FMO DATABASE

FMODB ID: KV583

Calculation Name: 4IOH-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4IOH

Chain ID: A

ChEMBL ID:

UniProt ID: Q8DJY4

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-894998.946953
FMO2-HF: Nuclear repulsion	847840.673597
FMO2-HF: Total energy	-47158.273356
FMO2-MP2: Total energy	-47289.177322

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:2:MET)

Summations of interaction energy for fragment #1(A:2:MET)

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.
-34.462	-32.512	0.086	-0.846	-1.19	-0.003

Interaction energy analysis for fragmet #1(A:2:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.878 / q_NPA : 0.922

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

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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	4	THR	0	0.007	0.005	3.187	-2.080	-0.238	0.087	-0.839	-1.090	-0.003
4	A	5	MET	0	-0.002	0.006	4.735	1.264	1.372	-0.001	-0.007	-0.100	0.000
5	A	6	ASN	0	0.035	0.018	7.289	1.965	1.965	0.000	0.000	0.000	0.000
6	A	7	VAL	0	0.014	-0.005	11.054	-0.581	-0.581	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.019	-0.004	13.690	0.685	0.685	0.000	0.000	0.000	0.000
8	A	9	GLY	0	-0.010	0.007	10.519	0.515	0.515	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.017	0.005	10.257	-1.354	-1.354	0.000	0.000	0.000	0.000
10	A	11	PRO	0	0.010	-0.020	8.438	-1.497	-1.497	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.065	-0.020	8.477	2.650	2.650	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.904	-0.945	10.286	-19.626	-19.626	0.000	0.000	0.000	0.000
13	A	14	CYS	0	-0.031	-0.015	13.792	0.483	0.483	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.040	-0.021	16.341	0.895	0.895	0.000	0.000	0.000	0.000
15	A	17	GLN	0	0.021	0.015	21.208	0.125	0.125	0.000	0.000	0.000	0.000
16	A	18	ASN	0	-0.030	-0.014	24.935	-0.101	-0.101	0.000	0.000	0.000	0.000
17	A	19	PRO	0	0.012	0.006	27.509	0.185	0.185	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.008	0.002	21.394	-0.141	-0.141	0.000	0.000	0.000	0.000
19	A	21	THR	0	0.044	0.018	23.088	0.371	0.371	0.000	0.000	0.000	0.000
20	A	22	GLY	0	0.073	0.029	22.870	-0.617	-0.617	0.000	0.000	0.000	0.000
21	A	23	PHE	0	-0.025	-0.021	23.939	0.310	0.310	0.000	0.000	0.000	0.000
22	A	24	TYR	0	-0.048	-0.038	20.882	0.221	0.221	0.000	0.000	0.000	0.000
23	A	25	ARG	1	0.849	0.938	21.431	11.256	11.256	0.000	0.000	0.000	0.000
24	A	26	ASP	-1	-0.732	-0.855	17.176	-17.280	-17.280	0.000	0.000	0.000	0.000
25	A	27	GLY	0	0.009	0.004	17.933	-0.815	-0.815	0.000	0.000	0.000	0.000
26	A	28	PHE	0	-0.033	-0.016	15.198	0.102	0.102	0.000	0.000	0.000	0.000
27	A	29	CYS	0	-0.070	0.024	20.260	0.323	0.323	0.000	0.000	0.000	0.000
28	A	30	ARG	1	0.855	0.914	17.546	17.271	17.271	0.000	0.000	0.000	0.000
29	A	31	THR	0	0.064	0.024	21.359	0.399	0.399	0.000	0.000	0.000	0.000
30	A	32	GLY	0	-0.019	-0.033	21.449	-0.919	-0.919	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.004	-0.007	22.973	0.496	0.496	0.000	0.000	0.000	0.000
32	A	34	GLY	0	0.010	0.015	25.252	0.425	0.425	0.000	0.000	0.000	0.000
33	A	35	ASP	-1	-0.835	-0.885	26.714	-10.749	-10.749	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.020	0.002	28.338	-0.055	-0.055	0.000	0.000	0.000	0.000
