FMO DATABASE

FMODB ID: 2JNJR

Calculation Name: 1A0K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A0K

Chain ID: A

ChEMBL ID:

UniProt ID: Q42449

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptAll
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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1111271.32111
FMO2-HF: Nuclear repulsion	1061381.219912
FMO2-HF: Total energy	-49890.101198
FMO2-MP2: Total energy	-50034.757149

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:2:SER)

Summations of interaction energy for fragment #1(A:2: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.
-22.102	-21.044	15.966	-8.445	-8.578	-0.017

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.019 / q_NPA : 0.007

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	4	GLN	0	-0.016	-0.042	2.889	-3.569	-0.076	0.409	-1.856	-2.046	0.009
4	A	5	SER	0	0.021	0.028	1.967	-15.329	-19.037	15.531	-6.083	-5.740	-0.024
5	A	6	TYR	0	-0.020	-0.019	3.510	-1.355	-0.082	0.026	-0.506	-0.792	-0.002
6	A	7	VAL	0	-0.007	-0.003	5.825	0.670	0.670	0.000	0.000	0.000	0.000
7	A	8	ASP	-1	-0.842	-0.932	6.757	0.476	0.476	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.896	-0.954	5.853	-2.452	-2.452	0.000	0.000	0.000	0.000
9	A	10	HIS	0	-0.019	-0.016	6.265	0.016	0.016	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.053	-0.009	10.198	0.245	0.245	0.000	0.000	0.000	0.000
11	A	12	MET	0	-0.078	-0.030	11.196	0.155	0.155	0.000	0.000	0.000	0.000
12	A	13	CYS	0	-0.026	0.004	12.154	0.085	0.085	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.892	-0.958	13.672	-0.272	-0.272	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.026	-0.021	17.516	-0.035	-0.035	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.940	-0.971	20.036	-0.185	-0.185	0.000	0.000	0.000	0.000
16	A	17	GLY	0	-0.011	0.005	21.880	0.023	0.023	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.017	-0.007	21.488	0.042	0.042	0.000	0.000	0.000	0.000
18	A	19	HIS	1	0.901	0.955	16.123	0.168	0.168	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.000	-0.003	14.969	0.048	0.048	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.072	-0.059	17.639	0.016	0.016	0.000	0.000	0.000	0.000
21	A	22	ALA	0	-0.038	-0.027	16.025	0.045	0.045	0.000	0.000	0.000	0.000
22	A	23	ALA	0	0.022	0.010	12.604	-0.051	-0.051	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.004	-0.001	11.183	0.144	0.144	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.016	0.020	7.294	-0.180	-0.180	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.007	-0.001	10.856	0.170	0.170	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.094	0.049	13.241	-0.101	-0.101	0.000	0.000	0.000	0.000
27	A	28	GLN	0	-0.051	-0.038	14.070	0.063	0.063	0.000	0.000	0.000	0.000
28	A	29	ASP	-1	-0.843	-0.898	15.872	0.042	0.042	0.000	0.000	0.000	0.000
29	A	30	GLY	0	-0.017	-0.013	17.250	0.016	0.016	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.086	-0.064	13.515	0.022	0.022	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.011	-0.010	10.873	-0.064	-0.064	0.000	0.000	0.000	0.000
32	A	33	TRP	0	-0.047	-0.016	7.789	0.074	0.074	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.001	0.004	6.000	0.393	0.393	0.000	0.000	0.000	0.000
34	A	35	GLN	0	-0.050	-0.028	8.039	-0.376	-0.376	0.000	0.000	0.000	0.000
35	A	36	SER	0	0.068	0.060	10.075	0.166	0.166	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.004	-0.023	12.055	0.016	0.016	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.938	0.969	14.520	-0.024	-0.024	0.000	0.000	0.000	0.000
38	A	39	PHE	0	0.003	0.016	14.642	-0.043	-0.043	0.000	0.000	0.000	0.000
39	A	40	PRO	0	0.008	0.016	16.695	0.037	0.037	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.005	-0.015	19.051	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.016	0.003	18.939	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.815	0.886	21.616	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.054	0.017	23.513	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.067	0.021	24.509	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.809	-0.869	24.475	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.036	0.016	19.425	-0.017	-0.017	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.835	-0.929	22.845	-0.043	-0.043	0.000	0.000	0.000	0.000
48	A	49	GLY	0	-0.023	-0.002	25.488	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.004	-0.018	21.716	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.827	0.923	20.999	0.032	0.032	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.804	0.889	24.310	0.051	0.051	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.849	-0.933	27.150	-0.115	-0.115	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.009	-0.014	20.963	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.828	-0.897	24.564	-0.153	-0.153	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.890	-0.915	28.103	-0.058	-0.058	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.015	-0.009	28.634	0.004	0.004	0.000	0.000	0.000	0.000
57	A	58	GLY	0	-0.002	-0.003	30.706	0.004	0.004	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.015	-0.009	30.300	0.010	0.010	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.002	-0.009	27.295	0.008	0.008	0.000	0.000	0.000	0.000
60	A	61	ALA	0	-0.047	-0.012	31.674	0.003	0.003	0.000	0.000	0.000	0.000
61	A	62	PRO	0	-0.025	-0.012	33.888	0.003	0.003	0.000	0.000	0.000	0.000
62	A	63	THR	0	-0.003	0.000	32.670	0.003	0.003	0.000	0.000	0.000	0.000
