FMO DATABASE

FMODB ID: 66M8Z

Calculation Name: 1O6A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O6A

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-20

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	87
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-502647.95193
FMO2-HF: Nuclear repulsion	468747.241257
FMO2-HF: Total energy	-33900.710673
FMO2-MP2: Total energy	-34000.400786

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:68:SER)

Summations of interaction energy for fragment #1(A:68:SER)

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.
-13.094	-9.165	3.918	-2.923	-4.924	0.015

Interaction energy analysis for fragmet #1(A:68:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.014 / q_NPA : -0.026

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	70	LYS	1	0.909	0.942	2.643	-5.154	-2.378	0.848	-1.422	-2.201	0.010
4	A	71	LEU	0	-0.016	-0.016	2.349	-6.171	-5.311	3.063	-1.413	-2.511	0.005
5	A	72	GLU	-1	-0.872	-0.930	3.952	-2.602	-2.309	0.007	-0.088	-0.212	0.000
6	A	73	LEU	0	-0.038	-0.019	6.017	0.151	0.151	0.000	0.000	0.000	0.000
7	A	74	LEU	0	-0.080	-0.051	6.625	0.056	0.056	0.000	0.000	0.000	0.000
8	A	75	LEU	0	-0.034	-0.009	6.987	-0.065	-0.065	0.000	0.000	0.000	0.000
9	A	76	ASP	-1	-0.869	-0.931	9.786	-0.147	-0.147	0.000	0.000	0.000	0.000
10	A	77	ILE	0	-0.110	-0.030	11.405	0.027	0.027	0.000	0.000	0.000	0.000
11	A	78	PRO	0	-0.005	-0.003	14.344	-0.025	-0.025	0.000	0.000	0.000	0.000
12	A	79	LEU	0	-0.016	-0.003	13.506	0.044	0.044	0.000	0.000	0.000	0.000
13	A	80	LYS	1	0.936	0.967	17.862	-0.122	-0.122	0.000	0.000	0.000	0.000
14	A	81	VAL	0	0.023	0.012	19.816	0.012	0.012	0.000	0.000	0.000	0.000
15	A	82	THR	0	-0.036	-0.018	22.267	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	83	VAL	0	0.019	0.003	25.139	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	84	GLU	-1	-0.838	-0.883	27.571	0.073	0.073	0.000	0.000	0.000	0.000
18	A	85	LEU	0	0.023	0.002	30.218	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	86	GLY	0	0.059	0.012	33.255	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	87	ARG	1	0.762	0.873	27.298	-0.078	-0.078	0.000	0.000	0.000	0.000
21	A	88	THR	0	0.082	0.035	34.882	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	89	ARG	1	0.905	0.953	36.300	-0.056	-0.056	0.000	0.000	0.000	0.000
23	A	90	MET	0	0.020	0.016	39.345	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	91	THR	0	0.014	0.004	42.106	0.003	0.003	0.000	0.000	0.000	0.000
25	A	92	LEU	0	0.075	0.031	44.105	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	93	LYS	1	0.915	0.958	45.340	-0.035	-0.035	0.000	0.000	0.000	0.000
27	A	94	ARG	1	0.954	0.984	46.022	-0.032	-0.032	0.000	0.000	0.000	0.000
28	A	95	VAL	0	0.013	-0.009	42.553	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	96	LEU	0	-0.039	-0.028	45.618	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	97	GLU	-1	-0.881	-0.933	48.635	0.031	0.031	0.000	0.000	0.000	0.000
31	A	98	MET	0	-0.113	-0.033	43.167	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	99	ILE	0	0.013	0.015	48.977	0.000	0.000	0.000	0.000	0.000	0.000
33	A	100	HIS	0	0.042	0.000	49.252	0.000	0.000	0.000	0.000	0.000	0.000
34	A	101	GLY	0	0.011	0.000	49.180	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	102	SER	0	-0.049	-0.010	47.914	0.000	0.000	0.000	0.000	0.000	0.000
36	A	103	ILE	0	0.030	0.015	46.025	0.000	0.000	0.000	0.000	0.000	0.000
37	A	104	ILE	0	-0.055	-0.040	41.016	0.002	0.002	0.000	0.000	0.000	0.000
38	A	105	GLU	-1	-0.927	-0.948	42.543	0.019	0.019	0.000	0.000	0.000	0.000
39	A	106	LEU	0	-0.077	-0.053	36.660	0.004	0.004	0.000	0.000	0.000	0.000
40	A	107	ASP	-1	-0.898	-0.953	34.267	0.042	0.042	0.000	0.000	0.000	0.000
