FMO DATABASE

FMODB ID: 5G4LZ

Calculation Name: 1E09-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1E09

Chain ID: A

ChEMBL ID:

UniProt ID: O24248

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	159
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-1504574.419538
FMO2-HF: Nuclear repulsion	1444425.772751
FMO2-HF: Total energy	-60148.646787
FMO2-MP2: Total energy	-60329.161127

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:GLY)

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

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.
-96.389	-93.339	0.064	-1.63	-1.484	-0.011

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.869 / q_NPA : 0.919

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	3	PHE	0	-0.002	0.008	2.934	-11.024	-8.611	0.063	-1.391	-1.085	-0.010
122	A	122	THR	0	0.008	0.014	3.991	2.241	2.440	0.001	-0.060	-0.140	0.000
127	A	127	GLU	-1	-0.946	-0.980	3.917	-71.602	-71.164	0.000	-0.179	-0.259	-0.001
4	A	4	THR	0	0.031	0.004	5.485	3.089	3.089	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.026	-0.022	8.671	0.303	0.303	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.827	-0.897	12.106	-18.841	-18.841	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.093	-0.062	15.681	0.168	0.168	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.852	-0.911	19.245	-14.958	-14.958	0.000	0.000	0.000	0.000
9	A	9	PHE	0	-0.040	-0.015	22.292	0.325	0.325	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.010	-0.002	26.060	0.138	0.138	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.058	-0.056	29.583	0.050	0.050	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.929	-0.968	32.425	-8.558	-8.558	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.035	0.002	34.340	0.341	0.341	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.040	0.019	34.466	-0.224	-0.224	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.098	0.051	31.230	-0.041	-0.041	0.000	0.000	0.000	0.000
16	A	16	PRO	0	-0.031	-0.029	32.485	-0.153	-0.153	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.784	0.904	34.771	8.394	8.394	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.076	0.036	27.879	-0.088	-0.088	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.005	0.005	27.887	-0.115	-0.115	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.878	0.944	30.834	8.840	8.840	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.045	0.012	32.168	-0.055	-0.055	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.023	-0.033	23.966	-0.067	-0.067	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.029	-0.005	26.749	-0.378	-0.378	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.063	-0.041	29.047	0.056	0.056	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.775	-0.877	32.559	-8.724	-8.724	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.040	0.004	28.184	0.048	0.048	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.839	-0.938	29.966	-11.030	-11.030	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.043	-0.037	31.837	0.218	0.218	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.046	-0.007	30.684	0.168	0.168	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.062	0.023	28.066	0.168	0.168	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.028	-0.010	31.390	0.127	0.127	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.885	0.940	34.157	8.626	8.626	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.054	-0.003	31.201	0.215	0.215	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.029	0.008	31.933	0.220	0.220	0.000	0.000	0.000	0.000
35	A	35	PRO	0	0.010	0.006	32.378	-0.309	-0.309	0.000	0.000	0.000	0.000
36	A	36	GLN	0	-0.034	-0.019	33.011	-0.179	-0.179	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.038	0.037	27.937	-0.190	-0.190	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.017	-0.016	25.865	-0.314	-0.314	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.904	0.963	29.941	10.038	10.038	0.000	0.000	0.000	0.000
40	A	40	HIS	1	0.815	0.886	31.434	10.367	10.367	0.000	0.000	0.000	0.000
41	A	41	SER	0	0.040	0.045	29.433	-0.462	-0.462	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.815	-0.887	29.640	-9.632	-9.632	0.000	0.000	0.000	0.000
43	A	43	ILE	0	0.018	0.010	29.293	-0.507	-0.507	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.052	-0.018	26.369	0.296	0.296	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.913	-0.963	26.190	-11.854	-11.854	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.021	-0.017	28.547	-0.340	-0.340	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.907	-0.961	30.343	-9.114	-9.114	0.000	0.000	0.000	0.000
