FMO DATABASE

FMODB ID: YZLG2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-608602.338316
FMO2-HF: Nuclear repulsion	573889.768484
FMO2-HF: Total energy	-34712.569832
FMO2-MP2: Total energy	-34817.134187

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.
-23.261	-23.978	17.935	-9.15	-8.064	0.025

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 : 0.002 / 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	77	ARG	1	0.811	0.868	2.960	-2.582	1.046	0.589	-1.928	-2.288	-0.005
4	A	78	PRO	0	0.020	0.019	4.642	0.650	0.759	-0.001	-0.018	-0.091	0.000
5	A	79	THR	0	-0.036	-0.012	7.672	0.143	0.143	0.000	0.000	0.000	0.000
6	A	80	VAL	0	-0.030	-0.019	9.921	0.164	0.164	0.000	0.000	0.000	0.000
7	A	81	ILE	0	0.000	0.005	13.394	-0.047	-0.047	0.000	0.000	0.000	0.000
8	A	82	ARG	1	0.828	0.869	16.230	0.396	0.396	0.000	0.000	0.000	0.000
9	A	83	TRP	0	0.022	-0.004	19.842	-0.031	-0.031	0.000	0.000	0.000	0.000
10	A	84	SER	0	0.008	-0.019	23.278	0.016	0.016	0.000	0.000	0.000	0.000
11	A	85	GLU	-1	-0.907	-0.931	25.932	-0.254	-0.254	0.000	0.000	0.000	0.000
12	A	86	GLY	0	-0.006	0.016	28.224	0.021	0.021	0.000	0.000	0.000	0.000
13	A	87	GLY	0	0.040	0.028	29.559	-0.014	-0.014	0.000	0.000	0.000	0.000
14	A	88	LYS	1	0.784	0.873	31.171	0.194	0.194	0.000	0.000	0.000	0.000
15	A	89	GLU	-1	-0.944	-0.988	28.172	-0.227	-0.227	0.000	0.000	0.000	0.000
16	A	90	VAL	0	0.042	0.031	23.264	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	91	PHE	0	-0.011	-0.011	22.263	0.000	0.000	0.000	0.000	0.000	0.000
18	A	92	ILE	0	0.028	0.026	16.269	0.011	0.011	0.000	0.000	0.000	0.000
19	A	93	SER	0	-0.035	-0.037	18.344	0.008	0.008	0.000	0.000	0.000	0.000
20	A	94	GLY	0	0.105	0.022	16.348	-0.014	-0.014	0.000	0.000	0.000	0.000
21	A	95	SER	0	-0.007	0.014	12.928	0.047	0.047	0.000	0.000	0.000	0.000
22	A	96	PHE	0	0.019	0.024	10.902	0.054	0.054	0.000	0.000	0.000	0.000
23	A	97	ASN	0	-0.007	-0.010	11.447	0.055	0.055	0.000	0.000	0.000	0.000
24	A	98	ASN	0	-0.039	-0.017	13.691	0.078	0.078	0.000	0.000	0.000	0.000
25	A	99	TRP	0	-0.003	0.009	16.340	0.048	0.048	0.000	0.000	0.000	0.000
26	A	100	SER	0	-0.040	-0.013	17.257	0.047	0.047	0.000	0.000	0.000	0.000
27	A	101	THR	0	-0.008	-0.016	18.752	0.049	0.049	0.000	0.000	0.000	0.000
28	A	102	LYS	1	0.837	0.970	19.515	0.254	0.254	0.000	0.000	0.000	0.000
29	A	103	ILE	0	0.023	0.013	15.681	0.048	0.048	0.000	0.000	0.000	0.000
30	A	104	PRO	0	0.002	-0.010	19.762	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	105	LEU	0	-0.006	0.004	19.318	-0.048	-0.048	0.000	0.000	0.000	0.000
32	A	106	ILE	0	-0.025	-0.012	21.190	0.049	0.049	0.000	0.000	0.000	0.000
33	A	107	LYS	1	0.912	0.969	23.544	0.205	0.205	0.000	0.000	0.000	0.000
34	A	108	SER	0	-0.042	-0.047	25.152	0.020	0.020	0.000	0.000	0.000	0.000
35	A	109	HIS	0	-0.002	0.004	27.156	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	110	ASN	0	-0.031	-0.017	29.479	0.006	0.006	0.000	0.000	0.000	0.000
37	A	111	ASP	-1	-0.743	-0.836	24.123	-0.313	-0.313	0.000	0.000	0.000	0.000
38	A	112	PHE	0	-0.032	-0.013	23.920	0.023	0.023	0.000	0.000	0.000	0.000
39	A	113	VAL	0	0.011	0.007	19.368	-0.032	-0.032	0.000	0.000	0.000	0.000
40	A	114	ALA	0	0.007	-0.003	16.978	0.039	0.039	0.000	0.000	0.000	0.000
41	A	115	ILE	0	-0.001	-0.003	11.714	-0.013	-0.013	0.000	0.000	0.000	0.000
42	A	116	LEU	0	-0.012	-0.002	11.570	0.122	0.122	0.000	0.000	0.000	0.000
43	A	117	ASP	-1	-0.872	-0.942	7.608	-2.193	-2.193	0.000	0.000	0.000	0.000
