FMO DATABASE

FMODB ID: 4YY3N

Calculation Name: 2O1A-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | 1,2-ethanediol

Ligand 3-letter code: SO4 | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2O1A

Chain ID: A

ChEMBL ID:

UniProt ID: Q99UX4

Base Structure: X-ray

Registration Date: 2025-10-05

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	-1071118.553446
FMO2-HF: Nuclear repulsion	1022028.567847
FMO2-HF: Total energy	-49089.985599
FMO2-MP2: Total energy	-49235.119618

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:17:GLN)

Summations of interaction energy for fragment #1(A:17:GLN)

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.
57.772	64.575	1.376	-2.895	-5.282	-0.027

Interaction energy analysis for fragmet #1(A:17:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.822 / q_NPA : 0.907

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	19	THR	0	0.007	0.006	2.307	-5.250	-2.168	0.995	-1.031	-3.045	-0.003
4	A	20	SER	0	-0.055	-0.031	4.688	2.877	3.006	-0.001	-0.018	-0.110	0.000
34	A	50	LYS	1	0.885	0.946	4.656	34.283	34.380	-0.001	-0.008	-0.087	0.000
35	A	51	GLN	0	0.001	-0.018	4.688	-1.690	-1.389	-0.001	-0.033	-0.267	0.000
36	A	52	ASN	0	-0.029	-0.032	4.559	6.851	7.009	-0.001	-0.012	-0.145	0.000
122	A	138	ALA	-1	-0.770	-0.856	2.592	-51.963	-48.927	0.385	-1.793	-1.628	-0.024
5	A	21	GLN	0	0.030	0.017	8.474	0.769	0.769	0.000	0.000	0.000	0.000
6	A	22	PRO	0	0.001	0.013	11.368	0.183	0.183	0.000	0.000	0.000	0.000
7	A	23	ILE	0	-0.019	-0.015	15.190	0.038	0.038	0.000	0.000	0.000	0.000
8	A	24	ASN	0	0.009	-0.006	17.405	0.008	0.008	0.000	0.000	0.000	0.000
9	A	25	PHE	0	-0.033	-0.021	21.137	-0.237	-0.237	0.000	0.000	0.000	0.000
10	A	26	GLN	0	0.013	0.013	23.380	0.424	0.424	0.000	0.000	0.000	0.000
11	A	27	VAL	0	-0.019	-0.018	26.703	-0.028	-0.028	0.000	0.000	0.000	0.000
12	A	28	GLN	0	-0.006	-0.016	28.561	0.350	0.350	0.000	0.000	0.000	0.000
13	A	29	LYS	1	0.826	0.883	31.562	7.735	7.735	0.000	0.000	0.000	0.000
14	A	30	ASP	-1	-0.868	-0.943	34.264	-8.597	-8.597	0.000	0.000	0.000	0.000
15	A	31	GLY	0	-0.018	0.001	35.552	0.182	0.182	0.000	0.000	0.000	0.000
16	A	32	SER	0	-0.013	0.000	36.250	0.069	0.069	0.000	0.000	0.000	0.000
17	A	33	SER	0	0.025	0.010	33.030	-0.165	-0.165	0.000	0.000	0.000	0.000
18	A	34	GLU	-1	-0.824	-0.890	33.635	-7.899	-7.899	0.000	0.000	0.000	0.000
19	A	35	LYS	1	0.990	0.999	32.775	8.239	8.239	0.000	0.000	0.000	0.000
