FMO DATABASE

FMODB ID: 98922

Calculation Name: 3S0A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3S0A

Chain ID: A

ChEMBL ID:

UniProt ID: Q1W640

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

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	117
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1027027.445404
FMO2-HF: Nuclear repulsion	978260.409782
FMO2-HF: Total energy	-48767.035622
FMO2-MP2: Total energy	-48904.72048

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: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.
-12.39	-4.687	7.942	-4.242	-11.403	-0.027

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 : -0.046 / q_NPA : -0.023

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

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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	ILE	0	0.048	0.014	3.228	-2.254	-0.006	0.046	-1.019	-1.275	0.001
4	A	4	GLU	-1	-0.828	-0.901	5.926	0.699	0.699	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.872	-0.940	2.230	-6.729	-4.100	3.237	-2.396	-3.470	-0.023
6	A	6	LEU	0	0.015	0.000	2.988	0.183	2.228	3.151	-1.744	-3.451	-0.003
7	A	7	LYS	1	0.789	0.882	3.741	0.403	-1.061	0.083	1.747	-0.367	-0.001
8	A	8	THR	0	0.027	0.019	6.830	-0.092	-0.092	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.812	0.894	3.331	-1.679	-0.903	0.051	-0.174	-0.653	0.001
10	A	10	LEU	0	-0.026	-0.027	6.362	-0.611	-0.611	0.000	0.000	0.000	0.000
11	A	11	HIS	0	-0.006	0.008	7.995	-0.230	-0.230	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.032	-0.012	9.101	-0.185	-0.185	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.787	-0.897	7.506	0.207	0.207	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.001	-0.016	10.415	-0.122	-0.122	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.030	-0.005	13.045	-0.078	-0.078	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.018	-0.001	12.657	-0.045	-0.045	0.000	0.000	0.000	0.000
17	A	17	CYS	0	0.025	0.036	13.572	-0.037	-0.037	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.927	0.977	15.696	-0.149	-0.149	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.084	-0.042	18.311	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.959	-0.968	17.309	0.068	0.068	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.059	-0.036	18.796	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.017	-0.015	21.438	-0.011	-0.011	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.077	-0.027	19.555	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.882	-0.933	22.893	0.074	0.074	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.026	-0.050	19.164	0.000	0.000	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.036	-0.008	22.019	0.008	0.008	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.931	0.954	23.090	-0.058	-0.058	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.002	0.000	18.082	0.005	0.005	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.046	0.014	18.255	0.039	0.039	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.835	-0.901	19.623	0.095	0.095	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.027	-0.031	15.839	0.001	0.001	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.057	-0.024	14.346	0.012	0.012	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.901	-0.958	15.891	0.133	0.133	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.017	-0.008	17.942	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.056	-0.018	18.699	-0.024	-0.024	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.023	-0.003	17.863	0.004	0.004	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.861	-0.928	21.693	0.040	0.040	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.029	-0.029	22.309	0.002	0.002	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.851	-0.926	24.223	0.024	0.024	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.799	-0.862	25.083	0.059	0.059	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.993	0.984	24.541	-0.033	-0.033	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.913	0.941	23.317	-0.059	-0.059	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.061	0.050	20.449	0.012	0.012	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.057	-0.041	19.697	0.008	0.008	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.069	-0.034	19.426	0.001	0.001	0.000	0.000	0.000	0.000
46	A	46	TYR	0	0.015	0.011	15.351	0.011	0.011	0.000	0.000	0.000	0.000
47	A	47	CYS	0	-0.024	-0.005	15.352	0.023	0.023	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.844	-0.936	14.569	0.041	0.041	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.049	0.022	9.693	0.007	0.007	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.032	-0.022	9.951	0.004	0.004	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.842	0.922	10.883	-0.056	-0.056	0.000	0.000	0.000	0.000
52	A	53	ASN	0	0.000	0.017	9.664	-0.081	-0.081	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.047	-0.024	3.082	-0.355	0.009	0.026	-0.061	-0.329	0.000
