FMO DATABASE

FMODB ID: LR3N9

Calculation Name: 1F3U-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1F3U

Chain ID: A

ChEMBL ID:

UniProt ID: P35269

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-780199.813956
FMO2-HF: Nuclear repulsion	736279.088247
FMO2-HF: Total energy	-43920.725709
FMO2-MP2: Total energy	-44050.925425

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:ALA)

Summations of interaction energy for fragment #1(A:2: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.
-84.148	-84.054	16.935	-9.713	-7.314	-0.108

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.771 / q_NPA : 0.861

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	ARG	1	0.975	0.976	3.851	31.003	32.406	-0.021	-0.696	-0.685	0.000
5	A	6	GLU	-1	-0.870	-0.899	1.831	-125.626	-127.259	16.957	-8.968	-6.356	-0.108
6	A	7	LEU	0	-0.008	0.002	5.275	1.103	1.160	-0.001	-0.002	-0.054	0.000
7	A	8	ASP	-1	-0.809	-0.898	4.774	-45.926	-45.812	-0.001	-0.011	-0.102	0.000
102	A	103	LYS	1	0.803	0.916	3.630	42.225	42.378	0.001	-0.036	-0.117	0.000
4	A	5	GLY	0	0.039	0.020	7.062	2.095	2.095	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.015	-0.004	6.147	5.762	5.762	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.021	-0.020	7.670	4.410	4.410	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.062	0.042	10.179	2.226	2.226	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.025	0.014	13.054	1.842	1.842	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.949	0.963	11.879	24.813	24.813	0.000	0.000	0.000	0.000
13	A	14	GLN	0	-0.047	-0.013	13.322	0.198	0.198	0.000	0.000	0.000	0.000
14	A	15	ASN	0	-0.051	-0.019	16.104	1.116	1.116	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.025	-0.016	15.735	1.018	1.018	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.001	0.010	18.421	-0.089	-0.089	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.000	-0.002	19.469	0.161	0.161	0.000	0.000	0.000	0.000
18	A	19	TRP	0	0.003	-0.014	22.477	0.607	0.607	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.013	0.013	24.645	-0.281	-0.281	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.018	-0.018	26.509	0.407	0.407	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.875	0.942	29.249	8.591	8.591	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.025	0.003	30.575	0.244	0.244	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.007	0.011	33.200	-0.025	-0.025	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.986	0.992	31.487	9.492	9.492	0.000	0.000	0.000	0.000
25	A	26	TYR	0	0.090	0.034	35.519	-0.168	-0.168	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.017	0.025	34.870	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.050	-0.034	31.119	-0.177	-0.177	0.000	0.000	0.000	0.000
28	A	29	GLN	0	-0.005	-0.024	32.428	-0.218	-0.218	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.015	-0.009	34.842	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	31	TRP	0	-0.024	-0.034	29.525	-0.151	-0.151	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.021	-0.010	31.030	-0.141	-0.141	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.814	0.914	32.045	7.900	7.900	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.003	0.014	31.354	0.191	0.191	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.014	0.007	32.348	-0.081	-0.081	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.025	0.007	32.172	-0.063	-0.063	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.932	0.964	28.854	9.299	9.299	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.016	0.019	27.990	-0.367	-0.367	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.961	-0.983	29.370	-9.489	-9.489	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.036	0.011	30.887	0.265	0.265	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.024	-0.001	33.343	0.316	0.316	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.889	0.947	33.424	8.508	8.508	0.000	0.000	0.000	0.000
42	A	43	LEU	0	0.013	0.021	30.404	0.155	0.155	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.952	0.976	33.829	7.547	7.547	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.013	-0.002	32.053	-0.038	-0.038	0.000	0.000	0.000	0.000
45	A	46	ALA	0	-0.011	0.003	36.659	0.065	0.065	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.945	0.964	34.830	8.696	8.696	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.042	0.021	41.141	0.107	0.107	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.021	0.002	43.635	-0.154	-0.154	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.006	0.004	43.842	0.074	0.074	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.820	0.894	42.995	7.088	7.088	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.018	-0.018	36.795	-0.097	-0.097	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.837	-0.878	40.047	-7.115	-7.115	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.008	-0.004	34.141	-0.136	-0.136	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.021	-0.011	37.055	0.048	0.048	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.015	0.010	33.143	-0.203	-0.203	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.004	0.009	36.470	0.290	0.290	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.012	0.002	36.442	-0.208	-0.208	0.000	0.000	0.000	0.000
