FMO DATABASE

FMODB ID: 66L4Z

Calculation Name: 4EXW-A-Xray318

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4EXW

Chain ID: A

ChEMBL ID:

UniProt ID: Q1J1N6

Base Structure: X-ray

Registration Date: 2021-09-07

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:

Apendix: None

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	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1101173.592779
FMO2-HF: Nuclear repulsion	1049344.222396
FMO2-HF: Total energy	-51829.370383
FMO2-MP2: Total energy	-51982.625233

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:-5:GLY )

Summations of interaction energy for fragment #1(A:-5:GLY )

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.
1.025	1.97	-0.002	-0.338	-0.605	0

Interaction energy analysis for fragmet #1(A:-5:GLY )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.017 / q_NPA : -0.020

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].
3	A	-3	ASP	-1	-0.868	-0.934	3.799	0.096	1.041	-0.002	-0.338	-0.605
4	A	-2	PRO	0	-0.044	-0.026	6.460	0.183	0.183	0.000	0.000	0.000
5	A	-1	PHE	0	-0.031	-0.012	9.481	0.032	0.032	0.000	0.000	0.000
6	A	0	THR	0	0.000	0.014	10.160	-0.069	-0.069	0.000	0.000	0.000
7	A	1	MET	0	-0.001	-0.004	12.145	-0.012	-0.012	0.000	0.000	0.000
8	A	2	LEU	0	-0.046	-0.015	10.965	-0.038	-0.038	0.000	0.000	0.000
9	A	3	HIS	1	0.850	0.888	15.200	0.227	0.227	0.000	0.000	0.000
10	A	4	ILE	0	0.007	0.023	18.435	-0.022	-0.022	0.000	0.000	0.000
11	A	5	GLU	-1	-0.913	-0.955	20.069	-0.104	-0.104	0.000	0.000	0.000
12	A	6	PHE	0	0.005	-0.015	21.957	-0.002	-0.002	0.000	0.000	0.000
13	A	7	ILE	0	-0.027	-0.010	26.000	0.002	0.002	0.000	0.000	0.000
14	A	8	THR	0	-0.018	-0.013	29.541	0.002	0.002	0.000	0.000	0.000
15	A	9	ASP	-1	-0.834	-0.926	31.451	-0.036	-0.036	0.000	0.000	0.000
16	A	10	LEU	0	-0.059	-0.033	34.421	0.002	0.002	0.000	0.000	0.000
17	A	11	GLY	0	-0.025	-0.005	34.387	0.000	0.000	0.000	0.000	0.000
18	A	12	ALA	0	-0.032	-0.004	33.493	-0.003	-0.003	0.000	0.000	0.000
19	A	13	LYS	1	0.969	0.985	27.751	0.094	0.094	0.000	0.000	0.000
20	A	14	VAL	0	-0.001	0.000	27.282	0.001	0.001	0.000	0.000	0.000
21	A	15	THR	0	-0.008	-0.004	22.498	-0.009	-0.009	0.000	0.000	0.000
22	A	16	VAL	0	-0.025	-0.009	21.581	0.009	0.009	0.000	0.000	0.000
23	A	17	ASP	-1	-0.854	-0.908	20.115	-0.132	-0.132	0.000	0.000	0.000
24	A	18	VAL	0	-0.033	-0.025	15.252	0.020	0.020	0.000	0.000	0.000
25	A	19	GLU	-1	-0.867	-0.921	15.096	0.020	0.020	0.000	0.000	0.000
