FMO DATABASE

FMODB ID: 46LVN

Calculation Name: 3OQ3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3OQ3

Chain ID: A

ChEMBL ID:

UniProt ID: P07349

Base Structure: X-ray

Registration Date: 2025-10-04

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	164
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1726939.118853
FMO2-HF: Nuclear repulsion	1660078.307341
FMO2-HF: Total energy	-66860.811512
FMO2-MP2: Total energy	-67054.471635

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:CYS)

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

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.
-151.86	-135.542	35.314	-20.388	-31.244	-0.105

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.764 / q_NPA : 0.876

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	LEU	0	-0.027	-0.022	2.802	10.650	11.989	5.069	-1.480	-4.928	-0.001
4	A	4	PRO	0	-0.030	-0.017	4.969	0.165	0.208	0.003	-0.018	-0.028	0.000
50	A	50	GLU	-1	-0.847	-0.935	1.798	-126.041	-127.375	13.102	-6.743	-5.026	-0.081
54	A	54	ILE	0	-0.003	0.003	2.098	3.222	2.590	5.780	-1.223	-3.925	-0.002
55	A	55	PRO	0	0.033	0.012	5.055	2.673	2.775	-0.002	-0.003	-0.096	0.000
95	A	95	ASP	-1	-0.785	-0.874	3.936	-35.531	-35.057	0.015	-0.215	-0.274	-0.001
96	A	96	LEU	0	0.009	-0.009	2.204	-15.685	-12.085	3.534	-2.563	-4.572	-0.034
97	A	97	LYS	1	0.883	0.934	2.475	16.814	19.843	2.384	-2.250	-3.162	-0.023
100	A	101	MET	0	-0.043	-0.025	2.587	-2.469	1.328	1.554	-2.448	-2.903	0.024
101	A	102	GLN	0	-0.011	-0.011	2.393	-21.990	-16.504	3.871	-3.354	-6.003	0.013
102	A	103	GLN	0	-0.001	-0.002	4.072	0.361	0.775	0.004	-0.091	-0.327	0.000
5	A	5	GLN	0	0.010	-0.003	8.226	1.938	1.938	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.037	0.037	5.485	0.117	0.117	0.000	0.000	0.000	0.000
7	A	7	HIS	0	-0.003	-0.005	8.198	4.316	4.316	0.000	0.000	0.000	0.000
8	A	8	ASN	0	0.057	0.019	9.834	0.375	0.375	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.028	-0.028	12.198	1.320	1.320	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.813	0.898	9.108	24.821	24.821	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.043	0.037	10.940	0.937	0.937	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.974	0.996	14.631	15.791	15.791	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.866	0.940	16.001	17.587	17.587	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.056	0.033	16.176	0.783	0.783	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.031	0.007	17.573	0.793	0.793	0.000	0.000	0.000	0.000
16	A	16	THR	0	-0.060	-0.057	19.921	0.863	0.863	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.036	-0.012	20.397	0.737	0.737	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.032	0.023	19.944	0.599	0.599	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.030	-0.007	22.958	0.494	0.494	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.919	0.959	25.766	11.286	11.286	0.000	0.000	0.000	0.000
21	A	21	MET	0	-0.041	-0.002	22.611	0.403	0.403	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.878	0.940	27.373	9.826	9.826	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.895	0.939	29.699	9.170	9.170	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.027	0.022	32.898	0.299	0.299	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.042	0.025	33.853	-0.323	-0.323	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.044	0.005	31.907	0.172	0.172	0.000	0.000	0.000	0.000
27	A	27	LEU	0	0.006	0.000	34.487	0.072	0.072	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.006	-0.009	37.970	0.141	0.141	0.000	0.000	0.000	0.000
29	A	29	CYS	0	0.008	0.015	32.632	-0.094	-0.094	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.003	0.008	35.653	-0.162	-0.162	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.974	0.982	37.273	7.114	7.114	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.819	-0.890	34.161	-8.159	-8.159	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.874	0.954	32.044	8.384	8.384	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.911	0.956	29.020	10.099	10.099	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.823	-0.889	27.851	-11.057	-11.057	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.004	-0.006	24.564	0.232	0.232	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.050	0.032	24.884	-0.223	-0.223	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.011	-0.012	17.286	-0.267	-0.267	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.007	0.019	18.008	0.259	0.259	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.006	-0.021	18.864	-0.697	