FMO DATABASE

FMODB ID: 9L472

Calculation Name: 1NO4-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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	OptHSide
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	-383716.524733
FMO2-HF: Nuclear repulsion	353096.099877
FMO2-HF: Total energy	-30620.424856
FMO2-MP2: Total energy	-30711.408298

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.
-13.033	-7.595	9.863	-3.375	-11.927	-0.058

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 : -0.012 / q_NPA : -0.021

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	-0.090	0.079	3.960	-0.204	0.272	0.000	-0.169	-0.308	0.000
4	A	4	LYS	0	0.164	-0.075	3.812	1.207	2.588	-0.008	-0.601	-0.772	0.003
5	A	4	LYS	1	0.688	0.994	6.584	-0.112	-0.112	0.000	0.000	0.000	0.000
6	A	5	PRO	0	-0.023	-0.137	6.181	-0.121	-0.121	0.000	0.000	0.000	0.000
7	A	6	GLU	0	0.115	-0.023	8.568	-0.043	-0.043	0.000	0.000	0.000	0.000
8	A	6	GLU	-1	-0.876	-0.781	11.130	0.118	0.118	0.000	0.000	0.000	0.000
9	A	7	GLU	0	0.063	-0.089	8.534	0.076	0.076	0.000	0.000	0.000	0.000
10	A	7	GLU	-1	-0.932	-0.820	6.501	-1.136	-1.136	0.000	0.000	0.000	0.000
11	A	8	HIS	0	0.116	-0.064	7.651	-0.144	-0.144	0.000	0.000	0.000	0.000
12	A	8	HIS	0	-0.113	0.070	6.611	0.049	0.049	0.000	0.000	0.000	0.000
13	A	9	GLU	0	0.083	-0.122	8.595	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	9	GLU	-1	-0.988	-0.847	12.192	0.252	0.252	0.000	0.000	0.000	0.000
15	A	10	ASP	0	0.084	-0.118	12.022	0.011	0.011	0.000	0.000	0.000	0.000
16	A	10	ASP	-1	-1.025	-0.844	12.378	-0.082	-0.082	0.000	0.000	0.000	0.000
17	A	11	ILE	0	0.058	-0.104	11.533	0.006	0.006	0.000	0.000	0.000	0.000
18	A	11	ILE	0	-0.111	0.078	8.927	-0.012	-0.012	0.000	0.000	0.000	0.000
19	A	12	LEU	0	0.044	-0.140	12.465	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	12	LEU	0	-0.069	0.113	11.632	0.011	0.011	0.000	0.000	0.000	0.000
21	A	13	ASN	0	0.083	-0.079	14.127	0.004	0.004	0.000	0.000	0.000	0.000
22	A	13	ASN	0	-0.124	0.073	16.654	0.010	0.010	0.000	0.000	0.000	0.000
23	A	14	LYS	0	0.119	-0.083	16.196	0.007	0.007	0.000	0.000	0.000	0.000
24	A	14	LYS	1	0.743	1.001	16.097	0.112	0.112	0.000	0.000	0.000	0.000
25	A	15	LEU	0	0.003	-0.133	16.605	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	15	LEU	0	-0.103	0.093	14.148	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	16	LEU	0	0.091	-0.087	17.995	0.003	0.003	0.000	0.000	0.000	0.000
28	A	16	LEU	0	-0.097	0.103	19.450	0.003	0.003	0.000	0.000	0.000	0.000
29	A	17	ASP	0	0.051	-0.136	20.462	0.008	0.008	0.000	0.000	0.000	0.000
30	A	17	ASP	-1	-0.945	-0.814	22.340	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	18	PRO	0	-0.028	-0.115	23.197	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	19	GLU	0	0.071	-0.014	25.302	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	19	GLU	-1	-0.993	-0.845	27.220	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	20	LEU	0	0.138	-0.099	22.357	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	20	LEU	0	-0.156	0.100	19.213	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	21	ALA	0	0.112	-0.097	23.807	0.005	0.005	0.000	0.000	0.000	0.000
