FMO DATABASE

FMODB ID: 7JR5K

Calculation Name: 1X8Z-A-Xray310

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: 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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	150
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1209538.887243
FMO2-HF: Nuclear repulsion	1150065.124719
FMO2-HF: Total energy	-59473.762524
FMO2-MP2: Total energy	-59640.122726

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:-2:ACE )

Summations of interaction energy for fragment #1(A:-2:ACE )

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.
-0.16	-3.733	10.004	-2.911	-3.519	-0.038

Interaction energy analysis for fragmet #1(A:-2:ACE )

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 : -0.029

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	0	ASP	-1	-0.876	-0.924	3.803	-0.079	0.844	-0.008	-0.401	-0.514	0.000
4	A	1	SER	0	0.020	-0.008	7.033	0.025	0.025	0.000	0.000	0.000	0.000
5	A	2	SER	0	0.019	0.027	8.519	0.022	0.022	0.000	0.000	0.000	0.000
6	A	3	GLU	-1	-0.862	-0.905	9.691	-0.925	-0.925	0.000	0.000	0.000	0.000
7	A	4	MET	0	-0.013	-0.012	5.143	0.250	0.250	0.000	0.000	0.000	0.000
8	A	5	SER	0	0.012	-0.011	10.058	0.128	0.128	0.000	0.000	0.000	0.000
9	A	6	THR	0	-0.062	-0.047	13.146	0.072	0.072	0.000	0.000	0.000	0.000
10	A	7	ILE	0	-0.033	-0.010	11.788	0.067	0.067	0.000	0.000	0.000	0.000
11	A	17	CYS	0	0.018	0.018	13.148	0.004	0.004	0.000	0.000	0.000	0.000
12	A	9	ASP	-1	-0.901	-0.931	15.359	-0.183	-0.183	0.000	0.000	0.000	0.000
13	A	10	LYS	1	0.853	0.910	18.088	0.313	0.313	0.000	0.000	0.000	0.000
14	A	11	THR	0	-0.054	-0.013	17.456	0.013	0.013	0.000	0.000	0.000	0.000
15	A	12	LEU	0	-0.012	-0.019	20.208	0.011	0.011	0.000	0.000	0.000	0.000
16	A	13	ASN	0	0.012	-0.013	20.079	0.016	0.016	0.000	0.000	0.000	0.000
17	A	14	PRO	0	0.077	0.047	16.928	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	15	SER	0	0.023	0.021	15.409	-0.024	-0.024	0.000	0.000	0.000	0.000
19	A	16	PHE	0	-0.022	-0.005	15.004	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	18	LEU	0	0.083	0.020	10.605	-0.088	-0.088	0.000	0.000	0.000	0.000
21	A	19	LYS	1	0.935	0.974	10.121	0.016	0.016	0.000	0.000	0.000	0.000
22	A	20	PHE	0	-0.047	-0.014	10.770	0.012	0.012	0.000	0.000	0.000	0.000
23	A	21	LEU	0	0.064	0.009	8.309	0.008	0.008	0.000	0.000	0.000	0.000
24	A	22	ASN	0	0.081	0.031	5.838	-0.511	-0.511	0.000	0.000	0.000	0.000
25	A	23	THR	0	-0.138	-0.068	5.932	0.250	0.250	0.000	0.000	0.000	0.000
26	A	24	LYS	1	0.857	0.927	7.813	0.450	0.450	0.000	0.000	0.000	0.000
27	A	25	PHE	0	-0.029	0.000	3.873	0.261	0.464	0.004	-0.065	-0.141	0.000
28	A	26	ALA	0	0.049	0.039	2.825	-1.954	-2.523	1.761	-0.491	-0.701	-0.014
29	A	27	SER	0	0.013	-0.003	2.542	2.458	0.459	8.063	-3.851	-2.212	-0.022
30	A	28	PRO	0	-0.027	-0.004	3.090	-0.435	-2.566	0.184	1.897	0.049	-0.002
31	A	29	ASN	0	0.054	0.037	5.955	-0.168	-0.168	0.000	0.000	0.000	0.000
32	A	30	LEU	0	0.089	0.014	9.489	-0.047	-0.047	0.000	0.000	0.000	0.000
