FMO DATABASE

FMODB ID: 8G41Y

Calculation Name: 1MYO-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1MYO

Chain ID: A

ChEMBL ID:

UniProt ID: P62775

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-916064.228665
FMO2-HF: Nuclear repulsion	870581.557638
FMO2-HF: Total energy	-45482.671026
FMO2-MP2: Total energy	-45614.025754

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.
-116.165	-112.674	11.296	-8.476	-6.31	-0.099

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 : 1 / q_Mulliken : 0.780 / q_NPA : 0.872

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	ASP	-1	-0.794	-0.891	1.818	-106.562	-103.241	11.297	-8.428	-6.189	-0.099
4	A	4	LYS	1	0.936	0.965	4.410	38.965	39.135	-0.001	-0.048	-0.121	0.000
5	A	5	GLU	-1	-0.809	-0.862	7.323	-30.617	-30.617	0.000	0.000	0.000	0.000
6	A	6	PHE	0	0.011	0.002	6.231	3.184	3.184	0.000	0.000	0.000	0.000
7	A	7	MET	0	-0.026	-0.020	8.181	4.072	4.072	0.000	0.000	0.000	0.000
8	A	8	TRP	0	-0.001	-0.007	10.029	2.775	2.775	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.067	0.039	12.070	1.996	1.996	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.094	-0.047	11.694	1.586	1.586	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.869	0.950	14.937	19.410	19.410	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.105	-0.084	16.282	1.472	1.472	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.072	0.029	18.112	0.726	0.726	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.781	-0.849	15.354	-18.230	-18.230	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.015	-0.041	15.746	-1.291	-1.291	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.890	-0.962	16.751	-16.031	-16.031	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.873	-0.941	12.210	-23.704	-23.704	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.044	-0.036	11.347	-1.514	-1.514	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.876	0.948	12.949	15.150	15.150	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.879	-0.927	13.099	-21.780	-21.780	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.064	-0.064	6.352	-3.279	-3.279	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.055	-0.032	10.935	-0.082	-0.082	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.023	-0.018	13.617	1.480	1.480	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.832	0.934	9.650	28.490	28.490	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.021	0.000	14.093	1.293	1.293	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.988	-0.975	15.295	-16.204	-16.204	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.816	-0.911	10.642	-27.063	-27.063	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.066	-0.022	11.868	-1.898	-1.898	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.039	-0.029	13.027	1.654	1.654	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.913	0.964	5.481	38.916	38.916	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.032	-0.025	10.317	0.255	0.255	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.011	0.002	6.853	-2.080	-2.080	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.859	-0.932	7.111	-25.224	-25.224	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.043	0.020	9.061	-1.610	-1.610	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.039	-0.017	11.173	0.983	0.983	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.891	0.954	12.899	20.026	20.026	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.907	0.950	12.142	14.523	14.523	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.025	-0.007	12.173	0.886	0.886	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.014	0.017	13.831	0.621	0.621	0.000	0.000	0.000	0.000
40	A	40	HIS	0	-0.055	-0.012	16.752	1.039	1.039	0.000	0.000	0.000	0.000
41	A	41	TYR	0	0.023	-0.005	12.422	0.908	0.908	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.049	0.042	16.675	0.551	0.551	0.000	0.000	0.000	0.000
43	A	43	ALA	0	-0.018	-0.018	18.567	0.737	0.737	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.879	-0.922	19.740	-14.005	-14.005	0.000	0.000	0.000	0.000
45	A	45	CYS	0	-0.024	-0.017	19.173	0.643	0.643	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.018	0.016	19.465	-0.335	-0.335	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.040	-0.025	20.296	0.793	0.793	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.059	-0.042	23.635	0.564	0.564	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.843	-0.904	22.936	-12.610	-12.610	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.067	-0.031	16.762	-0.236	-0.236	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.045	-0.025	19.306	-0.567	-0.567	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.880	-0.946	20.982	-11.855	-11.855	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.026	0.001	15.973	0.117	0.117	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.042	-0.017	15.677	-0.085	-0.085	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.008	-0.015	17.798	-0.075	-0.075	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.030	-0.017	20.963	0.776	0.776	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.902	0.973	17.865	17.083	17.083	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.085	0.047	19.023	0.497	0.497	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.010	-0.017	20.334	0.310	0.310	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.776	-0.897	17.755	-17.040	-17.040	0.000	0.000	0.000	0.000
