FMO DATABASE

FMODB ID: 9L762

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1272127.175638
FMO2-HF: Nuclear repulsion	1215158.156107
FMO2-HF: Total energy	-56969.019531
FMO2-MP2: Total energy	-57136.479387

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.
6.184	7.817	-0.019	-0.667	-0.947	-0.002

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 : 0.874 / q_NPA : 0.914

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	GLN	0	0.103	0.053	3.805	2.095	3.728	-0.019	-0.667	-0.947	-0.002
4	A	4	THR	0	-0.012	-0.013	5.909	-0.159	-0.159	0.000	0.000	0.000	0.000
5	A	5	PHE	0	0.013	0.024	7.401	-1.018	-1.018	0.000	0.000	0.000	0.000
6	A	6	MET	0	-0.012	-0.003	7.445	-0.351	-0.351	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.021	0.016	10.390	0.802	0.802	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.014	-0.018	13.695	-0.323	-0.323	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.752	-0.868	15.927	-12.625	-12.625	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.090	-0.047	18.772	-0.530	-0.530	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.037	-0.017	14.470	0.385	0.385	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.062	-0.032	17.913	-0.483	-0.483	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.877	-0.931	20.521	-11.190	-11.190	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.721	0.846	21.789	12.513	12.513	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.804	0.899	26.349	10.147	10.147	0.000	0.000	0.000	0.000
16	A	16	TRP	0	0.014	-0.016	29.545	-0.029	-0.029	0.000	0.000	0.000	0.000
17	A	17	TYR	-1	-0.798	-0.886	28.711	-10.020	-10.020	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.010	-0.013	33.897	0.056	0.056	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.021	-0.009	34.049	-0.059	-0.059	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.868	-0.925	38.121	-7.361	-7.361	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.042	-0.046	40.820	-0.121	-0.121	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.972	-0.992	42.338	-6.396	-6.396	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.023	0.017	44.963	-0.063	-0.063	0.000	0.000	0.000	0.000
24	A	24	GLN	0	0.024	0.024	40.534	-0.254	-0.254	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.004	-0.007	41.169	0.011	0.011	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.024	0.015	39.215	-0.188	-0.188	0.000	0.000	0.000	0.000
27	A	27	GLY	0	-0.028	-0.009	36.777	-0.187	-0.187	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.946	0.971	35.303	7.907	7.907	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.106	0.060	35.070	-0.208	-0.208	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.046	-0.050	34.318	-0.180	-0.180	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.025	-0.003	30.735	-0.311	-0.311	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.884	-0.929	29.953	-10.092	-10.092	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.056	0.034	29.755	-0.377	-0.377	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.005	-0.001	28.442	-0.264	-0.264	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.106	-0.060	25.542	-0.570	-0.570	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.054	0.037	24.939	-0.571	-0.571	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.005	0.002	25.747	-0.363	-0.363	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.876	0.935	19.448	13.238	13.238	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.084	0.043	21.172	-0.678	-0.678	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.820	0.907	19.843	13.469	13.469	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.070	0.038	21.823	-0.601	-0.601	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.812	0.900	19.730	12.091	12.091	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.041	0.015	17.123	-0.531	-0.531	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.005	0.000	15.786	-0.976	-0.976	0.000	0.000	0.000	0.000
45	A	45	TYR	0	-0.016	-0.010	15.245	0.086	0.086	0.000	0.000	0.000	0.000
