FMO DATABASE

FMODB ID: 4YG6N

Calculation Name: 2XVS-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 1,2-ethanediol | chloride ion | iodide ion

Ligand 3-letter code: EDO | CL | IOD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2XVS

Chain ID: A

ChEMBL ID:

UniProt ID: Q8N0Z6

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	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1591407.952924
FMO2-HF: Nuclear repulsion	1527995.328052
FMO2-HF: Total energy	-63412.624872
FMO2-MP2: Total energy	-63598.186921

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:-1:SER)

Summations of interaction energy for fragment #1(A:-1: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.
70.724	72.785	0.058	-0.979	-1.139	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.899 / q_NPA : 0.939

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	261	ARG	1	0.955	0.975	3.528	38.752	40.466	0.059	-0.837	-0.936	-0.001
141	A	399	LYS	1	0.830	0.914	3.753	59.584	59.931	-0.001	-0.142	-0.203	0.000
4	A	262	GLN	0	0.062	0.022	6.330	-1.059	-1.059	0.000	0.000	0.000	0.000
5	A	263	ARG	1	0.835	0.877	9.271	18.830	18.830	0.000	0.000	0.000	0.000
6	A	264	GLU	-1	-0.803	-0.905	6.778	-41.295	-41.295	0.000	0.000	0.000	0.000
7	A	265	GLN	0	-0.019	-0.017	7.165	-2.084	-2.084	0.000	0.000	0.000	0.000
8	A	266	GLN	0	0.071	0.033	8.991	2.374	2.374	0.000	0.000	0.000	0.000
9	A	267	LEU	0	-0.033	-0.004	12.456	1.595	1.595	0.000	0.000	0.000	0.000
10	A	268	LEU	0	0.004	-0.014	8.465	0.827	0.827	0.000	0.000	0.000	0.000
11	A	269	GLU	-1	-0.866	-0.928	10.707	-23.303	-23.303	0.000	0.000	0.000	0.000
12	A	270	PHE	0	-0.038	-0.019	13.552	1.531	1.531	0.000	0.000	0.000	0.000
13	A	271	LEU	0	-0.015	0.003	15.027	1.281	1.281	0.000	0.000	0.000	0.000
14	A	272	ASP	-1	-0.781	-0.850	13.109	-21.910	-21.910	0.000	0.000	0.000	0.000
15	A	273	ARG	1	0.921	0.958	16.446	16.020	16.020	0.000	0.000	0.000	0.000
16	A	274	LEU	0	0.004	0.002	19.251	0.894	0.894	0.000	0.000	0.000	0.000
17	A	275	THR	0	-0.015	-0.024	18.914	0.745	0.745	0.000	0.000	0.000	0.000
18	A	276	SER	0	0.024	0.025	20.710	0.923	0.923	0.000	0.000	0.000	0.000
19	A	277	LEU	0	-0.027	0.003	22.545	0.702	0.702	0.000	0.000	0.000	0.000
20	A	278	LEU	0	-0.028	-0.018	23.975	0.584	0.584	0.000	0.000	0.000	0.000
21	A	279	GLU	-1	-0.893	-0.934	25.284	-10.988	-10.988	0.000	0.000	0.000	0.000
22	A	280	SER	0	-0.086	-0.064	26.221	0.551	0.551	0.000	0.000	0.000	0.000
23	A	281	LYS	1	0.883	0.944	28.460	9.571	9.571	0.000	0.000	0.000	0.000
24	A	282	GLY	0	0.005	-0.001	28.260	0.324	0.324	0.000	0.000	0.000	0.000
25	A	283	LYS	1	0.904	0.950	26.677	11.317	11.317	0.000	0.000	0.000	0.000
