FMO DATABASE

FMODB ID: 7Y2NK

Calculation Name: 1NO4-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1NO4

Chain ID: A

ChEMBL ID:

UniProt ID: P13848

Base Structure: X-ray

Registration Date: 2025-07-14

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-383648.009827
FMO2-HF: Nuclear repulsion	353029.628936
FMO2-HF: Total energy	-30618.380891
FMO2-MP2: Total energy	-30709.425154

3D Structure

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:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-7.875	-4.94	12.598	-3.756	-11.776	-0.041

Interaction energy analysis for fragmet #1(A:2:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.006 / q_NPA : -0.010

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].
3	A	3	LEU	0	-0.104	0.081	3.773	-0.167	0.323	0.001	-0.190	-0.301	0.000
4	A	4	LYS	0	0.155	-0.093	3.727	0.348	1.761	-0.007	-0.642	-0.764	0.003
5	A	4	LYS	1	0.667	1.000	6.719	0.159	0.159	0.000	0.000	0.000	0.000
6	A	5	PRO	0	-0.022	-0.131	6.181	-0.050	-0.050	0.000	0.000	0.000	0.000
7	A	6	GLU	0	0.106	-0.027	8.170	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	6	GLU	-1	-0.907	-0.804	11.215	-0.083	-0.083	0.000	0.000	0.000	0.000
9	A	7	GLU	0	0.098	-0.075	8.535	0.126	0.126	0.000	0.000	0.000	0.000
10	A	7	GLU	-1	-0.912	-0.801	6.416	-1.530	-1.530	0.000	0.000	0.000	0.000
11	A	8	HIS	0	0.118	-0.070	7.462	-0.051	-0.051	0.000	0.000	0.000	0.000
12	A	8	HIS	0	-0.115	0.073	6.422	-0.063	-0.063	0.000	0.000	0.000	0.000
13	A	9	GLU	0	0.087	-0.127	8.425	0.033	0.033	0.000	0.000	0.000	0.000
14	A	9	GLU	-1	-0.990	-0.844	11.947	0.023	0.023	0.000	0.000	0.000	0.000
15	A	10	ASP	0	0.101	-0.116	11.869	0.044	0.044	0.000	0.000	0.000	0.000
16	A	10	ASP	-1	-1.013	-0.840	12.182	-0.244	-0.244	0.000	0.000	0.000	0.000
17	A	11	ILE	0	0.036	-0.114	11.526	0.041	0.041	0.000	0.000	0.000	0.000
18	A	11	ILE	0	-0.105	0.079	9.067	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	12	LEU	0	0.027	-0.155	12.354	0.014	0.014	0.000	0.000	0.000	0.000
20	A	12	LEU	0	-0.057	0.132	11.470	0.012	0.012	0.000	0.000	0.000	0.000
21	A	13	ASN	0	0.086	-0.082	14.009	0.023	0.023	0.000	0.000	0.000	0.000
22	A	13	ASN	0	-0.116	0.080	16.546	0.019	0.019	0.000	0.000	0.000	0.000
23	A	14	LYS	0	0.103	-0.096	16.122	0.021	0.021	0.000	0.000	0.000	0.000
24	A	14	LYS	1	0.790	1.052	16.169	0.181	0.181	0.000	0.000	0.000	0.000
25	A	15	LEU	0	-0.011	-0.155	16.567	0.006	0.006	0.000	0.000	0.000	0.000
26	A	15	LEU	0	-0.086	0.104	14.334	0.001	0.001	0.000	0.000	0.000	0.000
27	A	16	LEU	0	0.093	-0.084	17.981	0.010	0.010	0.000	0.000	0.000	0.000
28	A	16	LEU	0	-0.093	0.110	19.342	0.002	0.002	0.000	0.000	0.000	0.000
29	A	17	ASP	0	0.034	-0.134	20.372	0.014	0.014	0.000	0.000	0.000	0.000
30	A	17	ASP	-1	-0.958	-0.812	22.408	-0.069	-0.069	0.000	0.000	0.000	0.000
31	A	18	PRO	0	-0.039	-0.131	23.163	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	19	GLU	0	0.084	-0.021	25.301	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	19	GLU	-1	-0.997	-0.842	27.185	-0.046	-0.046	0.000	0.000	0.000	0.000
