FMO DATABASE

FMODB ID: N181Q

Calculation Name: 1X8Z-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1X8Z

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LNF2

Base Structure: X-ray

Registration Date: 2023-03-13

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	149
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1203602.575023
FMO2-HF: Nuclear repulsion	1144278.291244
FMO2-HF: Total energy	-59324.283779
FMO2-MP2: Total energy	-59489.883297

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:-1:MET)

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

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.
-26.157	-18.558	18.861	-8.211	-18.251	-0.028

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / q_NPA : -0.019

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	1	SER	0	0.025	0.003	3.054	-1.545	0.293	0.152	-0.822	-1.168	-0.005
4	A	2	SER	0	0.015	0.023	5.071	0.455	0.629	-0.001	-0.013	-0.160	0.000
5	A	3	GLU	-1	-0.882	-0.930	2.539	-10.315	-8.699	2.253	-1.563	-2.306	-0.020
6	A	4	MET	0	-0.004	-0.006	2.467	-2.246	-1.238	5.373	-1.606	-4.776	0.011
7	A	5	SER	0	0.005	-0.010	3.392	0.609	0.677	0.032	0.189	-0.289	0.000
8	A	6	THR	0	-0.049	-0.028	6.604	0.291	0.291	0.000	0.000	0.000	0.000
9	A	7	ILE	0	-0.024	-0.006	2.680	-0.167	0.196	0.454	-0.120	-0.698	0.000
10	A	8	CYS	0	-0.014	0.001	6.610	0.622	0.622	0.000	0.000	0.000	0.000
11	A	9	ASP	-1	-0.875	-0.934	8.219	-0.110	-0.110	0.000	0.000	0.000	0.000
12	A	10	LYS	1	0.841	0.922	10.389	0.622	0.622	0.000	0.000	0.000	0.000
13	A	11	THR	0	-0.057	-0.037	9.499	0.059	0.059	0.000	0.000	0.000	0.000
14	A	12	LEU	0	0.017	-0.009	12.502	0.001	0.001	0.000	0.000	0.000	0.000
15	A	13	ASN	0	0.014	0.015	13.783	0.014	0.014	0.000	0.000	0.000	0.000
16	A	14	PRO	0	0.080	0.056	11.067	0.131	0.131	0.000	0.000	0.000	0.000
17	A	15	SER	0	-0.014	-0.007	10.830	0.182	0.182	0.000	0.000	0.000	0.000
18	A	16	PHE	0	-0.003	-0.005	11.950	0.136	0.136	0.000	0.000	0.000	0.000
19	A	18	LEU	0	0.087	0.034	7.021	0.783	0.783	0.000	0.000	0.000	0.000
20	A	19	LYS	1	0.948	0.986	7.354	-0.291	-0.291	0.000	0.000	0.000	0.000
21	A	20	PHE	0	-0.023	-0.001	7.942	0.025	0.025	0.000	0.000	0.000	0.000
22	A	21	LEU	0	0.042	0.000	2.334	-1.959	-1.175	2.278	-0.633	-2.430	0.009
23	A	22	ASN	0	-0.003	-0.015	4.434	-0.698	-0.341	0.007	-0.079	-0.286	0.000
24	A	23	THR	0	-0.111	-0.078	5.386	-0.813	-0.772	-0.001	0.000	-0.039	0.000
25	A	24	LYS	1	0.884	0.955	6.381	-1.493	-1.493	0.000	0.000	0.000	0.000
26	A	25	PHE	0	-0.006	-0.002	2.337	-2.101	-1.214	3.235	-1.117	-3.006	0.003
27	A	26	ALA	0	0.029	0.029	2.050	-8.214	-8.104	5.079	-2.396	-2.792	-0.026
28	A	27	SER	0	0.016	0.015	4.055	0.392	0.715	0.001	-0.049	-0.274	0.000
29	A	28	PRO	0	-0.012	0.006	5.105	-0.500	-0.470	-0.001	-0.002	-0.027	0.000
30	A	29	ASN	0	0.024	0.002	8.147	-0.029	-0.029	0.000	0.000	0.000	0.000
31	A	30	LEU	0	0.072	0.022	11.500	0.008	0.008	0.000	0.000	0.000	0.000
32	A	31	GLN	0	0.049	0.019	14.963	-0.017	-0.017	0.000	0.000	0.000	0.000
33	A	32	ALA	0	0.014	0.008	11.948	-0.015	-0.015	0.000	0.000	0.000	0.000
34	A	33	LEU	0	0.001	0.012	10.767	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	34	ALA	0	0.044	0.035	14.132	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	35	LYS	1	0.825	0.897	16.606	-0.244	-0.244	0.000	0.000	0.000	0.000
37	A	36	THR	0	0.009	-0.011	13.975	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	37	THR	0	-0.020	-0.014	16.586	-0.026	-0.026	0.000	0.000	0.000	0.000
39	A	38	LEU	0	0.050	0.042	18.936	-0.026	-0.026	0.000	0.000	0.000	0.000
40	A	39	ASP	-1	-0.815	-0.872	18.842	0.196	0.196	0.000	0.000	0.000	0.000
41	A	40	SER	0	-0.068	-0.041	18.710	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	41	THR	0	-0.026	-0.038	21.408	-0.020	-0.020	0.000	0.000	0.000	0.000
43	A	42	GLN	0	0.050	0.018	23.746	-0.019	-0.019	0.000	0.000	0.000	0.000
44	A	43	ALA	0	-0.008	0.013	23.993	-0.013	-0.013	0.000	0.000	0.000	0.000
45	A	44	ARG	1	0.854	0.925	23.691	-0.089	-0.089	0.000	0.000	0.000	0.000