58	A	59	ASN	0	0.038	0.014	35.445	0.267	0.267	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.902	-0.961	38.519	-6.902	-6.902	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.872	-0.922	38.100	-7.772	-7.772	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.000	-0.011	34.556	0.100	0.100	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.058	-0.011	39.109	0.072	0.072	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.049	-0.041	42.300	0.330	0.330	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.005	0.021	38.812	0.121	0.121	0.000	0.000	0.000	0.000
65	A	66	HIS	0	0.013	0.018	42.187	-0.126	-0.126	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.834	-0.906	41.856	-7.462	-7.462	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.027	-0.037	44.787	0.135	0.135	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.034	0.011	48.239	0.025	0.025	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.047	-0.013	49.110	0.102	0.102	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.855	0.945	46.126	6.648	6.648	0.000	0.000	0.000	0.000
71	A	72	PRO	0	0.043	0.020	50.415	0.099	0.099	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.030	0.003	53.698	0.008	0.008	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.013	0.000	53.655	-0.137	-0.137	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.051	0.028	49.853	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.097	-0.056	49.659	-0.179	-0.179	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.051	0.029	46.889	0.003	0.003	0.000	0.000	0.000	0.000
77	A	78	PRO	0	0.009	-0.006	41.901	0.008	0.008	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.937	0.979	43.353	6.536	6.536	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.880	-0.919	41.075	-7.609	-7.609	0.000	0.000	0.000	0.000
80	A	81	HIS	0	0.022	0.009	38.236	0.122	0.122	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.034	0.021	38.655	-0.256	-0.256	0.000	0.000	0.000	0.000
82	A	83	PHE	0	-0.005	-0.039	31.803	-0.161	-0.161	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.022	-0.003	37.413	0.139	0.139	0.000	0.000	0.000	0.000
84	A	85	LEU	0	0.009	-0.003	33.934	-0.250	-0.250	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.015	-0.019	32.981	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	87	SER	0	0.021	0.002	32.794	-0.316	-0.316	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.042	0.007	26.359	0.009	0.009	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.007	0.008	28.895	-0.195	-0.195	0.000	0.000	0.000	0.000
89	A	90	GLY	0	-0.007	0.009	30.388	0.016	0.016	0.000	0.000	0.000	0.000
90	A	91	GLN	0	-0.024	-0.027	25.927	0.181	0.181	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.001	0.012	21.247	-0.126	-0.126	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.017	-0.008	22.103	-0.115	-0.115	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.006	-0.002	16.841	0.250	0.250	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.005	0.002	16.599	0.467	0.467	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.030	-0.014	12.675	-0.717	-0.717	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.063	-0.050	11.789	0.838	0.838	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.884	-0.951	11.429	-22.565	-22.565	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.054	-0.026	9.114	1.335	1.335	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.009	-0.029	11.728	-0.282	-0.282	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.038	-0.010	8.383	1.230	1.230	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.885	-0.938	8.846	-25.816	-25.816	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.061	0.033	6.880	3.513	3.513	0.000	0.000	0.000	0.000
104	A	105	SER	0	-0.056	-0.057	6.720	-6.473	-6.473	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.006	-0.006	9.022	3.047	3.047	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.791	-0.854	11.607	-24.231	-24.231	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.000	-0.012	13.845	0.601	0.601	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.038	-0.010	16.960	-0.141	-0.141	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.033	-0.018	20.091	0.448	0.448	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.002	-0.001	23.401	0.294	0.294	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.066	-0.030	26.070	0.548	0.548	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.941	0.985	27.905	10.179	10.179	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.022	0.012	30.142	0.338	0.338	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.846	-0.904	32.265	-8.662	-8.662	0.000	0.000	0.000	0.000
115	A	116	CYS	0	-0.045	0.003	34.332	0.314	0.314	0.000	0.000	0.000	0.000
116	A	117	ARG	1	0.884	0.931	36.045	7.928	7.928	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.000	-0.022	39.632	-0.080	-0.080	0.000	0.000	0.000	0.000
118	A	119	ALA	-1	-0.925	-0.940	41.721	-6.865	-6.865	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:2:ALA)