FMO DATABASE

FMODB ID: N3R2Q

Calculation Name: 3O48-A-Xray313

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3O48

Chain ID: A

ChEMBL ID:

UniProt ID: P40515

Base Structure: X-ray

Registration Date: 2021-09-06

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1198928.344741
FMO2-HF: Nuclear repulsion	1145443.874022
FMO2-HF: Total energy	-53484.470719
FMO2-MP2: Total energy	-53640.913428

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:4:ACE )

Summations of interaction energy for fragment #1(A:4:ACE )

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.
1.322	1.999	-0.004	-0.258	-0.416	0

Interaction energy analysis for fragmet #1(A:4:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.013 / q_NPA : -0.017

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].
3	A	6	PHE	0	-0.007	0.010	3.873	1.125	1.802	-0.004	-0.258	-0.416
4	A	7	TRP	0	0.023	0.006	6.544	0.031	0.031	0.000	0.000	0.000
5	A	8	PRO	0	0.034	0.033	9.869	0.071	0.071	0.000	0.000	0.000
6	A	9	THR	0	-0.010	0.014	13.415	0.046	0.046	0.000	0.000	0.000
7	A	10	LEU	0	0.049	0.011	15.340	-0.004	-0.004	0.000	0.000	0.000
8	A	11	LYS	1	0.920	0.956	18.320	0.102	0.102	0.000	0.000	0.000
9	A	12	ASP	-1	-0.764	-0.884	16.166	-0.216	-0.216	0.000	0.000	0.000
10	A	13	ALA	0	-0.036	-0.015	18.661	-0.002	-0.002	0.000	0.000	0.000
11	A	14	TYR	0	-0.038	-0.013	20.253	0.013	0.013	0.000	0.000	0.000
12	A	15	GLU	-1	-0.929	-0.956	22.055	-0.124	-0.124	0.000	0.000	0.000
13	A	16	PRO	0	-0.013	0.005	23.610	-0.013	-0.013	0.000	0.000	0.000
14	A	17	LEU	0	-0.038	-0.014	22.762	-0.007	-0.007	0.000	0.000	0.000
15	A	18	TYR	0	0.001	-0.009	26.496	0.010	0.010	0.000	0.000	0.000
16	A	19	PRO	0	0.073	0.027	29.509	-0.005	-0.005	0.000	0.000	0.000
17	A	20	GLN	0	0.055	0.014	31.544	-0.004	-0.004	0.000	0.000	0.000
18	A	21	GLN	0	0.007	0.007	26.391	0.000	0.000	0.000	0.000	0.000
19	A	22	LEU	0	0.032	0.025	26.202	-0.009	-0.009	0.000	0.000	0.000
20	A	23	GLU	-1	-0.755	-0.863	28.096	-0.081	-0.081	0.000	0.000	0.000
21	A	24	ILE	0	-0.024	-0.013	27.676	0.000	0.000	0.000	0.000	0.000
22	A	25	LEU	0	-0.034	-0.016	23.183	-0.005	-0.005	0.000	0.000	0.000
23	A	26	ARG	1	0.841	0.906	26.452	0.076	0.076	0.000	0.000	0.000
24	A	27	GLN	0	-0.016	-0.021	28.723	0.002	0.002	0.000	0.000	0.000
25	A	28	GLN	0	-0.027	-0.001	25.089	0.007	0.007	0.000	0.000	0.000
26	A	29	VAL	0	-0.001	0.014	24.745	0.001	0.001	0.000	0.000	0.000
27	A	30	VAL	0	-0.021	-0.017	27.262	0.006	0.006	0.000	0.000	0.000
28	A	31	SER	0	-0.087	-0.045	29.266	0.004	0.004	0.000	0.000	0.000
29	A	32	GLU	-1	-0.743	-0.829	24.615	-0.151	-0.151	0.000	0.000	0.000
30	A	33	GLY	0	0.052	0.031	28.853	0.001	0.001	0.000	0.000	0.000
31	A	34	GLY	0	-0.016	-0.023	28.832	0.006	0.006	0.000	0.000	0.000
32	A	35	PRO	0	-0.024	-0.018	27.155	-0.008	-0.008	0.000	0.000	0.000
33	A	36	THR	0	-0.053	-0.020	26.716	-0.001	-0.001	0.000	0.000	0.000
34	A	37	ALA	0	0.007	0.033	25.315	-0.004	-0.004	0.000	0.000	0.000
35	A	38	THR	0	-0.011	-0.039	20.799	-0.011	-0.011	0.000	0.000	0.000
36	A	39	ILE	0	0.014	-0.003	16.665	-0.005	-0.005	0.000	0.000	0.000
37	A	40	GLN	0	-0.050	-0.032	14.909	-0.032	-0.032	0.000	0.000	0.000
