FMO DATABASE

FMODB ID: P3N1L

Calculation Name: 3EUR-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EUR

Chain ID: A

ChEMBL ID:

UniProt ID: Q5LF10

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	141
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1360404.307018
FMO2-HF: Nuclear repulsion	1304915.045974
FMO2-HF: Total energy	-55489.261044
FMO2-MP2: Total energy	-55653.352008

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:ACE)

Summations of interaction energy for fragment #1(A:-1: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.
1.731	3.211	0	-0.604	-0.874	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.040 / q_NPA : 0.011

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].
3	A	1	LYS	1	0.981	0.989	3.805	1.535	2.582	-0.013	-0.497	-0.536
4	A	2	ASN	0	0.069	0.029	5.158	0.348	0.348	0.000	0.000	0.000
5	A	3	ARG	1	0.938	0.987	6.626	1.022	1.022	0.000	0.000	0.000
6	A	4	LEU	0	0.058	0.025	8.178	0.004	0.004	0.000	0.000	0.000
7	A	5	GLY	0	0.031	0.018	10.000	-0.108	-0.108	0.000	0.000	0.000
8	A	6	THR	0	-0.086	-0.044	4.622	-0.247	-0.221	-0.001	-0.007	-0.017
9	A	7	LYS	1	0.926	0.976	4.727	-0.658	-0.602	-0.001	-0.007	-0.048
10	A	8	ALA	0	0.041	0.027	4.337	0.122	0.226	-0.001	-0.016	-0.087
11	A	9	LEU	0	0.000	0.010	3.573	0.211	0.458	0.016	-0.077	-0.186
12	A	10	ASN	0	0.037	0.025	6.421	-0.425	-0.425	0.000	0.000	0.000
13	A	11	PHE	0	0.003	-0.009	9.344	0.013	0.013	0.000	0.000	0.000
14	A	12	THR	0	0.025	0.005	12.401	-0.001	-0.001	0.000	0.000	0.000
15	A	13	TYR	0	0.010	0.022	16.050	-0.014	-0.014	0.000	0.000	0.000
16	A	14	THR	0	-0.029	-0.011	18.806	0.001	0.001	0.000	0.000	0.000
17	A	15	LEU	0	0.031	0.016	22.485	-0.008	-0.008	0.000	0.000	0.000
18	A	16	ASP	-1	-0.838	-0.925	25.267	0.069	0.069	0.000	0.000	0.000
19	A	17	SER	0	0.014	0.010	28.636	0.000	0.000	0.000	0.000	0.000
20	A	18	GLY	0	0.006	0.006	27.283	-0.003	-0.003	0.000	0.000	0.000
21	A	19	VAL	0	-0.021	-0.009	24.323	0.008	0.008	0.000	0.000	0.000
22	A	20	LYS	1	0.899	0.946	20.977	-0.157	-0.157	0.000	0.000	0.000
23	A	21	GLY	0	0.032	0.026	19.530	-0.008	-0.008	0.000	0.000	0.000
24	A	22	THR	0	-0.014	-0.003	14.033	0.028	0.028	0.000	0.000	0.000
25	A	23	LEU	0	0.051	0.023	10.006	-0.025	-0.025	0.000	0.000	0.000
26	A	24	TYR	0	-0.088	-0.089	6.131	0.093	0.093	0.000	0.000	0.000
27	A	25	GLN	0	-0.027	-0.009	12.796	-0.042	-0.042	0.000	0.000	0.000
28	A	26	PHE	0	0.008	0.026	15.911	-0.033	-0.033	0.000	0.000	0.000
29	A	27	PRO	0	-0.023	0.002	17.085	0.006	0.006	0.000	0.000	0.000