33	A	31	GLN	0	0.040	0.015	12.648	-0.055	-0.055	0.000	0.000	0.000	0.000
34	A	32	ALA	0	-0.018	-0.006	9.459	-0.057	-0.057	0.000	0.000	0.000	0.000
35	A	33	LEU	0	-0.003	0.005	8.490	-0.066	-0.066	0.000	0.000	0.000	0.000
36	A	34	ALA	0	0.046	0.033	11.602	-0.084	-0.084	0.000	0.000	0.000	0.000
37	A	35	LYS	1	0.852	0.898	13.984	-0.193	-0.193	0.000	0.000	0.000	0.000
38	A	36	THR	0	-0.016	0.000	11.498	-0.062	-0.062	0.000	0.000	0.000	0.000
39	A	37	THR	0	-0.033	-0.036	14.105	-0.049	-0.049	0.000	0.000	0.000	0.000
40	A	38	LEU	0	0.054	0.027	16.364	-0.035	-0.035	0.000	0.000	0.000	0.000
41	A	39	ASP	-1	-0.801	-0.863	16.890	0.103	0.103	0.000	0.000	0.000	0.000
42	A	40	SER	0	-0.065	-0.040	16.697	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	41	THR	0	-0.023	-0.028	19.242	-0.017	-0.017	0.000	0.000	0.000	0.000
44	A	42	GLN	0	0.057	0.029	21.819	-0.023	-0.023	0.000	0.000	0.000	0.000
45	A	43	ALA	0	-0.025	0.003	21.973	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	44	ARG	1	0.884	0.946	21.715	-0.057	-0.057	0.000	0.000	0.000	0.000
47	A	45	ALA	0	0.071	0.027	25.060	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	46	THR	0	0.029	0.013	27.043	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	47	GLN	0	-0.081	-0.047	24.343	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	48	THR	0	-0.025	-0.020	29.063	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	49	LEU	0	0.057	0.045	31.364	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	50	LYS	1	0.951	0.970	30.838	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	51	LYS	1	0.860	0.940	33.623	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	52	LEU	0	0.006	-0.003	35.168	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	53	GLN	0	0.081	0.034	37.342	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	54	SER	0	-0.034	0.009	38.125	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	55	ILE	0	-0.062	-0.038	37.523	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	56	ILE	0	-0.041	-0.019	41.238	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	57	ASP	-1	-0.934	-0.967	42.570	0.014	0.014	0.000	0.000	0.000	0.000
60	A	58	GLY	0	-0.082	-0.026	44.079	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	59	GLY	0	-0.058	-0.015	45.838	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	60	VAL	0	-0.006	-0.010	44.451	0.000	0.000	0.000	0.000	0.000	0.000
63	A	61	ASP	-1	-0.869	-0.940	47.870	0.015	0.015	0.000	0.000	0.000	0.000
64	A	62	PRO	0	0.018	-0.018	49.097	0.001	0.001	0.000	0.000	0.000	0.000
65	A	63	ARG	1	0.908	0.957	47.156	-0.017	-0.017	0.000	0.000	0.000	0.000
66	A	64	SER	0	0.010	0.003	44.851	0.002	0.002	0.000	0.000	0.000	0.000
67	A	65	LYS	1	0.920	0.961	44.688	-0.014	-0.014	0.000	0.000	0.000	0.000
68	A	66	LEU	0	-0.032	0.001	45.324	0.001	0.001	0.000	0.000	0.000	0.000
69	A	67	ALA	0	0.057	0.032	42.585	0.001	0.001	0.000	0.000	0.000	0.000
70	A	68	TYR	0	0.038	-0.009	38.841	0.002	0.002	0.000	0.000	0.000	0.000
71	A	69	ARG	1	0.960	0.975	40.399	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	70	SER	0	0.046	0.044	41.257	0.000	0.000	0.000	0.000	0.000	0.000