26	A	284	VAL	0	-0.029	-0.002	30.726	0.360	0.360	0.000	0.000	0.000	0.000
27	A	285	LYS	1	0.978	0.987	34.165	7.923	7.923	0.000	0.000	0.000	0.000
28	A	286	THR	0	0.102	0.035	36.810	0.079	0.079	0.000	0.000	0.000	0.000
29	A	287	LYS	1	0.986	0.987	39.064	7.286	7.286	0.000	0.000	0.000	0.000
30	A	288	LYS	1	0.909	0.969	38.520	7.866	7.866	0.000	0.000	0.000	0.000
31	A	289	LEU	0	0.086	0.055	35.141	0.130	0.130	0.000	0.000	0.000	0.000
32	A	290	GLN	0	0.042	0.020	39.288	0.154	0.154	0.000	0.000	0.000	0.000
33	A	291	SER	0	-0.073	-0.039	42.468	0.126	0.126	0.000	0.000	0.000	0.000
34	A	292	MET	0	-0.042	-0.018	36.381	0.063	0.063	0.000	0.000	0.000	0.000
35	A	293	LEU	0	0.061	0.040	39.459	0.109	0.109	0.000	0.000	0.000	0.000
36	A	294	GLY	0	0.016	0.013	42.898	0.117	0.117	0.000	0.000	0.000	0.000
37	A	295	SER	0	-0.097	-0.058	43.965	0.120	0.120	0.000	0.000	0.000	0.000
38	A	296	LEU	0	0.014	0.010	41.598	0.019	0.019	0.000	0.000	0.000	0.000
39	A	297	ARG	1	0.901	0.943	45.629	6.503	6.503	0.000	0.000	0.000	0.000
40	A	298	PRO	0	0.090	0.046	47.419	-0.118	-0.118	0.000	0.000	0.000	0.000
41	A	299	ALA	0	0.047	0.017	48.776	-0.053	-0.053	0.000	0.000	0.000	0.000
42	A	300	HIS	0	-0.016	-0.012	44.367	-0.122	-0.122	0.000	0.000	0.000	0.000
43	A	301	LEU	0	0.037	0.021	44.433	-0.183	-0.183	0.000	0.000	0.000	0.000
44	A	302	GLY	0	0.024	0.017	46.127	-0.063	-0.063	0.000	0.000	0.000	0.000
45	A	303	PRO	0	0.021	0.005	46.969	0.076	0.076	0.000	0.000	0.000	0.000
46	A	304	CYS	0	-0.031	-0.017	43.643	0.006	0.006	0.000	0.000	0.000	0.000
47	A	305	SER	0	-0.072	-0.045	47.255	0.001	0.001	0.000	0.000	0.000	0.000
48	A	306	ASP	-1	-0.928	-0.948	50.206	-5.922	-5.922	0.000	0.000	0.000	0.000
49	A	307	GLY	0	-0.011	0.008	51.926	0.119	0.119	0.000	0.000	0.000	0.000
50	A	308	HIS	-1	-0.884	-0.960	53.113	-5.789	-5.789	0.000	0.000	0.000	0.000
51	A	309	TYR	0	-0.090	-0.042	43.276	-0.117	-0.117	0.000	0.000	0.000	0.000
52	A	310	GLN	0	-0.036	-0.022	47.771	0.045	0.045	0.000	0.000	0.000	0.000
53	A	311	SER	0	-0.006	-0.018	43.952	-0.180	-0.180	0.000	0.000	0.000	0.000
54	A	312	ALA	0	-0.009	-0.011	40.719	0.058	0.058	0.000	0.000	0.000	0.000
55	A	313	SER	0	-0.073	-0.038	42.775	0.014	0.014	0.000	0.000	0.000	0.000
56	A	314	GLY	0	-0.002	0.003	44.565	0.105	0.105	0.000	0.000	0.000	0.000
57	A	315	GLN	0	-0.024	-0.012	47.676	0.260	0.260	0.000	0.000	0.000	0.000
58	A	316	LYS	0	-0.018	0.007	48.874	-0.131	-0.131	0.000	0.000	0.000	0.000
59	A	317	VAL	0	-0.050	-0.030	47.042	0.063	0.063	0.000	0.000	0.000	0.000
60	A	318	THR	0	0.049	0.030	49.763	-0.075	-0.075	0.000	0.000	0.000	0.000
