FMO DATABASE

FMODB ID: K3R83

Calculation Name: 4O2T-A-Xray322

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: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	168
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1814682.137558
FMO2-HF: Nuclear repulsion	1745885.092644
FMO2-HF: Total energy	-68797.044914
FMO2-MP2: Total energy	-68995.868399

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.
0.29	1.659	-0.005	-0.696	-0.668	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 : 0.043 / q_NPA : 0.016

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	0.013	0.010	3.797	0.161	1.530	-0.005	-0.696	-0.668	0.003
4	A	26	TYR	0	0.067	0.015	6.481	0.486	0.486	0.000	0.000	0.000	0.000
5	A	27	THR	0	0.020	-0.002	8.881	0.243	0.243	0.000	0.000	0.000	0.000
6	A	28	ASP	-1	-0.894	-0.943	7.991	-1.804	-1.804	0.000	0.000	0.000	0.000
7	A	29	MET	0	-0.019	-0.003	6.278	0.285	0.285	0.000	0.000	0.000	0.000
8	A	30	LEU	0	0.007	0.005	9.856	0.230	0.230	0.000	0.000	0.000	0.000
9	A	31	LYS	1	0.924	0.980	12.847	0.854	0.854	0.000	0.000	0.000	0.000
10	A	32	ASP	-1	-0.883	-0.947	10.197	-0.781	-0.781	0.000	0.000	0.000	0.000
11	A	33	GLU	-1	-0.744	-0.885	13.472	-0.233	-0.233	0.000	0.000	0.000	0.000
12	A	34	LYS	1	0.925	0.970	15.315	0.405	0.405	0.000	0.000	0.000	0.000
13	A	35	LYS	1	0.939	0.971	16.130	0.380	0.380	0.000	0.000	0.000	0.000
14	A	36	ALA	0	-0.007	-0.008	16.624	0.045	0.045	0.000	0.000	0.000	0.000
15	A	37	ILE	0	0.024	0.009	18.576	0.041	0.041	0.000	0.000	0.000	0.000
16	A	38	GLU	-1	-0.905	-0.954	21.143	-0.247	-0.247	0.000	0.000	0.000	0.000
17	A	39	ARG	1	0.926	0.963	20.132	0.148	0.148	0.000	0.000	0.000	0.000
18	A	40	PHE	0	-0.004	0.004	22.387	0.022	0.022	0.000	0.000	0.000	0.000
19	A	41	ILE	0	0.011	-0.011	24.190	0.014	0.014	0.000	0.000	0.000	0.000
20	A	42	ASP	-1	-0.968	-0.979	26.700	-0.101	-0.101	0.000	0.000	0.000	0.000
21	A	43	ASP	-1	-0.980	-0.993	26.414	-0.050	-0.050	0.000	0.000	0.000	0.000
22	A	44	LYS	1	0.881	0.954	27.111	0.053	0.053	0.000	0.000	0.000	0.000
23	A	45	GLY	0	-0.015	0.014	30.274	0.006	0.006	0.000	0.000	0.000	0.000
24	A	46	LEU	0	-0.060	-0.034	28.212	0.006	0.006	0.000	0.000	0.000	0.000
25	A	47	GLU	-1	-0.957	-0.975	32.014	-0.081	-0.081	0.000	0.000	0.000	0.000
26	A	48	ILE	0	-0.028	-0.030	28.839	0.002	0.002	0.000	0.000	0.000	0.000
27	A	49	LEU	0	-0.031	-0.013	31.984	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	50	ASP	-1	-0.892	-0.952	32.472	-0.132	-0.132	0.000	0.000	0.000	0.000
29	A	51	ASP	-1	-0.907	-0.956	33.999	-0.090	-0.090	0.000	0.000	0.000	0.000
30	A	52	PHE	0	-0.070	-0.045	34.301	0.003	0.003	0.000	0.000	0.000	0.000
31	A	53	PRO	0	-0.008	0.012	37.236	0.001	0.001	0.000	0.000	0.000	0.000
32	A	54	ALA	0	-0.004	-0.007	40.234	0.002	0.002	0.000	0.000	0.000	0.000
33	A	55	ASP	-1	-0.907	-0.966	43.673	-0.040	-0.040	0.000	0.000	0.000	0.000
34	A	56	SER	0	-0.098	-0.049	39.339	0.002	0.002	0.000	0.000	0.000	0.000
35	A	57	VAL	0	-0.011	0.011	40.286	0.003	0.003	0.000	0.000	0.000	0.000
36	A	58	PHE	0	0.008	0.000	34.504	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	59	LYS	1	0.938	0.961	38.923	0.056	0.056	0.000	0.000	0.000	0.000
38	A	60	GLU	-1	-0.949	-0.983	35.071	-0.044	-0.044	0.000	0.000	0.000	0.000
39	A	61	ASN	0	0.027	0.010	34.244	0.003	0.003	0.000	0.000	0.000	0.000
