FMO DATABASE

FMODB ID: MZK2Z

Calculation Name: 2F15-A-Xray549

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

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F15

Chain ID: A

ChEMBL ID: CHEMBL2117

UniProt ID: O43741

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	89
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-607535.9104
FMO2-HF: Nuclear repulsion	572823.536222
FMO2-HF: Total energy	-34712.374178
FMO2-MP2: Total energy	-34816.908957

3D Structure Molmil

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.
-113.089	-109.965	9.97	-6.022	-7.071	-0.067

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 : 1 / q_Mulliken : 0.794 / q_NPA : 0.883

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	0.841	0.889	2.170	19.597	23.736	2.467	-3.225	-3.380	-0.036
4	A	78	PRO	0	0.045	0.029	4.331	3.285	3.381	-0.001	-0.027	-0.069	0.000
45	A	119	PRO	0	-0.037	-0.027	3.552	-6.954	-6.640	0.002	-0.137	-0.179	0.000
46	A	120	GLU	-1	-0.882	-0.950	4.023	-30.327	-29.917	-0.001	-0.029	-0.379	0.000
83	A	157	LYS	1	0.894	0.951	4.545	23.618	23.721	-0.001	-0.007	-0.094	0.000
84	A	158	SER	0	0.044	0.020	1.881	-10.523	-12.851	7.506	-2.580	-2.598	-0.031
85	A	159	ASP	-1	-0.846	-0.909	3.917	-30.034	-29.618	-0.001	-0.016	-0.400	0.000
86	A	160	PHE	0	-0.050	-0.041	5.354	1.128	1.102	-0.001	-0.001	0.028	0.000
5	A	79	THR	0	-0.035	-0.009	7.953	1.203	1.203	0.000	0.000	0.000	0.000
6	A	80	VAL	0	-0.030	-0.018	10.138	0.878	0.878	0.000	0.000	0.000	0.000
7	A	81	ILE	0	0.002	0.008	13.843	0.068	0.068	0.000	0.000	0.000	0.000
8	A	82	ARG	1	0.831	0.878	16.466	13.343	13.343	0.000	0.000	0.000	0.000
9	A	83	TRP	0	0.017	0.004	20.060	-0.178	-0.178	0.000	0.000	0.000	0.000
10	A	84	SER	0	0.015	-0.011	23.501	0.065	0.065	0.000	0.000	0.000	0.000
11	A	85	GLU	-1	-0.897	-0.936	26.491	-10.725	-10.725	0.000	0.000	0.000	0.000
12	A	86	GLY	0	-0.017	0.008	28.831	0.399	0.399	0.000	0.000	0.000	0.000
13	A	87	GLY	0	0.058	0.035	29.830	-0.232	-0.232	0.000	0.000	0.000	0.000
14	A	88	LYS	1	0.782	0.871	31.499	9.454	9.454	0.000	0.000	0.000	0.000
15	A	89	GLU	-1	-0.915	-0.970	28.388	-11.047	-11.047	0.000	0.000	0.000	0.000
16	A	90	VAL	0	0.046	0.026	23.596	0.079	0.079	0.000	0.000	0.000	0.000
17	A	91	PHE	0	-0.029	-0.015	22.687	-0.370	-0.370	0.000	0.000	0.000	0.000
18	A	92	ILE	0	0.027	0.023	17.027	0.306	0.306	0.000	0.000	0.000	0.000
19	A	93	SER	0	-0.037	-0.037	18.069	-0.279	-0.279	0.000	0.000	0.000	0.000
