FMO DATABASE

FMODB ID: 655GZ

Calculation Name: 6OGF-Q-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6OGF

Chain ID: Q

ChEMBL ID:

UniProt ID: P0ADY7

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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-899206.374767
FMO2-HF: Nuclear repulsion	851663.277244
FMO2-HF: Total energy	-47543.097523
FMO2-MP2: Total energy	-47681.796214

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:ALA)

Summations of interaction energy for fragment #1(A:1: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.
268.201	269.811	0.038	-0.549	-1.098	-0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.876 / q_NPA : 0.926

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	VAL	0	0.092	0.046	3.867	2.061	2.973	-0.008	-0.340	-0.564	0.000
6	A	6	LEU	0	-0.062	-0.021	2.874	-0.175	0.367	0.047	-0.181	-0.408	-0.002
11	A	11	ARG	1	0.927	0.960	4.348	49.530	49.686	-0.001	-0.028	-0.126	0.000
4	A	4	ASN	0	0.084	0.037	5.420	4.263	4.263	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.023	-0.037	5.141	7.046	7.046	0.000	0.000	0.000	0.000
7	A	7	VAL	0	0.027	0.017	7.143	2.907	2.907	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.969	1.007	10.445	25.093	25.093	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.913	0.942	9.944	25.706	25.706	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.064	0.047	9.190	-3.429	-3.429	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.058	0.040	9.198	2.384	2.384	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.937	0.972	11.692	18.390	18.390	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.963	0.975	13.079	22.843	22.843	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.041	0.015	15.841	0.426	0.426	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.023	0.017	19.506	0.060	0.060	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.955	0.979	22.165	13.001	13.001	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.051	0.034	24.669	0.125	0.125	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.005	-0.021	27.293	-0.111	-0.111	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.052	-0.037	30.443	0.283	0.283	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.022	0.019	31.902	0.119	0.119	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.036	-0.012	34.500	0.251	0.251	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.005	-0.011	37.505	0.210	0.210	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.844	-0.936	31.981	-9.708	-9.708	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.009	0.004	32.560	0.070	0.070	0.000	0.000	0.000	0.000
26	A	26	CYS	0	0.018	0.011	34.330	0.300	0.300	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.004	0.012	37.901	-0.058	-0.058	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.006	-0.019	39.392	0.010	0.010	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.902	0.970	41.011	7.583	7.583	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.995	1.005	43.867	6.455	6.455	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.017	-0.007	46.846	-0.132	-0.132	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.029	-0.021	48.529	0.087	0.087	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.075	-0.007	50.981	0.082	0.082	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.034	0.026	50.022	0.038	0.038	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.945	0.958	50.146	6.072	6.072	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.009	-0.004	51.380	-0.168	-0.168	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.034	0.014	46.987	0.074	0.074	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.041	-0.040	51.044	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.002	0.013	46.076	0.047	0.047	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.059	0.021	46.605	0.100	0.100	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.097	-0.038	44.342	-0.173	-0.173	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.960	0.987	36.365	8.590	8.590	0.000	0.000	0.000	0.000
43	A	43	LYS	1	1.004	0.975	39.256	7.870	7.870	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.027	0.033	40.938	0.095	0.095	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.026	-0.001	43.179	0.191	0.191	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.037	0.018	46.206	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.054	0.016	49.510	0.093	0.093	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.015	0.008	49.645	-0.148	-0.148	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.832	0.915	44.591	7.032	7.032	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.998	1.004	49.540	5.899	5.899	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.044	-0.025	45.983	-0.162	-0.162	0.000	0.000	0.000	0.000
52	A	52	CYS	0	0.002	0.012	48.184	0.178	0.178	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.895	0.967	46.200	6.313	6.313	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.006	-0.002	45.705	0.135	0.135	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.982	1.001	45.383	6.749	6.749	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.016	-0.007	41.619	0.114	0.114	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.053	-0.049	45.437	0.063	0.063	0.000	0.000	0.000	0.000
