FMO DATABASE

FMODB ID: 3J75L

Calculation Name: 3AHP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3AHP

Chain ID: A

ChEMBL ID:

UniProt ID: E7FH74

Base Structure: X-ray

Registration Date: 2023-09-22

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	106
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-771126.739544
FMO2-HF: Nuclear repulsion	728529.225651
FMO2-HF: Total energy	-42597.513893
FMO2-MP2: Total energy	-42717.11335

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-113.557	-111.699	-0.012	-0.845	-1.001	0.003

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.974 / q_NPA : 0.975

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	5	GLU	-1	-0.754	-0.867	3.893	-28.688	-26.966	-0.012	-0.832	-0.878	0.003
4	A	6	GLN	0	-0.066	-0.040	6.833	2.280	2.280	0.000	0.000	0.000	0.000
5	A	7	LEU	0	-0.011	-0.010	5.742	-3.883	-3.883	0.000	0.000	0.000	0.000
6	A	8	LEU	0	-0.002	0.008	9.448	2.826	2.826	0.000	0.000	0.000	0.000
7	A	9	ILE	0	-0.013	-0.022	10.551	-2.286	-2.286	0.000	0.000	0.000	0.000
8	A	10	PHE	0	0.006	0.006	12.886	1.984	1.984	0.000	0.000	0.000	0.000
9	A	11	THR	0	-0.030	-0.034	15.311	-0.699	-0.699	0.000	0.000	0.000	0.000
10	A	12	THR	0	0.015	-0.006	18.035	0.572	0.572	0.000	0.000	0.000	0.000
11	A	13	CYS	0	-0.031	0.010	21.737	-0.111	-0.111	0.000	0.000	0.000	0.000
12	A	14	PRO	0	0.048	0.024	24.847	0.214	0.214	0.000	0.000	0.000	0.000
13	A	15	ASP	-1	-0.808	-0.900	28.367	-10.074	-10.074	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.055	0.003	28.593	-0.400	-0.400	0.000	0.000	0.000	0.000
15	A	17	ASP	-1	-0.898	-0.940	29.542	-9.679	-9.679	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.074	-0.050	25.706	-0.133	-0.133	0.000	0.000	0.000	0.000
17	A	19	ALA	0	0.049	0.025	25.095	-0.396	-0.396	0.000	0.000	0.000	0.000
18	A	20	CYS	0	0.007	-0.011	25.328	-0.353	-0.353	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.883	0.962	27.272	10.187	10.187	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.031	0.019	21.677	-0.172	-0.172	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.001	-0.011	22.453	-0.507	-0.507	0.000	0.000	0.000	0.000
22	A	24	THR	0	-0.064	-0.044	23.409	-0.164	-0.164	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.047	0.027	24.605	-0.146	-0.146	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.016	-0.003	17.396	-0.345	-0.345	0.000	0.000	0.000	0.000
25	A	27	VAL	0	-0.034	-0.019	20.486	-0.519	-0.519	0.000	0.000	0.000	0.000
26	A	28	GLU	-1	-0.966	-0.985	22.354	-11.075	-11.075	0.000	0.000	0.000	0.000
27	A	29	ALA	0	-0.058	-0.030	21.466	0.149	0.149	0.000	0.000	0.000	0.000
28	A	30	LYS	1	0.892	0.950	20.325	12.411	12.411	0.000	0.000	0.000	0.000
29	A	31	LEU	0	0.010	0.014	16.523	-0.771	-0.771	0.000	0.000	0.000	0.000
30	A	32	ALA	0	-0.023	-0.020	15.402	-1.568	-1.568	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.008	0.023	16.853	0.907	0.907	0.000	0.000	0.000	0.000
