FMO DATABASE

FMODB ID: RY2V8

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

Total energy (hartree)

FMO2-HF: Electronic energy	-637882.626976
FMO2-HF: Nuclear repulsion	602043.0175
FMO2-HF: Total energy	-35839.609476
FMO2-MP2: Total energy	-35945.055459

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.
-2.476	-0.014000000000001	0.636	-1.321	-1.772	0.005

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 : 0.160 / q_NPA : 0.035

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	0.081	3.371	-0.732	0.214	0.029	-0.487	-0.487	0.002
5	A	3	ASN	0	0.106	-0.042	3.826	-0.641	0.549	-0.010	-0.604	-0.576	0.001
6	A	3	ASN	0	-0.083	0.061	6.005	0.013	0.013	0.000	0.000	0.000	0.000
7	A	4	ALA	0	0.103	-0.113	3.497	0.999	1.043	0.018	0.136	-0.197	0.000
8	A	4	ALA	0	-0.060	0.091	2.511	-0.131	-0.074	0.602	-0.325	-0.333	0.002
9	A	5	GLU	0	0.068	-0.125	4.599	0.343	0.400	-0.001	-0.011	-0.044	0.000
10	A	5	GLU	-1	-0.939	-0.813	5.817	-1.538	-1.538	0.000	0.000	0.000	0.000
11	A	6	ASP	0	0.083	-0.140	6.825	0.364	0.364	0.000	0.000	0.000	0.000
12	A	6	ASP	-1	-0.999	-0.825	8.618	-1.145	-1.145	0.000	0.000	0.000	0.000
13	A	7	LEU	0	0.073	-0.137	7.630	0.246	0.246	0.000	0.000	0.000	0.000
14	A	7	LEU	0	-0.094	0.117	6.148	0.004	0.004	0.000	0.000	0.000	0.000
15	A	8	PHE	0	0.052	-0.103	8.632	0.238	0.238	0.000	0.000	0.000	0.000
16	A	8	PHE	0	-0.031	0.105	8.228	-0.040	-0.040	0.000	0.000	0.000	0.000
17	A	9	ILE	0	0.085	-0.100	9.849	0.138	0.138	0.000	0.000	0.000	0.000
18	A	9	ILE	0	-0.056	0.108	10.939	0.022	0.022	0.000	0.000	0.000	0.000
19	A	10	ASN	0	0.042	-0.076	11.889	0.092	0.092	0.000	0.000	0.000	0.000
20	A	10	ASN	0	-0.111	0.041	12.105	0.031	0.031	0.000	0.000	0.000	0.000
21	A	11	LEU	0	0.049	-0.122	12.490	0.067	0.067	0.000	0.000	0.000	0.000
22	A	11	LEU	0	-0.060	0.104	10.819	0.008	0.008	0.000	0.000	0.000	0.000
23	A	12	ALA	0	0.190	-0.032	14.059	0.060	0.060	0.000	0.000	0.000	0.000
24	A	12	ALA	0	-0.091	0.071	14.816	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	13	LYS	0	0.141	-0.034	16.012	0.045	0.045	0.000	0.000	0.000	0.000
26	A	13	LYS	1	0.849	1.031	15.812	0.435	0.435	0.000	0.000	0.000	0.000
27	A	14	SER	0	0.034	-0.059	17.557	0.025	0.025	0.000	0.000	0.000	0.000
28	A	14	SER	0	-0.076	0.028	17.699	0.005	0.005	0.000	0.000	0.000	0.000
29	A	15	LEU	0	-0.097	-0.139	19.102	0.028	0.028	0.000	0.000	0.000	0.000
30	A	15	LEU	0	-0.072	0.102	16.667	0.001	0.001	0.000	0.000	0.000	0.000
31	A	16	LEU	0	0.033	-0.090	20.063	0.027	0.027	0.000	0.000	0.000	0.000
32	A	16	LEU	0	-0.109	0.043	19.471	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	17	GLY	0	0.021	-0.090	21.870	0.003	0.003	0.000	0.000	0.000	0.000
34	A	18	ASP	0	0.091	-0.027	21.067	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	18	ASP	-1	-0.943	-0.813	22.428	-0.245	-0.245	0.000	0.000	0.000	0.000
36	A	19	ASP	0	0.167	-0.098	21.615	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	19	ASP	-1	-0.999	-0.871	25.068	-0.185	-0.185	0.000	0.000	0.000	0.000
38	A	20	VAL	0	-0.005	-0.121	21.072	0.000	0.000	0.000	0.000	0.000	0.000
39	A	20	VAL	0	-0.079	0.101	19.074	0.000	0.000	0.000	0.000	0.000	0.000
40	A	21	ILE	0	0.086	-0.101	17.255	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	21	ILE	0	-0.087	0.123	16.327	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	22	ASP	0	0.088	-0.129	17.014	-0.070	-0.070	0.000	0.000	0.000	0.000
