FMO DATABASE

FMODB ID: 3K5GL

Calculation Name: 2FL4-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FL4

Chain ID: A

ChEMBL ID:

UniProt ID: Q836M4

Base Structure: X-ray

Registration Date: 2025-10-04

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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1379444.617131
FMO2-HF: Nuclear repulsion	1318658.54697
FMO2-HF: Total energy	-60786.070161
FMO2-MP2: Total energy	-60961.985639

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:0:GLY)

Summations of interaction energy for fragment #1(A:0: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.
-139.071	-133.608	6.658	-6.886	-5.235	-0.094

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.799 / q_NPA : 0.888

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	2	GLU	-1	-0.844	-0.923	1.937	-114.273	-108.894	6.659	-6.880	-5.158	-0.094
4	A	3	ILE	0	0.004	0.004	5.201	5.840	5.924	-0.001	-0.006	-0.077	0.000
5	A	4	HIS	1	0.821	0.898	8.816	30.292	30.292	0.000	0.000	0.000	0.000
6	A	5	PHE	0	0.037	0.019	11.513	0.080	0.080	0.000	0.000	0.000	0.000
7	A	6	GLU	-1	-0.845	-0.914	14.133	-21.506	-21.506	0.000	0.000	0.000	0.000
8	A	7	LYS	1	0.943	0.969	17.377	14.799	14.799	0.000	0.000	0.000	0.000
9	A	8	VAL	0	0.056	0.036	20.890	-0.392	-0.392	0.000	0.000	0.000	0.000
10	A	9	THR	0	-0.001	-0.003	21.982	0.615	0.615	0.000	0.000	0.000	0.000
11	A	10	SER	0	-0.023	-0.047	24.558	0.123	0.123	0.000	0.000	0.000	0.000
12	A	11	ASP	-1	-0.902	-0.929	21.540	-13.530	-13.530	0.000	0.000	0.000	0.000
13	A	12	ASN	0	-0.006	-0.009	18.294	0.491	0.491	0.000	0.000	0.000	0.000
14	A	13	ARG	1	0.927	0.984	21.018	10.999	10.999	0.000	0.000	0.000	0.000
15	A	14	LYS	1	0.921	0.963	24.013	11.131	11.131	0.000	0.000	0.000	0.000
16	A	15	ALA	0	-0.023	0.002	19.099	0.093	0.093	0.000	0.000	0.000	0.000
17	A	16	VAL	0	-0.021	-0.012	19.919	-0.225	-0.225	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.860	-0.954	21.881	-11.592	-11.592	0.000	0.000	0.000	0.000
19	A	18	ASN	0	-0.099	-0.049	23.076	0.724	0.724	0.000	0.000	0.000	0.000
20	A	19	LEU	0	0.010	0.012	18.246	-0.607	-0.607	0.000	0.000	0.000	0.000
21	A	20	GLN	0	-0.039	-0.023	20.219	0.650	0.650	0.000	0.000	0.000	0.000
22	A	21	VAL	0	0.036	0.035	21.338	-0.333	-0.333	0.000	0.000	0.000	0.000
23	A	22	PHE	0	-0.005	-0.018	23.445	0.769	0.769	0.000	0.000	0.000	0.000
24	A	23	ALA	0	-0.024	-0.021	24.954	-0.253	-0.253	0.000	0.000	0.000	0.000
25	A	24	GLU	-1	-0.870	-0.927	21.667	-14.634	-14.634	0.000	0.000	0.000	0.000
26	A	25	GLN	0	-0.046	-0.039	26.065	0.462	0.462	0.000	0.000	0.000	0.000
27	A	26	GLN	0	0.014	0.002	26.812	0.338	0.338	0.000	0.000	0.000	0.000
28	A	27	ALA	0	0.076	0.050	24.558	0.155	0.155	0.000	0.000	0.000	0.000
29	A	28	PHE	0	-0.046	-0.017	26.611	0.254	0.254	0.000	0.000	0.000	0.000
30	A	29	ILE	0	-0.011	0.004	29.823	0.319	0.319	0.000	0.000	0.000	0.000
31	A	30	GLU	-1	-0.908	-0.956	27.580	-10.528	-10.528	0.000	0.000	0.000	0.000