38	A	41	SER	0	-0.012	-0.033	18.132	-0.012	-0.012	0.000	0.000	0.000
39	A	42	ARG	1	0.831	0.919	21.588	0.123	0.123	0.000	0.000	0.000
40	A	43	PHE	0	0.006	-0.003	13.646	0.015	0.015	0.000	0.000	0.000
41	A	44	ASN	0	0.017	0.003	17.920	-0.023	-0.023	0.000	0.000	0.000
42	A	45	TYR	0	0.014	0.014	19.823	0.011	0.011	0.000	0.000	0.000
43	A	46	ALA	0	0.025	0.013	20.303	0.009	0.009	0.000	0.000	0.000
44	A	47	TRP	0	0.037	0.004	17.168	0.012	0.012	0.000	0.000	0.000
45	A	48	GLY	0	-0.005	-0.017	19.979	0.007	0.007	0.000	0.000	0.000
46	A	49	LEU	0	-0.044	-0.019	23.046	0.010	0.010	0.000	0.000	0.000
47	A	50	ILE	0	-0.013	0.004	19.956	0.009	0.009	0.000	0.000	0.000
48	A	51	LYS	1	0.910	0.970	19.536	0.204	0.204	0.000	0.000	0.000
49	A	52	SER	0	-0.055	-0.010	23.465	0.008	0.008	0.000	0.000	0.000
50	A	53	THR	0	0.049	0.012	27.234	0.002	0.002	0.000	0.000	0.000
51	A	54	ASP	-1	-0.910	-0.939	29.625	-0.049	-0.049	0.000	0.000	0.000
52	A	55	VAL	0	0.104	0.034	29.883	-0.003	-0.003	0.000	0.000	0.000
53	A	56	ASN	0	-0.055	-0.028	30.028	0.002	0.002	0.000	0.000	0.000
54	A	57	ASP	-1	-0.875	-0.939	28.480	-0.076	-0.076	0.000	0.000	0.000
55	A	58	GLU	-1	-0.903	-0.955	25.845	-0.072	-0.072	0.000	0.000	0.000
56	A	59	ARG	1	0.925	0.959	25.604	0.036	0.036	0.000	0.000	0.000
57	A	60	LEU	0	-0.036	-0.014	27.101	0.000	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.043	0.009	24.079	-0.004	-0.004	0.000	0.000	0.000
59	A	62	VAL	0	0.038	0.022	22.097	-0.010	-0.010	0.000	0.000	0.000
60	A	63	LYS	1	0.939	0.990	23.035	0.049	0.049	0.000	0.000	0.000
61	A	64	ILE	0	0.022	0.015	22.594	0.000	0.000	0.000	0.000	0.000
62	A	65	LEU	0	0.009	-0.003	16.684	-0.006	-0.006	0.000	0.000	0.000
63	A	66	THR	0	-0.060	-0.051	19.694	0.001	0.001	0.000	0.000	0.000
64	A	67	ASP	-1	-0.940	-0.965	21.727	-0.058	-0.058	0.000	0.000	0.000
65	A	68	ILE	0	-0.028	-0.013	18.344	-0.001	-0.001	0.000	0.000	0.000
66	A	69	TYR	0	-0.030	-0.016	14.633	0.000	0.000	0.000	0.000	0.000
67	A	70	LYS	1	0.870	0.919	17.836	0.038	0.038	0.000	0.000	0.000
68	A	71	GLU	-1	-0.820	-0.894	20.377	-0.081	-0.081	0.000	0.000	0.000
69	A	72	ALA	0	-0.020	0.002	14.922	-0.007	-0.007	0.000	0.000	0.000
70	A	73	GLU	-1	-0.927	-0.965	15.154	-0.086	-0.086	0.000	0.000	0.000
71	A	74	SER	0	-0.017	-0.020	11.211	0.020	0.020	0.000	0.000	0.000
72	A	75	ARG	1	0.946	0.978	10.176	0.281	0.281	0.000	0.000	0.000
73	A	76	ARG	1	0.922	0.973	11.525	0.024	0.024	0.000	0.000	0.000
74	A	77	ARG	1	0.971	0.981	6.978	-0.223	-0.223	0.000	0.000	0.000
75	A	78	GLU	-1	-0.895	-0.938	8.850	-0.612	-0.612	0.000	0.000	0.000
76	A	79	CYS	0	-0.003	-0.010	9.882	0.053	0.053	0.000	0.000	0.000
77	A	80	LEU	0	0.005	0.017	12.249	0.023	0.023	0.000	0.000	0.000
78	A	81	TYR	0	-0.040	-0.021	10.542	0.042	0.042	0.000	0.000	0.000
79	A	82	TYR	0	0.020	-0.006	11.353	0.040	0.040	0.000	0.000	0.000
80	A	83	LEU	0	0.001	-0.004	15.156	0.019	0.019	0.000	0.000	0.000
81	A	84	THR	0	-0.050	-0.020	15.568	0.025	0.025	0.000	0.000	0.000
82	A	85	ILE	0	-0.022	-0.008	15.017	0.010	0.010	0.000	0.000	0.000
83	A	86	GLY	0	0.029	0.010	18.448	0.008	0.008	0.000	0.000	0.000
84	A	87	CYS	0	-0.036	-0.022	20.842	0.008	0.008	0.000	0.000	0.000
