FMO DATABASE

FMODB ID: 14K4Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-940369.281491
FMO2-HF: Nuclear repulsion	894830.584146
FMO2-HF: Total energy	-45538.697345
FMO2-MP2: Total energy	-45672.22055

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.
-2.592	0.441	-8.673617379884E-19	-1.307	-1.726	0.004

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 : 0.033 / q_NPA : 0.016

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	0.007	0.024	3.868	-0.032	1.939	-0.014	-1.067	-0.889	0.004
4	A	-5	TYR	0	-0.028	-0.011	5.955	0.565	0.565	0.000	0.000	0.000	0.000
5	A	-4	PHE	0	-0.054	-0.018	3.438	-0.183	0.077	0.011	-0.055	-0.217	0.000
6	A	-3	GLN	0	-0.035	-0.024	4.156	0.564	0.829	0.000	-0.044	-0.221	0.000
7	A	-2	SER	0	-0.044	-0.029	7.963	-0.132	-0.132	0.000	0.000	0.000	0.000
8	A	-1	ASN	0	-0.009	0.002	6.382	0.049	0.049	0.000	0.000	0.000	0.000
9	A	0	ALA	0	0.024	0.009	8.787	-0.006	-0.006	0.000	0.000	0.000	0.000
10	A	1	VAL	0	-0.014	-0.003	10.955	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	2	VAL	0	0.030	0.022	13.240	0.009	0.009	0.000	0.000	0.000	0.000
12	A	3	VAL	0	-0.039	-0.022	15.820	-0.025	-0.025	0.000	0.000	0.000	0.000
13	A	4	TYR	0	0.021	-0.014	16.397	0.008	0.008	0.000	0.000	0.000	0.000
14	A	5	GLY	0	0.081	0.011	21.554	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	6	ALA	0	0.031	0.047	25.285	0.009	0.009	0.000	0.000	0.000	0.000
16	A	7	ASP	-1	-0.806	-0.892	28.715	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	8	VAL	0	-0.018	-0.001	31.212	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	9	ILE	0	0.016	0.016	31.311	0.002	0.002	0.000	0.000	0.000	0.000
19	A	10	CYS	0	0.010	0.039	28.934	0.006	0.006	0.000	0.000	0.000	0.000
20	A	11	ALA	0	0.025	-0.004	31.110	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	12	SER	0	0.012	0.008	30.175	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	13	CYS	0	-0.077	-0.029	29.033	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	14	VAL	0	0.015	0.017	31.449	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	15	ASN	0	-0.035	-0.020	33.923	0.003	0.003	0.000	0.000	0.000	0.000
25	A	16	ALA	0	-0.033	0.001	28.417	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	17	PRO	0	-0.034	-0.023	27.486	0.004	0.004	0.000	0.000	0.000	0.000
27	A	18	THR	0	0.040	0.021	28.072	0.003	0.003	0.000	0.000	0.000	0.000
28	A	19	SER	0	-0.005	-0.035	25.373	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	20	LYS	1	0.847	0.909	24.687	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	21	ASP	-1	-0.816	-0.900	25.903	-0.051	-0.051	0.000	0.000	0.000	0.000
31	A	22	ILE	0	0.001	-0.005	21.506	-0.014	-0.014	0.000	0.000	0.000	0.000
32	A	23	TYR	0	0.040	0.016	19.236	-0.015	-0.015	0.000	0.000	0.000	0.000
33	A	24	ASP	-1	-0.889	-0.950	21.783	-0.055	-0.055	0.000	0.000	0.000	0.000
34	A	25	TRP	0	-0.066	-0.023	20.872	-0.016	-0.016	0.000	0.000	0.000	0.000
