FMO DATABASE

FMODB ID: V5GQ1

Calculation Name: 1XTE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1XTE

Chain ID: A

ChEMBL ID:

UniProt ID: Q9ERE3

Base Structure: X-ray

Registration Date: 2023-09-19

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	OptHSide
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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1015003.514807
FMO2-HF: Nuclear repulsion	967019.794418
FMO2-HF: Total energy	-47983.720388
FMO2-MP2: Total energy	-48125.54379

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:4:LYS)

Summations of interaction energy for fragment #1(A:4:LYS)

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.
64.657	67.077	8.715	-5.82	-5.317	-0.059

Interaction energy analysis for fragmet #1(A:4:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.962 / q_NPA : 0.974

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

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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	SER	0	-0.081	-0.039	1.855	-43.095	-41.000	8.715	-5.789	-5.022	-0.059
4	A	7	CYS	0	-0.014	0.004	3.637	7.869	8.165	0.001	-0.031	-0.267	0.000
5	A	8	PRO	0	0.010	0.002	5.243	1.634	1.663	-0.001	0.000	-0.028	0.000
6	A	9	SER	0	0.021	0.030	8.812	-0.428	-0.428	0.000	0.000	0.000	0.000
7	A	10	VAL	0	-0.012	-0.010	10.860	1.188	1.188	0.000	0.000	0.000	0.000
8	A	11	SER	0	0.030	0.025	14.578	0.564	0.564	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.022	0.001	17.878	0.242	0.242	0.000	0.000	0.000	0.000
10	A	13	PRO	0	0.034	0.022	20.717	0.721	0.721	0.000	0.000	0.000	0.000
11	A	14	SER	0	-0.037	-0.023	23.458	0.442	0.442	0.000	0.000	0.000	0.000
12	A	15	SER	0	0.026	0.000	26.397	-0.358	-0.358	0.000	0.000	0.000	0.000
13	A	16	ASP	-1	-0.859	-0.895	29.123	-10.699	-10.699	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.846	-0.908	32.187	-8.307	-8.307	0.000	0.000	0.000	0.000
15	A	18	HIS	0	-0.002	-0.002	31.969	0.154	0.154	0.000	0.000	0.000	0.000
16	A	19	ARG	1	0.981	0.976	36.844	7.497	7.497	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.797	-0.884	39.126	-8.209	-8.209	0.000	0.000	0.000	0.000
18	A	21	LYS	1	1.014	0.997	42.488	6.765	6.765	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.921	0.957	45.320	6.419	6.419	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.840	0.919	39.578	8.078	8.078	0.000	0.000	0.000	0.000
21	A	24	ARG	1	0.921	0.960	39.368	7.886	7.886	0.000	0.000	0.000	0.000
22	A	25	PHE	0	-0.054	-0.030	33.753	-0.090	-0.090	0.000	0.000	0.000	0.000
23	A	26	THR	0	0.069	0.036	31.061	0.102	0.102	0.000	0.000	0.000	0.000
24	A	27	VAL	0	-0.058	-0.023	28.285	-0.218	-0.218	0.000	0.000	0.000	0.000
25	A	28	TYR	0	-0.006	-0.020	25.295	0.112	0.112	0.000	0.000	0.000	0.000
26	A	29	LYS	1	0.840	0.909	23.606	11.592	11.592	0.000	0.000	0.000	0.000
27	A	30	VAL	0	-0.006	-0.022	18.395	-0.092	-0.092	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.005	0.011	17.427	0.324	0.324	0.000	0.000	0.000	0.000
29	A	32	VAL	0	-0.030	-0.026	13.819	-0.669	-0.669	0.000	0.000	0.000	0.000
30	A	33	SER	0	0.035	-0.021	11.073	0.572	0.572	0.000	0.000	0.000	0.000