43	A	22	ASP	-1	-0.974	-0.833	20.970	-0.284	-0.284	0.000	0.000	0.000	0.000
44	A	23	VAL	0	0.054	-0.083	18.653	-0.018	-0.018	0.000	0.000	0.000	0.000
45	A	23	VAL	0	-0.104	0.066	18.566	0.007	0.007	0.000	0.000	0.000	0.000
46	A	24	LEU	0	0.119	-0.108	15.114	0.004	0.004	0.000	0.000	0.000	0.000
47	A	24	LEU	0	-0.104	0.106	13.090	0.006	0.006	0.000	0.000	0.000	0.000
48	A	25	ARG	0	0.018	-0.113	13.965	-0.101	-0.101	0.000	0.000	0.000	0.000
49	A	25	ARG	1	0.746	1.004	11.149	0.774	0.774	0.000	0.000	0.000	0.000
50	A	26	ILE	0	0.189	-0.044	14.198	-0.067	-0.067	0.000	0.000	0.000	0.000
51	A	26	ILE	0	-0.043	0.078	18.255	0.008	0.008	0.000	0.000	0.000	0.000
52	A	27	LEU	0	-0.034	-0.091	15.022	0.017	0.017	0.000	0.000	0.000	0.000
53	A	27	LEU	0	-0.115	0.044	14.528	0.008	0.008	0.000	0.000	0.000	0.000
54	A	28	LEU	0	0.061	-0.095	10.851	0.041	0.041	0.000	0.000	0.000	0.000
55	A	28	LEU	0	-0.093	0.067	8.623	-0.029	-0.029	0.000	0.000	0.000	0.000
56	A	29	ASP	0	0.069	-0.071	10.736	-0.139	-0.139	0.000	0.000	0.000	0.000
57	A	29	ASP	-1	-0.976	-0.849	13.830	-0.573	-0.573	0.000	0.000	0.000	0.000
58	A	30	LYS	0	0.106	-0.088	13.305	0.010	0.010	0.000	0.000	0.000	0.000
59	A	30	LYS	1	0.727	0.988	16.201	0.248	0.248	0.000	0.000	0.000	0.000
60	A	31	GLY	0	0.014	-0.067	11.892	0.039	0.039	0.000	0.000	0.000	0.000
61	A	32	THR	0	-0.074	-0.049	12.784	0.022	0.022	0.000	0.000	0.000	0.000
62	A	32	THR	0	-0.023	0.060	15.089	0.025	0.025	0.000	0.000	0.000	0.000
63	A	33	GLU	0	0.062	-0.100	15.627	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	33	GLU	-1	-0.964	-0.853	17.935	-0.174	-0.174	0.000	0.000	0.000	0.000
65	A	34	MET	0	0.055	-0.078	18.111	0.021	0.021	0.000	0.000	0.000	0.000
66	A	34	MET	0	-0.061	0.149	17.753	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	35	THR	0	0.024	-0.123	20.319	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	35	THR	0	-0.023	0.113	24.392	0.004	0.004	0.000	0.000	0.000	0.000
69	A	36	ASP	0	0.140	-0.051	23.574	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	36	ASP	-1	-0.874	-0.842	25.718	-0.150	-0.150	0.000	0.000	0.000	0.000
71	A	37	GLU	0	0.030	-0.116	25.140	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	37	GLU	-1	-1.003	-0.895	27.400	-0.121	-0.121	0.000	0.000	0.000	0.000
73	A	38	GLU	0	0.113	-0.058	23.629	0.005	0.005	0.000	0.000	0.000	0.000
74	A	38	GLU	-1	-0.923	-0.841	22.224	-0.209	-0.209	0.000	0.000	0.000	0.000
75	A	39	ILE	0	0.101	-0.091	21.844	0.001	0.001	0.000	0.000	0.000	0.000
76	A	39	ILE	0	-0.061	0.101	20.053	0.000	0.000	0.000	0.000	0.000	0.000
77	A	40	ALA	0	0.082	-0.090	22.564	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	40	ALA	0	-0.082	0.073	26.685	0.003	0.003	0.000	0.000	0.000	0.000
79	A	41	ASN	0	0.034	-0.073	26.084	0.007	0.007	0.000	0.000	0.000	0.000
80	A	41	ASN	0	-0.146	0.025	27.029	0.000	0.000	0.000	0.000	0.000	0.000
81	A	42	GLN	0	-0.020	-0.114	23.992	0.014	0.014	0.000	0.000	0.000	0.000
82	A	42	GLN	0	-0.077	0.094	22.332	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	43	LEU	0	0.075	-0.164	23.431	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	43	LEU	0	-0.079	0.149	21.373	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	44	ASN	0	0.089	-0.065	24.758	0.004	0.004	0.000	0.000	0.000	0.000
