FMO DATABASE

FMODB ID: 497ZN

Calculation Name: 2F15-A-Xray372

Preferred Name: AMP-activated protein kinase, beta-2 subunit

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2F15

Chain ID: A

ChEMBL ID: CHEMBL2117

UniProt ID: O43741

Base Structure: X-ray

Registration Date: 2023-09-20

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	89
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-609559.83315
FMO2-HF: Nuclear repulsion	574848.188141
FMO2-HF: Total energy	-34711.645009
FMO2-MP2: Total energy	-34816.284542

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:75:GLN)

Summations of interaction energy for fragment #1(A:75:GLN)

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.
-0.376	-15.427	29.334	-7.169	-7.115	-0.029

Interaction energy analysis for fragmet #1(A:75:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.025 / q_NPA : -0.029

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

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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	77	ARG	1	0.839	0.914	3.230	-1.058	1.920	0.047	-1.579	-1.447	-0.005
4	A	78	PRO	0	0.053	0.043	5.032	1.354	1.424	-0.001	-0.003	-0.066	0.000
5	A	79	THR	0	-0.032	-0.009	8.552	-0.105	-0.105	0.000	0.000	0.000	0.000
6	A	80	VAL	0	-0.009	0.005	10.740	0.264	0.264	0.000	0.000	0.000	0.000
7	A	81	ILE	0	-0.008	-0.002	14.353	0.025	0.025	0.000	0.000	0.000	0.000
8	A	82	ARG	1	0.873	0.905	16.996	0.599	0.599	0.000	0.000	0.000	0.000
9	A	83	TRP	0	0.013	-0.002	20.496	0.007	0.007	0.000	0.000	0.000	0.000
10	A	84	SER	0	0.005	-0.017	23.724	0.007	0.007	0.000	0.000	0.000	0.000
11	A	85	GLU	-1	-0.906	-0.946	26.467	-0.318	-0.318	0.000	0.000	0.000	0.000
12	A	86	GLY	0	-0.048	-0.010	28.886	0.026	0.026	0.000	0.000	0.000	0.000
13	A	87	GLY	0	0.070	0.051	30.481	0.003	0.003	0.000	0.000	0.000	0.000
14	A	88	LYS	1	0.813	0.882	31.696	0.206	0.206	0.000	0.000	0.000	0.000
15	A	89	GLU	-1	-0.928	-0.982	28.666	-0.213	-0.213	0.000	0.000	0.000	0.000
16	A	90	VAL	0	0.027	0.030	24.011	0.009	0.009	0.000	0.000	0.000	0.000
17	A	91	PHE	0	-0.034	-0.016	22.768	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	92	ILE	0	0.033	0.032	17.205	0.009	0.009	0.000	0.000	0.000	0.000
19	A	93	SER	0	-0.029	-0.018	18.173	0.037	0.037	0.000	0.000	0.000	0.000
20	A	94	GLY	0	0.100	0.019	16.144	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	95	SER	0	-0.015	0.011	13.053	0.033	0.033	0.000	0.000	0.000	0.000
22	A	96	PHE	0	0.018	0.028	10.447	0.099	0.099	0.000	0.000	0.000	0.000
23	A	97	ASN	0	0.000	-0.001	11.228	0.179	0.179	0.000	0.000	0.000	0.000
24	A	98	ASN	0	-0.021	-0.003	13.858	0.018	0.018	0.000	0.000	0.000	0.000
25	A	99	TRP	0	-0.016	0.003	16.183	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	100	SER	0	-0.053	-0.029	16.789	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	101	THR	0	-0.010	-0.021	18.268	0.005	0.005	0.000	0.000	0.000	0.000
28	A	102	LYS	1	0.906	0.967	19.039	0.133	0.133	0.000	0.000	0.000	0.000
29	A	103	ILE	0	0.005	-0.001	15.241	0.030	0.030	0.000	0.000	0.000	0.000
30	A	104	PRO	0	0.027	0.009	19.525	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	105	LEU	0	-0.023	-0.005	20.309	-0.053	-0.053	0.000	0.000	0.000	0.000
32	A	106	ILE	0	-0.021	-0.013	21.264	0.061	0.061	0.000	0.000	0.000	0.000
33	A	107	LYS	1	0.923	0.975	23.751	0.250	0.250	0.000	0.000	0.000	0.000
34	A	108	SER	0	-0.091	-0.068	24.920	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	109	HIS	0	0.003	0.009	26.930	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	110	ASN	0	-0.026	-0.010	29.409	0.003	0.003	0.000	0.000	0.000	0.000
37	A	111	ASP	-1	-0.766	-0.860	25.004	-0.448	-0.448	0.000	0.000	0.000	0.000
38	A	112	PHE	0	-0.044	-0.016	24.352	0.023	0.023	0.000	0.000	0.000	0.000
39	A	113	VAL	0	0.016	0.008	18.874	-0.036	-0.036	0.000	0.000	0.000	0.000
