FMO DATABASE

FMODB ID: P596Z

Calculation Name: 1LQ9-A-Xray13

Preferred Name:

Target Type:

Ligand Name: tetraethylene glycol

ligand 3-letter code: PG4

PDB ID: 1LQ9

Chain ID: A

ChEMBL ID:

UniProt ID: Q53908

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	113
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-808810.829704
FMO2-HF: Nuclear repulsion	766524.662612
FMO2-HF: Total energy	-42286.167093
FMO2-MP2: Total energy	-42411.008629

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:ALA)

Summations of interaction energy for fragment #1(A:2: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.
-109.482	-100.03	6.774	-7.427	-8.798	-0.082

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.818 / q_NPA : 0.906

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	4	VAL	0	0.027	-0.002	3.420	-3.553	-2.063	0.072	-0.663	-0.899	-0.001
4	A	5	ASN	0	-0.003	0.001	5.570	0.158	0.158	0.000	0.000	0.000	0.000
5	A	6	ASP	-1	-0.827	-0.894	2.690	-48.510	-46.248	0.506	-1.308	-1.459	-0.013
6	A	7	PRO	0	0.034	0.005	4.645	-0.207	-0.155	-0.001	-0.005	-0.046	0.000
7	A	8	ARG	1	0.841	0.911	3.052	49.440	50.006	0.129	-0.219	-0.476	-0.001
8	A	9	VAL	0	-0.038	-0.010	3.024	-0.672	-0.251	0.135	-0.127	-0.429	-0.001
9	A	10	GLY	0	0.034	0.025	5.673	3.119	3.119	0.000	0.000	0.000	0.000
10	A	11	PHE	0	-0.102	-0.066	8.393	3.129	3.129	0.000	0.000	0.000	0.000
11	A	12	VAL	0	0.036	0.011	7.397	-3.332	-3.332	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.003	0.008	9.844	3.064	3.064	0.000	0.000	0.000	0.000
13	A	14	VAL	0	-0.001	-0.004	11.297	-2.099	-2.099	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.021	-0.013	13.580	1.674	1.674	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.012	-0.002	15.803	-0.697	-0.697	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.012	-0.005	16.048	0.673	0.673	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.009	0.019	20.695	-0.174	-0.174	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.007	-0.029	22.774	0.159	0.159	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.831	-0.891	25.431	-10.823	-10.823	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.046	0.023	26.723	0.427	0.427	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.025	-0.004	24.627	-0.375	-0.375	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.048	-0.012	24.638	-0.397	-0.397	0.000	0.000	0.000	0.000
23	A	24	THR	0	0.004	-0.029	24.490	-0.262	-0.262	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.050	-0.027	20.843	-0.276	-0.276	0.000	0.000	0.000	0.000
25	A	26	HIS	0	-0.024	0.000	20.511	-1.050	-1.050	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.991	0.987	21.104	11.275	11.275	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.037	0.024	18.987	-0.260	-0.260	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.006	-0.008	15.293	-0.852	-0.852	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.968	-0.976	17.157	-14.312	-14.312	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.006	0.002	19.415	-0.204	-0.204	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.044	-0.025	15.220	-0.316	-0.316	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.084	-0.054	13.148	-1.002	-1.002	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.043	0.030	15.605	-0.104	-0.104	0.000	0.000	0.000	0.000
34	A	35	GLY	0	-0.004	-0.001	17.342	0.807	0.807	0.000	0.000	0.000	0.000
35	A	36	VAL	0	-0.029	-0.012	18.248	0.030	0.030	0.000	0.000	0.000	0.000
36	A	37	GLN	0	-0.024	-0.031	13.651	-0.407	-0.407	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.789	-0.862	14.291	-21.803	-21.803	0.000	0.000	0.000	0.000
38	A	39	TRP	0	-0.005	-0.021	14.485	-1.264	-1.264	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.025	-0.008	10.850	-0.110	-0.110	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.765	0.856	9.929	22.425	22.425	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.944	-0.956	9.818	-20.706	-20.706	0.000	0.000	0.000	0.000
42	A	43	VAL	0	-0.056	-0.010	12.081	1.153	1.153	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.041	0.006	11.041	-2.398	-2.398	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.039	0.006	9.025	1.094	1.094	0.000	0.000	0.000	0.000
45	A	46	PHE	0	-0.019	0.002	7.691	-3.755	-3.755	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.049	-0.020	2.679	-4.670	-3.853	0.409	-0.291	-0.935	-0.002
47	A	48	SER	0	-0.048	-0.064	2.772	-6.566	-5.025	0.103	-0.841	-0.802	-0.006
48	A	49	ALA	0	0.021	0.012	4.939	4.928	4.949	-0.001	-0.003	-0.018	0.000
49	A	50	THR	0	-0.011	0.014	6.109	-0.467	-0.467	0.000	0.000	0.000	0.000
50	A	51	TYR	0	0.003	-0.003	8.603	1.471	1.471	0.000	0.000	0.000	0.000
51	A	52	HIS	0	-0.037	-0.023	9.931	-1.124	-1.124	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.047	0.031	14.427	0.687	0.687	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.042	-0.030	18.212	-0.251	-0.251	0.000	0.000	0.000	0.000
