FMO DATABASE

FMODB ID: MR8YZ

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-800118.745819
FMO2-HF: Nuclear repulsion	757224.485241
FMO2-HF: Total energy	-42894.260578
FMO2-MP2: Total energy	-43019.895326

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:1:MET)

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

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.
-135.965	-127.146	16.638	-12.021	-13.435	-0.135

Interaction energy analysis for fragmet #1(A:1:MET)

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 : 0.930

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	3	ALA	0	0.050	0.047	3.573	2.459	4.178	-0.002	-0.880	-0.838	-0.001
62	A	62	TYR	0	-0.063	-0.040	4.013	-0.604	-0.289	0.000	-0.032	-0.283	0.000
64	A	64	MET	0	-0.057	-0.020	2.242	-2.232	-2.061	1.521	-0.393	-1.298	-0.001
108	A	108	SER	0	0.024	0.013	4.085	-3.080	-2.967	-0.001	-0.055	-0.057	0.000
109	A	109	ASP	-1	-0.690	-0.850	1.992	-89.289	-87.233	4.857	-3.567	-3.346	-0.053
110	A	110	GLY	0	-0.073	-0.035	4.680	2.861	3.005	-0.001	-0.011	-0.132	0.000
111	A	111	LYS	1	0.781	0.896	3.325	54.142	55.046	0.045	-0.245	-0.703	-0.001
112	A	112	GLU	-2	-1.862	-1.930	1.874	-167.247	-163.850	10.219	-6.838	-6.778	-0.079
4	A	4	LYS	1	0.930	0.960	6.153	25.361	25.361	0.000	0.000	0.000	0.000
5	A	5	ALA	0	0.044	0.044	9.862	0.951	0.951	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.029	-0.031	13.405	0.277	0.277	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.015	0.017	16.669	0.543	0.543	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.956	0.967	19.947	13.380	13.380	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.015	-0.019	22.680	0.277	0.277	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.086	0.065	23.473	0.532	0.532	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.920	0.948	26.446	9.506	9.506	0.000	0.000	0.000	0.000
12	A	12	ILE	0	0.003	0.012	27.147	0.452	0.452	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.029	-0.014	28.662	-0.146	-0.146	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.079	0.025	27.047	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.959	0.974	27.301	9.202	9.202	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.939	0.963	29.176	9.039	9.039	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.030	0.032	23.723	0.060	0.060	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.912	0.945	23.748	12.086	12.086	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.004	0.010	24.666	-0.195	-0.195	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.016	0.010	23.746	0.035	0.035	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.035	-0.006	19.099	-0.271	-0.271	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.818	-0.898	20.157	-14.626	-14.626	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.052	-0.011	21.538	-0.144	-0.144	0.000	0.000	0.000	0.000
24	A	24	ILE	0	0.015	0.003	17.539	0.061	0.061	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.803	0.894	15.837	15.502	15.502	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.019	0.010	13.678	1.041	1.041	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.868	0.952	14.681	15.139	15.139	0.000	0.000	0.000	0.000
28	A	28	ASN	0	0.051	0.014	12.673	-1.261	-1.261	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.057	0.014	11.725	1.320	1.320	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.032	0.017	13.683	1.232	1.232	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.865	-0.936	16.895	-14.890	-14.890	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.036	-0.011	16.190	0.936	0.936	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.017	0.000	16.510	1.045	1.045	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.015	0.015	19.728	0.855	0.855	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.011	-0.003	20.637	0.779	0.779	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.064	-0.027	19.442	0.745	0.745	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.878	0.936	22.577	13.622	13.622	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.022	0.031	25.846	0.522	0.522	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.043	-0.012	25.916	0.414	0.414	0.000	0.000	0.000	0.000
40	A	40	ASN	0	0.028	0.017	28.605	-0.264	-0.264	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.894	0.940	28.662	10.295	10.295	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.026	-0.002	29.687	-0.163	-0.163	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.027	-0.046	26.020	0.008	0.008	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.040	0.030	24.894	-0.430	-0.430	0.000	0.000	0.000	0.000
