FMO DATABASE

FMODB ID: 851ZY

Calculation Name: 1O5L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O5L

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X0Q3

Base Structure: X-ray

Registration Date: 2023-09-20

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

DOI:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1103788.59086
FMO2-HF: Nuclear repulsion	1052981.032726
FMO2-HF: Total energy	-50807.558134
FMO2-MP2: Total energy	-50957.874609

3D Structure

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.
-23.594	-12.611	15.396	-6.41	-19.97	-0.053

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 : -0.025 / q_NPA : -0.002

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	LEU	0	0.015	-0.013	2.695	-0.493	2.809	1.486	-1.069	-3.718	-0.001
4	A	4	LYS	1	0.904	0.963	4.158	-1.137	-1.003	0.003	0.059	-0.196	0.000
5	A	5	LYS	1	0.897	0.960	2.846	-8.869	-7.065	1.214	-0.964	-2.055	0.011
6	A	6	LEU	0	-0.008	-0.012	4.661	-0.896	-0.666	0.001	-0.028	-0.203	0.000
7	A	7	LEU	0	-0.011	-0.008	7.742	-0.396	-0.396	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.026	-0.016	10.338	-0.140	-0.140	0.000	0.000	0.000	0.000
9	A	9	CYS	0	-0.053	-0.010	9.128	-0.081	-0.081	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.024	0.012	12.516	-0.091	-0.091	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.877	0.969	14.592	-0.017	-0.017	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.022	-0.005	15.287	0.009	0.009	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.017	-0.003	17.420	-0.024	-0.024	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.033	-0.018	18.451	0.009	0.009	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.050	0.029	19.321	-0.012	-0.012	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.861	0.917	22.950	-0.073	-0.073	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.925	0.955	25.195	-0.036	-0.036	0.000	0.000	0.000	0.000
18	A	18	GLY	0	-0.017	-0.007	25.812	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.853	-0.910	25.270	0.036	0.036	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.003	-0.003	24.655	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.076	-0.033	18.595	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.792	0.891	20.395	0.082	0.082	0.000	0.000	0.000	0.000
23	A	23	HIS	0	-0.003	0.001	23.128	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	24	GLN	0	0.028	0.014	25.125	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.902	-0.958	25.739	-0.106	-0.106	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.842	-0.902	24.112	-0.068	-0.068	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.019	-0.019	23.710	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	28	ILE	0	-0.010	0.009	17.095	0.008	0.008	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.842	-0.919	20.037	-0.103	-0.103	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.810	-0.893	16.317	-0.019	-0.019	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.027	-0.010	10.229	-0.027	-0.027	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.005	0.000	13.273	0.088	0.088	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.004	-0.007	6.933	-0.074	-0.074	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.012	0.021	10.605	0.102	0.102	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.016	-0.010	10.052	0.004	0.004	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.835	-0.947	11.937	0.413	0.413	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.019	0.025	14.908	-0.018	-0.018	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.018	-0.014	16.795	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.058	-0.014	15.988	0.014	0.014	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.840	0.899	19.071	0.034	0.034	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.001	0.013	18.970	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.873	-0.953	21.938	-0.057	-0.057	0.000	0.000	0.000	0.000
43	A	43	HIS	0	0.021	0.013	25.599	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.024	-0.009	27.567	0.010	0.010	0.000	0.000	0.000	0.000
45	A	45	SER	0	0.011	-0.019	30.716	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.876	-0.954	33.797	-0.078	-0.078	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.095	-0.048	36.819	0.002	0.002	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.009	0.012	35.515	0.005	0.005	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.852	0.931	33.552	0.060	0.060	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.087	0.060	29.299	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.062	-0.019	28.937	0.008	0.008	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.783	-0.875	24.383	-0.069	-0.069	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.116	-0.056	22.365	0.000	0.000	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.841	-0.926	18.937	-0.216	-0.216	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.891	-0.933	19.095	-0.020	-0.020	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.033	-0.011	13.370	-0.033	-0.033	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.844	0.901	14.132	0.080	0.080	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.042	-0.005	11.198	-0.065	-0.065	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.045	-0.020	6.855	0.056	0.056	0.000	0.000	0.000	0.000
