FMO DATABASE

FMODB ID: 9G6Y2

Calculation Name: 4O2T-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4O2T

Chain ID: A

ChEMBL ID:

UniProt ID: A6LCN0

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:

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	168
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1819010.593735
FMO2-HF: Nuclear repulsion	1750211.85981
FMO2-HF: Total energy	-68798.733925
FMO2-MP2: Total energy	-68997.715723

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:0:GLY)

Summations of interaction energy for fragment #1(A:0:GLY)

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.
0.306	1.93	-0.009	-0.853	-0.763	0.004

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.050 / q_NPA : 0.025

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	25	SER	0	-0.001	-0.017	3.797	-0.134	1.490	-0.009	-0.853	-0.763	0.004
4	A	26	TYR	0	0.095	0.026	6.461	0.438	0.438	0.000	0.000	0.000	0.000
5	A	27	THR	0	0.031	0.007	8.866	0.203	0.203	0.000	0.000	0.000	0.000
6	A	28	ASP	-1	-0.846	-0.896	7.982	-1.813	-1.813	0.000	0.000	0.000	0.000
7	A	29	MET	0	-0.002	0.003	6.331	0.244	0.244	0.000	0.000	0.000	0.000
8	A	30	LEU	0	0.010	0.009	9.846	0.210	0.210	0.000	0.000	0.000	0.000
9	A	31	LYS	1	0.856	0.942	12.211	1.215	1.215	0.000	0.000	0.000	0.000
10	A	32	ASP	-1	-0.853	-0.924	10.608	-0.822	-0.822	0.000	0.000	0.000	0.000
11	A	33	GLU	-1	-0.730	-0.870	13.476	-0.221	-0.221	0.000	0.000	0.000	0.000
12	A	34	LYS	1	0.811	0.885	15.313	0.394	0.394	0.000	0.000	0.000	0.000
13	A	35	LYS	1	0.870	0.935	14.299	0.561	0.561	0.000	0.000	0.000	0.000
14	A	36	ALA	0	-0.006	-0.008	16.580	0.044	0.044	0.000	0.000	0.000	0.000
15	A	37	ILE	0	0.025	0.009	18.577	0.041	0.041	0.000	0.000	0.000	0.000
16	A	38	GLU	-1	-0.801	-0.879	21.141	-0.270	-0.270	0.000	0.000	0.000	0.000
17	A	39	ARG	1	0.946	0.974	19.984	0.190	0.190	0.000	0.000	0.000	0.000
18	A	40	PHE	0	0.029	0.019	22.361	0.025	0.025	0.000	0.000	0.000	0.000
19	A	41	ILE	0	0.006	-0.014	24.189	0.015	0.015	0.000	0.000	0.000	0.000
20	A	42	ASP	-1	-0.965	-0.974	26.704	-0.122	-0.122	0.000	0.000	0.000	0.000
21	A	43	ASP	-1	-0.979	-0.993	26.421	-0.075	-0.075	0.000	0.000	0.000	0.000
22	A	44	LYS	1	0.858	0.941	26.149	0.075	0.075	0.000	0.000	0.000	0.000
23	A	45	GLY	0	-0.022	0.016	30.272	0.007	0.007	0.000	0.000	0.000	0.000
24	A	46	LEU	0	-0.057	-0.028	28.258	0.007	0.007	0.000	0.000	0.000	0.000
25	A	47	GLU	-1	-0.849	-0.899	32.011	-0.080	-0.080	0.000	0.000	0.000	0.000
26	A	48	ILE	0	-0.018	-0.029	28.791	0.003	0.003	0.000	0.000	0.000	0.000
27	A	49	LEU	0	-0.027	-0.007	31.987	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	50	ASP	-1	-0.914	-0.964	32.472	-0.126	-0.126	0.000	0.000	0.000	0.000
29	A	51	ASP	-1	-0.897	-0.941	33.996	-0.079	-0.079	0.000	0.000	0.000	0.000
30	A	52	PHE	0	-0.064	-0.054	33.976	0.002	0.002	0.000	0.000	0.000	0.000
31	A	53	PRO	0	-0.006	0.015	37.234	0.001	0.001	0.000	0.000	0.000	0.000
32	A	54	ALA	0	-0.004	-0.012	40.236	0.002	0.002	0.000	0.000	0.000	0.000
33	A	55	ASP	-1	-0.921	-0.972	43.676	-0.036	-0.036	0.000	0.000	0.000	0.000
34	A	56	SER	0	-0.074	-0.032	39.303	0.002	0.002	0.000	0.000	0.000	0.000
35	A	57	VAL	0	-0.026	0.001	40.292	0.003	0.003	0.000	0.000	0.000	0.000
36	A	58	PHE	0	0.014	-0.001	34.744	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	59	LYS	1	0.854	0.927	38.941	0.066	0.066	0.000	0.000	0.000	0.000
