FMO DATABASE

FMODB ID: Z79ZN

Calculation Name: 1EO1-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EO1

Chain ID: A

ChEMBL ID:

UniProt ID: O27243

Base Structure: SolutionNMR

Registration Date: 2025-09-02

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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-908331.846119
FMO2-HF: Nuclear repulsion	862218.175651
FMO2-HF: Total energy	-46113.670468
FMO2-MP2: Total energy	-46248.100387

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.
-16.098	-11.01	4.25	-2.698	-6.639	-0.009

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 : 0.810 / q_NPA : 0.887

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	0.032	0.015	3.844	0.171	2.135	-0.011	-0.803	-1.150	-0.003
31	A	31	MET	0	-0.013	0.005	4.366	2.575	2.802	-0.001	-0.019	-0.206	0.000
32	A	32	LYS	1	0.901	0.952	3.495	30.664	31.129	0.002	-0.347	-0.120	-0.003
67	A	67	LYS	1	0.894	0.942	2.632	42.591	43.999	0.427	-0.484	-1.351	-0.003
68	A	68	ALA	0	-0.008	-0.008	4.090	1.649	2.078	0.003	-0.059	-0.373	0.000
88	A	88	LYS	1	0.767	0.881	2.586	36.813	37.016	2.183	-0.486	-1.900	0.003
104	A	104	PHE	0	-0.041	-0.018	2.894	-3.282	-2.890	1.647	-0.500	-1.539	-0.003
4	A	4	ALA	0	0.017	0.013	5.567	2.108	2.108	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.007	-0.004	9.127	0.089	0.089	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.002	-0.006	12.054	0.895	0.895	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.019	-0.024	15.148	0.435	0.435	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.024	-0.007	15.868	-0.430	-0.430	0.000	0.000	0.000	0.000
9	A	9	GLY	0	-0.009	-0.002	18.082	0.311	0.311	0.000	0.000	0.000	0.000
10	A	10	THR	0	-0.012	-0.020	19.572	-0.473	-0.473	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.888	-0.945	20.810	-13.403	-13.403	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.013	0.010	20.067	-0.644	-0.644	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.010	0.006	21.998	0.323	0.323	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.028	-0.012	21.555	0.366	0.366	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.876	-0.945	20.253	-13.753	-13.753	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.002	0.007	16.795	0.102	0.102	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.046	-0.034	18.859	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.928	0.946	21.584	11.325	11.325	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.025	0.022	21.065	-0.222	-0.222	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.028	-0.007	16.178	-0.053	-0.053	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.031	-0.015	19.569	0.272	0.272	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.910	0.932	21.954	10.907	10.907	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.017	0.019	19.022	0.264	0.264	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.025	-0.018	19.998	-0.598	-0.598	0.000	0.000	0.000	0.000
25	A	25	TYR	0	0.051	0.035	19.394	0.470	0.470	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.009	-0.005	12.193	-0.034	-0.034	0.000	0.000	0.000	0.000
27	A	27	MET	0	0.023	0.035	13.425	-0.608	-0.608	0.000	0.000	0.000	0.000
28	A	28	ILE	0	-0.045	-0.028	9.435	-1.885	-1.885	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.054	0.024	7.976	1.231	1.231	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.915	-0.966	5.873	-46.209	-46.209	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.918	0.939	5.415	27.156	27.156	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.045	0.031	7.043	3.598	3.598	0.000	0.000	0.000	0.000
35	A	35	ASN	0	0.043	0.029	8.659	2.254	2.254	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.028	-0.024	8.365	-4.474	-4.474	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.931	-0.966	8.652	-24.022	-24.022	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.045	-0.015	9.700	1.228	1.228	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.016	-0.014	10.438	-2.565	-2.565	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.901	-0.940	13.000	-21.483	-21.483	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.004	-0.015	14.359	-0.736	-0.736	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.003	0.014	14.720	0.425	0.425	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.814	-0.909	17.983	-14.403	-14.403	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.106	-0.045	20.135	-0.615	-0.615	0.000	0.000	0.000	0.000
45	A	45	PRO	0	0.011	0.012	22.048	0.509	0.509	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.036	-0.004	24.950	0.534	0.534	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.016	-0.003	24.708	0.027	0.027	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.052	-0.042	26.617	0.028	0.028	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.044	0.028	30.310	0.307	0.307	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.009	0.017	27.905	0.319	0.319	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.022	0.018	30.294	0.004	0.004	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.019	-0.011	28.796	-0.231	-0.231	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.020	0.005	25.371	-0.421	-0.421	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.008	-0.006	23.079	0.173	0.173	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.050	0.019	19.637	-0.606	-0.606	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.916	0.960	19.255	12.304	12.304	0.000	0.000	0.000	0.000