20	A	94	GLY	0	0.102	0.019	16.224	0.370	0.370	0.000	0.000	0.000	0.000
21	A	95	SER	0	-0.007	0.012	13.087	0.145	0.145	0.000	0.000	0.000	0.000
22	A	96	PHE	0	0.016	0.022	10.570	-0.518	-0.518	0.000	0.000	0.000	0.000
23	A	97	ASN	0	-0.017	-0.014	10.796	-1.195	-1.195	0.000	0.000	0.000	0.000
24	A	98	ASN	0	-0.035	-0.015	13.110	1.355	1.355	0.000	0.000	0.000	0.000
25	A	99	TRP	0	-0.001	0.012	15.725	1.089	1.089	0.000	0.000	0.000	0.000
26	A	100	SER	0	-0.037	-0.012	16.344	0.990	0.990	0.000	0.000	0.000	0.000
27	A	101	THR	0	-0.013	-0.020	17.935	0.796	0.796	0.000	0.000	0.000	0.000
28	A	102	LYS	1	0.872	0.983	18.802	11.984	11.984	0.000	0.000	0.000	0.000
29	A	103	ILE	0	0.020	0.011	15.216	0.361	0.361	0.000	0.000	0.000	0.000
30	A	104	PRO	0	0.015	-0.001	19.727	0.172	0.172	0.000	0.000	0.000	0.000
31	A	105	LEU	0	-0.017	-0.003	19.786	-0.789	-0.789	0.000	0.000	0.000	0.000
32	A	106	ILE	0	-0.022	-0.009	20.748	0.788	0.788	0.000	0.000	0.000	0.000
33	A	107	LYS	1	0.884	0.948	23.137	10.479	10.479	0.000	0.000	0.000	0.000
34	A	108	SER	0	-0.055	-0.052	24.768	0.014	0.014	0.000	0.000	0.000	0.000
35	A	109	HIS	0	-0.005	0.002	26.823	0.020	0.020	0.000	0.000	0.000	0.000
36	A	110	ASN	0	-0.016	-0.009	28.957	0.077	0.077	0.000	0.000	0.000	0.000
37	A	111	ASP	-1	-0.750	-0.838	24.571	-11.874	-11.874	0.000	0.000	0.000	0.000
38	A	112	PHE	0	-0.044	-0.029	23.957	0.252	0.252	0.000	0.000	0.000	0.000
39	A	113	VAL	0	0.024	0.009	19.039	-0.301	-0.301	0.000	0.000	0.000	0.000
40	A	114	ALA	0	-0.004	-0.001	16.774	0.330	0.330	0.000	0.000	0.000	0.000
41	A	115	ILE	0	-0.010	-0.005	11.185	-0.151	-0.151	0.000	0.000	0.000	0.000
42	A	116	LEU	0	-0.009	0.000	11.645	0.365	0.365	0.000	0.000	0.000	0.000
43	A	117	ASP	-1	-0.871	-0.940	7.358	-34.684	-34.684	0.000	0.000	0.000	0.000
44	A	118	LEU	0	-0.015	-0.004	7.713	-1.812	-1.812	0.000	0.000	0.000	0.000
47	A	121	GLY	0	-0.007	0.009	5.956	-0.225	-0.225	0.000	0.000	0.000	0.000
48	A	122	GLU	-1	-0.888	-0.932	9.151	-19.576	-19.576	0.000	0.000	0.000	0.000
49	A	123	HIS	0	-0.024	-0.019	8.134	2.573	2.573	0.000	0.000	0.000	0.000
50	A	124	GLN	0	0.031	0.016	13.328	1.826	1.826	0.000	0.000	0.000	0.000
51	A	125	TYR	0	-0.007	-0.015	16.508	-0.884	-0.884	0.000	0.000	0.000	0.000
52	A	126	LYS	1	0.841	0.923	18.532	13.380	13.380	0.000	0.000	0.000	0.000
53	A	127	PHE	0	0.061	0.023	20.448	-0.622	-0.622	0.000	0.000	0.000	0.000
