FMO DATABASE

FMODB ID: QKJ9Y

Calculation Name: 1MUI-A-Xray547

Preferred Name:

Target Type:

Ligand Name: n-{1-benzyl-4-[2-(2,6-dimethyl-phenoxy)-acetylamino]-3-hydroxy-5-phenyl-pentyl}-3-methyl-2-(2-oxo-tetrahydro-pyrimidin-1-yl)-butyramide

Ligand 3-letter code: AB1

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1MUI

Chain ID: A

ChEMBL ID:

UniProt ID: Q903J0

Base Structure: X-ray

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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-679300.615368
FMO2-HF: Nuclear repulsion	641537.51942
FMO2-HF: Total energy	-37763.095948
FMO2-MP2: Total energy	-37872.660684

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:PRO)

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

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.
-23.513	-19.871	0.217	-1.494	-2.366	-0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.871 / q_NPA : 0.913

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	ILE	0	0.012	0.004	3.044	-4.186	-1.181	0.175	-1.319	-1.861	-0.007
4	A	4	THR	0	0.011	0.008	5.089	3.964	3.987	-0.001	-0.005	-0.017	0.000
67	A	67	CYS	0	-0.025	-0.016	4.205	-5.703	-5.289	0.042	-0.132	-0.325	-0.001
69	A	69	HIS	0	-0.025	0.000	3.516	5.575	5.775	0.001	-0.038	-0.163	0.000
5	A	5	LEU	0	0.032	0.000	8.732	-0.439	-0.439	0.000	0.000	0.000	0.000
6	A	6	TRP	0	0.006	0.011	11.761	1.999	1.999	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.018	-0.006	12.083	0.792	0.792	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.974	0.985	12.208	15.391	15.391	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.049	0.035	8.449	-0.356	-0.356	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.012	-0.005	9.485	0.055	0.055	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.015	-0.005	5.437	-3.887	-3.887	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.008	0.019	8.029	3.028	3.028	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.003	-0.016	9.369	-2.381	-2.381	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.890	0.942	12.041	19.269	19.269	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.046	0.011	14.772	-0.284	-0.284	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.022	0.019	17.701	0.568	0.568	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.041	-0.023	20.157	0.547	0.547	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.044	-0.009	19.985	0.051	0.051	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.016	0.001	14.982	-0.768	-0.768	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.911	0.946	15.071	15.668	15.668	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.875	-0.939	12.096	-22.866	-22.866	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.036	-0.026	11.645	1.716	1.716	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.006	0.005	10.823	-1.952	-1.952	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.008	-0.013	5.838	0.077	0.077	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.853	-0.937	10.397	-18.193	-18.193	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.013	-0.017	12.012	0.516	0.516	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.003	-0.001	14.436	0.841	0.841	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.001	0.026	16.955	1.024	1.024	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.838	-0.900	17.294	-15.621	-15.621	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.861	-0.930	18.537	-14.355	-14.355	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.013	-0.010	16.073	-0.795	-0.795	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.042	-0.025	18.097	0.992	0.992	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.006	-0.004	16.463	-0.781	-0.781	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.821	-0.916	19.877	-14.070	-14.070	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.829	-0.907	22.171	-11.025	-11.025	0.000	0.000	0.000	0.000
36	A	36	MET	0	-0.013	0.007	20.882	-0.436	-0.436	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.004	0.012	25.359	0.094	0.094	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.020	0.001	21.560	-0.515	-0.515	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.001	-0.011	24.836	0.363	0.363	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.016	0.030	26.627	0.343	0.343	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.962	0.973	28.153	9.187	9.187	0.000	0.000	0.000	0.000
42	A	42	TRP	0	0.019	0.011	28.646	-0.278	-0.278	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.939	0.963	29.681	9.954	9.954	0.000	0.000	0.000	0.000
44	A	44	PRO	0	-0.033	-0.010	30.342	-0.328	-0.328	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.909	0.962	25.077	12.577	12.577	0.000	0.000	0.000	0.000
46	A	46	MET	0	-0.039	-0.031	30.079	0.133	0.133	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.034	0.023	23.866	-0.093	-0.093	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.013	0.008	27.841	0.285	0.285	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.032	0.010	25.703	-0.542	-0.542	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.002	-0.012	25.547	0.338	0.338	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.018	0.014	27.516	0.321	0.321	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.001	0.015	30.209	0.373	0.373	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.033	-0.019	29.827	-0.356	-0.356	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.039	0.028	25.279	0.249	0.249	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.918	0.949	29.695	9.211	9.211	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.010	0.008	25.351	-0.113	-0.113	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.756	0.869	27.513	11.022	11.022	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.027	-0.034	25.404	-0.358	-0.358	0.000	0.000	0.000	0.000
59	A	59	TYR	0	0.015	0.000	23.728	0.549	0.549	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.817	-0.897	23.500	-12.601	-12.601	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.009	-0.019	21.908	-0.178	-0.178	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.003	0.014	18.875	0.135	0.135	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.001	0.002	16.032	-0.678	-0.678	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.000	-0.009	12.892	0.397	0.397	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.857	-0.915	11.535	-20.798	-20.798	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.045	0.019	7.281	0.360	0.360	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.005	0.002	5.252	-4.527	-4.527	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.858	0.922	8.184	22.630	22.630	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.035	0.021	11.548	-0.232	-0.232	0.000	0.000	0.000	0.000
72	A	72	ILE	0	0.006	-0.005	13.355	0.877	0.877	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.049	0.032	17.088	-0.053	-0.053	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.073	-0.042	19.037	0.312	0.312	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.007	0.002	18.311	-0.777	-0.777	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.028	-0.008	20.881	0.937	0.937	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.025	0.021	22.211	-0.469	-0.469	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.030	-0.007	24.378	0.700	0.700	0.000	0.000	0.000	0.000
79	A	79	PRO	0	-0.021	0.021	25.024	-0.397	-0.397	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.023	-0.024	20.508	0.270	0.270	0.000	0.000	0.000	0.000
81	A	81	PRO	0	-0.019	-0.023	22.280	0.012	0.012	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.016	0.016	17.332	-0.198	-0.198	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.043	-0.018	15.661	0.806	0.806	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.004	0.000	15.091	-1.091	-1.091	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.007	-0.007	10.954	0.726	0.726	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.097	0.049	13.299	-0.890	-0.890	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.851	0.886	13.948	15.888	15.888	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.020	0.001	14.867	-1.238	-1.238	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.016	0.001	12.721	0.206	0.206	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.027	-0.019	9.098	-1.945	-1.945	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.008	-0.014	9.774	-2.226	-2.226	0.000	0.000	0.000	0.000
92	A	92	GLN	0	-0.039	-0.026	12.057	-0.663	-0.663	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.038	-0.015	6.458	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.003	0.013	6.917	-5.243	-5.243	0.000	0.000	0.000	0.000
95	A	95	CYS	0	-0.080	-0.032	6.129	-4.058	-4.058	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.009	-0.008	7.009	4.278	4.278	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.023	-0.010	8.307	-2.661	-2.661	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.040	-0.034	10.487	2.704	2.704	0.000	0.000	0.000	0.000
99	A	99	PHE	-1	-0.928	-0.940	12.167	-20.206	-20.206	0.000	0.000	0.000	0.000

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