34	A	20	LEU	0	0.136	-0.109	22.409	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	20	LEU	0	-0.163	0.115	19.250	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	21	ALA	0	0.104	-0.102	23.881	0.007	0.007	0.000	0.000	0.000	0.000
37	A	21	ALA	0	-0.082	0.112	24.139	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	22	GLN	0	0.112	-0.105	22.767	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	22	GLN	0	-0.045	0.121	22.200	0.007	0.007	0.000	0.000	0.000	0.000
40	A	23	SER	0	0.039	-0.098	21.681	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	23	SER	0	-0.001	0.095	22.169	0.006	0.006	0.000	0.000	0.000	0.000
42	A	24	GLU	0	0.057	-0.094	19.236	-0.019	-0.019	0.000	0.000	0.000	0.000
43	A	24	GLU	-1	-0.963	-0.867	19.833	-0.169	-0.169	0.000	0.000	0.000	0.000
44	A	25	ARG	0	0.162	-0.066	17.942	-0.027	-0.027	0.000	0.000	0.000	0.000
45	A	25	ARG	1	0.765	1.046	19.449	0.081	0.081	0.000	0.000	0.000	0.000
46	A	26	THR	0	-0.034	-0.109	17.316	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	26	THR	0	-0.090	0.035	18.329	0.008	0.008	0.000	0.000	0.000	0.000
48	A	27	GLU	0	0.146	-0.102	16.030	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	27	GLU	-1	-1.003	-0.828	14.740	-0.272	-0.272	0.000	0.000	0.000	0.000
50	A	28	ALA	0	0.090	-0.102	13.593	-0.056	-0.056	0.000	0.000	0.000	0.000
51	A	28	ALA	0	-0.073	0.116	14.365	0.006	0.006	0.000	0.000	0.000	0.000
52	A	29	LEU	0	0.049	-0.134	12.284	-0.055	-0.055	0.000	0.000	0.000	0.000
53	A	29	LEU	0	-0.093	0.109	14.368	0.007	0.007	0.000	0.000	0.000	0.000
54	A	30	GLN	0	0.085	-0.107	12.029	0.004	0.004	0.000	0.000	0.000	0.000
55	A	30	GLN	0	-0.043	0.134	12.938	0.029	0.029	0.000	0.000	0.000	0.000
56	A	31	GLN	0	0.067	-0.119	9.603	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	31	GLN	0	-0.039	0.113	9.308	0.075	0.075	0.000	0.000	0.000	0.000
58	A	32	LEU	0	0.096	-0.102	7.725	-0.205	-0.205	0.000	0.000	0.000	0.000
59	A	32	LEU	0	-0.074	0.128	8.668	0.015	0.015	0.000	0.000	0.000	0.000
60	A	33	ARG	0	0.102	-0.085	7.608	0.042	0.042	0.000	0.000	0.000	0.000
61	A	33	ARG	1	0.789	1.032	10.782	0.167	0.167	0.000	0.000	0.000	0.000
62	A	34	VAL	0	0.017	-0.139	7.636	0.102	0.102	0.000	0.000	0.000	0.000
63	A	34	VAL	0	-0.063	0.111	6.624	0.003	0.003	0.000	0.000	0.000	0.000
64	A	35	ASN	0	0.107	-0.062	3.750	-0.246	-0.067	0.002	-0.032	-0.149	0.000
65	A	35	ASN	0	-0.027	0.115	2.885	-2.587	-1.012	0.222	-1.079	-0.717	-0.007
66	A	36	TYR	0	0.092	-0.116	3.003	-1.044	0.114	0.190	-0.521	-0.827	-0.006
67	A	36	TYR	0	-0.078	0.109	6.925	0.066	0.066	0.000	0.000	0.000	0.000
68	A	37	GLY	0	-0.060	-0.113	5.551	0.312	0.312	0.000	0.000	0.000	0.000
69	A	38	SER	0	0.066	0.002	3.655	0.421	0.475	0.001	0.099	-0.153	0.000
70	A	38	SER	0	-0.006	0.100	2.330	-1.591	-0.435	0.865	-0.843	-1.179	-0.005
71	A	39	PHE	0	0.092	-0.096	1.923	-0.545	-1.344	4.799	-2.203	-1.797	0.005
72	A	39	PHE	0	-0.121	0.093	2.715	-0.016	1.223	1.489	-0.410	-2.319	0.000
