FMO DATABASE

FMODB ID: 5GK8Z

Calculation Name: 2A2P-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A2P

Chain ID: A

ChEMBL ID:

UniProt ID: Q8VHC3

Base Structure: SolutionNMR

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	128
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1068118.838996
FMO2-HF: Nuclear repulsion	1015118.498604
FMO2-HF: Total energy	-53000.340392
FMO2-MP2: Total energy	-53154.10024

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:24:MET)

Summations of interaction energy for fragment #1(A:24: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.
-50.79	-46.173	1.615	-2.4	-3.831	-0.02

Interaction energy analysis for fragmet #1(A:24:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.842 / q_NPA : 0.903

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	26	ASN	0	-0.017	-0.021	2.610	-2.867	1.598	1.616	-2.385	-3.695	-0.020
4	A	27	TYR	0	0.070	0.042	4.825	4.310	4.462	-0.001	-0.015	-0.136	0.000
5	A	28	ARG	1	0.881	0.924	8.419	27.843	27.843	0.000	0.000	0.000	0.000
6	A	29	PRO	0	0.035	0.033	11.602	0.407	0.407	0.000	0.000	0.000	0.000
7	A	30	ASP	-1	-0.866	-0.922	15.274	-17.413	-17.413	0.000	0.000	0.000	0.000
8	A	31	TRP	0	0.018	-0.015	15.018	1.448	1.448	0.000	0.000	0.000	0.000
9	A	32	ASN	0	-0.074	-0.040	19.646	0.855	0.855	0.000	0.000	0.000	0.000
10	A	33	ARG	1	0.986	0.986	20.633	15.575	15.575	0.000	0.000	0.000	0.000
11	A	34	LEU	0	0.013	0.019	19.120	0.447	0.447	0.000	0.000	0.000	0.000
12	A	35	ARG	1	0.921	0.961	23.182	11.582	11.582	0.000	0.000	0.000	0.000
13	A	36	GLY	0	0.060	0.027	25.751	0.330	0.330	0.000	0.000	0.000	0.000
14	A	37	LEU	0	-0.065	-0.020	22.106	0.333	0.333	0.000	0.000	0.000	0.000
15	A	38	ALA	0	-0.038	-0.023	26.220	-0.014	-0.014	0.000	0.000	0.000	0.000
16	A	39	ARG	1	0.883	0.960	27.762	10.608	10.608	0.000	0.000	0.000	0.000
17	A	40	GLY	0	0.051	0.032	25.629	-0.316	-0.316	0.000	0.000	0.000	0.000
18	A	41	ARG	1	0.810	0.891	26.556	10.784	10.784	0.000	0.000	0.000	0.000
19	A	42	VAL	0	0.041	0.028	23.531	-0.356	-0.356	0.000	0.000	0.000	0.000
20	A	43	GLU	-1	-0.842	-0.904	26.104	-10.026	-10.026	0.000	0.000	0.000	0.000
21	A	44	THR	0	0.083	0.027	26.494	-0.669	-0.669	0.000	0.000	0.000	0.000
22	A	45	CYS	0	-0.106	-0.015	28.430	0.665	0.665	0.000	0.000	0.000	0.000
23	A	46	GLY	0	0.032	0.010	31.008	-0.171	-0.171	0.000	0.000	0.000	0.000
24	A	47	GLY	0	-0.028	-0.002	33.344	0.141	0.141	0.000	0.000	0.000	0.000
25	A	49	GLN	0	0.013	-0.004	29.860	0.151	0.151	0.000	0.000	0.000	0.000
26	A	50	LEU	0	0.029	0.018	23.892	-0.104	-0.104	0.000	0.000	0.000	0.000