61	A	319	LEU	0	-0.032	-0.015	44.217	-0.119	-0.119	0.000	0.000	0.000	0.000
62	A	320	GLU	-1	-0.817	-0.889	46.213	-6.827	-6.827	0.000	0.000	0.000	0.000
63	A	321	LEU	0	-0.037	-0.027	43.309	-0.184	-0.184	0.000	0.000	0.000	0.000
64	A	322	LYS	1	0.817	0.898	41.791	7.290	7.290	0.000	0.000	0.000	0.000
65	A	323	PRO	0	0.012	0.002	40.019	-0.115	-0.115	0.000	0.000	0.000	0.000
66	A	324	LEU	0	0.027	0.008	34.173	-0.097	-0.097	0.000	0.000	0.000	0.000
67	A	325	SER	0	-0.043	-0.021	35.410	-0.130	-0.130	0.000	0.000	0.000	0.000
68	A	326	THR	0	-0.075	-0.051	36.468	0.071	0.071	0.000	0.000	0.000	0.000
69	A	327	LEU	0	-0.036	0.000	34.899	0.091	0.091	0.000	0.000	0.000	0.000
70	A	328	GLN	0	0.014	0.003	35.300	-0.306	-0.306	0.000	0.000	0.000	0.000
71	A	329	PRO	0	-0.020	-0.022	31.216	-0.146	-0.146	0.000	0.000	0.000	0.000
72	A	330	GLY	0	0.011	0.019	32.106	0.209	0.209	0.000	0.000	0.000	0.000
73	A	331	VAL	0	0.004	-0.008	33.547	-0.029	-0.029	0.000	0.000	0.000	0.000
74	A	332	ASN	0	-0.027	-0.010	35.521	0.343	0.343	0.000	0.000	0.000	0.000
75	A	333	SER	0	0.036	-0.006	38.861	0.114	0.114	0.000	0.000	0.000	0.000
76	A	334	GLY	0	0.004	0.010	42.008	0.064	0.064	0.000	0.000	0.000	0.000
77	A	335	ALA	0	-0.019	0.008	41.192	0.135	0.135	0.000	0.000	0.000	0.000
78	A	336	VAL	0	0.009	-0.004	41.633	-0.095	-0.095	0.000	0.000	0.000	0.000
79	A	337	ILE	0	-0.015	0.009	36.582	0.004	0.004	0.000	0.000	0.000	0.000
80	A	338	LEU	0	0.011	-0.016	40.401	0.035	0.035	0.000	0.000	0.000	0.000
81	A	339	GLY	0	0.004	0.008	38.093	0.016	0.016	0.000	0.000	0.000	0.000
82	A	340	LYS	1	0.793	0.888	37.957	7.714	7.714	0.000	0.000	0.000	0.000
83	A	341	VAL	0	0.005	0.014	32.671	-0.250	-0.250	0.000	0.000	0.000	0.000
84	A	342	VAL	0	-0.016	-0.017	31.119	0.190	0.190	0.000	0.000	0.000	0.000
85	A	343	PHE	0	0.022	-0.007	25.882	-0.126	-0.126	0.000	0.000	0.000	0.000
86	A	344	SER	0	0.011	0.005	28.101	0.026	0.026	0.000	0.000	0.000	0.000
87	A	345	LEU	0	-0.062	-0.024	21.147	-0.187	-0.187	0.000	0.000	0.000	0.000
88	A	346	THR	0	-0.017	-0.026	22.897	0.184	0.184	0.000	0.000	0.000	0.000
89	A	347	THR	0	-0.013	-0.005	18.168	-0.230	-0.230	0.000	0.000	0.000	0.000
90	A	348	GLU	-1	-0.819	-0.917	14.513	-18.835	-18.835	0.000	0.000	0.000	0.000
91	A	349	GLU	-1	-0.823	-0.882	17.142	-16.839	-16.839	0.000	0.000	0.000	0.000
92	A	350	LYS	1	0.838	0.925	20.167	14.162	14.162	0.000	0.000	0.000	0.000
93	A	351	VAL	0	0.039	0.051	22.178	0.663	0.663	0.000	0.000	0.000	0.000
94	A	352	PRO	0	0.003	0.005	21.666	-0.806	-0.806	0.000	0.000	0.000	0.000
95	A	353	PHE	0	0.038	0.035	24.517	-0.366	-0.366	0.000	0.000	0.000	0.000
96	A	354	THR	0	-0.018	-0.012	24.114	0.030	0.030	0.000	0.000	0.000	0.000