26	A	20	SER	0	0.060	0.019	10.834	-0.019	-0.019	0.000	0.000	0.000
27	A	21	ALA	0	0.033	0.000	8.166	0.019	0.019	0.000	0.000	0.000
28	A	22	ASP	-1	-0.898	-0.950	8.149	0.574	0.574	0.000	0.000	0.000
29	A	23	LYS	1	0.860	0.927	10.669	-0.061	-0.061	0.000	0.000	0.000
30	A	24	LEU	0	-0.003	0.008	12.999	-0.011	-0.011	0.000	0.000	0.000
31	A	25	LEU	0	0.006	-0.019	13.600	0.008	0.008	0.000	0.000	0.000
32	A	26	ASP	-1	-0.888	-0.941	16.002	0.060	0.060	0.000	0.000	0.000
33	A	27	VAL	0	-0.001	0.001	17.957	0.000	0.000	0.000	0.000	0.000
34	A	28	GLN	0	-0.014	-0.023	16.818	-0.014	-0.014	0.000	0.000	0.000
35	A	29	ARG	1	0.848	0.921	17.295	0.003	0.003	0.000	0.000	0.000
36	A	30	GLN	0	-0.020	0.004	22.236	0.007	0.007	0.000	0.000	0.000
37	A	31	TYR	0	-0.002	-0.010	23.344	0.004	0.004	0.000	0.000	0.000
38	A	32	GLY	0	0.066	0.048	24.418	-0.001	-0.001	0.000	0.000	0.000
39	A	33	ARG	1	0.835	0.899	24.330	0.012	0.012	0.000	0.000	0.000
40	A	34	LEU	0	-0.044	-0.011	28.235	0.004	0.004	0.000	0.000	0.000
41	A	35	GLY	0	-0.036	-0.004	29.339	0.001	0.001	0.000	0.000	0.000
42	A	36	TRP	0	-0.026	-0.004	26.832	-0.004	-0.004	0.000	0.000	0.000
43	A	37	THR	0	0.000	-0.005	26.080	0.000	0.000	0.000	0.000	0.000
44	A	38	SER	0	-0.053	-0.034	22.071	-0.007	-0.007	0.000	0.000	0.000
45	A	39	GLY	0	0.007	0.014	23.449	-0.007	-0.007	0.000	0.000	0.000
46	A	40	GLU	-1	-0.939	-0.970	24.602	-0.076	-0.076	0.000	0.000	0.000
47	A	41	VAL	0	-0.044	-0.021	25.517	-0.006	-0.006	0.000	0.000	0.000
48	A	42	PRO	0	-0.014	0.008	24.182	0.001	0.001	0.000	0.000	0.000
49	A	43	VAL	0	0.083	0.026	26.844	0.008	0.008	0.000	0.000	0.000
50	A	44	GLY	0	-0.018	-0.005	29.399	-0.001	-0.001	0.000	0.000	0.000
51	A	45	GLY	0	-0.010	0.000	28.737	0.004	0.004	0.000	0.000	0.000
52	A	46	TYR	0	0.009	-0.012	22.748	-0.002	-0.002	0.000	0.000	0.000
53	A	47	GLN	0	-0.041	-0.021	23.034	0.015	0.015	0.000	0.000	0.000
54	A	48	PHE	0	-0.009	0.000	20.371	-0.011	-0.011	0.000	0.000	0.000
55	A	49	PRO	0	0.015	-0.007	19.437	0.004	0.004	0.000	0.000	0.000
56	A	50	LEU	0	0.015	0.002	22.589	0.004	0.004	0.000	0.000	0.000
57	A	51	GLU	-1	-0.943	-0.976	23.634	0.002	0.002	0.000	0.000	0.000
58	A	52	ASN	0	-0.016	-0.033	20.543	0.000	0.000	0.000	0.000	0.000
59	A	53	GLU	-1	-0.814	-0.895	24.011	-0.016	-0.016	0.000	0.000	0.000
60	A	54	PRO	0	0.009	0.012	27.266	0.000	0.000	0.000	0.000	0.000
61	A	55	ASP	-1	-0.874	-0.942	25.093	0.012	0.012	0.000	0.000	0.000
62	A	56	PHE	0	0.019	0.011	21.517	0.001	0.001	0.000	0.000	0.000
