FMO DATABASE

FMODB ID: N6G9Q

Calculation Name: 1EYU-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EYU

Chain ID: A

ChEMBL ID:

UniProt ID: P23657

Base Structure: X-ray

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	156
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1546878.749771
FMO2-HF: Nuclear repulsion	1484235.530412
FMO2-HF: Total energy	-62643.219359
FMO2-MP2: Total energy	-62830.374217

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-17.102	-13.771	1.084	-1.767	-2.648	-0.012

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.868 / q_NPA : 0.926

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	4	PRO	0	0.057	0.019	3.104	-4.930	-2.882	0.099	-0.990	-1.157	-0.005
5	A	6	LEU	0	-0.023	-0.009	2.477	-0.866	0.366	0.986	-0.772	-1.446	-0.007
6	A	7	ASN	0	0.005	-0.012	4.989	1.513	1.564	-0.001	-0.005	-0.045	0.000
4	A	5	ASP	-1	-0.821	-0.902	5.580	-26.060	-26.060	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.877	0.929	7.442	27.460	27.460	0.000	0.000	0.000	0.000
8	A	9	LEU	0	-0.008	0.004	7.401	1.527	1.527	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.029	-0.033	6.244	1.539	1.539	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.977	-0.974	10.167	-16.617	-16.617	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.052	0.016	12.902	1.089	1.089	0.000	0.000	0.000	0.000
12	A	13	TRP	0	-0.039	-0.011	12.338	0.603	0.603	0.000	0.000	0.000	0.000
13	A	14	PRO	0	0.046	0.024	14.364	0.792	0.792	0.000	0.000	0.000	0.000
14	A	15	HIS	0	0.005	-0.006	17.836	0.698	0.698	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.047	-0.014	14.165	0.494	0.494	0.000	0.000	0.000	0.000
16	A	17	GLN	0	-0.051	-0.023	17.043	0.127	0.127	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.809	-0.898	19.496	-12.226	-12.226	0.000	0.000	0.000	0.000
18	A	19	TYR	0	-0.074	-0.046	21.429	0.767	0.767	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.003	-0.012	20.896	0.082	0.082	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.882	-0.938	22.823	-12.281	-12.281	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.043	-0.027	25.321	0.612	0.612	0.000	0.000	0.000	0.000
22	A	23	ALA	0	0.005	0.004	25.316	0.467	0.467	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.009	0.011	26.144	0.397	0.397	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.880	0.945	28.137	9.531	9.531	0.000	0.000	0.000	0.000
25	A	26	HIS	0	-0.078	-0.050	30.557	0.661	0.661	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.051	0.041	31.649	0.099	0.099	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.048	-0.026	26.209	0.023	0.023	0.000	0.000	0.000	0.000
28	A	29	ASN	0	0.010	-0.013	26.266	-0.298	-0.298	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.795	-0.883	21.449	-14.600	-14.600	0.000	0.000	0.000	0.000
30	A	31	ILE	0	-0.023	-0.014	19.388	0.479	0.479	0.000	0.000	0.000	0.000
31	A	32	PHE	0	-0.037	-0.023	16.510	-0.113	-0.113	0.000	0.000	0.000	0.000
32	A	33	GLN	0	-0.049	-0.016	20.335	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.850	-0.927	23.189	-11.030	-11.030	0.000	0.000	0.000	0.000
34	A	35	ASN	0	-0.071	-0.040	25.139	0.289	0.289	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.085	0.055	25.502	0.260	0.260	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.031	0.005	23.390	0.274	0.274	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.856	0.931	24.430	11.981	11.981	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.004	0.016	27.031	0.362	0.362	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.054	0.026	26.981	0.373	0.373	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.009	-0.014	26.307	0.510	0.510	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.031	0.011	30.834	0.304	0.304	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.029	0.016	32.470	0.290	0.290	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.016	-0.013	30.671	0.253	0.253	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.050	-0.010	33.442	0.174	0.174	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.061	-0.065	36.580	0.267	0.267	0.000	0.000	0.000	0.000
46	A	47	GLY	0	-0.007	0.009	38.199	0.235	0.235	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.049	-0.014	37.795	0.093	0.093	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.002	-0.010	36.849	-0.255	-0.255	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.004	0.000	32.326	0.146	0.146	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.030	0.020	35.365	-0.129	-0.129	0.000	0.000	0.000	0.000
