FMO DATABASE

FMODB ID: K9VN3

Calculation Name: 1AC6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AC6

Chain ID: A

ChEMBL ID:

UniProt ID: P06323

Base Structure: X-ray

Registration Date: 2023-06-26

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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-846247.250104
FMO2-HF: Nuclear repulsion	803978.751283
FMO2-HF: Total energy	-42268.498821
FMO2-MP2: Total energy	-42392.963307

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:1:ASP)

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

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.
-142.134	-136.765	23.216	-12.259	-16.33	0.134

Interaction energy analysis for fragmet #1(A:1:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.838 / q_NPA : -0.939

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	3	VAL	0	0.054	0.007	3.884	-0.055	1.916	-0.017	-1.015	-0.938	0.002
4	A	4	THR	0	-0.035	-0.016	7.046	-1.552	-1.552	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.005	-0.014	10.744	1.453	1.453	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.015	0.004	13.988	-0.173	-0.173	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.911	-0.916	16.907	15.022	15.022	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.013	0.010	18.343	-0.682	-0.682	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.012	-0.018	21.539	0.082	0.082	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.003	0.012	22.197	-0.122	-0.122	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.015	-0.021	24.878	-0.034	-0.034	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.018	-0.001	27.156	-0.050	-0.050	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.050	-0.028	30.385	-0.246	-0.246	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.862	-0.938	32.111	8.843	8.843	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.898	-0.952	33.423	8.476	8.476	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.852	-0.905	30.767	9.170	9.170	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.037	-0.015	25.658	0.241	0.241	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.019	0.013	22.857	0.127	0.127	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.048	-0.042	21.102	0.172	0.172	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.008	0.010	17.354	-0.219	-0.219	0.000	0.000	0.000	0.000
21	A	21	HIS	0	0.001	-0.005	16.790	0.150	0.150	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.046	-0.022	10.988	1.343	1.343	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.012	-0.001	10.592	-1.542	-1.542	0.000	0.000	0.000	0.000
24	A	24	TYR	0	0.007	-0.007	5.523	0.236	0.236	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.017	0.004	4.768	-1.526	-1.324	-0.001	-0.042	-0.160	0.000
26	A	26	ALA	0	0.046	0.017	2.290	0.023	2.807	6.726	-5.093	-4.418	0.013
27	A	27	SER	0	-0.010	0.007	2.249	-23.966	-24.872	1.729	1.431	-2.255	0.026
28	A	28	GLY	0	-0.013	-0.003	4.387	3.354	3.509	-0.001	-0.028	-0.127	0.000
29	A	29	TYR	0	-0.012	-0.001	7.338	-2.605	-2.605	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.005	0.021	5.204	-1.290	-1.290	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.003	0.005	7.322	-4.929	-4.929	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.010	0.009	7.439	3.552	3.552	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.011	-0.031	9.336	-2.216	-2.216	0.000	0.000	0.000	0.000
34	A	34	TRP	0	0.035	0.017	11.899	0.501	0.501	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.006	-0.008	12.099	-0.715	-0.715	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.026	0.019	16.192	0.004	0.004	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.014	-0.005	19.471	0.791	0.791	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.023	0.022	21.306	-0.058	-0.058	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.020	-0.034	25.030	0.164	0.164	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.018	0.018	26.138	-0.384	-0.384	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.837	-0.888	23.684	12.259	12.259	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.004	0.007	20.642	0.177	0.177	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.047	-0.031	15.933	-0.295	-0.295	0.000	0.000	0.000	0.000
44	A	44	GLN	0	0.035	0.024	18.229	0.390	0.390	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.014	-0.011	15.356	0.386	0.386	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.038	0.005	17.315	-0.908	-0.908	0.000	0.000	0.000	0.000