63	A	57	ASP	-1	-0.777	-0.878	22.348	-0.009	-0.009	0.000	0.000	0.000
64	A	58	TRP	0	0.024	-0.006	23.799	-0.011	-0.011	0.000	0.000	0.000
65	A	59	SER	0	-0.057	-0.036	24.526	-0.006	-0.006	0.000	0.000	0.000
66	A	60	LEU	0	-0.010	-0.002	19.037	-0.007	-0.007	0.000	0.000	0.000
67	A	61	ILE	0	-0.044	-0.017	21.997	-0.013	-0.013	0.000	0.000	0.000
68	A	62	GLY	0	0.017	0.014	24.582	0.001	0.001	0.000	0.000	0.000
69	A	63	ALA	0	-0.082	-0.031	27.378	0.002	0.002	0.000	0.000	0.000
70	A	64	ARG	1	0.945	0.960	29.287	0.022	0.022	0.000	0.000	0.000
71	A	65	LYS	1	0.964	0.989	30.829	0.005	0.005	0.000	0.000	0.000
72	A	66	TRP	0	-0.035	-0.033	34.063	0.000	0.000	0.000	0.000	0.000
73	A	67	THR	0	0.042	0.019	37.772	-0.001	-0.001	0.000	0.000	0.000
74	A	68	ASN	0	-0.023	0.003	40.960	0.001	0.001	0.000	0.000	0.000
75	A	69	PRO	0	0.001	-0.004	43.875	0.001	0.001	0.000	0.000	0.000
76	A	70	GLU	-1	-0.921	-0.959	47.310	-0.012	-0.012	0.000	0.000	0.000
77	A	71	GLY	0	-0.026	-0.007	46.033	0.001	0.001	0.000	0.000	0.000
78	A	72	GLU	-1	-0.980	-0.990	41.777	-0.015	-0.015	0.000	0.000	0.000
79	A	73	GLU	-1	-0.864	-0.928	36.268	-0.010	-0.010	0.000	0.000	0.000
80	A	74	MET	0	-0.070	-0.030	37.729	-0.003	-0.003	0.000	0.000	0.000
81	A	75	ILE	0	-0.016	-0.005	31.259	0.001	0.001	0.000	0.000	0.000
82	A	76	LEU	0	-0.035	-0.023	34.323	-0.002	-0.002	0.000	0.000	0.000
83	A	77	HIS	0	0.014	-0.010	28.236	-0.003	-0.003	0.000	0.000	0.000
84	A	78	ARG	1	0.996	0.994	30.909	0.064	0.064	0.000	0.000	0.000
85	A	79	GLY	0	0.037	0.032	34.442	0.000	0.000	0.000	0.000	0.000
86	A	80	HIS	0	-0.082	-0.033	35.955	-0.001	-0.001	0.000	0.000	0.000
87	A	81	ALA	0	0.050	0.018	36.660	0.000	0.000	0.000	0.000	0.000
88	A	82	TYR	0	-0.069	-0.017	34.025	-0.001	-0.001	0.000	0.000	0.000
89	A	83	ARG	1	1.024	1.013	36.669	0.027	0.027	0.000	0.000	0.000
90	A	84	ARG	1	0.838	0.917	33.200	0.012	0.012	0.000	0.000	0.000
91	A	85	ARG	1	0.899	0.948	35.759	0.032	0.032	0.000	0.000	0.000
92	A	86	GLU	-1	-0.833	-0.919	35.413	-0.015	-0.015	0.000	0.000	0.000
93	A	87	LEU	0	-0.080	-0.053	34.230	-0.001	-0.001	0.000	0.000	0.000
94	A	88	GLU	-1	-0.842	-0.907	35.486	-0.016	-0.016	0.000	0.000	0.000
95	A	89	ALA	0	-0.053	-0.028	35.669	-0.002	-0.002	0.000	0.000	0.000
96	A	90	NME	0	-0.022	0.005	37.275	-0.001	-0.001	0.000	0.000	0.000
97	A	98	ACE	0	-0.030	-0.031	32.046	-0.001	-0.001	0.000	0.000	0.000
98	A	99	ALA	0	0.071	0.023	32.168	0.003	0.003	0.000	0.000	0.000
99	A	100	ALA	0	-0.084	-0.038	30.843	-0.003	-0.003	0.000	0.000	0.000