37	A	21	ALA	0	-0.083	0.106	24.038	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	22	GLN	0	0.110	-0.082	22.604	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	22	GLN	0	-0.039	0.117	21.938	0.008	0.008	0.000	0.000	0.000	0.000
40	A	23	SER	0	0.042	-0.090	21.520	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	23	SER	0	0.002	0.087	21.936	0.005	0.005	0.000	0.000	0.000	0.000
42	A	24	GLU	0	0.041	-0.089	19.200	-0.020	-0.020	0.000	0.000	0.000	0.000
43	A	24	GLU	-1	-0.940	-0.821	19.913	-0.126	-0.126	0.000	0.000	0.000	0.000
44	A	25	ARG	0	0.200	-0.068	17.793	-0.019	-0.019	0.000	0.000	0.000	0.000
45	A	25	ARG	1	0.724	1.033	19.392	0.030	0.030	0.000	0.000	0.000	0.000
46	A	26	THR	0	-0.019	-0.121	17.317	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	26	THR	0	-0.108	0.023	18.173	0.006	0.006	0.000	0.000	0.000	0.000
48	A	27	GLU	0	0.121	-0.095	15.635	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	27	GLU	-1	-1.000	-0.838	14.539	-0.248	-0.248	0.000	0.000	0.000	0.000
50	A	28	ALA	0	0.115	-0.081	13.450	-0.055	-0.055	0.000	0.000	0.000	0.000
51	A	28	ALA	0	-0.081	0.103	14.353	0.007	0.007	0.000	0.000	0.000	0.000
52	A	29	LEU	0	0.079	-0.116	12.261	-0.033	-0.033	0.000	0.000	0.000	0.000
53	A	29	LEU	0	-0.099	0.091	14.862	0.006	0.006	0.000	0.000	0.000	0.000
54	A	30	GLN	0	0.068	-0.112	12.206	0.009	0.009	0.000	0.000	0.000	0.000
55	A	30	GLN	0	-0.033	0.144	12.382	0.030	0.030	0.000	0.000	0.000	0.000
56	A	31	GLN	0	0.042	-0.115	9.210	-0.038	-0.038	0.000	0.000	0.000	0.000
57	A	31	GLN	0	-0.024	0.107	9.095	0.055	0.055	0.000	0.000	0.000	0.000
58	A	32	LEU	0	0.085	-0.092	7.629	-0.198	-0.198	0.000	0.000	0.000	0.000
59	A	32	LEU	0	-0.076	0.117	8.617	0.019	0.019	0.000	0.000	0.000	0.000
60	A	33	ARG	0	0.116	-0.059	8.049	0.049	0.049	0.000	0.000	0.000	0.000
61	A	33	ARG	1	0.766	1.000	11.132	0.155	0.155	0.000	0.000	0.000	0.000
62	A	34	VAL	0	0.023	-0.135	7.514	0.054	0.054	0.000	0.000	0.000	0.000
63	A	34	VAL	0	-0.082	0.101	6.154	0.003	0.003	0.000	0.000	0.000	0.000
64	A	35	ASN	0	0.108	-0.064	3.596	-0.341	-0.126	0.004	-0.052	-0.167	0.000
65	A	35	ASN	0	-0.017	0.096	2.601	-4.044	-2.273	0.894	-1.309	-1.355	-0.017
66	A	36	TYR	0	0.105	-0.087	3.563	-0.838	-0.183	0.020	-0.254	-0.422	-0.002
67	A	36	TYR	0	-0.095	0.102	7.171	0.068	0.068	0.000	0.000	0.000	0.000
68	A	37	GLY	0	-0.048	-0.123	5.629	0.219	0.219	0.000	0.000	0.000	0.000
69	A	38	SER	0	0.079	0.005	3.661	0.449	0.376	0.009	0.228	-0.165	0.000
70	A	38	SER	0	-0.012	0.089	2.568	-0.464	0.543	0.459	-0.636	-0.830	0.000
71	A	39	PHE	0	0.053	-0.070	2.093	-1.454	-2.050	3.379	-0.940	-1.843	0.000
72	A	39	PHE	0	-0.106	0.087	2.261	1.365	1.550	2.168	-0.356	-1.997	-0.001
73	A	40	VAL	0	0.079	-0.102	2.644	3.804	0.187	0.281	3.649	-0.312	0.002
74	A	40	VAL	0	-0.107	0.086	6.909	-0.019	-0.019	0.000	0.000	0.000	0.000