47	A	47	PHE	0	-0.014	-0.020	16.002	-0.656	-0.656	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.921	0.963	12.655	-21.412	-21.412	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.014	0.024	13.402	-1.377	-1.377	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.165	-0.119	12.510	1.969	1.969	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.943	0.970	13.074	-15.486	-15.486	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.726	-0.883	14.700	18.654	18.654	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.761	0.845	15.755	-17.973	-17.973	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.812	-0.860	16.513	17.959	17.959	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.852	0.900	17.229	-11.877	-11.877	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.017	0.029	17.446	-0.326	-0.326	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.018	-0.027	18.416	-0.502	-0.502	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.001	-0.005	21.355	-0.229	-0.229	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.863	0.924	22.039	-12.949	-12.949	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.034	0.023	25.901	-0.249	-0.249	0.000	0.000	0.000	0.000
61	A	61	PHE	0	0.008	0.002	21.357	-0.053	-0.053	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.851	-0.923	20.578	12.643	12.643	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.036	0.029	16.153	0.020	0.020	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.023	-0.014	17.636	-0.108	-0.108	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.058	-0.027	9.625	0.607	0.607	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.016	0.014	13.885	-0.643	-0.643	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.975	0.987	10.357	-24.732	-24.732	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.866	-0.919	12.850	18.562	18.562	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.003	0.004	14.602	0.149	0.149	0.000	0.000	0.000	0.000
70	A	70	THR	0	-0.045	-0.024	9.020	-0.919	-0.919	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.016	-0.014	10.487	0.729	0.729	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.011	-0.019	11.631	0.119	0.119	0.000	0.000	0.000	0.000
73	A	73	HIS	0	0.039	0.035	13.545	-0.133	-0.133	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.006	0.025	16.510	-0.363	-0.363	0.000	0.000	0.000	0.000
75	A	75	GLN	0	-0.026	-0.037	18.415	-0.475	-0.475	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.838	0.907	22.212	-10.814	-10.814	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.027	-0.002	25.322	-0.165	-0.165	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.032	-0.005	28.775	-0.152	-0.152	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.023	0.000	26.986	0.293	0.293	0.000	0.000	0.000	0.000
80	A	80	GLN	0	0.051	0.020	29.692	-0.407	-0.407	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.769	-0.897	30.241	9.629	9.629	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.050	-0.028	29.755	0.148	0.148	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.857	-0.914	26.084	11.283	11.283	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.004	-0.010	25.589	0.633	0.633	0.000	0.000	0.000	0.000
85	A	85	ALA	0	-0.031	-0.009	23.307	-0.114	-0.114	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.035	-0.008	18.455	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	87	TYR	0	-0.026	-0.032	17.961	0.394	0.394	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.026	-0.030	13.078	0.352	0.352	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.000	-0.018	8.279	0.703	0.703	0.000	0.000	0.000	0.000
90	A	91	LEU	0	0.011	0.014	2.355	-0.852	-0.354	0.767	-0.272	-0.994	-0.001
91	A	92	SER	0	-0.032	-0.009	5.773	3.167	3.167	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.060	0.013	4.197	-5.549	-5.484	0.002	-0.085	0.018	0.000
93	A	96	GLY	0	0.031	0.032	2.612	4.878	7.503	1.102	-1.674	-2.053	0.017
94	A	97	ASN	0	-0.033	-0.035	3.475	-4.779	-4.735	0.063	0.313	-0.420	0.004
95	A	98	ASN	0	-0.028	-0.007	6.190	-3.917	-3.917	0.000	0.000	0.000	0.000
96	A	99	LYS	1	0.855	0.939	1.786	-114.276	-117.265	12.605	-5.362	-4.254	0.074
97	A	100	LEU	0	-0.012	-0.008	5.877	6.065	6.065	0.000	0.000	0.000	0.000
98	A	101	THR	0	-0.013	-0.001	2.583	-1.766	-0.846	0.241	-0.432	-0.729	-0.001
99	A	102	PHE	0	0.023	-0.004	5.543	-0.888	-0.888	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.014	0.015	8.377	1.434	1.434	0.000	0.000	0.000	0.000
101	A	104	ALA	0	-0.019	-0.030	10.275	-0.677	-0.677	0.000	0.000	0.000	0.000
102	A	105	GLY	0	0.013	0.016	13.640	-0.845	-0.845	0.000	0.000	0.000	0.000
103	A	106	THR	0	-0.042	-0.033	15.779	0.048	0.048	0.000	0.000	0.000	0.000
104	A	107	LYS	1	0.885	0.951	18.900	-11.088	-11.088	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.000	0.010	22.408	-0.237	-0.237	0.000	0.000	0.000	0.000
106	A	109	THR	0	-0.048	-0.045	24.059	-0.108	-0.108	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.002	0.011	27.830	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	111	LYS	1	0.928	0.965	30.640	-8.630	-8.630	0.000	0.000	0.000	0.000
109	A	112	PRO	0	-0.029	0.001	34.447	-0.189	-0.189	0.000	0.000	0.000	0.000

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