FMO DATABASE

FMODB ID: QMY2Y

Calculation Name: 3FCD-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3FCD

Chain ID: A

ChEMBL ID:

UniProt ID: Q93AH5

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1047837.548161
FMO2-HF: Nuclear repulsion	997274.140775
FMO2-HF: Total energy	-50563.407386
FMO2-MP2: Total energy	-50709.360662

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:4:ILE)

Summations of interaction energy for fragment #1(A:4:ILE)

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.
-141.392	-134.472	6.411	-4.049	-9.28	-0.031

Interaction energy analysis for fragmet #1(A:4:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.829 / q_NPA : 0.902

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	6	GLN	0	0.043	0.014	3.567	5.731	8.372	0.012	-1.142	-1.511	-0.006
4	A	7	ILE	0	-0.001	-0.007	3.816	-4.307	-3.706	0.011	-0.112	-0.500	0.000
67	A	70	ILE	0	0.005	0.007	2.459	-3.372	-2.823	1.608	-0.462	-1.694	-0.004
68	A	71	ASP	-1	-0.735	-0.818	4.728	-32.329	-32.140	-0.001	-0.022	-0.166	0.000
69	A	72	VAL	0	-0.095	-0.068	2.169	-21.370	-20.105	3.824	-1.845	-3.245	-0.017
70	A	73	SER	0	0.019	0.003	3.194	8.350	8.798	0.011	-0.145	-0.313	-0.001
71	A	74	ASP	-1	-0.843	-0.909	4.703	-36.381	-36.244	-0.001	-0.005	-0.130	0.000
75	A	78	LEU	0	-0.072	-0.027	2.699	-0.669	-0.093	0.895	-0.232	-1.239	-0.003
116	A	119	PHE	0	0.004	0.000	3.089	-4.389	-3.875	0.052	-0.084	-0.482	0.000
5	A	8	THR	0	0.011	0.028	5.828	2.657	2.657	0.000	0.000	0.000	0.000
6	A	9	PRO	0	0.027	0.015	9.318	0.225	0.225	0.000	0.000	0.000	0.000
7	A	10	PHE	0	0.007	-0.010	12.391	-0.090	-0.090	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.011	0.017	14.554	0.781	0.781	0.000	0.000	0.000	0.000
9	A	12	HIS	0	0.003	-0.012	16.924	0.437	0.437	0.000	0.000	0.000	0.000
10	A	13	ILE	0	-0.028	-0.018	21.041	0.415	0.415	0.000	0.000	0.000	0.000
11	A	14	PRO	0	0.012	-0.020	23.959	0.109	0.109	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.751	-0.880	26.980	-9.641	-9.641	0.000	0.000	0.000	0.000
13	A	16	MET	0	-0.007	0.004	21.544	-0.346	-0.346	0.000	0.000	0.000	0.000
14	A	17	GLN	0	0.004	0.017	25.965	-0.425	-0.425	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.891	-0.933	28.438	-9.642	-9.642	0.000	0.000	0.000	0.000
16	A	19	ALA	0	-0.005	-0.002	23.168	-0.132	-0.132	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.006	-0.013	22.399	-0.400	-0.400	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.006	-0.008	24.804	0.018	0.018	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.030	-0.001	23.733	0.111	0.111	0.000	0.000	0.000	0.000
20	A	23	PHE	0	0.018	-0.020	19.775	-0.159	-0.159	0.000	0.000	0.000	0.000
21	A	24	CYS	0	-0.037	-0.016	22.069	-0.520	-0.520	0.000	0.000	0.000	0.000
22	A	25	ASP	-1	-0.898	-0.948	23.719	-10.789	-10.789	0.000	0.000	0.000	0.000
23	A	26	THR	0	-0.096	-0.040	26.225	0.439	0.439	0.000	0.000	0.000	0.000
24	A	27	LEU	0	-0.073	-0.039	21.429	0.013	0.013	0.000	0.000	0.000	0.000
25	A	28	GLY	0	0.004	0.020	21.738	-0.430	-0.430	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.042	-0.041	15.138	-0.526	-0.526	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.860	-0.918	19.008	-14.382	-14.382	0.000	0.000	0.000	0.000
28	A	31	LEU	0	-0.024	-0.023	18.820	-0.833	-0.833	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.788	0.898	16.128	17.164	17.164	0.000	0.000	0.000	0.000
