FMO DATABASE

FMODB ID: NLR3Q

Calculation Name: 6DNU-A-Xray547

Preferred Name:

Target Type:

Ligand Name: hexaethylene glycol

Ligand 3-letter code: P6G

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6DNU

Chain ID: A

ChEMBL ID:

UniProt ID: C6S7X6

Base Structure: X-ray

Registration Date: 2025-10-06

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-968289.521414
FMO2-HF: Nuclear repulsion	921643.689342
FMO2-HF: Total energy	-46645.832072
FMO2-MP2: Total energy	-46779.891383

3D Structure Molmil

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:0:ALA)

Summations of interaction energy for fragment #1(A:0: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.
-196.553	-195.216	-0.003	-0.553	-0.78	-0.001

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / q_NPA : 0.915

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	2	PHE	0	-0.002	0.009	3.851	-0.086	1.205	-0.002	-0.546	-0.742	-0.001
59	A	59	PHE	0	-0.018	-0.010	4.794	-11.032	-10.986	-0.001	-0.007	-0.038	0.000
4	A	3	ALA	0	0.047	0.012	6.225	3.008	3.008	0.000	0.000	0.000	0.000
5	A	4	ASP	-1	-0.841	-0.897	9.096	-21.482	-21.482	0.000	0.000	0.000	0.000
6	A	5	THR	0	-0.030	-0.058	10.247	-2.024	-2.024	0.000	0.000	0.000	0.000
7	A	6	ALA	0	-0.029	-0.016	12.881	0.180	0.180	0.000	0.000	0.000	0.000
8	A	7	ALA	0	-0.009	-0.020	8.606	-0.166	-0.166	0.000	0.000	0.000	0.000
9	A	8	LEU	0	-0.011	0.003	7.857	-1.443	-1.443	0.000	0.000	0.000	0.000
10	A	9	LYS	1	0.967	0.985	9.401	18.225	18.225	0.000	0.000	0.000	0.000
11	A	10	ALA	0	0.040	0.030	11.869	0.205	0.205	0.000	0.000	0.000	0.000
12	A	11	ALA	0	-0.013	0.008	7.386	0.685	0.685	0.000	0.000	0.000	0.000
13	A	12	MET	0	-0.003	0.008	9.458	0.149	0.149	0.000	0.000	0.000	0.000
14	A	13	ASP	-1	-0.887	-0.950	11.031	-18.304	-18.304	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.100	-0.064	11.662	1.842	1.842	0.000	0.000	0.000	0.000
16	A	15	ALA	0	0.034	0.023	10.246	1.231	1.231	0.000	0.000	0.000	0.000
17	A	16	LEU	0	-0.023	-0.013	12.372	1.432	1.432	0.000	0.000	0.000	0.000
18	A	17	LYS	1	0.881	0.940	15.609	18.571	18.571	0.000	0.000	0.000	0.000
19	A	18	GLU	-1	-0.962	-0.978	14.088	-17.796	-17.796	0.000	0.000	0.000	0.000
20	A	19	HIS	0	-0.027	-0.017	15.917	-0.192	-0.192	0.000	0.000	0.000	0.000
21	A	20	PRO	0	0.007	0.020	17.111	-0.589	-0.589	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.923	-0.955	19.652	-15.553	-15.553	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.870	0.940	14.383	20.496	20.496	0.000	0.000	0.000	0.000
24	A	23	PRO	0	0.025	0.030	15.212	-0.410	-0.410	0.000	0.000	0.000	0.000
25	A	24	VAL	0	-0.019	-0.005	10.827	-1.425	-1.425	0.000	0.000	0.000	0.000
26	A	25	VAL	0	-0.003	-0.005	10.211	1.950	1.950	0.000	0.000	0.000	0.000
27	A	26	LEU	0	-0.021	0.003	9.469	-3.358	-3.358	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.850	-0.927	8.950	-26.968	-26.968	0.000	0.000	0.000	0.000
29	A	28	PHE	0	-0.012	-0.004	10.211	-2.454	-2.454	0.000	0.000	0.000	0.000
30	A	29	TYR	0	0.009	-0.038	9.958	1.479	1.479	0.000	0.000	0.000	0.000
31	A	30	ALA	0	0.050	0.007	11.921	0.505	0.505	0.000	0.000	0.000	0.000
32	A	31	ASP	-1	-0.845	-0.895	13.076	-21.609	-21.609	0.000	0.000	0.000	0.000
33	A	32	TRP	0	-0.057	-0.029	15.172	0.634	0.634	0.000	0.000	0.000	0.000
34	A	33	CYS	0	-0.069	-0.003	12.654	0.781	0.781	0.000	0.000	0.000	0.000
35	A	34	ILE	0	0.010	-0.001	16.087	-0.874	-0.874	0.000	0.000	0.000	0.000
36	A	35	SER	0	0.087	0.034	17.273	-0.372	-0.372	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.899	0.954	12.775	17.372	17.372	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.904	-0.960	14.195	-15.360	-15.360	0.000	0.000	0.000	0.000
39	A	39	MET	0	-0.010	0.008	13.567	0.493	0.493	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.003	0.001	10.117	-0.603	-0.603	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.041	-0.008	11.609	-0.555	-0.555	0.000	0.000	0.000	0.000
42	A	42	TYR	0	-0.065	-0.029	14.440	0.873	0.873	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.008	-0.030	14.679	1.310	1.310	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.004	-0.002	9.648	0.160	0.160	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.008	-0.011	10.314	-2.185	-2.185	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.047	-0.004	11.987	0.319	0.319	0.000	0.000	0.000	0.000
47	A	47	PRO	0	-0.008	-0.005	14.549	-0.739	-0.739	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.849	-0.951	16.219	-16.406	-16.406	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.014	-0.008	12.609	0.497	0.497	0.000	0.000	0.000	0.000
50	A	50	HIS	0	-0.027	-0.010	10.051	-0.743	-0.743	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.090	-0.026	13.262	0.251	0.251	0.000	0.000	0.000	0.000
52	A	52	ALA	0	-0.011	0.000	16.060	0.791	0.791	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.024	-0.013	11.232	0.147	0.147	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.825	-0.917	10.846	-27.067	-27.067	0.000	0.000	0.000	0.000
