FMO DATABASE

FMODB ID: LJ2L9

Calculation Name: 4O2T-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1814911.535384
FMO2-HF: Nuclear repulsion	1746113.653742
FMO2-HF: Total energy	-68797.881642
FMO2-MP2: Total energy	-68996.716801

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: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.
0.384	1.597	-0.007	-0.581	-0.624	0.003

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 : 0.037 / q_NPA : 0.008

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	0.014	0.011	3.797	0.200	1.413	-0.007	-0.581	-0.624	0.003
4	A	26	TYR	0	0.065	0.014	6.476	0.482	0.482	0.000	0.000	0.000	0.000
5	A	27	THR	0	0.020	-0.003	8.877	0.243	0.243	0.000	0.000	0.000	0.000
6	A	28	ASP	-1	-0.895	-0.942	7.991	-1.683	-1.683	0.000	0.000	0.000	0.000
7	A	29	MET	0	-0.019	-0.003	6.286	0.292	0.292	0.000	0.000	0.000	0.000
8	A	30	LEU	0	0.012	0.007	9.853	0.222	0.222	0.000	0.000	0.000	0.000
9	A	31	LYS	1	0.918	0.978	12.847	0.781	0.781	0.000	0.000	0.000	0.000
10	A	32	ASP	-1	-0.881	-0.946	10.199	-0.675	-0.675	0.000	0.000	0.000	0.000
11	A	33	GLU	-1	-0.747	-0.886	13.473	-0.239	-0.239	0.000	0.000	0.000	0.000
12	A	34	LYS	1	0.928	0.970	15.316	0.383	0.383	0.000	0.000	0.000	0.000
13	A	35	LYS	1	0.936	0.971	16.132	0.319	0.319	0.000	0.000	0.000	0.000
14	A	36	ALA	0	-0.002	-0.006	16.625	0.042	0.042	0.000	0.000	0.000	0.000
15	A	37	ILE	0	0.023	0.008	18.577	0.038	0.038	0.000	0.000	0.000	0.000
16	A	38	GLU	-1	-0.909	-0.956	21.144	-0.227	-0.227	0.000	0.000	0.000	0.000
17	A	39	ARG	1	0.928	0.964	20.133	0.110	0.110	0.000	0.000	0.000	0.000
18	A	40	PHE	0	-0.005	0.004	22.387	0.020	0.020	0.000	0.000	0.000	0.000
19	A	41	ILE	0	0.014	-0.011	24.191	0.012	0.012	0.000	0.000	0.000	0.000
20	A	42	ASP	-1	-0.971	-0.980	26.701	-0.084	-0.084	0.000	0.000	0.000	0.000
21	A	43	ASP	-1	-0.977	-0.992	26.415	-0.033	-0.033	0.000	0.000	0.000	0.000
22	A	44	LYS	1	0.887	0.956	27.111	0.042	0.042	0.000	0.000	0.000	0.000
23	A	45	GLY	0	-0.020	0.013	30.275	0.004	0.004	0.000	0.000	0.000	0.000
24	A	46	LEU	0	-0.061	-0.034	28.211	0.004	0.004	0.000	0.000	0.000	0.000
25	A	47	GLU	-1	-0.957	-0.974	32.014	-0.076	-0.076	0.000	0.000	0.000	0.000
26	A	48	ILE	0	-0.028	-0.030	28.838	0.002	0.002	0.000	0.000	0.000	0.000
27	A	49	LEU	0	-0.028	-0.012	31.983	0.000	0.000	0.000	0.000	0.000	0.000
28	A	50	ASP	-1	-0.892	-0.952	32.470	-0.129	-0.129	0.000	0.000	0.000	0.000
29	A	51	ASP	-1	-0.908	-0.955	33.997	-0.093	-0.093	0.000	0.000	0.000	0.000
30	A	52	PHE	0	-0.071	-0.045	34.299	0.003	0.003	0.000	0.000	0.000	0.000
31	A	53	PRO	0	-0.006	0.013	37.235	0.001	0.001	0.000	0.000	0.000	0.000
32	A	54	ALA	0	-0.005	-0.007	40.232	0.001	0.001	0.000	0.000	0.000	0.000
33	A	55	ASP	-1	-0.905	-0.966	43.672	-0.041	-0.041	0.000	0.000	0.000	0.000
34	A	56	SER	0	-0.101	-0.050	39.338	0.002	0.002	0.000	0.000	0.000	0.000
35	A	57	VAL	0	-0.012	0.010	40.285	0.003	0.003	0.000	0.000	0.000	0.000
36	A	58	PHE	0	0.008	0.001	34.503	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	59	LYS	1	0.939	0.962	38.922	0.052	0.052	0.000	0.000	0.000	0.000
38	A	60	GLU	-1	-0.949	-0.984	35.071	-0.039	-0.039	0.000	0.000	0.000	0.000
39	A	61	ASN	0	0.026	0.009	34.244	0.002	0.002	0.000	0.000	0.000	0.000
40	A	62	GLN	0	0.013	0.016	33.743	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	63	PHE	0	-0.015	-0.020	29.084	0.006	0.006	0.000	0.000	0.000	0.000