30	A	33	TYR	0	0.002	-0.005	17.884	0.097	0.097	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.917	0.957	19.788	11.516	11.516	0.000	0.000	0.000	0.000
32	A	35	HIS	0	-0.002	0.010	22.052	0.385	0.385	0.000	0.000	0.000	0.000
33	A	36	SER	0	-0.017	-0.010	22.989	-0.132	-0.132	0.000	0.000	0.000	0.000
34	A	37	ASN	0	0.009	0.004	23.797	-0.080	-0.080	0.000	0.000	0.000	0.000
35	A	38	TYR	0	0.036	0.025	14.664	-0.462	-0.462	0.000	0.000	0.000	0.000
36	A	39	ALA	0	0.003	-0.012	19.203	0.419	0.419	0.000	0.000	0.000	0.000
37	A	40	TYR	0	-0.054	-0.035	11.537	-1.167	-1.167	0.000	0.000	0.000	0.000
38	A	41	LEU	0	0.026	-0.001	15.691	0.929	0.929	0.000	0.000	0.000	0.000
39	A	42	GLU	-1	-0.817	-0.887	12.891	-23.037	-23.037	0.000	0.000	0.000	0.000
40	A	43	LEU	0	0.022	0.031	14.712	1.174	1.174	0.000	0.000	0.000	0.000
41	A	44	SER	0	-0.017	-0.023	14.756	-0.571	-0.571	0.000	0.000	0.000	0.000
42	A	45	GLY	0	0.004	0.007	13.322	-0.672	-0.672	0.000	0.000	0.000	0.000
43	A	46	CYS	0	-0.075	-0.023	10.311	-2.432	-2.432	0.000	0.000	0.000	0.000
44	A	47	GLY	0	0.028	0.010	9.912	1.937	1.937	0.000	0.000	0.000	0.000
45	A	48	LEU	0	-0.052	-0.034	11.131	-0.591	-0.591	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.807	0.868	9.066	26.609	26.609	0.000	0.000	0.000	0.000
47	A	50	LEU	0	-0.005	0.001	14.951	0.518	0.518	0.000	0.000	0.000	0.000
48	A	51	LEU	0	-0.004	-0.005	18.575	-0.130	-0.130	0.000	0.000	0.000	0.000
49	A	52	GLU	-1	-0.838	-0.937	20.844	-10.818	-10.818	0.000	0.000	0.000	0.000
50	A	53	GLU	-1	-0.732	-0.832	24.704	-10.187	-10.187	0.000	0.000	0.000	0.000
51	A	54	PRO	0	-0.035	0.002	23.020	0.311	0.311	0.000	0.000	0.000	0.000
52	A	55	ALA	0	0.010	-0.022	25.113	-0.264	-0.264	0.000	0.000	0.000	0.000
53	A	56	ARG	1	0.775	0.881	27.130	9.733	9.733	0.000	0.000	0.000	0.000
54	A	57	LYS	1	0.808	0.888	28.695	10.430	10.430	0.000	0.000	0.000	0.000
55	A	58	ILE	0	-0.027	0.023	25.983	0.212	0.212	0.000	0.000	0.000	0.000
56	A	59	ILE	0	-0.007	-0.019	29.979	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	60	PRO	0	-0.059	-0.029	33.127	0.184	0.184	0.000	0.000	0.000	0.000
58	A	61	ASP	-1	-0.855	-0.935	30.090	-9.929	-9.929	0.000	0.000	0.000	0.000
59	A	62	GLY	0	-0.018	-0.017	28.884	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	63	ILE	0	-0.074	-0.023	24.230	-0.283	-0.283	0.000	0.000	0.000	0.000
61	A	64	ALA	0	0.027	0.023	21.877	-0.178	-0.178	0.000	0.000	0.000	0.000
62	A	65	ARG	1	0.834	0.908	19.890	12.850	12.850	0.000	0.000	0.000	0.000
63	A	66	VAL	0	-0.013	0.005	13.569	-0.356	-0.356	0.000	0.000	0.000	0.000
64	A	67	ALA	0	0.049	0.034	14.577	0.356	0.356	0.000	0.000	0.000	0.000
65	A	68	ILE	0	-0.026	-0.018	8.183	-0.672	-0.672	0.000	0.000	0.000	0.000
66	A	69	CYS	0	-0.032	0.003	8.672	1.160	1.160	0.000	0.000	0.000	0.000
72	A	75	ILE	0	0.034	0.019	6.173	-2.177	-2.177	0.000	0.000	0.000	0.000
73	A	76	ASP	-1	-0.754	-0.837	7.169	-21.382	-21.382	0.000	0.000	0.000	0.000
74	A	77	SER	0	-0.011	-0.023	8.514	2.500	2.500	0.000	0.000	0.000	0.000
76	A	79	HIS	0	0.029	0.000	6.190	2.746	2.746	0.000	0.000	0.000	0.000
77	A	80	THR	0	-0.015	-0.003	8.784	2.342	2.342	0.000	0.000	0.000	0.000
78	A	81	LYS	1	0.886	0.940	6.698	29.726	29.726	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.020	-0.015	5.061	0.616	0.616	0.000	0.000	0.000	0.000
80	A	83	SER	0	0.029	0.018	9.345	1.523	1.523	0.000	0.000	0.000	0.000
81	A	84	PRO	0	0.014	0.009	12.763	0.665	0.665	0.000	0.000	0.000	0.000
