FMO DATABASE

FMODB ID: MZ45Z

Calculation Name: 1DE3-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1DE3

Chain ID: A

ChEMBL ID:

UniProt ID: P00655

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	148
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1438077.345606
FMO2-HF: Nuclear repulsion	1378581.474203
FMO2-HF: Total energy	-59495.871403
FMO2-MP2: Total energy	-59670.290716

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:ALA)

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

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.
95.405	98.327	5.374	-4.17	-4.128	-0.047

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.835 / 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	3	THR	0	0.011	-0.003	3.529	-11.675	-10.496	-0.001	-0.582	-0.596	-0.001
26	A	26	ASN	0	0.026	0.009	1.996	-32.721	-32.122	5.310	-3.271	-2.639	-0.045
27	A	27	GLN	0	0.088	0.045	3.227	3.412	3.815	0.021	-0.098	-0.327	0.000
28	A	28	ASN	0	-0.020	-0.018	3.223	4.781	5.433	0.045	-0.201	-0.496	-0.001
29	A	29	LYS	1	0.960	1.009	4.555	48.163	48.252	-0.001	-0.018	-0.070	0.000
4	A	4	TRP	0	0.005	0.003	5.717	6.323	6.323	0.000	0.000	0.000	0.000
5	A	5	THR	0	-0.007	-0.007	8.874	0.326	0.326	0.000	0.000	0.000	0.000
6	A	6	CYS	0	-0.088	-0.020	11.729	1.691	1.691	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.040	-0.026	15.183	-0.130	-0.130	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.001	-0.001	18.446	-0.109	-0.109	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.808	-0.904	20.604	-12.161	-12.161	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.003	-0.018	20.121	0.299	0.299	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.961	0.981	24.892	10.393	10.393	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.012	-0.015	27.113	0.346	0.346	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.020	0.006	28.567	0.369	0.369	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.939	0.973	30.650	9.920	9.920	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.021	-0.032	29.993	0.319	0.319	0.000	0.000	0.000	0.000
16	A	16	ASN	0	-0.063	-0.029	32.984	0.245	0.245	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.975	1.005	30.281	9.866	9.866	0.000	0.000	0.000	0.000
18	A	18	TYR	0	-0.017	-0.009	27.209	-0.282	-0.282	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.860	-0.911	25.268	-11.707	-11.707	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.011	-0.020	21.676	-0.413	-0.413	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.903	0.963	19.695	14.454	14.454	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.956	0.972	15.255	16.709	16.709	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.007	0.013	14.556	-0.460	-0.460	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.003	0.007	7.480	-0.711	-0.711	0.000	0.000	0.000	0.000
25	A	25	TYR	0	0.080	0.030	8.509	0.855	0.855	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.032	0.034	7.565	3.875	3.875	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.887	-0.943	5.860	-30.574	-30.574	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.033	0.018	8.191	2.613	2.613	0.000	0.000	0.000	0.000
33	A	33	ASN	0	0.001	-0.013	10.078	2.524	2.524	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.037	-0.014	11.373	1.734	1.734	0.000	0.000	0.000	0.000
35	A	35	HIS	1	0.787	0.876	9.690	26.122	26.122	0.000	0.000	0.000	0.000
36	A	36	HIS	0	0.052	0.041	13.802	1.128	1.128	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.010	0.011	16.209	1.096	1.096	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.019	0.013	18.434	-0.238	-0.238	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.046	-0.039	19.336	-0.370	-0.370	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.008	-0.007	22.296	0.588	0.588	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.809	-0.875	24.718	-11.583	-11.583	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.006	0.009	26.016	0.393	0.393	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.875	0.946	26.855	10.425	10.425	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.002	-0.009	23.925	0.190	0.190	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.005	0.009	26.890	0.168	0.168	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.057	-0.057	24.231	0.176	0.176	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.079	-0.042	26.315	-0.120	-0.120	0.000	0.000	0.000	0.000