35	A	26	LEU	0	0.009	-0.003	16.445	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	27	GLN	0	-0.004	0.001	19.076	-0.023	-0.023	0.000	0.000	0.000	0.000
37	A	28	PRO	0	-0.030	-0.027	20.056	-0.023	-0.023	0.000	0.000	0.000	0.000
38	A	29	LEU	0	-0.060	-0.005	19.230	-0.013	-0.013	0.000	0.000	0.000	0.000
39	A	30	LEU	0	0.070	0.036	13.898	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	31	LYS	1	0.927	0.970	17.354	0.127	0.127	0.000	0.000	0.000	0.000
41	A	32	ARG	1	0.810	0.893	19.140	0.185	0.185	0.000	0.000	0.000	0.000
42	A	33	LYS	1	0.924	0.968	18.128	0.290	0.290	0.000	0.000	0.000	0.000
43	A	34	TYR	0	-0.012	-0.034	14.077	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	35	PRO	0	-0.007	-0.008	15.518	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	36	ASN	0	-0.015	-0.004	15.384	0.063	0.063	0.000	0.000	0.000	0.000
46	A	37	ILE	0	0.006	0.021	9.929	-0.040	-0.040	0.000	0.000	0.000	0.000
47	A	38	SER	0	-0.002	0.018	11.757	0.096	0.096	0.000	0.000	0.000	0.000
48	A	39	PHE	0	0.024	-0.006	11.012	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	40	LYS	1	0.861	0.926	11.091	-0.146	-0.146	0.000	0.000	0.000	0.000
50	A	41	TYR	0	0.039	0.014	14.066	-0.016	-0.016	0.000	0.000	0.000	0.000
51	A	42	THR	0	-0.001	-0.005	16.826	0.029	0.029	0.000	0.000	0.000	0.000
52	A	43	TYR	0	-0.059	-0.023	18.710	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	44	ILE	0	0.017	0.015	18.786	0.006	0.006	0.000	0.000	0.000	0.000
54	A	45	ASP	-1	-0.812	-0.904	22.560	0.023	0.023	0.000	0.000	0.000	0.000
55	A	46	ILE	0	0.041	0.012	24.196	0.006	0.006	0.000	0.000	0.000	0.000
56	A	47	THR	0	-0.020	-0.012	26.565	0.001	0.001	0.000	0.000	0.000	0.000
57	A	48	LYS	1	0.723	0.840	28.385	-0.028	-0.028	0.000	0.000	0.000	0.000
58	A	49	ASP	-1	-0.882	-0.935	26.986	0.091	0.091	0.000	0.000	0.000	0.000
59	A	50	ASN	0	-0.120	-0.058	23.962	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	51	ASP	-1	-0.873	-0.930	25.911	0.103	0.103	0.000	0.000	0.000	0.000
61	A	52	ASN	0	-0.184	-0.095	20.868	0.024	0.024	0.000	0.000	0.000	0.000
62	A	53	LEU	0	0.058	0.034	20.521	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	54	THR	0	-0.061	-0.054	15.091	0.026	0.026	0.000	0.000	0.000	0.000
64	A	55	ASP	-1	-0.882	-0.951	16.400	0.287	0.287	0.000	0.000	0.000	0.000
65	A	56	HIS	0	-0.033	-0.044	11.008	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	57	ASP	-1	-0.771	-0.838	15.945	0.163	0.163	0.000	0.000	0.000	0.000
67	A	58	LEU	0	0.020	0.022	18.390	-0.026	-0.026	0.000	0.000	0.000	0.000
68	A	59	GLN	0	-0.047	-0.023	15.950	-0.036	-0.036	0.000	0.000	0.000	0.000
69	A	60	PHE	0	-0.037	-0.035	14.193	-0.029	-0.029	0.000	0.000	0.000	0.000
70	A	61	ILE	0	0.006	0.000	19.836	-0.021	-0.021	0.000	0.000	0.000	0.000
71	A	62	GLU	-1	-0.884	-0.935	23.215	0.091	0.091	0.000	0.000	0.000	0.000
72	A	63	ARG	1	0.767	0.843	17.385	-0.095	-0.095	0.000	0.000	0.000	0.000
73	A	64	ILE	0	-0.052	-0.017	22.411	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	65	GLU	-1	-0.925	-0.966	25.528	0.040	0.040	0.000	0.000	0.000	0.000
