FMO DATABASE

FMODB ID: P894Y

Calculation Name: 2OXG-A-Xray19

Preferred Name:

Target Type:

Ligand Name: 1,2-ethanediol

ligand 3-letter code: EDO

PDB ID: 2OXG

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LCU9

Base Structure: X-ray

Registration Date: 2018-06-04

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	Apo structure with with a 3 angstrom solvent shell.
Procedure	Auto-FMO protocol ver. 1.20180227

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	116
LigandCharge	SO4=-2
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-774918.053339
FMO2-HF: Nuclear repulsion	732364.274861
FMO2-HF: Total energy	-42553.778477
FMO2-MP2: Total energy	-42677.620459

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:ALA)

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

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.
-236.704	-231.451	24.102	-15.712	-13.639	-0.174

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.738 / q_NPA : 0.849

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	ASP	-1	-1.000	-1.005	3.766	-32.961	-31.585	-0.003	-0.603	-0.770	0.000
4	A	4	ALA	0	0.017	0.023	3.266	4.651	4.939	0.012	-0.065	-0.235	0.000
5	A	5	LYS	1	0.933	0.954	5.261	29.572	29.604	-0.001	-0.002	-0.028	0.000
6	A	6	PRO	0	0.017	0.016	9.050	1.277	1.277	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.920	0.960	11.259	18.843	18.843	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.030	0.023	14.676	0.243	0.243	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.845	0.916	17.377	14.429	14.429	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.052	0.020	21.065	-0.034	-0.034	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.004	0.008	23.660	-0.055	-0.055	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.023	0.012	26.811	-0.099	-0.099	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.014	0.004	27.868	0.114	0.114	0.000	0.000	0.000	0.000
14	A	14	ALA	0	-0.007	0.012	31.010	-0.089	-0.089	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.939	0.981	32.856	8.401	8.401	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.021	0.004	35.063	-0.201	-0.201	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.067	-0.042	34.770	0.297	0.297	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.935	-0.960	33.191	-9.373	-9.373	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.024	-0.010	30.139	-0.244	-0.244	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.004	0.004	26.383	0.106	0.106	0.000	0.000	0.000	0.000
21	A	21	THR	0	0.001	0.003	24.513	-0.106	-0.106	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.033	-0.010	19.943	-0.095	-0.095	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.910	0.954	19.831	12.629	12.629	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.018	0.006	15.042	-0.148	-0.148	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.051	-0.020	12.446	0.346	0.346	0.000	0.000	0.000	0.000
26	A	26	ILE	0	0.008	0.018	7.014	-0.410	-0.410	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.045	-0.017	7.219	1.590	1.590	0.000	0.000	0.000	0.000
28	A	28	HIS	0	0.037	-0.007	3.061	3.024	3.665	0.124	-0.215	-0.549	-0.001
29	A	29	LYS	1	0.987	0.986	3.577	45.853	45.992	0.001	-0.034	-0.106	0.000
30	A	30	MET	0	-0.021	0.014	6.714	1.618	1.618	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.798	-0.859	7.644	-20.432	-20.432	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.090	0.024	9.589	-0.305	-0.305	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.018	0.007	12.607	0.458	0.458	0.000	0.000	0.000	0.000
34	A	34	GLN	0	-0.036	-0.024	14.186	1.647	1.647	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.807	0.897	11.596	21.366	21.366	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.930	0.967	16.658	13.057	13.057	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.799	-0.906	16.705	-15.502	-15.502	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.001	-0.005	18.269	0.605	0.605	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.919	-0.953	21.174	-12.480	-12.480	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.016	-0.007	22.068	0.368	0.368	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.811	0.900	19.412	14.891	14.891	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.047	-0.020	17.313	-0.195	-0.195	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.004	0.008	11.707	-0.254	-0.254	0.000	0.000	0.000	0.000
44	A	44	PRO	0	-0.013	-0.017	11.057	0.144	0.144	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.857	0.902	10.039	23.584	23.584	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.072	-0.025	5.347	-3.343	-3.343	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.061	-0.037	6.412	-1.268	-1.268	0.000	0.000	0.000	0.000
48	A	48	ILE	0	0.017	0.003	5.576	-2.600	-2.600	0.000	0.000	0.000	0.000
49	A	49	ASN	0	-0.046	-0.031	7.896	4.331	4.331	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.872	0.921	10.970	21.690	21.690	0.000	0.000	0.000	0.000
51	A	51	PHE	0	-0.022	-0.005	11.510	-2.326	-2.326	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.008	0.002	13.647	1.132	1.132	0.000	0.000	0.000	0.000
