FMO DATABASE

FMODB ID: 2KZQR

Calculation Name: 1XG8-A-Xray316

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	111
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-943897.139892
FMO2-HF: Nuclear repulsion	898359.896861
FMO2-HF: Total energy	-45537.24303
FMO2-MP2: Total energy	-45670.988344

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.
-180.795	-178.204	0.003	-1.165	-1.428	-0.005

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 : 1 / q_Mulliken : 0.833 / q_NPA : 0.904

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	0.051	0.034	3.827	4.977	6.480	-0.012	-0.719	-0.772	-0.002
4	A	-5	TYR	0	-0.009	-0.008	6.139	5.155	5.155	0.000	0.000	0.000	0.000
5	A	-4	PHE	0	-0.057	-0.012	3.777	3.091	3.265	0.002	-0.026	-0.149	0.000
6	A	-3	GLN	0	-0.056	-0.027	4.862	-1.036	-1.036	0.000	0.000	0.000	0.000
7	A	-2	SER	0	-0.047	-0.029	8.501	-0.157	-0.157	0.000	0.000	0.000	0.000
8	A	-1	ASN	0	-0.041	-0.030	6.527	-4.474	-4.474	0.000	0.000	0.000	0.000
9	A	0	ALA	0	0.040	0.014	9.064	2.566	2.566	0.000	0.000	0.000	0.000
10	A	1	VAL	0	-0.018	0.010	10.992	-0.917	-0.917	0.000	0.000	0.000	0.000
11	A	2	VAL	0	0.034	0.014	13.393	1.101	1.101	0.000	0.000	0.000	0.000
12	A	3	VAL	0	-0.046	-0.025	16.101	-0.133	-0.133	0.000	0.000	0.000	0.000
13	A	4	TYR	0	0.022	-0.018	16.408	0.259	0.259	0.000	0.000	0.000	0.000
14	A	5	GLY	0	0.062	-0.015	21.367	0.060	0.060	0.000	0.000	0.000	0.000
15	A	6	ALA	0	0.039	0.045	24.996	0.090	0.090	0.000	0.000	0.000	0.000
16	A	7	ASP	-1	-0.939	-0.967	28.473	-9.333	-9.333	0.000	0.000	0.000	0.000
17	A	8	VAL	0	0.013	0.012	31.184	0.350	0.350	0.000	0.000	0.000	0.000
18	A	9	ILE	0	-0.001	-0.012	31.081	-0.290	-0.290	0.000	0.000	0.000	0.000
19	A	10	CYS	0	0.028	0.045	28.936	0.152	0.152	0.000	0.000	0.000	0.000
20	A	11	ALA	0	0.025	-0.004	31.080	0.105	0.105	0.000	0.000	0.000	0.000
21	A	12	SER	0	0.021	0.004	30.261	0.317	0.317	0.000	0.000	0.000	0.000
22	A	13	CYS	0	-0.099	-0.046	28.934	-0.167	-0.167	0.000	0.000	0.000	0.000
23	A	14	VAL	0	0.021	0.026	31.482	-0.058	-0.058	0.000	0.000	0.000	0.000
24	A	15	ASN	0	-0.033	-0.029	34.304	0.175	0.175	0.000	0.000	0.000	0.000
25	A	16	ALA	0	-0.040	-0.003	28.847	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	17	PRO	0	-0.020	-0.012	27.322	0.142	0.142	0.000	0.000	0.000	0.000
27	A	18	THR	0	0.078	0.066	28.072	-0.347	-0.347	0.000	0.000	0.000	0.000
28	A	19	SER	0	0.055	0.013	25.105	-0.503	-0.503	0.000	0.000	0.000	0.000
29	A	20	LYS	1	0.919	0.945	24.759	9.364	9.364	0.000	0.000	0.000	0.000
30	A	21	ASP	-1	-0.830	-0.912	26.305	-10.129	-10.129	0.000	0.000	0.000	0.000
31	A	22	ILE	0	-0.015	0.000	21.564	-0.315	-0.315	0.000	0.000	0.000	0.000
32	A	23	TYR	0	0.018	0.009	19.871	-0.698	-0.698	0.000	0.000	0.000	0.000
33	A	24	ASP	-1	-0.867	-0.927	22.159	-11.605	-11.605	0.000	0.000	0.000	0.000
34	A	25	TRP	0	-0.098	-0.053	21.141	-0.216	-0.216	0.000	0.000	0.000	0.000
