FMO DATABASE

FMODB ID: 8G7ZY

Calculation Name: 6FXC-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6FXC

Chain ID: A

ChEMBL ID:

UniProt ID: Q2YSH7

Base Structure: ElectronMicroscopy

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	97
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-632343.863646
FMO2-HF: Nuclear repulsion	594534.896724
FMO2-HF: Total energy	-37808.966922
FMO2-MP2: Total energy	-37921.442729

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:6:ILE)

Summations of interaction energy for fragment #1(A:6: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.
-134.673	-122.34	23.796	-14.981	-21.146	-0.156

Interaction energy analysis for fragmet #1(A:6:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.805 / q_NPA : 0.892

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	8	ILE	0	0.038	0.038	2.305	1.175	2.991	2.159	-1.128	-2.846	-0.002
4	A	9	ARG	1	0.940	0.977	4.170	33.043	33.149	0.000	-0.022	-0.084	0.000
70	A	75	ASP	-1	-0.910	-0.953	3.372	-48.925	-48.079	0.035	-0.295	-0.585	-0.001
71	A	76	ILE	0	0.029	0.013	2.183	5.166	5.113	4.110	-0.835	-3.222	-0.002
72	A	77	VAL	0	-0.033	-0.036	2.573	-16.376	-13.510	1.065	-1.924	-2.006	-0.025
73	A	78	ASN	0	0.010	0.028	4.444	1.827	1.900	-0.001	-0.004	-0.068	0.000
74	A	79	PRO	0	-0.012	-0.010	2.513	-0.323	0.241	0.827	-0.237	-1.153	0.001
75	A	80	THR	0	0.031	0.031	4.295	3.126	3.165	0.000	-0.024	-0.016	0.000
82	A	87	LEU	0	-0.088	-0.033	3.212	-0.772	-0.358	0.037	-0.080	-0.371	0.000
95	A	100	ILE	0	-0.004	-0.018	4.298	-4.991	-4.912	-0.001	-0.008	-0.070	0.000
96	A	101	LYS	1	0.881	0.948	2.931	62.153	63.157	0.063	-0.323	-0.745	-0.002
97	A	102	LEU	-1	-0.781	-0.884	1.862	-137.009	-132.430	15.502	-10.101	-9.980	-0.125
5	A	10	LEU	0	0.045	0.015	7.833	0.948	0.948	0.000	0.000	0.000	0.000
6	A	11	LYS	1	0.879	0.932	10.556	19.429	19.429	0.000	0.000	0.000	0.000
7	A	12	ALA	0	0.121	0.064	14.212	0.206	0.206	0.000	0.000	0.000	0.000
8	A	13	TYR	0	0.019	0.013	17.676	0.083	0.083	0.000	0.000	0.000	0.000
9	A	14	ASP	-1	-0.804	-0.875	20.781	-11.514	-11.514	0.000	0.000	0.000	0.000
10	A	15	HIS	0	-0.003	-0.006	19.766	-0.820	-0.820	0.000	0.000	0.000	0.000
11	A	16	ARG	1	0.870	0.898	19.752	11.135	11.135	0.000	0.000	0.000	0.000
12	A	17	VAL	0	0.032	0.021	18.546	-0.176	-0.176	0.000	0.000	0.000	0.000
13	A	18	ILE	0	-0.007	0.002	13.336	-0.638	-0.638	0.000	0.000	0.000	0.000
14	A	19	ASP	-1	-0.940	-0.954	14.895	-16.207	-16.207	0.000	0.000	0.000	0.000
15	A	20	GLN	0	0.028	0.007	16.080	-0.391	-0.391	0.000	0.000	0.000	0.000
16	A	21	SER	0	-0.007	-0.022	13.774	-0.147	-0.147	0.000	0.000	0.000	0.000