73	A	111	CYS	0	-0.048	0.003	34.259	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	72	VAL	0	-0.052	-0.025	36.689	0.003	0.003	0.000	0.000	0.000	0.000
75	A	73	ASP	-1	-0.859	-0.917	37.148	0.035	0.035	0.000	0.000	0.000	0.000
76	A	74	GLU	-1	-0.930	-0.966	35.596	0.051	0.051	0.000	0.000	0.000	0.000
77	A	75	TYR	0	-0.067	-0.092	29.592	0.007	0.007	0.000	0.000	0.000	0.000
78	A	76	GLU	-1	-0.950	-0.965	32.675	0.039	0.039	0.000	0.000	0.000	0.000
79	A	77	SER	0	0.016	0.016	33.906	0.003	0.003	0.000	0.000	0.000	0.000
80	A	78	ALA	0	-0.045	-0.018	29.988	0.006	0.006	0.000	0.000	0.000	0.000
81	A	79	ILE	0	-0.048	-0.030	28.926	0.007	0.007	0.000	0.000	0.000	0.000
82	A	80	GLY	0	0.067	0.044	28.968	0.005	0.005	0.000	0.000	0.000	0.000
83	A	81	ASN	0	0.017	-0.003	29.395	0.006	0.006	0.000	0.000	0.000	0.000
84	A	82	LEU	0	-0.042	-0.040	24.253	0.011	0.011	0.000	0.000	0.000	0.000
85	A	83	GLU	-1	-0.945	-0.961	25.159	0.073	0.073	0.000	0.000	0.000	0.000
86	A	84	GLU	-1	-0.887	-0.952	26.262	0.082	0.082	0.000	0.000	0.000	0.000
87	A	85	ALA	0	-0.039	-0.031	23.982	0.009	0.009	0.000	0.000	0.000	0.000
88	A	86	PHE	0	-0.072	-0.030	18.805	0.022	0.022	0.000	0.000	0.000	0.000
89	A	87	GLU	-1	-0.922	-0.951	22.543	0.096	0.096	0.000	0.000	0.000	0.000
90	A	88	HIS	0	-0.038	-0.026	24.333	0.002	0.002	0.000	0.000	0.000	0.000
91	A	89	LEU	0	-0.019	-0.008	16.763	0.018	0.018	0.000	0.000	0.000	0.000
92	A	90	ALA	0	-0.059	-0.013	20.064	0.022	0.022	0.000	0.000	0.000	0.000
93	A	91	SER	0	-0.038	-0.036	21.303	0.001	0.001	0.000	0.000	0.000	0.000
94	A	92	GLY	0	-0.020	0.013	20.701	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	93	ASP	-1	-0.826	-0.904	21.704	0.138	0.138	0.000	0.000	0.000	0.000
96	A	94	GLY	0	0.002	-0.015	22.301	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	95	MET	0	-0.019	-0.005	22.930	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	96	GLY	0	0.046	0.011	26.523	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	97	MET	0	-0.058	-0.029	18.825	0.002	0.002	0.000	0.000	0.000	0.000
100	A	98	ASN	0	-0.035	-0.011	23.782	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	99	MET	0	-0.017	0.002	25.379	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.996	0.991	27.213	-0.094	-0.094	0.000	0.000	0.000	0.000
103	A	101	VAL	0	0.005	-0.005	22.709	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	102	SER	0	-0.033	-0.021	26.089	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	103	ALA	0	0.030	0.028	28.437	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	104	ALA	0	-0.006	-0.001	27.285	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	105	LEU	0	-0.069	-0.028	26.060	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	106	ASP	-1	-0.861	-0.928	28.610	0.073	0.073	0.000	0.000	0.000	0.000
109	A	107	GLY	0	0.082	0.044	32.267	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	108	ALA	0	-0.058	-0.042	29.180	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	109	ASP	-1	-0.893	-0.966	31.215	0.057	0.057	0.000	0.000	0.000	0.000
