FMO DATABASE

FMODB ID: 74L4K

Calculation Name: 1VSD-A-Xray549

Preferred Name:

Target Type:

Ligand Name: 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid | hydroxyethylcysteine

Ligand 3-letter code: EPE | OCY

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VSD

Chain ID: A

ChEMBL ID:

UniProt ID: O92956

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1307029.896842
FMO2-HF: Nuclear repulsion	1251046.460845
FMO2-HF: Total energy	-55983.435997
FMO2-MP2: Total energy	-56146.888363

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:54:GLY)

Summations of interaction energy for fragment #1(A:54:GLY)

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.
81.741	83.569	0.031	-0.813	-1.046	-0.005

Interaction energy analysis for fragmet #1(A:54:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.916

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	56	GLY	0	0.008	0.018	2.833	7.955	9.732	0.032	-0.787	-1.022	-0.005
4	A	57	PRO	0	0.028	0.019	4.083	1.551	1.602	-0.001	-0.026	-0.024	0.000
5	A	58	LEU	0	0.031	0.010	6.448	-3.224	-3.224	0.000	0.000	0.000	0.000
6	A	59	GLN	0	0.059	0.026	7.451	1.011	1.011	0.000	0.000	0.000	0.000
7	A	60	ILE	0	0.007	0.012	10.186	2.026	2.026	0.000	0.000	0.000	0.000
8	A	61	TRP	0	0.049	0.033	13.493	0.836	0.836	0.000	0.000	0.000	0.000
9	A	62	GLN	0	0.032	0.017	16.545	1.130	1.130	0.000	0.000	0.000	0.000
10	A	63	THR	0	-0.030	-0.006	19.901	-0.112	-0.112	0.000	0.000	0.000	0.000
11	A	64	ASP	-1	-0.798	-0.881	23.044	-11.066	-11.066	0.000	0.000	0.000	0.000
12	A	65	PHE	0	-0.043	-0.030	26.702	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	66	THR	0	0.011	0.012	30.082	0.344	0.344	0.000	0.000	0.000	0.000
14	A	67	LEU	0	-0.002	0.005	32.004	0.060	0.060	0.000	0.000	0.000	0.000
15	A	68	GLU	-1	-0.819	-0.916	34.589	-8.645	-8.645	0.000	0.000	0.000	0.000
16	A	69	PRO	0	0.021	-0.009	36.547	0.067	0.067	0.000	0.000	0.000	0.000
17	A	70	ARG	1	0.889	0.939	38.321	8.095	8.095	0.000	0.000	0.000	0.000
18	A	71	MET	0	0.002	0.015	34.071	0.170	0.170	0.000	0.000	0.000	0.000
19	A	72	ALA	0	0.022	0.029	38.270	-0.021	-0.021	0.000	0.000	0.000	0.000
20	A	73	PRO	0	0.007	-0.005	41.115	0.082	0.082	0.000	0.000	0.000	0.000
21	A	74	ARG	1	0.872	0.931	34.692	8.913	8.913	0.000	0.000	0.000	0.000
22	A	75	SER	0	0.072	0.039	36.361	-0.222	-0.222	0.000	0.000	0.000	0.000
23	A	76	TRP	0	0.004	0.009	33.817	-0.158	-0.158	0.000	0.000	0.000	0.000
24	A	77	LEU	0	0.018	0.007	30.393	-0.095	-0.095	0.000	0.000	0.000	0.000
25	A	78	ALA	0	0.004	0.020	27.632	-0.045	-0.045	0.000	0.000	0.000	0.000
26	A	79	VAL	0	0.010	-0.006	24.107	-0.129	-0.129	0.000	0.000	0.000	0.000
