FMO DATABASE

FMODB ID: JV349

Calculation Name: 1QB3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1QB3

Chain ID: A

ChEMBL ID:

UniProt ID: P20486

Base Structure: X-ray

Registration Date: 2025-10-05

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	113
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-832334.542006
FMO2-HF: Nuclear repulsion	786058.971345
FMO2-HF: Total energy	-46275.570661
FMO2-MP2: Total energy	-46411.313469

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:6:HIS)

Summations of interaction energy for fragment #1(A:6:HIS)

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.
-31.579	-40.935	37.245	-13.347	-14.538	0.074

Interaction energy analysis for fragmet #1(A:6:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.042 / q_NPA : -0.012

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	8	PHE	0	-0.016	0.011	2.365	-1.485	3.217	0.391	-2.163	-2.930	-0.003
4	A	9	GLN	0	0.052	0.021	1.861	-17.923	-26.460	17.205	-4.644	-4.023	0.039
5	A	10	GLY	0	0.057	0.037	5.877	0.559	0.623	-0.001	-0.002	-0.060	0.000
67	A	72	ASP	0	-0.046	-0.053	1.838	-15.205	-20.830	19.651	-6.535	-7.490	0.038
68	A	73	GLU	-1	-0.726	-0.819	5.558	2.382	2.422	-0.001	-0.003	-0.035	0.000
6	A	11	ARG	1	0.699	0.791	9.163	-2.673	-2.673	0.000	0.000	0.000	0.000
7	A	12	LYS	1	0.931	0.977	7.647	0.169	0.169	0.000	0.000	0.000	0.000
8	A	13	LEU	0	-0.024	0.009	9.959	-0.629	-0.629	0.000	0.000	0.000	0.000
9	A	14	THR	0	0.004	-0.034	11.968	-0.325	-0.325	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.890	-0.955	13.717	-0.045	-0.045	0.000	0.000	0.000	0.000
11	A	16	GLN	0	0.004	-0.004	15.650	0.088	0.088	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.739	-0.805	15.933	1.500	1.500	0.000	0.000	0.000	0.000
13	A	18	ARG	1	0.868	0.927	10.686	-2.231	-2.231	0.000	0.000	0.000	0.000
14	A	19	ALA	0	-0.007	-0.009	15.073	0.061	0.061	0.000	0.000	0.000	0.000
15	A	20	ARG	1	0.926	0.966	18.151	-0.778	-0.778	0.000	0.000	0.000	0.000
16	A	21	VAL	0	-0.004	-0.007	16.284	0.019	0.019	0.000	0.000	0.000	0.000
17	A	22	LEU	0	-0.033	-0.024	13.828	0.091	0.091	0.000	0.000	0.000	0.000
18	A	23	GLU	-1	-0.928	-0.942	17.868	0.682	0.682	0.000	0.000	0.000	0.000
19	A	24	PHE	0	0.030	-0.013	20.583	-0.068	-0.068	0.000	0.000	0.000	0.000
20	A	25	GLN	0	-0.001	0.003	13.682	-0.120	-0.120	0.000	0.000	0.000	0.000
21	A	26	ASP	-1	-0.912	-0.956	18.692	1.015	1.015	0.000	0.000	0.000	0.000
22	A	27	SER	0	-0.087	-0.048	21.370	-0.100	-0.100	0.000	0.000	0.000	0.000
23	A	28	ILE	0	-0.067	-0.021	16.781	0.025	0.025	0.000	0.000	0.000	0.000
24	A	29	HIS	0	-0.017	-0.002	20.578	0.008	0.008	0.000	0.000	0.000	0.000
25	A	30	TYR	0	0.055	0.022	15.481	0.318	0.318	0.000	0.000	0.000	0.000
26	A	31	SER	0	-0.010	0.001	20.755	-0.106	-0.106	0.000	0.000	0.000	0.000
27	A	32	PRO	0	0.014	-0.007	21.803	0.107	0.107	0.000	0.000	0.000	0.000
28	A	33	ARG	1	0.863	0.936	19.066	-1.554	-1.554	0.000	0.000	0.000	0.000
29	A	34	TYR	0	-0.014	-0.001	22.615	-0.125	-0.125	0.000	0.000	0.000	0.000
30	A	35	SER	0	0.000	-0.004	22.989	0.129	0.129	0.000	0.000	0.000	0.000
