FMO DATABASE

FMODB ID: YY8Y2

Calculation Name: 1XG8-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1XG8

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

Base Structure: X-ray

Registration Date: 2023-06-20

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	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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-942990.324016
FMO2-HF: Nuclear repulsion	897452.961263
FMO2-HF: Total energy	-45537.362754
FMO2-MP2: Total energy	-45671.107084

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:-8:ALA)

Summations of interaction energy for fragment #1(A:-8:ALA)

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.
-4.543	-1.457	-0.005	-1.532	-1.55	0.003

Interaction energy analysis for fragmet #1(A:-8:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.039 / q_NPA : 0.023

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	-6	LEU	0	0.026	0.016	3.827	-0.197	2.004	-0.021	-1.193	-0.988	0.005
4	A	-5	TYR	0	-0.022	-0.017	6.153	0.586	0.586	0.000	0.000	0.000	0.000
5	A	-4	PHE	0	-0.047	-0.007	3.774	0.070	0.263	0.001	-0.031	-0.163	0.000
6	A	-3	GLN	0	-0.048	-0.022	4.850	0.918	0.918	0.000	0.000	0.000	0.000
7	A	-2	SER	0	-0.051	-0.031	8.504	-0.176	-0.176	0.000	0.000	0.000	0.000
8	A	-1	ASN	0	-0.043	-0.032	6.532	-0.032	-0.032	0.000	0.000	0.000	0.000
9	A	0	ALA	0	0.042	0.015	9.060	0.023	0.023	0.000	0.000	0.000	0.000
10	A	1	VAL	0	-0.019	0.010	10.989	-0.045	-0.045	0.000	0.000	0.000	0.000
11	A	2	VAL	0	0.032	0.012	13.393	0.031	0.031	0.000	0.000	0.000	0.000
12	A	3	VAL	0	-0.043	-0.024	16.098	-0.031	-0.031	0.000	0.000	0.000	0.000
13	A	4	TYR	0	0.021	-0.019	16.403	0.009	0.009	0.000	0.000	0.000	0.000
14	A	5	GLY	0	0.060	-0.015	21.363	-0.017	-0.017	0.000	0.000	0.000	0.000
15	A	6	ALA	0	0.039	0.045	24.993	0.011	0.011	0.000	0.000	0.000	0.000
16	A	7	ASP	-1	-0.939	-0.967	28.470	-0.043	-0.043	0.000	0.000	0.000	0.000
17	A	8	VAL	0	0.013	0.013	31.182	0.000	0.000	0.000	0.000	0.000	0.000
18	A	9	ILE	0	0.003	-0.011	31.080	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	10	CYS	0	0.026	0.045	28.936	0.005	0.005	0.000	0.000	0.000	0.000
20	A	11	ALA	0	0.025	-0.005	31.079	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	12	SER	0	0.021	0.003	30.265	0.000	0.000	0.000	0.000	0.000	0.000
22	A	13	CYS	0	-0.099	-0.046	28.937	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	14	VAL	0	0.023	0.026	31.483	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	15	ASN	0	-0.033	-0.029	34.308	0.003	0.003	0.000	0.000	0.000	0.000
25	A	16	ALA	0	-0.043	-0.004	28.852	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	17	PRO	0	-0.020	-0.012	27.328	0.005	0.005	0.000	0.000	0.000	0.000
27	A	18	THR	0	0.081	0.067	28.076	0.000	0.000	0.000	0.000	0.000	0.000
28	A	19	SER	0	0.056	0.012	25.105	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	20	LYS	1	0.917	0.944	24.760	0.030	0.030	0.000	0.000	0.000	0.000
30	A	21	ASP	-1	-0.831	-0.912	26.307	-0.091	-0.091	0.000	0.000	0.000	0.000
31	A	22	ILE	0	-0.016	-0.001	21.567	-0.015	-0.015	0.000	0.000	0.000	0.000
