FMO DATABASE

FMODB ID: MR27Z

Calculation Name: 1J6Y-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1J6Y

Chain ID: A

ChEMBL ID:

UniProt ID: Q9SL42

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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	-915807.535769
FMO2-HF: Nuclear repulsion	869668.309009
FMO2-HF: Total energy	-46139.226759
FMO2-MP2: Total energy	-46273.928193

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:HIS)

Summations of interaction energy for fragment #1(A:1: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.
22.755	24.631	-0.026	-0.759	-1.09	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.796 / 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	ALA	0	0.048	0.028	3.826	2.946	4.822	-0.026	-0.759	-1.090	-0.001
4	A	4	SER	0	-0.005	-0.002	6.706	4.493	4.493	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.940	0.972	7.087	17.333	17.333	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.840	-0.914	6.220	-43.036	-43.036	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.056	-0.035	7.127	5.735	5.735	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.014	0.028	9.622	0.567	0.567	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.965	0.980	11.553	21.185	21.185	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.015	-0.021	14.590	0.709	0.709	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.009	-0.008	18.387	-0.074	-0.074	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.014	0.014	21.577	-0.029	-0.029	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.043	0.050	24.564	0.088	0.088	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.070	-0.021	28.114	-0.212	-0.212	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.018	0.013	30.457	0.286	0.286	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.915	0.966	34.223	7.676	7.676	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.016	0.032	34.112	0.047	0.047	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.018	0.007	38.089	-0.118	-0.118	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.006	0.007	35.279	-0.069	-0.069	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.007	-0.014	34.238	0.131	0.131	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.905	0.940	31.247	9.517	9.517	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.950	0.977	36.319	8.566	8.566	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.946	0.989	37.417	7.811	7.811	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.103	0.057	33.655	-0.080	-0.080	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.095	-0.054	31.997	-0.312	-0.312	0.000	0.000	0.000	0.000
26	A	26	TRP	0	0.058	0.026	32.550	0.169	0.169	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.909	0.977	35.928	8.404	8.404	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.889	-0.953	38.442	-7.767	-7.767	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.002	-0.002	41.467	-0.042	-0.042	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.886	-0.943	44.483	-6.926	-6.926	0.000	0.000	0.000	0.000
31	A	31	GLY	0	-0.010	-0.008	45.333	0.031	0.031	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.857	0.912	48.685	6.564	6.564	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.004	0.020	43.541	-0.072	-0.072	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.032	0.012	46.529	0.162	0.162	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.026	0.017	46.554	-0.154	-0.154	0.000	0.000	0.000	0.000
36	A	36	THR	0	-0.057	-0.039	42.663	0.003	0.003	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.016	0.004	39.167	0.051	0.051	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.035	0.007	41.149	-0.181	-0.181	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.968	0.965	33.726	8.884	8.884	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.903	-0.935	38.616	-7.316	-7.316	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.061	0.027	40.278	-0.127	-0.127	0.000	0.000	0.000	0.000
42	A	42	ALA	0	-0.015	-0.014	36.477	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.040	0.030	35.460	-0.168	-0.168	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.800	-0.886	37.326	-7.685	-7.685	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.026	-0.013	37.864	0.056	0.056	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.020	0.003	31.648	-0.031	-0.031	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.828	0.909	35.410	7.880	7.880	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.021	0.000	37.491	0.023	0.023	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.012	-0.009	33.517	-0.044	-0.044	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.830	0.903	31.438	9.475	9.475	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.863	-0.896	33.945	-8.298	-8.298	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.876	-0.945	36.752	-7.925	-7.925	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.102	-0.055	30.628	-0.190	-0.190	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.062	-0.030	32.189	-0.365	-0.365	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.064	-0.055	33.737	-0.080	-0.080	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.033	0.020	36.703	0.176	0.176	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.834	0.919	29.071	10.092	10.092	