FMO DATABASE

FMODB ID: 6556Z

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: 2025-10-06

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	89
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-597574.959561
FMO2-HF: Nuclear repulsion	563202.209619
FMO2-HF: Total energy	-34372.749942
FMO2-MP2: Total energy	-34474.959474

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.
71.599	72.495	11.145	-6.488	-5.553	-0.08

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 : 0.806 / 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	4	LYS	1	0.906	0.951	3.829	40.793	41.979	-0.005	-0.468	-0.713	0.000
23	A	24	ASP	-1	-0.730	-0.868	1.774	-119.730	-121.463	11.036	-5.563	-3.740	-0.078
24	A	25	ALA	0	-0.034	-0.019	2.726	11.116	12.076	0.116	-0.412	-0.664	-0.002
25	A	26	ARG	1	0.897	0.947	3.674	61.860	62.212	0.000	-0.039	-0.313	0.000
64	A	65	ALA	0	-0.078	-0.031	4.943	-6.044	-6.003	-0.001	-0.003	-0.038	0.000
65	A	66	LYS	1	0.953	0.966	4.685	36.297	36.387	-0.001	-0.003	-0.085	0.000
4	A	5	ILE	0	0.059	0.039	6.286	1.183	1.183	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.841	0.895	7.682	33.226	33.226	0.000	0.000	0.000	0.000
6	A	7	LEU	0	0.021	0.013	11.757	1.418	1.418	0.000	0.000	0.000	0.000
7	A	8	THR	0	-0.017	-0.010	14.148	-0.853	-0.853	0.000	0.000	0.000	0.000
8	A	9	ARG	1	0.824	0.920	15.948	15.235	15.235	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.043	0.014	19.407	0.056	0.056	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.038	0.024	22.675	0.071	0.071	0.000	0.000	0.000	0.000
11	A	12	SER	0	0.021	0.010	26.228	-0.126	-0.126	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.971	0.976	27.736	9.657	9.657	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.928	0.952	28.704	9.837	9.837	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.022	0.027	28.784	0.033	0.033	0.000	0.000	0.000	0.000
15	A	16	PRO	0	-0.005	0.000	24.063	-0.260	-0.260	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.070	0.041	23.616	0.086	0.086	0.000	0.000	0.000	0.000
17	A	18	TYR	0	-0.027	-0.029	19.030	-0.478	-0.478	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.926	0.959	17.464	16.055	16.055	0.000	0.000	0.000	0.000
19	A	20	ILE	0	-0.033	-0.012	15.961	-1.044	-1.044	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.006	-0.007	11.509	0.540	0.540	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.031	0.033	8.463	-2.161	-2.161	0.000	0.000	0.000	0.000
22	A	23	ALA	0	0.038	0.000	7.873	2.115	2.115	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.032	0.002	6.113	6.879	6.879	0.000	0.000	0.000	0.000
27	A	28	PRO	0	0.074	0.032	8.522	-0.380	-0.380	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.828	0.885	11.925	17.780	17.780	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.751	-0.852	13.247	-18.203	-18.203	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.021	0.022	14.024	1.146	1.146	0.000	0.000	0.000	0.000
31	A	32	ARG	1	0.926	0.971	9.683	26.508	26.508	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.017	0.004	11.139	-2.418	-2.418	0.000	0.000	0.000	0.000
33	A	34	ILE	0	-0.088	-0.033	6.780	-0.953	-0.953	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.771	-0.898	11.236	-18.286	-18.286	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.070	-0.045	13.645	-0.815	-0.815	0.000	0.000	0.000	0.000
36	A	37	ILE	0	0.083	0.075	13.324	0.877	0.877	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.064	0.028	17.429	1.044	1.044	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.099	-0.043	19.695	-0.133	-0.133	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.037	0.007	20.844	0.078	0.078	0.000	0.000	0.000	0.000
40	A	41	ASN	0	0.007	-0.009	22.706	-0.283	-0.283	0.000	0.000	0.000	0.000
41	A	42	PRO	0	-0.016	-0.009	23.835	0.292	0.292	0.000	0.000	0.000	0.000
42	A	43	THR	0	-0.011	0.005	26.575	0.232	0.232	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.045	-0.042	29.873	0.321	0.321	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.031	0.010	31.692	0.128	0.128	0.000	0.000	0.000	0.000
45	A	46	ASN	0	-0.022	-0.015	33.267	0.173	0.173	0.000	0.000	0.000	0.000
46	A	47	ALA	0	-0.004	0.024	30.080	-0.086	-0.086	0.000	0.000	0.000	0.000
47	A	48	PRO	0	0.022	0.004	25.100	-0.128	-0.128	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.841	-0.909	25.560	-11.159	-11.159	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.010	0.018	21.950	-0.341	-0.341	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.847	0.928	23.419	12.693	12.693	0.000	0.000	0.000	0.000
51	A	52	VAL	0	0.011	-0.017	18.820	-0.759	-0.759	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.804	-0.898	19.697	-15.211	-15.211	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.837	-0.912	19.478	-14.366	-14.366	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.059	0.034	18.946	-0.647	-0.647	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.041	-0.005	16.565	-0.552	-0.552	0.000	0.000	0.000	0.000
56	A	57	ALA	0	-0.028	-0.033	14.997	-1.407	-1.407	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.018	-0.003	13.978	-1.526	-1.526	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.914	0.989	13.437	19.650	19.650	0.000	0.000	0.000	0.000
59	A	60	TRP	0	-0.034	-0.030	9.353	-1.605	-1.605	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.063	-0.033	9.572	-2.607	-2.607	0.000	0.000	0.000	0.000
61	A	62	ASN	0	-0.034	-0.024	10.892	-0.100	-0.100	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.888	-0.928	9.731	-26.907	-26.907	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.012	0.005	5.860	-3.050	-3.050	0.000	0.000	0.000	0.000
66	A	67	PRO	0	0.053	0.021	7.235	-1.600	-1.600	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.027	-0.019	9.001	-0.978	-0.978	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.891	-0.939	10.718	-17.391	-17.391	0.000	0.000	0.000	0.000
69	A	70	THR	0	0.010	0.003	14.236	1.277	1.277	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.015	-0.020	12.153	0.806	0.806	0.000	0.000	0.000	0.000
71	A	72	HIS	0	0.014	0.019	13.772	-0.050	-0.050	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.024	0.017	15.372	1.009	1.009	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.031	-0.008	17.772	0.645	0.645	0.000	0.000	0.000	0.000
74	A	75	LEU	0	0.033	0.001	13.983	0.533	0.533	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.053	-0.024	18.242	0.606	0.606	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.895	0.956	20.529	12.671	12.671	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.919	-0.957	22.368	-12.631	-12.631	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.071	0.031	22.111	0.567	0.567	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.033	-0.015	17.000	-0.259	-0.259	0.000	0.000	0.000	0.000
80	A	81	MET	0	-0.028	-0.028	13.946	-0.680	-0.680	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.953	0.989	18.109	11.251	11.251	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.878	0.920	21.292	13.458	13.458	0.000	0.000	0.000	0.000
83	A	84	PHE	0	0.019	0.012	12.515	-0.108	-0.108	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.861	-0.923	18.155	-15.161	-15.161	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.900	-0.956	19.824	-12.066	-12.066	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.010	-0.007	17.988	-0.264	-0.264	0.000	0.000	0.000	0.000
87	A	88	LYS	1	0.828	0.919	16.284	15.483	15.483	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.805	0.888	18.996	11.694	11.694	0.000	0.000	0.000	0.000
89	A	90	ALA	-1	-0.913	-0.929	22.589	-11.974	-11.974	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)