FMO DATABASE

FMODB ID: 52M6Z

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	OptHSide
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	-609602.77411
FMO2-HF: Nuclear repulsion	574890.559163
FMO2-HF: Total energy	-34712.214947
FMO2-MP2: Total energy	-34816.846578

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.
-17.355	-14.478	9.337	-5.586	-6.629	0.012

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 : -0.015 / q_NPA : -0.026

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	77	ARG	1	0.812	0.883	3.570	1.234	3.654	0.036	-1.065	-1.392	0.001
4	A	78	PRO	0	0.090	0.053	5.150	0.528	0.597	-0.001	-0.004	-0.064	0.000
5	A	79	THR	0	-0.044	-0.010	8.373	-0.040	-0.040	0.000	0.000	0.000	0.000
6	A	80	VAL	0	-0.008	0.004	10.670	0.158	0.158	0.000	0.000	0.000	0.000
7	A	81	ILE	0	-0.006	-0.003	13.716	-0.026	-0.026	0.000	0.000	0.000	0.000
8	A	82	ARG	1	0.829	0.865	16.675	0.376	0.376	0.000	0.000	0.000	0.000
9	A	83	TRP	0	0.003	-0.002	20.303	-0.012	-0.012	0.000	0.000	0.000	0.000
10	A	84	SER	0	0.006	-0.012	23.325	0.018	0.018	0.000	0.000	0.000	0.000
11	A	85	GLU	-1	-0.896	-0.941	26.187	-0.256	-0.256	0.000	0.000	0.000	0.000
12	A	86	GLY	0	-0.055	-0.014	28.528	0.018	0.018	0.000	0.000	0.000	0.000
13	A	87	GLY	0	0.062	0.040	29.951	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	88	LYS	1	0.828	0.888	31.320	0.166	0.166	0.000	0.000	0.000	0.000
15	A	89	GLU	-1	-0.930	-0.981	28.309	-0.203	-0.203	0.000	0.000	0.000	0.000
16	A	90	VAL	0	0.041	0.035	23.278	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	91	PHE	0	-0.030	-0.023	22.528	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	92	ILE	0	0.036	0.038	16.590	0.003	0.003	0.000	0.000	0.000	0.000
19	A	93	SER	0	-0.032	-0.033	18.282	0.021	0.021	0.000	0.000	0.000	0.000
20	A	94	GLY	0	0.095	0.014	16.249	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	95	SER	0	-0.020	0.010	13.122	0.043	0.043	0.000	0.000	0.000	0.000
22	A	96	PHE	0	0.023	0.030	10.593	0.050	0.050	0.000	0.000	0.000	0.000
23	A	97	ASN	0	-0.001	-0.005	11.331	0.105	0.105	0.000	0.000	0.000	0.000
24	A	98	ASN	0	-0.031	-0.010	13.778	0.051	0.051	0.000	0.000	0.000	0.000
25	A	99	TRP	0	-0.012	0.008	16.277	0.034	0.034	0.000	0.000	0.000	0.000
26	A	100	SER	0	-0.033	-0.015	16.848	0.045	0.045	0.000	0.000	0.000	0.000
27	A	101	THR	0	-0.014	-0.020	18.283	0.044	0.044	0.000	0.000	0.000	0.000
28	A	102	LYS	1	0.869	0.967	19.087	0.207	0.207	0.000	0.000	0.000	0.000
29	A	103	ILE	0	0.025	0.011	15.103	0.037	0.037	0.000	0.000	0.000	0.000
30	A	104	PRO	0	0.013	-0.001	19.543	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	105	LEU	0	-0.018	-0.003	19.346	-0.037	-0.037	0.000	0.000	0.000	0.000
32	A	106	ILE	0	-0.029	-0.019	21.299	0.046	0.046	0.000	0.000	0.000	0.000
33	A	107	LYS	1	0.893	0.956	23.696	0.188	0.188	0.000	0.000	0.000	0.000
34	A	108	SER	0	-0.059	-0.056	25.075	0.015	0.015	0.000	0.000	0.000	0.000
35	A	109	HIS	0	-0.005	0.004	27.067	-0.007	-0.007	0.000	0.000	0.000	0.000
36	A	110	ASN	0	-0.022	-0.011	29.439	0.004	0.004	0.000	0.000	0.000	0.000
37	A	111	ASP	-1	-0.752	-0.836	24.818	-0.299	-0.299	0.000	0.000	0.000	0.000
38	A	112	PHE	0	-0.023	-0.003	24.067	0.024	0.024	0.000	0.000	0.000	0.000
39	A	113	VAL	0	0.024	0.012	19.577	-0.034	-0.034	0.000	0.000	0.000	0.000
40	A	114	ALA	0	0.017	0.009	17.050	0.039	0.039	0.000	0.000	0.000	0.000
41	A	115	ILE	0	-0.015	-0.010	12.122	-0.033	-0.033	0.000	0.000	0.000	0.000
42	A	116	LEU	0	-0.041	-0.034	11.637	0.079	0.079	0.000	0.000	0.000	0.000
43	A	117	ASP	-1	-0.879	-0.944	7.506	-1.915	-1.915	0.000	0.000	0.000	0.000