54	A	55	THR	0	0.049	0.007	19.958	0.412	0.412	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.857	-0.900	22.279	-12.638	-12.638	0.000	0.000	0.000	0.000
56	A	57	GLY	0	-0.005	-0.014	23.662	0.557	0.557	0.000	0.000	0.000	0.000
57	A	58	THR	0	-0.059	-0.032	24.483	0.015	0.015	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.036	0.012	20.505	0.082	0.082	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.003	0.020	16.397	-0.371	-0.371	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.001	-0.005	13.642	0.349	0.349	0.000	0.000	0.000	0.000
61	A	62	ASN	0	0.004	0.004	10.431	-3.101	-3.101	0.000	0.000	0.000	0.000
62	A	63	TYR	0	-0.001	0.007	5.918	0.647	0.647	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.038	0.003	7.484	-3.738	-3.738	0.000	0.000	0.000	0.000
64	A	65	GLN	0	0.003	0.037	1.988	-29.515	-27.233	5.422	-3.970	-3.734	-0.058
65	A	66	TRP	0	0.063	0.030	5.945	-1.179	-1.179	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.895	-0.962	6.716	-30.880	-30.880	0.000	0.000	0.000	0.000
67	A	68	SER	0	-0.007	-0.006	8.156	2.391	2.391	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.803	-0.885	11.541	-16.899	-16.899	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.018	-0.011	14.243	0.071	0.071	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.010	0.007	11.698	0.656	0.656	0.000	0.000	0.000	0.000
71	A	72	TYR	0	0.046	0.025	12.345	1.019	1.019	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.840	0.894	13.910	16.234	16.234	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.057	-0.031	17.115	0.813	0.813	0.000	0.000	0.000	0.000
74	A	75	ASN	0	0.022	0.012	14.047	1.675	1.675	0.000	0.000	0.000	0.000
75	A	76	PHE	0	-0.015	-0.003	14.407	-0.468	-0.468	0.000	0.000	0.000	0.000
76	A	77	GLY	0	-0.021	-0.009	16.487	0.849	0.849	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.026	-0.020	19.334	0.849	0.849	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.797	-0.874	19.293	-14.873	-14.873	0.000	0.000	0.000	0.000
79	A	80	PRO	0	0.035	0.018	21.311	-0.333	-0.333	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.945	0.960	18.586	16.070	16.070	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.050	-0.016	18.535	-0.247	-0.247	0.000	0.000	0.000	0.000
82	A	83	ALA	0	-0.024	-0.014	19.817	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.940	-0.976	22.984	-12.335	-12.335	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.009	0.010	15.996	0.139	0.139	0.000	0.000	0.000	0.000
85	A	86	ARG	1	0.882	0.936	20.616	12.549	12.549	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.899	-0.960	21.817	-11.204	-11.204	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.070	0.040	22.017	0.272	0.272	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.050	-0.015	17.335	0.082	0.082	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.127	-0.065	21.959	0.298	0.298	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.031	-0.035	25.080	0.491	0.491	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.037	0.002	23.228	0.361	0.361	0.000	0.000	0.000	0.000
92	A	93	PRO	0	-0.009	-0.021	26.685	0.084	0.084	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.087	0.044	28.018	-0.262	-0.262	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.044	-0.014	23.011	-0.313	-0.313	0.000	0.000	0.000	0.000
95	A	96	MET	0	-0.037	-0.013	26.434	0.427	0.427	0.000	0.000	0.000	0.000
96	A	97	GLY	0	-0.017	-0.016	26.793	0.469	0.469	0.000	0.000	0.000	0.000
97	A	98	PRO	0	-0.011	-0.005	25.252	-0.415	-0.415	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.006	0.007	19.969	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.933	0.974	20.807	13.179	13.179	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.005	0.002	17.515	-0.788	-0.788	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.014	-0.002	16.778	1.020	1.020	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.005	0.004	14.760	-1.237	-1.237	0.000	0.000	0.000	0.000
103	A	104	MET	0	-0.041	-0.014	12.140	0.981	0.981	0.000	0.000	0.000	0.000
104	A	105	THR	0	0.007	0.003	11.472	-0.775	-0.775	0.000	0.000	0.000	0.000
105	A	106	PRO	0	0.010	0.014	7.747	1.961	1.961	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.944	0.960	10.882	19.584	19.584	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.007	-0.001	13.124	1.119	1.119	0.000	0.000	0.000	0.000
108	A	109	ALA	0	-0.026	-0.004	10.895	-0.886	-0.886	0.000	0.000	0.000	0.000
109	A	110	ILE	0	0.025	0.012	12.971	1.196	1.196	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.028	-0.010	9.925	-1.359	-1.359	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.032	-0.026	13.648	1.157	1.157	0.000	0.000	0.000	0.000
112	A	113	SER	-1	-0.933	-0.947	16.477	-16.438	-16.438	0.000	0.000	0.000	0.000
113	A	301	PG4	0	-0.020	-0.004	23.370	0.003	0.003	0.000	0.000	0.000	0.000

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