38	A	60	GLU	-1	-0.910	-0.969	35.079	-0.048	-0.048	0.000	0.000	0.000	0.000
39	A	61	ASN	0	0.025	0.003	34.241	0.004	0.004	0.000	0.000	0.000	0.000
40	A	62	GLN	0	-0.023	-0.015	33.737	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	63	PHE	0	-0.001	-0.010	29.097	0.007	0.007	0.000	0.000	0.000	0.000
42	A	64	VAL	0	0.017	0.027	31.727	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	65	LEU	0	-0.016	-0.006	25.065	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	66	LEU	0	0.002	0.008	27.637	0.002	0.002	0.000	0.000	0.000	0.000
45	A	67	ASP	-1	-0.849	-0.923	27.049	-0.126	-0.126	0.000	0.000	0.000	0.000
46	A	68	ASN	0	-0.135	-0.089	24.151	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	69	GLY	0	0.019	0.008	22.396	-0.015	-0.015	0.000	0.000	0.000	0.000
48	A	70	VAL	0	-0.047	-0.015	23.088	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	71	TYR	0	0.015	0.016	23.026	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	72	LEU	0	-0.004	-0.017	27.139	0.010	0.010	0.000	0.000	0.000	0.000
51	A	73	ASN	0	-0.022	-0.004	30.214	0.002	0.002	0.000	0.000	0.000	0.000
52	A	74	ILE	0	0.009	0.001	33.251	0.006	0.006	0.000	0.000	0.000	0.000
53	A	75	ILE	0	-0.025	-0.007	34.470	0.000	0.000	0.000	0.000	0.000	0.000
54	A	76	ASP	-1	-0.886	-0.948	37.941	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	77	LYS	1	0.960	0.966	38.775	0.023	0.023	0.000	0.000	0.000	0.000
56	A	78	GLY	0	0.033	0.017	40.370	0.000	0.000	0.000	0.000	0.000	0.000
57	A	79	SER	0	-0.032	-0.009	41.748	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	80	ASP	-1	-0.822	-0.918	42.688	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.043	0.008	41.945	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	82	ARG	1	0.845	0.915	38.347	0.021	0.021	0.000	0.000	0.000	0.000
61	A	83	ALA	0	0.024	0.021	35.592	0.003	0.003	0.000	0.000	0.000	0.000
62	A	84	VAL	0	-0.002	-0.006	37.213	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	85	GLN	0	0.020	0.007	29.903	0.004	0.004	0.000	0.000	0.000	0.000
64	A	86	TYR	0	-0.061	-0.053	29.541	0.001	0.001	0.000	0.000	0.000	0.000
65	A	87	LYS	1	0.876	0.947	33.995	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	88	THR	0	0.038	0.035	36.321	0.002	0.002	0.000	0.000	0.000	0.000
67	A	89	LYS	1	0.842	0.919	35.141	-0.041	-0.041	0.000	0.000	0.000	0.000
68	A	90	MET	0	-0.019	0.007	32.919	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	91	LEU	0	0.003	-0.002	33.504	0.007	0.007	0.000	0.000	0.000	0.000
70	A	92	TYR	0	-0.023	-0.044	25.652	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	93	ARG	1	0.849	0.905	32.086	-0.033	-0.033	0.000	0.000	0.000	0.000
72	A	94	CYS	0	-0.035	-0.008	27.888	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	95	LYS	1	0.862	0.933	28.143	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	96	MET	0	-0.012	0.005	20.757	-0.015	-0.015	0.000	0.000	0.000	0.000
75	A	97	SER	0	0.031	0.006	22.654	0.018	0.018	0.000	0.000	0.000	0.000
76	A	98	TYR	0	-0.047	-0.035	16.405	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	99	PHE	0	-0.006	-0.030	18.487	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	100	MET	0	-0.058	0.002	11.665	-0.037	-0.037	0.000	0.000	0.000	0.000
79	A	101	ASP	-1	-0.870	-0.933	12.470	-0.214	-0.214	0.000	0.000	0.000	0.000
80	A	102	SER	0	-0.067	-0.037	15.465	0.040	0.040	0.000	0.000	0.000	0.000