75	A	41	SER	0	0.013	-0.112	6.035	0.161	0.161	0.000	0.000	0.000	0.000
76	A	41	SER	0	-0.038	0.074	6.634	0.009	0.009	0.000	0.000	0.000	0.000
77	A	42	GLU	0	0.133	-0.078	4.486	0.211	0.271	-0.001	-0.011	-0.048	0.000
78	A	42	GLU	-1	-0.925	-0.808	2.429	-11.656	-7.682	2.658	-2.924	-3.708	-0.043
79	A	43	TYR	0	0.103	-0.100	5.890	0.110	0.110	0.000	0.000	0.000	0.000
80	A	43	TYR	0	-0.113	0.094	6.761	0.059	0.059	0.000	0.000	0.000	0.000
81	A	44	ASN	0	0.065	-0.085	7.638	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	44	ASN	0	-0.115	0.057	10.212	0.069	0.069	0.000	0.000	0.000	0.000
83	A	45	ASP	0	0.111	-0.123	9.523	0.057	0.057	0.000	0.000	0.000	0.000
84	A	45	ASP	-1	-1.006	-0.827	9.222	-0.318	-0.318	0.000	0.000	0.000	0.000
85	A	46	LEU	0	0.074	-0.118	9.445	-0.048	-0.048	0.000	0.000	0.000	0.000
86	A	46	LEU	0	-0.074	0.120	8.884	0.026	0.026	0.000	0.000	0.000	0.000
87	A	47	THR	0	0.018	-0.112	10.859	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	47	THR	0	-0.070	0.065	11.522	0.018	0.018	0.000	0.000	0.000	0.000
89	A	48	LYS	0	0.074	-0.098	13.385	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	48	LYS	1	0.735	1.012	14.651	-0.111	-0.111	0.000	0.000	0.000	0.000
91	A	49	SER	0	0.012	-0.106	14.332	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	49	SER	0	-0.043	0.083	13.271	0.005	0.005	0.000	0.000	0.000	0.000
93	A	50	HIS	0	0.084	-0.080	15.085	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	50	HIS	0	-0.087	0.091	14.845	0.007	0.007	0.000	0.000	0.000	0.000
95	A	51	GLU	0	0.040	-0.130	16.583	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	51	GLU	-1	-0.836	-0.779	17.930	0.123	0.123	0.000	0.000	0.000	0.000
97	A	52	LYS	0	0.088	-0.071	18.797	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	52	LYS	1	0.723	0.979	19.265	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	53	LEU	0	0.054	-0.109	19.403	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	53	LEU	0	-0.086	0.099	17.410	0.001	0.001	0.000	0.000	0.000	0.000
101	A	54	ALA	0	0.120	-0.103	20.712	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	54	ALA	0	-0.073	0.115	21.189	0.004	0.004	0.000	0.000	0.000	0.000
103	A	55	ALA	0	0.078	-0.111	22.608	0.000	0.000	0.000	0.000	0.000	0.000
104	A	55	ALA	0	-0.091	0.104	24.181	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	56	GLU	0	0.085	-0.100	24.201	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	56	GLU	-1	-0.890	-0.783	22.894	0.016	0.016	0.000	0.000	0.000	0.000
107	A	57	LYS	0	0.087	-0.087	24.932	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	57	LYS	1	0.780	1.021	24.616	-0.097	-0.097	0.000	0.000	0.000	0.000
109	A	58	ASP	0	0.118	-0.115	26.542	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	58	ASP	-1	-0.965	-0.804	27.693	0.089	0.089	0.000	0.000	0.000	0.000
111	A	59	ASP	0	0.038	-0.160	28.724	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	59	ASP	-1	-0.983	-0.827	29.590	0.029	0.029	0.000	0.000	0.000	0.000