46	A	46	THR	0	0.017	-0.005	11.341	-1.085	-1.085	0.000	0.000	0.000	0.000
47	A	47	PRO	0	-0.019	-0.004	12.292	0.880	0.880	0.000	0.000	0.000	0.000
48	A	48	HIS	0	-0.006	-0.011	11.556	-0.315	-0.315	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.004	-0.004	14.873	0.348	0.348	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.894	-0.947	17.311	-12.366	-12.366	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.007	0.018	17.453	0.640	0.640	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.083	0.017	20.188	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.808	-0.872	23.494	-11.312	-11.312	0.000	0.000	0.000	0.000
54	A	54	TYR	0	-0.044	-0.012	27.094	-0.126	-0.126	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.006	0.002	30.316	0.073	0.073	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.001	0.005	32.951	0.085	0.085	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.021	-0.018	36.253	0.014	0.014	0.000	0.000	0.000	0.000
58	A	58	ILE	0	0.054	0.026	38.840	0.127	0.127	0.000	0.000	0.000	0.000
59	A	59	ASN	0	0.085	0.051	42.363	0.069	0.069	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.045	0.022	42.716	0.160	0.160	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.027	-0.031	44.019	0.050	0.050	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.900	0.949	46.669	6.312	6.312	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.050	0.046	41.788	-0.067	-0.067	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.863	-0.931	44.919	-6.329	-6.329	0.000	0.000	0.000	0.000
65	A	65	PHE	0	-0.043	-0.048	43.148	-0.220	-0.220	0.000	0.000	0.000	0.000
66	A	66	THR	0	0.061	0.038	44.629	0.099	0.099	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.017	0.012	47.216	-0.095	-0.095	0.000	0.000	0.000	0.000
68	A	68	ASN	0	0.093	0.041	49.745	0.016	0.016	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.803	0.911	42.848	7.007	7.007	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.912	-0.973	46.918	-6.071	-6.071	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.068	0.037	49.530	0.028	0.028	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.887	-0.944	48.607	-6.097	-6.097	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.854	0.917	40.053	7.382	7.382	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.022	0.010	45.788	-0.015	-0.015	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.003	-0.002	39.563	-0.230	-0.230	0.000	0.000	0.000	0.000
76	A	76	TYR	0	0.008	-0.008	42.485	0.158	0.158	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.949	0.969	41.711	6.546	6.546	0.000	0.000	0.000	0.000
78	A	78	HIS	0	0.058	0.032	41.886	0.097	0.097	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.022	-0.012	42.371	-0.093	-0.093	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.001	0.006	39.313	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	81	HIS	0	-0.010	-0.004	43.196	0.126	0.126	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.041	0.004	46.963	-0.050	-0.050	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.037	0.022	49.209	0.082	0.082	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.013	0.011	47.655	0.048	0.048	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.041	-0.020	44.605	-0.164	-0.164	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.943	0.964	46.454	6.301	6.301	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.003	-0.006	46.283	-0.128	-0.128	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.001	0.011	45.990	0.099	0.099	0.000	0.000	0.000	0.000
89	A	89	THR	0	0.051	0.033	46.956	-0.142	-0.142	0.000	0.000	0.000	0.000
90	A	90	ALA	0	0.003	0.000	45.193	-0.035	-0.035	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.027	0.020	46.636	-0.057	-0.057	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.907	-0.952	49.963	-5.783	-5.783	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.010	-0.025	43.612	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.852	0.931	47.389	6.311	6.311	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.877	0.951	48.451	5.754	5.754	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.037	-0.015	50.225	0.065	0.065	0.000	0.000	0.000	0.000