42	A	64	VAL	0	0.022	0.028	31.722	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	65	LEU	0	-0.011	-0.002	25.209	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	66	LEU	0	0.002	0.004	27.663	0.001	0.001	0.000	0.000	0.000	0.000
45	A	67	ASP	-1	-0.840	-0.920	27.049	-0.156	-0.156	0.000	0.000	0.000	0.000
46	A	68	ASN	0	-0.123	-0.064	24.030	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	69	GLY	0	0.009	-0.001	22.395	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	70	VAL	0	-0.041	-0.013	23.085	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	71	TYR	0	0.014	0.014	23.034	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	72	LEU	0	-0.001	-0.011	27.134	0.009	0.009	0.000	0.000	0.000	0.000
51	A	73	ASN	0	-0.016	0.005	30.207	0.003	0.003	0.000	0.000	0.000	0.000
52	A	74	ILE	0	0.004	-0.001	33.243	0.004	0.004	0.000	0.000	0.000	0.000
53	A	75	ILE	0	-0.023	-0.007	34.748	0.001	0.001	0.000	0.000	0.000	0.000
54	A	76	ASP	-1	-0.898	-0.959	37.931	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	77	LYS	1	1.018	1.003	38.766	0.038	0.038	0.000	0.000	0.000	0.000
56	A	78	GLY	0	0.036	0.017	40.363	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	79	SER	0	-0.036	-0.008	41.739	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	80	ASP	-1	-0.860	-0.944	42.681	-0.031	-0.031	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.051	-0.010	41.959	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	82	ARG	1	0.882	0.941	38.593	0.040	0.040	0.000	0.000	0.000	0.000
61	A	83	ALA	0	0.027	0.021	35.587	0.002	0.002	0.000	0.000	0.000	0.000
62	A	84	VAL	0	-0.001	-0.006	37.210	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	85	GLN	0	0.006	-0.006	30.130	0.003	0.003	0.000	0.000	0.000	0.000
64	A	86	TYR	0	-0.061	-0.046	29.651	0.001	0.001	0.000	0.000	0.000	0.000
65	A	87	LYS	1	0.894	0.950	33.993	0.033	0.033	0.000	0.000	0.000	0.000
66	A	88	THR	0	0.058	0.045	36.231	0.002	0.002	0.000	0.000	0.000	0.000
67	A	89	LYS	1	0.948	0.985	35.134	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	90	MET	0	-0.010	0.011	32.831	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	91	LEU	0	0.018	0.008	33.494	0.006	0.006	0.000	0.000	0.000	0.000
70	A	92	TYR	0	-0.030	-0.054	25.737	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	93	ARG	1	0.847	0.918	32.057	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	94	CYS	0	-0.035	-0.011	27.823	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	95	LYS	1	0.953	0.990	28.120	-0.017	-0.017	0.000	0.000	0.000	0.000
74	A	96	MET	0	-0.001	0.010	20.686	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	97	SER	0	-0.010	-0.017	22.672	0.020	0.020	0.000	0.000	0.000	0.000
76	A	98	TYR	0	-0.053	-0.034	16.586	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	99	PHE	0	-0.006	-0.031	18.504	0.002	0.002	0.000	0.000	0.000	0.000
78	A	100	MET	0	-0.063	-0.003	11.493	-0.029	-0.029	0.000	0.000	0.000	0.000
79	A	101	ASP	-1	-0.852	-0.929	12.020	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	102	SER	0	-0.076	-0.046	15.468	0.042	0.042	0.000	0.000	0.000	0.000
81	A	103	THR	0	0.014	-0.003	18.560	-0.024	-0.024	0.000	0.000	0.000	0.000