35	A	26	LEU	0	0.001	-0.015	17.072	-0.247	-0.247	0.000	0.000	0.000	0.000
36	A	27	GLN	0	-0.027	-0.019	19.283	-0.675	-0.675	0.000	0.000	0.000	0.000
37	A	28	PRO	0	-0.066	-0.037	20.085	-0.314	-0.314	0.000	0.000	0.000	0.000
38	A	29	LEU	0	-0.062	-0.022	19.366	-0.056	-0.056	0.000	0.000	0.000	0.000
39	A	30	LEU	0	0.034	0.015	14.430	0.005	0.005	0.000	0.000	0.000	0.000
40	A	31	LYS	1	0.986	1.016	17.610	12.673	12.673	0.000	0.000	0.000	0.000
41	A	32	ARG	1	0.872	0.935	19.382	12.468	12.468	0.000	0.000	0.000	0.000
42	A	33	LYS	1	0.895	0.943	18.547	14.340	14.340	0.000	0.000	0.000	0.000
43	A	34	TYR	0	-0.045	-0.074	14.315	0.103	0.103	0.000	0.000	0.000	0.000
44	A	35	PRO	0	-0.009	-0.003	15.945	-0.514	-0.514	0.000	0.000	0.000	0.000
45	A	36	ASN	0	-0.023	-0.016	15.480	0.726	0.726	0.000	0.000	0.000	0.000
46	A	37	ILE	0	0.009	0.029	10.294	-1.088	-1.088	0.000	0.000	0.000	0.000
47	A	38	SER	0	0.012	0.017	11.834	0.955	0.955	0.000	0.000	0.000	0.000
48	A	39	PHE	0	0.024	0.006	10.803	-1.949	-1.949	0.000	0.000	0.000	0.000
49	A	40	LYS	1	0.901	0.956	12.117	22.547	22.547	0.000	0.000	0.000	0.000
50	A	41	TYR	0	0.036	0.000	14.423	-0.833	-0.833	0.000	0.000	0.000	0.000
51	A	42	THR	0	0.012	0.010	17.096	0.294	0.294	0.000	0.000	0.000	0.000
52	A	43	TYR	0	-0.050	-0.020	18.717	-0.096	-0.096	0.000	0.000	0.000	0.000
53	A	44	ILE	0	0.031	0.021	18.997	0.247	0.247	0.000	0.000	0.000	0.000
54	A	45	ASP	-1	-0.854	-0.952	22.603	-10.283	-10.283	0.000	0.000	0.000	0.000
55	A	46	ILE	0	-0.002	-0.024	24.161	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	47	THR	0	0.008	0.030	26.475	0.396	0.396	0.000	0.000	0.000	0.000
57	A	48	LYS	1	0.831	0.911	28.250	10.307	10.307	0.000	0.000	0.000	0.000
58	A	49	ASP	-1	-0.844	-0.893	27.112	-10.593	-10.593	0.000	0.000	0.000	0.000
59	A	50	ASN	0	-0.139	-0.096	26.612	0.209	0.209	0.000	0.000	0.000	0.000
60	A	51	ASP	-1	-0.869	-0.928	23.338	-12.379	-12.379	0.000	0.000	0.000	0.000
61	A	52	ASN	0	-0.124	-0.060	20.658	0.463	0.463	0.000	0.000	0.000	0.000
62	A	53	LEU	0	-0.010	-0.004	20.608	-0.785	-0.785	0.000	0.000	0.000	0.000
63	A	54	THR	0	-0.020	-0.009	15.679	-0.108	-0.108	0.000	0.000	0.000	0.000
64	A	55	ASP	-1	-0.932	-0.981	16.496	-15.748	-15.748	0.000	0.000	0.000	0.000
65	A	56	HIS	0	-0.003	-0.003	10.992	0.182	0.182	0.000	0.000	0.000	0.000
66	A	57	ASP	-1	-0.788	-0.870	16.054	-15.959	-15.959	0.000	0.000	0.000	0.000
67	A	58	LEU	0	-0.038	-0.007	18.397	0.363	0.363	0.000	0.000	0.000	0.000
68	A	59	GLN	0	0.038	0.031	15.672	-0.528	-0.528	0.000	0.000	0.000	0.000
69	A	60	PHE	0	-0.041	-0.050	13.957	0.410	0.410	0.000	0.000	0.000	0.000
70	A	61	ILE	0	-0.002	-0.008	19.667	0.490	0.490	0.000	0.000	0.000	0.000
71	A	62	GLU	-1	-0.898	-0.944	22.759	-11.179	-11.179	0.000	0.000	0.000	0.000
72	A	63	ARG	1	0.844	0.914	17.554	15.460	15.460	0.000	0.000	0.000	0.000
73	A	64	ILE	0	-0.073	-0.021	21.949	0.295	0.295	0.000	0.000	0.000	0.000