97	A	97	ASN	0	-0.034	-0.018	44.595	-0.181	-0.181	0.000	0.000	0.000	0.000
98	A	98	PRO	0	0.054	0.027	45.259	-0.120	-0.120	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.763	-0.884	41.987	-6.956	-6.956	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.948	0.968	40.485	6.798	6.798	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.057	-0.015	40.262	-0.156	-0.156	0.000	0.000	0.000	0.000
102	A	102	ILE	0	0.047	0.040	37.658	-0.159	-0.159	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.917	-0.960	36.166	-8.321	-8.321	0.000	0.000	0.000	0.000
104	A	104	ASN	0	-0.047	-0.036	35.202	-0.333	-0.333	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.060	-0.035	35.076	-0.159	-0.159	0.000	0.000	0.000	0.000
106	A	106	ILE	0	0.033	0.019	31.476	-0.219	-0.219	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.895	0.947	30.833	8.695	8.695	0.000	0.000	0.000	0.000
108	A	108	GLY	0	-0.021	-0.004	30.189	-0.253	-0.253	0.000	0.000	0.000	0.000
109	A	109	MET	0	-0.079	-0.022	29.306	-0.086	-0.086	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.021	0.006	26.126	-0.513	-0.513	0.000	0.000	0.000	0.000
111	A	111	PRO	0	-0.033	-0.008	21.792	0.107	0.107	0.000	0.000	0.000	0.000
112	A	112	SER	0	0.070	0.027	24.489	0.014	0.014	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.014	-0.013	20.412	0.050	0.050	0.000	0.000	0.000	0.000
114	A	114	ARG	1	0.981	0.967	21.548	12.201	12.201	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.001	0.021	18.566	0.282	0.282	0.000	0.000	0.000	0.000
116	A	116	GLY	0	0.040	0.033	22.283	0.169	0.169	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.887	-0.955	24.456	-9.560	-9.560	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.861	0.938	24.326	12.034	12.034	0.000	0.000	0.000	0.000
119	A	119	GLN	0	0.079	0.032	20.865	0.350	0.350	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.037	0.013	26.158	0.292	0.292	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.811	0.900	29.118	10.268	10.268	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.802	0.913	24.940	11.565	11.565	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.010	0.008	30.426	0.021	0.021	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.000	-0.005	33.283	0.100	0.100	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.036	-0.009	36.933	0.066	0.066	0.000	0.000	0.000	0.000
126	A	126	TYR	0	0.005	-0.033	39.524	0.112	0.112	0.000	0.000	0.000	0.000
127	A	127	GLY	0	-0.025	-0.009	43.228	-0.017	-0.017	0.000	0.000	0.000	0.000
128	A	128	GLY	0	-0.065	-0.040	46.095	0.186	0.186	0.000	0.000	0.000	0.000
129	A	129	ALA	0	-0.007	-0.007	45.838	-0.078	-0.078	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.938	-0.943	45.624	-6.487	-6.487	0.000	0.000	0.000	0.000
131	A	131	HIS	0	0.030	0.004	40.524	-0.120	-0.120	0.000	0.000	0.000	0.000
132	A	132	PRO	0	0.007	-0.008	42.042	0.040	0.040	0.000	0.000	0.000	0.000
133	A	133	HIS	0	-0.006	0.021	38.088	0.043	0.043	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.055	0.025	39.446	-0.167	-0.167	0.000	0.000	0.000	0.000
135	A	135	ALA	0	-0.020	-0.016	40.492	-0.046	-0.046	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.070	-0.035	34.380	0.059	0.059	0.000	0.000	0.000	0.000
137	A	137	GLN	0	-0.055	-0.014	35.536	-0.331	-0.331	0.000	0.000	0.000	0.000
138	A	138	PRO	0	-0.010	0.001	35.342	-0.190	-0.190	0.000	0.000	0.000	0.000
139	A	139	GLU	-1	-0.833	-0.898	33.584	-9.014	-9.014	0.000	0.000	0.000	0.000
140	A	140	ASN	0	-0.019	-0.020	36.253	-0.071	-0.071	0.000	0.000	0.000	0.000
141	A	141	TYR	-1	-0.850	-0.920	29.919	-10.161	-10.161	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.894	-0.937	35.469	-7.829	-7.829	0.000	0.000	0.000	0.000
143	A	143	LEU	0	-0.045	-0.029	34.516	-0.295	-0.295	0.000	0.000	0.000	0.000
144	A	144	ARG	1	0.737	0.853	30.726	9.596	9.596	0.000	0.000	0.000	0.000
145	A	145	GLY	-1	-0.961	-0.966	34.434	-8.845	-8.845	0.000	0.000	0.000	0.000

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