48	A	48	TYR	0	0.026	0.015	21.041	-0.113	-0.113	0.000	0.000	0.000	0.000
49	A	49	PRO	0	0.007	0.023	19.120	0.014	0.014	0.000	0.000	0.000	0.000
50	A	50	HIS	0	-0.029	-0.022	21.168	0.783	0.783	0.000	0.000	0.000	0.000
51	A	51	TRP	0	-0.003	-0.016	22.147	-0.541	-0.541	0.000	0.000	0.000	0.000
52	A	52	PHE	0	-0.011	-0.009	20.262	0.122	0.122	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.039	0.007	22.788	-0.063	-0.063	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.015	0.013	22.148	-0.085	-0.085	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.032	0.017	24.084	0.152	0.152	0.000	0.000	0.000	0.000
56	A	56	TYR	0	-0.034	-0.045	24.513	0.350	0.350	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.871	-0.957	29.234	-9.336	-9.336	0.000	0.000	0.000	0.000
58	A	58	GLY	0	-0.025	-0.011	29.571	0.102	0.102	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.884	-0.930	30.638	-8.828	-8.828	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.015	-0.024	29.981	-0.082	-0.082	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.907	0.969	31.066	8.598	8.598	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.012	0.021	28.321	-0.159	-0.159	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.073	0.058	31.927	0.318	0.318	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.918	0.940	34.756	7.929	7.929	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.029	0.018	33.431	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.913	0.956	31.207	8.800	8.800	0.000	0.000	0.000	0.000
67	A	67	THR	0	0.017	0.010	26.267	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.011	0.028	24.843	-0.254	-0.254	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.013	-0.011	18.737	-0.154	-0.154	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.965	0.980	20.847	12.504	12.504	0.000	0.000	0.000	0.000
71	A	71	PHE	0	0.045	-0.001	15.198	-0.541	-0.541	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.004	0.011	16.380	-0.787	-0.787	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.922	0.952	14.328	18.379	18.379	0.000	0.000	0.000	0.000
74	A	74	SER	0	0.079	0.031	19.129	0.129	0.129	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.873	-0.945	20.261	-12.914	-12.914	0.000	0.000	0.000	0.000
76	A	76	CYS	0	-0.169	-0.086	11.798	-0.350	-0.350	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.904	-0.939	20.255	-12.186	-12.186	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.890	0.957	23.443	12.139	12.139	0.000	0.000	0.000	0.000
79	A	79	PRO	0	-0.025	0.006	25.574	-0.122	-0.122	0.000	0.000	0.000	0.000
80	A	80	PRO	0	-0.008	0.005	25.041	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.840	0.917	26.780	9.703	9.703	0.000	0.000	0.000	0.000
82	A	82	HIS	1	0.839	0.908	27.445	10.438	10.438	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.009	0.000	29.524	0.415	0.415	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.905	0.940	31.797	8.175	8.175	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.829	-0.910	30.071	-9.547	-9.547	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.020	-0.006	27.289	-0.400	-0.400	0.000	0.000	0.000	0.000
87	A	87	ASN	0	0.000	-0.007	26.987	-0.238	-0.238	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.020	0.007	29.119	0.328	0.328	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.977	0.987	30.694	9.029	9.029	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.033	-0.036	27.798	-0.079	-0.079	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.806	-0.888	27.347	-10.946	-10.946	0.000	0.000	0.000	0.000
92	A	92	HIS	0	-0.008	-0.003	24.239	0.063	0.063	0.000	0.000	0.000	0.000
93	A	93	TYR	0	-0.040	-0.018	23.557	-0.223	-0.223	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.007	0.014	18.406	-0.523	-0.523	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.000	-0.002	18.414	0.547	0.547	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.794	-0.914	17.943	-16.098	-16.098	0.000	0.000	0.000	0.000