74	A	65	GLU	-1	-0.932	-0.965	25.277	-10.002	-10.002	0.000	0.000	0.000	0.000
75	A	66	GLN	0	-0.157	-0.068	26.785	0.521	0.521	0.000	0.000	0.000	0.000
76	A	67	ASP	-1	-0.965	-0.992	28.525	-10.008	-10.008	0.000	0.000	0.000	0.000
77	A	68	GLU	-1	-0.895	-0.915	22.640	-13.422	-13.422	0.000	0.000	0.000	0.000
78	A	69	LEU	0	-0.065	-0.031	19.466	-0.349	-0.349	0.000	0.000	0.000	0.000
79	A	70	PHE	0	-0.018	-0.028	23.942	0.557	0.557	0.000	0.000	0.000	0.000
80	A	71	TYR	0	0.012	-0.013	23.584	-0.561	-0.561	0.000	0.000	0.000	0.000
81	A	72	PRO	0	-0.022	-0.035	22.653	0.451	0.451	0.000	0.000	0.000	0.000
82	A	73	LEU	0	0.014	0.046	18.263	-0.079	-0.079	0.000	0.000	0.000	0.000
83	A	74	ILE	0	-0.076	-0.041	15.200	-0.084	-0.084	0.000	0.000	0.000	0.000
84	A	75	THR	0	0.019	0.017	12.953	-0.579	-0.579	0.000	0.000	0.000	0.000
85	A	76	MET	0	-0.044	-0.029	8.072	0.962	0.962	0.000	0.000	0.000	0.000
86	A	77	ASN	0	-0.053	-0.054	5.383	1.245	1.245	0.000	0.000	0.000	0.000
87	A	78	ASP	-1	-0.829	-0.920	8.049	-24.944	-24.944	0.000	0.000	0.000	0.000
88	A	79	GLU	-1	-0.883	-0.922	6.390	-37.361	-37.361	0.000	0.000	0.000	0.000
89	A	80	TYR	0	-0.050	-0.087	10.621	0.689	0.689	0.000	0.000	0.000	0.000
90	A	81	VAL	0	-0.078	-0.023	12.358	-0.702	-0.702	0.000	0.000	0.000	0.000
91	A	82	ALA	0	-0.056	-0.049	14.703	0.676	0.676	0.000	0.000	0.000	0.000
92	A	83	ASP	-1	-0.764	-0.828	18.526	-13.800	-13.800	0.000	0.000	0.000	0.000
93	A	84	GLY	0	0.047	0.033	21.633	0.341	0.341	0.000	0.000	0.000	0.000
94	A	85	TYR	0	-0.044	-0.018	25.304	0.219	0.219	0.000	0.000	0.000	0.000
95	A	86	ILE	0	0.015	0.017	20.850	-0.465	-0.465	0.000	0.000	0.000	0.000
96	A	87	GLN	0	-0.035	-0.025	22.514	0.264	0.264	0.000	0.000	0.000	0.000
97	A	88	THR	0	0.031	-0.012	21.112	-0.588	-0.588	0.000	0.000	0.000	0.000
98	A	89	LYS	1	0.917	0.955	19.905	12.343	12.343	0.000	0.000	0.000	0.000
99	A	90	GLN	0	0.081	0.057	18.203	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	91	ILE	0	0.060	0.042	15.762	-0.978	-0.978	0.000	0.000	0.000	0.000
101	A	92	THR	0	0.013	-0.014	14.950	-0.650	-0.650	0.000	0.000	0.000	0.000
102	A	93	ARG	1	0.909	0.953	15.060	14.027	14.027	0.000	0.000	0.000	0.000
103	A	94	PHE	0	0.038	0.039	9.156	-0.760	-0.760	0.000	0.000	0.000	0.000
104	A	95	ILE	0	0.035	0.012	10.510	-2.245	-2.245	0.000	0.000	0.000	0.000
105	A	96	ASP	-1	-0.844	-0.890	10.791	-20.817	-20.817	0.000	0.000	0.000	0.000
106	A	97	GLN	0	0.003	0.008	8.382	-0.248	-0.248	0.000	0.000	0.000	0.000
107	A	98	LYS	1	0.864	0.924	5.059	39.950	39.950	0.000	0.000	0.000	0.000
108	A	99	LEU	0	-0.047	-0.013	8.342	-1.815	-1.815	0.000	0.000	0.000	0.000
109	A	100	VAL	0	-0.067	-0.033	10.498	0.347	0.347	0.000	0.000	0.000	0.000
110	A	101	ASN	0	-0.130	-0.066	9.227	2.505	2.505	0.000	0.000	0.000	0.000
111	A	102	GLU	-2	-1.833	-1.909	3.608	-112.524	-111.610	0.013	-0.420	-0.507	-0.003

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