100	A	101	VAL	0	0.033	0.035	30.636	0.003	0.003	0.000	0.000	0.000
101	A	102	LYS	1	0.885	0.953	30.887	0.038	0.038	0.000	0.000	0.000
102	A	103	TYR	0	0.048	0.029	30.522	0.004	0.004	0.000	0.000	0.000
103	A	104	SER	0	-0.054	-0.045	33.213	-0.004	-0.004	0.000	0.000	0.000
104	A	105	ARG	1	0.905	0.964	35.927	0.045	0.045	0.000	0.000	0.000
105	A	106	GLY	0	-0.002	0.002	39.092	-0.002	-0.002	0.000	0.000	0.000
106	A	107	ALA	0	0.022	0.020	40.996	-0.001	-0.001	0.000	0.000	0.000
107	A	108	LYS	1	0.816	0.891	39.250	0.043	0.043	0.000	0.000	0.000
108	A	109	ASN	0	0.004	0.004	44.388	-0.001	-0.001	0.000	0.000	0.000
109	A	110	THR	0	0.012	-0.001	42.433	-0.001	-0.001	0.000	0.000	0.000
110	A	111	ASP	-1	-0.822	-0.933	38.412	-0.047	-0.047	0.000	0.000	0.000
111	A	112	PRO	0	-0.015	0.025	38.317	0.002	0.002	0.000	0.000	0.000
112	A	113	GLU	-1	-0.894	-0.942	37.681	-0.051	-0.051	0.000	0.000	0.000
113	A	114	NME	0	-0.038	-0.016	34.789	-0.001	-0.001	0.000	0.000	0.000
114	A	123	ACE	0	-0.052	-0.039	45.612	0.000	0.000	0.000	0.000	0.000
115	A	124	GLU	-1	-0.854	-0.922	41.780	-0.038	-0.038	0.000	0.000	0.000
116	A	125	TYR	0	-0.081	-0.047	39.059	0.002	0.002	0.000	0.000	0.000
117	A	126	VAL	0	0.123	0.077	34.729	-0.002	-0.002	0.000	0.000	0.000
118	A	127	THR	0	-0.118	-0.091	31.803	0.002	0.002	0.000	0.000	0.000
119	A	128	LEU	0	0.027	0.032	29.056	-0.003	-0.003	0.000	0.000	0.000
120	A	129	ALA	0	0.016	-0.010	27.056	-0.007	-0.007	0.000	0.000	0.000
121	A	130	ILE	0	-0.045	-0.024	27.453	0.008	0.008	0.000	0.000	0.000
122	A	131	PHE	0	0.009	0.012	24.690	-0.006	-0.006	0.000	0.000	0.000
123	A	132	ARG	1	1.011	0.979	26.044	0.058	0.058	0.000	0.000	0.000
124	A	133	GLY	0	0.016	0.027	25.309	-0.006	-0.006	0.000	0.000	0.000
125	A	134	GLY	0	0.012	0.012	21.657	0.000	0.000	0.000	0.000	0.000
126	A	135	LYS	1	0.995	1.004	14.817	0.071	0.071	0.000	0.000	0.000
127	A	136	ARG	1	0.910	0.954	19.212	-0.031	-0.031	0.000	0.000	0.000
128	A	137	GLN	0	-0.050	-0.028	14.158	-0.024	-0.024	0.000	0.000	0.000
129	A	138	GLU	-1	-0.840	-0.933	16.311	0.046	0.046	0.000	0.000	0.000
130	A	139	ARG	1	0.916	0.970	12.326	0.140	0.140	0.000	0.000	0.000
131	A	140	TYR	0	-0.029	-0.023	16.142	-0.019	-0.019	0.000	0.000	0.000
132	A	141	ALA	0	0.042	0.041	19.118	-0.004	-0.004	0.000	0.000	0.000
133	A	142	VAL	0	-0.031	-0.014	21.062	0.001	0.001	0.000	0.000	0.000
134	A	143	PRO	0	-0.032	-0.014	20.775	0.007	0.007	0.000	0.000	0.000
135	A	144	NME	0	0.022	0.026	22.844	-0.004	-0.004	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-5:GLY )