-1.010	-0.837	23.428	-0.222	-0.222	0.000	0.000	0.000	0.000
117	A	60	GLN	0	-0.002	-0.117	19.810	0.018	0.018	0.000	0.000	0.000	0.000
118	A	60	GLN	0	-0.136	0.062	19.131	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	61	GLY	0	0.036	-0.092	17.202	-0.020	-0.020	0.000	0.000	0.000	0.000
120	A	62	PHE	0	0.062	-0.020	14.124	-0.070	-0.070	0.000	0.000	0.000	0.000
121	A	62	PHE	0	-0.088	0.113	13.239	0.006	0.006	0.000	0.000	0.000	0.000
122	A	63	VAL	0	0.049	-0.091	14.039	-0.123	-0.123	0.000	0.000	0.000	0.000
123	A	63	VAL	0	-0.084	0.087	15.767	0.005	0.005	0.000	0.000	0.000	0.000
124	A	64	SER	0	0.073	-0.075	16.373	0.046	0.046	0.000	0.000	0.000	0.000
125	A	64	SER	0	-0.053	0.041	16.258	0.019	0.019	0.000	0.000	0.000	0.000
126	A	65	TYR	0	0.023	-0.082	18.272	-0.029	-0.029	0.000	0.000	0.000	0.000
127	A	65	TYR	0	-0.108	0.064	21.502	0.018	0.018	0.000	0.000	0.000	0.000
128	A	66	ARG	0	0.118	-0.107	20.902	0.009	0.009	0.000	0.000	0.000	0.000
129	A	66	ARG	1	0.752	1.023	20.693	0.255	0.255	0.000	0.000	0.000	0.000
130	A	67	LYS	0	0.134	-0.068	23.146	0.000	0.000	0.000	0.000	0.000	0.000
131	A	67	LYS	1	0.805	1.046	27.448	0.166	0.166	0.000	0.000	0.000	0.000
132	A	68	THR	0	-0.101	-0.135	26.712	0.007	0.007	0.000	0.000	0.000	0.000
133	A	68	THR	0	0.005	0.099	25.678	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	69	ARG	0	0.112	-0.061	28.167	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	69	ARG	1	0.867	1.032	32.085	0.111	0.111	0.000	0.000	0.000	0.000
136	A	70	ASP	0	0.139	-0.075	30.534	0.009	0.009	0.000	0.000	0.000	0.000
137	A	70	ASP	-1	-0.913	-0.781	28.348	-0.161	-0.161	0.000	0.000	0.000	0.000
138	A	71	LYS	0	0.100	-0.047	31.604	0.003	0.003	0.000	0.000	0.000	0.000
139	A	71	LYS	1	0.795	0.988	35.213	0.078	0.078	0.000	0.000	0.000	0.000
140	A	72	ASP	0	0.075	-0.104	35.246	0.000	0.000	0.000	0.000	0.000	0.000
141	A	72	ASP	-1	-0.923	-0.847	36.818	-0.081	-0.081	0.000	0.000	0.000	0.000
142	A	73	SER	0	-0.052	-0.132	34.279	0.007	0.007	0.000	0.000	0.000	0.000
143	A	73	SER	0	-0.026	0.086	33.547	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	74	GLY	0	-0.032	-0.100	35.785	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	75	TRP	0	0.016	-0.026	34.797	0.004	0.004	0.000	0.000	0.000	0.000
146	A	75	TRP	0	-0.047	0.111	34.044	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	76	PHE	0	0.112	-0.047	31.815	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	76	PHE	0	-0.121	0.044	30.972	0.001	0.001	0.000	0.000	0.000	0.000
149	A	77	ILE	0	0.033	-0.133	28.388	0.004	0.004	0.000	0.000	0.000	0.000
150	A	77	ILE	0	-0.026	0.149	26.378	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	78	TYR	0	0.055	-0.105	25.679	0.000	0.000	0.000	0.000	0.000	0.000
152	A	78	TYR	0	-0.068	0.083	25.041	0.013	0.013	0.000	0.000	0.000	0.000
153	A	79	TYR	0	0.105	-0.074	22.246	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	79	TYR	0	-0.108	0.071	21.353	0.002	0.002	0.000	0.000	0.000	0.000
155	A	80	TRP	0	0.068	-0.091	19.398	0.007	0.007	0.000	0.000	0.000	0.000
156	A	80	TRP	0	-0.071	0.090	19.188	0.001	0.001	0.000	0.000	0.000	0.000
157	A	81	LYS	0	0.142	-0.080	15.270	0.013	0.013	0.000	0.000	0.000	0.000
158	A	81	LYS	1	0.809	1.031	10.925	0.886	0.886	0.000	0.000	0.000	0.000
159	A	82	PRO	0	0.010	-0.073	11.080	0.052	0.052	0.000	0.000	0.000	0.000
160	A	83	ASN	0	0.058	0.012	11.481	-0.132	-0.132	0.000	0.000	0.000	0.000
161	A	83	ASN	0	-0.095	0.091	12.982	0.020	0.020	0.000	0.000	0.000	0.000
162	A	84	ILE	0	0.127	-0.088	7.599	0.211	0.211	0.000	0.000	0.000	0.000
163	A	84	ILE	0	-0.035	0.121	5.429	-0.004	-0.004	0.000	0.000	0.000	0.000
164	A	85	ASP	0	0.101	-0.107	6.845	-0.345	-0.345	0.000	0.000	0.000	0.000
165	A	85	ASP	-1	-0.928	-0.829	7.274	-1.612	-1.612	0.000	0.000	0.000	0.000
166	A	86	GLN	0	0.032	-0.072	7.863	0.110	0.110	0.000	0.000	0.000	0.000
167	A	86	GLN	0	-0.068	0.075	12.065	-0.031	-0.031	0.000	0.000	0.000	0.000
168	A	87	ILE	0	0.032	-0.073	8.690	0.214	0.214	0.000	0.000	0.000	0.000
169	A	87	ILE	0	-0.089	0.107	6.661	0.004	0.004	0.000	0.000	0.000	0.000
170	A	88	ASN	0	-0.116	-0.168	5.158	0.444	0.453	-0.001	-0.006	-0.002	0.000
171	A	88	ASN	0	0.017	-0.027	2.832	-1.370	-0.288	0.383	-0.436	-1.031	-0.006

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