FMO DATABASE

FMODB ID: G6MK1

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	OptH
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	-1101283.271779
FMO2-HF: Nuclear repulsion	1050476.907302
FMO2-HF: Total energy	-50806.364477
FMO2-MP2: Total energy	-50956.625307

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.
-18.26	-12.041	17.663	-6.81	-17.07	-0.047

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 : -0.021 / q_NPA : 0.005

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	3	LEU	0	0.029	-0.007	2.640	-1.196	2.202	1.238	-1.197	-3.439	0.003
4	A	4	LYS	1	0.971	0.993	4.099	-1.002	-0.798	0.003	-0.013	-0.193	0.000
5	A	5	LYS	1	0.945	0.970	4.874	-3.421	-3.156	0.000	-0.036	-0.229	0.000
6	A	6	LEU	0	0.005	-0.001	5.315	-0.684	-0.513	-0.001	-0.019	-0.151	0.000
7	A	7	LEU	0	-0.013	-0.011	7.960	-0.352	-0.352	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.027	-0.014	10.482	-0.135	-0.135	0.000	0.000	0.000	0.000
9	A	9	CYS	0	-0.056	-0.009	9.396	-0.091	-0.091	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.040	0.020	12.805	-0.075	-0.075	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.945	0.994	14.735	-0.112	-0.112	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.028	0.000	15.233	0.015	0.015	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.041	-0.016	17.372	-0.029	-0.029	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.026	-0.013	18.397	0.008	0.008	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.070	0.037	19.041	-0.010	-0.010	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.845	0.921	22.891	-0.097	-0.097	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.969	0.975	25.132	-0.048	-0.048	0.000	0.000	0.000	0.000
18	A	18	GLY	0	-0.022	-0.009	25.743	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.874	-0.927	25.137	0.062	0.062	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.002	0.003	24.606	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.072	-0.030	18.607	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.885	0.937	20.125	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	23	HIS	0	-0.003	0.004	23.102	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	24	GLN	0	0.070	0.031	25.111	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.910	-0.961	25.580	-0.061	-0.061	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.862	-0.917	24.088	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.016	-0.018	23.589	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	28	ILE	0	-0.046	-0.010	17.036	0.010	0.010	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.963	-0.994	20.032	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.849	-0.925	16.386	0.084	0.084	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.030	-0.017	10.184	-0.037	-0.037	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.017	-0.008	13.263	0.083	0.083	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.012	0.000	7.022	-0.058	-0.058	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.012	0.014	10.568	0.077	0.077	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.037	-0.020	9.949	0.001	0.001	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.942	-1.007	11.866	0.335	0.335	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.022	0.024	14.832	-0.015	-0.015	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.016	-0.042	16.724	-0.013	-0.013	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.048	-0.012	15.839	0.013	0.013	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.972	0.994	19.018	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.021	0.000	18.891	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.866	-0.954	21.907	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	43	HIS	0	0.012	0.009	25.571	0.004	0.004	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.022	-0.007	27.549	0.007	0.007	0.000	0.000	0.000	0.000
45	A	45	SER	0	0.001	-0.015	30.698	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.880	-0.957	33.771	-0.053	-0.053	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.064	-0.036	36.717	0.001	0.001	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.009	0.014	35.492	0.004	0.004	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.854	0.933	33.713	0.042	0.042	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.063	0.046	29.318	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.084	-0.042	29.047	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.871	-0.946	24.375	-0.046	-0.046	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.131	-0.057	22.007	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.843	-0.937	18.768	-0.177	-0.177	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.963	-0.974	19.015	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.041	-0.019	13.401	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.938	0.964	14.095	0.035	0.035	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.052	-0.006	11.123	-0.051	-0.051	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.035	-0.016	6.756	0.054	0.054	0.000	0.000	0.000	0.000