44	A	118	LEU	0	-0.055	-0.030	7.175	0.393	0.393	0.000	0.000	0.000	0.000
45	A	119	PRO	0	-0.017	-0.008	3.434	-2.585	-1.927	0.021	-0.306	-0.373	0.001
46	A	120	GLU	-1	-0.889	-0.952	3.622	-1.898	-1.352	0.000	-0.072	-0.475	0.000
47	A	121	GLY	0	0.008	0.010	5.308	0.879	0.926	-0.001	-0.002	-0.043	0.000
48	A	122	GLU	-1	-0.885	-0.919	8.943	-0.999	-0.999	0.000	0.000	0.000	0.000
49	A	123	HIS	0	-0.016	-0.015	7.759	0.586	0.586	0.000	0.000	0.000	0.000
50	A	124	GLN	0	0.027	0.015	12.965	0.127	0.127	0.000	0.000	0.000	0.000
51	A	125	TYR	0	-0.010	-0.022	16.119	-0.033	-0.033	0.000	0.000	0.000	0.000
52	A	126	LYS	1	0.836	0.914	18.212	0.399	0.399	0.000	0.000	0.000	0.000
53	A	127	PHE	0	0.077	0.030	19.836	-0.022	-0.022	0.000	0.000	0.000	0.000
54	A	128	PHE	0	-0.048	-0.009	23.323	0.033	0.033	0.000	0.000	0.000	0.000
55	A	129	VAL	0	0.041	0.005	26.111	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	130	ASP	-1	-0.790	-0.878	28.474	-0.190	-0.190	0.000	0.000	0.000	0.000
57	A	131	GLY	0	0.007	0.002	30.587	0.012	0.012	0.000	0.000	0.000	0.000
58	A	132	GLN	0	-0.063	-0.028	30.690	0.011	0.011	0.000	0.000	0.000	0.000
59	A	133	TRP	0	-0.018	-0.008	22.731	-0.019	-0.019	0.000	0.000	0.000	0.000
60	A	134	VAL	0	-0.028	-0.021	26.489	0.013	0.013	0.000	0.000	0.000	0.000
61	A	135	HIS	0	0.001	-0.012	24.046	-0.030	-0.030	0.000	0.000	0.000	0.000
62	A	136	ASP	-1	-0.799	-0.890	22.366	-0.376	-0.376	0.000	0.000	0.000	0.000
63	A	137	PRO	0	-0.044	-0.025	24.288	-0.020	-0.020	0.000	0.000	0.000	0.000
64	A	138	SER	0	-0.040	-0.036	23.962	0.009	0.009	0.000	0.000	0.000	0.000
65	A	139	GLU	-1	-0.919	-0.955	18.886	-0.619	-0.619	0.000	0.000	0.000	0.000
66	A	140	PRO	0	-0.020	-0.003	18.855	0.041	0.041	0.000	0.000	0.000	0.000
67	A	141	VAL	0	-0.031	-0.025	21.020	-0.031	-0.031	0.000	0.000	0.000	0.000
68	A	142	VAL	0	-0.009	0.003	19.503	0.010	0.010	0.000	0.000	0.000	0.000
69	A	143	THR	0	0.003	-0.003	22.801	0.010	0.010	0.000	0.000	0.000	0.000
70	A	144	SER	0	-0.042	-0.036	21.936	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	145	GLN	0	0.043	0.004	21.586	0.018	0.018	0.000	0.000	0.000	0.000
72	A	146	LEU	0	-0.039	-0.026	23.206	0.025	0.025	0.000	0.000	0.000	0.000
73	A	147	GLY	0	0.017	0.025	25.971	0.019	0.019	0.000	0.000	0.000	0.000
74	A	148	THR	0	-0.057	-0.009	23.873	0.009	0.009	0.000	0.000	0.000	0.000
75	A	149	ILE	0	0.031	0.026	25.281	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	150	ASN	0	-0.024	-0.008	20.381	0.037	0.037	0.000	0.000	0.000	0.000
77	A	151	ASN	0	0.061	0.033	19.441	0.031	0.031	0.000	0.000	0.000	0.000
78	A	152	LEU	0	-0.030	-0.011	16.113	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	153	ILE	0	0.011	0.010	12.065	0.040	0.040	0.000	0.000	0.000	0.000
80	A	154	HIS	0	-0.064	-0.051	10.385	-0.238	-0.238	0.000	0.000	0.000	0.000
81	A	155	VAL	0	-0.031	-0.011	5.640	0.294	0.294	0.000	0.000	0.000	0.000
82	A	156	LYS	1	0.977	0.982	7.348	0.599	0.599	0.000	0.000	0.000	0.000
83	A	157	LYS	1	0.915	0.956	4.175	-2.006	-1.948	-0.001	-0.012	-0.045	0.000
84	A	158	SER	0	0.016	-0.004	2.019	-14.551	-15.936	9.284	-4.075	-3.824	0.010
85	A	159	ASP	-1	-0.852	-0.913	4.032	4.782	5.233	0.000	-0.050	-0.402	0.000
86	A	160	PHE	0	-0.046	-0.036	5.221	-1.537	-1.524	-0.001	0.000	-0.011	0.000
87	A	161	GLU	-1	-0.797	-0.884	6.650	-0.393	-0.393	0.000	0.000	0.000	0.000
88	A	162	VAL	0	-0.047	-0.006	7.490	-0.365	-0.365	0.000	0.000	0.000	0.000
89	A	163	PHE	0	-0.040	0.000	9.795	-0.397	-0.397	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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