31	A	34	VAL	0	-0.006	0.000	7.986	-2.196	-2.196	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.013	0.000	6.648	0.249	0.249	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.913	0.947	7.401	29.019	29.019	0.000	0.000	0.000	0.000
34	A	37	SER	0	0.019	0.018	10.418	2.313	2.313	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.819	-0.880	12.274	-21.849	-21.849	0.000	0.000	0.000	0.000
36	A	39	TRP	0	-0.043	-0.019	13.017	1.307	1.307	0.000	0.000	0.000	0.000
37	A	40	PHE	0	0.050	0.013	18.210	-0.309	-0.309	0.000	0.000	0.000	0.000
38	A	41	VAL	0	-0.071	-0.030	19.296	0.270	0.270	0.000	0.000	0.000	0.000
39	A	42	PHE	0	0.014	0.008	22.084	0.126	0.126	0.000	0.000	0.000	0.000
40	A	43	ARG	1	0.845	0.937	22.317	13.730	13.730	0.000	0.000	0.000	0.000
41	A	44	ARG	1	0.956	0.966	26.217	10.376	10.376	0.000	0.000	0.000	0.000
42	A	45	TYR	0	0.046	-0.004	27.999	-0.171	-0.171	0.000	0.000	0.000	0.000
43	A	46	ALA	0	-0.009	-0.012	28.675	-0.203	-0.203	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.810	-0.886	26.302	-11.576	-11.576	0.000	0.000	0.000	0.000
45	A	48	PHE	0	0.042	0.020	21.707	-0.287	-0.287	0.000	0.000	0.000	0.000
46	A	49	ASP	-1	-0.804	-0.901	25.378	-10.512	-10.512	0.000	0.000	0.000	0.000
47	A	50	LYS	1	0.971	1.002	27.265	11.591	11.591	0.000	0.000	0.000	0.000
48	A	51	LEU	0	0.017	0.017	19.926	0.077	0.077	0.000	0.000	0.000	0.000
49	A	52	TYR	0	0.022	0.015	24.171	-0.203	-0.203	0.000	0.000	0.000	0.000
50	A	53	ASN	0	-0.079	-0.053	25.110	0.178	0.178	0.000	0.000	0.000	0.000
51	A	54	SER	0	-0.055	-0.023	25.054	0.351	0.351	0.000	0.000	0.000	0.000
52	A	55	LEU	0	0.053	0.011	19.667	0.095	0.095	0.000	0.000	0.000	0.000
53	A	56	LYS	1	0.888	0.950	23.582	11.293	11.293	0.000	0.000	0.000	0.000
54	A	57	LYS	1	0.911	0.954	25.824	10.145	10.145	0.000	0.000	0.000	0.000
55	A	58	GLN	0	0.015	0.026	23.451	-0.212	-0.212	0.000	0.000	0.000	0.000
56	A	59	PHE	0	0.017	0.013	19.508	-0.054	-0.054	0.000	0.000	0.000	0.000
57	A	60	PRO	0	0.013	0.006	23.537	-0.168	-0.168	0.000	0.000	0.000	0.000
58	A	61	ALA	0	0.003	-0.005	23.624	0.190	0.190	0.000	0.000	0.000	0.000
59	A	62	MET	0	-0.011	0.006	18.893	-0.388	-0.388	0.000	0.000	0.000	0.000
60	A	63	ALA	0	-0.037	0.005	22.362	-0.070	-0.070	0.000	0.000	0.000	0.000
61	A	64	LEU	0	0.044	0.026	19.909	-0.036	-0.036	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.930	0.950	23.431	13.618	13.618	0.000	0.000	0.000	0.000
63	A	66	ILE	0	0.030	0.022	24.278	-0.534	-0.534	0.000	0.000	0.000	0.000
64	A	67	PRO	0	0.007	0.012	26.361	0.405	0.405	0.000	0.000	0.000	0.000
65	A	68	ALA	0	0.040	0.034	29.245	0.029	0.029	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.909	0.950	32.762	9.452	9.452	0.000	0.000	0.000	0.000
67	A	70	ARG	1	0.885	0.952	33.981	7.795	7.795	0.000	0.000	0.000	0.000
68	A	71	ILE	0	0.022	0.018	36.907	-0.105	-0.105	0.000	0.000	0.000	0.000
69	A	72	PHE	0	-0.002	-0.008	38.918	0.099	0.099	0.000	0.000	0.000	0.000
70	A	73	GLY	0	0.085	0.028	42.589	0.056	0.056	0.000	0.000	0.000	0.000
71	A	74	ASP	-1	-0.826	-0.912	41.660	-7.819	-7.819	0.000	0.000	0.000	0.000
72	A	75	ASN	0	-0.077	-0.035	37.053	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	76	PHE	0	-0.077	-0.066	36.737	-0.310	-0.310	0.000	0.000	0.000	0.000
74	A	77	ASP	-1	-0.809	-0.881	38.463	-8.144	-8.144	0.000	0.000	0.000	0.000