54	A	128	PHE	0	-0.045	-0.015	23.855	0.510	0.510	0.000	0.000	0.000	0.000
55	A	129	VAL	0	0.054	0.012	26.300	-0.219	-0.219	0.000	0.000	0.000	0.000
56	A	130	ASP	-1	-0.793	-0.881	28.897	-9.830	-9.830	0.000	0.000	0.000	0.000
57	A	131	GLY	0	0.020	0.016	31.030	0.338	0.338	0.000	0.000	0.000	0.000
58	A	132	GLN	0	-0.078	-0.042	31.107	0.301	0.301	0.000	0.000	0.000	0.000
59	A	133	TRP	0	-0.012	-0.007	22.688	-0.467	-0.467	0.000	0.000	0.000	0.000
60	A	134	VAL	0	-0.018	-0.004	27.047	0.276	0.276	0.000	0.000	0.000	0.000
61	A	135	HIS	0	-0.014	-0.020	24.870	-0.668	-0.668	0.000	0.000	0.000	0.000
62	A	136	ASP	-1	-0.782	-0.882	23.129	-12.701	-12.701	0.000	0.000	0.000	0.000
63	A	137	PRO	0	-0.043	-0.020	25.164	-0.216	-0.216	0.000	0.000	0.000	0.000
64	A	138	SER	0	-0.068	-0.045	24.710	0.204	0.204	0.000	0.000	0.000	0.000
65	A	139	GLU	-1	-0.903	-0.948	19.560	-15.788	-15.788	0.000	0.000	0.000	0.000
66	A	140	PRO	0	-0.020	-0.005	19.576	0.515	0.515	0.000	0.000	0.000	0.000
67	A	141	VAL	0	-0.016	-0.010	21.904	-0.433	-0.433	0.000	0.000	0.000	0.000
68	A	142	VAL	0	-0.020	-0.004	19.795	0.081	0.081	0.000	0.000	0.000	0.000
69	A	143	THR	0	-0.013	-0.006	23.100	0.377	0.377	0.000	0.000	0.000	0.000
70	A	144	SER	0	-0.017	-0.020	21.945	-0.317	-0.317	0.000	0.000	0.000	0.000
71	A	145	GLN	0	0.025	-0.006	21.829	0.538	0.538	0.000	0.000	0.000	0.000
72	A	146	LEU	0	-0.024	-0.010	23.272	0.418	0.418	0.000	0.000	0.000	0.000
73	A	147	GLY	0	0.004	0.011	26.236	0.454	0.454	0.000	0.000	0.000	0.000
74	A	148	THR	0	-0.050	-0.012	23.885	0.206	0.206	0.000	0.000	0.000	0.000
75	A	149	ILE	0	0.029	0.024	25.134	-0.374	-0.374	0.000	0.000	0.000	0.000
76	A	150	ASN	0	-0.016	-0.003	20.797	0.530	0.530	0.000	0.000	0.000	0.000
77	A	151	ASN	0	0.046	0.016	20.511	0.471	0.471	0.000	0.000	0.000	0.000
78	A	152	LEU	0	-0.035	-0.023	16.297	-0.493	-0.493	0.000	0.000	0.000	0.000
79	A	153	ILE	0	0.027	0.021	13.024	0.397	0.397	0.000	0.000	0.000	0.000
80	A	154	HIS	0	-0.064	-0.044	11.585	-2.439	-2.439	0.000	0.000	0.000	0.000
81	A	155	VAL	0	-0.031	-0.010	6.879	1.104	1.104	0.000	0.000	0.000	0.000
82	A	156	LYS	1	1.002	0.993	8.083	20.601	20.601	0.000	0.000	0.000	0.000
87	A	161	GLU	-1	-0.821	-0.892	6.361	-27.976	-27.976	0.000	0.000	0.000	0.000
88	A	162	VAL	0	-0.069	-0.032	7.862	0.029	0.029	0.000	0.000	0.000	0.000
89	A	163	PHE	-1	-0.966	-0.960	10.153	-16.007	-16.007	0.000	0.000	0.000	0.000

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