82	A	104	ILE	0	-0.012	0.015	18.111	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	105	VAL	0	0.006	0.009	21.633	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	106	ALA	0	-0.028	-0.010	20.749	0.016	0.016	0.000	0.000	0.000	0.000
85	A	107	ILE	0	-0.021	-0.013	22.731	0.008	0.008	0.000	0.000	0.000	0.000
86	A	108	GLU	-1	-0.880	-0.953	25.960	0.038	0.038	0.000	0.000	0.000	0.000
87	A	109	ASN	0	0.001	0.003	29.446	0.001	0.001	0.000	0.000	0.000	0.000
88	A	110	TYR	0	0.046	0.020	32.182	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	111	GLY	0	0.032	0.030	33.922	0.002	0.002	0.000	0.000	0.000	0.000
90	A	112	PRO	0	-0.005	0.011	36.334	0.003	0.003	0.000	0.000	0.000	0.000
91	A	113	HIS	0	0.000	-0.005	34.237	0.003	0.003	0.000	0.000	0.000	0.000
92	A	114	SER	0	-0.034	-0.008	34.257	0.005	0.005	0.000	0.000	0.000	0.000
93	A	115	ASN	0	0.039	0.003	35.366	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	116	GLY	0	-0.002	0.001	37.339	0.005	0.005	0.000	0.000	0.000	0.000
95	A	117	THR	0	-0.019	0.003	32.975	0.001	0.001	0.000	0.000	0.000	0.000
96	A	118	SER	0	-0.010	-0.010	34.328	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	119	PRO	0	-0.001	-0.011	33.370	0.003	0.003	0.000	0.000	0.000	0.000
98	A	120	ILE	0	-0.025	0.006	27.156	0.006	0.006	0.000	0.000	0.000	0.000
99	A	121	ALA	0	0.021	0.006	30.913	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	122	PHE	0	-0.059	-0.030	28.696	0.003	0.003	0.000	0.000	0.000	0.000
101	A	123	THR	0	0.002	0.008	30.520	0.000	0.000	0.000	0.000	0.000	0.000
102	A	124	TYR	0	0.004	0.012	30.342	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	125	GLY	0	0.011	-0.015	29.263	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	126	ASP	-1	-0.902	-0.927	26.670	-0.015	-0.015	0.000	0.000	0.000	0.000
105	A	127	TYR	0	-0.012	-0.014	21.444	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	128	SER	0	-0.035	-0.039	19.066	0.016	0.016	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.939	0.965	19.282	-0.037	-0.037	0.000	0.000	0.000	0.000
108	A	130	ASN	0	0.063	0.021	15.185	0.011	0.011	0.000	0.000	0.000	0.000
109	A	131	SER	0	-0.030	-0.008	16.047	0.050	0.050	0.000	0.000	0.000	0.000
110	A	132	PRO	0	0.058	0.020	15.763	-0.021	-0.021	0.000	0.000	0.000	0.000
111	A	133	TYR	0	-0.040	-0.027	18.024	0.002	0.002	0.000	0.000	0.000	0.000
112	A	134	ASP	-1	-0.833	-0.896	21.184	0.043	0.043	0.000	0.000	0.000	0.000
113	A	135	PRO	0	0.051	0.023	21.764	0.007	0.007	0.000	0.000	0.000	0.000
114	A	136	SER	0	-0.022	-0.030	22.773	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	137	TYR	0	0.004	0.039	13.116	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	138	TYR	0	-0.051	-0.037	17.351	0.008	0.008	0.000	0.000	0.000	0.000
117	A	139	TYR	0	-0.018	0.005	20.032	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	140	VAL	0	0.034	0.048	22.298	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	141	SER	0	0.010	0.003	20.786	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.874	-0.945	21.759	-0.157	-0.157	0.000	0.000	0.000	0.000
121	A	143	GLY	0	0.047	0.005	22.337	0.003	0.003	0.000	0.000	0.000	0.000
122	A	144	MET	0	-0.047	-0.004	23.821	0.003	0.003	0.000	0.000	0.000	0.000
123	A	145	GLN	0	0.046	0.005	25.681	0.011	0.011	0.000	0.000	0.000	0.000
124	A	146	GLU	-1	-0.833	-0.904	26.500	-0.107	-0.107	0.000	0.000	0.000	0.000
125	A	147	PRO	0	0.035	0.009	28.532	0.000	0.000	0.000	0.000	0.000	0.000