45	A	45	PRO	0	0.071	0.038	24.259	-0.501	-0.501	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.080	-0.038	23.446	-0.090	-0.090	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.012	-0.022	19.651	-0.366	-0.366	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.830	-0.900	19.399	-14.771	-14.771	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.985	0.994	19.393	12.162	12.162	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.047	-0.024	15.974	-0.316	-0.316	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.024	0.007	14.798	-0.936	-0.936	0.000	0.000	0.000	0.000
52	A	52	MET	0	0.021	0.010	14.583	-1.138	-1.138	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.023	-0.005	15.042	-0.907	-0.907	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.033	-0.027	11.041	-0.663	-0.663	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.014	0.011	10.117	-2.119	-2.119	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.059	0.034	10.854	-0.917	-0.917	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.074	-0.050	9.417	0.519	0.519	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.017	-0.020	6.631	-1.442	-1.442	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.939	-0.964	7.086	-22.272	-22.272	0.000	0.000	0.000	0.000
60	A	60	HIS	0	-0.049	-0.033	9.789	1.073	1.073	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.051	-0.024	8.609	1.837	1.837	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.879	-0.910	5.306	-29.662	-29.662	0.000	0.000	0.000	0.000
65	A	65	ASN	0	0.047	0.012	6.487	5.127	5.127	0.000	0.000	0.000	0.000
66	A	66	THR	0	-0.005	-0.033	8.999	-1.352	-1.352	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.968	-0.961	10.742	-19.319	-19.319	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.917	-0.945	8.160	-32.081	-32.081	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.026	-0.008	6.182	-4.625	-4.625	0.000	0.000	0.000	0.000
70	A	70	VAL	0	-0.016	-0.011	7.959	4.333	4.333	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.016	-0.016	8.983	-2.903	-2.903	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.863	0.932	6.877	40.111	40.111	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.894	-0.950	11.053	-21.608	-21.608	0.000	0.000	0.000	0.000
74	A	74	ALA	0	0.067	0.020	13.464	-0.082	-0.082	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.050	-0.025	13.985	1.952	1.952	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.028	0.014	19.162	-0.011	-0.011	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.034	0.021	20.204	0.131	0.131	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.919	-0.981	23.286	-10.239	-10.239	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.019	0.015	26.155	-0.281	-0.281	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.019	0.017	27.489	0.346	0.346	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.040	-0.024	30.743	0.119	0.119	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.064	0.032	33.778	0.239	0.239	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.935	0.964	36.261	8.468	8.468	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.897	0.947	38.741	7.941	7.941	0.000	0.000	0.000	0.000
85	A	85	PHE	0	0.086	0.040	42.351	-0.053	-0.053	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.933	0.964	45.854	6.653	6.653	0.000	0.000	0.000	0.000
87	A	87	PRO	0	0.060	0.039	48.065	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.914	0.956	48.656	6.376	6.376	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.096	0.034	53.150	0.060	0.060	0.000	0.000	0.000	0.000
90	A	90	GLN	0	0.047	0.024	56.925	-0.112	-0.112	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.063	0.043	57.296	0.014	0.014	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.903	0.966	53.532	5.550	5.550	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.035	0.016	49.939	-0.061	-0.061	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.028	-0.027	47.486	0.011	0.011	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.034	0.019	42.926	-0.038	-0.038	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.018	-0.010	40.191	-0.087	-0.087	0.000	0.000	0.000	0.000
97	A	97	ASN	0	0.005	-0.005	36.571	-0.110	-0.110	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.930	0.969	35.583	7.854	7.854	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.907	0.959	31.491	9.361	9.361	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.001	0.001	28.503	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.019	-0.007	24.579	0.055	0.055	0.000	0.000	0.000	0.000
102	A	102	HIS	0	-0.020	0.003	21.072	-0.106	-0.106	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.007	0.001	19.040	-0.101	-0.101	0.000	0.000	0.000	0.000
104	A	104	THR	0	0.024	0.012	14.117	-0.070	-0.070	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.036	-0.009	12.486	0.836	0.836	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.016	-0.002	8.713	0.420	0.420	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.013	-0.003	7.878	1.997	1.997	0.000	0.000	0.000	0.000

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