40	A	62	GLN	0	0.012	0.015	33.742	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	63	PHE	0	-0.014	-0.020	29.085	0.006	0.006	0.000	0.000	0.000	0.000
42	A	64	VAL	0	0.018	0.027	31.723	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	65	LEU	0	-0.003	0.000	25.212	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	66	LEU	0	-0.002	0.004	27.665	0.001	0.001	0.000	0.000	0.000	0.000
45	A	67	ASP	-1	-0.840	-0.920	27.051	-0.151	-0.151	0.000	0.000	0.000	0.000
46	A	68	ASN	0	-0.124	-0.064	24.032	-0.021	-0.021	0.000	0.000	0.000	0.000
47	A	69	GLY	0	0.007	-0.001	22.397	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	70	VAL	0	-0.038	-0.013	23.087	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	71	TYR	0	0.010	0.012	23.036	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	72	LEU	0	0.002	-0.009	27.135	0.010	0.010	0.000	0.000	0.000	0.000
51	A	73	ASN	0	-0.014	0.005	30.208	0.003	0.003	0.000	0.000	0.000	0.000
52	A	74	ILE	0	0.003	-0.001	33.243	0.005	0.005	0.000	0.000	0.000	0.000
53	A	75	ILE	0	-0.027	-0.008	34.748	0.001	0.001	0.000	0.000	0.000	0.000
54	A	76	ASP	-1	-0.897	-0.959	37.931	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	77	LYS	1	1.016	1.001	38.766	0.035	0.035	0.000	0.000	0.000	0.000
56	A	78	GLY	0	0.040	0.020	40.363	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	79	SER	0	-0.037	-0.007	41.739	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	80	ASP	-1	-0.861	-0.945	42.681	-0.027	-0.027	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.049	-0.008	41.959	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	82	ARG	1	0.877	0.939	38.594	0.033	0.033	0.000	0.000	0.000	0.000
61	A	83	ALA	0	0.031	0.023	35.587	0.003	0.003	0.000	0.000	0.000	0.000
62	A	84	VAL	0	-0.003	-0.008	37.210	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	85	GLN	0	0.002	-0.008	30.131	0.003	0.003	0.000	0.000	0.000	0.000
64	A	86	TYR	0	-0.066	-0.048	29.652	0.001	0.001	0.000	0.000	0.000	0.000
65	A	87	LYS	1	0.891	0.949	33.993	0.020	0.020	0.000	0.000	0.000	0.000
66	A	88	THR	0	0.064	0.046	36.231	0.002	0.002	0.000	0.000	0.000	0.000
67	A	89	LYS	1	0.949	0.985	35.134	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	90	MET	0	-0.012	0.011	32.827	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	91	LEU	0	0.024	0.012	33.493	0.007	0.007	0.000	0.000	0.000	0.000
70	A	92	TYR	0	-0.032	-0.056	25.734	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	93	ARG	1	0.851	0.920	32.055	-0.025	-0.025	0.000	0.000	0.000	0.000
72	A	94	CYS	0	-0.033	-0.012	27.822	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	95	LYS	1	0.946	0.988	28.121	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	96	MET	0	0.005	0.012	20.690	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	97	SER	0	-0.014	-0.018	22.674	0.020	0.020	0.000	0.000	0.000	0.000
76	A	98	TYR	0	-0.053	-0.034	16.588	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	99	PHE	0	-0.005	-0.030	18.504	0.001	0.001	0.000	0.000	0.000	0.000
78	A	100	MET	0	-0.066	-0.005	11.488	-0.032	-0.032	0.000	0.000	0.000	0.000
79	A	101	ASP	-1	-0.853	-0.929	12.020	-0.085	-0.085	0.000	0.000	0.000	0.000
80	A	102	SER	0	-0.079	-0.047	15.468	0.045	0.045	0.000	0.000	0.000	0.000
81	A	103	THR	0	0.015	-0.004	18.561	-0.023	-0.023	0.000	0.000	0.000	0.000
82	A	104	ILE	0	-0.014	0.014	18.112	0.000	0.000	0.000	0.000	0.000	0.000