41	A	108	LYS	1	0.815	0.918	30.988	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	109	LEU	0	0.000	0.006	36.320	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	110	THR	0	-0.012	-0.018	37.160	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	111	GLY	0	-0.005	-0.010	37.462	0.000	0.000	0.000	0.000	0.000	0.000
45	A	112	GLU	-1	-0.911	-0.950	33.083	0.011	0.011	0.000	0.000	0.000	0.000
46	A	113	PRO	0	-0.046	0.006	29.126	0.000	0.000	0.000	0.000	0.000	0.000
47	A	114	VAL	0	-0.009	-0.017	28.509	0.008	0.008	0.000	0.000	0.000	0.000
48	A	115	ASP	-1	-0.807	-0.905	26.650	0.026	0.026	0.000	0.000	0.000	0.000
49	A	116	ILE	0	-0.038	-0.016	21.722	0.002	0.002	0.000	0.000	0.000	0.000
50	A	117	LEU	0	-0.013	-0.017	21.993	0.005	0.005	0.000	0.000	0.000	0.000
51	A	118	VAL	0	0.009	-0.004	16.476	-0.010	-0.010	0.000	0.000	0.000	0.000
52	A	119	ASN	0	0.009	-0.003	16.794	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	120	GLY	0	0.001	-0.001	20.028	0.020	0.020	0.000	0.000	0.000	0.000
54	A	121	LYS	1	0.880	0.961	17.369	-0.272	-0.272	0.000	0.000	0.000	0.000
55	A	122	LEU	0	0.023	0.019	20.319	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	123	ILE	0	-0.005	-0.005	16.535	0.003	0.003	0.000	0.000	0.000	0.000
57	A	124	ALA	0	-0.008	-0.013	19.445	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	125	ARG	1	0.887	0.946	21.895	0.012	0.012	0.000	0.000	0.000	0.000
59	A	126	GLY	0	0.037	0.009	25.265	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	127	GLU	-1	-0.845	-0.902	27.582	-0.044	-0.044	0.000	0.000	0.000	0.000
61	A	128	VAL	0	0.000	-0.005	30.168	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	129	VAL	0	-0.051	-0.025	30.107	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	130	VAL	0	0.036	0.015	32.875	0.005	0.005	0.000	0.000	0.000	0.000
64	A	131	ILE	0	-0.064	-0.037	29.505	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	132	ASP	-1	-0.930	-0.967	32.811	-0.041	-0.041	0.000	0.000	0.000	0.000
66	A	133	GLU	-1	-0.904	-0.943	35.391	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	134	ASN	0	-0.066	-0.029	32.042	0.004	0.004	0.000	0.000	0.000	0.000
68	A	135	PHE	0	-0.019	-0.016	32.557	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	136	GLY	0	0.019	0.010	29.075	0.000	0.000	0.000	0.000	0.000	0.000
70	A	137	VAL	0	-0.037	-0.016	25.403	0.004	0.004	0.000	0.000	0.000	0.000
71	A	138	ARG	1	0.874	0.946	26.328	0.062	0.062	0.000	0.000	0.000	0.000
72	A	139	ILE	0	-0.018	-0.019	20.325	0.008	0.008	0.000	0.000	0.000	0.000
73	A	140	THR	0	-0.006	-0.013	24.514	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	141	GLU	-1	-0.851	-0.905	24.038	-0.022	-0.022	0.000	0.000	0.000	0.000
75	A	142	ILE	0	-0.059	-0.040	17.472	0.004	0.004	0.000	0.000	0.000	0.000
76	A	143	VAL	0	0.062	0.058	15.855	-0.014	-0.014	0.000	0.000	0.000	0.000
77	A	144	SER	0	0.030	0.010	14.254	-0.044	-0.044	0.000	0.000	0.000	0.000
78	A	145	PRO	0	0.014	-0.023	10.472	0.049	0.049	0.000	0.000	0.000	0.000
79	A	146	LYS	1	0.959	0.981	8.836	0.089	0.089	0.000	0.000	0.000	0.000
80	A	147	GLU	-1	-0.809	-0.912	10.369	0.089	0.089	0.000	0.000	0.000	0.000
81	A	148	ARG	1	0.842	0.925	12.291	0.188	0.188	0.000	0.000	0.000	0.000
82	A	149	LEU	0	0.016	0.002	5.885	0.074	0.074	0.000	0.000	0.000	0.000
83	A	150	GLU	-1	-0.920	-0.960	10.003	0.310	0.310	0.000	0.000	0.000	0.000
84	A	151	LEU	0	0.026	0.010	11.509	0.047	0.047	0.000	0.000	0.000	0.000
85	A	152	LEU	0	-0.064	-0.035	12.120	0.006	0.006	0.000	0.000	0.000	0.000
86	A	153	ASN	0	-0.101	-0.045	8.732	0.239	0.239	0.000	0.000	0.000	0.000
87	A	154	GLU	-1	-0.960	-0.958	12.175	0.276	0.276	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:68:SER)