51	A	52	PRO	0	-0.004	-0.004	35.226	-0.244	-0.244	0.000	0.000	0.000	0.000
52	A	53	GLY	0	-0.028	-0.028	35.576	0.213	0.213	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.770	0.904	31.015	9.626	9.626	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.840	-0.926	36.430	-7.954	-7.954	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.033	-0.027	33.465	-0.196	-0.196	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.080	-0.034	30.014	-0.213	-0.213	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.725	-0.854	34.052	-8.256	-8.256	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.034	-0.032	36.809	-0.183	-0.183	0.000	0.000	0.000	0.000
59	A	60	VAL	0	0.013	0.004	38.633	0.190	0.190	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.744	-0.853	41.018	-6.985	-6.985	0.000	0.000	0.000	0.000
61	A	62	ASN	0	-0.040	-0.034	43.576	0.019	0.019	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.036	-0.014	45.690	0.128	0.128	0.000	0.000	0.000	0.000
63	A	64	GLY	0	-0.021	0.000	45.939	0.112	0.112	0.000	0.000	0.000	0.000
64	A	65	GLN	0	-0.096	-0.043	46.280	0.141	0.141	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.899	-0.957	42.304	-7.454	-7.454	0.000	0.000	0.000	0.000
66	A	67	TYR	0	-0.059	-0.060	40.710	0.163	0.163	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.800	-0.881	37.530	-8.643	-8.643	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.016	-0.007	34.869	0.072	0.072	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.762	0.889	34.465	8.428	8.428	0.000	0.000	0.000	0.000
70	A	71	SER	0	0.044	0.017	30.082	-0.016	-0.016	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.086	-0.037	30.946	-0.100	-0.100	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.057	0.036	25.305	0.143	0.143	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.048	0.014	29.002	0.059	0.059	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.819	-0.893	27.114	-10.745	-10.745	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.062	-0.019	24.370	-0.065	-0.065	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.018	-0.015	28.929	0.351	0.351	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.932	0.946	32.174	9.471	9.471	0.000	0.000	0.000	0.000
78	A	79	GLY	0	-0.010	-0.002	35.168	0.333	0.333	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.048	0.028	34.676	-0.261	-0.261	0.000	0.000	0.000	0.000
80	A	81	SER	0	0.005	-0.011	32.300	0.183	0.183	0.000	0.000	0.000	0.000
81	A	82	THR	0	-0.004	-0.013	34.741	0.030	0.030	0.000	0.000	0.000	0.000
82	A	83	HIS	0	0.115	0.044	35.711	-0.095	-0.095	0.000	0.000	0.000	0.000
83	A	84	HIS	0	-0.046	-0.022	31.460	-0.069	-0.069	0.000	0.000	0.000	0.000
84	A	85	HIS	1	0.829	0.878	35.223	8.367	8.367	0.000	0.000	0.000	0.000
85	A	86	MET	0	0.024	0.041	38.670	0.152	0.152	0.000	0.000	0.000	0.000
86	A	87	ASN	0	0.011	-0.016	41.211	0.163	0.163	0.000	0.000	0.000	0.000
87	A	88	PRO	0	0.078	0.026	44.764	-0.100	-0.100	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.001	0.012	44.966	0.051	0.051	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.036	-0.017	40.053	-0.072	-0.072	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.035	-0.020	43.067	-0.041	-0.041	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.053	-0.033	45.426	0.020	0.020	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.869	0.968	40.136	7.745	7.745	0.000	0.000	0.000	0.000
93	A	94	TYR	0	0.051	0.004	39.098	-0.019	-0.019	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.788	0.870	44.305	6.346	6.346	0.000	0.000	0.000	0.000
95	A	96	GLN	0	-0.020	-0.019	47.648	0.215	0.215	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.012	0.036	43.004	0.083	0.083	0.000	0.000	0.000	0.000
97	A	98	PRO	0	-0.018	-0.007	45.029	-0.024	-0.024	0.000	0.000	0.000	0.000
98	A	99	TRP	0	-0.051	-0.025	39.499	-0.315	-0.315	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.010	0.001	37.411	0.126	0.126	0.000	0.000	0.000	0.000
100	A	101	PHE	0	-0.027	-0.022	37.154	-0.244	-0.244	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.033	0.021	33.309	0.123	0.123	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.024	-0.033	33.298	-0.237	-0.237	0.000	0.000	0.000	0.000
