FMO DATABASE

FMODB ID: QK5KY

Calculation Name: 1EAL-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1EAL

Chain ID: A

ChEMBL ID:

UniProt ID: P10289

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1063914.596482
FMO2-HF: Nuclear repulsion	1014696.097541
FMO2-HF: Total energy	-49218.498941
FMO2-MP2: Total energy	-49362.649013

3D Structure

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.
-62.17	-58.664	1.313	-1.805	-3.015	-0.015

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 : 0.827 / q_NPA : 0.906

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	-0.019	0.001	3.807	3.382	4.714	-0.014	-0.493	-0.825	-0.001
42	A	42	GLN	0	-0.067	-0.041	4.386	-9.903	-9.732	-0.001	-0.016	-0.154	0.000
47	A	47	PHE	0	0.008	-0.006	4.197	-2.917	-2.794	-0.001	-0.026	-0.095	0.000
85	A	85	MET	0	-0.036	-0.031	2.069	-6.296	-5.836	1.271	-0.660	-1.072	-0.009
88	A	88	GLY	0	-0.022	-0.022	4.296	-3.675	-3.590	-0.001	-0.008	-0.077	0.000
89	A	89	LYS	1	0.910	0.987	3.498	13.483	14.005	0.010	-0.300	-0.232	-0.002
103	A	103	ILE	0	-0.053	-0.023	2.875	-1.248	-0.435	0.049	-0.302	-0.560	-0.003
4	A	4	GLY	0	0.047	0.023	5.963	1.298	1.298	0.000	0.000	0.000	0.000
5	A	5	LYS	1	0.950	0.994	9.125	18.917	18.917	0.000	0.000	0.000	0.000
6	A	6	TYR	0	-0.013	-0.050	6.195	-1.173	-1.173	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.931	-0.966	12.692	-15.248	-15.248	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.036	-0.011	14.471	-0.831	-0.831	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.989	-1.006	16.554	-15.901	-15.901	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.040	0.029	18.264	1.258	1.258	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.920	-0.964	18.190	-16.804	-16.804	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.930	0.972	20.154	13.648	13.648	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.039	-0.034	22.200	0.159	0.159	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.063	0.015	24.856	-0.055	-0.055	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.906	-0.940	25.712	-9.931	-9.931	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.899	-0.962	27.983	-10.255	-10.255	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.027	-0.009	20.727	0.029	0.029	0.000	0.000	0.000	0.000
18	A	18	MET	0	0.029	0.012	24.051	0.097	0.097	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.947	0.981	27.641	9.551	9.551	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.903	0.943	27.642	11.126	11.126	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.026	-0.004	22.786	0.026	0.026	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.032	-0.004	27.117	0.070	0.070	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.016	0.007	26.286	-0.085	-0.085	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.017	0.009	30.532	0.234	0.234	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.055	0.002	32.780	-0.260	-0.260	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.793	-0.875	33.839	-9.466	-9.466	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.028	-0.015	29.587	-0.209	-0.209	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.002	-0.002	29.173	-0.418	-0.418	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.838	-0.894	29.656	-9.688	-9.688	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.825	0.890	29.193	9.661	9.661	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.009	-0.010	25.559	-0.309	-0.309	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.769	0.875	25.398	9.499	9.499	0.000	0.000	0.000	0.000
33	A	33	ASN	0	0.040	0.018	24.464	0.061	0.061	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.068	-0.014	24.633	0.090	0.090	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.963	0.989	21.456	14.214	14.214	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.010	-0.003	17.698	0.259	0.259	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.027	-0.004	16.297	-0.421	-0.421	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.003	-0.002	11.552	0.270	0.270	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.910	-0.964	11.643	-21.903	-21.903	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.021	0.008	6.289	0.023	0.023	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.982	0.989	8.556	20.053	20.053	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.871	-0.916	8.024	-19.753	-19.753	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.022	-0.020	8.825	-2.543	-2.543	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.014	-0.019	8.744	-2.005	-2.005	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.019	-0.007	9.818	0.574	0.574	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.003	-0.005	9.155	2.775	2.775	0.000	0.000	0.000	0.000
49	A	49	TRP	0	0.025	0.010	5.491	-3.026	-3.026	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.001	-0.004	11.164	2.557	2.557	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.076	0.048	13.616	-0.314	-0.314	0.000	0.000	0.000	0.000
52	A	52	GLN	0	-0.001	0.000	15.863	1.143	1.143	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.016	0.013	19.291	-0.256	-0.256	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.012	-0.009	22.341	0.190	0.190	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.005	0.008	25.038	0.434	0.434	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.017	-0.006	25.513	-0.378	-0.378	0.000	0.000	0.000	0.000
57	A	57	HIS	0	-0.010	0.015	22.693	0.248	0.248	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.015	-0.031	19.013	-0.491	-0.491	0.000	0.000	0.000	0.000