17	A	22	ALA	0	-0.028	-0.009	11.488	-1.389	-1.389	0.000	0.000	0.000	0.000
18	A	23	GLU	-1	-0.904	-0.961	12.067	-17.584	-17.584	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.938	0.988	10.798	21.079	21.079	0.000	0.000	0.000	0.000
20	A	25	ILE	0	-0.037	-0.009	6.150	-0.318	-0.318	0.000	0.000	0.000	0.000
21	A	26	VAL	0	0.038	0.019	9.486	-1.252	-1.252	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.947	-0.957	11.042	-16.353	-16.353	0.000	0.000	0.000	0.000
23	A	28	THR	0	-0.019	-0.042	11.347	-0.900	-0.900	0.000	0.000	0.000	0.000
24	A	29	ALA	0	-0.014	-0.005	7.538	-0.481	-0.481	0.000	0.000	0.000	0.000
25	A	30	LYS	1	0.886	0.917	9.335	18.791	18.791	0.000	0.000	0.000	0.000
26	A	31	ARG	1	0.857	0.944	12.178	19.812	19.812	0.000	0.000	0.000	0.000
27	A	32	SER	0	-0.062	-0.047	10.077	1.367	1.367	0.000	0.000	0.000	0.000
28	A	33	GLY	0	-0.002	0.001	11.130	0.100	0.100	0.000	0.000	0.000	0.000
29	A	34	ALA	0	0.001	-0.007	7.652	-2.179	-2.179	0.000	0.000	0.000	0.000
30	A	35	ASP	-1	-0.794	-0.910	6.418	-30.301	-30.301	0.000	0.000	0.000	0.000
31	A	36	VAL	0	-0.059	-0.028	7.215	-1.311	-1.311	0.000	0.000	0.000	0.000
32	A	37	SER	0	0.000	0.025	7.486	3.429	3.429	0.000	0.000	0.000	0.000
33	A	38	GLY	0	0.008	-0.005	8.657	-1.245	-1.245	0.000	0.000	0.000	0.000
34	A	39	PRO	0	0.010	-0.001	10.635	-1.023	-1.023	0.000	0.000	0.000	0.000
35	A	40	ILE	0	0.017	0.021	11.373	1.745	1.745	0.000	0.000	0.000	0.000
36	A	41	PRO	0	-0.044	-0.038	12.976	-0.775	-0.775	0.000	0.000	0.000	0.000
37	A	42	LEU	0	-0.010	0.003	11.597	-0.121	-0.121	0.000	0.000	0.000	0.000
38	A	43	PRO	0	-0.008	-0.005	15.748	0.679	0.679	0.000	0.000	0.000	0.000
39	A	44	THR	0	-0.056	-0.034	18.716	-0.280	-0.280	0.000	0.000	0.000	0.000
40	A	45	GLU	-1	-0.899	-0.939	19.166	-15.304	-15.304	0.000	0.000	0.000	0.000
41	A	46	LYS	1	0.914	0.954	21.397	10.858	10.858	0.000	0.000	0.000	0.000
42	A	47	SER	0	0.026	0.024	24.893	-0.067	-0.067	0.000	0.000	0.000	0.000
43	A	48	VAL	0	-0.035	-0.024	27.675	0.033	0.033	0.000	0.000	0.000	0.000
44	A	49	TYR	0	0.025	0.021	27.979	0.107	0.107	0.000	0.000	0.000	0.000
45	A	50	THR	0	-0.017	-0.022	33.821	0.125	0.125	0.000	0.000	0.000	0.000
46	A	51	ILE	0	0.002	0.023	37.465	0.075	0.075	0.000	0.000	0.000	0.000
47	A	52	ILE	0	0.019	-0.009	39.967	0.044	0.044	0.000	0.000	0.000	0.000
48	A	53	ARG	1	0.886	0.923	42.757	7.095	7.095	0.000	0.000	0.000	0.000
49	A	54	ALA	0	-0.051	-0.009	44.956	0.080	0.080	0.000	0.000	0.000	0.000
50	A	55	VAL	0	0.023	0.010	47.301	-0.067	-0.067	0.000	0.000	0.000	0.000
51	A	56	HIS	0	0.007	-0.009	48.727	0.015	0.015	0.000	0.000	0.000	0.000
52	A	57	LYS	1	0.934	0.990	50.498	5.608	5.608	0.000	0.000	0.000	0.000
