FMO DATABASE

FMODB ID: VZK21

Calculation Name: 5OQL-W-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5OQL

Chain ID: W

ChEMBL ID:

UniProt ID: G0S3T2

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-974442.619019
FMO2-HF: Nuclear repulsion	929003.723096
FMO2-HF: Total energy	-45438.895923
FMO2-MP2: Total energy	-45572.215237

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:7:ALA)

Summations of interaction energy for fragment #1(A:7: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.
12.578	14.932	3.311	-1.959	-3.707	-0.016

Interaction energy analysis for fragmet #1(A:7:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / q_NPA : 0.916

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	9	TRP	0	0.050	0.030	3.761	-0.362	1.801	-0.007	-0.960	-1.196	-0.003
4	A	10	PRO	0	0.104	0.080	5.216	3.896	4.045	-0.001	-0.013	-0.136	0.000
56	A	62	LEU	0	0.063	-0.009	2.275	-0.311	-0.291	1.239	-0.361	-0.898	-0.004
60	A	66	LEU	0	-0.011	-0.011	2.269	-3.153	-3.131	2.080	-0.625	-1.477	-0.009
5	A	11	LYS	1	0.850	0.922	6.554	39.999	39.999	0.000	0.000	0.000	0.000
6	A	12	ALA	0	0.062	0.026	9.290	1.983	1.983	0.000	0.000	0.000	0.000
7	A	13	GLU	-1	-0.917	-0.966	12.786	-19.536	-19.536	0.000	0.000	0.000	0.000
8	A	14	ASP	-1	-0.952	-0.989	15.009	-16.308	-16.308	0.000	0.000	0.000	0.000
9	A	15	PRO	0	0.032	0.011	17.262	0.949	0.949	0.000	0.000	0.000	0.000
10	A	16	ALA	0	-0.002	0.003	20.481	0.108	0.108	0.000	0.000	0.000	0.000
11	A	17	LEU	0	0.013	0.025	15.767	0.088	0.088	0.000	0.000	0.000	0.000
12	A	18	VAL	0	0.011	-0.014	14.879	-0.349	-0.349	0.000	0.000	0.000	0.000
13	A	19	GLN	0	-0.029	-0.014	17.568	0.358	0.358	0.000	0.000	0.000	0.000
14	A	20	GLU	-1	-0.770	-0.857	21.288	-13.304	-13.304	0.000	0.000	0.000	0.000
15	A	21	LEU	0	-0.017	-0.007	15.315	0.078	0.078	0.000	0.000	0.000	0.000
16	A	22	LEU	0	-0.056	-0.028	17.419	0.182	0.182	0.000	0.000	0.000	0.000
17	A	23	ASP	-1	-0.888	-0.959	20.662	-11.986	-11.986	0.000	0.000	0.000	0.000
18	A	24	CYS	0	0.016	0.023	22.411	0.542	0.542	0.000	0.000	0.000	0.000
19	A	25	VAL	0	-0.008	-0.006	18.784	0.252	0.252	0.000	0.000	0.000	0.000
20	A	26	GLN	0	0.017	0.010	22.224	0.799	0.799	0.000	0.000	0.000	0.000
21	A	27	GLN	0	-0.032	-0.025	25.296	0.191	0.191	0.000	0.000	0.000	0.000
22	A	28	ALA	0	0.022	0.003	24.018	0.389	0.389	0.000	0.000	0.000	0.000
23	A	29	SER	0	-0.090	-0.059	25.164	0.261	0.261	0.000	0.000	0.000	0.000
24	A	30	HIS	0	-0.025	-0.013	26.672	0.400	0.400	0.000	0.000	0.000	0.000
25	A	31	TYR	0	-0.061	-0.032	29.393	0.372	0.372	0.000	0.000	0.000	0.000
26	A	32	ARG	1	0.894	0.944	28.735	10.400	10.400	0.000	0.000	0.000	0.000
27	A	33	GLN	0	0.012	0.016	25.899	-0.254	-0.254	0.000	0.000	0.000	0.000
28	A	34	LEU	0	-0.022	0.005	20.850	-0.495	-0.495	0.000	0.000	0.000	0.000
29	A	35	LYS	1	0.877	0.949	20.768	12.580	12.580	0.000	0.000	0.000	0.000
30	A	36	LYS	1	0.924	0.946	19.446	11.803	11.803	0.000	0.000	0.000	0.000
31	A	37	GLY	0	0.042	0.028	16.879	0.422	0.422	0.000	0.000	0.000	0.000
32	A	38	ALA	0	0.059	0.033	13.536	0.155	0.155	0.000	0.000	0.000	0.000
33	A	39	ASN	0	0.014	0.020	15.060	-0.462	-0.462	0.000	0.000	0.000	0.000