46	A	45	ALA	0	0.065	0.020	26.996	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	46	THR	0	0.001	-0.014	29.210	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	47	GLN	0	-0.068	-0.039	26.061	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	48	THR	0	-0.004	-0.005	31.391	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	49	LEU	0	0.038	0.043	33.474	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	50	LYS	1	0.950	0.975	32.378	-0.068	-0.068	0.000	0.000	0.000	0.000
52	A	51	LYS	1	0.845	0.911	35.263	-0.032	-0.032	0.000	0.000	0.000	0.000
53	A	52	LEU	0	-0.003	-0.008	36.966	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	53	GLN	0	0.045	0.019	39.493	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	54	SER	0	-0.010	0.004	40.050	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	55	ILE	0	-0.070	-0.028	39.652	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	56	ILE	0	-0.045	-0.017	43.121	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	57	ASP	-1	-0.905	-0.945	44.898	0.030	0.030	0.000	0.000	0.000	0.000
59	A	58	GLY	0	-0.047	-0.013	45.769	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	59	GLY	0	-0.039	-0.012	47.274	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	60	VAL	0	-0.030	-0.019	46.233	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	61	ASP	-1	-0.809	-0.875	49.523	0.017	0.017	0.000	0.000	0.000	0.000
63	A	62	PRO	0	0.041	0.000	50.852	0.001	0.001	0.000	0.000	0.000	0.000
64	A	63	ARG	1	0.905	0.966	49.802	-0.015	-0.015	0.000	0.000	0.000	0.000
65	A	64	SER	0	-0.011	-0.057	46.915	0.002	0.002	0.000	0.000	0.000	0.000
66	A	65	LYS	1	0.823	0.909	46.508	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	66	LEU	0	-0.014	0.004	47.334	0.002	0.002	0.000	0.000	0.000	0.000
68	A	67	ALA	0	0.040	0.017	44.725	0.002	0.002	0.000	0.000	0.000	0.000
69	A	68	TYR	0	0.043	-0.006	40.902	0.002	0.002	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.958	0.974	42.410	-0.027	-0.027	0.000	0.000	0.000	0.000
71	A	70	SER	0	0.005	-0.004	43.601	0.002	0.002	0.000	0.000	0.000	0.000
72	A	71	CYS	0	-0.025	-0.006	36.653	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	72	VAL	0	-0.025	-0.008	38.876	0.004	0.004	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.880	-0.928	39.494	0.044	0.044	0.000	0.000	0.000	0.000
75	A	74	GLU	-1	-0.909	-0.937	37.458	0.055	0.055	0.000	0.000	0.000	0.000
76	A	75	TYR	0	-0.025	-0.057	31.852	0.008	0.008	0.000	0.000	0.000	0.000
77	A	76	GLU	-1	-0.897	-0.966	35.096	0.056	0.056	0.000	0.000	0.000	0.000
78	A	77	SER	0	-0.005	-0.003	36.615	0.003	0.003	0.000	0.000	0.000	0.000
79	A	78	ALA	0	-0.019	-0.005	32.423	0.005	0.005	0.000	0.000	0.000	0.000
80	A	79	ILE	0	-0.056	-0.039	31.284	0.007	0.007	0.000	0.000	0.000	0.000
81	A	80	GLY	0	0.089	0.055	31.238	0.007	0.007	0.000	0.000	0.000	0.000
82	A	81	ASN	0	-0.014	-0.011	31.746	0.006	0.006	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.041	-0.033	26.396	0.009	0.009	0.000	0.000	0.000	0.000
84	A	83	GLU	-1	-0.910	-0.951	27.330	0.103	0.103	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.838	-0.921	28.717	0.092	0.092	0.000	0.000	0.000	0.000
86	A	85	ALA	0	-0.046	-0.023	26.286	0.005	0.005	0.000	0.000	0.000	0.000
87	A	86	PHE	0	-0.031	-0.022	21.655	0.017	0.017	0.000	0.000	0.000	0.000
88	A	87	GLU	-1	-0.912	-0.950	24.995	0.117	0.117	0.000	0.000	0.000	0.000
89	A	88	HIS	0	-0.035	-0.009	27.204	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.005	-0.007	19.518	0.007	0.007	0.000	0.000	0.000	0.000
91	A	90	ALA	0	-0.048	-0.018	22.615	0.013	0.013	0.000	0.000	0.000	0.000
92	A	91	SER	0	-0.057	-0.033	23.855	0.001	0.001	0.000	0.000	0.000	0.000
93	A	92	GLY	0	-0.039	-0.013	22.922	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	93	ASP	-1	-0.820	-0.898	23.958	0.112	0.112	0.000	0.000	0.000	0.000
95	A	94	GLY	0	0.019	-0.005	24.356	0.000	0.000	0.000	0.000	0.000	0.000
96	A	95	MET	0	-0.022	-0.007	24.985	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	96	GLY	0	0.062	0.013	28.638	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	97	MET	0	-0.024	-0.001	21.322	0.002	0.002	0.000	0.000	0.000	0.000