44	A	118	LEU	0	-0.017	-0.003	7.347	0.220	0.220	0.000	0.000	0.000	0.000
45	A	119	PRO	0	-0.011	-0.006	3.917	-2.454	-2.079	0.003	-0.163	-0.215	0.000
46	A	120	GLU	-1	-0.887	-0.954	3.585	-2.076	-1.382	0.002	-0.116	-0.579	0.000
47	A	121	GLY	0	-0.007	0.009	5.130	1.062	1.124	-0.001	-0.003	-0.057	0.000
48	A	122	GLU	-1	-0.896	-0.930	8.793	-1.014	-1.014	0.000	0.000	0.000	0.000
49	A	123	HIS	0	-0.023	-0.021	7.822	0.649	0.649	0.000	0.000	0.000	0.000
50	A	124	GLN	0	0.043	0.022	13.105	0.134	0.134	0.000	0.000	0.000	0.000
51	A	125	TYR	0	-0.015	-0.022	16.027	-0.046	-0.046	0.000	0.000	0.000	0.000
52	A	126	LYS	1	0.825	0.915	18.136	0.445	0.445	0.000	0.000	0.000	0.000
53	A	127	PHE	0	0.066	0.028	19.763	-0.031	-0.031	0.000	0.000	0.000	0.000
54	A	128	PHE	0	-0.053	-0.022	23.047	0.034	0.034	0.000	0.000	0.000	0.000
55	A	129	VAL	0	0.056	0.009	25.931	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	130	ASP	-1	-0.799	-0.889	28.314	-0.208	-0.208	0.000	0.000	0.000	0.000
57	A	131	GLY	0	0.020	0.016	30.687	0.016	0.016	0.000	0.000	0.000	0.000
58	A	132	GLN	0	-0.075	-0.043	30.701	0.011	0.011	0.000	0.000	0.000	0.000
59	A	133	TRP	0	-0.002	0.002	22.729	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	134	VAL	0	-0.019	-0.007	26.357	0.014	0.014	0.000	0.000	0.000	0.000
61	A	135	HIS	0	0.005	-0.013	23.750	-0.040	-0.040	0.000	0.000	0.000	0.000
62	A	136	ASP	-1	-0.789	-0.882	22.238	-0.383	-0.383	0.000	0.000	0.000	0.000
63	A	137	PRO	0	-0.034	-0.019	24.242	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	138	SER	0	-0.086	-0.052	23.719	0.021	0.021	0.000	0.000	0.000	0.000
65	A	139	GLU	-1	-0.898	-0.949	18.268	-0.630	-0.630	0.000	0.000	0.000	0.000
66	A	140	PRO	0	-0.019	-0.004	18.100	0.041	0.041	0.000	0.000	0.000	0.000
67	A	141	VAL	0	-0.024	-0.018	20.635	-0.036	-0.036	0.000	0.000	0.000	0.000
68	A	142	VAL	0	-0.022	-0.006	19.663	0.012	0.012	0.000	0.000	0.000	0.000
69	A	143	THR	0	-0.001	0.007	22.987	0.005	0.005	0.000	0.000	0.000	0.000
70	A	144	SER	0	-0.008	-0.012	21.946	-0.016	-0.016	0.000	0.000	0.000	0.000
71	A	145	GLN	0	0.012	-0.014	21.534	0.023	0.023	0.000	0.000	0.000	0.000
72	A	146	LEU	0	-0.019	-0.006	23.233	0.027	0.027	0.000	0.000	0.000	0.000
73	A	147	GLY	0	-0.004	0.004	26.264	0.019	0.019	0.000	0.000	0.000	0.000
74	A	148	THR	0	-0.044	-0.013	23.983	0.007	0.007	0.000	0.000	0.000	0.000
75	A	149	ILE	0	0.025	0.018	25.009	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	150	ASN	0	-0.015	0.005	20.699	0.042	0.042	0.000	0.000	0.000	0.000
77	A	151	ASN	0	0.046	0.016	19.288	0.035	0.035	0.000	0.000	0.000	0.000
78	A	152	LEU	0	-0.042	-0.023	15.819	-0.024	-0.024	0.000	0.000	0.000	0.000
79	A	153	ILE	0	0.021	0.018	11.839	0.043	0.043	0.000	0.000	0.000	0.000
80	A	154	HIS	0	-0.059	-0.047	10.176	-0.236	-0.236	0.000	0.000	0.000	0.000
81	A	155	VAL	0	-0.029	-0.009	5.220	0.340	0.340	0.000	0.000	0.000	0.000
82	A	156	LYS	1	0.984	0.981	6.756	0.035	0.035	0.000	0.000	0.000	0.000
83	A	157	LYS	1	0.912	0.967	3.427	-2.067	-1.854	0.005	-0.069	-0.148	0.000
84	A	158	SER	0	0.016	-0.023	1.772	-16.487	-22.711	17.338	-6.795	-4.318	0.030
85	A	159	ASP	-1	-0.854	-0.910	4.074	4.290	4.716	0.001	-0.058	-0.369	0.000
86	A	160	PHE	0	-0.044	-0.035	5.393	-1.376	-1.376	-0.001	0.000	0.001	0.000
87	A	161	GLU	-1	-0.788	-0.866	6.417	0.404	0.404	0.000	0.000	0.000	0.000
88	A	162	VAL	0	-0.048	-0.012	6.999	-0.464	-0.464	0.000	0.000	0.000	0.000
89	A	163	PHE	0	-0.054	-0.012	9.474	-0.488	-0.488	0.000	0.000	0.000	0.000

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