20	A	36	SER	0	0.031	0.006	32.279	0.376	0.376	0.000	0.000	0.000	0.000
21	A	37	HIS	1	0.863	0.919	33.106	8.421	8.421	0.000	0.000	0.000	0.000
22	A	38	MET	0	0.018	0.024	27.922	0.035	0.035	0.000	0.000	0.000	0.000
23	A	39	ASP	-1	-0.797	-0.894	27.800	-11.092	-11.092	0.000	0.000	0.000	0.000
24	A	40	ASP	-1	-0.816	-0.890	28.809	-9.430	-9.430	0.000	0.000	0.000	0.000
25	A	41	TYR	0	-0.029	-0.010	29.970	0.011	0.011	0.000	0.000	0.000	0.000
26	A	42	MET	0	-0.025	-0.004	23.298	-0.223	-0.223	0.000	0.000	0.000	0.000
27	A	43	GLN	0	-0.033	-0.008	22.994	-0.184	-0.184	0.000	0.000	0.000	0.000
28	A	44	HIS	1	0.800	0.908	22.773	11.144	11.144	0.000	0.000	0.000	0.000
29	A	45	PRO	0	0.011	0.010	19.264	0.305	0.305	0.000	0.000	0.000	0.000
30	A	46	GLY	0	0.027	0.015	18.672	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	47	LYS	1	0.877	0.932	11.652	21.279	21.279	0.000	0.000	0.000	0.000
32	A	48	VAL	0	0.031	0.026	10.680	0.297	0.297	0.000	0.000	0.000	0.000
33	A	49	ILE	0	-0.031	-0.027	7.595	-1.298	-1.298	0.000	0.000	0.000	0.000
37	A	53	ASN	0	-0.013	-0.012	6.053	2.893	2.893	0.000	0.000	0.000	0.000
38	A	54	LYS	1	1.004	1.036	7.878	26.303	26.303	0.000	0.000	0.000	0.000
39	A	55	TYR	0	0.073	0.023	8.768	-2.880	-2.880	0.000	0.000	0.000	0.000
40	A	56	TYR	0	-0.018	-0.011	9.642	1.982	1.982	0.000	0.000	0.000	0.000
41	A	57	PHE	0	0.025	0.021	12.604	-0.634	-0.634	0.000	0.000	0.000	0.000
42	A	58	GLN	0	-0.018	-0.019	13.257	0.297	0.297	0.000	0.000	0.000	0.000
43	A	59	THR	0	0.002	-0.002	15.719	0.576	0.576	0.000	0.000	0.000	0.000
44	A	60	VAL	0	0.013	0.003	19.318	-0.332	-0.332	0.000	0.000	0.000	0.000
45	A	61	LEU	0	-0.022	0.002	22.156	0.387	0.387	0.000	0.000	0.000	0.000
46	A	62	ASN	0	0.027	-0.012	25.600	-0.367	-0.367	0.000	0.000	0.000	0.000
47	A	63	ASN	0	0.008	-0.001	28.702	0.121	0.121	0.000	0.000	0.000	0.000
48	A	64	ALA	0	0.006	0.006	27.427	0.153	0.153	0.000	0.000	0.000	0.000
49	A	65	SER	0	-0.077	-0.071	29.370	0.149	0.149	0.000	0.000	0.000	0.000
50	A	66	PHE	0	0.008	-0.005	32.497	0.250	0.250	0.000	0.000	0.000	0.000
51	A	67	TRP	0	-0.050	-0.033	27.306	0.097	0.097	0.000	0.000	0.000	0.000
52	A	68	LYS	1	0.931	0.982	30.763	8.137	8.137	0.000	0.000	0.000	0.000
53	A	69	GLU	-1	-0.856	-0.928	30.844	-9.543	-9.543	0.000	0.000	0.000	0.000
54	A	70	TYR	0	0.017	0.008	23.580	0.147	0.147	0.000	0.000	0.000	0.000
55	A	71	LYS	1	0.877	0.943	26.911	10.110	10.110	0.000	0.000	0.000	0.000