-0.697	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.848	-0.919	19.397	-14.760	-14.760	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.802	0.907	17.036	14.135	14.135	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.001	0.001	13.646	-1.330	-1.330	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.039	0.020	15.758	-0.161	-0.161	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.042	0.010	13.444	-0.114	-0.114	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.041	-0.017	14.382	-0.493	-0.493	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.008	0.004	15.897	1.251	1.251	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.064	-0.017	11.074	-0.466	-0.466	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.120	0.060	8.413	-0.847	-0.847	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.028	0.024	5.292	-1.584	-1.584	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.029	0.009	6.127	2.281	2.281	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.008	0.001	7.853	2.067	2.067	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.007	0.006	6.763	2.595	2.595	0.000	0.000	0.000	0.000
57	A	57	LEU	0	0.015	-0.006	7.397	2.481	2.481	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.004	0.027	5.221	2.354	2.354	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.737	-0.824	7.185	-15.355	-15.355	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.021	-0.010	10.743	1.559	1.559	0.000	0.000	0.000	0.000
61	A	61	THR	0	-0.020	-0.032	9.355	1.558	1.558	0.000	0.000	0.000	0.000
62	A	62	GLN	0	0.015	0.012	10.965	0.243	0.243	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.051	-0.035	12.497	1.871	1.871	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.013	-0.009	14.673	1.074	1.074	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.018	0.006	13.226	0.882	0.882	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.020	0.003	16.273	0.591	0.591	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.020	-0.002	18.468	0.775	0.775	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.023	-0.030	19.566	0.681	0.681	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.041	0.007	18.150	0.208	0.208	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.046	-0.013	21.129	0.545	0.545	0.000	0.000	0.000	0.000
71	A	71	LYS	1	1.001	0.998	23.825	8.969	8.969	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.890	-0.950	27.147	-9.444	-9.444	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.040	-0.037	24.481	0.085	0.085	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.018	-0.020	26.698	0.119	0.119	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.008	0.017	27.907	0.184	0.184	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.023	0.002	28.467	0.194	0.194	0.000	0.000	0.000	0.000
77	A	77	TRP	0	-0.019	-0.010	25.883	0.158	0.158	0.000	0.000	0.000	0.000
78	A	78	ASN	0	0.018	0.011	28.880	0.058	0.058	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.099	0.049	27.064	-0.345	-0.345	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.080	0.036	25.798	-0.304	-0.304	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.062	-0.020	24.996	-0.388	-0.388	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.008	0.002	22.677	-0.568	-0.568	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.851	-0.920	21.360	-11.829	-11.829	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.035	-0.036	20.195	-0.653	-0.653	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.049	-0.027	18.118	-0.844	-0.844	0.000	0.000	0.000	0.000
86	A	86	CYS	0	-0.015	-0.013	16.960	-0.960	-0.960	0.000	0.000	0.000	0.000
87	A	87	ASN	0	0.004	0.013	15.570	-0.904	-0.904	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.821	-0.907	14.617	-17.796	-17.796	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.010	0.000	12.693	-1.572	-1.572	0.000	0.000	0.000	0.000
90	A	90	HIS	0	-0.005	-0.013	10.581	-0.491	-0.491	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.007	-0.004	10.128	-1.739	-1.739	0.000	0.000	0.000	0.000
92	A	92	GLN	0	0.030	0.012	8.279	-2.252	-2.252	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.023	-0.002	6.704	-2.956	-2.956	0.000	0.000	0.000	0.000
94	A	94	ASN	0	-0.025	-0.011	6.004	-1.732	-1.732	0.000	0.000	0.000	0.000
103	A	104	VAL	0	-0.034	-0.011	6.859	1.184	1.184	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.000	-0.005	8.760	0.562	0.562	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.037	-0.018	8.790	0.982	0.982	0.000	0.000	0.000	0.000
