FMO DATABASE

FMODB ID: J4839

Calculation Name: 2I2Q-A-Xray547

Preferred Name:

Target Type:

Ligand Name: lauryl dimethylamine-n-oxide | sulfate ion | 1,2-ethanediol

Ligand 3-letter code: LDA | SO4 | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2I2Q

Chain ID: A

ChEMBL ID:

UniProt ID: P78929

Base Structure: X-ray

Registration Date: 2025-10-04

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	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1041015.779928
FMO2-HF: Nuclear repulsion	992471.83206
FMO2-HF: Total energy	-48543.947868
FMO2-MP2: Total energy	-48685.498255

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
6.275	11.997	1.674	-3.192	-4.204	-0.017

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.863 / q_NPA : 0.918

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	4	SER	0	0.066	0.036	2.325	-4.839	-1.718	1.569	-2.129	-2.561	-0.016
4	A	5	GLY	0	-0.018	0.013	3.186	6.566	7.656	0.094	-0.505	-0.679	0.002
5	A	6	VAL	0	-0.041	-0.023	4.281	0.203	0.518	-0.001	-0.055	-0.259	0.000
6	A	7	LYS	1	0.938	0.969	3.517	23.400	23.818	0.006	-0.214	-0.211	-0.001
104	A	105	THR	0	-0.122	-0.072	3.188	-3.906	-3.312	0.005	-0.247	-0.352	-0.002
107	A	108	ARG	1	0.881	0.950	3.966	44.567	44.751	0.001	-0.042	-0.142	0.000
7	A	8	VAL	0	0.014	0.008	6.237	2.523	2.523	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.011	0.009	8.673	0.355	0.355	0.000	0.000	0.000	0.000
9	A	10	PRO	0	0.004	-0.026	12.047	0.331	0.331	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.797	-0.888	14.722	-14.396	-14.396	0.000	0.000	0.000	0.000
11	A	12	CYS	0	-0.047	-0.010	12.507	1.037	1.037	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.032	-0.011	11.085	0.171	0.171	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.933	-0.969	14.914	-13.411	-13.411	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.091	0.043	18.569	0.543	0.543	0.000	0.000	0.000	0.000
15	A	16	PHE	0	-0.020	-0.002	16.297	0.485	0.485	0.000	0.000	0.000	0.000
16	A	17	GLN	0	-0.003	-0.013	17.645	0.289	0.289	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.836	-0.897	20.116	-11.342	-11.342	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.028	-0.007	21.347	0.471	0.471	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.817	0.903	18.100	16.431	16.431	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.094	-0.049	21.884	0.355	0.355	0.000	0.000	0.000	0.000
21	A	22	GLY	0	0.020	0.017	25.315	0.430	0.430	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.775	0.891	26.256	11.738	11.738	0.000	0.000	0.000	0.000
23	A	24	SER	0	-0.031	-0.028	27.065	0.302	0.302	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.051	-0.021	22.891	0.073	0.073	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.774	0.875	26.108	10.182	10.182	0.000	0.000	0.000	0.000
26	A	27	TYR	0	-0.014	-0.052	23.267	-0.260	-0.260	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.016	-0.011	18.672	0.136	0.136	0.000	0.000	0.000	0.000
28	A	29	VAL	0	0.027	0.029	19.134	-0.439	-0.439	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.038	-0.014	14.199	-0.269	-0.269	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.894	0.938	15.015	15.040	15.040	0.000	0.000	0.000	0.000
31	A	32	MET	0	-0.031	-0.005	8.516	-1.359	-1.359	0.000	0.000	0.000	0.000
32	A	33	ASN	0	0.061	0.031	12.328	0.909	0.909	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.842	-0.920	14.258	-16.387	-16.387	0.000	0.000	0.000	0.000
34	A	35	THR	0	-0.047	-0.034	13.876	-0.380	-0.380	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.866	0.933	11.035	18.039	18.039	0.000	0.000	0.000	0.000
36	A	37	THR	0	0.018	0.004	8.634	-2.267	-2.267	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.949	-0.984	7.963	-28.131	-28.131	0.000	0.000	0.000	0.000
38	A	39	ILE	0	-0.007	0.007	7.923	1.825	1.825	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.025	0.003	10.753	-0.213	-0.213	0.000	0.000	0.000	0.000
40	A	41	VAL	0	0.045	0.012	14.345	0.035	0.035	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.842	-0.878	17.544	-13.850	-13.850	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.878	0.926	20.272	11.626	11.626	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.867	0.936	21.589	12.845	12.845	0.000	0.000	0.000	0.000
44	A	45	SER	0	0.029	0.018	23.530	0.511	0.511	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.032	0.006	26.832	-0.229	-0.229	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.830	-0.892	29.650	-8.918	-8.918	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.925	0.941	30.161	8.537	8.537	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.881	-0.926	32.381	-8.679	-8.679	0.000	0.000	0.000	0.000
49	A	50	PHE	0	-0.026	-0.021	27.325	-0.419	-0.419	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.855	-0.932	30.387	-9.044	-9.044	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.070	-0.049	30.444	-0.037	-0.037	0.000	0.000	0.000	0.000
52	A	53	PHE	0	-0.049	-0.026	22.915	-0.447	-0.447	0.000	0.000	0.000	0.000
53	A	54	LEU	0	-0.021	-0.017	26.791	-0.407	-0.407	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.002	0.011	28.365	-0.099	-0.099	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.836	-0.882	25.174	-10.967	-10.967	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.030	-0.009	22.206	-0.762	-0.762	0.000	0.000	0.000	0.000