97	A	355	PHE	0	0.037	-0.005	26.614	0.022	0.022	0.000	0.000	0.000	0.000
98	A	356	GLY	0	0.031	0.026	29.065	-0.121	-0.121	0.000	0.000	0.000	0.000
99	A	357	LEU	0	0.001	-0.002	30.007	0.305	0.305	0.000	0.000	0.000	0.000
100	A	358	VAL	0	0.010	0.006	33.242	-0.210	-0.210	0.000	0.000	0.000	0.000
101	A	359	ASP	-1	-0.759	-0.873	35.837	-8.239	-8.239	0.000	0.000	0.000	0.000
102	A	360	SER	0	-0.039	-0.023	38.416	0.220	0.220	0.000	0.000	0.000	0.000
103	A	361	ASP	-1	-0.896	-0.964	38.056	-7.956	-7.956	0.000	0.000	0.000	0.000
104	A	362	GLY	0	0.002	0.017	36.417	-0.160	-0.160	0.000	0.000	0.000	0.000
105	A	363	PRO	0	0.023	-0.010	30.964	-0.085	-0.085	0.000	0.000	0.000	0.000
106	A	364	CYS	0	-0.090	-0.021	29.834	0.122	0.122	0.000	0.000	0.000	0.000
107	A	365	TYR	0	0.046	0.025	29.603	-0.355	-0.355	0.000	0.000	0.000	0.000
108	A	366	ALA	0	0.006	0.002	26.174	0.084	0.084	0.000	0.000	0.000	0.000
109	A	367	VAL	0	0.005	0.018	28.223	0.156	0.156	0.000	0.000	0.000	0.000
110	A	368	MET	0	-0.066	-0.032	22.351	-0.412	-0.412	0.000	0.000	0.000	0.000
111	A	369	VAL	0	0.022	0.017	27.843	0.158	0.158	0.000	0.000	0.000	0.000
112	A	370	TYR	0	0.003	-0.005	23.735	-0.526	-0.526	0.000	0.000	0.000	0.000
113	A	371	ASN	0	0.010	-0.012	29.431	0.092	0.092	0.000	0.000	0.000	0.000
114	A	372	ILE	0	0.008	0.005	29.580	0.324	0.324	0.000	0.000	0.000	0.000
115	A	373	VAL	0	-0.002	0.009	31.543	-0.183	-0.183	0.000	0.000	0.000	0.000
116	A	374	GLN	0	-0.009	0.002	34.010	0.080	0.080	0.000	0.000	0.000	0.000
117	A	375	SER	0	-0.029	-0.018	34.483	-0.328	-0.328	0.000	0.000	0.000	0.000
118	A	376	TRP	0	0.015	-0.018	32.083	0.032	0.032	0.000	0.000	0.000	0.000
119	A	377	GLY	0	0.000	0.000	33.092	-0.348	-0.348	0.000	0.000	0.000	0.000
120	A	378	VAL	0	-0.030	-0.001	33.102	0.263	0.263	0.000	0.000	0.000	0.000
121	A	379	LEU	0	-0.005	-0.009	33.510	-0.319	-0.319	0.000	0.000	0.000	0.000
122	A	380	ILE	0	-0.010	-0.012	31.135	0.038	0.038	0.000	0.000	0.000	0.000
123	A	381	GLY	0	-0.045	-0.025	35.238	0.222	0.222	0.000	0.000	0.000	0.000
124	A	382	ASP	-1	-0.786	-0.861	37.416	-7.929	-7.929	0.000	0.000	0.000	0.000
125	A	383	SER	0	-0.057	-0.054	38.535	-0.171	-0.171	0.000	0.000	0.000	0.000
126	A	384	VAL	0	-0.008	-0.005	36.114	0.036	0.036	0.000	0.000	0.000	0.000
127	A	385	ALA	0	0.012	0.011	39.106	-0.039	-0.039	0.000	0.000	0.000	0.000
128	A	386	ILE	0	-0.042	-0.026	34.767	-0.124	-0.124	0.000	0.000	0.000	0.000
129	A	387	PRO	0	0.068	0.034	39.024	0.024	0.024	0.000	0.000	0.000	0.000
130	A	388	GLU	-1	-0.748	-0.846	39.270	-7.703	-7.703	0.000	0.000	0.000	0.000
131	A	389	PRO	0	-0.025	0.008	35.323	-0.238	-0.238	0.000	0.000	0.000	0.000