35	A	37	GLY	0	-0.047	-0.024	30.976	0.285	0.285	0.000	0.000	0.000	0.000
36	A	38	ALA	0	0.032	0.020	27.978	0.081	0.081	0.000	0.000	0.000	0.000
37	A	39	HIS	1	0.816	0.885	27.184	11.018	11.018	0.000	0.000	0.000	0.000
38	A	40	VAL	0	-0.001	-0.002	24.596	-0.458	-0.458	0.000	0.000	0.000	0.000
39	A	41	VAL	0	0.040	0.022	25.794	-0.370	-0.370	0.000	0.000	0.000	0.000
40	A	42	CYS	0	-0.026	-0.010	24.596	0.294	0.294	0.000	0.000	0.000	0.000
41	A	43	ALA	0	0.042	0.027	27.100	0.114	0.114	0.000	0.000	0.000	0.000
42	A	44	GLN	0	-0.063	-0.045	30.367	-0.243	-0.243	0.000	0.000	0.000	0.000
43	A	45	MET	0	-0.048	-0.011	32.292	0.343	0.343	0.000	0.000	0.000	0.000
44	A	46	THR	0	0.073	0.001	35.336	0.018	0.018	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.013	-0.007	38.906	0.026	0.026	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.802	-0.862	41.088	-7.713	-7.713	0.000	0.000	0.000	0.000
47	A	49	PHE	0	0.079	0.036	35.825	0.051	0.051	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.023	-0.006	36.947	0.013	0.013	0.000	0.000	0.000	0.000
49	A	51	THR	0	-0.058	-0.038	40.554	0.119	0.119	0.000	0.000	0.000	0.000
50	A	52	PHE	0	0.016	0.011	41.454	0.156	0.156	0.000	0.000	0.000	0.000
51	A	53	THR	0	0.032	0.011	38.173	0.076	0.076	0.000	0.000	0.000	0.000
52	A	54	ARG	1	0.863	0.931	41.435	7.390	7.390	0.000	0.000	0.000	0.000
53	A	55	SER	0	-0.099	-0.056	43.537	0.125	0.125	0.000	0.000	0.000	0.000
54	A	56	ARG	1	0.884	0.955	42.656	7.327	7.327	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.017	0.019	43.642	-0.053	-0.053	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.094	-0.065	36.357	-0.248	-0.248	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.700	-0.834	39.604	-7.872	-7.872	0.000	0.000	0.000	0.000
58	A	60	LEU	0	0.005	0.014	34.724	-0.177	-0.177	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.003	-0.005	36.692	-0.179	-0.179	0.000	0.000	0.000	0.000
60	A	62	THR	0	-0.058	-0.055	39.334	0.094	0.094	0.000	0.000	0.000	0.000
61	A	63	PRO	0	-0.079	-0.038	37.709	-0.198	-0.198	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.053	0.028	35.723	0.225	0.225	0.000	0.000	0.000	0.000
63	A	65	PRO	0	-0.006	-0.007	35.370	-0.282	-0.282	0.000	0.000	0.000	0.000
64	A	66	ALA	0	0.006	0.013	35.546	-0.061	-0.061	0.000	0.000	0.000	0.000
65	A	67	TYR	0	0.010	-0.003	29.321	-0.109	-0.109	0.000	0.000	0.000	0.000
66	A	68	GLN	0	-0.021	-0.007	30.370	-0.259	-0.259	0.000	0.000	0.000	0.000
67	A	69	PHE	0	0.019	0.013	31.023	-0.346	-0.346	0.000	0.000	0.000	0.000
68	A	70	PRO	0	-0.019	-0.007	32.261	0.348	0.348	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.053	0.031	33.976	-0.215	-0.215	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.005	0.003	31.679	-0.019	-0.019	0.000	0.000	0.000	0.000
71	A	73	LYS	1	0.852	0.919	34.932	9.184	9.184	0.000	0.000	0.000	0.000
72	A	74	PRO	0	0.003	-0.015	35.691	-0.200	-0.200	0.000	0.000	0.000	0.000
73	A	75	GLY	0	-0.015	0.008	34.996	0.045	0.045	0.000	0.000	0.000	0.000
74	A	76	ASP	-1	-0.802	-0.896	31.485	-10.043	-10.043	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.902	0.950	27.148	11.161	11.161	0.000	0.000	0.000	0.000
76	A	78	TRP	0	0.002	-0.011	28.186	-0.183	-0.183	0.000	0.000	0.000	0.000