32	A	31	SER	0	-0.042	-0.036	27.903	0.024	0.024	0.000	0.000	0.000	0.000
33	A	32	MET	0	-0.046	0.003	30.024	0.272	0.272	0.000	0.000	0.000	0.000
34	A	33	ALA	0	0.006	0.004	32.629	0.314	0.314	0.000	0.000	0.000	0.000
35	A	34	GLU	-1	-0.813	-0.889	30.205	-9.989	-9.989	0.000	0.000	0.000	0.000
36	A	35	ASN	0	-0.026	-0.036	32.864	0.060	0.060	0.000	0.000	0.000	0.000
37	A	36	LEU	0	-0.031	-0.011	34.883	0.285	0.285	0.000	0.000	0.000	0.000
38	A	37	LYS	1	0.851	0.918	32.470	10.141	10.141	0.000	0.000	0.000	0.000
39	A	38	GLU	-1	-0.920	-0.969	32.059	-9.912	-9.912	0.000	0.000	0.000	0.000
40	A	39	SER	0	-0.066	-0.039	36.754	0.225	0.225	0.000	0.000	0.000	0.000
41	A	40	ASP	-1	-0.985	-0.969	40.094	-7.479	-7.479	0.000	0.000	0.000	0.000
42	A	41	GLN	0	-0.033	-0.012	39.087	0.174	0.174	0.000	0.000	0.000	0.000
43	A	42	PHE	0	-0.022	-0.013	35.979	0.062	0.062	0.000	0.000	0.000	0.000
44	A	43	PRO	0	0.005	-0.010	41.650	0.055	0.055	0.000	0.000	0.000	0.000
45	A	44	GLU	-1	-0.966	-0.970	41.809	-7.666	-7.666	0.000	0.000	0.000	0.000
46	A	45	TRP	0	-0.045	-0.029	35.700	-0.055	-0.055	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.847	-0.894	43.022	-6.655	-6.655	0.000	0.000	0.000	0.000
48	A	47	SER	0	0.033	-0.008	40.620	-0.228	-0.228	0.000	0.000	0.000	0.000
49	A	48	ALA	0	-0.017	0.003	43.081	0.176	0.176	0.000	0.000	0.000	0.000
50	A	49	GLY	0	0.004	0.005	43.447	-0.206	-0.206	0.000	0.000	0.000	0.000
51	A	50	ILE	0	-0.046	-0.025	43.388	0.212	0.212	0.000	0.000	0.000	0.000
52	A	51	TYR	0	0.021	-0.012	45.964	-0.144	-0.144	0.000	0.000	0.000	0.000
53	A	52	ASP	-1	-0.860	-0.901	48.768	-6.207	-6.207	0.000	0.000	0.000	0.000
54	A	53	GLY	0	0.005	-0.001	51.234	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	54	ASN	0	-0.009	-0.012	52.228	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	55	GLN	0	-0.077	-0.028	45.449	-0.024	-0.024	0.000	0.000	0.000	0.000
57	A	56	LEU	0	0.014	0.014	42.029	0.021	0.021	0.000	0.000	0.000	0.000
58	A	57	ILE	0	-0.008	-0.007	44.197	-0.103	-0.103	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.000	-0.009	41.274	-0.141	-0.141	0.000	0.000	0.000	0.000
60	A	59	TYR	0	-0.009	-0.009	37.305	0.006	0.006	0.000	0.000	0.000	0.000
61	A	60	ALA	0	-0.011	-0.007	40.795	-0.063	-0.063	0.000	0.000	0.000	0.000
62	A	61	MET	0	0.000	0.019	37.161	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	62	TYR	0	-0.067	-0.061	41.005	-0.068	-0.068	0.000	0.000	0.000	0.000
64	A	63	GLY	0	0.088	0.040	43.191	0.040	0.040	0.000	0.000	0.000	0.000
65	A	64	ARG	1	0.837	0.937	44.558	6.832	6.832	0.000	0.000	0.000	0.000
66	A	65	TRP	0	0.128	0.078	36.419	0.055	0.055	0.000	0.000	0.000	0.000
67	A	66	GLN	0	-0.077	-0.023	42.376	0.111	0.111	0.000	0.000	0.000	0.000
68	A	67	ASP	-1	-0.939	-0.977	43.088	-7.203	-7.203	0.000	0.000	0.000	0.000
69	A	68	GLY	0	-0.033	-0.041	46.558	0.164	0.164	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.801	0.874	44.084	7.379	7.379	0.000	0.000	0.000	0.000
