FMO DATABASE

FMODB ID: 17LNZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1017937.575166
FMO2-HF: Nuclear repulsion	969953.224643
FMO2-HF: Total energy	-47984.350524
FMO2-MP2: Total energy	-48126.070647

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.
61.85	62.808	11.681	-6.846	-5.793	-0.071

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 : 0.959 / q_NPA : 0.973

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	SER	0	-0.054	-0.030	1.786	-49.489	-48.829	11.677	-6.833	-5.503	-0.071
4	A	7	CYS	0	0.002	0.008	3.379	11.232	11.530	0.004	-0.013	-0.290	0.000
5	A	8	PRO	0	-0.001	0.006	5.458	0.672	0.672	0.000	0.000	0.000	0.000
6	A	9	SER	0	-0.001	0.000	8.835	-0.659	-0.659	0.000	0.000	0.000	0.000
7	A	10	VAL	0	-0.010	-0.008	10.846	1.301	1.301	0.000	0.000	0.000	0.000
8	A	11	SER	0	0.022	0.017	14.643	0.572	0.572	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.022	-0.001	18.032	0.232	0.232	0.000	0.000	0.000	0.000
10	A	13	PRO	0	0.038	0.033	20.601	0.767	0.767	0.000	0.000	0.000	0.000
11	A	14	SER	0	-0.038	-0.026	23.372	0.454	0.454	0.000	0.000	0.000	0.000
12	A	15	SER	0	0.016	-0.012	26.399	-0.369	-0.369	0.000	0.000	0.000	0.000
13	A	16	ASP	-1	-0.793	-0.865	29.229	-10.720	-10.720	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.820	-0.898	32.145	-8.133	-8.133	0.000	0.000	0.000	0.000
15	A	18	HIS	0	0.021	0.015	32.095	0.159	0.159	0.000	0.000	0.000	0.000
16	A	19	ARG	1	0.875	0.913	36.511	7.699	7.699	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.793	-0.874	39.196	-8.188	-8.188	0.000	0.000	0.000	0.000
18	A	21	LYS	1	1.008	0.985	42.585	6.766	6.766	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.926	0.965	45.502	6.387	6.387	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.854	0.928	39.578	8.083	8.083	0.000	0.000	0.000	0.000
21	A	24	ARG	1	0.885	0.944	39.167	7.893	7.893	0.000	0.000	0.000	0.000
22	A	25	PHE	0	-0.028	-0.028	33.462	-0.079	-0.079	0.000	0.000	0.000	0.000
23	A	26	THR	0	0.039	0.027	31.121	0.076	0.076	0.000	0.000	0.000	0.000
24	A	27	VAL	0	-0.042	-0.016	28.354	-0.238	-0.238	0.000	0.000	0.000	0.000
25	A	28	TYR	0	-0.008	-0.019	25.493	0.121	0.121	0.000	0.000	0.000	0.000
26	A	29	LYS	1	0.825	0.907	23.753	11.503	11.503	0.000	0.000	0.000	0.000
27	A	30	VAL	0	-0.016	-0.023	18.588	-0.057	-0.057	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.008	0.013	17.172	0.353	0.353	0.000	0.000	0.000	0.000
29	A	32	VAL	0	-0.014	-0.023	13.925	-0.376	-0.376	0.000	0.000	0.000	0.000
30	A	33	SER	0	0.049	0.002	11.001	0.195	0.195	0.000	0.000	0.000	0.000
31	A	34	VAL	0	0.003	-0.003	7.854	-1.680	-1.680	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.039	0.031	6.332	-0.548	-0.548	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.885	0.926	6.941	29.648	29.648	0.000	0.000	0.000	0.000
34	A	37	SER	0	0.023	0.027	10.040	2.378	2.378	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.860	-0.913	12.126	-22.407	-22.407	0.000	0.000	0.000	0.000
36	A	39	TRP	0	-0.028	-0.014	12.901	1.149	1.149	0.000	0.000	0.000	0.000