113	A	60	LEU	0	0.080	-0.117	29.548	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	60	LEU	0	-0.087	0.116	27.525	0.000	0.000	0.000	0.000	0.000	0.000
115	A	61	ILE	0	0.081	-0.094	30.886	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	61	ILE	0	-0.090	0.100	29.217	0.001	0.001	0.000	0.000	0.000	0.000
117	A	62	VAL	0	0.061	-0.114	32.615	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	62	VAL	0	-0.083	0.110	33.557	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	63	SER	0	0.012	-0.111	34.305	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	63	SER	0	-0.017	0.098	34.396	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	64	ASN	0	0.097	-0.086	34.801	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	64	ASN	0	-0.089	0.085	33.127	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	65	SER	0	0.127	-0.056	36.396	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	65	SER	0	-0.068	0.074	37.197	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	66	LYS	0	-0.031	-0.131	38.367	0.000	0.000	0.000	0.000	0.000	0.000
126	A	66	LYS	1	0.871	1.054	38.084	-0.027	-0.027	0.000	0.000	0.000	0.000
127	A	67	LEU	0	0.090	-0.064	39.574	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	67	LEU	0	-0.067	0.115	37.805	0.000	0.000	0.000	0.000	0.000	0.000
129	A	68	PHE	0	0.108	-0.085	40.077	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	68	PHE	0	-0.079	0.088	36.352	0.000	0.000	0.000	0.000	0.000	0.000
131	A	69	ARG	0	0.190	-0.049	41.670	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	69	ARG	1	0.780	1.019	40.400	-0.033	-0.033	0.000	0.000	0.000	0.000
133	A	70	GLN	0	0.080	-0.084	43.973	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	70	GLN	0	-0.127	0.078	44.368	0.001	0.001	0.000	0.000	0.000	0.000
135	A	71	ILE	0	0.003	-0.138	44.594	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	71	ILE	0	-0.067	0.117	43.298	0.000	0.000	0.000	0.000	0.000	0.000
137	A	72	GLY	0	0.061	-0.091	45.893	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	73	LEU	0	0.030	-0.012	47.616	0.000	0.000	0.000	0.000	0.000	0.000
139	A	73	LEU	0	-0.082	0.074	48.600	0.000	0.000	0.000	0.000	0.000	0.000
140	A	74	THR	0	0.072	-0.074	49.860	0.000	0.000	0.000	0.000	0.000	0.000
141	A	74	THR	0	-0.008	0.091	49.694	0.000	0.000	0.000	0.000	0.000	0.000
142	A	75	GLU	0	0.087	-0.106	50.373	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	75	GLU	-1	-0.982	-0.823	48.398	0.020	0.020	0.000	0.000	0.000	0.000
144	A	76	LYS	0	0.173	-0.056	51.853	0.000	0.000	0.000	0.000	0.000	0.000
145	A	76	LYS	1	0.685	0.980	52.078	-0.020	-0.020	0.000	0.000	0.000	0.000
146	A	77	GLN	0	-0.095	-0.156	53.629	0.000	0.000	0.000	0.000	0.000	0.000
147	A	77	GLN	0	-0.083	0.090	54.650	0.001	0.001	0.000	0.000	0.000	0.000
148	A	78	GLU	0	-0.092	-0.136	55.061	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	78	GLU	-1	-0.923	-0.942	54.740	0.012	0.012	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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