53	A	58	TYR	0	0.000	-0.014	50.262	0.039	0.039	0.000	0.000	0.000	0.000
54	A	59	LYS	0	0.124	0.086	46.094	-0.183	-0.183	0.000	0.000	0.000	0.000
55	A	60	ASP	-1	-0.953	-0.984	47.941	-6.294	-6.294	0.000	0.000	0.000	0.000
56	A	61	SER	0	-0.016	0.008	46.982	-0.056	-0.056	0.000	0.000	0.000	0.000
57	A	62	ARG	1	0.873	0.896	41.984	7.246	7.246	0.000	0.000	0.000	0.000
58	A	63	GLU	-1	-0.829	-0.889	38.456	-7.653	-7.653	0.000	0.000	0.000	0.000
59	A	64	GLN	0	-0.047	-0.018	35.676	-0.118	-0.118	0.000	0.000	0.000	0.000
60	A	65	PHE	0	0.043	0.010	33.020	0.045	0.045	0.000	0.000	0.000	0.000
61	A	66	GLU	-1	-0.948	-0.978	29.024	-9.962	-9.962	0.000	0.000	0.000	0.000
62	A	67	GLN	0	-0.011	0.003	23.831	-0.213	-0.213	0.000	0.000	0.000	0.000
63	A	68	ARG	1	0.965	0.952	23.690	11.125	11.125	0.000	0.000	0.000	0.000
64	A	69	THR	0	-0.009	0.013	18.208	-0.366	-0.366	0.000	0.000	0.000	0.000
65	A	70	HIS	0	-0.015	-0.018	18.236	-0.289	-0.289	0.000	0.000	0.000	0.000
66	A	71	LYS	0	0.064	0.049	13.784	-0.499	-0.499	0.000	0.000	0.000	0.000
67	A	72	ARG	1	0.941	0.962	11.238	18.441	18.441	0.000	0.000	0.000	0.000
68	A	73	LEU	0	-0.020	-0.014	6.820	-1.254	-1.254	0.000	0.000	0.000	0.000
69	A	74	ILE	0	0.045	0.032	5.110	2.588	2.588	0.000	0.000	0.000	0.000
76	A	81	PRO	0	0.023	-0.002	7.455	-1.372	-1.372	0.000	0.000	0.000	0.000
77	A	82	LYS	1	0.867	0.924	9.613	19.506	19.506	0.000	0.000	0.000	0.000
78	A	83	THR	0	-0.018	0.011	5.458	-0.743	-0.743	0.000	0.000	0.000	0.000
79	A	84	VAL	0	0.031	0.009	5.275	-0.590	-0.590	0.000	0.000	0.000	0.000
80	A	85	ASP	-1	-0.765	-0.861	7.209	-18.689	-18.689	0.000	0.000	0.000	0.000
81	A	86	ALA	0	-0.017	-0.007	7.931	1.292	1.292	0.000	0.000	0.000	0.000
83	A	88	MET	0	0.013	-0.005	7.740	0.252	0.252	0.000	0.000	0.000	0.000
84	A	89	GLY	0	0.014	0.027	10.944	1.655	1.655	0.000	0.000	0.000	0.000
85	A	90	LEU	0	-0.029	-0.015	12.671	-0.294	-0.294	0.000	0.000	0.000	0.000
86	A	91	ASN	0	-0.040	-0.038	13.704	1.960	1.960	0.000	0.000	0.000	0.000
87	A	92	LEU	0	-0.004	-0.001	14.494	-0.770	-0.770	0.000	0.000	0.000	0.000
88	A	93	PRO	0	0.022	0.023	16.549	-0.295	-0.295	0.000	0.000	0.000	0.000
89	A	94	SER	0	-0.036	-0.016	17.474	0.289	0.289	0.000	0.000	0.000	0.000
90	A	95	GLY	0	0.036	0.006	19.289	0.507	0.507	0.000	0.000	0.000	0.000
91	A	96	VAL	0	-0.071	-0.035	13.471	0.036	0.036	0.000	0.000	0.000	0.000
92	A	97	ASP	-1	-0.903	-0.940	14.142	-19.266	-19.266	0.000	0.000	0.000	0.000
93	A	98	ILE	0	-0.008	-0.025	7.734	-0.771	-0.771	0.000	0.000	0.000	0.000
94	A	99	GLU	-1	-0.929	-0.957	8.476	-30.071	-30.071	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ILE)