FMO DATABASE

FMODB ID: M8M1Z

Calculation Name: 2V8Q-B-Xray547

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

Target Type: SINGLE PROTEIN

Ligand Name: adenosine monophosphate

Ligand 3-letter code: AMP

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2V8Q

Chain ID: B

ChEMBL ID: CHEMBL2117

UniProt ID: O43741

Base Structure: X-ray

Registration Date: 2025-10-04

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	83
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-449272.642043
FMO2-HF: Nuclear repulsion	415627.333807
FMO2-HF: Total energy	-33645.308236
FMO2-MP2: Total energy	-33742.323123

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:190:GLY)

Summations of interaction energy for fragment #1(A:190:GLY)

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.
-8.263	-7.161	-0.01	-0.455	-0.637	-0.002

Interaction energy analysis for fragmet #1(A:190:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.828 / q_NPA : 0.897

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	192	GLU	-1	-0.772	-0.853	3.817	-40.372	-39.270	-0.010	-0.455	-0.637	-0.002
4	A	193	MET	0	-0.027	-0.025	6.030	2.199	2.199	0.000	0.000	0.000	0.000
5	A	194	TYR	0	-0.039	-0.035	9.227	3.374	3.374	0.000	0.000	0.000	0.000
6	A	195	ALA	0	-0.018	-0.011	12.755	0.621	0.621	0.000	0.000	0.000	0.000
7	A	196	PHE	0	0.025	0.012	14.324	0.924	0.924	0.000	0.000	0.000	0.000
8	A	197	ARG	1	0.940	0.961	18.142	16.251	16.251	0.000	0.000	0.000	0.000
9	A	198	SER	0	-0.002	-0.010	21.842	0.260	0.260	0.000	0.000	0.000	0.000
10	A	199	GLU	-1	-0.953	-0.964	25.153	-11.746	-11.746	0.000	0.000	0.000	0.000
11	A	200	GLU	-1	-0.858	-0.933	26.891	-10.350	-10.350	0.000	0.000	0.000	0.000
12	A	201	ARG	1	0.891	0.936	27.968	10.666	10.666	0.000	0.000	0.000	0.000
13	A	202	PHE	0	-0.036	-0.026	30.398	0.269	0.269	0.000	0.000	0.000	0.000
14	A	203	LYS	1	0.984	1.011	33.203	9.331	9.331	0.000	0.000	0.000	0.000
15	A	204	SER	0	-0.015	-0.001	34.355	0.078	0.078	0.000	0.000	0.000	0.000
16	A	205	PRO	0	0.004	-0.004	37.415	-0.117	-0.117	0.000	0.000	0.000	0.000
17	A	206	PRO	0	-0.001	0.011	39.031	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	207	ILE	0	0.016	0.000	40.726	0.158	0.158	0.000	0.000	0.000	0.000
19	A	208	LEU	0	-0.004	-0.003	43.968	-0.016	-0.016	0.000	0.000	0.000	0.000
20	A	209	PRO	0	0.003	0.007	46.638	-0.037	-0.037	0.000	0.000	0.000	0.000
21	A	210	PRO	0	0.001	0.004	46.154	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	211	HIS	0	-0.014	-0.028	47.993	0.003	0.003	0.000	0.000	0.000	0.000
23	A	212	LEU	0	0.015	0.026	48.049	0.109	0.109	0.000	0.000	0.000	0.000
24	A	213	LEU	0	-0.001	-0.002	51.790	-0.032	-0.032	0.000	0.000	0.000	0.000
25	A	214	GLN	0	-0.012	-0.017	51.512	0.053	0.053	0.000	0.000	0.000	0.000
26	A	215	VAL	0	0.002	0.001	54.573	0.028	0.028	0.000	0.000	0.000	0.000
27	A	216	ILE	0	-0.007	0.003	57.780	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	217	LEU	0	-0.014	-0.006	60.885	0.031	0.031	0.000	0.000	0.000	0.000
29	A	218	ASN	0	0.019	0.007	64.483	0.008	0.008	0.000	0.000	0.000	0.000
30	A	219	LYS	1	0.836	0.895	67.026	4.361	4.361	0.000	0.000	0.000	0.000
31	A	220	ASP	-1	-0.799	-0.891	70.765	-4.298	-4.298	0.000	0.000	0.000	0.000
32	A	221	THR	0	-0.019	-0.007	73.314	0.011	0.011	0.000	0.000	0.000	0.000
33	A	222	ASN	0	0.005	-0.002	75.462	0.061	0.061	0.000	0.000	0.000	0.000
34	A	223	ILE	0	0.039	0.023	77.139	-0.029	-0.029	0.000	0.000	0.000	0.000
35	A	224	SER	0	-0.026	-0.004	78.270	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	225	CYS	0	-0.059	-0.046	75.723	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	226	ASP	-1	-0.851	-0.923	69.488	-4.658	-4.658	0.000	0.000	0.000	0.000
