FMO DATABASE

FMODB ID: LQVL9

Calculation Name: 1A03-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1A03

Chain ID: A

ChEMBL ID:

UniProt ID: P30801

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-599932.08963
FMO2-HF: Nuclear repulsion	564358.09141
FMO2-HF: Total energy	-35573.99822
FMO2-MP2: Total energy	-35677.719596

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.
-107.143	-99.752	6.199	-7.31	-6.282	-0.092

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 : 0.803 / q_NPA : 0.896

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	SER	0	0.003	-0.001	2.914	6.158	8.581	0.130	-1.031	-1.524	-0.002
4	A	4	PRO	0	0.070	0.017	4.709	-0.078	0.054	-0.001	-0.016	-0.114	0.000
6	A	6	ASP	-1	-0.878	-0.939	1.924	-109.539	-104.862	6.071	-6.251	-4.498	-0.090
7	A	7	GLN	0	0.017	0.004	4.752	7.065	7.224	-0.001	-0.012	-0.146	0.000
5	A	5	LEU	0	0.038	0.033	5.448	2.085	2.085	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.029	0.019	7.893	3.318	3.318	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.015	-0.003	5.575	2.752	2.752	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.020	0.017	7.834	2.376	2.376	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.025	-0.020	8.874	3.111	3.111	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.005	0.018	11.942	1.955	1.955	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.025	-0.005	9.733	1.851	1.851	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.018	0.021	12.711	1.392	1.392	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.049	-0.030	14.236	1.643	1.643	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.049	0.028	16.555	1.097	1.097	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.011	0.022	15.989	0.575	0.575	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.857	0.905	18.049	15.975	15.975	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.107	-0.056	20.387	0.700	0.700	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.032	0.004	21.004	0.809	0.809	0.000	0.000	0.000	0.000
21	A	21	GLY	0	-0.015	-0.014	23.398	0.639	0.639	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.880	0.955	22.466	13.178	13.178	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.924	-0.959	26.351	-10.088	-10.088	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.000	0.000	25.960	0.269	0.269	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.928	-0.950	20.413	-14.573	-14.573	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.897	0.944	22.314	10.944	10.944	0.000	0.000	0.000	0.000
27	A	27	HIS	0	-0.074	-0.047	15.916	-0.714	-0.714	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.061	-0.061	20.481	-0.700	-0.700	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.019	0.026	23.238	0.230	0.230	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.034	0.019	25.110	0.564	0.564	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.847	0.906	28.623	9.465	9.465	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.849	0.933	30.833	10.100	10.100	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.739	-0.885	26.710	-11.094	-11.094	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.020	0.035	28.529	-0.099	-0.099	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.909	0.965	29.465	8.786	8.786	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.819	-0.914	30.448	-10.163	-10.163	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.047	-0.010	25.860	0.068	0.068	0.000	0.000	0.000	0.000
38	A	38	ILE	0	0.090	0.044	29.616	0.215	0.215	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.061	-0.043	32.585	0.175	0.175	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.852	0.920	29.330	10.894	10.894	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.860	-0.934	30.233	-10.611	-10.611	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.010	0.006	32.159	0.212	0.212	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.045	-0.008	34.588	0.152	0.152	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.064	-0.053	37.002	0.216	0.216	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.020	0.033	38.842	0.211	0.211	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.014	-0.023	35.974	0.154	0.154	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.856	0.919	37.503	7.621	7.621	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.001	0.009	32.937	0.036	0.036	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.055	-0.003	31.504	0.126	0.126	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.866	-0.922	34.198	-8.464	-8.464	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.028	-0.015	35.821	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.922	-0.935	28.258	-11.274	-11.274	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.032	0.009	31.182	-0.191	-0.191	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.050	-0.024	33.007	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.891	0.961	26.447	11.861	11.861	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.041	-0.023	26.914	-0.253	-0.253	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.010	-0.006	29.389	-0.087	-0.087	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.912	-0.938	31.935	-9.595	-9.595	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.887	-0.953	26.147	-12.337	-12.337	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.006	-0.001	24.484	-0.358	-0.358	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.802	-0.920	27.617	-10.697	-10.697	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.787	0.896	28.816	10.563	10.563	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.113	-0.080	31.221	0.286	0.286	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.844	0.940	27.971	11.081	11.081	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.748	-0.863	30.612	-9.534	-9.534	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.010	-0.014	31.443	-0.107	-0.107	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.899	-0.940	27.037	-11.659	-11.659	0.000	0.000	0.000	0.000
68	A	68	VAL	0	0.000	0.026	25.876	0.082	0.082	0.000	0.000	0.000	0.000
69	A	69	ASN	0	-0.024	-0.022	22.278	-0.918	-0.918	0.000	0.000	0.000	0.000
70	A	70	PHE	0	0.060	0.020	13.941	-0.112	-0.112	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.007	-0.010	19.442	-0.578	-0.578	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.779	-0.893	20.786	-12.129	-12.129	0.000	0.000	0.000	0.000
73	A	73	TYR	0	0.019	0.015	16.585	0.305	0.305	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.034	-0.011	14.988	-0.474	-0.474	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.013	-0.019	18.783	-0.127	-0.127	0.000	0.000	0.000	0.000
76	A	76	PHE	0	0.065	0.043	21.911	0.111	0.111	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.038	-0.017	15.272	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.003	-0.003	19.946	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.010	0.001	20.669	0.314	0.314	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.064	-0.019	22.005	0.558	0.558	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.032	0.001	19.562	0.302	0.302	0.000	0.000	0.000	0.000
82	A	82	MET	0	-0.028	-0.012	21.597	0.302	0.302	0.000	0.000	0.000	0.000
83	A	83	ILE	0	0.002	-0.001	24.340	0.526	0.526	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.034	-0.012	22.711	0.343	0.343	0.000	0.000	0.000	0.000
85	A	85	ASN	0	0.025	-0.004	24.104	-0.236	-0.236	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.981	-0.972	24.585	-10.954	-10.954	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.025	0.005	21.815	-0.238	-0.238	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.079	-0.028	18.939	-0.729	-0.729	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.786	0.890	19.269	11.430	11.430	0.000	0.000	0.000	0.000
90	A	90	GLY	-1	-0.918	-0.946	20.077	-13.552	-13.552	0.000	0.000	0.000	0.000

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