73	A	40	VAL	0	0.072	-0.109	2.684	4.260	0.046	0.216	4.207	-0.209	0.000
74	A	40	VAL	0	-0.085	0.093	6.963	-0.042	-0.042	0.000	0.000	0.000	0.000
75	A	41	SER	0	-0.006	-0.105	6.079	0.085	0.085	0.000	0.000	0.000	0.000
76	A	41	SER	0	-0.028	0.088	6.614	-0.037	-0.037	0.000	0.000	0.000	0.000
77	A	42	GLU	0	0.115	-0.095	4.727	-0.070	-0.010	-0.001	-0.009	-0.049	0.000
78	A	42	GLU	-1	-0.961	-0.819	2.430	-4.958	-4.334	4.821	-2.133	-3.312	-0.031
79	A	43	TYR	0	0.101	-0.108	5.746	0.026	0.026	0.000	0.000	0.000	0.000
80	A	43	TYR	0	-0.101	0.103	6.408	0.027	0.027	0.000	0.000	0.000	0.000
81	A	44	ASN	0	0.085	-0.091	7.433	-0.077	-0.077	0.000	0.000	0.000	0.000
82	A	44	ASN	0	-0.127	0.060	9.982	0.068	0.068	0.000	0.000	0.000	0.000
83	A	45	ASP	0	0.120	-0.128	9.454	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	45	ASP	-1	-1.011	-0.823	9.318	0.008	0.008	0.000	0.000	0.000	0.000
85	A	46	LEU	0	0.057	-0.142	9.626	-0.101	-0.101	0.000	0.000	0.000	0.000
86	A	46	LEU	0	-0.071	0.135	9.260	0.026	0.026	0.000	0.000	0.000	0.000
87	A	47	THR	0	0.023	-0.120	11.174	-0.035	-0.035	0.000	0.000	0.000	0.000
88	A	47	THR	0	-0.040	0.086	11.477	0.000	0.000	0.000	0.000	0.000	0.000
89	A	48	LYS	0	0.046	-0.098	13.403	-0.026	-0.026	0.000	0.000	0.000	0.000
90	A	48	LYS	1	0.815	1.067	14.413	-0.189	-0.189	0.000	0.000	0.000	0.000
91	A	49	SER	0	0.007	-0.100	14.576	-0.028	-0.028	0.000	0.000	0.000	0.000
92	A	49	SER	0	-0.032	0.089	13.502	0.000	0.000	0.000	0.000	0.000	0.000
93	A	50	HIS	0	0.092	-0.072	15.384	-0.035	-0.035	0.000	0.000	0.000	0.000
94	A	50	HIS	0	-0.098	0.086	15.159	0.001	0.001	0.000	0.000	0.000	0.000
95	A	51	GLU	0	0.084	-0.117	16.927	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	51	GLU	-1	-0.952	-0.834	17.616	0.208	0.208	0.000	0.000	0.000	0.000
97	A	52	LYS	0	0.084	-0.097	19.043	-0.016	-0.016	0.000	0.000	0.000	0.000
98	A	52	LYS	1	0.842	1.060	19.466	-0.072	-0.072	0.000	0.000	0.000	0.000
99	A	53	LEU	0	0.050	-0.117	19.640	-0.021	-0.021	0.000	0.000	0.000	0.000
100	A	53	LEU	0	-0.086	0.105	17.737	0.001	0.001	0.000	0.000	0.000	0.000
101	A	54	ALA	0	0.100	-0.108	21.063	-0.016	-0.016	0.000	0.000	0.000	0.000
102	A	54	ALA	0	-0.065	0.119	21.529	0.003	0.003	0.000	0.000	0.000	0.000
103	A	55	ALA	0	0.106	-0.108	22.952	-0.007	-0.007	0.000	0.000	0.000	0.000
104	A	55	ALA	0	-0.097	0.109	24.496	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	56	GLU	0	0.064	-0.128	24.437	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	56	GLU	-1	-0.997	-0.845	23.396	0.083	0.083	0.000	0.000	0.000	0.000
107	A	57	LYS	0	0.081	-0.077	25.176	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	57	LYS	1	0.850	1.059	25.093	-0.138	-0.138	0.000	0.000	0.000	0.000
109	A	58	ASP	0	0.092	-0.143	26.789	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	58	ASP	-1	-1.001	-0.830	28.176	0.117	0.117	0.000	0.000	0.000	0.000
111	A	59	ASP	0	0.047	-0.145	29.004	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	59	ASP	-1	-1.000	-0.828	29.669	0.062	0.062	0.000	0.000	0.000	0.000
