FMO DATABASE

FMODB ID: R9LR8

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	OptH
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	-843782.91712
FMO2-HF: Nuclear repulsion	801515.57327
FMO2-HF: Total energy	-42267.34385
FMO2-MP2: Total energy	-42391.779444

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.
-91.679	-83.954	18.191	-11.58	-14.339	0.07

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 : -0.870 / q_NPA : -0.968

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	0.024	0.008	3.806	-1.565	1.554	-0.037	-1.705	-1.378	0.004
4	A	4	THR	0	-0.027	-0.009	6.771	-1.651	-1.651	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.018	-0.010	10.411	1.269	1.269	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.013	0.006	13.356	-0.184	-0.184	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.920	-0.918	16.645	15.508	15.508	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.004	0.007	18.004	-0.694	-0.694	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.043	-0.034	21.154	0.155	0.155	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.011	0.011	21.702	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.025	-0.028	24.682	0.015	0.015	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.024	0.001	25.963	-0.043	-0.043	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.045	-0.007	29.787	-0.191	-0.191	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.853	-0.958	31.942	8.819	8.819	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.971	-0.981	32.936	8.470	8.470	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.894	-0.940	30.064	9.484	9.484	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.027	0.009	24.849	0.193	0.193	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.013	-0.015	22.272	0.133	0.133	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.018	-0.020	20.789	0.159	0.159	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.024	0.012	16.274	-0.122	-0.122	0.000	0.000	0.000	0.000
21	A	21	HIS	0	-0.001	-0.006	16.118	0.118	0.118	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.054	-0.023	10.282	1.330	1.330	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.004	0.019	10.453	-1.609	-1.609	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.007	-0.011	5.332	-0.345	-0.345	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.032	-0.011	3.881	-1.227	-0.710	0.001	-0.192	-0.326	0.000
26	A	26	ALA	0	0.058	0.033	2.087	4.867	4.143	16.240	-8.836	-6.680	0.021
27	A	27	SER	0	-0.019	0.008	2.722	-24.474	-24.790	0.250	1.841	-1.775	0.021
28	A	28	GLY	0	-0.024	-0.011	4.692	6.334	6.492	-0.001	-0.010	-0.147	0.000
29	A	29	TYR	0	-0.033	-0.009	7.386	-2.033	-2.033	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.002	0.012	4.509	-2.387	-2.225	-0.001	-0.012	-0.149	0.000
31	A	31	ALA	0	0.015	0.023	6.607	-5.317	-5.317	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.010	0.005	7.573	3.929	3.929	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.027	-0.031	9.451	-2.510	-2.510	0.000	0.000	0.000	0.000
34	A	34	TRP	0	0.057	0.022	11.963	0.463	0.463	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.041	-0.023	13.080	-0.657	-0.657	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.032	0.009	16.092	0.103	0.103	0.000	0.000	0.000	0.000
37	A	37	GLN	0	0.029	0.026	18.989	0.764	0.764	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.013	0.021	20.834	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.014	-0.023	24.585	0.148	0.148	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.006	0.010	26.091	-0.338	-0.338	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.875	-0.935	24.015	11.587	11.587	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.009	0.000	20.937	0.292	0.292	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.032	-0.025	16.198	-0.235	-0.235	0.000	0.000	0.000	0.000
44	A	44	GLN	0	0.014	0.013	18.430	-0.078	-0.078	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.012	-0.012	15.221	0.461	0.461	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.021	0.011	17.203	-0.862	-0.862	0.000	0.000	0.000	0.000
47	A	47	PHE	0	-0.036	-0.024	16.251	-0.712	-0.712	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.939	0.967	11.807	-21.743	-21.743	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.026	0.044	13.669	-1.270	-1.270	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.129	-0.080	12.452	1.761	1.761	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.946	0.973	12.590	-16.006	-16.006	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.775	-0.921	14.232	20.079	20.079	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.849	0.915	15.240	-18.091	-18.091	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.888	-0.929	16.569	17.219	17.219	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.984	0.976	17.214	-11.944	-11.944	0.000	0.000	0.000	0.000