56	A	72	PHE	0	0.039	0.012	23.113	0.197	0.197	0.000	0.000	0.000	0.000
57	A	73	TYR	0	0.015	0.011	24.905	-0.076	-0.076	0.000	0.000	0.000	0.000
58	A	74	ASN	0	0.020	-0.005	22.482	0.338	0.338	0.000	0.000	0.000	0.000
59	A	75	ALA	0	0.047	0.015	24.245	0.378	0.378	0.000	0.000	0.000	0.000
60	A	76	ASN	0	-0.039	-0.008	26.288	0.559	0.559	0.000	0.000	0.000	0.000
61	A	77	ASN	0	-0.042	-0.030	27.971	0.226	0.226	0.000	0.000	0.000	0.000
62	A	78	GLN	0	0.044	0.034	24.892	0.006	0.006	0.000	0.000	0.000	0.000
63	A	79	GLU	-1	-0.919	-0.963	25.152	-11.352	-11.352	0.000	0.000	0.000	0.000
64	A	80	LEU	0	-0.063	-0.017	19.793	-0.432	-0.432	0.000	0.000	0.000	0.000
65	A	81	ALA	0	0.010	0.011	18.952	0.199	0.199	0.000	0.000	0.000	0.000
66	A	82	THR	0	-0.018	-0.016	19.455	-0.410	-0.410	0.000	0.000	0.000	0.000
67	A	83	THR	0	-0.004	-0.005	16.080	-0.332	-0.332	0.000	0.000	0.000	0.000
68	A	84	VAL	0	0.000	0.000	18.222	-0.200	-0.200	0.000	0.000	0.000	0.000
69	A	85	VAL	0	-0.038	-0.011	14.306	-0.510	-0.510	0.000	0.000	0.000	0.000
70	A	86	ASN	0	-0.015	-0.026	16.820	0.231	0.231	0.000	0.000	0.000	0.000
71	A	87	ASP	-1	-0.785	-0.848	19.754	-12.168	-12.168	0.000	0.000	0.000	0.000
72	A	88	ASN	0	-0.002	0.002	23.573	0.544	0.544	0.000	0.000	0.000	0.000
73	A	89	LYS	1	0.988	0.966	25.224	11.772	11.772	0.000	0.000	0.000	0.000
74	A	90	LYS	1	0.954	0.993	28.258	10.665	10.665	0.000	0.000	0.000	0.000
75	A	91	ALA	0	-0.018	-0.008	27.253	0.310	0.310	0.000	0.000	0.000	0.000
76	A	92	ASP	-1	-0.778	-0.843	29.366	-9.875	-9.875	0.000	0.000	0.000	0.000
77	A	93	THR	0	-0.012	0.000	24.981	-0.046	-0.046	0.000	0.000	0.000	0.000
78	A	94	ARG	1	0.871	0.897	22.794	12.275	12.275	0.000	0.000	0.000	0.000
79	A	95	THR	0	-0.027	0.002	17.449	-0.051	-0.051	0.000	0.000	0.000	0.000
80	A	96	ILE	0	0.002	-0.006	18.787	-0.129	-0.129	0.000	0.000	0.000	0.000
81	A	97	ASN	0	0.043	0.026	12.308	-0.080	-0.080	0.000	0.000	0.000	0.000
82	A	98	VAL	0	0.015	0.000	16.475	0.609	0.609	0.000	0.000	0.000	0.000
83	A	99	ALA	0	-0.008	0.001	15.468	-0.912	-0.912	0.000	0.000	0.000	0.000
84	A	100	VAL	0	-0.020	-0.017	14.238	1.081	1.081	0.000	0.000	0.000	0.000
85	A	101	GLU	-1	-0.865	-0.932	14.535	-19.514	-19.514	0.000	0.000	0.000	0.000
86	A	102	PRO	0	-0.014	-0.021	12.048	0.636	0.636	0.000	0.000	0.000	0.000
87	A	103	GLY	0	-0.017	-0.001	14.728	0.702	0.702	0.000	0.000	0.000	0.000
88	A	104	TYR	0	0.007	0.000	17.793	0.900	0.900	0.000	0.000	0.000	0.000
89	A	105	LYS	1	0.975	0.977	19.250	11.698	11.698	0.000	0.000	0.000	0.000