106	A	107	GLN	0	-0.009	0.012	9.517	-1.688	-1.688	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.843	-0.921	8.547	-31.254	-31.254	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.011	-0.002	11.161	0.287	0.287	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.066	0.042	13.211	0.194	0.194	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.031	0.016	14.238	0.196	0.196	0.000	0.000	0.000	0.000
111	A	112	THR	0	-0.020	-0.032	14.568	0.195	0.195	0.000	0.000	0.000	0.000
112	A	113	GLN	0	-0.007	0.000	8.786	0.279	0.279	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.931	-0.973	12.727	-15.770	-15.770	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.896	-0.947	15.548	-14.418	-14.418	0.000	0.000	0.000	0.000
115	A	116	SER	0	0.007	-0.015	13.813	0.812	0.812	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.013	0.001	10.340	0.518	0.518	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.018	-0.006	14.258	0.918	0.918	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.012	-0.005	17.975	0.829	0.829	0.000	0.000	0.000	0.000
119	A	120	VAL	0	0.017	0.005	13.833	0.793	0.793	0.000	0.000	0.000	0.000
120	A	121	ARG	1	0.826	0.881	14.636	16.279	16.279	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.924	0.950	17.961	12.875	12.875	0.000	0.000	0.000	0.000
122	A	123	TYR	0	-0.060	-0.045	18.506	0.483	0.483	0.000	0.000	0.000	0.000
123	A	124	PHE	0	0.073	0.016	15.712	0.539	0.539	0.000	0.000	0.000	0.000
124	A	125	HIS	0	-0.008	0.016	20.466	0.255	0.255	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.840	0.910	23.026	12.477	12.477	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.012	0.004	21.202	0.462	0.462	0.000	0.000	0.000	0.000
127	A	128	THR	0	-0.028	-0.037	22.455	0.483	0.483	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.023	-0.001	25.328	0.341	0.341	0.000	0.000	0.000	0.000
129	A	130	TYR	0	0.008	-0.014	28.331	0.292	0.292	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.005	0.005	26.447	0.312	0.312	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.932	0.973	25.871	10.438	10.438	0.000	0.000	0.000	0.000
132	A	133	GLU	-1	-0.921	-0.960	31.411	-8.539	-8.539	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.822	0.894	32.589	8.596	8.596	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.914	0.959	34.289	7.771	7.771	0.000	0.000	0.000	0.000
135	A	136	HIS	0	0.039	0.022	27.953	0.021	0.021	0.000	0.000	0.000	0.000
136	A	137	SER	0	-0.001	0.007	32.320	0.008	0.008	0.000	0.000	0.000	0.000
137	A	138	PRO	0	0.036	-0.001	33.089	-0.242	-0.242	0.000	0.000	0.000	0.000
138	A	140	ALA	0	0.023	0.027	31.317	-0.212	-0.212	0.000	0.000	0.000	0.000
139	A	141	TRP	0	0.040	0.012	24.424	-0.495	-0.495	0.000	0.000	0.000	0.000
140	A	142	GLU	-1	-0.762	-0.861	27.754	-10.599	-10.599	0.000	0.000	0.000	0.000
141	A	143	VAL	0	-0.035	-0.012	28.228	-0.328	-0.328	0.000	0.000	0.000	0.000
142	A	144	VAL	0	0.022	0.009	23.700	-0.387	-0.387	0.000	0.000	0.000	0.000
143	A	145	ARG	1	0.785	0.862	23.707	10.560	10.560	0.000	0.000	0.000	0.000
144	A	146	ALA	0	-0.048	-0.024	23.710	-0.475	-0.475	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.752	-0.813	22.471	-12.931	-12.931	0.000	0.000	0.000	0.000
146	A	148	VAL	0	0.038	0.013	18.335	-0.634	-0.634	0.000	0.000	0.000	0.000
147	A	149	TRP	0	-0.005	0.002	19.064	-0.717	-0.717	0.000	0.000	0.000	0.000
148	A	150	ARG	1	0.858	0.909	20.219	12.026	12.026	0.000	0.000	0.000	0.000
149	A	151	ALA	0	0.007	0.020	17.235	-0.597	-0.597	0.000	0.000	0.000	0.000
150	A	152	LEU	0	0.028	0.015	14.230	-1.096	-1.096	0.000	0.000	0.000	0.000
151	A	153	SER	0	-0.018	-0.026	15.743	-1.017	-1.017	0.000	0.000	0.000	0.000
152	A	154	SER	0	-0.052	-0.037	17.652	-0.238	-0.238	0.000	0.000	0.000	0.000
153	A	155	SER	0	0.000	-0.006	12.160	-0.855	-0.855	0.000	0.000	0.000	0.000
154	A	156	VAL	0	-0.039	-0.021	12.877	-1.719	-1.719	0.000	0.000	0.000	0.000
155	A	157	ASN	0	-0.018	-0.021	13.863	-1.062	-1.062	0.000	0.000	0.000	0.000
156	A	158	LEU	0	-0.020	0.000	11.609	0.248	0.248	0.000	0.000	0.000	0.000
157	A	159	LEU	0	0.011	0.004	7.543	-0.955	-0.955	0.000	0.000	0.000	0.000
158	A	160	ALA	0	-0.030	-0.017	10.672	-0.986	-0.986	0.000	0.000	0.000	0.000
159	A	161	ARG	1	0.845	0.944	13.314	20.294	20.294	0.000	0.000	0.000	0.000
160	A	162	LEU	0	0.058	0.018	8.319	0.274	0.274	0.000	0.000	0.000	0.000
161	A	163	SER	0	-0.032	-0.010	9.222	0.220	0.220	0.000	0.000	0.000	0.000
162	A	164	LYS	1	0.849	0.918	10.119	20.912	20.912	0.000	0.000	0.000	0.000
163	A	165	GLU	-1	-0.979	-0.988	12.129	-19.899	-19.899	0.000	0.000	0.000	0.000
164	A	166	GLU	-2	-1.896	-1.931	7.091	-65.808	-65.808	0.000	0.000	0.000	0.000

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