32	A	23	TYR	0	0.016	0.008	19.869	-0.021	-0.021	0.000	0.000	0.000	0.000
33	A	24	ASP	-1	-0.868	-0.928	22.162	-0.101	-0.101	0.000	0.000	0.000	0.000
34	A	25	TRP	0	-0.096	-0.052	21.148	-0.017	-0.017	0.000	0.000	0.000	0.000
35	A	26	LEU	0	0.002	-0.014	17.077	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	27	GLN	0	-0.028	-0.019	19.289	-0.020	-0.020	0.000	0.000	0.000	0.000
37	A	28	PRO	0	-0.063	-0.035	20.092	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	29	LEU	0	-0.061	-0.022	19.376	-0.016	-0.016	0.000	0.000	0.000	0.000
39	A	30	LEU	0	0.035	0.015	14.438	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	31	LYS	1	0.983	1.014	17.621	0.171	0.171	0.000	0.000	0.000	0.000
41	A	32	ARG	1	0.875	0.935	19.391	0.212	0.212	0.000	0.000	0.000	0.000
42	A	33	LYS	1	0.894	0.944	18.560	0.320	0.320	0.000	0.000	0.000	0.000
43	A	34	TYR	0	-0.046	-0.074	14.329	0.002	0.002	0.000	0.000	0.000	0.000
44	A	35	PRO	0	-0.007	-0.003	15.956	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	36	ASN	0	-0.023	-0.017	15.493	0.067	0.067	0.000	0.000	0.000	0.000
46	A	37	ILE	0	0.007	0.028	10.304	-0.034	-0.034	0.000	0.000	0.000	0.000
47	A	38	SER	0	0.012	0.017	11.842	0.042	0.042	0.000	0.000	0.000	0.000
48	A	39	PHE	0	0.024	0.006	10.812	-0.060	-0.060	0.000	0.000	0.000	0.000
49	A	40	LYS	1	0.904	0.959	12.112	-0.022	-0.022	0.000	0.000	0.000	0.000
50	A	41	TYR	0	0.035	0.000	14.422	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	42	THR	0	0.009	0.008	17.095	0.031	0.031	0.000	0.000	0.000	0.000
52	A	43	TYR	0	-0.049	-0.019	18.713	-0.013	-0.013	0.000	0.000	0.000	0.000
53	A	44	ILE	0	0.017	0.015	18.987	0.011	0.011	0.000	0.000	0.000	0.000
54	A	45	ASP	-1	-0.850	-0.951	22.597	-0.020	-0.020	0.000	0.000	0.000	0.000
55	A	46	ILE	0	0.002	-0.022	24.155	0.006	0.006	0.000	0.000	0.000	0.000
56	A	47	THR	0	0.010	0.032	26.469	0.003	0.003	0.000	0.000	0.000	0.000
57	A	48	LYS	1	0.828	0.905	28.248	0.012	0.012	0.000	0.000	0.000	0.000
58	A	49	ASP	-1	-0.858	-0.908	27.104	0.039	0.039	0.000	0.000	0.000	0.000
59	A	50	ASN	0	-0.137	-0.077	24.012	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	51	ASP	-1	-0.870	-0.929	25.994	0.067	0.067	0.000	0.000	0.000	0.000
61	A	52	ASN	0	-0.182	-0.101	20.917	0.021	0.021	0.000	0.000	0.000	0.000
62	A	53	LEU	0	0.054	0.023	20.684	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	54	THR	0	-0.026	-0.001	15.666	0.023	0.023	0.000	0.000	0.000	0.000
64	A	55	ASP	-1	-0.923	-0.976	16.510	0.216	0.216	0.000	0.000	0.000	0.000
65	A	56	HIS	0	0.000	-0.001	11.003	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	57	ASP	-1	-0.787	-0.871	16.069	0.058	0.058	0.000	0.000	0.000	0.000
67	A	58	LEU	0	-0.036	-0.007	18.387	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	59	GLN	0	0.038	0.031	15.679	-0.025	-0.025	0.000	0.000	0.000	0.000
69	A	60	PHE	0	-0.042	-0.050	13.967	-0.031	-0.031	0.000	0.000	0.000	0.000
70	A	61	ILE	0	0.001	-0.007	19.660	-0.017	-0.017	0.000	0.000	0.000	0.000
71	A	62	GLU	-1	-0.898	-0.945	22.771	0.061	0.061	0.000	0.000	0.000	0.000