63	A	64	GLY	0	-0.037	-0.011	32.417	0.006	0.006	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.059	0.030	24.615	0.005	0.005	0.000	0.000	0.000	0.000
65	A	66	PHE	0	-0.030	-0.021	28.031	0.002	0.002	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.017	0.009	21.863	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.047	0.024	24.356	0.003	0.003	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.053	-0.042	24.815	0.012	0.012	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.849	-0.893	26.722	-0.027	-0.027	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.874	0.935	28.092	0.041	0.041	0.000	0.000	0.000	0.000
71	A	72	TYR	0	0.017	0.003	24.768	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	MET	0	-0.042	-0.028	29.386	0.004	0.004	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.047	0.027	29.208	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.050	-0.025	28.770	0.006	0.006	0.000	0.000	0.000	0.000
75	A	76	GLN	0	-0.007	-0.005	29.339	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.035	0.030	26.455	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.916	-0.976	22.871	-0.284	-0.284	0.000	0.000	0.000	0.000
78	A	79	GLN	0	-0.013	-0.017	25.595	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.040	0.035	25.508	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	81	ALA	0	-0.015	0.003	21.573	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.048	-0.028	20.695	-0.030	-0.030	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.023	0.028	22.540	0.029	0.029	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.792	0.863	23.140	0.233	0.233	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.037	0.008	25.475	0.018	0.018	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.762	0.876	26.810	0.103	0.103	0.000	0.000	0.000	0.000
86	A	87	LYS	1	0.820	0.904	27.501	0.051	0.051	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.029	0.029	29.997	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	PRO	0	0.056	0.036	29.980	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.072	0.051	26.812	-0.013	-0.013	0.000	0.000	0.000	0.000
90	A	91	GLY	0	-0.066	-0.050	25.210	0.006	0.006	0.000	0.000	0.000	0.000
91	A	92	VAL	0	-0.049	-0.009	20.852	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	THR	0	0.019	0.001	19.968	0.016	0.016	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.008	-0.002	18.586	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.838	0.940	16.401	0.439	0.439	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.806	0.907	16.509	0.145	0.145	0.000	0.000	0.000	0.000
96	A	97	THR	0	0.007	-0.018	13.015	-0.013	-0.013	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.023	-0.023	15.424	0.068	0.068	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.039	-0.010	12.307	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.014	0.003	11.948	0.059	0.059	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.023	0.000	13.969	0.014	0.014	0.000	0.000	0.000	0.000
101	A	102	VAL	0	0.019	0.021	11.887	0.007	0.007	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.025	-0.006	14.073	0.069	0.069	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.017	-0.008	14.915	-0.034	-0.034	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.004	-0.002	17.274	0.018	0.018	0.000	0.000	0.000	0.000
105	A	106	TYR	0	0.022	-0.001	19.641	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.809	-0.888	22.233	-0.068	-0.068	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.924	-0.952	25.050	-0.096	-0.096	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.037	-0.028	26.211	0.010	0.010	0.000	0.000	0.000	0.000
109	A	110	MET	0	-0.015	0.021	18.804	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.026	-0.039	24.816	0.010	0.010	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.047	0.008	24.125	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.001	0.002	23.988	-0.018	-0.018	0.000	0.000	0.000	0.000
113	A	114	GLN	0	0.039	0.023	21.491	-0.010	-0.010	0.000	0.000	0.000	0.000
114	A	115	CYS	0	-0.022	0.001	19.755	-0.046	-0.046	0.000	0.000	0.000	0.000
115	A	116	ASN	0	0.053	0.024	19.121	-0.039	-0.039	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.025	0.004	18.461	-0.044	-0.044	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.014	-0.024	15.012	-0.067	-0.067	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.010	0.005	14.449	-0.113	-0.113	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.782	-0.890	14.971	-0.392	-0.392	0.000	0.000	0.000	0.000
120	A	121	ARG	1	0.858	0.939	13.481	0.766	0.766	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.018	0.002	7.885	-0.065	-0.065	0.000	0.000	0.000	0.000
122	A	123	GLY	0	0.031	0.004	11.458	-0.097	-0.097	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.802	-0.918	13.719	-0.467	-0.467	0.000	0.000	0.000	0.000
124	A	125	TYR	0	0.035	0.039	6.877	-0.279	-0.279	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.017	-0.015	7.362	-0.046	-0.046	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.052	-0.007	11.004	0.096	0.096	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.962	-0.980	13.576	-0.563	-0.563	0.000	0.000	0.000	0.000
128	A	129	SER	0	-0.092	-0.044	9.564	0.004	0.004	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.945	-0.972	11.433	-0.280	-0.280	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.045	-0.015	7.684	0.107	0.107	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)