71	A	70	VAL	0	0.000	-0.003	45.885	-0.091	-0.091	0.000	0.000	0.000	0.000
72	A	71	TRP	0	0.011	0.001	39.437	0.066	0.066	0.000	0.000	0.000	0.000
73	A	72	LEU	0	-0.049	-0.024	41.628	0.110	0.110	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.842	-0.928	37.952	-8.273	-8.273	0.000	0.000	0.000	0.000
75	A	74	ARG	1	0.871	0.937	32.072	9.436	9.436	0.000	0.000	0.000	0.000
76	A	75	PHE	0	-0.003	-0.004	37.760	0.309	0.309	0.000	0.000	0.000	0.000
77	A	76	LEU	0	-0.005	0.003	34.619	-0.232	-0.232	0.000	0.000	0.000	0.000
78	A	77	ILE	0	-0.022	-0.013	38.757	0.274	0.274	0.000	0.000	0.000	0.000
79	A	78	ASP	-1	-0.776	-0.856	38.641	-8.486	-8.486	0.000	0.000	0.000	0.000
80	A	79	GLN	0	0.044	0.012	34.634	0.362	0.362	0.000	0.000	0.000	0.000
81	A	80	ARG	1	0.828	0.886	38.636	7.993	7.993	0.000	0.000	0.000	0.000
82	A	81	PHE	0	0.033	0.022	41.855	0.185	0.185	0.000	0.000	0.000	0.000
83	A	82	GLN	0	-0.012	-0.011	36.970	0.164	0.164	0.000	0.000	0.000	0.000
84	A	83	GLY	0	-0.019	-0.014	42.144	0.078	0.078	0.000	0.000	0.000	0.000
85	A	84	GLN	0	-0.053	-0.029	44.111	0.277	0.277	0.000	0.000	0.000	0.000
86	A	85	GLY	0	-0.012	-0.003	47.148	0.122	0.122	0.000	0.000	0.000	0.000
87	A	86	TYR	0	-0.005	-0.034	46.165	-0.029	-0.029	0.000	0.000	0.000	0.000
88	A	87	GLY	0	0.040	0.022	44.369	0.036	0.036	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.886	0.941	45.279	6.564	6.564	0.000	0.000	0.000	0.000
90	A	89	ALA	0	-0.021	-0.007	47.948	0.092	0.092	0.000	0.000	0.000	0.000
91	A	90	ALA	0	0.045	0.019	46.643	0.086	0.086	0.000	0.000	0.000	0.000
92	A	91	CYS	0	0.014	0.022	45.484	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.973	0.984	47.268	6.204	6.204	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.011	-0.008	50.892	0.100	0.100	0.000	0.000	0.000	0.000
95	A	94	LEU	0	0.011	0.016	45.317	0.088	0.088	0.000	0.000	0.000	0.000
96	A	95	MET	0	-0.012	-0.003	48.312	-0.021	-0.021	0.000	0.000	0.000	0.000
97	A	96	LEU	0	0.020	0.000	50.388	0.071	0.071	0.000	0.000	0.000	0.000
98	A	97	LYS	1	0.906	0.946	51.567	6.145	6.145	0.000	0.000	0.000	0.000
99	A	98	LEU	0	-0.024	-0.003	46.866	0.036	0.036	0.000	0.000	0.000	0.000
100	A	99	ILE	0	-0.022	-0.012	51.410	0.012	0.012	0.000	0.000	0.000	0.000
101	A	100	GLU	-1	-0.938	-0.943	54.292	-5.647	-5.647	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.864	0.938	50.697	6.495	6.495	0.000	0.000	0.000	0.000
103	A	102	TYR	0	0.012	0.003	48.516	0.021	0.021	0.000	0.000	0.000	0.000
104	A	103	GLN	0	-0.005	-0.010	54.325	-0.013	-0.013	0.000	0.000	0.000	0.000
105	A	104	THR	0	-0.029	0.004	50.937	0.092	0.092	0.000	0.000	0.000	0.000
106	A	105	ASN	0	0.067	0.026	54.345	-0.023	-0.023	0.000	0.000	0.000	0.000
107	A	106	LYS	1	0.823	0.907	50.220	6.335	6.335	0.000	0.000	0.000	0.000
108	A	107	LEU	0	-0.033	-0.002	47.357	-0.040	-0.040	0.000	0.000	0.000	0.000
109	A	108	TYR	0	-0.034	-0.026	43.144	0.067	0.067	0.000	0.000	0.000	0.000