97	A	97	PHE	0	-0.011	0.006	15.291	0.826	0.826	0.000	0.000	0.000	0.000
98	A	98	PRO	0	-0.023	-0.005	16.167	-1.129	-1.129	0.000	0.000	0.000	0.000
99	A	99	THR	0	0.024	0.008	11.315	-0.200	-0.200	0.000	0.000	0.000	0.000
100	A	100	PHE	0	0.019	-0.006	13.096	0.783	0.783	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.051	-0.022	10.698	-1.920	-1.920	0.000	0.000	0.000	0.000
102	A	102	ASP	-1	-0.899	-0.945	10.090	-23.201	-23.201	0.000	0.000	0.000	0.000
103	A	103	GLY	0	-0.089	-0.071	10.016	-1.485	-1.485	0.000	0.000	0.000	0.000
104	A	104	HIS	0	0.028	0.017	10.703	-1.060	-1.060	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.831	-0.919	14.180	-19.471	-19.471	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.082	-0.044	16.215	1.306	1.306	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.992	1.003	18.716	12.890	12.890	0.000	0.000	0.000	0.000
108	A	108	PHE	0	0.022	-0.017	18.916	0.742	0.742	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.856	-0.914	22.703	-11.157	-11.157	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.033	-0.021	25.593	0.608	0.608	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.967	0.988	27.586	9.299	9.299	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.893	0.963	30.234	9.005	9.005	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.037	0.006	30.263	0.255	0.255	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.922	0.984	25.502	11.791	11.791	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.942	-0.958	22.508	-13.341	-13.341	0.000	0.000	0.000	0.000
116	A	116	ASN	0	0.033	0.009	24.566	0.151	0.151	0.000	0.000	0.000	0.000
117	A	117	PRO	0	-0.010	0.002	21.655	-0.469	-0.469	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.049	0.033	17.991	0.154	0.154	0.000	0.000	0.000	0.000
119	A	119	PRO	0	-0.039	-0.027	17.886	0.354	0.354	0.000	0.000	0.000	0.000
120	A	120	ALA	0	0.034	0.001	14.291	0.259	0.259	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.797	0.893	15.590	14.701	14.701	0.000	0.000	0.000	0.000
122	A	122	VAL	0	-0.038	-0.009	10.994	-0.661	-0.661	0.000	0.000	0.000	0.000
123	A	123	ILE	0	0.003	0.008	13.537	1.258	1.258	0.000	0.000	0.000	0.000
124	A	124	TYR	0	0.016	-0.003	13.791	-1.508	-1.508	0.000	0.000	0.000	0.000
125	A	125	THR	0	0.068	0.034	15.652	0.718	0.718	0.000	0.000	0.000	0.000
126	A	126	TYR	0	0.018	0.023	18.231	-0.558	-0.558	0.000	0.000	0.000	0.000
127	A	127	PRO	0	0.027	-0.005	20.839	0.351	0.351	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.013	-0.023	18.270	-0.841	-0.841	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.865	0.949	14.580	16.372	16.372	0.000	0.000	0.000	0.000
130	A	130	VAL	0	-0.028	-0.007	13.550	-1.556	-1.556	0.000	0.000	0.000	0.000
131	A	131	PHE	0	-0.003	-0.007	8.225	0.160	0.160	0.000	0.000	0.000	0.000
132	A	133	GLY	0	0.037	0.005	10.776	-0.485	-0.485	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.061	-0.015	8.567	-0.045	-0.045	0.000	0.000	0.000	0.000
134	A	135	ILE	0	0.017	0.013	12.493	0.098	0.098	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.049	0.005	16.132	-0.267	-0.267	0.000	0.000	0.000	0.000
136	A	137	HIS	0	-0.036	0.020	18.078	0.082	0.082	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.013	-0.008	21.553	0.070	0.070	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.930	0.991	22.693	11.073	11.073	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.841	-0.941	23.639	-11.702	-11.702	0.000	0.000	0.000	0.000
140	A	141	ASN	0	-0.037	-0.025	22.082	-0.575	-0.575	0.000	0.000	0.000	0.000
141	A	142	GLN	0	0.001	-0.007	23.425	0.309	0.309	0.000	0.000	0.000	0.000
142	A	143	GLY	0	0.015	0.018	26.015	0.281	0.281	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.846	-0.930	24.791	-11.699	-11.699	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.035	-0.008	20.072	-0.434	-0.434	0.000	0.000	0.000	0.000
145	A	146	LYS	1	0.963	0.988	19.208	16.256	16.256	0.000	0.000	0.000	0.000
146	A	147	LEU	0	0.007	-0.001	14.497	-0.751	-0.751	0.000	0.000	0.000	0.000
147	A	149	SER	0	0.025	0.010	13.410	0.356	0.356	0.000	0.000	0.000	0.000
148	A	150	HIS	0	0.007	0.018	8.197	-1.264	-1.264	0.000	0.000	0.000	0.000

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