75	A	78	PRO	0	0.027	-0.003	35.803	-0.303	-0.303	0.000	0.000	0.000	0.000
76	A	79	ASP	-1	-0.857	-0.924	34.483	-9.092	-9.092	0.000	0.000	0.000	0.000
77	A	80	PHE	0	-0.027	-0.012	33.984	-0.379	-0.379	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.028	-0.019	31.444	-0.428	-0.428	0.000	0.000	0.000	0.000
79	A	82	LYS	1	0.955	0.983	29.798	9.926	9.926	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.009	0.005	28.919	-0.466	-0.466	0.000	0.000	0.000	0.000
81	A	84	ARG	1	0.862	0.931	28.662	9.504	9.504	0.000	0.000	0.000	0.000
82	A	85	ARG	1	0.902	0.949	24.873	11.698	11.698	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.005	0.005	24.492	-0.662	-0.662	0.000	0.000	0.000	0.000
84	A	87	GLY	0	0.015	0.004	23.743	-0.526	-0.526	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.063	-0.036	23.809	-0.309	-0.309	0.000	0.000	0.000	0.000
86	A	89	ASN	0	0.026	0.008	18.886	-0.802	-0.802	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.788	-0.879	19.141	-17.231	-17.231	0.000	0.000	0.000	0.000
88	A	91	PHE	0	-0.060	-0.027	19.223	-0.701	-0.701	0.000	0.000	0.000	0.000
89	A	92	ILE	0	0.013	-0.012	17.490	-0.479	-0.479	0.000	0.000	0.000	0.000
90	A	93	GLN	0	-0.020	-0.017	14.815	-0.841	-0.841	0.000	0.000	0.000	0.000
91	A	94	ASN	0	-0.010	-0.012	14.151	-1.916	-1.916	0.000	0.000	0.000	0.000
92	A	95	LEU	0	0.003	-0.002	14.929	-0.752	-0.752	0.000	0.000	0.000	0.000
93	A	96	VAL	0	-0.020	-0.010	11.015	-0.551	-0.551	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.801	0.895	9.999	16.606	16.606	0.000	0.000	0.000	0.000
95	A	98	TYR	0	0.009	0.008	10.246	-1.775	-1.775	0.000	0.000	0.000	0.000
96	A	99	PRO	0	0.072	0.044	8.967	0.969	0.969	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.911	-0.957	10.763	-18.137	-18.137	0.000	0.000	0.000	0.000
98	A	101	LEU	0	-0.037	-0.022	13.745	1.621	1.621	0.000	0.000	0.000	0.000
99	A	102	TYR	0	-0.009	-0.017	6.414	-0.176	-0.176	0.000	0.000	0.000	0.000
100	A	103	ASN	0	-0.023	-0.025	9.714	-0.369	-0.369	0.000	0.000	0.000	0.000
101	A	104	HIS	0	-0.019	0.000	13.488	0.904	0.904	0.000	0.000	0.000	0.000
102	A	105	PRO	0	0.062	0.012	17.116	-0.340	-0.340	0.000	0.000	0.000	0.000
103	A	106	ASP	-1	-0.900	-0.949	19.232	-13.410	-13.410	0.000	0.000	0.000	0.000
104	A	107	VAL	0	-0.039	-0.018	15.371	0.405	0.405	0.000	0.000	0.000	0.000
105	A	108	ARG	1	0.877	0.900	10.862	24.697	24.697	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.007	0.008	16.640	0.163	0.163	0.000	0.000	0.000	0.000
107	A	110	PHE	0	-0.032	-0.032	19.420	0.561	0.561	0.000	0.000	0.000	0.000
108	A	111	LEU	0	0.035	0.002	14.493	0.634	0.634	0.000	0.000	0.000	0.000
109	A	112	GLN	0	-0.063	-0.035	17.190	-0.271	-0.271	0.000	0.000	0.000	0.000
110	A	113	MET	0	-0.008	-0.011	10.965	0.254	0.254	0.000	0.000	0.000	0.000
111	A	114	ASP	-1	-0.778	-0.829	14.442	-22.161	-22.161	0.000	0.000	0.000	0.000
112	A	115	SER	0	-0.044	-0.021	16.814	1.354	1.354	0.000	0.000	0.000	0.000
113	A	116	PRO	0	0.053	0.022	18.643	-0.609	-0.609	0.000	0.000	0.000	0.000
114	A	117	ARG	1	0.926	0.954	20.414	13.310	13.310	0.000	0.000	0.000	0.000
115	A	118	HIS	1	0.808	0.920	16.780	17.705	17.705	0.000	0.000	0.000	0.000
116	A	119	GLN	0	0.073	0.059	16.041	-0.570	-0.570	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LYS)