37	A	40	PHE	0	0.041	0.013	18.093	-0.272	-0.272	0.000	0.000	0.000	0.000
38	A	41	VAL	0	-0.055	-0.019	19.142	0.054	0.054	0.000	0.000	0.000	0.000
39	A	42	PHE	0	0.019	0.009	21.941	0.172	0.172	0.000	0.000	0.000	0.000
40	A	43	ARG	1	0.847	0.925	22.332	13.625	13.625	0.000	0.000	0.000	0.000
41	A	44	ARG	1	0.934	0.956	26.369	10.423	10.423	0.000	0.000	0.000	0.000
42	A	45	TYR	0	0.025	-0.020	28.376	-0.157	-0.157	0.000	0.000	0.000	0.000
43	A	46	ALA	0	0.019	0.000	28.782	-0.217	-0.217	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.806	-0.874	26.299	-11.563	-11.563	0.000	0.000	0.000	0.000
45	A	48	PHE	0	0.038	0.019	22.019	-0.314	-0.314	0.000	0.000	0.000	0.000
46	A	49	ASP	-1	-0.799	-0.896	25.445	-10.414	-10.414	0.000	0.000	0.000	0.000
47	A	50	LYS	1	0.883	0.947	25.843	12.159	12.159	0.000	0.000	0.000	0.000
48	A	51	LEU	0	0.020	0.034	19.896	0.064	0.064	0.000	0.000	0.000	0.000
49	A	52	TYR	0	0.043	0.016	24.125	-0.195	-0.195	0.000	0.000	0.000	0.000
50	A	53	ASN	0	-0.058	-0.036	25.252	0.124	0.124	0.000	0.000	0.000	0.000
51	A	54	SER	0	-0.030	-0.033	25.064	0.236	0.236	0.000	0.000	0.000	0.000
52	A	55	LEU	0	0.031	0.027	19.772	0.065	0.065	0.000	0.000	0.000	0.000
53	A	56	LYS	1	0.869	0.926	23.722	11.178	11.178	0.000	0.000	0.000	0.000
54	A	57	LYS	1	0.913	0.950	26.089	10.260	10.260	0.000	0.000	0.000	0.000
55	A	58	GLN	0	-0.012	0.008	23.738	-0.051	-0.051	0.000	0.000	0.000	0.000
56	A	59	PHE	0	0.036	0.021	19.509	-0.043	-0.043	0.000	0.000	0.000	0.000
57	A	60	PRO	0	0.001	0.002	23.739	-0.159	-0.159	0.000	0.000	0.000	0.000
58	A	61	ALA	0	0.010	-0.006	24.234	0.147	0.147	0.000	0.000	0.000	0.000
59	A	62	MET	0	-0.008	0.010	19.207	-0.385	-0.385	0.000	0.000	0.000	0.000
60	A	63	ALA	0	-0.022	0.001	22.777	-0.097	-0.097	0.000	0.000	0.000	0.000
61	A	64	LEU	0	0.015	0.013	20.459	0.067	0.067	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.895	0.940	22.403	14.207	14.207	0.000	0.000	0.000	0.000
63	A	66	ILE	0	0.022	0.010	24.475	-0.548	-0.548	0.000	0.000	0.000	0.000
64	A	67	PRO	0	-0.001	0.023	26.657	0.388	0.388	0.000	0.000	0.000	0.000
65	A	68	ALA	0	0.054	0.038	29.571	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.876	0.949	32.940	9.633	9.633	0.000	0.000	0.000	0.000
67	A	70	ARG	1	0.885	0.950	34.134	7.755	7.755	0.000	0.000	0.000	0.000
68	A	71	ILE	0	0.025	0.013	37.230	-0.145	-0.145	0.000	0.000	0.000	0.000
69	A	72	PHE	0	0.012	-0.012	39.231	0.100	0.100	0.000	0.000	0.000	0.000
70	A	73	GLY	0	0.092	0.041	42.583	0.107	0.107	0.000	0.000	0.000	0.000
71	A	74	ASP	-1	-0.774	-0.886	41.404	-7.856	-7.856	0.000	0.000	0.000	0.000
72	A	75	ASN	0	-0.072	-0.043	36.766	-0.018	-0.018	0.000	0.000	0.000	0.000
73	A	76	PHE	0	-0.096	-0.059	36.513	-0.339	-0.339	0.000	0.000	0.000	0.000
74	A	77	ASP	-1	-0.772	-0.871	38.090	-8.272	-8.272	0.000	0.000	0.000	0.000
75	A	78	PRO	0	0.029	0.009	35.797	-0.315	-0.315	0.000	0.000	0.000	0.000
76	A	79	ASP	-1	-0.830	-0.906	34.386	-9.339	-9.339	0.000	0.000	0.000	0.000
77	A	80	PHE	0	-0.025	-0.007	33.842	-0.346	-0.346	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.030	-0.014	31.525	-0.406	-0.406	0.000	0.000	0.000	0.000