126	A	148	LEU	0	-0.020	0.000	31.543	0.004	0.004	0.000	0.000	0.000	0.000
127	A	149	LYS	1	0.806	0.913	29.618	0.104	0.104	0.000	0.000	0.000	0.000
128	A	150	TYR	0	-0.023	-0.022	32.000	0.002	0.002	0.000	0.000	0.000	0.000
129	A	151	VAL	0	-0.053	-0.011	35.187	0.003	0.003	0.000	0.000	0.000	0.000
130	A	152	GLY	0	0.019	0.012	37.637	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	153	ASP	-1	-0.842	-0.934	38.663	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	154	ARG	1	0.908	0.945	39.383	0.001	0.001	0.000	0.000	0.000	0.000
133	A	155	ALA	0	0.017	0.039	37.033	0.001	0.001	0.000	0.000	0.000	0.000
134	A	156	LYS	1	0.898	0.936	35.536	0.011	0.011	0.000	0.000	0.000	0.000
135	A	157	VAL	0	0.003	0.006	30.806	-0.004	-0.004	0.000	0.000	0.000	0.000
136	A	158	LYS	1	0.904	0.969	30.256	0.046	0.046	0.000	0.000	0.000	0.000
137	A	159	MET	0	-0.032	-0.015	26.044	-0.009	-0.009	0.000	0.000	0.000	0.000
138	A	160	ILE	0	-0.004	0.019	21.952	0.009	0.009	0.000	0.000	0.000	0.000
139	A	161	VAL	0	-0.013	-0.002	20.006	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	162	PRO	0	0.030	0.025	17.875	0.009	0.009	0.000	0.000	0.000	0.000
141	A	163	PHE	0	0.030	0.008	11.599	-0.008	-0.008	0.000	0.000	0.000	0.000
142	A	164	LYS	1	0.891	0.946	15.396	0.402	0.402	0.000	0.000	0.000	0.000
143	A	165	ARG	1	0.841	0.925	16.200	0.228	0.228	0.000	0.000	0.000	0.000
144	A	166	GLY	0	0.081	0.043	17.444	0.030	0.030	0.000	0.000	0.000	0.000
145	A	167	ALA	0	0.011	0.010	18.117	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	168	TYR	0	0.032	0.008	11.948	-0.037	-0.037	0.000	0.000	0.000	0.000
147	A	169	ASN	0	0.006	-0.010	13.267	0.057	0.057	0.000	0.000	0.000	0.000
148	A	170	ASP	-1	-0.803	-0.889	12.581	0.086	0.086	0.000	0.000	0.000	0.000
149	A	171	GLN	0	-0.118	-0.064	12.311	-0.079	-0.079	0.000	0.000	0.000	0.000
150	A	172	SER	0	-0.063	-0.028	8.944	-0.131	-0.131	0.000	0.000	0.000	0.000
151	A	173	ASN	0	-0.072	-0.035	7.513	0.188	0.188	0.000	0.000	0.000	0.000
152	A	174	GLY	0	0.013	0.011	9.180	-0.057	-0.057	0.000	0.000	0.000	0.000
153	A	175	GLN	0	-0.079	-0.048	10.530	-0.040	-0.040	0.000	0.000	0.000	0.000
154	A	176	PRO	0	0.002	0.019	13.748	0.006	0.006	0.000	0.000	0.000	0.000
155	A	177	VAL	0	-0.027	-0.015	17.162	0.034	0.034	0.000	0.000	0.000	0.000
156	A	178	TYR	0	0.018	-0.008	20.121	-0.019	-0.019	0.000	0.000	0.000	0.000
157	A	179	TYR	0	0.017	-0.010	23.356	0.015	0.015	0.000	0.000	0.000	0.000
158	A	180	GLU	-1	-0.915	-0.963	26.635	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	181	ILE	0	-0.008	-0.021	29.384	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	182	LEU	0	-0.026	-0.005	28.413	0.007	0.007	0.000	0.000	0.000	0.000
161	A	183	GLU	-1	-0.933	-0.962	31.755	-0.003	-0.003	0.000	0.000	0.000	0.000
162	A	184	TYR	0	-0.002	-0.024	29.781	0.003	0.003	0.000	0.000	0.000	0.000
163	A	185	ILE	0	-0.034	-0.027	35.222	0.000	0.000	0.000	0.000	0.000	0.000
164	A	186	PHE	0	0.034	0.004	37.030	0.000	0.000	0.000	0.000	0.000	0.000
165	A	187	GLU	-1	-0.935	-0.993	36.931	0.014	0.014	0.000	0.000	0.000	0.000
166	A	188	GLU	-1	-0.994	-0.996	40.045	-0.013	-0.013	0.000	0.000	0.000	0.000
167	A	189	ASN	0	-0.069	-0.031	42.875	0.000	0.000	0.000	0.000	0.000	0.000
168	A	190	LEU	0	-0.082	-0.025	40.467	0.001	0.001	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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