27	A	51	ASN	0	0.019	0.005	24.757	-0.516	-0.516	0.000	0.000	0.000	0.000
28	A	52	ARG	1	0.960	0.972	23.621	12.401	12.401	0.000	0.000	0.000	0.000
29	A	53	LEU	0	0.019	0.036	19.856	-0.331	-0.331	0.000	0.000	0.000	0.000
30	A	54	LYS	1	0.893	0.943	21.079	12.882	12.882	0.000	0.000	0.000	0.000
31	A	55	GLU	-1	-0.837	-0.929	16.192	-16.451	-16.451	0.000	0.000	0.000	0.000
32	A	56	VAL	0	0.045	0.027	18.235	0.435	0.435	0.000	0.000	0.000	0.000
33	A	57	LYS	1	0.930	0.954	20.185	12.270	12.270	0.000	0.000	0.000	0.000
34	A	58	ALA	0	-0.016	0.005	21.205	0.486	0.486	0.000	0.000	0.000	0.000
35	A	59	PHE	0	0.062	0.035	19.709	0.365	0.365	0.000	0.000	0.000	0.000
36	A	60	VAL	0	-0.033	-0.022	21.815	0.548	0.548	0.000	0.000	0.000	0.000
37	A	61	THR	0	-0.082	-0.054	24.944	0.654	0.654	0.000	0.000	0.000	0.000
38	A	62	GLU	-1	-0.957	-0.971	24.490	-12.176	-12.176	0.000	0.000	0.000	0.000
39	A	63	ASP	-1	-0.798	-0.906	21.456	-14.464	-14.464	0.000	0.000	0.000	0.000
40	A	64	ILE	0	0.007	0.009	24.761	0.222	0.222	0.000	0.000	0.000	0.000
41	A	65	GLN	0	-0.029	-0.011	26.059	0.651	0.651	0.000	0.000	0.000	0.000
42	A	66	LEU	0	-0.075	-0.027	25.956	0.312	0.312	0.000	0.000	0.000	0.000
43	A	67	TYR	0	-0.019	-0.024	18.979	-0.029	-0.029	0.000	0.000	0.000	0.000
44	A	68	HIS	0	0.036	0.010	25.661	0.153	0.153	0.000	0.000	0.000	0.000
45	A	69	ASN	0	-0.019	-0.017	25.931	-0.585	-0.585	0.000	0.000	0.000	0.000
46	A	70	LEU	0	-0.009	0.020	23.268	0.004	0.004	0.000	0.000	0.000	0.000
47	A	71	VAL	0	0.005	0.002	27.281	0.259	0.259	0.000	0.000	0.000	0.000
48	A	72	MET	0	0.023	0.017	28.573	-0.269	-0.269	0.000	0.000	0.000	0.000
49	A	73	LYS	1	0.888	0.947	29.563	9.916	9.916	0.000	0.000	0.000	0.000
50	A	74	HIS	0	0.057	0.027	30.772	-0.339	-0.339	0.000	0.000	0.000	0.000
51	A	75	LEU	0	-0.023	-0.017	30.635	0.366	0.366	0.000	0.000	0.000	0.000
52	A	76	PRO	0	0.006	-0.015	33.851	-0.051	-0.051	0.000	0.000	0.000	0.000
53	A	77	GLY	0	0.036	-0.006	33.118	0.083	0.083	0.000	0.000	0.000	0.000
54	A	78	ALA	0	-0.031	0.001	29.514	0.070	0.070	0.000	0.000	0.000	0.000
55	A	79	ASP	-1	-0.874	-0.936	24.481	-12.141	-12.141	0.000	0.000	0.000	0.000
56	A	80	PRO	0	-0.058	-0.030	22.306	0.142	0.142	0.000	0.000	0.000	0.000
57	A	81	GLU	-1	-0.817	-0.902	22.161	-13.995	-13.995	0.000	0.000	0.000	0.000
58	A	82	LEU	0	-0.020	-0.005	20.024	0.655	0.655	0.000	0.000	0.000	0.000
59	A	83	VAL	0	0.006	-0.001	22.943	-0.206	-0.206	0.000	0.000	0.000	0.000
60	A	84	LEU	0	0.024	0.010	20.312	0.247	0.247	0.000	0.000	0.000	0.000