79	A	82	LYS	1	0.873	0.928	30.031	9.168	9.168	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.013	0.010	28.955	-0.483	-0.483	0.000	0.000	0.000	0.000
81	A	84	ARG	1	0.847	0.914	28.682	9.369	9.369	0.000	0.000	0.000	0.000
82	A	85	ARG	1	0.898	0.947	25.215	11.534	11.534	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.026	0.015	24.600	-0.640	-0.640	0.000	0.000	0.000	0.000
84	A	87	GLY	0	0.008	-0.003	23.848	-0.536	-0.536	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.052	-0.036	23.992	-0.330	-0.330	0.000	0.000	0.000	0.000
86	A	89	ASN	0	0.020	0.014	19.072	-0.767	-0.767	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.762	-0.867	19.261	-16.534	-16.534	0.000	0.000	0.000	0.000
88	A	91	PHE	0	-0.056	-0.013	19.560	-0.563	-0.563	0.000	0.000	0.000	0.000
89	A	92	ILE	0	0.013	-0.010	17.709	-0.513	-0.513	0.000	0.000	0.000	0.000
90	A	93	GLN	0	-0.018	-0.030	15.111	-0.738	-0.738	0.000	0.000	0.000	0.000
91	A	94	ASN	0	-0.020	-0.007	14.714	-1.609	-1.609	0.000	0.000	0.000	0.000
92	A	95	LEU	0	-0.024	-0.010	15.668	-0.509	-0.509	0.000	0.000	0.000	0.000
93	A	96	VAL	0	-0.005	-0.009	10.884	-0.557	-0.557	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.835	0.914	10.339	16.187	16.187	0.000	0.000	0.000	0.000
95	A	98	TYR	0	0.020	0.011	11.119	-1.233	-1.233	0.000	0.000	0.000	0.000
96	A	99	PRO	0	0.045	0.017	9.022	0.659	0.659	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.905	-0.952	10.907	-18.729	-18.729	0.000	0.000	0.000	0.000
98	A	101	LEU	0	-0.030	-0.011	14.171	1.336	1.336	0.000	0.000	0.000	0.000
99	A	102	TYR	0	-0.010	-0.013	6.878	-0.523	-0.523	0.000	0.000	0.000	0.000
100	A	103	ASN	0	0.001	-0.009	9.636	-0.685	-0.685	0.000	0.000	0.000	0.000
101	A	104	HIS	0	0.009	0.011	13.633	0.895	0.895	0.000	0.000	0.000	0.000
102	A	105	PRO	0	0.038	0.011	17.224	-0.412	-0.412	0.000	0.000	0.000	0.000
103	A	106	ASP	-1	-0.860	-0.931	19.401	-13.197	-13.197	0.000	0.000	0.000	0.000
104	A	107	VAL	0	-0.014	-0.003	15.329	0.324	0.324	0.000	0.000	0.000	0.000
105	A	108	ARG	1	0.836	0.876	10.141	26.370	26.370	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.001	0.013	16.310	0.128	0.128	0.000	0.000	0.000	0.000
107	A	110	PHE	0	-0.036	-0.027	19.346	0.495	0.495	0.000	0.000	0.000	0.000
108	A	111	LEU	0	0.045	0.011	14.265	0.662	0.662	0.000	0.000	0.000	0.000
109	A	112	GLN	0	-0.039	-0.017	17.166	-0.148	-0.148	0.000	0.000	0.000	0.000
110	A	113	MET	0	0.003	0.005	10.570	0.467	0.467	0.000	0.000	0.000	0.000
111	A	114	ASP	-1	-0.771	-0.839	13.937	-22.931	-22.931	0.000	0.000	0.000	0.000
112	A	115	SER	0	-0.066	-0.039	16.189	1.346	1.346	0.000	0.000	0.000	0.000
113	A	116	PRO	0	0.057	0.019	18.364	-0.595	-0.595	0.000	0.000	0.000	0.000
114	A	117	ARG	1	0.901	0.946	19.771	13.413	13.413	0.000	0.000	0.000	0.000
115	A	118	HIS	1	0.832	0.927	16.293	18.186	18.186	0.000	0.000	0.000	0.000
116	A	119	GLN	0	0.039	0.047	15.331	-0.457	-0.457	0.000	0.000	0.000	0.000

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