48	A	48	GLY	0	-0.002	-0.012	28.529	0.101	0.101	0.000	0.000	0.000	0.000
49	A	49	GLY	0	-0.009	0.007	28.196	-0.200	-0.200	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.032	0.009	24.595	-0.237	-0.237	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.034	-0.020	23.412	0.381	0.381	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.038	-0.018	24.413	0.152	0.152	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.008	0.014	22.082	-0.770	-0.770	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.882	0.936	24.560	11.976	11.976	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.878	0.927	24.560	10.230	10.230	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.008	0.015	24.230	0.567	0.567	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.022	-0.021	25.987	-0.124	-0.124	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.041	0.006	22.546	0.152	0.152	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.073	-0.043	28.324	0.326	0.326	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.952	-0.960	27.886	-11.309	-11.309	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.021	0.009	28.312	-0.395	-0.395	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.059	-0.030	29.284	0.312	0.312	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.007	-0.004	26.201	0.192	0.192	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.014	-0.013	28.748	0.019	0.019	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.123	0.075	25.592	-0.334	-0.334	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.132	-0.084	23.961	0.656	0.656	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.033	0.014	20.402	-0.723	-0.723	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.847	0.918	20.868	14.192	14.192	0.000	0.000	0.000	0.000
69	A	69	HIS	0	-0.033	-0.038	20.055	-0.900	-0.900	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.993	1.004	18.978	16.409	16.409	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.034	-0.008	20.386	-0.737	-0.737	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.960	-0.965	17.208	-17.783	-17.783	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.006	-0.014	20.202	0.497	0.497	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.038	-0.027	22.793	-0.035	-0.035	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.813	-0.850	25.605	-12.206	-12.206	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.897	0.911	27.856	10.104	10.104	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.940	-0.951	31.022	-9.461	-9.461	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.043	-0.037	27.932	0.109	0.109	0.000	0.000	0.000	0.000
79	A	79	TYR	0	-0.005	0.010	28.573	-0.070	-0.070	0.000	0.000	0.000	0.000
80	A	80	SER	0	0.017	-0.043	23.708	-0.228	-0.228	0.000	0.000	0.000	0.000
81	A	81	TYR	0	-0.050	-0.038	23.403	0.378	0.378	0.000	0.000	0.000	0.000
82	A	82	SER	0	0.067	0.031	18.569	-0.340	-0.340	0.000	0.000	0.000	0.000
83	A	83	TYR	0	0.004	0.001	18.639	0.737	0.737	0.000	0.000	0.000	0.000
84	A	84	THR	0	0.005	0.009	14.362	-0.801	-0.801	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.059	-0.010	15.500	1.210	1.210	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.041	-0.034	15.049	-1.354	-1.354	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.748	-0.854	16.702	-13.895	-13.895	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.074	0.010	18.625	0.221	0.221	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.887	-0.930	18.021	-15.127	-15.127	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.029	-0.020	17.155	-0.470	-0.470	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.061	-0.020	13.222	-1.362	-1.362	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.052	0.025	13.406	-1.576	-1.576	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.897	-0.946	14.307	-18.881	-18.881	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.115	-0.058	10.061	-1.766	-1.766	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.051	-0.036	8.238	-5.009	-5.009	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.831	-0.905	10.022	-20.171	-20.171	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.911	0.963	10.253	25.502	25.502	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.008	0.013	10.127	-3.576	-3.576	0.000	0.000	0.000	0.000
99	A	99	SER	0	0.000	-0.011	11.327	2.789	2.789	0.000	0.000	0.000	0.000