30	A	28	ALA	0	0.030	-0.012	18.660	-0.013	-0.013	0.000	0.000	0.000
31	A	29	GLU	-1	-0.878	-0.915	18.319	0.048	0.048	0.000	0.000	0.000
32	A	30	TYR	0	0.034	0.018	17.877	-0.001	-0.001	0.000	0.000	0.000
33	A	31	THR	0	-0.029	-0.026	15.342	0.016	0.016	0.000	0.000	0.000
34	A	32	LEU	0	0.012	0.008	16.507	-0.008	-0.008	0.000	0.000	0.000
35	A	33	LEU	0	-0.025	-0.008	12.719	0.012	0.012	0.000	0.000	0.000
36	A	34	PHE	0	0.038	-0.001	16.628	-0.020	-0.020	0.000	0.000	0.000
37	A	35	ILE	0	-0.002	0.000	13.959	0.013	0.013	0.000	0.000	0.000
38	A	36	ASN	0	0.028	-0.011	18.532	-0.022	-0.022	0.000	0.000	0.000
39	A	37	ASN	0	0.051	-0.005	21.941	0.009	0.009	0.000	0.000	0.000
40	A	38	PRO	0	0.009	-0.024	24.276	-0.007	-0.007	0.000	0.000	0.000
41	A	39	GLY	0	0.015	0.038	27.480	-0.003	-0.003	0.000	0.000	0.000
42	A	40	CYS	0	-0.058	-0.034	26.493	-0.005	-0.005	0.000	0.000	0.000
43	A	41	HIS	0	0.065	0.024	29.675	0.002	0.002	0.000	0.000	0.000
44	A	42	ALA	0	0.036	0.028	27.162	0.000	0.000	0.000	0.000	0.000
45	A	43	CYS	0	-0.008	0.000	26.030	0.003	0.003	0.000	0.000	0.000
46	A	44	ALA	0	0.006	0.015	27.231	0.003	0.003	0.000	0.000	0.000
47	A	45	GLU	-1	-0.863	-0.941	30.516	0.006	0.006	0.000	0.000	0.000
48	A	46	MET	0	-0.045	-0.007	22.575	0.001	0.001	0.000	0.000	0.000
49	A	47	ILE	0	-0.043	-0.028	27.256	0.003	0.003	0.000	0.000	0.000
50	A	48	GLU	-1	-0.887	-0.946	28.471	0.017	0.017	0.000	0.000	0.000
51	A	49	GLY	0	0.013	0.004	29.512	-0.001	-0.001	0.000	0.000	0.000
52	A	50	LEU	0	-0.078	-0.052	23.794	0.000	0.000	0.000	0.000	0.000
53	A	51	LYS	1	0.864	0.935	27.858	-0.028	-0.028	0.000	0.000	0.000
54	A	52	ALA	0	0.029	0.034	30.971	0.000	0.000	0.000	0.000	0.000
55	A	53	SER	0	-0.050	-0.032	28.985	-0.001	-0.001	0.000	0.000	0.000
56	A	54	PRO	0	0.040	0.010	30.913	0.003	0.003	0.000	0.000	0.000
57	A	55	VAL	0	0.027	0.019	26.921	0.003	0.003	0.000	0.000	0.000
58	A	56	ILE	0	0.016	-0.003	24.541	0.004	0.004	0.000	0.000	0.000
59	A	57	ASN	0	-0.056	-0.039	27.304	0.009	0.009	0.000	0.000	0.000
60	A	58	GLY	0	0.023	0.027	30.268	0.003	0.003	0.000	0.000	0.000
61	A	59	PHE	0	0.009	-0.011	24.439	0.005	0.005	0.000	0.000	0.000
62	A	60	THR	0	-0.045	-0.025	25.524	0.005	0.005	0.000	0.000	0.000
63	A	61	ALA	0	-0.012	0.004	27.524	0.005	0.005	0.000	0.000	0.000
64	A	62	ALA	0	-0.027	-0.015	28.913	0.002	0.002	0.000	0.000	0.000
65	A	63	LYS	1	0.879	0.938	27.216	-0.045	-0.045	0.000	0.000	0.000
66	A	64	LYS	1	0.882	0.955	24.201	-0.018	-0.018	0.000	0.000	0.000
67	A	65	LEU	0	0.003	0.003	21.267	0.007	0.007	0.000	0.000	0.000