75	A	66	GLN	0	-0.150	-0.081	27.019	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	67	ASP	-1	-0.968	-0.991	28.634	0.008	0.008	0.000	0.000	0.000	0.000
77	A	68	GLU	-1	-0.856	-0.871	22.124	0.049	0.049	0.000	0.000	0.000	0.000
78	A	69	LEU	0	-0.055	-0.019	19.956	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	70	PHE	0	0.011	-0.012	24.230	0.001	0.001	0.000	0.000	0.000	0.000
80	A	71	TYR	0	-0.003	-0.023	24.023	0.002	0.002	0.000	0.000	0.000	0.000
81	A	72	PRO	0	-0.011	-0.030	22.945	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	73	LEU	0	0.011	0.032	17.925	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	74	ILE	0	-0.079	-0.037	15.234	0.003	0.003	0.000	0.000	0.000	0.000
84	A	75	THR	0	0.062	0.030	12.729	-0.022	-0.022	0.000	0.000	0.000	0.000
85	A	76	MET	0	-0.051	-0.037	7.878	-0.046	-0.046	0.000	0.000	0.000	0.000
86	A	77	ASN	0	-0.054	-0.042	5.251	0.100	0.100	0.000	0.000	0.000	0.000
87	A	78	ASP	-1	-0.813	-0.877	8.043	0.538	0.538	0.000	0.000	0.000	0.000
88	A	79	GLU	-1	-0.846	-0.915	6.089	-0.675	-0.675	0.000	0.000	0.000	0.000
89	A	80	TYR	0	-0.024	-0.048	10.203	-0.056	-0.056	0.000	0.000	0.000	0.000
90	A	81	VAL	0	-0.079	-0.027	12.297	-0.061	-0.061	0.000	0.000	0.000	0.000
91	A	82	ALA	0	-0.047	-0.044	14.681	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	83	ASP	-1	-0.778	-0.862	18.553	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	84	GLY	0	0.073	0.051	21.768	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	85	TYR	0	-0.060	-0.039	25.127	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	86	ILE	0	-0.003	0.007	20.651	-0.013	-0.013	0.000	0.000	0.000	0.000
96	A	87	GLN	0	-0.014	-0.009	22.662	-0.014	-0.014	0.000	0.000	0.000	0.000
97	A	88	THR	0	0.037	-0.008	21.327	-0.011	-0.011	0.000	0.000	0.000	0.000
98	A	89	LYS	1	0.920	0.952	20.036	0.180	0.180	0.000	0.000	0.000	0.000
99	A	90	GLN	0	0.052	0.039	18.288	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	91	ILE	0	0.051	0.036	16.008	-0.035	-0.035	0.000	0.000	0.000	0.000
101	A	92	THR	0	-0.077	-0.043	15.044	-0.023	-0.023	0.000	0.000	0.000	0.000
102	A	93	ARG	1	0.940	0.972	14.830	0.209	0.209	0.000	0.000	0.000	0.000
103	A	94	PHE	0	0.027	0.032	8.774	-0.091	-0.091	0.000	0.000	0.000	0.000
104	A	95	ILE	0	0.052	0.022	10.478	-0.138	-0.138	0.000	0.000	0.000	0.000
105	A	96	ASP	-1	-0.832	-0.908	10.934	-0.632	-0.632	0.000	0.000	0.000	0.000
106	A	97	GLN	0	0.005	0.013	8.993	-0.164	-0.164	0.000	0.000	0.000	0.000
107	A	98	LYS	1	0.800	0.897	4.364	1.501	1.567	-0.001	-0.004	-0.061	0.000
108	A	99	LEU	0	-0.038	-0.030	8.364	-0.299	-0.299	0.000	0.000	0.000	0.000
109	A	100	VAL	0	-0.074	-0.023	10.412	0.027	0.027	0.000	0.000	0.000	0.000
110	A	101	ASN	0	-0.042	-0.014	9.279	0.163	0.163	0.000	0.000	0.000	0.000
111	A	102	GLU	-1	-0.869	-0.925	3.949	-4.591	-4.120	0.004	-0.137	-0.338	0.000

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