31	A	36	ASP	-1	-0.778	-0.858	24.246	1.383	1.383	0.000	0.000	0.000	0.000
32	A	37	ASP	-1	-0.943	-0.970	25.635	0.984	0.984	0.000	0.000	0.000	0.000
33	A	38	ASN	0	-0.121	-0.058	22.308	-0.035	-0.035	0.000	0.000	0.000	0.000
34	A	39	TYR	0	0.000	0.007	16.220	0.002	0.002	0.000	0.000	0.000	0.000
35	A	40	GLU	-1	-0.883	-0.928	18.707	1.728	1.728	0.000	0.000	0.000	0.000
36	A	41	TYR	0	-0.043	-0.054	18.798	0.285	0.285	0.000	0.000	0.000	0.000
37	A	42	ARG	1	0.813	0.885	16.518	-2.452	-2.452	0.000	0.000	0.000	0.000
38	A	43	HIS	0	0.010	0.012	18.996	0.124	0.124	0.000	0.000	0.000	0.000
39	A	44	VAL	0	0.014	-0.004	16.113	-0.071	-0.071	0.000	0.000	0.000	0.000
40	A	45	MET	0	-0.038	-0.007	19.437	-0.041	-0.041	0.000	0.000	0.000	0.000
41	A	46	LEU	0	0.053	0.019	17.681	-0.026	-0.026	0.000	0.000	0.000	0.000
42	A	47	PRO	0	0.028	0.028	21.730	-0.119	-0.119	0.000	0.000	0.000	0.000
43	A	48	LYS	1	1.004	0.964	24.451	-0.990	-0.990	0.000	0.000	0.000	0.000
44	A	49	ALA	0	-0.072	-0.028	26.602	-0.015	-0.015	0.000	0.000	0.000	0.000
45	A	50	MET	0	0.052	0.050	17.120	-0.068	-0.068	0.000	0.000	0.000	0.000
46	A	51	LEU	0	0.023	-0.001	21.549	0.048	0.048	0.000	0.000	0.000	0.000
47	A	52	LYS	1	0.875	0.939	23.204	-0.947	-0.947	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.055	-0.018	20.933	-0.101	-0.101	0.000	0.000	0.000	0.000
49	A	54	ILE	0	-0.015	0.017	17.660	0.071	0.071	0.000	0.000	0.000	0.000
50	A	55	PRO	0	0.025	0.012	16.389	-0.141	-0.141	0.000	0.000	0.000	0.000
51	A	56	SER	0	0.040	0.011	19.464	0.173	0.173	0.000	0.000	0.000	0.000
52	A	57	ASP	-1	-0.771	-0.856	16.172	2.252	2.252	0.000	0.000	0.000	0.000
53	A	58	TYR	0	-0.032	-0.035	11.858	0.550	0.550	0.000	0.000	0.000	0.000
54	A	59	PHE	0	-0.075	-0.032	17.074	0.127	0.127	0.000	0.000	0.000	0.000
55	A	60	ASN	0	-0.008	0.003	20.135	-0.091	-0.091	0.000	0.000	0.000	0.000
56	A	61	SER	0	-0.021	-0.040	21.751	-0.064	-0.064	0.000	0.000	0.000	0.000
57	A	62	GLU	-1	-0.893	-0.921	25.081	1.136	1.136	0.000	0.000	0.000	0.000
58	A	63	VAL	0	-0.058	-0.025	24.575	-0.067	-0.067	0.000	0.000	0.000	0.000
59	A	64	GLY	0	-0.021	-0.003	25.469	-0.055	-0.055	0.000	0.000	0.000	0.000
60	A	65	THR	0	-0.023	-0.010	21.787	-0.046	-0.046	0.000	0.000	0.000	0.000
61	A	66	LEU	0	-0.019	-0.014	17.228	-0.016	-0.016	0.000	0.000	0.000	0.000
62	A	67	ARG	1	0.773	0.853	12.002	-4.005	-4.005	0.000	0.000	0.000	0.000
63	A	68	ILE	0	0.012	0.009	12.242	0.242	0.242	0.000	0.000	0.000	0.000
64	A	69	LEU	0	-0.039	-0.007	11.382	0.056	0.056	0.000	0.000	0.000	0.000
65	A	70	THR	0	0.003	-0.035	6.123	0.724	0.724	0.000	0.000	0.000	0.000
66	A	71	GLU	-1	-0.793	-0.887	4.950	11.819	11.819	0.000	0.000	0.000	0.000
69	A	74	TRP	0	0.018	0.010	9.260	-1.177	-1.177	0.000	0.000	0.000	0.000
70	A	75	ARG	1	0.773	0.872	5.927	-9.351	-9.351	0.000	0.000	0.000	0.000
71	A	76	GLY	0	-0.009	-0.002	8.772	-1.502	-1.502	0.000	0.000	0.000	0.000
72	A	77	LEU	0	-0.029	-0.014	10.183	-1.061	-1.061	0.000	0.000	0.000	0.000
73	A	78	GLY	0	0.019	0.006	11.856	-0.515	-0.515	0.000	0.000	0.000	0.000