56	A	56	GLY	0	-0.007	0.019	17.812	-0.487	-0.487	0.000	0.000	0.000	0.000
57	A	57	SER	0	0.011	-0.022	18.775	-0.513	-0.513	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.020	-0.015	21.495	-0.334	-0.334	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.909	0.964	22.091	-12.758	-12.758	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.038	0.018	25.936	-0.245	-0.245	0.000	0.000	0.000	0.000
61	A	61	PHE	0	-0.002	0.015	20.905	0.026	0.026	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.916	-0.974	20.332	12.697	12.697	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.009	0.007	15.988	0.058	0.058	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.038	-0.016	17.493	-0.206	-0.206	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.059	-0.029	9.255	0.856	0.856	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.031	0.022	13.867	-0.546	-0.546	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.994	0.984	10.483	-26.394	-26.394	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.930	-0.967	13.049	18.079	18.079	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.028	-0.009	14.812	0.018	0.018	0.000	0.000	0.000	0.000
70	A	70	THR	0	-0.018	-0.006	9.178	-0.683	-0.683	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.038	-0.010	10.457	0.734	0.734	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.022	-0.028	11.189	0.142	0.142	0.000	0.000	0.000	0.000
73	A	73	HIS	0	0.040	0.020	13.121	0.048	0.048	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.014	0.015	16.237	-0.314	-0.314	0.000	0.000	0.000	0.000
75	A	75	GLN	0	-0.017	-0.022	18.355	-0.312	-0.312	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.867	0.927	22.083	-11.032	-11.032	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.011	0.005	25.239	-0.115	-0.115	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.034	0.018	28.626	-0.194	-0.194	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.079	-0.030	26.569	0.097	0.097	0.000	0.000	0.000	0.000
80	A	80	GLN	0	0.099	0.057	29.136	-0.428	-0.428	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.773	-0.896	29.858	9.485	9.485	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.113	-0.064	30.289	0.306	0.306	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.845	-0.922	25.809	11.437	11.437	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.040	-0.028	25.282	0.555	0.555	0.000	0.000	0.000	0.000
85	A	85	ALA	0	-0.036	-0.020	22.914	-0.076	-0.076	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.014	0.007	18.074	-0.068	-0.068	0.000	0.000	0.000	0.000
87	A	87	TYR	0	-0.024	-0.004	17.359	0.453	0.453	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.047	-0.034	12.537	0.439	0.439	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.038	-0.004	7.964	0.695	0.695	0.000	0.000	0.000	0.000
90	A	91	LEU	0	0.014	0.015	2.387	-6.490	-3.761	1.654	-1.795	-2.588	0.020
91	A	92	SER	0	-0.045	-0.012	5.981	2.147	2.147	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.091	0.028	4.326	-3.092	-3.021	-0.001	-0.022	-0.049	0.000
93	A	96	GLY	0	0.029	0.016	3.469	-2.669	-1.553	0.057	-0.460	-0.714	0.003
94	A	97	ASN	0	-0.038	-0.034	4.006	-6.697	-6.345	0.013	-0.215	-0.151	0.001
95	A	98	ASN	0	0.000	-0.007	7.273	-3.645	-3.645	0.000	0.000	0.000	0.000
96	A	99	LYS	1	0.932	1.003	4.737	-52.795	-52.733	-0.001	-0.002	-0.058	0.000
97	A	100	LEU	0	-0.027	-0.017	6.572	5.272	5.272	0.000	0.000	0.000	0.000
98	A	101	THR	0	-0.017	0.005	3.708	-1.170	-0.691	0.017	-0.172	-0.324	0.000
99	A	102	PHE	0	0.003	-0.010	5.995	-0.654	-0.654	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.033	0.023	8.528	1.242	1.242	0.000	0.000	0.000	0.000
101	A	104	ALA	0	-0.009	-0.024	10.186	-0.649	-0.649	0.000	0.000	0.000	0.000
102	A	105	GLY	0	-0.001	0.006	13.636	-0.776	-0.776	0.000	0.000	0.000	0.000
103	A	106	THR	0	-0.055	-0.043	15.728	-0.128	-0.128	0.000	0.000	0.000	0.000
104	A	107	LYS	1	0.943	0.961	18.689	-11.354	-11.354	0.000	0.000	0.000	0.000
105	A	108	LEU	0	-0.014	-0.002	22.172	-0.220	-0.220	0.000	0.000	0.000	0.000
106	A	109	THR	0	-0.044	-0.031	24.018	-0.222	-0.222	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.007	0.012	27.309	0.021	0.021	0.000	0.000	0.000	0.000
108	A	111	LYS	1	0.976	0.990	30.209	-8.476	-8.476	0.000	0.000	0.000	0.000
109	A	112	PRO	0	-0.010	0.008	33.976	-0.087	-0.087	0.000	0.000	0.000	0.000

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