57	A	57	THR	0	0.031	0.024	17.042	-0.673	-0.673	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.028	0.017	14.960	-0.988	-0.988	0.000	0.000	0.000	0.000
59	A	59	GLN	0	0.004	0.002	14.338	-0.741	-0.741	0.000	0.000	0.000	0.000
60	A	60	ILE	0	0.009	0.001	15.147	-0.539	-0.539	0.000	0.000	0.000	0.000
61	A	61	ILE	0	0.016	0.011	10.779	-1.271	-1.271	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.002	-0.012	10.408	-2.440	-2.440	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.031	-0.006	10.456	-1.471	-1.471	0.000	0.000	0.000	0.000
64	A	64	ASN	0	0.007	0.012	10.596	0.438	0.438	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.020	-0.008	7.344	-3.037	-3.037	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.033	-0.018	5.308	-8.446	-8.446	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.017	0.008	5.500	-0.048	-0.048	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.001	0.012	8.172	1.590	1.590	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.006	-0.008	11.060	0.889	0.889	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.036	-0.001	14.652	-0.185	-0.185	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.004	0.013	18.193	0.378	0.378	0.000	0.000	0.000	0.000
74	A	74	PRO	0	-0.037	-0.007	20.225	0.075	0.075	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.031	0.016	22.876	0.476	0.476	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.012	-0.006	20.930	-0.577	-0.577	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.029	0.019	20.504	-0.362	-0.362	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.026	0.009	16.910	-0.277	-0.277	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.009	-0.012	15.150	-0.665	-0.665	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.911	-0.941	17.054	-13.133	-13.133	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.025	0.006	17.259	-0.429	-0.429	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.009	-0.020	11.666	-0.610	-0.610	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.022	-0.019	13.114	-1.906	-1.906	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.937	-0.958	14.485	-15.350	-15.350	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.058	-0.026	12.967	-0.058	-0.058	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.018	0.008	11.897	-0.891	-0.891	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.098	-0.044	7.662	-2.799	-2.799	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.022	0.017	7.994	-1.294	-1.294	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.008	-0.016	6.069	-0.997	-0.997	0.000	0.000	0.000	0.000
91	A	91	ARG	1	0.799	0.889	11.171	15.813	15.813	0.000	0.000	0.000	0.000
92	A	92	ALA	0	0.034	0.020	14.475	-0.412	-0.412	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.011	-0.002	16.028	0.525	0.525	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.023	0.041	18.683	0.708	0.708	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.031	-0.032	18.645	-0.351	-0.351	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.053	0.013	18.408	0.698	0.698	0.000	0.000	0.000	0.000
97	A	97	VAL	0	-0.036	0.002	14.812	-0.837	-0.837	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.863	-0.943	14.686	-16.827	-16.827	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.868	-0.946	14.811	-17.316	-17.316	0.000	0.000	0.000	0.000
100	A	100	ASN	0	-0.013	-0.001	11.384	-0.218	-0.218	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.010	-0.004	10.208	-2.267	-2.267	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.893	0.956	9.861	15.437	15.437	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.040	0.005	11.725	-0.737	-0.737	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.080	-0.050	7.412	-2.627	-2.627	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.889	-0.945	8.634	-19.101	-19.101	0.000	0.000	0.000	0.000
107	A	107	GLY	0	-0.055	-0.015	7.828	1.026	1.026	0.000	0.000	0.000	0.000
108	A	108	ASN	0	-0.011	-0.003	8.585	1.711	1.711	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.037	-0.008	11.097	1.015	1.015	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.809	-0.876	10.690	-16.321	-16.321	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.738	-0.862	5.617	-31.073	-31.073	0.000	0.000	0.000	0.000
112	A	112	ILE	0	-0.041	-0.023	10.056	1.244	1.244	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.861	0.915	6.250	23.228	23.228	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.070	0.043	11.465	1.237	1.237	0.000	0.000	0.000	0.000
115	A	115	PRO	0	-0.053	-0.017	12.380	-0.725	-0.725	0.000	0.000	0.000	0.000
116	A	116	GLY	0	0.089	0.037	13.744	0.946	0.946	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.062	-0.030	13.986	0.633	0.633	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.028	0.019	16.743	-0.078	-0.078	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.927	0.951	17.869	12.133	12.133	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.064	0.030	21.145	0.300	0.300	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.947	0.978	22.528	11.609	11.609	0.000	0.000	0.000	0.000
122	A	122	ARG	1	0.908	0.954	26.211	10.011	10.011	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.960	0.969	28.258	9.143	9.143	0.000	0.000	0.000	0.000
124	A	124	ARG	0	0.133	0.089	31.845	-0.537	-0.537	0.000	0.000	0.000	0.000

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