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.034	0.019	35.069	0.054	0.054	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.041	-0.026	33.070	-0.099	-0.099	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.010	-0.011	25.702	0.016	0.016	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.804	-0.898	27.799	-9.890	-9.890	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.938	-0.951	29.303	-8.697	-8.697	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.044	0.007	32.474	0.051	0.051	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.020	0.019	27.734	0.118	0.118	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.060	-0.031	29.111	-0.338	-0.338	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.911	0.960	30.677	8.168	8.168	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.086	-0.034	32.994	0.141	0.141	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.086	-0.001	28.609	-0.294	-0.294	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.801	-0.884	27.127	-11.023	-11.023	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.039	-0.011	29.126	-0.036	-0.036	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.019	-0.012	24.025	-0.021	-0.021	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.010	-0.030	24.417	-0.160	-0.160	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.006	0.015	26.100	0.031	0.031	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.883	0.936	26.269	10.873	10.873	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.887	0.934	18.419	14.817	14.817	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.094	0.056	24.281	-0.294	-0.294	0.000	0.000	0.000	0.000
77	A	77	GLY	0	-0.032	-0.004	23.456	0.086	0.086	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.889	-0.977	17.625	-16.477	-16.477	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.027	-0.005	17.627	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	80	GLY	0	-0.022	0.004	14.901	-0.590	-0.590	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.094	-0.071	10.095	-0.695	-0.695	0.000	0.000	0.000	0.000
82	A	82	PHE	0	0.009	0.008	11.929	-0.847	-0.847	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.027	0.008	10.261	-0.204	-0.204	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.935	0.983	11.224	24.195	24.195	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.018	0.004	13.315	0.463	0.463	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.031	-0.023	14.449	-0.190	-0.190	0.000	0.000	0.000	0.000
87	A	87	MET	0	0.019	0.042	17.080	0.142	0.142	0.000	0.000	0.000	0.000
88	A	88	GLN	0	0.025	-0.006	19.912	0.766	0.766	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.975	0.985	21.164	12.299	12.299	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.048	0.040	22.586	-0.201	-0.201	0.000	0.000	0.000	0.000
91	A	91	PHE	0	0.096	0.034	19.258	0.006	0.006	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.908	-0.962	15.992	-18.832	-18.832	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.919	-0.961	19.275	-14.423	-14.423	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.000	0.002	21.559	0.040	0.040	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.077	-0.051	17.960	0.210	0.210	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.108	-0.077	12.138	-0.766	-0.766	0.000	0.000	0.000	0.000
97	A	97	ALA	0	-0.003	0.013	18.609	-0.037	-0.037	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.028	0.015	21.755	0.483	0.483	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.880	0.930	20.890	11.596	11.596	0.000	0.000	0.000	0.000
100	A	100	VAL	0	-0.029	-0.021	21.981	0.131	0.131	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.012	-0.001	24.484	0.033	0.033	0.000	0.000	0.000	0.000
102	A	102	ASP	-1	-0.839	-0.917	28.243	-10.260	-10.260	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.051	-0.012	26.984	0.092	0.092	0.000	0.000	0.000	0.000
104	A	104	SER	0	-0.010	-0.011	25.571	-0.074	-0.074	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.825	-0.906	27.470	-9.674	-9.674	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.058	-0.026	30.435	0.204	0.204	0.000	0.000	0.000	0.000
107	A	107	VAL	0	0.000	0.009	25.231	-0.284	-0.284	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.881	-0.956	28.627	-9.679	-9.679	0.000	0.000	0.000	0.000
109	A	109	THR	0	-0.060	-0.060	25.555	0.113	0.113	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.892	-0.928	23.646	-12.929	-12.929	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.068	-0.049	27.008	0.359	0.359	0.000	0.000	0.000	0.000
112	A	112	GLY	0	-0.079	-0.086	29.600	0.482	0.482	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.003	0.021	31.194	-0.057	-0.057	0.000	0.000	0.000	0.000
114	A	114	HIS	0	0.012	-0.006	26.746	0.154	0.154	0.000	0.000	0.000	0.000
115	A	115	ILE	0	0.028	0.013	27.697	0.166	0.166	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.004	0.005	21.728	-0.208	-0.208	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.910	0.971	23.238	11.003	11.003	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.927	0.979	16.502	16.506	16.506	0.000	0.000	0.000	0.000
119	A	119	THR	0	-0.036	-0.012	20.124	-0.286	-0.286	0.000	0.000	0.000	0.000
120	A	120	ALA	-1	-0.833	-0.912	22.026	-11.195	-11.195	0.000	0.000	0.000	0.000

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