57	A	58	PRO	0	-0.043	-0.020	21.631	0.370	0.370	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.761	-0.863	24.418	-10.045	-10.045	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.836	0.900	25.467	9.964	9.964	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.820	-0.905	19.455	-15.491	-15.491	0.000	0.000	0.000	0.000
61	A	62	CYS	0	-0.092	-0.010	17.071	0.183	0.183	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.769	0.845	16.570	14.662	14.662	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.052	-0.042	10.760	-0.954	-0.954	0.000	0.000	0.000	0.000
64	A	65	ALA	0	0.034	0.021	15.916	0.383	0.383	0.000	0.000	0.000	0.000
65	A	66	ILE	0	-0.065	-0.019	17.003	-0.557	-0.557	0.000	0.000	0.000	0.000
66	A	67	TYR	0	0.074	0.026	19.667	0.380	0.380	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.839	-0.904	23.429	-11.465	-11.465	0.000	0.000	0.000	0.000
68	A	69	PHE	0	0.010	0.002	25.646	0.449	0.449	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.822	-0.903	27.990	-9.454	-9.454	0.000	0.000	0.000	0.000
70	A	71	PHE	0	-0.048	-0.020	29.377	0.094	0.094	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.017	-0.011	33.745	0.017	0.017	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.026	-0.006	33.821	0.001	0.001	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.008	0.015	37.983	0.156	0.156	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.833	-0.917	35.825	-8.458	-8.458	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.015	0.007	38.735	0.058	0.058	0.000	0.000	0.000	0.000
76	A	77	VAL	0	-0.051	-0.016	34.984	-0.145	-0.145	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.856	0.924	31.272	9.231	9.231	0.000	0.000	0.000	0.000
78	A	79	ASN	0	0.004	0.001	28.442	-0.251	-0.251	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.879	0.935	25.196	11.478	11.478	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.045	0.044	20.245	0.058	0.058	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.008	-0.006	21.548	-0.409	-0.409	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.025	0.002	12.581	-0.498	-0.498	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.027	0.003	18.039	0.377	0.377	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.037	-0.023	15.803	-1.011	-1.011	0.000	0.000	0.000	0.000
85	A	86	TRP	0	0.033	0.013	17.300	0.511	0.511	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.045	-0.066	18.136	-1.052	-1.052	0.000	0.000	0.000	0.000
87	A	88	PRO	0	0.044	0.043	20.394	0.168	0.168	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.887	-0.956	23.436	-11.618	-11.618	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.020	0.019	25.608	-0.110	-0.110	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.009	0.024	21.551	-0.034	-0.034	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.009	-0.006	21.218	-0.186	-0.186	0.000	0.000	0.000	0.000
92	A	93	ILE	0	0.066	0.029	20.248	-0.756	-0.756	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.962	0.976	17.102	15.311	15.311	0.000	0.000	0.000	0.000
94	A	95	SER	0	-0.069	-0.055	16.241	-1.333	-1.333	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.891	0.949	15.686	11.517	11.517	0.000	0.000	0.000	0.000
96	A	97	MET	0	-0.014	-0.003	15.028	-0.672	-0.672	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.002	0.009	11.154	-1.517	-1.517	0.000	0.000	0.000	0.000
98	A	99	TYR	0	0.072	0.044	10.770	-2.510	-2.510	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.004	0.015	11.633	-1.364	-1.364	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.043	-0.043	9.198	-1.001	-1.001	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.040	-0.025	6.626	-5.098	-5.098	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.964	1.003	7.336	18.422	18.422	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.874	-0.954	7.371	-26.639	-26.639	0.000	0.000	0.000	0.000
105	A	106	LEU	0	0.022	0.027	5.574	0.206	0.206	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.828	0.888	8.963	19.841	19.841	0.000	0.000	0.000	0.000
108	A	109	ALA	0	-0.017	0.006	8.799	0.299	0.299	0.000	0.000	0.000	0.000
109	A	110	PHE	0	-0.018	-0.001	10.362	1.568	1.568	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.026	0.006	13.882	0.693	0.693	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.026	-0.001	16.028	0.513	0.513	0.000	0.000	0.000	0.000
112	A	113	ILE	0	-0.024	0.007	16.089	0.570	0.570	0.000	0.000	0.000	0.000
113	A	114	GLY	0	0.006	0.013	19.191	0.094	0.094	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.072	-0.055	21.294	0.839	0.839	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.794	-0.856	16.237	-17.839	-17.839	0.000	0.000	0.000	0.000
116	A	117	ILE	0	0.008	0.002	19.613	0.618	0.618	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.004	-0.004	17.105	-1.438	-1.438	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.013	0.008	20.263	0.570	0.570	0.000	0.000	0.000	0.000
119	A	120	THR	0	-0.050	-0.028	21.971	-0.608	-0.608	0.000	0.000	0.000	0.000
120	A	121	ASP	-1	-0.856	-0.921	24.163	-10.080	-10.080	0.000	0.000	0.000	0.000
121	A	122	PHE	0	-0.055	-0.042	27.047	-0.322	-0.322	0.000	0.000	0.000	0.000
122	A	123	SER	-1	-0.909	-0.938	29.892	-8.909	-8.909	0.000	0.000	0.000	0.000

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