90	A	106	SER	0	-0.001	0.011	22.032	-0.028	-0.028	0.000	0.000	0.000	0.000
91	A	107	LEU	0	-0.046	-0.007	19.869	-0.341	-0.341	0.000	0.000	0.000	0.000
92	A	108	THR	0	0.048	0.034	23.987	0.335	0.335	0.000	0.000	0.000	0.000
93	A	109	THR	0	-0.058	-0.038	26.180	-0.362	-0.362	0.000	0.000	0.000	0.000
94	A	110	LYS	1	0.920	0.944	28.449	9.315	9.315	0.000	0.000	0.000	0.000
95	A	111	VAL	0	0.023	0.010	28.918	-0.279	-0.279	0.000	0.000	0.000	0.000
96	A	112	HIS	0	-0.109	-0.064	31.696	0.236	0.236	0.000	0.000	0.000	0.000
97	A	113	ILE	0	0.019	0.012	31.749	-0.164	-0.164	0.000	0.000	0.000	0.000
98	A	114	VAL	0	-0.056	-0.042	35.471	0.297	0.297	0.000	0.000	0.000	0.000
99	A	115	VAL	0	0.014	0.009	37.457	-0.171	-0.171	0.000	0.000	0.000	0.000
100	A	116	PRO	0	0.017	-0.007	39.377	0.200	0.200	0.000	0.000	0.000	0.000
101	A	117	GLN	0	0.026	0.018	42.599	0.215	0.215	0.000	0.000	0.000	0.000
102	A	118	ILE	0	-0.014	0.005	42.158	0.137	0.137	0.000	0.000	0.000	0.000
103	A	119	ASN	0	-0.040	-0.020	45.248	0.019	0.019	0.000	0.000	0.000	0.000
104	A	120	TYR	0	0.022	0.032	38.206	0.064	0.064	0.000	0.000	0.000	0.000
105	A	121	ASN	0	0.011	-0.006	40.611	-0.347	-0.347	0.000	0.000	0.000	0.000
106	A	122	HIS	0	0.040	0.029	36.978	0.274	0.274	0.000	0.000	0.000	0.000
107	A	123	ARG	1	0.920	0.956	35.910	8.245	8.245	0.000	0.000	0.000	0.000
108	A	124	TYR	0	0.003	0.007	33.087	0.225	0.225	0.000	0.000	0.000	0.000
109	A	125	THR	0	0.025	0.018	33.390	-0.156	-0.156	0.000	0.000	0.000	0.000
110	A	126	THR	0	-0.037	-0.026	30.346	0.142	0.142	0.000	0.000	0.000	0.000
111	A	127	HIS	1	0.839	0.909	28.292	9.559	9.559	0.000	0.000	0.000	0.000
112	A	128	LEU	0	-0.018	0.000	22.246	0.206	0.206	0.000	0.000	0.000	0.000
113	A	129	GLU	-1	-0.782	-0.871	24.349	-11.178	-11.178	0.000	0.000	0.000	0.000
114	A	130	PHE	0	0.000	-0.022	19.241	-0.201	-0.201	0.000	0.000	0.000	0.000
115	A	131	GLU	-1	-0.887	-0.938	21.405	-12.192	-12.192	0.000	0.000	0.000	0.000
116	A	132	LYS	1	0.912	0.952	18.486	13.715	13.715	0.000	0.000	0.000	0.000
117	A	133	ALA	0	-0.016	-0.010	18.607	-0.043	-0.043	0.000	0.000	0.000	0.000
118	A	134	ILE	0	-0.005	0.008	13.485	-0.489	-0.489	0.000	0.000	0.000	0.000
119	A	135	PRO	0	0.013	0.016	11.183	0.243	0.243	0.000	0.000	0.000	0.000
120	A	136	THR	0	0.025	0.005	9.476	-0.727	-0.727	0.000	0.000	0.000	0.000
121	A	137	LEU	0	-0.048	-0.023	5.912	0.124	0.124	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:17:GLN)