61	A	85	LEU	0	-0.015	-0.017	25.027	0.321	0.321	0.000	0.000	0.000	0.000
62	A	86	SER	0	0.037	0.025	28.466	-0.168	-0.168	0.000	0.000	0.000	0.000
63	A	87	ARG	1	0.976	0.970	30.376	9.595	9.595	0.000	0.000	0.000	0.000
64	A	88	ASN	0	0.001	0.013	32.647	-0.026	-0.026	0.000	0.000	0.000	0.000
65	A	89	TYR	0	-0.043	-0.049	32.963	0.063	0.063	0.000	0.000	0.000	0.000
66	A	90	GLN	0	0.025	0.023	32.814	-0.026	-0.026	0.000	0.000	0.000	0.000
67	A	91	GLU	-1	-0.955	-0.979	29.272	-10.732	-10.732	0.000	0.000	0.000	0.000
68	A	92	LEU	0	-0.062	-0.021	26.084	0.227	0.227	0.000	0.000	0.000	0.000
69	A	93	GLU	-1	-0.864	-0.931	21.436	-14.339	-14.339	0.000	0.000	0.000	0.000
70	A	94	ARG	1	0.762	0.854	23.614	12.135	12.135	0.000	0.000	0.000	0.000
71	A	95	ILE	0	0.031	0.024	16.977	-0.427	-0.427	0.000	0.000	0.000	0.000
72	A	96	PRO	0	0.025	0.011	18.606	0.242	0.242	0.000	0.000	0.000	0.000
73	A	97	LEU	0	-0.014	-0.009	17.651	-0.983	-0.983	0.000	0.000	0.000	0.000
74	A	98	SER	0	-0.033	-0.037	17.576	-0.403	-0.403	0.000	0.000	0.000	0.000
75	A	99	GLN	0	-0.016	-0.004	15.025	0.634	0.634	0.000	0.000	0.000	0.000
76	A	100	MET	0	-0.002	0.018	10.152	-1.926	-1.926	0.000	0.000	0.000	0.000
77	A	101	THR	0	0.043	0.016	11.437	2.022	2.022	0.000	0.000	0.000	0.000
78	A	102	ARG	1	0.957	0.967	14.155	15.617	15.617	0.000	0.000	0.000	0.000
79	A	103	ASP	-1	-0.969	-0.967	11.595	-24.278	-24.278	0.000	0.000	0.000	0.000
80	A	104	GLU	-1	-0.837	-0.935	7.718	-37.607	-37.607	0.000	0.000	0.000	0.000
81	A	105	ILE	0	-0.047	-0.013	11.751	0.407	0.407	0.000	0.000	0.000	0.000
82	A	106	ASN	0	-0.035	-0.051	15.341	0.483	0.483	0.000	0.000	0.000	0.000
83	A	107	ALA	0	0.009	0.018	11.467	0.717	0.717	0.000	0.000	0.000	0.000
84	A	108	LEU	0	0.014	0.011	13.563	0.393	0.393	0.000	0.000	0.000	0.000
85	A	109	VAL	0	0.000	-0.017	14.799	0.916	0.916	0.000	0.000	0.000	0.000
86	A	110	GLN	0	-0.035	-0.022	15.778	1.398	1.398	0.000	0.000	0.000	0.000
87	A	111	GLU	-1	-0.877	-0.923	11.721	-23.874	-23.874	0.000	0.000	0.000	0.000
88	A	112	LEU	0	-0.093	-0.044	15.624	0.758	0.758	0.000	0.000	0.000	0.000
89	A	113	GLY	0	-0.002	0.016	19.006	0.756	0.756	0.000	0.000	0.000	0.000
90	A	114	PHE	0	-0.042	-0.031	20.979	0.822	0.822	0.000	0.000	0.000	0.000
91	A	115	TYR	0	0.021	0.015	22.181	-0.416	-0.416	0.000	0.000	0.000	0.000
92	A	116	ARG	1	0.936	0.972	20.557	14.608	14.608	0.000	0.000	0.000	0.000
93	A	117	LYS	1	0.853	0.946	24.872	10.055	10.055	0.000	0.000	0.000	0.000
94	A	118	SER	0	0.008	-0.017	27.353	-0.269	-0.269	0.000	0.000	0.000	0.000
95	A	119	ALA	0	0.031	0.017	29.150	0.103	0.103	0.000	0.000	0.000	0.000