81	A	103	THR	0	0.025	0.007	18.555	-0.016	-0.016	0.000	0.000	0.000	0.000
82	A	104	ILE	0	-0.009	0.008	18.066	0.003	0.003	0.000	0.000	0.000	0.000
83	A	105	VAL	0	-0.009	-0.002	21.622	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	106	ALA	0	-0.030	-0.008	20.767	0.017	0.017	0.000	0.000	0.000	0.000
85	A	107	ILE	0	-0.014	-0.011	22.715	0.013	0.013	0.000	0.000	0.000	0.000
86	A	108	GLU	-1	-0.868	-0.951	25.942	0.028	0.028	0.000	0.000	0.000	0.000
87	A	109	ASN	0	-0.016	-0.010	29.429	0.000	0.000	0.000	0.000	0.000	0.000
88	A	110	TYR	0	0.033	0.024	32.198	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	111	GLY	0	0.040	0.034	33.905	0.000	0.000	0.000	0.000	0.000	0.000
90	A	112	PRO	0	-0.002	0.002	36.467	0.004	0.004	0.000	0.000	0.000	0.000
91	A	113	HIS	0	0.005	-0.001	33.988	0.004	0.004	0.000	0.000	0.000	0.000
92	A	114	SER	0	-0.033	0.002	34.090	0.006	0.006	0.000	0.000	0.000	0.000
93	A	115	ASN	0	0.029	0.004	35.348	0.001	0.001	0.000	0.000	0.000	0.000
94	A	116	GLY	0	0.015	0.008	37.321	0.005	0.005	0.000	0.000	0.000	0.000
95	A	117	THR	0	-0.027	-0.002	33.021	0.004	0.004	0.000	0.000	0.000	0.000
96	A	118	SER	0	-0.001	0.005	34.359	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	119	PRO	0	-0.003	-0.011	33.387	0.003	0.003	0.000	0.000	0.000	0.000
98	A	120	ILE	0	-0.027	0.005	27.021	0.007	0.007	0.000	0.000	0.000	0.000
99	A	121	ALA	0	0.008	-0.002	30.927	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	122	PHE	0	-0.047	-0.021	28.684	0.006	0.006	0.000	0.000	0.000	0.000
101	A	123	THR	0	0.012	0.007	30.536	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	124	TYR	0	-0.008	0.005	30.348	0.001	0.001	0.000	0.000	0.000	0.000
103	A	125	GLY	0	0.018	-0.011	29.266	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	126	ASP	-1	-0.895	-0.920	26.698	0.050	0.050	0.000	0.000	0.000	0.000
105	A	127	TYR	0	-0.018	-0.014	21.548	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	128	SER	0	-0.033	-0.024	19.071	0.019	0.019	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.866	0.914	19.286	-0.124	-0.124	0.000	0.000	0.000	0.000
108	A	130	ASN	0	0.052	0.016	15.185	-0.013	-0.013	0.000	0.000	0.000	0.000
109	A	131	SER	0	-0.026	-0.006	16.054	0.073	0.073	0.000	0.000	0.000	0.000
110	A	132	PRO	0	0.061	0.029	16.074	-0.036	-0.036	0.000	0.000	0.000	0.000
111	A	133	TYR	0	-0.016	-0.011	18.037	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	134	ASP	-1	-0.794	-0.848	21.196	0.120	0.120	0.000	0.000	0.000	0.000
113	A	135	PRO	0	0.075	0.029	21.777	0.011	0.011	0.000	0.000	0.000	0.000
114	A	136	SER	0	-0.015	-0.035	22.824	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	137	TYR	0	-0.013	0.024	13.018	-0.013	-0.013	0.000	0.000	0.000	0.000
116	A	138	TYR	0	-0.059	-0.053	17.428	0.013	0.013	0.000	0.000	0.000	0.000
117	A	139	TYR	0	-0.015	0.000	20.046	-0.019	-0.019	0.000	0.000	0.000	0.000
118	A	140	VAL	0	0.026	0.036	22.308	-0.015	-0.015	0.000	0.000	0.000	0.000
119	A	141	SER	0	0.023	0.012	20.820	0.003	0.003	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.796	-0.870	21.764	-0.099	-0.099	0.000	0.000	0.000	0.000
121	A	143	GLY	0	0.044	0.003	22.341	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	144	MET	0	-0.038	0.001	23.826	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	145	GLN	0	0.031	-0.007	25.571	0.004	0.004	0.000	0.000	0.000	0.000
124	A	146	GLU	-1	-0.804	-0.875	26.512	-0.068	-0.068	0.000	0.000	0.000	0.000