54	A	55	ASN	0	-0.085	-0.039	7.414	-0.077	-0.077	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.023	-0.005	8.080	-0.034	-0.034	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.032	0.000	11.353	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.834	-0.923	13.952	-0.056	-0.056	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.990	0.968	16.090	0.050	0.050	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.056	-0.026	18.331	0.014	0.014	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.037	-0.031	18.421	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.024	0.024	18.891	0.000	0.000	0.000	0.000	0.000	0.000
62	A	63	PHE	0	0.027	0.017	14.392	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.907	0.959	13.045	0.112	0.112	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.067	0.022	12.956	-0.017	-0.017	0.000	0.000	0.000	0.000
65	A	66	GLN	0	0.000	-0.006	10.689	0.056	0.056	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.029	0.013	8.773	-0.082	-0.082	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.028	0.009	7.886	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.936	0.969	9.350	0.256	0.256	0.000	0.000	0.000	0.000
69	A	70	ALA	0	-0.010	0.005	5.703	-0.038	-0.038	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.028	0.020	3.730	-0.520	-0.291	0.001	-0.029	-0.201	0.000
71	A	72	MET	0	-0.008	-0.017	5.899	0.114	0.114	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.922	-0.964	8.568	-0.503	-0.503	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.050	-0.014	2.329	-1.005	-0.129	1.347	-0.566	-1.657	-0.002
74	A	75	LEU	0	-0.079	-0.043	6.537	0.092	0.092	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.045	-0.018	9.666	0.054	0.054	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.794	-0.866	11.986	-0.208	-0.208	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.854	-0.935	13.697	-0.208	-0.208	0.000	0.000	0.000	0.000
78	A	79	ASN	0	-0.035	-0.034	14.508	0.010	0.010	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.008	-0.035	16.170	0.024	0.024	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.005	0.019	11.596	0.031	0.031	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.901	0.949	14.906	0.176	0.176	0.000	0.000	0.000	0.000
82	A	83	GLN	0	-0.024	-0.012	17.811	0.021	0.021	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.059	0.045	13.618	0.012	0.012	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.044	-0.030	14.758	0.010	0.010	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.057	-0.043	17.235	0.010	0.010	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.835	-0.866	20.083	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.078	-0.032	17.279	0.008	0.008	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.047	-0.034	18.408	0.006	0.006	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.042	-0.031	19.418	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	ILE	0	0.028	0.029	19.955	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.017	-0.020	23.585	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.834	-0.926	24.506	0.013	0.013	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.874	-0.938	25.586	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	95	ASN	0	-0.024	0.010	26.197	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.036	0.004	22.388	0.003	0.003	0.000	0.000	0.000	0.000
96	A	97	HIS	1	0.869	0.926	21.473	-0.028	-0.028	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.058	0.042	21.893	0.007	0.007	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.938	0.976	20.224	0.018	0.018	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.009	0.003	17.604	0.001	0.001	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.021	-0.015	17.689	0.010	0.010	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.903	0.950	19.511	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.017	-0.005	15.936	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.025	0.014	13.767	0.003	0.003	0.000	0.000	0.000	0.000
104	A	105	GLN	0	0.012	0.003	15.881	0.006	0.006	0.000	0.000	0.000	0.000
105	A	107	VAL	0	0.048	0.008	11.863	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.038	-0.030	15.144	0.016	0.016	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.795	0.900	16.153	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.083	-0.054	15.241	-0.017	-0.017	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.933	0.955	12.234	-0.065	-0.065	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.048	0.050	13.685	0.036	0.036	0.000	0.000	0.000	0.000
111	A	113	MET	0	0.041	0.032	10.465	0.051	0.051	0.000	0.000	0.000	0.000
112	A	114	LYS	1	0.913	0.957	12.141	-0.082	-0.082	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.093	-0.060	13.981	-0.022	-0.022	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.018	0.000	7.702	-0.059	-0.059	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.797	-0.906	11.038	0.344	0.344	0.000	0.000	0.000	0.000
116	A	118	PHE	0	-0.117	-0.046	12.653	-0.048	-0.048	0.000	0.000	0.000	0.000
117	A	119	LEU	0	-0.025	0.013	10.689	-0.039	-0.039	0.000	0.000	0.000	0.000

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