60	A	60	GLN	0	0.044	0.009	6.979	-0.229	-0.229	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.022	-0.013	6.147	0.181	0.181	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.007	0.004	9.550	-0.063	-0.063	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.003	0.003	13.342	0.011	0.011	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.000	-0.069	10.490	0.048	0.048	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.002	-0.007	12.512	0.000	0.000	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.006	0.008	15.056	0.015	0.015	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.009	0.008	12.166	0.026	0.026	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.008	-0.026	12.207	0.025	0.025	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.034	0.008	17.385	0.002	0.002	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.029	-0.011	20.682	0.006	0.006	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.989	-0.985	24.091	-0.080	-0.080	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.004	0.028	20.055	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.948	0.950	21.964	0.084	0.084	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.017	-0.009	17.350	-0.017	-0.017	0.000	0.000	0.000	0.000
75	A	75	PRO	0	-0.005	0.005	20.337	0.010	0.010	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.044	-0.014	21.206	0.002	0.002	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.040	0.031	23.110	0.002	0.002	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.021	-0.012	18.341	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.037	0.019	21.652	0.015	0.015	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.008	0.016	21.235	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.017	-0.003	21.497	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.930	-0.950	20.470	0.091	0.091	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.025	-0.002	21.916	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.031	-0.002	17.790	0.004	0.004	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.886	0.946	16.091	-0.252	-0.252	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.034	0.017	13.996	0.008	0.008	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.018	0.009	9.497	0.013	0.013	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.046	-0.035	13.002	-0.049	-0.049	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.014	-0.013	9.737	0.041	0.041	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.059	0.037	14.073	-0.051	-0.051	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.939	0.974	15.036	0.114	0.114	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.923	-0.952	15.098	-0.111	-0.111	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.033	0.024	12.622	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	94	PHE	0	-0.031	-0.030	6.944	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.050	0.014	10.597	-0.081	-0.081	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.926	-0.961	12.178	-0.141	-0.141	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.052	-0.044	7.478	-0.036	-0.036	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.019	-0.002	7.028	-0.245	-0.245	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.051	-0.025	8.749	-0.161	-0.161	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.880	0.953	9.539	0.108	0.108	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.857	-0.920	3.498	-4.309	-3.418	0.016	-0.448	-0.460	-0.003
102	A	102	ARG	1	0.975	0.981	6.066	0.665	0.665	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.905	-0.956	2.120	-4.651	-6.128	10.358	-3.837	-5.044	-0.032
104	A	104	LEU	0	0.002	0.007	2.140	-3.686	-1.739	2.670	-1.656	-2.961	-0.002
105	A	105	LEU	0	0.004	0.005	2.940	1.983	0.465	0.075	1.716	-0.273	-0.001
106	A	106	LEU	0	-0.029	-0.034	5.992	0.248	0.248	0.000	0.000	0.000	0.000
107	A	107	PHE	0	-0.003	0.006	2.503	-2.938	-0.714	3.305	-1.311	-4.217	-0.012
108	A	108	PHE	0	0.054	0.014	4.690	0.477	0.591	-0.001	-0.009	-0.103	0.000
109	A	109	LEU	0	0.016	0.002	6.628	0.250	0.250	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.944	0.986	6.909	1.494	1.494	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.853	-0.874	7.193	-0.673	-0.673	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.045	0.027	9.124	0.183	0.183	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.048	-0.050	12.036	0.132	0.132	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.873	-0.924	11.316	-0.471	-0.471	0.000	0.000	0.000	0.000
115	A	115	HIS	0	-0.034	-0.016	11.574	0.151	0.151	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.033	-0.014	15.316	0.069	0.069	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.818	0.902	15.668	0.434	0.434	0.000	0.000	0.000	0.000
118	A	118	VAL	0	0.033	0.017	16.995	0.042	0.042	0.000	0.000	0.000	0.000
119	A	119	VAL	0	-0.016	-0.005	19.346	0.037	0.037	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.021	-0.008	21.445	0.035	0.035	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.870	-0.941	21.644	-0.240	-0.240	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.965	0.989	23.673	0.164	0.164	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.009	-0.003	25.520	0.018	0.018	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.049	0.031	26.391	0.015	0.015	0.000	0.000	0.000	0.000
125	A	125	PHE	0	-0.018	0.005	25.315	0.013	0.013	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.033	-0.010	29.108	0.011	0.011	0.000	0.000	0.000	0.000
127	A	127	THR	0	-0.099	-0.067	31.308	0.009	0.009	0.000	0.000	0.000	0.000
128	A	128	THR	0	-0.095	-0.059	32.196	0.005	0.005	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.985	1.013	34.763	0.087	0.087	0.000	0.000	0.000	0.000

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