38	A	227	PRO	0	-0.055	-0.007	70.295	-0.029	-0.029	0.000	0.000	0.000	0.000
39	A	228	ALA	0	0.003	-0.017	64.737	-0.041	-0.041	0.000	0.000	0.000	0.000
40	A	229	LEU	0	-0.041	0.003	66.375	0.001	0.001	0.000	0.000	0.000	0.000
41	A	230	LEU	0	0.001	-0.008	60.469	-0.078	-0.078	0.000	0.000	0.000	0.000
42	A	231	PRO	0	-0.027	-0.006	61.074	0.078	0.078	0.000	0.000	0.000	0.000
43	A	232	GLU	-1	-0.814	-0.903	61.749	-5.293	-5.293	0.000	0.000	0.000	0.000
44	A	233	PRO	0	0.008	-0.002	62.113	-0.063	-0.063	0.000	0.000	0.000	0.000
45	A	234	ASN	0	-0.030	-0.006	57.044	-0.121	-0.121	0.000	0.000	0.000	0.000
46	A	235	HIS	0	-0.039	-0.048	56.381	-0.180	-0.180	0.000	0.000	0.000	0.000
47	A	236	VAL	0	-0.085	-0.041	51.342	-0.016	-0.016	0.000	0.000	0.000	0.000
48	A	237	MET	0	0.024	0.025	52.662	-0.077	-0.077	0.000	0.000	0.000	0.000
49	A	238	LEU	0	-0.027	-0.021	54.296	0.068	0.068	0.000	0.000	0.000	0.000
50	A	239	ASN	0	-0.042	-0.043	51.878	-0.023	-0.023	0.000	0.000	0.000	0.000
51	A	240	HIS	0	-0.005	0.017	48.294	-0.066	-0.066	0.000	0.000	0.000	0.000
52	A	241	LEU	0	-0.047	-0.019	52.308	0.125	0.125	0.000	0.000	0.000	0.000
53	A	242	TYR	0	0.007	0.007	53.901	-0.063	-0.063	0.000	0.000	0.000	0.000
54	A	243	ALA	0	-0.002	-0.017	56.721	0.026	0.026	0.000	0.000	0.000	0.000
55	A	244	LEU	0	-0.011	0.009	58.984	0.011	0.011	0.000	0.000	0.000	0.000
56	A	245	SER	0	-0.005	-0.014	60.727	-0.086	-0.086	0.000	0.000	0.000	0.000
57	A	246	ILE	0	-0.013	0.005	58.407	0.078	0.078	0.000	0.000	0.000	0.000
58	A	247	LYS	1	0.891	0.941	62.354	4.644	4.644	0.000	0.000	0.000	0.000
59	A	248	ASP	-1	-0.851	-0.929	66.086	-4.605	-4.605	0.000	0.000	0.000	0.000
60	A	249	SER	0	-0.013	-0.004	64.979	0.014	0.014	0.000	0.000	0.000	0.000
61	A	250	VAL	0	-0.018	-0.001	64.847	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	251	MET	0	-0.006	-0.005	58.699	-0.087	-0.087	0.000	0.000	0.000	0.000
63	A	252	VAL	0	0.014	0.003	62.167	0.067	0.067	0.000	0.000	0.000	0.000
64	A	253	LEU	0	0.007	0.011	57.012	-0.073	-0.073	0.000	0.000	0.000	0.000
65	A	254	SER	0	-0.026	-0.040	58.858	0.110	0.110	0.000	0.000	0.000	0.000
66	A	255	ALA	0	0.077	0.041	56.302	-0.112	-0.112	0.000	0.000	0.000	0.000
67	A	256	THR	0	-0.003	0.019	57.711	0.139	0.139	0.000	0.000	0.000	0.000
68	A	257	HIS	0	0.043	0.038	55.680	-0.198	-0.198	0.000	0.000	0.000	0.000
69	A	258	ARG	1	0.908	0.944	55.682	5.689	5.689	0.000	0.000	0.000	0.000
70	A	259	TYR	0	0.048	0.022	58.966	-0.026	-0.026	0.000	0.000	0.000	0.000
71	A	260	LYS	1	0.942	0.967	60.601	5.040	5.040	0.000	0.000	0.000	0.000
72	A	261	LYS	1	0.979	0.985	60.757	5.022	5.022	0.000	0.000	0.000	0.000
73	A	262	LYS	1	0.961	0.993	63.280	4.746	4.746	0.000	0.000	0.000	0.000
74	A	263	TYR	0	0.050	0.011	58.702	-0.126	-0.126	0.000	0.000	0.000	0.000
75	A	264	VAL	0	0.021	0.010	62.203	0.093	0.093	0.000	0.000	0.000	0.000
76	A	265	THR	0	0.029	0.007	61.881	-0.078	-0.078	0.000	0.000	0.000	0.000
77	A	266	THR	0	-0.020	-0.001	61.243	0.097	0.097	0.000	0.000	0.000	0.000
78	A	267	LEU	0	0.029	0.021	61.973	-0.079	-0.079	0.000	0.000	0.000	0.000
79	A	268	LEU	0	-0.038	-0.017	60.115	0.055	0.055	0.000	0.000	0.000	0.000
80	A	269	TYR	0	0.030	0.017	62.934	-0.053	-0.053	0.000	0.000	0.000	0.000
81	A	270	LYS	1	0.924	0.958	58.095	5.499	5.499	0.000	0.000	0.000	0.000
82	A	271	PRO	0	0.039	0.015	63.431	-0.028	-0.028	0.000	0.000	0.000	0.000
83	A	272	ILE	-1	-0.935	-0.952	59.320	-5.343	-5.343	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:190:GLY)