125	A	147	PRO	0	0.044	0.010	28.570	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	148	LEU	0	-0.028	-0.002	31.442	0.002	0.002	0.000	0.000	0.000	0.000
127	A	149	LYS	1	0.777	0.883	29.481	0.069	0.069	0.000	0.000	0.000	0.000
128	A	150	TYR	0	-0.003	-0.012	31.471	0.000	0.000	0.000	0.000	0.000	0.000
129	A	151	VAL	0	-0.042	-0.006	35.024	0.001	0.001	0.000	0.000	0.000	0.000
130	A	152	GLY	0	0.025	0.018	37.644	0.001	0.001	0.000	0.000	0.000	0.000
131	A	153	ASP	-1	-0.798	-0.887	38.672	0.011	0.011	0.000	0.000	0.000	0.000
132	A	154	ARG	1	0.840	0.893	39.386	-0.014	-0.014	0.000	0.000	0.000	0.000
133	A	155	ALA	0	0.022	0.039	37.065	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	156	LYS	1	0.828	0.899	35.543	0.004	0.004	0.000	0.000	0.000	0.000
135	A	157	VAL	0	-0.002	0.001	30.947	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	158	LYS	1	0.878	0.956	30.279	0.050	0.050	0.000	0.000	0.000	0.000
137	A	159	MET	0	-0.045	-0.023	26.037	-0.007	-0.007	0.000	0.000	0.000	0.000
138	A	160	ILE	0	-0.005	0.014	21.926	0.006	0.006	0.000	0.000	0.000	0.000
139	A	161	VAL	0	-0.010	-0.001	20.099	-0.008	-0.008	0.000	0.000	0.000	0.000
140	A	162	PRO	0	0.028	0.023	17.840	0.008	0.008	0.000	0.000	0.000	0.000
141	A	163	PHE	0	0.023	0.003	11.347	0.009	0.009	0.000	0.000	0.000	0.000
142	A	164	LYS	1	0.871	0.933	15.392	0.353	0.353	0.000	0.000	0.000	0.000
143	A	165	ARG	1	0.795	0.888	16.200	0.167	0.167	0.000	0.000	0.000	0.000
144	A	166	GLY	0	0.074	0.036	17.449	0.021	0.021	0.000	0.000	0.000	0.000
145	A	167	ALA	0	0.003	0.016	18.152	0.001	0.001	0.000	0.000	0.000	0.000
146	A	168	TYR	0	0.050	0.014	11.831	-0.033	-0.033	0.000	0.000	0.000	0.000
147	A	169	ASN	0	-0.025	-0.020	13.277	0.089	0.089	0.000	0.000	0.000	0.000
148	A	170	ASP	-1	-0.776	-0.873	12.596	0.151	0.151	0.000	0.000	0.000	0.000
149	A	171	GLN	0	-0.115	-0.068	12.322	-0.054	-0.054	0.000	0.000	0.000	0.000
150	A	172	SER	0	-0.070	-0.038	9.039	-0.099	-0.099	0.000	0.000	0.000	0.000
151	A	173	ASN	0	-0.080	-0.046	7.524	0.237	0.237	0.000	0.000	0.000	0.000
152	A	174	GLY	0	0.007	0.008	9.196	-0.121	-0.121	0.000	0.000	0.000	0.000
153	A	175	GLN	0	-0.094	-0.061	10.539	-0.052	-0.052	0.000	0.000	0.000	0.000
154	A	176	PRO	0	0.008	0.019	13.760	0.024	0.024	0.000	0.000	0.000	0.000
155	A	177	VAL	0	-0.026	-0.016	17.173	0.025	0.025	0.000	0.000	0.000	0.000
156	A	178	TYR	0	0.019	-0.004	20.134	-0.019	-0.019	0.000	0.000	0.000	0.000
157	A	179	TYR	0	0.021	-0.005	23.374	0.016	0.016	0.000	0.000	0.000	0.000
158	A	180	GLU	-1	-0.833	-0.914	26.648	-0.012	-0.012	0.000	0.000	0.000	0.000
159	A	181	ILE	0	-0.009	-0.012	29.371	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	182	LEU	0	-0.028	-0.011	28.269	0.008	0.008	0.000	0.000	0.000	0.000
161	A	183	GLU	-1	-0.886	-0.935	31.768	0.006	0.006	0.000	0.000	0.000	0.000
162	A	184	TYR	0	-0.006	-0.024	29.727	0.005	0.005	0.000	0.000	0.000	0.000
163	A	185	ILE	0	-0.024	-0.024	35.233	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	186	PHE	0	0.052	0.010	37.041	0.003	0.003	0.000	0.000	0.000	0.000
165	A	187	GLU	-1	-0.832	-0.923	37.178	0.043	0.043	0.000	0.000	0.000	0.000
166	A	188	GLU	-1	-0.949	-0.984	40.056	0.011	0.011	0.000	0.000	0.000	0.000
167	A	189	ASN	0	-0.067	-0.043	42.883	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	190	LEU	0	-0.074	-0.019	40.367	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)