FMO DATABASE

FMODB ID: 8KQQY

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	80
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-518378.977306
FMO2-HF: Nuclear repulsion	486170.756827
FMO2-HF: Total energy	-32208.220479
FMO2-MP2: Total energy	-32303.84976

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:5:ASN)

Summations of interaction energy for fragment #1(A:5:ASN)

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.
140.651	142.306	0.01	-0.842	-0.824	-0.003

Interaction energy analysis for fragmet #1(A:5:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.841 / q_NPA : 0.910

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	7	ARG	1	0.920	0.964	3.414	36.625	38.280	0.010	-0.842	-0.824	-0.003
4	A	8	LYS	1	0.918	0.959	6.260	35.342	35.342	0.000	0.000	0.000	0.000
5	A	9	VAL	0	0.030	0.008	9.423	0.757	0.757	0.000	0.000	0.000	0.000
6	A	10	TYR	0	-0.014	-0.003	12.040	0.855	0.855	0.000	0.000	0.000	0.000
7	A	11	VAL	0	0.096	0.044	15.326	-0.086	-0.086	0.000	0.000	0.000	0.000
8	A	12	GLY	0	-0.036	-0.021	18.949	0.107	0.107	0.000	0.000	0.000	0.000
9	A	13	LYS	1	0.909	0.960	22.009	10.788	10.788	0.000	0.000	0.000	0.000
10	A	14	VAL	0	-0.025	0.002	25.205	-0.046	-0.046	0.000	0.000	0.000	0.000
11	A	15	VAL	0	-0.069	-0.034	26.921	0.378	0.378	0.000	0.000	0.000	0.000
12	A	16	SER	0	0.001	-0.025	28.711	0.398	0.398	0.000	0.000	0.000	0.000
13	A	17	ASP	-1	-0.829	-0.888	28.847	-10.873	-10.873	0.000	0.000	0.000	0.000
14	A	18	LYS	1	0.888	0.937	29.764	10.543	10.543	0.000	0.000	0.000	0.000
15	A	19	MET	0	0.044	0.018	30.367	-0.190	-0.190	0.000	0.000	0.000	0.000
16	A	20	ASP	-1	-0.923	-0.959	28.768	-11.145	-11.145	0.000	0.000	0.000	0.000
17	A	21	LYS	1	0.832	0.944	22.289	13.796	13.796	0.000	0.000	0.000	0.000
18	A	22	THR	0	-0.085	-0.063	24.196	-0.651	-0.651	0.000	0.000	0.000	0.000
19	A	23	ILE	0	0.080	0.066	23.332	0.437	0.437	0.000	0.000	0.000	0.000
20	A	24	THR	0	-0.085	-0.053	23.858	-0.590	-0.590	0.000	0.000	0.000	0.000
21	A	25	VAL	0	0.031	0.022	20.058	0.461	0.461	0.000	0.000	0.000	0.000
22	A	26	LEU	0	-0.049	-0.030	23.208	-0.110	-0.110	0.000	0.000	0.000	0.000
23	A	27	VAL	0	0.046	0.027	18.471	-0.024	-0.024	0.000	0.000	0.000	0.000
24	A	28	GLU	-1	-0.856	-0.924	21.728	-10.575	-10.575	0.000	0.000	0.000	0.000
25	A	29	THR	0	0.017	0.010	20.485	-0.172	-0.172	0.000	0.000	0.000	0.000
26	A	30	TYR	0	0.029	0.000	23.256	0.683	0.683	0.000	0.000	0.000	0.000
27	A	31	LYS	1	0.894	0.985	24.210	11.098	11.098	0.000	0.000	0.000	0.000
28	A	32	THR	0	0.043	0.007	25.343	0.456	0.456	0.000	0.000	0.000	0.000
29	A	33	HIS	0	-0.002	0.003	27.939	-0.248	-0.248	0.000	0.000	0.000	0.000
30	A	34	LYS	1	0.966	0.973	29.330	10.057	10.057	0.000	0.000	0.000	0.000
31	A	35	LEU	0	0.001	0.007	30.499	-0.026	-0.026	0.000	0.000	0.000	0.000
32	A	36	TYR	0	0.055	0.009	34.216	0.071	0.071	0.000	0.000	0.000	0.000
33	A	37	GLY	0	0.036	0.037	31.686	0.103	0.103	0.000	0.000	0.000	0.000
34	A	38	LYS	1	0.964	0.989	32.132	8.581	8.581	0.000	0.000	0.000	0.000
35	A	39	ARG	1	0.959	0.983	26.364	10.738	10.738	0.000	0.000	0.000	0.000
36	A	40	VAL	0	-0.025	-0.019	29.084	0.354	0.354	0.000	0.000	0.000	0.000
37	A	41	LYS	1	0.884	0.939	27.545	9.913	9.913	0.000	0.000	0.000	0.000