113	A	60	LEU	0	0.105	-0.121	29.746	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	60	LEU	0	-0.089	0.125	27.587	0.000	0.000	0.000	0.000	0.000	0.000
115	A	61	ILE	0	0.059	-0.104	31.139	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	61	ILE	0	-0.082	0.108	29.786	0.000	0.000	0.000	0.000	0.000	0.000
117	A	62	VAL	0	0.027	-0.124	32.883	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	62	VAL	0	-0.059	0.101	33.931	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	63	SER	0	0.017	-0.104	34.510	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	63	SER	0	-0.006	0.107	34.420	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	64	ASN	0	0.099	-0.089	34.955	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	64	ASN	0	-0.082	0.091	33.712	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	65	SER	0	0.102	-0.074	36.543	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	65	SER	0	-0.075	0.083	37.506	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	66	LYS	0	-0.026	-0.119	38.619	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	66	LYS	1	0.872	1.059	39.037	-0.048	-0.048	0.000	0.000	0.000	0.000
127	A	67	LEU	0	0.085	-0.089	39.709	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	67	LEU	0	-0.063	0.133	37.887	0.000	0.000	0.000	0.000	0.000	0.000
129	A	68	PHE	0	0.118	-0.093	40.221	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	68	PHE	0	-0.079	0.091	36.708	0.001	0.001	0.000	0.000	0.000	0.000
131	A	69	ARG	0	0.144	-0.061	41.815	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	69	ARG	1	0.794	1.020	40.756	-0.048	-0.048	0.000	0.000	0.000	0.000
133	A	70	GLN	0	0.098	-0.093	44.128	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	70	GLN	0	-0.125	0.093	44.619	0.001	0.001	0.000	0.000	0.000	0.000
135	A	71	ILE	0	0.015	-0.141	44.689	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	71	ILE	0	-0.030	0.119	43.225	0.000	0.000	0.000	0.000	0.000	0.000
137	A	72	GLY	0	0.039	-0.077	46.023	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	73	LEU	0	-0.001	-0.041	47.772	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	73	LEU	0	-0.082	0.075	48.625	0.000	0.000	0.000	0.000	0.000	0.000
140	A	74	THR	0	0.120	-0.042	49.965	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	74	THR	0	-0.022	0.073	49.853	0.000	0.000	0.000	0.000	0.000	0.000
142	A	75	GLU	0	0.075	-0.099	50.456	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	75	GLU	-1	-1.003	-0.834	48.303	0.031	0.031	0.000	0.000	0.000	0.000
144	A	76	LYS	0	0.111	-0.081	51.934	0.000	0.000	0.000	0.000	0.000	0.000
145	A	76	LYS	1	0.752	1.020	52.003	-0.031	-0.031	0.000	0.000	0.000	0.000
146	A	77	GLN	0	-0.059	-0.145	53.788	0.000	0.000	0.000	0.000	0.000	0.000
147	A	77	GLN	0	-0.123	0.067	54.298	0.001	0.001	0.000	0.000	0.000	0.000
148	A	78	GLU	0	-0.107	-0.143	55.153	-0.002	-0.002	0.000	0.000	0.000	0.000
149	A	78	GLU	-1	-0.897	-0.923	54.811	0.021	0.021	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)