112	A	110	THR	0	0.054	0.036	32.780	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	112	LEU	0	-0.081	-0.058	31.422	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	113	ASP	-1	-0.882	-0.940	35.668	0.042	0.042	0.000	0.000	0.000	0.000
115	A	114	ASP	-1	-0.888	-0.945	38.693	0.035	0.035	0.000	0.000	0.000	0.000
116	A	115	VAL	0	-0.032	-0.032	37.150	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	116	LYS	1	0.878	0.954	38.949	-0.039	-0.039	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.860	0.928	40.432	-0.028	-0.028	0.000	0.000	0.000	0.000
119	A	118	LEU	0	0.036	0.014	41.896	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	119	ARG	1	0.900	0.951	43.757	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	120	SER	0	-0.022	-0.005	42.836	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	121	VAL	0	0.049	0.028	38.141	0.001	0.001	0.000	0.000	0.000	0.000
123	A	122	ASP	-1	-0.777	-0.887	36.221	0.014	0.014	0.000	0.000	0.000	0.000
124	A	123	SER	0	0.032	-0.001	33.761	0.002	0.002	0.000	0.000	0.000	0.000
125	A	124	SER	0	-0.038	-0.002	31.368	0.003	0.003	0.000	0.000	0.000	0.000
126	A	125	VAL	0	0.073	0.027	31.274	0.004	0.004	0.000	0.000	0.000	0.000
127	A	126	VAL	0	0.007	0.020	32.331	0.005	0.005	0.000	0.000	0.000	0.000
128	A	127	ASN	0	-0.044	-0.041	28.312	0.002	0.002	0.000	0.000	0.000	0.000
129	A	128	ASN	0	0.085	0.037	27.244	0.008	0.008	0.000	0.000	0.000	0.000
130	A	129	SER	0	0.076	0.048	27.326	0.008	0.008	0.000	0.000	0.000	0.000
131	A	130	LYS	1	0.931	0.966	27.977	-0.035	-0.035	0.000	0.000	0.000	0.000
132	A	131	THR	0	-0.073	-0.033	22.454	0.008	0.008	0.000	0.000	0.000	0.000
133	A	132	ILE	0	0.021	0.004	23.352	0.013	0.013	0.000	0.000	0.000	0.000
134	A	133	LYS	1	0.883	0.954	24.398	-0.059	-0.059	0.000	0.000	0.000	0.000
135	A	134	ASN	0	-0.022	-0.009	21.456	0.012	0.012	0.000	0.000	0.000	0.000
136	A	135	LEU	0	-0.046	-0.023	18.426	0.017	0.017	0.000	0.000	0.000	0.000
137	A	136	CYS	0	0.012	0.004	20.143	0.021	0.021	0.000	0.000	0.000	0.000
138	A	137	GLY	0	0.056	0.032	22.301	0.009	0.009	0.000	0.000	0.000	0.000
139	A	138	ILE	0	-0.028	-0.017	15.516	0.016	0.016	0.000	0.000	0.000	0.000
140	A	139	ALA	0	-0.004	-0.005	18.212	0.029	0.029	0.000	0.000	0.000	0.000
141	A	140	LEU	0	0.017	0.024	19.345	0.016	0.016	0.000	0.000	0.000	0.000
142	A	141	VAL	0	-0.009	0.009	17.598	0.005	0.005	0.000	0.000	0.000	0.000
143	A	142	ILE	0	0.017	-0.009	14.009	0.011	0.011	0.000	0.000	0.000	0.000
144	A	143	SER	0	-0.024	-0.023	17.169	0.000	0.000	0.000	0.000	0.000	0.000
145	A	144	ASN	0	-0.021	-0.026	20.126	-0.015	-0.015	0.000	0.000	0.000	0.000
146	A	145	MET	0	-0.058	-0.032	15.512	0.012	0.012	0.000	0.000	0.000	0.000
147	A	146	LEU	0	-0.057	-0.001	17.051	0.029	0.029	0.000	0.000	0.000	0.000
148	A	147	PRO	0	-0.041	-0.024	17.766	-0.021	-0.021	0.000	0.000	0.000	0.000
149	A	148	ARG	1	0.877	0.950	20.878	-0.201	-0.201	0.000	0.000	0.000	0.000
150	A	149	ASN	-1	-0.913	-0.943	24.619	0.153	0.153	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:ACE )