83	A	105	VAL	0	0.009	0.010	21.634	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	106	ALA	0	-0.032	-0.011	20.751	0.017	0.017	0.000	0.000	0.000	0.000
85	A	107	ILE	0	-0.019	-0.012	22.733	0.010	0.010	0.000	0.000	0.000	0.000
86	A	108	GLU	-1	-0.880	-0.954	25.962	0.037	0.037	0.000	0.000	0.000	0.000
87	A	109	ASN	0	-0.001	0.002	29.448	0.000	0.000	0.000	0.000	0.000	0.000
88	A	110	TYR	0	0.047	0.022	32.180	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	111	GLY	0	0.033	0.029	33.923	0.002	0.002	0.000	0.000	0.000	0.000
90	A	112	PRO	0	-0.008	0.010	36.335	0.004	0.004	0.000	0.000	0.000	0.000
91	A	113	HIS	0	-0.002	-0.006	34.238	0.004	0.004	0.000	0.000	0.000	0.000
92	A	114	SER	0	-0.034	-0.008	34.258	0.006	0.006	0.000	0.000	0.000	0.000
93	A	115	ASN	0	0.039	0.004	35.367	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	116	GLY	0	-0.002	0.001	37.341	0.005	0.005	0.000	0.000	0.000	0.000
95	A	117	THR	0	-0.022	0.001	32.976	0.002	0.002	0.000	0.000	0.000	0.000
96	A	118	SER	0	-0.006	-0.008	34.325	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	119	PRO	0	0.003	-0.008	33.367	0.003	0.003	0.000	0.000	0.000	0.000
98	A	120	ILE	0	-0.030	0.003	27.154	0.007	0.007	0.000	0.000	0.000	0.000
99	A	121	ALA	0	0.023	0.008	30.911	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	122	PHE	0	-0.060	-0.032	28.695	0.004	0.004	0.000	0.000	0.000	0.000
101	A	123	THR	0	0.005	0.010	30.519	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	124	TYR	0	0.002	0.012	30.341	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	125	GLY	0	0.012	-0.015	29.264	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	126	ASP	-1	-0.902	-0.927	26.670	0.010	0.010	0.000	0.000	0.000	0.000
105	A	127	TYR	0	-0.016	-0.016	21.444	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	128	SER	0	-0.037	-0.039	19.066	0.019	0.019	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.939	0.966	19.281	-0.068	-0.068	0.000	0.000	0.000	0.000
108	A	130	ASN	0	0.066	0.021	15.184	0.002	0.002	0.000	0.000	0.000	0.000
109	A	131	SER	0	-0.035	-0.010	16.045	0.062	0.062	0.000	0.000	0.000	0.000
110	A	132	PRO	0	0.057	0.020	15.760	-0.026	-0.026	0.000	0.000	0.000	0.000
111	A	133	TYR	0	-0.039	-0.026	18.021	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	134	ASP	-1	-0.834	-0.897	21.181	0.074	0.074	0.000	0.000	0.000	0.000
113	A	135	PRO	0	0.054	0.024	21.762	0.009	0.009	0.000	0.000	0.000	0.000
114	A	136	SER	0	-0.020	-0.028	22.772	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	137	TYR	0	-0.002	0.038	13.114	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	138	TYR	0	-0.049	-0.037	17.347	0.011	0.011	0.000	0.000	0.000	0.000
117	A	139	TYR	0	-0.016	0.005	20.029	-0.015	-0.015	0.000	0.000	0.000	0.000
118	A	140	VAL	0	0.037	0.050	22.296	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	141	SER	0	0.009	0.002	20.782	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.870	-0.944	21.759	-0.136	-0.136	0.000	0.000	0.000	0.000
121	A	143	GLY	0	0.042	0.003	22.337	0.000	0.000	0.000	0.000	0.000	0.000
122	A	144	MET	0	-0.047	-0.003	23.821	0.001	0.001	0.000	0.000	0.000	0.000
123	A	145	GLN	0	0.051	0.008	25.682	0.008	0.008	0.000	0.000	0.000	0.000
124	A	146	GLU	-1	-0.838	-0.907	26.501	-0.096	-0.096	0.000	0.000	0.000	0.000
125	A	147	PRO	0	0.038	0.009	28.532	0.000	0.000	0.000	0.000	0.000	0.000