68	A	66	LYS	1	0.916	0.956	21.119	-0.089	-0.089	0.000	0.000	0.000
69	A	67	VAL	0	0.044	0.028	20.372	0.006	0.006	0.000	0.000	0.000
70	A	68	LEU	0	-0.037	-0.009	15.927	0.007	0.007	0.000	0.000	0.000
71	A	69	SER	0	-0.006	0.005	18.798	0.001	0.001	0.000	0.000	0.000
72	A	70	ILE	0	-0.035	-0.025	15.850	0.012	0.012	0.000	0.000	0.000
73	A	71	TYR	0	0.029	0.019	19.266	-0.009	-0.009	0.000	0.000	0.000
74	A	72	PRO	0	-0.016	-0.023	16.942	0.016	0.016	0.000	0.000	0.000
75	A	73	ASP	-1	-0.803	-0.875	18.749	0.062	0.062	0.000	0.000	0.000
76	A	74	GLU	-1	-0.779	-0.886	21.759	0.076	0.076	0.000	0.000	0.000
77	A	75	GLU	-1	-0.909	-0.941	24.704	0.048	0.048	0.000	0.000	0.000
78	A	76	LEU	0	-0.069	-0.037	25.753	0.000	0.000	0.000	0.000	0.000
79	A	77	ASP	-1	-0.847	-0.931	27.779	0.054	0.054	0.000	0.000	0.000
80	A	78	GLU	-1	-0.900	-0.954	29.706	0.033	0.033	0.000	0.000	0.000
81	A	79	TRP	0	0.002	-0.012	24.708	-0.001	-0.001	0.000	0.000	0.000
82	A	80	LYS	1	0.808	0.878	28.378	-0.077	-0.077	0.000	0.000	0.000
83	A	81	LYS	1	0.920	0.977	30.832	-0.031	-0.031	0.000	0.000	0.000
84	A	82	HIS	1	0.868	0.932	29.811	-0.038	-0.038	0.000	0.000	0.000
85	A	83	ARG	1	0.948	0.994	29.226	-0.061	-0.061	0.000	0.000	0.000
86	A	84	ASN	0	-0.062	-0.047	30.201	0.003	0.003	0.000	0.000	0.000
87	A	85	ASP	-1	-0.832	-0.895	30.655	0.032	0.032	0.000	0.000	0.000
88	A	86	PHE	0	-0.103	-0.046	25.000	-0.002	-0.002	0.000	0.000	0.000
89	A	87	ALA	0	0.031	0.019	28.866	-0.001	-0.001	0.000	0.000	0.000
90	A	88	LYS	1	0.940	0.970	28.862	-0.034	-0.034	0.000	0.000	0.000
91	A	89	GLU	-1	-0.899	-0.964	28.887	0.050	0.050	0.000	0.000	0.000
92	A	90	TRP	0	-0.061	-0.018	24.542	0.007	0.007	0.000	0.000	0.000
93	A	91	THR	0	-0.059	-0.023	21.675	0.004	0.004	0.000	0.000	0.000
94	A	92	ASN	0	0.047	0.011	22.288	0.006	0.006	0.000	0.000	0.000
95	A	93	GLY	0	0.004	-0.004	21.634	-0.001	-0.001	0.000	0.000	0.000
96	A	94	TYR	0	0.012	0.008	21.121	-0.005	-0.005	0.000	0.000	0.000
97	A	95	ASP	-1	-0.725	-0.877	15.949	0.240	0.240	0.000	0.000	0.000
98	A	96	LYS	1	0.898	0.961	18.992	-0.135	-0.135	0.000	0.000	0.000
99	A	97	GLU	-1	-0.923	-0.984	17.856	0.200	0.200	0.000	0.000	0.000
100	A	98	LEU	0	0.027	0.038	18.118	0.000	0.000	0.000	0.000	0.000
101	A	99	VAL	0	-0.023	-0.024	12.154	0.010	0.010	0.000	0.000	0.000
102	A	100	ILE	0	-0.029	-0.022	12.045	0.028	0.028	0.000	0.000	0.000
103	A	101	LYS	1	0.832	0.892	12.705	-0.082	-0.082	0.000	0.000	0.000
104	A	102	ASN	0	-0.014	-0.003	14.724	-0.027	-0.027	0.000	0.000	0.000
105	A	103	LYS	1	0.889	0.940	10.097	-0.477	-0.477	0.000	0.000	0.000