58	A	58	ASN	0	-0.001	-0.007	40.073	0.166	0.166	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.058	0.039	42.573	-0.124	-0.124	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.016	0.019	37.302	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.949	-0.970	42.450	-6.932	-6.932	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.034	0.019	40.053	-0.232	-0.232	0.000	0.000	0.000	0.000
63	A	63	THR	0	0.037	0.013	42.072	0.148	0.148	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.006	-0.007	42.343	-0.252	-0.252	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.027	-0.016	43.955	0.188	0.188	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.025	0.003	45.720	-0.036	-0.036	0.000	0.000	0.000	0.000
67	A	67	GLY	0	-0.009	0.004	48.247	0.029	0.029	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.001	-0.014	48.841	0.093	0.093	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.793	-0.870	51.849	-5.744	-5.744	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.061	0.023	55.224	0.009	0.009	0.000	0.000	0.000	0.000
71	A	71	HIS	0	-0.032	-0.030	55.847	-0.193	-0.193	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.016	-0.023	54.466	0.017	0.017	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.002	-0.001	52.228	-0.024	-0.024	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.039	-0.040	56.531	0.063	0.063	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.765	-0.859	55.206	-5.848	-5.848	0.000	0.000	0.000	0.000
76	A	76	HIS	0	0.109	0.056	57.113	0.050	0.050	0.000	0.000	0.000	0.000
77	A	77	SER	0	0.000	0.005	56.641	-0.068	-0.068	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.032	-0.018	52.771	-0.125	-0.125	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.002	-0.002	49.255	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.008	-0.008	46.208	-0.096	-0.096	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.018	-0.004	42.411	0.029	0.029	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.971	0.988	41.284	7.511	7.511	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.063	0.032	37.583	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.014	0.002	37.020	0.118	0.118	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.956	0.986	33.598	9.318	9.318	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.055	0.026	37.685	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.871	0.951	35.198	8.782	8.782	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.777	-0.889	37.827	-7.668	-7.668	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.023	0.008	40.882	0.074	0.074	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.014	0.002	38.470	-0.239	-0.239	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.019	0.018	37.496	0.154	0.154	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.008	-0.003	38.156	-0.131	-0.131	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.863	0.919	33.630	9.005	9.005	0.000	0.000	0.000	0.000
94	A	94	TYR	0	0.053	0.026	36.495	-0.183	-0.183	0.000	0.000	0.000	0.000
95	A	95	HIS	0	-0.062	-0.027	40.560	0.230	0.230	0.000	0.000	0.000	0.000
96	A	96	THR	0	0.028	0.019	43.813	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	97	VAL	0	-0.062	-0.042	45.837	-0.029	-0.029	0.000	0.000	0.000	0.000
98	A	98	ARG	1	0.856	0.922	48.390	6.120	6.120	0.000	0.000	0.000	0.000
99	A	99	GLY	0	-0.015	-0.018	51.555	-0.051	-0.051	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.083	-0.028	50.593	-0.041	-0.041	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.000	-0.015	50.745	0.073	0.073	0.000	0.000	0.000	0.000
102	A	102	ASP	-1	-0.814	-0.900	54.279	-5.429	-5.429	0.000	0.000	0.000	0.000
103	A	103	CYS	0	-0.049	0.025	51.355	0.003	0.003	0.000	0.000	0.000	0.000
104	A	104	SER	0	0.021	0.011	54.592	-0.018	-0.018	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.072	0.019	55.373	-0.060	-0.060	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.086	-0.061	53.567	0.068	0.068	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.925	0.979	56.701	5.406	5.406	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.821	-0.900	60.125	-5.265	-5.265	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.796	0.896	53.364	5.845	5.845	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.934	0.970	57.335	5.127	5.127	0.000	0.000	0.000	0.000
111	A	111	GLN	0	0.056	0.012	53.610	-0.032	-0.032	0.000	0.000	0.000	0.000
112	A	112	ALA	0	-0.003	-0.019	49.572	-0.050	-0.050	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.916	0.958	51.072	5.661	5.661	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.015	0.024	49.554	0.057	0.057	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.948	0.975	45.796	6.899	6.899	0.000	0.000	0.000	0.000
116	A	116	TYR	0	-0.026	-0.039	49.024	0.041	0.041	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.080	0.049	51.780	0.105	0.105	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.041	0.000	53.504	0.117	0.117	0.000	0.000	0.000	0.000
119	A	119	LYS	1	0.991	0.989	56.734	5.516	5.516	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.932	0.958	58.807	5.360	5.360	0.000	0.000	0.000	0.000
121	A	121	PRO	0	0.033	0.019	59.647	0.068	0.068	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.916	0.947	62.846	4.931	4.931	0.000	0.000	0.000	0.000
123	A	123	ALA	-1	-0.791	-0.868	65.308	-4.940	-4.940	0.000	0.000	0.000	0.000

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