32	A	34	CYS	0	-0.075	-0.044	18.248	1.131	1.131	0.000	0.000	0.000	0.000
33	A	35	VAL	0	0.048	0.026	18.570	-1.072	-1.072	0.000	0.000	0.000	0.000
34	A	36	GLN	0	-0.041	-0.008	20.689	0.152	0.152	0.000	0.000	0.000	0.000
35	A	37	ILE	0	0.042	0.015	21.910	-0.561	-0.561	0.000	0.000	0.000	0.000
36	A	38	GLY	0	-0.047	-0.010	24.585	0.293	0.293	0.000	0.000	0.000	0.000
37	A	39	GLN	0	-0.022	-0.028	26.118	0.415	0.415	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.016	0.001	27.987	-0.339	-0.339	0.000	0.000	0.000	0.000
39	A	41	VAL	0	-0.028	-0.016	24.651	0.042	0.042	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.820	-0.898	28.061	-9.714	-9.714	0.000	0.000	0.000	0.000
41	A	43	SER	0	-0.012	-0.021	25.308	-0.325	-0.325	0.000	0.000	0.000	0.000
42	A	44	ILE	0	-0.025	-0.017	26.550	0.410	0.410	0.000	0.000	0.000	0.000
43	A	45	TYR	0	-0.039	-0.024	25.059	-0.544	-0.544	0.000	0.000	0.000	0.000
44	A	46	GLN	0	-0.009	-0.006	26.106	0.536	0.536	0.000	0.000	0.000	0.000
45	A	47	TRP	0	-0.009	-0.014	26.620	-0.211	-0.211	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.899	-0.942	28.856	-9.232	-9.232	0.000	0.000	0.000	0.000
47	A	49	ASN	0	-0.072	-0.039	30.516	0.030	0.030	0.000	0.000	0.000	0.000
48	A	50	ASN	0	-0.050	-0.025	31.570	0.397	0.397	0.000	0.000	0.000	0.000
49	A	51	ILE	0	0.021	0.012	30.942	-0.277	-0.277	0.000	0.000	0.000	0.000
50	A	52	CYS	0	-0.043	-0.017	29.796	0.446	0.446	0.000	0.000	0.000	0.000
51	A	53	GLN	0	-0.044	-0.038	30.138	-0.152	-0.152	0.000	0.000	0.000	0.000
52	A	54	SER	0	0.009	0.017	28.387	0.370	0.370	0.000	0.000	0.000	0.000
53	A	55	HIS	0	-0.072	-0.034	29.226	-0.162	-0.162	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.796	-0.846	25.452	-12.337	-12.337	0.000	0.000	0.000	0.000
55	A	57	VAL	0	-0.023	-0.020	25.976	0.230	0.230	0.000	0.000	0.000	0.000
56	A	58	PRO	0	0.018	0.035	21.726	-0.432	-0.432	0.000	0.000	0.000	0.000
57	A	59	MET	0	-0.003	-0.018	20.128	0.643	0.643	0.000	0.000	0.000	0.000
58	A	60	GLN	0	-0.015	-0.004	17.315	-1.070	-1.070	0.000	0.000	0.000	0.000
59	A	61	ILE	0	0.048	0.026	14.993	0.813	0.813	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.847	0.925	14.273	15.590	15.590	0.000	0.000	0.000	0.000
61	A	63	CYS	0	0.005	0.010	11.045	1.335	1.335	0.000	0.000	0.000	0.000
62	A	64	MET	0	0.020	0.053	9.932	-1.488	-1.488	0.000	0.000	0.000	0.000
63	A	65	THR	0	-0.040	-0.062	4.041	0.661	0.797	0.000	-0.013	-0.123	0.000
64	A	66	THR	0	-0.037	-0.012	7.451	-1.336	-1.336	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.769	-0.870	9.606	-20.663	-20.663	0.000	0.000	0.000	0.000
66	A	68	TYR	0	-0.058	-0.045	8.773	-0.082	-0.082	0.000	0.000	0.000	0.000
67	A	69	PRO	0	0.020	-0.004	9.892	1.304	1.304	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.005	0.006	12.412	1.513	1.513	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.005	-0.010	12.575	1.162	1.162	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.871	-0.913	11.220	-25.033	-25.033	0.000	0.000	0.000	0.000