106	A	104	ASN	0	-0.033	-0.002	9.800	0.004	0.004	0.000	0.000	0.000
107	A	105	LEU	0	-0.051	-0.017	7.133	-0.008	-0.008	0.000	0.000	0.000
108	A	106	TYR	0	-0.048	-0.055	8.055	-0.029	-0.029	0.000	0.000	0.000
109	A	107	ASP	-1	-0.849	-0.892	10.808	-0.113	-0.113	0.000	0.000	0.000
110	A	108	LEU	0	0.045	0.005	13.434	0.010	0.010	0.000	0.000	0.000
111	A	109	ARG	1	0.811	0.879	15.917	0.112	0.112	0.000	0.000	0.000
112	A	110	ALA	0	0.012	0.015	18.709	0.002	0.002	0.000	0.000	0.000
113	A	111	ILE	0	-0.025	0.044	17.345	0.002	0.002	0.000	0.000	0.000
114	A	112	PRO	0	-0.060	-0.054	20.815	-0.002	-0.002	0.000	0.000	0.000
115	A	113	THR	0	0.021	0.016	16.381	-0.006	-0.006	0.000	0.000	0.000
116	A	114	LEU	0	-0.006	0.005	18.009	0.023	0.023	0.000	0.000	0.000
117	A	115	TYR	0	-0.015	-0.014	10.791	-0.042	-0.042	0.000	0.000	0.000
118	A	116	LEU	0	0.018	0.025	15.001	0.026	0.026	0.000	0.000	0.000
119	A	117	LEU	0	-0.025	-0.015	10.767	-0.015	-0.015	0.000	0.000	0.000
120	A	118	ASP	-1	-0.724	-0.875	13.122	0.078	0.078	0.000	0.000	0.000
121	A	119	LYS	1	1.006	1.004	14.394	-0.045	-0.045	0.000	0.000	0.000
122	A	120	ASN	0	-0.114	-0.053	11.830	0.043	0.043	0.000	0.000	0.000
123	A	121	LYS	1	0.818	0.900	9.744	-0.143	-0.143	0.000	0.000	0.000
124	A	122	THR	0	0.000	0.009	8.875	0.059	0.059	0.000	0.000	0.000
125	A	123	VAL	0	-0.055	-0.020	8.289	0.013	0.013	0.000	0.000	0.000
126	A	124	LEU	0	0.009	0.009	10.716	-0.060	-0.060	0.000	0.000	0.000
127	A	125	LEU	0	-0.006	-0.006	14.339	-0.023	-0.023	0.000	0.000	0.000
128	A	126	LYS	1	0.876	0.935	10.009	0.383	0.383	0.000	0.000	0.000
129	A	127	ASP	-1	-0.958	-0.988	13.792	-0.095	-0.095	0.000	0.000	0.000
130	A	128	ALA	0	0.012	0.030	16.424	-0.009	-0.009	0.000	0.000	0.000
131	A	129	THR	0	0.072	0.022	19.202	0.014	0.014	0.000	0.000	0.000
132	A	130	LEU	0	0.043	0.012	22.586	0.000	0.000	0.000	0.000	0.000
133	A	131	GLN	0	0.037	0.016	24.525	-0.004	-0.004	0.000	0.000	0.000
134	A	132	LYS	1	0.932	0.979	20.514	0.081	0.081	0.000	0.000	0.000
135	A	133	VAL	0	0.004	-0.008	19.858	-0.002	-0.002	0.000	0.000	0.000
136	A	134	GLU	-1	-0.851	-0.913	22.307	-0.007	-0.007	0.000	0.000	0.000
137	A	135	GLN	0	-0.025	-0.017	25.225	0.000	0.000	0.000	0.000	0.000
138	A	136	TYR	0	-0.010	-0.012	18.416	-0.006	-0.006	0.000	0.000	0.000
139	A	137	LEU	0	-0.035	-0.026	21.538	0.003	0.003	0.000	0.000	0.000
140	A	138	ALA	0	-0.087	-0.038	24.431	0.004	0.004	0.000	0.000	0.000
141	A	139	GLU	-2	-1.928	-1.940	23.808	-0.080	-0.080	0.000	0.000	0.000

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