61	A	61	ILE	0	0.003	0.000	19.908	0.171	0.171	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.003	0.000	23.193	0.070	0.070	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.033	0.024	20.047	0.137	0.137	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.059	-0.005	20.228	-0.267	-0.267	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.804	-0.884	21.016	-12.639	-12.639	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.908	0.945	19.548	15.223	15.223	0.000	0.000	0.000	0.000
67	A	67	HIS	0	-0.040	-0.044	16.539	0.933	0.933	0.000	0.000	0.000	0.000
68	A	68	HIS	0	-0.045	-0.004	21.733	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.056	0.033	22.601	0.346	0.346	0.000	0.000	0.000	0.000
70	A	70	THR	0	-0.009	-0.019	23.198	-0.633	-0.633	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.003	-0.016	20.913	0.292	0.292	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.035	0.018	23.044	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.017	0.004	26.460	0.248	0.248	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.061	-0.017	22.424	-0.025	-0.025	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.048	0.009	24.509	0.162	0.162	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.011	-0.003	26.378	0.407	0.407	0.000	0.000	0.000	0.000
77	A	77	TYR	0	-0.035	-0.023	26.873	0.264	0.264	0.000	0.000	0.000	0.000
78	A	78	GLU	0	-0.058	-0.037	23.433	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	79	GLY	0	-0.032	-0.013	28.412	0.121	0.121	0.000	0.000	0.000	0.000
80	A	80	HIS	0	0.028	0.017	25.138	0.451	0.451	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.004	-0.002	29.263	0.267	0.267	0.000	0.000	0.000	0.000
82	A	82	SER	0	0.001	-0.017	29.680	0.228	0.228	0.000	0.000	0.000	0.000
83	A	83	CYS	0	0.006	0.016	25.367	0.218	0.218	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.025	-0.001	27.815	-0.032	-0.032	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.927	0.974	29.703	9.111	9.111	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.007	0.023	27.103	0.220	0.220	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.001	-0.003	24.760	-0.109	-0.109	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.029	0.019	28.716	-0.080	-0.080	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.029	-0.005	31.858	0.311	0.311	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.870	0.936	24.610	12.593	12.593	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.013	0.013	30.289	-0.105	-0.105	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.044	-0.019	28.322	0.112	0.112	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.745	-0.884	29.302	-9.440	-9.440	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.833	0.906	31.408	8.843	8.843	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.008	-0.010	31.966	-0.045	-0.045	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.050	-0.011	28.701	-0.046	-0.046	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.835	0.897	25.301	12.233	12.233	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.028	0.040	28.009	-0.297	-0.297	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.050	-0.023	30.066	0.065	0.065	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.795	-0.895	32.285	-8.222	-8.222	0.000	0.000	0.000	0.000
101	A	101	GLY	0	-0.048	-0.044	34.675	-0.233	-0.233	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.011	-0.004	31.646	0.030	0.030	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.052	-0.045	32.391	0.147	0.147	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.066	0.023	32.881	-0.215	-0.215	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.043	-0.013	35.273	0.149	0.149	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.893	-0.954	36.429	-7.885	-7.885	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.062	-0.018	32.855	-0.117	-0.117	0.000	0.000	0.000	0.000
108	A	108	THR	0	0.002	-0.015	34.196	-0.057	-0.057	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.868	-0.953	36.495	-7.401	-7.401	0.000	0.000	0.000	0.000
110	A	110	ASN	0	0.003	0.015	34.712	0.144	0.144	0.000	0.000	0.000	0.000
111	A	111	GLN	0	0.046	0.003	38.291	-0.067	-0.067	0.000	0.000	0.000	0.000
112	A	112	ALA	0	-0.040	-0.017	35.622	-0.019	-0.019	0.000	0.000	0.000	0.000
113	A	113	ILE	0	0.008	0.026	32.281	-0.173	-0.173	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.855	0.948	35.162	7.952	7.952	0.000	0.000	0.000	0.000
115	A	115	ALA	0	-0.038	-0.024	36.868	0.093	0.093	0.000	0.000	0.000	0.000
116	A	116	LEU	0	-0.001	-0.004	31.214	-0.053	-0.053	0.000	0.000	0.000	0.000
117	A	117	LEU	0	-0.097	-0.042	35.891	-0.087	-0.087	0.000	0.000	0.000	0.000
118	A	118	GLN	-1	-0.961	-0.957	37.088	-7.925	-7.925	0.000	0.000	0.000	0.000

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