77	A	80	LEU	0	0.030	0.004	27.835	0.214	0.214	0.000	0.000	0.000	0.000
78	A	81	CYS	0	-0.058	-0.022	30.008	-0.325	-0.325	0.000	0.000	0.000	0.000
79	A	82	ALA	0	0.074	0.043	30.283	0.276	0.276	0.000	0.000	0.000	0.000
80	A	83	SER	0	0.010	0.002	32.203	0.173	0.173	0.000	0.000	0.000	0.000
81	A	84	ARG	1	0.800	0.875	35.215	8.333	8.333	0.000	0.000	0.000	0.000
82	A	85	TRP	0	-0.016	-0.006	33.558	0.154	0.154	0.000	0.000	0.000	0.000
83	A	86	ARG	1	0.935	0.966	35.594	8.689	8.689	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.825	-0.887	37.465	-7.581	-7.581	0.000	0.000	0.000	0.000
85	A	88	ALA	0	-0.006	-0.014	38.565	0.220	0.220	0.000	0.000	0.000	0.000
86	A	89	LEU	0	-0.037	0.001	37.179	0.151	0.151	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.935	-0.976	40.000	-7.612	-7.612	0.000	0.000	0.000	0.000
88	A	91	ALA	0	-0.062	-0.029	42.988	0.221	0.221	0.000	0.000	0.000	0.000
89	A	92	GLY	0	-0.027	-0.013	43.505	0.132	0.132	0.000	0.000	0.000	0.000
90	A	93	VAL	0	-0.048	-0.020	42.211	0.038	0.038	0.000	0.000	0.000	0.000
91	A	94	ALA	0	0.012	0.005	37.077	-0.129	-0.129	0.000	0.000	0.000	0.000
92	A	95	PRO	0	-0.042	-0.004	34.598	0.048	0.048	0.000	0.000	0.000	0.000
93	A	96	PRO	0	0.070	0.041	33.639	-0.165	-0.165	0.000	0.000	0.000	0.000
94	A	97	VAL	0	-0.021	-0.029	29.436	-0.274	-0.274	0.000	0.000	0.000	0.000
95	A	98	ILE	0	0.001	-0.006	24.481	0.055	0.055	0.000	0.000	0.000	0.000
96	A	99	LEU	0	0.025	0.012	25.559	-0.388	-0.388	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.927	-0.968	21.070	-13.007	-13.007	0.000	0.000	0.000	0.000
98	A	101	ALA	0	-0.046	-0.027	20.497	-0.899	-0.899	0.000	0.000	0.000	0.000
99	A	102	THR	0	-0.058	-0.019	22.278	0.267	0.267	0.000	0.000	0.000	0.000
100	A	103	HIS	0	0.019	0.029	19.744	0.173	0.173	0.000	0.000	0.000	0.000
101	A	104	ALA	0	0.045	0.011	22.218	0.549	0.549	0.000	0.000	0.000	0.000
102	A	105	SER	0	0.035	0.006	24.033	0.529	0.529	0.000	0.000	0.000	0.000
103	A	106	ALA	0	0.008	-0.002	26.250	0.507	0.507	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.027	-0.019	26.962	0.414	0.414	0.000	0.000	0.000	0.000
105	A	108	GLU	-1	-0.967	-0.972	27.292	-11.272	-11.272	0.000	0.000	0.000	0.000
106	A	109	TYR	0	-0.119	-0.063	30.257	0.344	0.344	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.033	-0.017	32.284	0.397	0.397	0.000	0.000	0.000	0.000
108	A	111	SER	0	-0.030	-0.034	32.930	-0.196	-0.196	0.000	0.000	0.000	0.000
109	A	112	LEU	0	0.028	-0.006	28.312	-0.286	-0.286	0.000	0.000	0.000	0.000
110	A	113	GLU	-1	-0.893	-0.964	31.579	-9.545	-9.545	0.000	0.000	0.000	0.000
111	A	114	ASP	-1	-0.792	-0.870	34.710	-8.995	-8.995	0.000	0.000	0.000	0.000
112	A	115	LEU	0	0.010	0.001	29.021	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.921	0.952	29.941	10.085	10.085	0.000	0.000	0.000	0.000
114	A	117	ALA	0	-0.036	-0.008	32.783	0.062	0.062	0.000	0.000	0.000	0.000
115	A	118	HIS	0	-0.010	0.003	35.080	0.045	0.045	0.000	0.000	0.000	0.000
116	A	119	ALA	0	0.044	0.033	31.222	-0.270	-0.270	0.000	0.000	0.000	0.000
117	A	120	LEU	0	-0.081	-0.054	29.752	0.197	0.197	0.000	0.000	0.000	0.000
118	A	121	GLY	-1	-0.954	-0.952	32.399	-9.175	-9.175	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:MET)