38	A	42	TYR	0	-0.019	-0.040	21.386	0.264	0.264	0.000	0.000	0.000	0.000
39	A	43	SER	0	0.078	0.033	25.151	-0.277	-0.277	0.000	0.000	0.000	0.000
40	A	44	LYS	1	0.893	0.950	21.145	13.798	13.798	0.000	0.000	0.000	0.000
41	A	45	LYS	1	0.982	1.003	22.857	10.540	10.540	0.000	0.000	0.000	0.000
42	A	46	TYR	0	-0.016	-0.008	17.675	-0.102	-0.102	0.000	0.000	0.000	0.000
43	A	47	LYS	1	0.953	0.978	21.042	12.354	12.354	0.000	0.000	0.000	0.000
44	A	48	THR	0	-0.043	-0.028	18.631	-1.078	-1.078	0.000	0.000	0.000	0.000
45	A	49	HIS	-1	-0.807	-0.923	18.922	-14.242	-14.242	0.000	0.000	0.000	0.000
46	A	50	ASP	-1	-0.809	-0.894	20.120	-13.627	-13.627	0.000	0.000	0.000	0.000
47	A	51	GLU	-1	-0.820	-0.932	19.557	-15.511	-15.511	0.000	0.000	0.000	0.000
48	A	52	ASN	0	-0.018	-0.005	23.434	0.154	0.154	0.000	0.000	0.000	0.000
49	A	53	ASN	0	-0.046	-0.021	26.788	0.351	0.351	0.000	0.000	0.000	0.000
50	A	54	SER	0	0.020	0.006	25.788	0.373	0.373	0.000	0.000	0.000	0.000
51	A	55	ALA	0	-0.024	-0.011	25.375	0.243	0.243	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.927	0.952	27.502	9.998	9.998	0.000	0.000	0.000	0.000
53	A	57	LEU	0	-0.032	-0.040	29.939	-0.285	-0.285	0.000	0.000	0.000	0.000
54	A	58	GLY	0	0.062	0.035	30.705	0.257	0.257	0.000	0.000	0.000	0.000
55	A	59	ASP	0	0.047	0.032	25.769	-0.336	-0.336	0.000	0.000	0.000	0.000
56	A	60	ILE	0	-0.053	-0.012	24.071	-0.095	-0.095	0.000	0.000	0.000	0.000
57	A	61	VAL	0	0.026	0.022	20.385	-0.214	-0.214	0.000	0.000	0.000	0.000
58	A	62	LYS	1	0.960	0.987	14.916	19.118	19.118	0.000	0.000	0.000	0.000
59	A	63	ILE	0	-0.037	-0.022	15.800	0.131	0.131	0.000	0.000	0.000	0.000
60	A	64	GLN	0	-0.015	-0.008	8.672	0.317	0.317	0.000	0.000	0.000	0.000
61	A	65	GLU	-1	-0.864	-0.928	7.961	-29.944	-29.944	0.000	0.000	0.000	0.000
62	A	66	THR	0	-0.047	-0.040	10.403	-3.245	-3.245	0.000	0.000	0.000	0.000
63	A	67	ARG	1	0.981	1.007	11.456	19.132	19.132	0.000	0.000	0.000	0.000
64	A	68	PRO	0	-0.002	-0.017	13.037	0.658	0.658	0.000	0.000	0.000	0.000
65	A	69	LEU	0	0.027	0.017	16.359	0.087	0.087	0.000	0.000	0.000	0.000
66	A	70	SER	0	0.018	0.009	19.088	0.954	0.954	0.000	0.000	0.000	0.000
67	A	71	ALA	0	0.067	0.043	21.128	-0.602	-0.602	0.000	0.000	0.000	0.000
68	A	72	THR	0	-0.012	-0.017	22.327	-0.403	-0.403	0.000	0.000	0.000	0.000
69	A	73	LYS	1	0.917	0.990	19.938	13.739	13.739	0.000	0.000	0.000	0.000
70	A	74	ARG	1	0.869	0.916	14.746	16.376	16.376	0.000	0.000	0.000	0.000
71	A	75	PHE	0	-0.008	0.001	13.480	-1.548	-1.548	0.000	0.000	0.000	0.000
72	A	76	ARG	1	0.944	0.983	11.981	24.516	24.516	0.000	0.000	0.000	0.000
73	A	77	LEU	0	0.062	0.020	16.567	-0.632	-0.632	0.000	0.000	0.000	0.000
74	A	78	VAL	0	-0.115	-0.063	14.211	-1.221	-1.221	0.000	0.000	0.000	0.000
75	A	79	GLU	-1	-0.882	-0.948	17.173	-15.584	-15.584	0.000	0.000	0.000	0.000
76	A	80	ILE	0	-0.006	-0.011	19.822	-0.059	-0.059	0.000	0.000	0.000	0.000
77	A	81	VAL	0	-0.008	0.028	21.614	0.131	0.131	0.000	0.000	0.000	0.000
78	A	82	GLU	-1	-0.865	-0.948	24.335	-11.520	-11.520	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.988	-1.009	27.688	-10.879	-10.879	0.000	0.000	0.000	0.000
80	A	84	SER	-1	-0.967	-0.970	30.237	-9.241	-9.241	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ASN)