FMO DATABASE

FMODB ID: 3JQML

Calculation Name: 1IUL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1IUL

Chain ID: A

ChEMBL ID:

UniProt ID: Q8GHJ5

Base Structure: X-ray

Registration Date: 2023-09-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1256585.467681
FMO2-HF: Nuclear repulsion	1203604.880572
FMO2-HF: Total energy	-52980.587109
FMO2-MP2: Total energy	-53136.619543

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
-20.245	-10.456	15.417	-8.292	-16.915	-0.054

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.030 / q_NPA : 0.004

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	ASP	-1	-0.745	-0.867	2.888	-3.094	-0.196	0.227	-1.519	-1.607	-0.002
4	A	4	GLN	0	-0.040	-0.023	5.552	0.390	0.390	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.836	-0.939	2.245	-14.308	-9.694	5.452	-4.324	-5.742	-0.050
6	A	6	LEU	0	0.009	-0.005	2.667	-0.030	0.387	4.895	-1.467	-3.845	0.006
7	A	7	ARG	1	0.870	0.930	3.696	-0.372	-0.706	0.036	0.588	-0.290	0.000
8	A	8	ALA	0	0.010	0.026	6.570	-0.057	-0.057	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.014	-0.010	2.268	-1.245	-0.669	4.320	-1.215	-3.680	-0.008
10	A	10	LEU	0	-0.021	-0.012	6.868	-0.377	-0.377	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.064	-0.037	8.929	-0.244	-0.244	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.021	0.001	9.997	-0.084	-0.084	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.050	-0.006	9.803	-0.088	-0.088	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.897	0.937	11.642	0.040	0.040	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.039	-0.042	14.515	0.030	0.030	0.000	0.000	0.000	0.000
16	A	16	ILE	0	0.001	0.001	12.354	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.001	0.020	13.928	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.004	-0.007	14.749	0.028	0.028	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.035	0.028	16.337	-0.017	-0.017	0.000	0.000	0.000	0.000
20	A	20	GLY	0	-0.036	-0.030	18.111	0.016	0.016	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.003	0.009	20.912	0.011	0.011	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.034	0.006	21.938	-0.012	-0.012	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.973	0.992	25.149	-0.038	-0.038	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.784	-0.852	28.185	0.068	0.068	0.000	0.000	0.000	0.000
25	A	25	PRO	0	0.020	0.002	27.317	0.008	0.008	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.056	-0.049	27.182	0.010	0.010	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.840	0.904	24.855	-0.055	-0.055	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.071	0.023	19.963	0.000	0.000	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.004	-0.002	20.188	0.014	0.014	0.000	0.000	0.000	0.000
30	A	30	HIS	0	-0.050	-0.024	21.266	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	31	TYR	0	0.049	-0.004	20.666	0.016	0.016	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.024	-0.002	15.906	0.011	0.011	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.043	0.023	18.081	0.020	0.020	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.830	0.906	19.099	-0.129	-0.129	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.075	-0.060	15.887	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.024	0.002	14.036	0.001	0.001	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.946	0.989	17.625	-0.082	-0.082	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.887	-0.921	20.560	0.131	0.131	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.072	-0.043	17.327	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.009	0.010	18.078	0.011	0.011	0.000	0.000	0.000	0.000
41	A	41	TYR	0	-0.069	-0.032	12.103	0.015	0.015	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.749	0.830	17.450	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.034	-0.028	17.025	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.011	0.004	18.063	-0.015	-0.015	0.000	0.000	0.000	0.000
45	A	45	PRO	0	-0.001	0.001	19.174	0.003	0.003	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.052	0.029	19.677	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.011	-0.045	21.577	0.001	0.001	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.044	0.027	24.301	0.001	0.001	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.800	0.896	25.412	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	50	PHE	0	-0.018	0.000	26.529	0.005	0.005	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.001	0.011	28.393	0.001	0.001	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.010	0.007	29.324	0.000	0.000	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.951	-0.979	30.098	0.025	0.025	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.909	-0.945	28.867	0.041	0.041	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.023	-0.028	25.009	0.006	0.006	0.000	0.000	0.000	0.000