71	A	73	GLN	0	0.018	0.009	14.474	1.631	1.631	0.000	0.000	0.000	0.000
72	A	74	LEU	0	-0.017	0.005	17.270	1.078	1.078	0.000	0.000	0.000	0.000
73	A	75	VAL	0	-0.002	-0.016	17.378	0.844	0.844	0.000	0.000	0.000	0.000
74	A	76	ILE	0	0.003	-0.003	16.368	0.689	0.689	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.043	-0.023	19.638	0.882	0.882	0.000	0.000	0.000	0.000
76	A	78	MET	0	-0.097	-0.039	22.456	0.630	0.630	0.000	0.000	0.000	0.000
77	A	79	HIS	0	-0.021	-0.012	21.830	0.741	0.741	0.000	0.000	0.000	0.000
78	A	80	PRO	0	-0.042	-0.021	24.157	0.186	0.186	0.000	0.000	0.000	0.000
79	A	81	TYR	0	-0.084	-0.069	23.301	0.516	0.516	0.000	0.000	0.000	0.000
80	A	82	GLU	-1	-0.918	-0.967	23.117	-12.137	-12.137	0.000	0.000	0.000	0.000
81	A	83	VAL	0	-0.059	-0.032	18.325	-0.634	-0.634	0.000	0.000	0.000	0.000
82	A	84	PRO	0	0.008	0.011	18.933	0.150	0.150	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.883	-0.901	17.453	-17.112	-17.112	0.000	0.000	0.000	0.000
84	A	86	PHE	0	0.012	0.000	11.840	0.363	0.363	0.000	0.000	0.000	0.000
85	A	87	ILE	0	0.000	0.010	11.531	-1.395	-1.395	0.000	0.000	0.000	0.000
86	A	88	ALA	0	0.034	0.020	7.442	0.639	0.639	0.000	0.000	0.000	0.000
87	A	89	THR	0	-0.026	-0.022	8.556	0.356	0.356	0.000	0.000	0.000	0.000
88	A	90	PRO	0	-0.045	-0.013	5.084	-0.256	-0.256	0.000	0.000	0.000	0.000
89	A	91	ILE	0	0.010	0.012	6.990	3.404	3.404	0.000	0.000	0.000	0.000
90	A	92	ILE	0	-0.020	-0.026	6.274	-2.446	-2.446	0.000	0.000	0.000	0.000
91	A	93	GLY	0	0.003	0.000	8.781	1.210	1.210	0.000	0.000	0.000	0.000
92	A	94	GLY	0	0.022	0.010	12.313	-0.230	-0.230	0.000	0.000	0.000	0.000
93	A	95	PHE	0	0.008	-0.001	15.762	0.279	0.279	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.054	0.026	16.641	-0.183	-0.183	0.000	0.000	0.000	0.000
95	A	97	PRO	0	0.020	0.001	17.644	-0.486	-0.486	0.000	0.000	0.000	0.000
96	A	98	TYR	0	0.009	0.016	17.290	-0.088	-0.088	0.000	0.000	0.000	0.000
97	A	99	LEU	0	0.022	0.013	12.685	-0.171	-0.171	0.000	0.000	0.000	0.000
98	A	100	GLN	0	-0.056	-0.032	15.234	-1.419	-1.419	0.000	0.000	0.000	0.000
99	A	101	TRP	0	-0.013	-0.008	17.257	-0.184	-0.184	0.000	0.000	0.000	0.000
100	A	102	ILE	0	-0.022	-0.023	13.661	0.191	0.191	0.000	0.000	0.000	0.000
101	A	103	LYS	1	0.848	0.890	11.812	21.599	21.599	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.888	-0.934	15.304	-15.013	-15.013	0.000	0.000	0.000	0.000
103	A	105	ASN	0	-0.093	-0.033	18.378	0.879	0.879	0.000	0.000	0.000	0.000
104	A	106	SER	0	0.039	0.027	15.189	0.176	0.176	0.000	0.000	0.000	0.000
105	A	107	PRO	0	-0.037	-0.028	16.982	-0.175	-0.175	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.087	-0.057	14.156	-0.075	-0.075	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)