126	A	148	LEU	0	-0.017	0.002	31.546	0.004	0.004	0.000	0.000	0.000	0.000
127	A	149	LYS	1	0.804	0.913	29.620	0.092	0.092	0.000	0.000	0.000	0.000
128	A	150	TYR	0	-0.027	-0.024	32.001	0.001	0.001	0.000	0.000	0.000	0.000
129	A	151	VAL	0	-0.053	-0.012	35.186	0.002	0.002	0.000	0.000	0.000	0.000
130	A	152	GLY	0	0.017	0.011	37.638	0.000	0.000	0.000	0.000	0.000	0.000
131	A	153	ASP	-1	-0.837	-0.930	38.663	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	154	ARG	1	0.911	0.947	39.382	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	155	ALA	0	0.016	0.038	37.033	0.000	0.000	0.000	0.000	0.000	0.000
134	A	156	LYS	1	0.894	0.934	35.536	0.008	0.008	0.000	0.000	0.000	0.000
135	A	157	VAL	0	0.003	0.006	30.806	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	158	LYS	1	0.899	0.967	30.255	0.049	0.049	0.000	0.000	0.000	0.000
137	A	159	MET	0	-0.027	-0.014	26.043	-0.009	-0.009	0.000	0.000	0.000	0.000
138	A	160	ILE	0	-0.007	0.018	21.952	0.008	0.008	0.000	0.000	0.000	0.000
139	A	161	VAL	0	-0.008	0.000	20.006	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	162	PRO	0	0.028	0.024	17.876	0.008	0.008	0.000	0.000	0.000	0.000
141	A	163	PHE	0	0.027	0.007	11.601	-0.002	-0.002	0.000	0.000	0.000	0.000
142	A	164	LYS	1	0.889	0.946	15.398	0.385	0.385	0.000	0.000	0.000	0.000
143	A	165	ARG	1	0.842	0.925	16.201	0.214	0.214	0.000	0.000	0.000	0.000
144	A	166	GLY	0	0.077	0.041	17.444	0.029	0.029	0.000	0.000	0.000	0.000
145	A	167	ALA	0	0.018	0.013	18.117	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	168	TYR	0	0.034	0.008	11.948	-0.038	-0.038	0.000	0.000	0.000	0.000
147	A	169	ASN	0	0.003	-0.009	13.266	0.076	0.076	0.000	0.000	0.000	0.000
148	A	170	ASP	-1	-0.804	-0.890	12.579	0.112	0.112	0.000	0.000	0.000	0.000
149	A	171	GLN	0	-0.118	-0.063	12.310	-0.079	-0.079	0.000	0.000	0.000	0.000
150	A	172	SER	0	-0.063	-0.028	8.943	-0.120	-0.120	0.000	0.000	0.000	0.000
151	A	173	ASN	0	-0.073	-0.036	7.512	0.214	0.214	0.000	0.000	0.000	0.000
152	A	174	GLY	0	0.010	0.010	9.179	-0.088	-0.088	0.000	0.000	0.000	0.000
153	A	175	GLN	0	-0.076	-0.048	10.530	-0.049	-0.049	0.000	0.000	0.000	0.000
154	A	176	PRO	0	0.000	0.018	13.747	0.012	0.012	0.000	0.000	0.000	0.000
155	A	177	VAL	0	-0.024	-0.014	17.162	0.033	0.033	0.000	0.000	0.000	0.000
156	A	178	TYR	0	0.010	-0.011	20.120	-0.020	-0.020	0.000	0.000	0.000	0.000
157	A	179	TYR	0	0.021	-0.009	23.355	0.016	0.016	0.000	0.000	0.000	0.000
158	A	180	GLU	-1	-0.916	-0.963	26.634	-0.006	-0.006	0.000	0.000	0.000	0.000
159	A	181	ILE	0	-0.007	-0.021	29.384	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	182	LEU	0	-0.029	-0.006	28.412	0.008	0.008	0.000	0.000	0.000	0.000
161	A	183	GLU	-1	-0.931	-0.963	31.754	0.001	0.001	0.000	0.000	0.000	0.000
162	A	184	TYR	0	-0.007	-0.027	29.781	0.004	0.004	0.000	0.000	0.000	0.000
163	A	185	ILE	0	-0.025	-0.023	35.221	0.000	0.000	0.000	0.000	0.000	0.000
164	A	186	PHE	0	0.020	-0.005	37.029	0.001	0.001	0.000	0.000	0.000	0.000
165	A	187	GLU	-1	-0.930	-0.990	36.929	0.026	0.026	0.000	0.000	0.000	0.000
166	A	188	GLU	-1	-1.009	-1.003	40.044	-0.004	-0.004	0.000	0.000	0.000	0.000
167	A	189	ASN	0	-0.102	-0.052	42.873	0.000	0.000	0.000	0.000	0.000	0.000
168	A	190	LEU	-1	-0.999	-0.980	40.469	0.013	0.013	0.000	0.000	0.000	0.000

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