56	A	56	PHE	0	-0.022	-0.023	21.953	0.003	0.003	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.036	-0.019	24.684	0.003	0.003	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.809	-0.876	23.013	0.011	0.011	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.906	-0.945	26.250	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.044	-0.018	25.119	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.034	0.033	23.203	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.012	-0.012	24.670	0.007	0.007	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.045	-0.042	22.871	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.022	-0.007	16.505	0.006	0.006	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.037	-0.024	20.111	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.840	-0.912	22.239	-0.048	-0.048	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.068	-0.024	18.150	0.010	0.010	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.945	0.967	21.946	0.061	0.061	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.827	-0.889	19.004	-0.040	-0.040	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.031	0.010	15.829	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.002	0.008	12.278	0.034	0.034	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.782	-0.869	10.470	-0.174	-0.174	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.040	-0.025	7.775	-0.032	-0.032	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.010	0.001	9.639	0.001	0.001	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.838	-0.935	10.958	0.387	0.387	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.026	-0.019	12.624	-0.060	-0.060	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.024	-0.002	14.687	0.037	0.037	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.875	0.955	17.880	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.050	0.019	18.559	0.005	0.005	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.092	0.032	18.522	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.051	-0.025	19.887	-0.015	-0.015	0.000	0.000	0.000	0.000
82	A	82	ALA	0	-0.040	-0.022	21.752	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.010	0.001	15.542	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	84	MET	0	0.003	0.004	18.726	-0.022	-0.022	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.899	-0.942	20.487	-0.075	-0.075	0.000	0.000	0.000	0.000
86	A	86	HIS	0	-0.047	-0.043	18.775	0.013	0.013	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.022	0.003	15.577	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	88	PRO	0	0.040	0.002	17.415	-0.031	-0.031	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.792	-0.859	19.148	-0.092	-0.092	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.006	-0.010	12.823	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.031	-0.011	14.128	-0.053	-0.053	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.051	-0.019	15.824	-0.027	-0.027	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.043	-0.023	14.412	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.809	0.905	12.307	0.599	0.599	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.002	0.007	10.159	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.015	0.006	8.348	-0.125	-0.125	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.051	-0.025	2.946	-0.902	-0.383	0.056	-0.085	-0.490	0.000
98	A	98	VAL	0	0.003	0.011	6.189	0.346	0.346	0.000	0.000	0.000	0.000
99	A	99	TRP	0	0.012	-0.022	6.174	0.313	0.313	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.035	-0.025	8.953	-0.107	-0.107	0.000	0.000	0.000	0.000
101	A	101	GLN	0	0.091	0.038	11.879	0.158	0.158	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.022	-0.028	14.325	-0.022	-0.022	0.000	0.000	0.000	0.000
103	A	103	GLY	0	-0.010	-0.002	16.026	-0.028	-0.028	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.078	-0.026	15.517	-0.039	-0.039	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.818	0.872	11.089	0.028	0.028	0.000	0.000	0.000	0.000
106	A	106	HIS	0	0.002	-0.007	14.563	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	107	PRO	0	0.020	0.009	14.883	-0.036	-0.036	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.872	-0.940	14.926	-0.170	-0.170	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.076	0.019	12.987	-0.048	-0.048	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.769	-0.856	10.706	-0.165	-0.165	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.906	0.969	11.094	0.185	0.185	0.000	0.000	0.000	0.000
112	A	112	ALA	0	0.067	0.027	13.089	-0.068	-0.068	0.000	0.000	0.000	0.000
113	A	113	LEU	0	0.018	0.013	10.092	-0.035	-0.035	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.922	0.961	7.642	1.126	1.126	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.971	-0.993	9.942	-0.430	-0.430	0.000	0.000	0.000	0.000
116	A	116	ALA	0	0.000	0.021	12.731	0.020	0.020	0.000	0.000	0.000	0.000
117	A	117	GLY	0	-0.036	-0.022	10.090	0.026	0.026	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.028	-0.004	7.860	-0.205	-0.205	0.000	0.000	0.000	0.000
119	A	119	PRO	0	-0.010	0.001	2.631	-0.516	-0.109	0.333	-0.135	-0.605	0.000
120	A	120	VAL	0	0.010	-0.003	4.448	0.562	0.667	-0.001	-0.005	-0.100	0.000
121	A	121	VAL	0	-0.012	0.009	3.906	-0.424	0.163	0.099	-0.130	-0.556	0.000
122	A	122	ALA	0	-0.009	-0.007	6.344	-0.214	-0.214	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.889	-0.929	9.794	0.275	0.275	0.000	0.000	0.000	0.000
124	A	124	ARG	1	0.921	0.956	4.958	-0.618	-0.618	0.000	0.000	0.000	0.000
125	A	125	CYS	0	-0.051	0.013	11.678	-0.023	-0.023	0.000	0.000	0.000	0.000
126	A	126	LEU	0	0.060	0.028	9.352	0.066	0.066	0.000	0.000	0.000	0.000
127	A	127	MET	0	0.023	0.025	11.951	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.041	-0.038	14.335	-0.015	-0.015	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.747	-0.841	8.531	0.830	0.830	0.000	0.000	0.000	0.000
130	A	130	HIS	0	0.039	0.048	10.872	0.011	0.011	0.000	0.000	0.000	0.000
131	A	131	LYS	1	0.876	0.921	12.260	-0.307	-0.307	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.718	0.818	7.796	-0.523	-0.523	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.048	-0.013	6.970	-0.060	-0.060	0.000	0.000	0.000	0.000
134	A	134	PHE	0	0.013	0.029	10.105	-0.072	-0.072	0.000	0.000	0.000	0.000

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