34	A	40	GLU	-1	-0.866	-0.937	18.139	-12.526	-12.526	0.000	0.000	0.000	0.000
35	A	41	THR	0	0.012	0.006	14.273	0.354	0.354	0.000	0.000	0.000	0.000
36	A	42	THR	0	0.040	0.004	15.177	-0.127	-0.127	0.000	0.000	0.000	0.000
37	A	43	LYS	1	0.926	0.966	16.655	13.051	13.051	0.000	0.000	0.000	0.000
38	A	44	SER	0	-0.045	-0.013	18.775	0.348	0.348	0.000	0.000	0.000	0.000
39	A	45	VAL	0	0.084	0.044	15.318	0.630	0.630	0.000	0.000	0.000	0.000
40	A	46	ASN	0	0.059	0.022	17.980	0.084	0.084	0.000	0.000	0.000	0.000
41	A	47	ARG	1	0.876	0.928	19.895	11.709	11.709	0.000	0.000	0.000	0.000
42	A	48	GLY	0	0.033	0.032	21.560	0.502	0.502	0.000	0.000	0.000	0.000
43	A	49	THR	0	-0.091	-0.051	22.582	0.409	0.409	0.000	0.000	0.000	0.000
44	A	50	SER	0	-0.087	-0.051	18.534	0.051	0.051	0.000	0.000	0.000	0.000
45	A	51	GLU	-1	-0.785	-0.868	20.824	-12.843	-12.843	0.000	0.000	0.000	0.000
46	A	52	LEU	0	0.020	0.016	16.302	-0.302	-0.302	0.000	0.000	0.000	0.000
47	A	53	VAL	0	-0.017	-0.013	12.872	0.509	0.509	0.000	0.000	0.000	0.000
48	A	54	ILE	0	0.017	0.019	13.291	-1.123	-1.123	0.000	0.000	0.000	0.000
49	A	55	LEU	0	-0.002	-0.011	7.739	0.822	0.822	0.000	0.000	0.000	0.000
50	A	56	ALA	0	0.006	0.009	10.509	0.102	0.102	0.000	0.000	0.000	0.000
51	A	57	ALA	0	-0.002	-0.006	7.002	-1.968	-1.968	0.000	0.000	0.000	0.000
52	A	58	ASP	-1	-0.850	-0.892	7.884	-22.216	-22.216	0.000	0.000	0.000	0.000
53	A	59	THR	0	-0.011	-0.024	7.858	3.259	3.259	0.000	0.000	0.000	0.000
54	A	60	GLN	0	-0.008	-0.004	8.610	-1.333	-1.333	0.000	0.000	0.000	0.000
55	A	61	PRO	0	0.014	0.019	9.142	-0.755	-0.755	0.000	0.000	0.000	0.000
57	A	63	SER	0	0.029	0.015	6.283	-1.512	-1.512	0.000	0.000	0.000	0.000
58	A	64	ILE	0	-0.022	-0.011	7.347	0.653	0.653	0.000	0.000	0.000	0.000
59	A	65	VAL	0	-0.030	-0.018	6.784	2.348	2.348	0.000	0.000	0.000	0.000
61	A	67	HIS	0	0.014	0.016	5.995	-1.291	-1.291	0.000	0.000	0.000	0.000
62	A	68	ILE	0	-0.010	-0.011	9.427	0.968	0.968	0.000	0.000	0.000	0.000
63	A	69	PRO	0	0.011	0.005	6.056	1.205	1.205	0.000	0.000	0.000	0.000
64	A	70	LEU	0	0.052	0.042	9.220	1.157	1.157	0.000	0.000	0.000	0.000
65	A	71	ILE	0	0.019	0.011	11.281	1.251	1.251	0.000	0.000	0.000	0.000
66	A	72	CYS	0	-0.102	-0.054	11.946	1.253	1.253	0.000	0.000	0.000	0.000
67	A	73	GLU	-1	-0.932	-0.951	11.703	-23.242	-23.242	0.000	0.000	0.000	0.000
68	A	74	GLU	-1	-0.932	-0.967	14.139	-14.330	-14.330	0.000	0.000	0.000	0.000
69	A	75	LYS	1	0.786	0.884	16.929	15.170	15.170	0.000	0.000	0.000	0.000
70	A	76	ASN	0	-0.019	0.005	17.192	0.336	0.336	0.000	0.000	0.000	0.000
71	A	77	VAL	0	-0.015	0.006	15.796	0.538	0.538	0.000	0.000	0.000	0.000
72	A	78	PRO	0	0.035	0.015	15.117	-1.403	-1.403	0.000	0.000	0.000	0.000
73	A	79	TYR	0	-0.002	-0.013	7.409	0.803	0.803	0.000	0.000	0.000	0.000
74	A	80	VAL	0	0.033	0.024	10.822	-1.494	-1.494	0.000	0.000	0.000	0.000
75	A	81	TYR	0	-0.023	-0.022	4.926	-3.196	-3.196	0.000	0.000	0.000	0.000
76	A	82	VAL	0	0.066	0.038	9.838	0.390	0.390	0.000	0.000	0.000	0.000
77	A	83	PRO	0	0.018	-0.010	11.052	-1.654	-1.654	0.000	0.000	0.000	0.000
78	A	84	SER	0	0.025	0.006	12.134	0.409	0.409	0.000	0.000	0.000	0.000