99	A	98	ASN	0	-0.060	-0.023	25.909	-0.011	-0.011	0.000	0.000	0.000	0.000
100	A	99	MET	0	-0.006	0.003	27.682	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	100	LYS	1	0.859	0.927	29.696	-0.097	-0.097	0.000	0.000	0.000	0.000
102	A	101	VAL	0	-0.014	-0.017	25.030	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	102	SER	0	-0.035	-0.026	28.337	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	103	ALA	0	0.055	0.039	30.944	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	104	ALA	0	-0.008	0.001	29.496	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	105	LEU	0	-0.078	-0.036	28.071	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	106	ASP	-1	-0.863	-0.937	30.912	0.061	0.061	0.000	0.000	0.000	0.000
108	A	107	GLY	0	0.059	0.046	34.537	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	108	ALA	0	-0.061	-0.042	31.598	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	109	ASP	-1	-0.811	-0.915	33.535	0.047	0.047	0.000	0.000	0.000	0.000
111	A	110	THR	0	0.025	0.017	35.305	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.065	-0.049	33.350	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.828	-0.903	37.938	0.030	0.030	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.823	-0.873	40.866	0.031	0.031	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.055	-0.029	39.140	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.740	0.846	41.158	-0.032	-0.032	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.927	0.970	42.682	-0.020	-0.020	0.000	0.000	0.000	0.000
118	A	118	LEU	0	0.005	0.020	44.145	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.904	0.940	46.362	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.022	-0.012	44.459	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	121	VAL	0	0.022	0.013	39.488	0.001	0.001	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.767	-0.862	37.809	0.024	0.024	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.056	0.017	35.076	0.003	0.003	0.000	0.000	0.000	0.000
124	A	124	SER	0	-0.034	-0.006	33.434	0.003	0.003	0.000	0.000	0.000	0.000
125	A	125	VAL	0	0.041	0.017	33.276	0.005	0.005	0.000	0.000	0.000	0.000
126	A	126	VAL	0	-0.005	0.012	34.121	0.005	0.005	0.000	0.000	0.000	0.000
127	A	127	ASN	0	-0.009	-0.021	29.988	0.001	0.001	0.000	0.000	0.000	0.000
128	A	128	ASN	0	0.025	0.032	29.035	0.004	0.004	0.000	0.000	0.000	0.000
129	A	129	SER	0	0.063	0.035	29.204	0.009	0.009	0.000	0.000	0.000	0.000
130	A	130	LYS	1	0.941	0.976	29.967	-0.029	-0.029	0.000	0.000	0.000	0.000
131	A	131	THR	0	-0.063	-0.041	24.345	0.005	0.005	0.000	0.000	0.000	0.000
132	A	132	ILE	0	0.030	0.014	25.367	0.013	0.013	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.842	0.922	26.614	-0.049	-0.049	0.000	0.000	0.000	0.000
134	A	134	ASN	0	-0.019	-0.007	23.890	0.004	0.004	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.034	-0.012	20.469	0.014	0.014	0.000	0.000	0.000	0.000
136	A	136	CYS	0	0.013	0.009	22.508	0.015	0.015	0.000	0.000	0.000	0.000
137	A	137	GLY	0	0.051	0.020	24.719	0.004	0.004	0.000	0.000	0.000	0.000
138	A	138	ILE	0	-0.021	-0.016	18.084	0.007	0.007	0.000	0.000	0.000	0.000
139	A	139	ALA	0	0.027	0.011	20.642	0.016	0.016	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.010	0.021	21.838	0.004	0.004	0.000	0.000	0.000	0.000
141	A	141	VAL	0	-0.014	0.000	19.847	-0.004	-0.004	0.000	0.000	0.000	0.000
142	A	142	ILE	0	-0.010	-0.019	16.639	0.003	0.003	0.000	0.000	0.000	0.000
143	A	143	SER	0	-0.022	-0.041	19.540	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	144	ASN	0	-0.040	-0.022	22.534	-0.012	-0.012	0.000	0.000	0.000	0.000
145	A	145	MET	0	-0.025	-0.002	18.250	0.006	0.006	0.000	0.000	0.000	0.000
146	A	146	LEU	0	-0.015	0.013	18.509	0.010	0.010	0.000	0.000	0.000	0.000
147	A	147	PRO	0	0.000	-0.001	19.757	-0.016	-0.016	0.000	0.000	0.000	0.000
148	A	148	ARG	1	0.845	0.921	22.872	-0.133	-0.133	0.000	0.000	0.000	0.000
149	A	149	ASN	0	0.028	0.022	26.706	0.001	0.001	0.000	0.000	0.000	0.000

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