40	A	114	ALA	0	0.016	0.012	17.397	0.056	0.056	0.000	0.000	0.000	0.000
41	A	115	ILE	0	-0.010	-0.010	12.037	-0.068	-0.068	0.000	0.000	0.000	0.000
42	A	116	LEU	0	-0.045	-0.038	12.074	0.120	0.120	0.000	0.000	0.000	0.000
43	A	117	ASP	-1	-0.872	-0.937	7.466	-2.649	-2.649	0.000	0.000	0.000	0.000
44	A	118	LEU	0	-0.053	-0.036	7.837	0.701	0.701	0.000	0.000	0.000	0.000
45	A	119	PRO	0	-0.011	-0.006	3.407	-2.166	-1.695	0.012	-0.223	-0.261	0.001
46	A	120	GLU	-1	-0.839	-0.938	3.871	-0.200	0.184	-0.001	-0.034	-0.348	0.000
47	A	121	GLY	0	-0.007	0.007	5.855	0.837	0.837	0.000	0.000	0.000	0.000
48	A	122	GLU	-1	-0.937	-0.959	8.899	-0.759	-0.759	0.000	0.000	0.000	0.000
49	A	123	HIS	0	-0.002	-0.014	7.778	0.480	0.480	0.000	0.000	0.000	0.000
50	A	124	GLN	0	0.036	0.029	12.878	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	125	TYR	0	-0.016	-0.020	16.106	0.003	0.003	0.000	0.000	0.000	0.000
52	A	126	LYS	1	0.884	0.958	18.108	0.249	0.249	0.000	0.000	0.000	0.000
53	A	127	PHE	0	0.073	0.025	20.601	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	128	PHE	0	-0.077	-0.019	23.672	0.039	0.039	0.000	0.000	0.000	0.000
55	A	129	VAL	0	0.039	0.006	26.268	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	130	ASP	-1	-0.795	-0.887	29.031	-0.205	-0.205	0.000	0.000	0.000	0.000
57	A	131	GLY	0	-0.004	-0.006	30.846	0.015	0.015	0.000	0.000	0.000	0.000
58	A	132	GLN	0	-0.042	-0.021	30.890	0.017	0.017	0.000	0.000	0.000	0.000
59	A	133	TRP	0	-0.026	-0.016	22.505	-0.020	-0.020	0.000	0.000	0.000	0.000
60	A	134	VAL	0	-0.041	-0.024	26.664	0.016	0.016	0.000	0.000	0.000	0.000
61	A	135	HIS	0	-0.019	-0.019	24.431	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	136	ASP	-1	-0.814	-0.924	22.925	-0.452	-0.452	0.000	0.000	0.000	0.000
63	A	137	PRO	0	-0.045	-0.023	25.171	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	138	SER	0	-0.037	-0.017	24.568	0.003	0.003	0.000	0.000	0.000	0.000
65	A	139	GLU	-1	-0.926	-0.950	19.458	-0.720	-0.720	0.000	0.000	0.000	0.000
66	A	140	PRO	0	-0.021	-0.006	19.941	0.064	0.064	0.000	0.000	0.000	0.000
67	A	141	VAL	0	-0.013	-0.015	21.709	-0.015	-0.015	0.000	0.000	0.000	0.000
68	A	142	VAL	0	-0.007	-0.001	19.577	0.018	0.018	0.000	0.000	0.000	0.000
69	A	143	THR	0	-0.002	-0.005	22.728	0.005	0.005	0.000	0.000	0.000	0.000
70	A	144	SER	0	-0.045	-0.044	21.659	0.020	0.020	0.000	0.000	0.000	0.000
71	A	145	GLN	0	0.051	0.007	21.538	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	146	LEU	0	-0.036	-0.026	23.512	0.013	0.013	0.000	0.000	0.000	0.000
73	A	147	GLY	0	0.014	0.024	25.904	0.002	0.002	0.000	0.000	0.000	0.000
74	A	148	THR	0	-0.047	0.009	23.757	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	149	ILE	0	0.048	0.035	25.198	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	150	ASN	0	-0.054	-0.057	20.207	0.001	0.001	0.000	0.000	0.000	0.000
77	A	151	ASN	0	0.058	0.033	20.097	0.020	0.020	0.000	0.000	0.000	0.000
78	A	152	LEU	0	-0.025	-0.011	15.886	0.026	0.026	0.000	0.000	0.000	0.000
79	A	153	ILE	0	0.008	0.012	12.786	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	154	HIS	0	-0.013	-0.017	11.212	-0.118	-0.118	0.000	0.000	0.000	0.000
81	A	155	VAL	0	-0.035	-0.013	6.693	-0.053	-0.053	0.000	0.000	0.000	0.000
82	A	156	LYS	1	0.985	0.985	7.926	1.739	1.739	0.000	0.000	0.000	0.000
83	A	157	LYS	1	1.020	1.044	4.538	-2.079	-1.998	-0.001	-0.007	-0.072	0.000
84	A	158	SER	0	-0.003	-0.012	1.764	0.691	-19.291	29.234	-5.217	-4.035	-0.024
85	A	159	ASP	-1	-0.917	-0.958	3.366	7.531	8.432	0.045	-0.102	-0.844	-0.001
86	A	160	PHE	0	-0.056	-0.042	4.841	-0.975	-0.929	-0.001	-0.004	-0.042	0.000
87	A	161	GLU	-1	-0.839	-0.936	6.096	-3.404	-3.404	0.000	0.000	0.000	0.000
88	A	162	VAL	0	-0.051	-0.003	7.879	-0.101	-0.101	0.000	0.000	0.000	0.000
89	A	163	PHE	0	-0.048	-0.007	9.855	-0.029	-0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:75:GLN)