82	A	85	ALA	0	-0.041	-0.020	11.545	0.836	0.836	0.000	0.000	0.000	0.000
83	A	86	LEU	0	-0.016	-0.016	9.964	0.473	0.473	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.923	-0.969	13.742	-14.610	-14.610	0.000	0.000	0.000	0.000
85	A	88	ASN	0	-0.113	-0.048	16.627	1.417	1.417	0.000	0.000	0.000	0.000
86	A	89	LEU	0	-0.034	-0.001	13.349	0.248	0.248	0.000	0.000	0.000	0.000
87	A	90	PRO	0	-0.012	-0.006	17.912	0.447	0.447	0.000	0.000	0.000	0.000
88	A	91	ALA	0	0.037	0.009	19.411	-0.498	-0.498	0.000	0.000	0.000	0.000
89	A	92	ASP	-1	-0.923	-0.961	20.265	-12.774	-12.774	0.000	0.000	0.000	0.000
90	A	93	GLN	0	-0.071	-0.041	17.563	-0.513	-0.513	0.000	0.000	0.000	0.000
91	A	94	VAL	0	-0.002	-0.006	13.297	-1.183	-1.183	0.000	0.000	0.000	0.000
92	A	95	GLU	-1	-0.929	-0.941	14.585	-14.221	-14.221	0.000	0.000	0.000	0.000
93	A	96	PRO	0	-0.019	-0.020	13.984	-1.273	-1.273	0.000	0.000	0.000	0.000
94	A	97	LEU	0	-0.057	-0.028	10.228	-0.210	-0.210	0.000	0.000	0.000	0.000
95	A	98	LYS	1	0.927	0.967	14.020	16.667	16.667	0.000	0.000	0.000	0.000
96	A	99	ASN	0	0.016	0.011	14.919	-2.070	-2.070	0.000	0.000	0.000	0.000
97	A	100	MET	0	-0.014	0.002	15.554	1.323	1.323	0.000	0.000	0.000	0.000
98	A	101	PRO	0	-0.011	-0.014	18.114	-0.168	-0.168	0.000	0.000	0.000	0.000
99	A	102	TYR	0	-0.077	-0.063	15.095	1.090	1.090	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.034	0.020	16.999	-0.666	-0.666	0.000	0.000	0.000	0.000
101	A	104	GLN	0	-0.022	-0.026	10.212	-0.338	-0.338	0.000	0.000	0.000	0.000
102	A	105	ARG	1	0.783	0.852	11.813	22.382	22.382	0.000	0.000	0.000	0.000
103	A	106	GLU	-1	-0.773	-0.850	10.485	-24.319	-24.319	0.000	0.000	0.000	0.000
104	A	107	PHE	0	0.011	0.005	6.887	1.018	1.018	0.000	0.000	0.000	0.000
105	A	108	GLN	0	-0.015	-0.018	10.100	-0.913	-0.913	0.000	0.000	0.000	0.000
106	A	109	VAL	0	0.012	0.002	10.241	0.429	0.429	0.000	0.000	0.000	0.000
107	A	110	ARG	1	0.880	0.957	12.679	13.143	13.143	0.000	0.000	0.000	0.000
108	A	111	MET	0	-0.028	-0.009	12.913	-1.232	-1.232	0.000	0.000	0.000	0.000
109	A	112	PRO	0	-0.008	-0.027	15.288	0.835	0.835	0.000	0.000	0.000	0.000
110	A	113	ASP	-1	-0.875	-0.931	17.317	-15.149	-15.149	0.000	0.000	0.000	0.000
111	A	114	GLY	0	-0.047	-0.012	19.143	0.696	0.696	0.000	0.000	0.000	0.000
112	A	115	ASP	-1	-0.809	-0.903	17.050	-14.155	-14.155	0.000	0.000	0.000	0.000
113	A	116	TRP	0	-0.009	-0.012	14.591	-0.649	-0.649	0.000	0.000	0.000	0.000
114	A	117	LEU	0	-0.004	-0.003	7.249	-0.365	-0.365	0.000	0.000	0.000	0.000
115	A	118	ASN	0	0.009	0.006	9.763	1.386	1.386	0.000	0.000	0.000	0.000
117	A	120	THR	0	-0.019	-0.051	6.500	3.149	3.149	0.000	0.000	0.000	0.000
118	A	121	ALA	0	0.035	0.017	6.821	-5.416	-5.416	0.000	0.000	0.000	0.000
119	A	122	PRO	0	0.055	0.035	8.753	2.602	2.602	0.000	0.000	0.000	0.000
120	A	123	LEU	0	-0.025	0.004	11.768	-0.852	-0.852	0.000	0.000	0.000	0.000
121	A	124	ALA	0	0.030	0.027	12.654	-0.195	-0.195	0.000	0.000	0.000	0.000
122	A	125	GLU	-1	-0.859	-0.944	14.002	-19.265	-19.265	0.000	0.000	0.000	0.000
123	A	126	GLY	0	-0.052	-0.024	17.170	0.147	0.147	0.000	0.000	0.000	0.000
124	A	127	HIS	0	-0.070	-0.038	17.868	0.949	0.949	0.000	0.000	0.000	0.000
125	A	128	HIS	0	-0.025	-0.011	19.717	0.004	0.004	0.000	0.000	0.000	0.000
126	A	129	HIS	0	-0.060	-0.022	15.492	1.704	1.704	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ILE)