110	A	109	LEU	0	0.013	0.010	40.261	-0.029	-0.029	0.000	0.000	0.000	0.000
111	A	110	SER	0	0.007	-0.010	35.469	0.146	0.146	0.000	0.000	0.000	0.000
112	A	111	VAL	0	-0.043	-0.026	35.814	0.005	0.005	0.000	0.000	0.000	0.000
113	A	112	TYR	0	0.033	0.032	26.535	0.058	0.058	0.000	0.000	0.000	0.000
114	A	113	ASP	-1	-0.855	-0.927	33.141	-9.095	-9.095	0.000	0.000	0.000	0.000
115	A	114	THR	0	0.015	0.007	29.871	0.282	0.282	0.000	0.000	0.000	0.000
116	A	115	ASN	0	0.038	0.032	33.202	0.303	0.303	0.000	0.000	0.000	0.000
117	A	116	SER	0	0.007	-0.025	35.261	0.324	0.324	0.000	0.000	0.000	0.000
118	A	117	SER	0	-0.055	-0.040	38.045	0.286	0.286	0.000	0.000	0.000	0.000
119	A	118	ALA	0	0.036	0.035	38.199	0.233	0.233	0.000	0.000	0.000	0.000
120	A	119	ILE	0	0.033	0.024	37.438	0.239	0.239	0.000	0.000	0.000	0.000
121	A	120	ARG	1	0.941	0.972	39.973	8.070	8.070	0.000	0.000	0.000	0.000
122	A	121	LEU	0	-0.062	-0.019	43.095	0.234	0.234	0.000	0.000	0.000	0.000
123	A	122	TYR	0	0.097	0.020	39.822	0.143	0.143	0.000	0.000	0.000	0.000
124	A	123	GLN	0	0.032	0.025	44.297	0.163	0.163	0.000	0.000	0.000	0.000
125	A	124	GLN	0	-0.039	-0.013	47.053	0.278	0.278	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.096	-0.053	47.391	0.153	0.153	0.000	0.000	0.000	0.000
127	A	126	GLY	0	0.029	0.020	49.969	0.090	0.090	0.000	0.000	0.000	0.000
128	A	127	PHE	0	-0.007	-0.014	45.465	0.039	0.039	0.000	0.000	0.000	0.000
129	A	128	VAL	0	-0.004	-0.012	46.821	-0.036	-0.036	0.000	0.000	0.000	0.000
130	A	129	PHE	0	-0.021	-0.019	39.412	-0.061	-0.061	0.000	0.000	0.000	0.000
131	A	130	ASN	0	-0.010	-0.025	43.818	-0.023	-0.023	0.000	0.000	0.000	0.000
132	A	131	GLY	0	-0.023	-0.005	43.060	0.102	0.102	0.000	0.000	0.000	0.000
133	A	132	GLU	-1	-0.783	-0.831	41.181	-7.551	-7.551	0.000	0.000	0.000	0.000
134	A	133	LEU	0	-0.050	-0.035	34.987	-0.129	-0.129	0.000	0.000	0.000	0.000
135	A	134	ASP	-1	-0.747	-0.859	35.087	-8.847	-8.847	0.000	0.000	0.000	0.000
136	A	135	THR	0	-0.070	-0.047	32.851	-0.355	-0.355	0.000	0.000	0.000	0.000
137	A	136	ASN	0	0.005	-0.010	29.902	-0.217	-0.217	0.000	0.000	0.000	0.000
138	A	137	GLY	0	-0.053	-0.035	29.926	-0.368	-0.368	0.000	0.000	0.000	0.000
139	A	138	GLU	-1	-0.836	-0.891	32.084	-9.870	-9.870	0.000	0.000	0.000	0.000
140	A	139	ARG	1	0.823	0.906	33.913	8.701	8.701	0.000	0.000	0.000	0.000
141	A	140	VAL	0	0.027	0.021	37.459	-0.021	-0.021	0.000	0.000	0.000	0.000
142	A	141	MET	0	-0.092	-0.051	40.228	0.183	0.183	0.000	0.000	0.000	0.000
143	A	142	GLU	-1	-0.760	-0.862	43.245	-6.768	-6.768	0.000	0.000	0.000	0.000
144	A	143	TRP	0	-0.008	-0.009	46.596	0.070	0.070	0.000	0.000	0.000	0.000
145	A	144	THR	0	-0.015	-0.019	49.492	0.004	0.004	0.000	0.000	0.000	0.000
146	A	145	HIS	0	-0.042	-0.011	52.947	0.035	0.035	0.000	0.000	0.000	0.000
147	A	146	GLN	-1	-0.942	-0.973	55.866	-5.481	-5.481	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)