96	A	120	PRO	0	0.051	0.021	31.935	-0.043	-0.043	0.000	0.000	0.000	0.000
97	A	121	GLU	-1	-0.940	-0.964	33.111	-8.286	-8.286	0.000	0.000	0.000	0.000
98	A	122	ALA	0	-0.054	-0.004	32.318	0.156	0.156	0.000	0.000	0.000	0.000
99	A	123	GLN	0	0.024	-0.003	33.772	0.043	0.043	0.000	0.000	0.000	0.000
100	A	124	VAL	0	-0.017	-0.022	29.526	-0.345	-0.345	0.000	0.000	0.000	0.000
101	A	125	PRO	0	0.019	0.034	29.474	0.358	0.358	0.000	0.000	0.000	0.000
102	A	126	PRO	0	0.040	-0.016	31.731	-0.195	-0.195	0.000	0.000	0.000	0.000
103	A	127	GLU	-1	-0.944	-0.964	28.382	-10.862	-10.862	0.000	0.000	0.000	0.000
104	A	128	TYR	0	0.017	-0.011	23.415	-0.442	-0.442	0.000	0.000	0.000	0.000
105	A	129	LEU	0	-0.035	-0.001	28.914	-0.072	-0.072	0.000	0.000	0.000	0.000
106	A	130	TRP	0	-0.007	-0.009	31.407	0.202	0.202	0.000	0.000	0.000	0.000
107	A	131	ALA	0	-0.010	0.028	26.027	-0.138	-0.138	0.000	0.000	0.000	0.000
108	A	132	PRO	0	-0.039	-0.026	23.828	0.204	0.204	0.000	0.000	0.000	0.000
109	A	133	ALA	0	-0.026	-0.016	25.874	-0.166	-0.166	0.000	0.000	0.000	0.000
110	A	134	LYS	1	0.934	0.963	24.070	12.105	12.105	0.000	0.000	0.000	0.000
111	A	135	PRO	0	0.024	0.001	30.170	0.146	0.146	0.000	0.000	0.000	0.000
112	A	136	PRO	0	-0.021	-0.011	33.622	-0.081	-0.081	0.000	0.000	0.000	0.000
113	A	137	GLU	-1	-0.859	-0.924	34.807	-8.965	-8.965	0.000	0.000	0.000	0.000
114	A	138	GLU	-1	-0.921	-0.960	37.520	-7.237	-7.237	0.000	0.000	0.000	0.000
115	A	139	ALA	0	-0.101	-0.054	37.886	0.109	0.109	0.000	0.000	0.000	0.000
116	A	140	SER	0	-0.069	-0.036	36.151	-0.060	-0.060	0.000	0.000	0.000	0.000
117	A	141	GLU	-1	-0.954	-0.959	38.333	-7.630	-7.630	0.000	0.000	0.000	0.000
118	A	142	HIS	1	0.849	0.909	40.389	7.585	7.585	0.000	0.000	0.000	0.000
119	A	143	ASP	-1	-0.874	-0.921	43.905	-7.167	-7.167	0.000	0.000	0.000	0.000
120	A	144	ASP	-1	-0.895	-0.946	46.567	-6.261	-6.261	0.000	0.000	0.000	0.000
121	A	145	LEU	0	-0.051	-0.034	45.988	0.080	0.080	0.000	0.000	0.000	0.000
122	A	146	GLU	-1	-0.873	-0.925	49.441	-5.784	-5.784	0.000	0.000	0.000	0.000
123	A	147	HIS	0	-0.053	-0.037	52.927	0.070	0.070	0.000	0.000	0.000	0.000
124	A	148	HIS	0	-0.015	0.011	47.721	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	149	HIS	0	-0.016	0.000	51.598	0.124	0.124	0.000	0.000	0.000	0.000
126	A	150	HIS	0	-0.046	-0.041	54.324	-0.065	-0.065	0.000	0.000	0.000	0.000
127	A	151	HIS	0	-0.076	-0.041	53.501	0.079	0.079	0.000	0.000	0.000	0.000
128	A	152	HIS	0	-0.002	0.005	55.400	-0.158	-0.158	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:MET)