72	A	63	ARG	1	0.846	0.915	17.566	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	64	ILE	0	-0.070	-0.021	21.946	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	65	GLU	-1	-0.934	-0.966	25.273	0.005	0.005	0.000	0.000	0.000	0.000
75	A	66	GLN	0	-0.160	-0.069	26.788	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	67	ASP	-1	-0.963	-0.991	28.535	-0.027	-0.027	0.000	0.000	0.000	0.000
77	A	68	GLU	-1	-0.892	-0.914	22.651	-0.026	-0.026	0.000	0.000	0.000	0.000
78	A	69	LEU	0	-0.067	-0.031	19.475	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	70	PHE	0	-0.017	-0.027	23.950	0.006	0.006	0.000	0.000	0.000	0.000
80	A	71	TYR	0	0.012	-0.013	23.584	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	72	PRO	0	-0.020	-0.035	22.655	0.003	0.003	0.000	0.000	0.000	0.000
82	A	73	LEU	0	0.017	0.048	18.262	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	74	ILE	0	-0.084	-0.044	15.203	0.004	0.004	0.000	0.000	0.000	0.000
84	A	75	THR	0	0.026	0.020	12.951	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	76	MET	0	-0.052	-0.032	8.080	0.002	0.002	0.000	0.000	0.000	0.000
86	A	77	ASN	0	-0.043	-0.050	5.367	0.191	0.191	0.000	0.000	0.000	0.000
87	A	78	ASP	-1	-0.829	-0.920	8.041	0.287	0.287	0.000	0.000	0.000	0.000
88	A	79	GLU	-1	-0.878	-0.919	6.398	-0.985	-0.985	0.000	0.000	0.000	0.000
89	A	80	TYR	0	-0.054	-0.089	10.629	-0.045	-0.045	0.000	0.000	0.000	0.000
90	A	81	VAL	0	-0.082	-0.026	12.355	-0.068	-0.068	0.000	0.000	0.000	0.000
91	A	82	ALA	0	-0.052	-0.048	14.703	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	83	ASP	-1	-0.764	-0.828	18.525	-0.113	-0.113	0.000	0.000	0.000	0.000
93	A	84	GLY	0	0.051	0.036	21.635	0.000	0.000	0.000	0.000	0.000	0.000
94	A	85	TYR	0	-0.047	-0.019	25.305	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	86	ILE	0	0.021	0.018	20.856	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	87	GLN	0	-0.039	-0.025	22.509	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	88	THR	0	0.030	-0.012	21.105	-0.018	-0.018	0.000	0.000	0.000	0.000
98	A	89	LYS	1	0.918	0.955	19.895	0.246	0.246	0.000	0.000	0.000	0.000
99	A	90	GLN	0	0.079	0.055	18.196	-0.022	-0.022	0.000	0.000	0.000	0.000
100	A	91	ILE	0	0.065	0.044	15.771	-0.046	-0.046	0.000	0.000	0.000	0.000
101	A	92	THR	0	0.013	-0.013	14.953	-0.038	-0.038	0.000	0.000	0.000	0.000
102	A	93	ARG	1	0.906	0.951	15.046	0.289	0.289	0.000	0.000	0.000	0.000
103	A	94	PHE	0	0.038	0.040	9.156	-0.104	-0.104	0.000	0.000	0.000	0.000
104	A	95	ILE	0	0.043	0.016	10.497	-0.168	-0.168	0.000	0.000	0.000	0.000
105	A	96	ASP	-1	-0.843	-0.890	10.775	-0.805	-0.805	0.000	0.000	0.000	0.000
106	A	97	GLN	0	0.009	0.012	8.375	-0.028	-0.028	0.000	0.000	0.000	0.000
107	A	98	LYS	1	0.875	0.931	5.049	1.897	1.897	0.000	0.000	0.000	0.000
108	A	99	LEU	0	-0.051	-0.017	8.324	-0.275	-0.275	0.000	0.000	0.000	0.000
109	A	100	VAL	0	-0.068	-0.034	10.479	0.013	0.013	0.000	0.000	0.000	0.000
110	A	101	ASN	0	-0.103	-0.049	9.288	0.245	0.245	0.000	0.000	0.000	0.000
111	A	102	GLU	-1	-0.918	-0.955	3.594	-6.722	-6.030	0.015	-0.308	-0.399	-0.002

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Interactive mode: IFIE and PIEDA for fragment #1(A:-8:ALA)