132	A	390	ASN	0	0.016	-0.004	32.202	-0.062	-0.062	0.000	0.000	0.000	0.000
133	A	391	LEU	0	-0.010	0.008	30.458	-0.424	-0.424	0.000	0.000	0.000	0.000
134	A	392	ARG	1	0.869	0.928	25.063	12.469	12.469	0.000	0.000	0.000	0.000
135	A	393	LEU	0	0.057	0.018	26.660	-0.177	-0.177	0.000	0.000	0.000	0.000
136	A	394	HIS	0	-0.027	0.003	21.077	0.247	0.247	0.000	0.000	0.000	0.000
137	A	395	ARG	1	0.979	0.980	20.469	13.158	13.158	0.000	0.000	0.000	0.000
138	A	396	ILE	0	-0.044	-0.014	14.644	-0.071	-0.071	0.000	0.000	0.000	0.000
139	A	397	GLN	0	0.007	0.003	13.760	-0.777	-0.777	0.000	0.000	0.000	0.000
140	A	398	HIS	0	-0.009	-0.023	9.101	-0.052	-0.052	0.000	0.000	0.000	0.000
142	A	400	GLY	0	0.018	0.015	6.838	-2.486	-2.486	0.000	0.000	0.000	0.000
143	A	401	LYS	1	0.829	0.922	9.140	28.294	28.294	0.000	0.000	0.000	0.000
144	A	402	ASP	-1	-0.829	-0.928	11.498	-17.893	-17.893	0.000	0.000	0.000	0.000
145	A	403	TYR	0	-0.043	-0.040	12.974	-0.082	-0.082	0.000	0.000	0.000	0.000
146	A	404	SER	0	0.003	0.003	17.836	0.301	0.301	0.000	0.000	0.000	0.000
147	A	405	PHE	0	0.013	0.003	19.308	0.292	0.292	0.000	0.000	0.000	0.000
148	A	406	SER	0	0.028	0.006	23.928	0.085	0.085	0.000	0.000	0.000	0.000
149	A	407	SER	0	-0.050	-0.042	25.320	-0.023	-0.023	0.000	0.000	0.000	0.000
150	A	408	VAL	0	0.045	0.030	27.428	0.061	0.061	0.000	0.000	0.000	0.000
151	A	409	ARG	1	0.771	0.874	27.958	10.529	10.529	0.000	0.000	0.000	0.000
152	A	410	VAL	0	0.025	0.001	30.096	0.326	0.326	0.000	0.000	0.000	0.000
153	A	411	GLU	-1	-0.791	-0.885	31.556	-10.213	-10.213	0.000	0.000	0.000	0.000
154	A	412	THR	0	0.055	0.016	33.184	-0.102	-0.102	0.000	0.000	0.000	0.000
155	A	413	PRO	0	-0.003	0.004	33.523	0.091	0.091	0.000	0.000	0.000	0.000
156	A	414	LEU	0	0.026	0.009	35.792	0.121	0.121	0.000	0.000	0.000	0.000
157	A	415	LEU	0	-0.009	0.007	36.639	0.151	0.151	0.000	0.000	0.000	0.000
158	A	416	LEU	0	-0.060	-0.018	34.628	0.009	0.009	0.000	0.000	0.000	0.000
159	A	417	VAL	0	0.036	0.022	39.262	0.173	0.173	0.000	0.000	0.000	0.000
160	A	418	VAL	0	0.024	0.016	38.480	-0.127	-0.127	0.000	0.000	0.000	0.000
161	A	419	ASN	0	-0.097	-0.077	41.285	0.235	0.235	0.000	0.000	0.000	0.000
162	A	420	GLY	0	0.015	0.003	43.885	0.174	0.174	0.000	0.000	0.000	0.000
163	A	421	LYS	1	0.880	0.957	44.979	7.135	7.135	0.000	0.000	0.000	0.000
164	A	422	PRO	0	0.056	0.023	43.741	-0.200	-0.200	0.000	0.000	0.000	0.000
165	A	423	GLN	0	-0.058	-0.023	39.089	-0.145	-0.145	0.000	0.000	0.000	0.000
166	A	424	GLY	-1	-0.897	-0.927	41.269	-7.294	-7.294	0.000	0.000	0.000	0.000

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