86	A	44	ASN	0	-0.126	0.067	27.823	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	45	ILE	0	0.081	-0.128	27.872	0.001	0.001	0.000	0.000	0.000	0.000
88	A	45	ILE	0	-0.004	0.141	24.698	0.001	0.001	0.000	0.000	0.000	0.000
89	A	46	LYS	0	0.083	-0.071	29.111	0.002	0.002	0.000	0.000	0.000	0.000
90	A	46	LYS	1	0.821	1.035	31.691	0.110	0.110	0.000	0.000	0.000	0.000
91	A	47	VAL	0	0.200	-0.114	28.409	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	47	VAL	0	-0.001	0.156	28.072	0.002	0.002	0.000	0.000	0.000	0.000
93	A	48	ASN	0	0.064	-0.043	28.709	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	48	ASN	0	-0.133	0.049	32.298	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	49	ASP	0	0.091	-0.121	29.040	0.001	0.001	0.000	0.000	0.000	0.000
96	A	49	ASP	-1	-0.929	-0.833	27.998	-0.170	-0.170	0.000	0.000	0.000	0.000
97	A	50	VAL	0	0.098	-0.118	25.250	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	50	VAL	0	-0.066	0.149	23.928	0.000	0.000	0.000	0.000	0.000	0.000
99	A	51	ARG	0	0.085	-0.079	24.495	-0.019	-0.019	0.000	0.000	0.000	0.000
100	A	51	ARG	1	0.756	1.002	27.193	0.135	0.135	0.000	0.000	0.000	0.000
101	A	52	LYS	0	0.033	-0.066	26.054	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	52	LYS	1	0.842	1.034	28.096	0.128	0.128	0.000	0.000	0.000	0.000
103	A	53	LYS	0	0.096	-0.070	23.268	0.008	0.008	0.000	0.000	0.000	0.000
104	A	53	LYS	1	0.811	1.066	22.199	0.211	0.211	0.000	0.000	0.000	0.000
105	A	54	LEU	0	0.087	-0.094	21.067	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	54	LEU	0	-0.100	0.091	19.918	0.001	0.001	0.000	0.000	0.000	0.000
107	A	55	ASN	0	0.147	-0.067	21.643	-0.015	-0.015	0.000	0.000	0.000	0.000
108	A	55	ASN	0	-0.109	0.043	25.565	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	56	LEU	0	0.088	-0.052	23.654	0.010	0.010	0.000	0.000	0.000	0.000
110	A	56	LEU	0	-0.087	0.088	23.319	0.001	0.001	0.000	0.000	0.000	0.000
111	A	57	LEU	0	0.121	-0.082	18.955	0.010	0.010	0.000	0.000	0.000	0.000
112	A	57	LEU	0	-0.108	0.069	16.711	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	58	GLU	0	0.089	-0.075	19.325	-0.016	-0.016	0.000	0.000	0.000	0.000
114	A	58	GLU	-1	-1.042	-0.897	21.130	-0.172	-0.172	0.000	0.000	0.000	0.000
115	A	59	GLU	0	0.130	-0.099	20.454	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	59	GLU	-1	-1.026	-0.823	23.377	-0.157	-0.157	0.000	0.000	0.000	0.000
117	A	60	GLN	0	0.010	-0.132	19.302	0.020	0.020	0.000	0.000	0.000	0.000
118	A	60	GLN	0	-0.149	0.044	18.752	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	61	GLY	0	-0.032	-0.094	17.059	0.006	0.006	0.000	0.000	0.000	0.000
120	A	62	PHE	0	-0.001	-0.056	14.053	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	62	PHE	0	-0.094	0.118	13.350	0.000	0.000	0.000	0.000	0.000	0.000
122	A	63	VAL	0	0.035	-0.114	14.232	-0.087	-0.087	0.000	0.000	0.000	0.000
123	A	63	VAL	0	-0.072	0.079	15.471	0.003	0.003	0.000	0.000	0.000	0.000
124	A	64	SER	0	0.056	-0.069	16.308	0.033	0.033	0.000	0.000	0.000	0.000
125	A	64	SER	0	-0.002	0.101	16.781	0.014	0.014	0.000	0.000	0.000	0.000
126	A	65	TYR	0	0.043	-0.072	18.364	-0.022	-0.022	0.000	0.000	0.000	0.000
127	A	65	TYR	0	-0.074	0.050	21.886	0.011	0.011	0.000	0.000	0.000	0.000
128	A	66	ARG	0	0.062	-0.121	21.226	0.011	0.011	0.000	0.000	0.000	0.000