59	A	59	ILE	0	-0.008	0.005	16.403	0.337	0.337	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.011	-0.011	15.842	-1.662	-1.662	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.018	-0.012	13.605	1.508	1.508	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.026	-0.031	12.897	-1.025	-1.025	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.003	0.014	8.024	1.424	1.424	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.027	0.014	11.155	-1.135	-1.135	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.002	0.004	6.680	-0.085	-0.085	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.011	0.020	10.376	1.361	1.361	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.899	0.942	13.697	17.583	17.583	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.845	-0.917	16.854	-13.918	-13.918	0.000	0.000	0.000	0.000
69	A	69	CYS	0	-0.106	-0.035	14.930	-0.725	-0.725	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.780	-0.891	17.094	-13.784	-13.784	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.026	-0.011	14.370	-0.916	-0.916	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.931	-0.975	18.230	-11.900	-11.900	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.014	0.004	17.619	0.147	0.147	0.000	0.000	0.000	0.000
74	A	74	ILE	0	0.012	-0.007	19.782	0.011	0.011	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.091	0.058	23.089	0.334	0.334	0.000	0.000	0.000	0.000
76	A	76	GLY	0	-0.031	-0.024	25.647	0.219	0.219	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.873	0.934	25.020	12.024	12.024	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.888	0.958	22.197	13.088	13.088	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.035	-0.029	20.312	0.491	0.491	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.893	0.938	20.425	12.881	12.881	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.015	-0.001	16.108	0.190	0.190	0.000	0.000	0.000	0.000
82	A	82	THR	0	0.025	0.022	16.504	-0.191	-0.191	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.015	-0.004	9.992	-0.297	-0.297	0.000	0.000	0.000	0.000
84	A	84	GLN	0	-0.023	-0.008	11.320	1.478	1.478	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.903	-0.941	7.875	-21.047	-21.047	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.019	0.008	7.998	-0.390	-0.390	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.031	-0.015	5.143	1.820	1.820	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.006	-0.015	6.879	2.667	2.667	0.000	0.000	0.000	0.000
92	A	92	VAL	0	0.036	0.010	10.653	0.064	0.064	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.001	0.004	13.298	1.424	1.424	0.000	0.000	0.000	0.000
94	A	94	SER	0	0.065	-0.003	16.955	-0.074	-0.074	0.000	0.000	0.000	0.000
95	A	95	PRO	0	-0.040	-0.014	19.818	0.099	0.099	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.041	-0.023	23.062	0.478	0.478	0.000	0.000	0.000	0.000
97	A	97	TYR	0	0.008	0.002	15.491	0.597	0.597	0.000	0.000	0.000	0.000
98	A	98	HIS	0	0.026	0.044	14.780	0.232	0.232	0.000	0.000	0.000	0.000
99	A	99	HIS	0	0.000	0.003	11.219	2.059	2.059	0.000	0.000	0.000	0.000
100	A	100	THR	0	-0.053	-0.029	10.466	-0.954	-0.954	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.022	0.015	6.975	1.665	1.665	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.818	-0.927	5.867	-44.680	-44.680	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.038	0.025	5.404	0.209	0.209	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.908	-0.960	8.577	-23.161	-23.161	0.000	0.000	0.000	0.000
106	A	106	GLY	0	-0.041	-0.017	8.662	1.766	1.766	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.874	0.943	9.431	22.658	22.658	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.009	0.004	7.075	-4.642	-4.642	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.016	-0.006	8.493	3.883	3.883	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.822	-0.923	9.300	-28.246	-28.246	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.019	-0.004	11.713	1.995	1.995	0.000	0.000	0.000	0.000
112	A	112	SER	0	0.020	0.021	14.149	-0.683	-0.683	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.064	-0.053	16.940	0.682	0.682	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.005	0.002	19.791	-0.184	-0.184	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.005	0.005	23.030	0.525	0.525	0.000	0.000	0.000	0.000
116	A	116	GLY	0	0.009	0.001	24.233	0.563	0.563	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.027	0.001	24.344	0.149	0.149	0.000	0.000	0.000	0.000
118	A	118	SER	0	0.007	0.004	19.837	-0.188	-0.188	0.000	0.000	0.000	0.000
119	A	119	TYR	0	0.016	-0.003	18.752	0.531	0.531	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.920	-0.957	16.091	-18.443	-18.443	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.823	0.898	14.767	20.397	20.397	0.000	0.000	0.000	0.000
122	A	122	VAL	0	0.017	0.026	13.619	-1.859	-1.859	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.020	-0.008	11.639	0.644	0.644	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.941	0.980	12.450	17.357	17.357	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.953	0.982	6.338	37.033	37.033	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.078	-0.037	12.016	1.729	1.729	0.000	0.000	0.000	0.000
127	A	127	ALA	-1	-0.871	-0.930	10.582	-25.850	-25.850	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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