74	A	79	ILE	0	-0.025	0.007	12.616	-0.397	-0.397	0.000	0.000	0.000	0.000
75	A	80	THR	0	-0.032	-0.033	11.106	0.724	0.724	0.000	0.000	0.000	0.000
76	A	81	GLN	0	0.032	0.033	11.646	-1.070	-1.070	0.000	0.000	0.000	0.000
77	A	82	SER	0	0.040	0.017	11.280	0.372	0.372	0.000	0.000	0.000	0.000
78	A	83	LEU	0	0.027	0.001	7.213	0.566	0.566	0.000	0.000	0.000	0.000
79	A	84	GLY	0	0.028	0.010	9.158	-0.756	-0.756	0.000	0.000	0.000	0.000
80	A	85	TRP	0	-0.030	-0.003	10.619	-0.536	-0.536	0.000	0.000	0.000	0.000
81	A	86	GLU	-1	-0.877	-0.940	10.466	4.856	4.856	0.000	0.000	0.000	0.000
82	A	87	HIS	0	-0.054	-0.022	11.630	-0.179	-0.179	0.000	0.000	0.000	0.000
83	A	88	TYR	0	-0.010	-0.034	13.376	0.044	0.044	0.000	0.000	0.000	0.000
84	A	89	GLU	-1	-0.872	-0.950	16.559	2.250	2.250	0.000	0.000	0.000	0.000
85	A	90	CYS	0	-0.086	-0.045	19.474	-0.214	-0.214	0.000	0.000	0.000	0.000
86	A	91	HIS	0	0.053	0.050	22.070	0.196	0.196	0.000	0.000	0.000	0.000
87	A	92	ALA	0	-0.001	0.006	24.014	-0.100	-0.100	0.000	0.000	0.000	0.000
88	A	93	PRO	0	-0.021	-0.011	27.171	0.019	0.019	0.000	0.000	0.000	0.000
89	A	94	GLU	-1	-0.861	-0.938	30.230	0.889	0.889	0.000	0.000	0.000	0.000
90	A	95	PRO	0	0.022	-0.006	31.772	-0.033	-0.033	0.000	0.000	0.000	0.000
91	A	96	HIS	0	-0.040	-0.004	34.032	-0.028	-0.028	0.000	0.000	0.000	0.000
92	A	97	ILE	0	-0.057	-0.024	34.274	-0.040	-0.040	0.000	0.000	0.000	0.000
93	A	98	LEU	0	0.007	0.007	34.705	0.041	0.041	0.000	0.000	0.000	0.000
94	A	99	LEU	0	-0.005	0.002	31.256	-0.018	-0.018	0.000	0.000	0.000	0.000
95	A	100	PHE	0	0.006	-0.003	35.557	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.952	0.969	33.732	-0.836	-0.836	0.000	0.000	0.000	0.000
97	A	102	ARG	1	0.924	0.975	38.504	-0.522	-0.522	0.000	0.000	0.000	0.000
98	A	103	PRO	0	0.066	0.037	39.849	0.019	0.019	0.000	0.000	0.000	0.000
99	A	104	LEU	0	0.024	-0.001	41.129	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	105	ASN	0	-0.028	-0.007	42.719	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	106	TYR	0	0.050	0.018	44.448	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.932	-0.966	45.830	0.387	0.387	0.000	0.000	0.000	0.000
103	A	108	ALA	0	-0.058	-0.031	47.818	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	109	GLU	-1	-0.844	-0.923	42.921	0.528	0.528	0.000	0.000	0.000	0.000
105	A	110	LEU	0	0.016	0.001	47.689	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	111	ARG	1	0.947	0.994	50.120	-0.383	-0.383	0.000	0.000	0.000	0.000
107	A	112	ALA	0	-0.010	-0.006	49.872	-0.016	-0.016	0.000	0.000	0.000	0.000
108	A	113	ALA	0	0.007	-0.011	49.912	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	114	THR	0	-0.072	-0.052	51.982	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	115	ALA	0	-0.029	-0.018	55.321	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	116	ALA	0	-0.034	-0.017	53.381	-0.009	-0.009	0.000	0.000	0.000	0.000
112	A	117	ALA	0	-0.058	-0.019	55.363	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	118	GLN	-1	-0.964	-0.956	56.998	0.255	0.255	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:HIS)