79	A	85	LYS	1	0.905	0.947	13.223	20.679	20.679	0.000	0.000	0.000	0.000
80	A	86	VAL	0	-0.040	-0.017	14.964	1.238	1.238	0.000	0.000	0.000	0.000
81	A	87	ALA	0	0.025	0.014	17.334	0.980	0.980	0.000	0.000	0.000	0.000
82	A	88	LEU	0	0.076	0.036	14.236	0.853	0.853	0.000	0.000	0.000	0.000
83	A	89	GLY	0	0.005	0.000	17.795	0.668	0.668	0.000	0.000	0.000	0.000
84	A	90	ARG	1	0.889	0.941	20.027	13.894	13.894	0.000	0.000	0.000	0.000
85	A	91	ALA	0	0.014	0.023	20.515	0.586	0.586	0.000	0.000	0.000	0.000
86	A	92	CYS	0	-0.028	-0.016	19.931	0.274	0.274	0.000	0.000	0.000	0.000
87	A	93	GLY	0	0.017	0.038	22.853	0.520	0.520	0.000	0.000	0.000	0.000
88	A	94	VAL	0	-0.012	-0.014	22.361	0.377	0.377	0.000	0.000	0.000	0.000
89	A	95	SER	0	-0.045	-0.014	24.837	0.328	0.328	0.000	0.000	0.000	0.000
90	A	96	ARG	1	0.930	0.960	21.718	12.759	12.759	0.000	0.000	0.000	0.000
91	A	97	ALA	0	-0.002	-0.007	17.165	-0.061	-0.061	0.000	0.000	0.000	0.000
92	A	98	VAL	0	-0.008	0.002	16.597	0.082	0.082	0.000	0.000	0.000	0.000
93	A	99	ILE	0	0.000	-0.007	11.402	-0.325	-0.325	0.000	0.000	0.000	0.000
94	A	100	ALA	0	0.021	0.004	11.828	-1.940	-1.940	0.000	0.000	0.000	0.000
95	A	101	VAL	0	-0.025	-0.015	13.654	1.416	1.416	0.000	0.000	0.000	0.000
96	A	102	SER	0	0.016	0.014	16.004	-0.892	-0.892	0.000	0.000	0.000	0.000
97	A	103	LEU	0	0.006	0.004	18.389	0.757	0.757	0.000	0.000	0.000	0.000
98	A	104	THR	0	0.025	0.012	21.579	-0.257	-0.257	0.000	0.000	0.000	0.000
99	A	105	SER	0	-0.024	-0.017	24.104	0.065	0.065	0.000	0.000	0.000	0.000
100	A	106	ASN	0	-0.038	-0.019	27.271	0.205	0.205	0.000	0.000	0.000	0.000
101	A	107	GLU	-1	-0.865	-0.923	30.906	-9.270	-9.270	0.000	0.000	0.000	0.000
102	A	108	ALA	0	0.010	0.006	33.381	-0.076	-0.076	0.000	0.000	0.000	0.000
103	A	109	SER	0	0.017	0.003	31.009	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	110	ASP	-1	-0.766	-0.891	32.262	-10.102	-10.102	0.000	0.000	0.000	0.000
105	A	111	LEU	0	0.016	0.013	26.081	-0.255	-0.255	0.000	0.000	0.000	0.000
106	A	112	ASN	0	0.026	0.013	27.447	-0.709	-0.709	0.000	0.000	0.000	0.000
107	A	113	SER	0	-0.019	-0.023	27.498	-0.245	-0.245	0.000	0.000	0.000	0.000
108	A	114	LYS	1	0.905	0.975	26.337	10.720	10.720	0.000	0.000	0.000	0.000
109	A	115	ILE	0	0.023	0.000	22.075	-0.486	-0.486	0.000	0.000	0.000	0.000
110	A	116	ARG	1	0.912	0.959	23.008	10.278	10.278	0.000	0.000	0.000	0.000
111	A	117	ALA	0	0.013	0.006	24.406	-0.245	-0.245	0.000	0.000	0.000	0.000
112	A	118	LEU	0	-0.031	-0.013	19.885	-0.380	-0.380	0.000	0.000	0.000	0.000
113	A	119	ARG	1	0.815	0.861	19.125	13.182	13.182	0.000	0.000	0.000	0.000
114	A	120	ASP	-1	-0.888	-0.924	19.519	-14.266	-14.266	0.000	0.000	0.000	0.000
115	A	121	LYS	1	0.807	0.865	19.504	13.134	13.134	0.000	0.000	0.000	0.000
116	A	122	VAL	0	-0.064	-0.020	14.041	-0.911	-0.911	0.000	0.000	0.000	0.000
117	A	123	GLU	-1	-0.813	-0.932	15.495	-18.643	-18.643	0.000	0.000	0.000	0.000
118	A	124	ARG	1	0.864	0.947	17.718	14.905	14.905	0.000	0.000	0.000	0.000
119	A	125	LEU	0	-0.146	-0.066	12.721	-0.157	-0.157	0.000	0.000	0.000	0.000
120	A	126	ALA	-1	-0.943	-0.957	12.247	-22.784	-22.784	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ALA)