60	A	60	GLN	0	0.035	0.007	7.038	-0.250	-0.250	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.023	-0.014	6.218	0.187	0.187	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.015	0.006	9.566	-0.045	-0.045	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.005	0.004	13.359	0.005	0.005	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.036	-0.018	10.862	0.070	0.070	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.018	-0.019	12.694	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.002	0.002	15.238	0.025	0.025	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.009	0.008	12.144	0.030	0.030	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.005	-0.020	12.131	0.033	0.033	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.009	0.018	17.448	0.000	0.000	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.022	-0.002	20.774	0.007	0.007	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.892	-0.931	24.162	-0.129	-0.129	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.007	0.020	20.016	0.004	0.004	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.852	0.889	22.062	0.139	0.139	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.002	-0.005	17.298	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	75	PRO	0	-0.004	0.005	20.478	0.016	0.016	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.043	-0.019	21.343	0.007	0.007	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.014	0.014	23.127	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.030	-0.013	18.386	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.047	0.023	21.685	0.016	0.016	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.012	0.018	21.290	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.034	0.005	21.556	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.938	-0.959	20.170	0.078	0.078	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.004	0.008	21.982	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.026	0.002	17.866	0.006	0.006	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.822	0.896	16.114	-0.266	-0.266	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.027	0.014	14.052	0.007	0.007	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.013	0.011	9.542	0.026	0.026	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.047	-0.056	13.033	-0.067	-0.067	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.007	-0.008	9.528	0.041	0.041	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.050	0.032	13.655	-0.061	-0.061	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.873	0.932	14.107	0.215	0.215	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.900	-0.949	14.073	-0.267	-0.267	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.009	0.007	11.935	-0.033	-0.033	0.000	0.000	0.000	0.000
94	A	94	PHE	0	-0.015	-0.019	7.137	-0.056	-0.056	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.031	0.006	9.611	-0.150	-0.150	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.842	-0.914	11.376	-0.345	-0.345	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.000	-0.012	6.928	-0.037	-0.037	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.025	-0.005	6.325	-0.323	-0.323	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.059	-0.023	7.966	-0.128	-0.128	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.781	0.891	9.429	0.345	0.345	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.828	-0.903	2.999	-6.630	-5.169	0.178	-0.795	-0.845	-0.008
102	A	102	ARG	1	0.980	0.979	5.829	0.672	0.672	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.888	-0.948	2.150	-4.280	-1.024	5.305	-3.343	-5.218	-0.038
104	A	104	LEU	0	0.011	0.001	2.148	-3.590	-2.376	4.448	-1.980	-3.683	-0.004
105	A	105	LEU	0	-0.002	0.003	2.762	3.444	0.721	0.160	2.881	-0.317	-0.002
106	A	106	LEU	0	-0.045	-0.035	6.381	0.371	0.371	0.000	0.000	0.000	0.000
107	A	107	PHE	0	0.001	0.004	2.530	-2.708	-0.497	2.602	-1.165	-3.648	-0.011
108	A	108	PHE	0	0.053	0.013	4.818	0.564	0.658	-0.001	-0.006	-0.087	0.000
109	A	109	LEU	0	0.019	0.008	6.746	0.328	0.328	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.947	0.984	7.183	1.424	1.424	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.854	-0.903	7.450	-0.833	-0.833	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.041	0.026	9.376	0.213	0.213	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.048	-0.047	12.237	0.154	0.154	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.837	-0.886	11.528	-0.460	-0.460	0.000	0.000	0.000	0.000
115	A	115	HIS	0	-0.057	-0.027	11.559	0.175	0.175	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.032	-0.016	15.371	0.076	0.076	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.757	0.837	15.740	0.462	0.462	0.000	0.000	0.000	0.000
118	A	118	VAL	0	0.035	0.018	16.883	0.049	0.049	0.000	0.000	0.000	0.000
119	A	119	VAL	0	-0.010	-0.003	19.378	0.043	0.043	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.002	0.000	21.449	0.030	0.030	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.876	-0.929	21.202	-0.266	-0.266	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.969	0.990	23.701	0.200	0.200	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.002	0.001	25.558	0.020	0.020	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.046	0.028	26.118	0.016	0.016	0.000	0.000	0.000	0.000
125	A	125	PHE	0	-0.017	0.005	25.356	0.015	0.015	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.031	-0.005	29.020	0.012	0.012	0.000	0.000	0.000	0.000
127	A	127	THR	0	-0.084	-0.062	31.314	0.010	0.010	0.000	0.000	0.000	0.000
128	A	128	THR	0	-0.084	-0.056	32.197	0.005	0.005	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.962	1.005	34.779	0.105	0.105	0.000	0.000	0.000	0.000

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