55	A	55	MET	0	-0.010	-0.010	7.223	-0.922	-0.922	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.949	-0.964	5.919	-50.093	-50.093	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.720	0.851	6.949	21.357	21.357	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.007	0.001	5.841	4.531	4.531	0.000	0.000	0.000	0.000
60	A	60	GLN	0	-0.025	-0.025	5.067	0.301	0.301	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.021	-0.015	6.649	-4.403	-4.403	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.778	-0.875	8.819	-23.025	-23.025	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.027	-0.018	10.498	1.205	1.205	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.035	-0.046	12.860	2.296	2.296	0.000	0.000	0.000	0.000
65	A	65	ALA	0	-0.046	-0.027	14.460	1.250	1.250	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.031	-0.012	16.291	0.692	0.692	0.000	0.000	0.000	0.000
67	A	67	THR	0	0.040	0.016	16.428	1.177	1.177	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.018	-0.013	18.975	-0.169	-0.169	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.825	-0.883	14.809	-19.877	-19.877	0.000	0.000	0.000	0.000
70	A	70	HIS	0	0.028	0.022	12.995	0.868	0.868	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.050	-0.029	17.111	0.535	0.535	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.046	-0.017	20.308	0.406	0.406	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.045	0.024	13.544	0.272	0.272	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.003	0.002	17.203	-0.063	-0.063	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.941	0.973	19.133	12.329	12.329	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-1.003	-0.993	19.319	-16.153	-16.153	0.000	0.000	0.000	0.000
77	A	77	TYR	0	0.000	-0.011	16.021	0.045	0.045	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.051	-0.013	19.974	0.235	0.235	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.060	-0.020	17.510	0.430	0.430	0.000	0.000	0.000	0.000
80	A	80	PHE	0	-0.021	-0.024	21.705	0.222	0.222	0.000	0.000	0.000	0.000
81	A	81	GLY	0	-0.003	-0.016	19.526	0.058	0.058	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.004	0.031	15.470	0.134	0.134	0.000	0.000	0.000	0.000
83	A	83	PRO	0	-0.015	-0.040	16.297	0.628	0.628	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.014	-0.004	15.562	1.106	1.106	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.032	0.009	12.235	-1.468	-1.468	0.000	0.000	0.000	0.000
86	A	86	PHE	0	0.010	-0.008	13.953	1.791	1.791	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.041	0.030	13.989	-1.899	-1.899	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.019	-0.023	14.486	1.315	1.315	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.866	0.913	15.819	14.130	14.130	0.000	0.000	0.000	0.000
90	A	90	SER	0	0.027	-0.003	18.534	0.277	0.277	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.915	-0.954	19.758	-13.299	-13.299	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.009	0.010	20.696	0.589	0.589	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.080	-0.021	21.642	-0.057	-0.057	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.906	0.951	18.860	13.938	13.938	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.014	-0.008	18.835	0.523	0.523	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.859	-0.931	20.770	-13.182	-13.182	0.000	0.000	0.000	0.000
97	A	97	PRO	0	-0.013	0.007	18.840	-0.579	-0.579	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.001	0.010	16.486	0.904	0.904	0.000	0.000	0.000	0.000
99	A	99	LEU	0	-0.014	-0.021	18.050	-0.847	-0.847	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.012	-0.007	19.453	0.602	0.602	0.000	0.000	0.000	0.000
101	A	101	PHE	0	-0.026	-0.009	17.639	-0.537	-0.537	0.000	0.000	0.000	0.000
102	A	102	VAL	0	-0.023	-0.006	18.780	0.973	0.973	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.992	1.007	18.687	11.901	11.901	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.091	0.037	17.773	-0.087	-0.087	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.848	-0.922	18.762	-13.606	-13.606	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.790	0.872	21.908	12.265	12.265	0.000	0.000	0.000	0.000
107	A	107	PHE	0	0.017	0.007	12.672	0.080	0.080	0.000	0.000	0.000	0.000
108	A	108	ILE	0	0.042	0.024	17.730	-0.297	-0.297	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.840	-0.911	19.143	-11.950	-11.950	0.000	0.000	0.000	0.000
110	A	110	TRP	0	-0.053	-0.015	15.031	0.175	0.175	0.000	0.000	0.000	0.000
111	A	111	TYR	0	0.049	0.020	14.588	-0.484	-0.484	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.881	-0.948	18.459	-14.736	-14.736	0.000	0.000	0.000	0.000
113	A	113	GLN	0	-0.137	-0.059	21.320	0.720	0.720	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.108	-0.073	19.929	0.736	0.736	0.000	0.000	0.000	0.000
115	A	115	ARG	0	0.039	0.035	18.666	-3.607	-3.607	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)