100	A	100	TYR	0	-0.023	-0.017	13.446	-1.467	-1.467	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.902	-0.947	16.304	-17.872	-17.872	0.000	0.000	0.000	0.000
102	A	102	THR	0	-0.046	-0.029	18.296	0.161	0.161	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.960	0.983	21.489	13.419	13.419	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.012	0.014	24.035	0.031	0.031	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.018	0.007	27.128	0.163	0.163	0.000	0.000	0.000	0.000
106	A	106	ALA	0	0.030	0.016	29.920	0.124	0.124	0.000	0.000	0.000	0.000
107	A	107	SER	0	0.003	-0.008	32.443	-0.156	-0.156	0.000	0.000	0.000	0.000
108	A	108	PRO	0	-0.014	-0.020	34.026	0.210	0.210	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.033	-0.021	35.745	0.243	0.243	0.000	0.000	0.000	0.000
110	A	110	GLY	0	-0.003	0.008	37.730	0.213	0.213	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.044	0.034	35.545	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.073	-0.023	31.676	-0.162	-0.162	0.000	0.000	0.000	0.000
113	A	113	ILE	0	0.018	-0.009	26.630	-0.061	-0.061	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.029	-0.012	24.193	-0.038	-0.038	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.842	0.921	18.026	16.609	16.609	0.000	0.000	0.000	0.000
116	A	116	SER	0	0.011	0.003	19.663	-0.146	-0.146	0.000	0.000	0.000	0.000
117	A	117	THR	0	-0.006	-0.034	13.941	-0.479	-0.479	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.025	0.006	13.505	0.437	0.437	0.000	0.000	0.000	0.000
119	A	119	HIS	0	0.064	0.022	9.030	-3.832	-3.832	0.000	0.000	0.000	0.000
120	A	120	TYR	0	0.020	0.010	7.236	2.819	2.819	0.000	0.000	0.000	0.000
121	A	121	HIS	0	0.006	-0.005	5.744	-7.585	-7.585	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.855	0.916	5.639	21.580	21.580	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.028	0.012	7.684	1.508	1.508	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.083	-0.037	6.028	-0.112	-0.112	0.000	0.000	0.000	0.000
126	A	126	VAL	0	0.043	0.039	6.214	2.583	2.583	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.016	0.004	5.793	5.786	5.786	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.992	0.995	8.411	20.186	20.186	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.899	-0.964	11.530	-22.284	-22.284	0.000	0.000	0.000	0.000
131	A	131	GLU	-1	-0.979	-0.993	12.904	-16.743	-16.743	0.000	0.000	0.000	0.000
132	A	132	HIS	0	0.009	0.019	12.206	1.597	1.597	0.000	0.000	0.000	0.000
133	A	133	VAL	0	0.059	0.032	10.748	1.076	1.076	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.908	0.955	13.575	17.882	17.882	0.000	0.000	0.000	0.000
135	A	135	ALA	0	0.047	0.025	16.424	1.017	1.017	0.000	0.000	0.000	0.000
136	A	136	GLY	0	0.031	0.012	16.481	0.838	0.838	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.952	0.978	13.800	22.355	22.355	0.000	0.000	0.000	0.000
138	A	138	GLU	-1	-0.893	-0.920	18.435	-12.651	-12.651	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.883	0.929	21.071	14.442	14.442	0.000	0.000	0.000	0.000
140	A	140	ALA	0	0.044	0.027	19.907	0.651	0.651	0.000	0.000	0.000	0.000
141	A	141	SER	0	-0.017	-0.025	21.755	0.698	0.698	0.000	0.000	0.000	0.000
142	A	142	ASN	0	-0.058	-0.037	23.945	0.826	0.826	0.000	0.000	0.000	0.000
143	A	143	LEU	0	0.020	0.005	23.437	0.555	0.555	0.000	0.000	0.000	0.000
144	A	144	PHE	0	0.025	0.009	21.614	0.383	0.383	0.000	0.000	0.000	0.000
145	A	145	LYS	1	0.957	0.982	27.192	12.036	12.036	0.000	0.000	0.000	0.000
146	A	146	LEU	0	0.003	0.020	29.128	0.491	0.491	0.000	0.000	0.000	0.000
147	A	147	ILE	0	0.030	0.020	27.480	0.410	0.410	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.781	-0.864	30.779	-9.879	-9.879	0.000	0.000	0.000	0.000
149	A	149	THR	0	-0.042	-0.048	33.448	0.429	0.429	0.000	0.000	0.000	0.000
150	A	150	TYR	0	-0.046	-0.015	34.898	0.340	0.340	0.000	0.000	0.000	0.000
151	A	151	LEU	0	0.032	0.015	34.109	0.287	0.287	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.927	0.974	37.453	8.644	8.644	0.000	0.000	0.000	0.000
153	A	153	GLY	0	-0.017	0.001	39.412	0.227	0.227	0.000	0.000	0.000	0.000
154	A	154	HIS	1	0.792	0.889	39.508	8.341	8.341	0.000	0.000	0.000	0.000
155	A	155	PRO	0	0.060	0.030	41.269	-0.166	-0.166	0.000	0.000	0.000	0.000
156	A	156	ASP	-1	-0.869	-0.930	43.569	-7.036	-7.036	0.000	0.000	0.000	0.000
157	A	157	ALA	0	-0.085	-0.041	38.765	-0.030	-0.030	0.000	0.000	0.000	0.000
158	A	158	TYR	0	0.031	0.006	35.585	-0.265	-0.265	0.000	0.000	0.000	0.000
159	A	159	ASN	-1	-0.878	-0.928	39.135	-8.055	-8.055	0.000	0.000	0.000	0.000

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