85	A	88	TYR	0	-0.034	-0.021	20.954	0.010	0.010	0.000	0.000	0.000
86	A	89	LYS	1	0.757	0.866	22.145	0.094	0.094	0.000	0.000	0.000
87	A	90	LEU	0	-0.021	0.006	24.563	0.004	0.004	0.000	0.000	0.000
88	A	91	GLY	0	-0.005	0.005	26.254	0.004	0.004	0.000	0.000	0.000
89	A	92	GLU	-1	-0.916	-0.955	25.257	-0.028	-0.028	0.000	0.000	0.000
90	A	93	TYR	0	0.050	0.002	24.358	0.002	0.002	0.000	0.000	0.000
91	A	94	SER	0	0.043	0.023	24.038	0.005	0.005	0.000	0.000	0.000
92	A	95	MET	0	-0.023	-0.014	22.904	0.011	0.011	0.000	0.000	0.000
93	A	96	ALA	0	0.035	0.016	20.278	0.003	0.003	0.000	0.000	0.000
94	A	97	LYS	1	0.930	0.966	19.260	-0.057	-0.057	0.000	0.000	0.000
95	A	98	ARG	1	0.949	0.972	19.722	-0.005	-0.005	0.000	0.000	0.000
96	A	99	TYR	0	0.009	-0.002	16.833	0.013	0.013	0.000	0.000	0.000
97	A	100	VAL	0	0.038	0.016	14.657	0.014	0.014	0.000	0.000	0.000
98	A	101	ASP	-1	-0.834	-0.918	14.859	0.129	0.129	0.000	0.000	0.000
99	A	102	THR	0	-0.058	-0.029	14.713	0.028	0.028	0.000	0.000	0.000
100	A	103	LEU	0	-0.061	-0.030	8.872	0.030	0.030	0.000	0.000	0.000
101	A	104	PHE	0	0.005	-0.010	10.864	0.091	0.091	0.000	0.000	0.000
102	A	105	GLU	-1	-0.938	-0.961	12.420	0.283	0.283	0.000	0.000	0.000
103	A	106	HIS	0	-0.101	-0.060	8.859	0.081	0.081	0.000	0.000	0.000
104	A	107	GLU	-1	-0.908	-0.965	5.732	1.241	1.241	0.000	0.000	0.000
105	A	108	ARG	1	0.959	0.992	8.796	-0.408	-0.408	0.000	0.000	0.000
106	A	109	ASN	0	-0.006	-0.002	9.555	-0.122	-0.122	0.000	0.000	0.000
107	A	110	ASN	0	0.002	0.021	5.484	-0.245	-0.245	0.000	0.000	0.000
108	A	111	LYS	1	1.003	0.987	8.562	-0.206	-0.206	0.000	0.000	0.000
109	A	112	GLN	0	-0.011	-0.011	8.539	-0.126	-0.126	0.000	0.000	0.000
110	A	113	VAL	0	0.051	0.024	8.899	-0.049	-0.049	0.000	0.000	0.000
111	A	114	GLY	0	0.012	0.015	11.605	-0.024	-0.024	0.000	0.000	0.000
112	A	115	ALA	0	-0.026	-0.018	13.837	-0.025	-0.025	0.000	0.000	0.000
113	A	116	LEU	0	-0.012	-0.003	14.297	-0.012	-0.012	0.000	0.000	0.000
114	A	117	LYS	1	0.909	0.946	15.700	-0.139	-0.139	0.000	0.000	0.000
115	A	118	SER	0	0.033	0.021	17.486	-0.004	-0.004	0.000	0.000	0.000
116	A	119	MET	0	-0.021	0.003	19.404	-0.008	-0.008	0.000	0.000	0.000
117	A	120	VAL	0	-0.030	-0.025	19.198	-0.007	-0.007	0.000	0.000	0.000
118	A	121	GLU	-1	-0.894	-0.953	21.140	0.087	0.087	0.000	0.000	0.000
119	A	122	ASP	-1	-0.887	-0.936	23.597	0.025	0.025	0.000	0.000	0.000
120	A	123	LYS	1	0.841	0.921	25.284	0.007	0.007	0.000	0.000	0.000
121	A	124	ILE	0	-0.013	-0.004	24.870	-0.001	-0.001	0.000	0.000	0.000
122	A	125	GLN	0	0.009	0.007	27.579	0.003	0.003	0.000	0.000	0.000
123	A	126	LYS	1	0.889	0.932	29.564	-0.011	-0.011	0.000	0.000	0.000
124	A	127	GLU	-1	-0.886	-0.914	31.101	0.008	0.008	0.000	0.000	0.000
125	A	128	GLU	-1	-0.889	-0.947	31.598	0.029	0.029	0.000	0.000	0.000
126	A	129	ASN	0	-0.023	-0.018	33.387	0.002	0.002	0.000	0.000	0.000
127	A	130	LEU	0	-0.039	-0.018	35.872	-0.001	-0.001	0.000	0.000	0.000
128	A	131	TYR	0	-0.123	-0.078	34.315	-0.002	-0.002	0.000	0.000	0.000
129	A	132	PHE	0	-0.087	-0.036	36.098	0.001	0.001	0.000	0.000	0.000
130	A	133	GLN	-1	-0.993	-0.975	39.368	0.012	0.012	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ACE )