53	A	53	CYS	0	-0.028	0.007	15.867	-0.482	-0.482	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.891	-0.944	18.633	-14.649	-14.649	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.012	-0.003	21.190	-0.278	-0.278	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.022	-0.021	24.168	0.000	0.000	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.003	0.009	23.069	0.423	0.423	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.010	0.010	24.102	0.029	0.029	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.038	-0.028	20.232	0.078	0.078	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.037	-0.011	22.276	0.646	0.646	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.001	-0.006	19.145	0.406	0.406	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.813	-0.890	18.012	-18.101	-18.101	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.027	-0.009	16.143	0.795	0.795	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.032	0.014	15.708	-1.403	-1.403	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.070	-0.032	11.912	0.863	0.863	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.870	-0.941	13.742	-18.406	-18.406	0.000	0.000	0.000	0.000
67	A	67	PRO	0	-0.053	-0.055	12.773	-0.304	-0.304	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.026	0.003	13.809	0.036	0.036	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.014	0.006	13.252	0.813	0.813	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.029	-0.016	13.633	-0.426	-0.426	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.009	-0.005	9.938	-0.531	-0.531	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.080	-0.036	9.591	-0.483	-0.483	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.047	0.039	8.872	1.960	1.960	0.000	0.000	0.000	0.000
74	A	74	TYR	0	-0.065	-0.062	12.018	-0.487	-0.487	0.000	0.000	0.000	0.000
75	A	75	PHE	0	0.003	-0.004	12.869	0.566	0.566	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.862	-0.927	17.523	-12.867	-12.867	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.008	-0.007	18.426	0.084	0.084	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.858	-0.933	23.518	-11.384	-11.384	0.000	0.000	0.000	0.000
79	A	79	ALA	0	-0.006	0.001	25.106	-0.050	-0.050	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.822	0.892	27.069	9.492	9.492	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.033	0.008	28.370	-0.194	-0.194	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.805	-0.875	30.774	-9.105	-9.105	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.030	-0.026	31.616	0.347	0.347	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.025	-0.009	30.500	-0.311	-0.311	0.000	0.000	0.000	0.000
85	A	85	GLY	0	-0.006	-0.006	27.657	0.101	0.101	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.950	-0.971	21.915	-14.524	-14.524	0.000	0.000	0.000	0.000
87	A	87	PHE	0	-0.001	-0.005	20.533	0.195	0.195	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.945	0.979	16.403	16.849	16.849	0.000	0.000	0.000	0.000
89	A	89	PHE	0	-0.037	-0.028	14.553	0.595	0.595	0.000	0.000	0.000	0.000
90	A	90	THR	0	0.038	0.019	11.419	-1.031	-1.031	0.000	0.000	0.000	0.000
91	A	91	TRP	0	-0.012	-0.015	8.403	1.206	1.206	0.000	0.000	0.000	0.000
92	A	92	TYR	0	0.024	0.004	8.137	-2.632	-2.632	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.743	-0.835	3.007	-77.380	-75.271	0.412	-1.234	-1.286	-0.010
94	A	94	ASP	-1	-0.705	-0.836	6.110	-26.824	-26.824	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.860	-0.897	1.727	-125.096	-124.715	13.924	-8.686	-5.619	-0.109
96	A	96	GLY	0	-0.007	-0.006	5.189	0.960	0.961	-0.001	-0.001	0.001	0.000
97	A	97	SER	0	-0.092	-0.058	2.700	-2.984	-1.115	0.846	-1.343	-1.371	-0.012
98	A	98	VAL	0	-0.013	-0.012	4.877	4.052	4.118	-0.001	-0.003	-0.062	0.000
99	A	99	TYR	0	-0.068	-0.061	1.887	-18.978	-20.627	8.789	-3.526	-3.614	-0.042
100	A	100	GLU	-1	-0.868	-0.948	7.670	-18.983	-18.983	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.910	-0.971	11.378	-20.796	-20.796	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.021	0.024	14.266	0.555	0.555	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.852	0.934	17.932	16.313	16.313	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.021	0.030	21.022	0.233	0.233	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.024	-0.021	24.568	0.019	0.019	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.016	-0.010	27.412	0.185	0.185	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.023	-0.031	31.097	-0.052	-0.052	0.000	0.000	0.000	0.000
108	A	108	ALA	-1	-0.909	-0.947	33.984	-8.205	-8.205	0.000	0.000	0.000	0.000
109	A	803	SO4	-2	-1.897	-1.940	18.926	-31.139	-31.139	0.000	0.000	0.000	0.000
110	B	806	EDO	0	0.000	0.000	28.069	-0.004	-0.004	0.000	0.000	0.000	0.000
111	B	807	EDO	0	0.018	0.023	34.045	-0.061	-0.061	0.000	0.000	0.000	0.000
112	F	804	EDO	0	0.025	0.021	33.377	0.134	0.134	0.000	0.000	0.000	0.000
113	A	903	HOH	0	-0.061	-0.044	18.333	-0.237	-0.237	0.000	0.000	0.000	0.000
114	B	813	HOH	0	-0.051	-0.045	33.331	-0.129	-0.129	0.000	0.000	0.000	0.000
115	B	867	HOH	0	-0.041	-0.015	19.528	0.193	0.193	0.000	0.000	0.000	0.000
116	F	882	HOH	0	0.007	0.001	35.640	-0.062	-0.062	0.000	0.000	0.000	0.000

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