129	A	66	ARG	1	0.798	1.062	21.647	0.145	0.145	0.000	0.000	0.000	0.000
130	A	67	LYS	0	0.203	-0.111	23.523	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	67	LYS	1	0.749	1.047	27.813	0.096	0.096	0.000	0.000	0.000	0.000
132	A	68	THR	0	-0.068	-0.138	27.099	0.008	0.008	0.000	0.000	0.000	0.000
133	A	68	THR	0	0.005	0.113	25.987	0.002	0.002	0.000	0.000	0.000	0.000
134	A	69	ARG	0	0.117	-0.050	28.543	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	69	ARG	1	0.825	1.010	33.109	0.057	0.057	0.000	0.000	0.000	0.000
136	A	70	ASP	0	0.124	-0.096	31.504	0.001	0.001	0.000	0.000	0.000	0.000
137	A	70	ASP	-1	-0.985	-0.808	29.116	-0.080	-0.080	0.000	0.000	0.000	0.000
138	A	71	LYS	0	0.050	-0.086	32.486	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	71	LYS	1	0.805	0.995	36.277	0.036	0.036	0.000	0.000	0.000	0.000
140	A	72	ASP	0	0.064	-0.088	36.218	0.000	0.000	0.000	0.000	0.000	0.000
141	A	72	ASP	-1	-0.930	-0.856	37.477	-0.041	-0.041	0.000	0.000	0.000	0.000
142	A	73	SER	0	-0.038	-0.107	35.755	0.004	0.004	0.000	0.000	0.000	0.000
143	A	73	SER	0	-0.020	0.090	34.300	0.000	0.000	0.000	0.000	0.000	0.000
144	A	74	GLY	0	0.001	-0.106	35.503	-0.004	-0.004	0.000	0.000	0.000	0.000
145	A	75	TRP	0	0.070	-0.040	35.154	0.000	0.000	0.000	0.000	0.000	0.000
146	A	75	TRP	0	-0.048	0.142	34.228	0.001	0.001	0.000	0.000	0.000	0.000
147	A	76	PHE	0	0.137	-0.055	32.303	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	76	PHE	0	-0.126	0.047	31.275	0.000	0.000	0.000	0.000	0.000	0.000
149	A	77	ILE	0	0.000	-0.136	28.739	0.000	0.000	0.000	0.000	0.000	0.000
150	A	77	ILE	0	0.005	0.170	26.915	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	78	TYR	0	0.092	-0.072	25.815	0.006	0.006	0.000	0.000	0.000	0.000
152	A	78	TYR	0	-0.069	0.085	25.119	0.008	0.008	0.000	0.000	0.000	0.000
153	A	79	TYR	0	0.046	-0.095	22.302	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	79	TYR	0	-0.077	0.102	21.311	0.001	0.001	0.000	0.000	0.000	0.000
155	A	80	TRP	0	0.096	-0.087	19.479	0.011	0.011	0.000	0.000	0.000	0.000
156	A	80	TRP	0	-0.082	0.119	19.023	-0.004	-0.004	0.000	0.000	0.000	0.000
157	A	81	LYS	0	0.122	-0.099	15.643	-0.003	-0.003	0.000	0.000	0.000	0.000
158	A	81	LYS	1	0.905	1.090	13.074	0.328	0.328	0.000	0.000	0.000	0.000
159	A	82	PRO	0	0.076	-0.056	10.970	0.049	0.049	0.000	0.000	0.000	0.000
160	A	83	ASN	0	0.061	0.033	11.544	-0.078	-0.078	0.000	0.000	0.000	0.000
161	A	83	ASN	0	-0.093	0.083	13.378	0.009	0.009	0.000	0.000	0.000	0.000
162	A	84	ILE	0	0.158	-0.112	7.799	0.201	0.201	0.000	0.000	0.000	0.000
163	A	84	ILE	0	-0.067	0.132	4.985	-0.046	-0.022	-0.001	-0.004	-0.018	0.000
164	A	85	ASP	0	0.147	-0.060	7.138	-0.046	-0.046	0.000	0.000	0.000	0.000
165	A	85	ASP	-1	-1.027	-0.869	7.654	-0.617	-0.617	0.000	0.000	0.000	0.000
166	A	86	GLN	0	0.020	-0.091	8.148	0.177	0.177	0.000	0.000	0.000	0.000
167	A	86	GLN	0	-0.081	0.056	12.145	-0.014	-0.014	0.000	0.000	0.000	0.000
168	A	87	ILE	0	0.018	-0.113	8.130	0.156	0.156	0.000	0.000	0.000	0.000
169	A	87	ILE	0	-0.103	0.082	6.061	-0.016	-0.016	0.000	0.000	0.000	0.000
170	A	88	ASN	0	-0.093	-0.125	5.778	0.142	0.142	0.000	0.000	0.000	0.000
171	A	88	ASN	0	0.015	-0.010	4.376	-0.609	-0.465	-0.001	-0.026	-0.117	0.000

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