103	A	104	TYR	0	0.029	-0.001	28.226	0.104	0.104	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.854	0.927	28.398	10.256	10.256	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.025	0.004	24.272	-0.351	-0.351	0.000	0.000	0.000	0.000
106	A	107	ILE	0	-0.034	-0.036	21.250	0.050	0.050	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.030	0.039	24.641	0.189	0.189	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.035	-0.013	27.369	0.143	0.143	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.920	-0.960	31.047	-9.279	-9.279	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.050	-0.041	33.705	0.312	0.312	0.000	0.000	0.000	0.000
111	A	112	ILE	0	0.015	0.012	35.170	-0.225	-0.225	0.000	0.000	0.000	0.000
112	A	113	TYR	0	0.008	0.005	37.961	0.174	0.174	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.951	0.983	40.655	6.623	6.623	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.086	-0.021	42.844	0.138	0.138	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.800	-0.904	45.448	-6.599	-6.599	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.059	0.026	48.251	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.869	0.919	49.232	6.180	6.180	0.000	0.000	0.000	0.000
118	A	119	ASP	-1	-0.809	-0.884	47.781	-6.310	-6.310	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.005	0.003	43.626	-0.101	-0.101	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.764	-0.860	47.407	-6.260	-6.260	0.000	0.000	0.000	0.000
121	A	122	PHE	0	0.029	0.008	48.514	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	123	TYR	0	-0.056	-0.051	44.149	-0.059	-0.059	0.000	0.000	0.000	0.000
123	A	124	TYR	0	0.033	0.025	44.653	-0.131	-0.131	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.773	-0.877	48.072	-5.962	-5.962	0.000	0.000	0.000	0.000
125	A	126	LYS	1	0.785	0.912	45.960	6.692	6.692	0.000	0.000	0.000	0.000
126	A	127	TRP	0	0.027	-0.014	42.281	-0.021	-0.021	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.797	-0.898	47.100	-6.291	-6.291	0.000	0.000	0.000	0.000
128	A	129	ARG	1	0.900	0.937	50.203	5.978	5.978	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.878	0.969	46.547	6.738	6.738	0.000	0.000	0.000	0.000
130	A	131	TRP	0	0.088	0.043	46.202	0.127	0.127	0.000	0.000	0.000	0.000
131	A	132	TYR	0	-0.024	-0.020	49.099	0.092	0.092	0.000	0.000	0.000	0.000
132	A	133	SER	0	-0.039	-0.018	52.450	0.127	0.127	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.873	-0.943	47.675	-6.613	-6.613	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.047	0.023	50.338	-0.051	-0.051	0.000	0.000	0.000	0.000
135	A	136	HIS	1	0.825	0.904	49.129	6.098	6.098	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.839	0.919	44.367	6.429	6.429	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.795	-0.856	40.955	-7.506	-7.506	0.000	0.000	0.000	0.000
138	A	139	ILE	0	-0.025	-0.016	41.078	-0.098	-0.098	0.000	0.000	0.000	0.000
139	A	140	ASN	0	0.008	0.002	34.360	-0.213	-0.213	0.000	0.000	0.000	0.000
140	A	141	ASN	0	0.022	0.018	32.796	0.087	0.087	0.000	0.000	0.000	0.000
141	A	142	PRO	0	0.013	0.027	36.688	-0.105	-0.105	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.837	0.928	33.973	8.913	8.913	0.000	0.000	0.000	0.000
143	A	144	ILE	0	0.054	0.044	38.929	0.235	0.235	0.000	0.000	0.000	0.000
144	A	145	PRO	0	-0.033	-0.018	39.177	-0.225	-0.225	0.000	0.000	0.000	0.000
145	A	146	VAL	0	0.054	0.025	35.994	0.145	0.145	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.890	0.940	39.333	6.891	6.891	0.000	0.000	0.000	0.000
147	A	148	TYR	0	-0.036	-0.039	42.629	0.190	0.190	0.000	0.000	0.000	0.000
148	A	149	VAL	0	0.053	0.017	39.719	0.165	0.165	0.000	0.000	0.000	0.000
149	A	150	MET	0	-0.032	-0.029	40.178	0.046	0.046	0.000	0.000	0.000	0.000
150	A	151	GLU	-1	-0.922	-0.936	43.231	-6.437	-6.437	0.000	0.000	0.000	0.000
151	A	152	HIS	1	0.849	0.918	46.310	6.682	6.682	0.000	0.000	0.000	0.000
152	A	153	GLY	0	0.029	0.019	44.687	0.082	0.082	0.000	0.000	0.000	0.000
153	A	154	THR	0	-0.043	-0.021	45.776	0.117	0.117	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.803	0.890	39.718	7.654	7.654	0.000	0.000	0.000	0.000
155	A	156	ILE	0	-0.040	-0.038	40.430	0.169	0.169	0.000	0.000	0.000	0.000
156	A	157	TYR	-1	-0.757	-0.836	34.002	-7.924	-7.924	0.000	0.000	0.000	0.000

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