27	A	80	THR	0	-0.019	-0.017	19.126	0.114	0.114	0.000	0.000	0.000	0.000
28	A	81	VAL	0	0.003	0.003	17.706	0.245	0.245	0.000	0.000	0.000	0.000
29	A	82	ASP	-1	-0.781	-0.870	12.609	-25.093	-25.093	0.000	0.000	0.000	0.000
30	A	83	THR	0	-0.102	-0.086	13.611	-0.064	-0.064	0.000	0.000	0.000	0.000
31	A	84	ALA	0	-0.047	-0.015	8.754	-0.484	-0.484	0.000	0.000	0.000	0.000
32	A	85	SER	0	0.001	-0.039	10.488	-0.279	-0.279	0.000	0.000	0.000	0.000
33	A	86	SER	0	-0.057	-0.030	12.636	1.522	1.522	0.000	0.000	0.000	0.000
34	A	87	ALA	0	0.029	0.038	15.501	1.261	1.261	0.000	0.000	0.000	0.000
35	A	88	ILE	0	-0.022	-0.020	17.413	0.059	0.059	0.000	0.000	0.000	0.000
36	A	89	VAL	0	0.043	0.014	19.997	0.360	0.360	0.000	0.000	0.000	0.000
37	A	90	VAL	0	-0.019	-0.017	22.610	0.186	0.186	0.000	0.000	0.000	0.000
38	A	91	THR	0	0.016	-0.004	26.319	0.284	0.284	0.000	0.000	0.000	0.000
39	A	92	GLN	0	-0.022	-0.015	29.141	0.083	0.083	0.000	0.000	0.000	0.000
40	A	93	HIS	0	0.000	-0.008	29.655	0.426	0.426	0.000	0.000	0.000	0.000
41	A	94	GLY	0	0.015	0.010	34.804	0.136	0.136	0.000	0.000	0.000	0.000
42	A	95	ARG	1	0.904	0.940	36.975	7.952	7.952	0.000	0.000	0.000	0.000
43	A	96	VAL	0	0.056	0.047	33.203	-0.191	-0.191	0.000	0.000	0.000	0.000
44	A	97	THR	0	-0.001	-0.008	33.758	0.195	0.195	0.000	0.000	0.000	0.000
45	A	98	SER	0	0.029	-0.009	31.293	-0.161	-0.161	0.000	0.000	0.000	0.000
46	A	99	VAL	0	-0.006	0.006	30.526	-0.346	-0.346	0.000	0.000	0.000	0.000
47	A	100	ALA	0	0.014	0.021	31.131	-0.230	-0.230	0.000	0.000	0.000	0.000
48	A	101	ALA	0	0.049	0.024	27.357	-0.285	-0.285	0.000	0.000	0.000	0.000
49	A	102	GLN	0	0.028	0.031	26.508	-0.342	-0.342	0.000	0.000	0.000	0.000
50	A	103	HIS	0	0.030	0.010	26.683	-0.572	-0.572	0.000	0.000	0.000	0.000
51	A	104	HIS	0	-0.004	0.014	23.553	0.242	0.242	0.000	0.000	0.000	0.000
52	A	105	TRP	0	0.036	-0.010	21.986	-0.280	-0.280	0.000	0.000	0.000	0.000
53	A	106	ALA	0	-0.028	-0.008	22.327	-0.620	-0.620	0.000	0.000	0.000	0.000
54	A	107	THR	0	-0.017	-0.009	23.616	-0.166	-0.166	0.000	0.000	0.000	0.000
55	A	108	ALA	0	-0.010	-0.009	20.236	-0.359	-0.359	0.000	0.000	0.000	0.000
56	A	109	ILE	0	-0.030	-0.020	18.065	-0.806	-0.806	0.000	0.000	0.000	0.000
57	A	110	ALA	0	-0.049	-0.015	18.734	-0.697	-0.697	0.000	0.000	0.000	0.000
58	A	111	VAL	0	-0.032	-0.007	19.325	-0.061	-0.061	0.000	0.000	0.000	0.000
59	A	112	LEU	0	-0.015	-0.007	15.385	-0.511	-0.511	0.000	0.000	0.000	0.000
60	A	113	GLY	0	0.022	0.032	14.142	-1.847	-1.847	0.000	0.000	0.000	0.000
61	A	114	ARG	1	0.891	0.923	14.211	18.587	18.587	0.000	0.000	0.000	0.000
62	A	115	PRO	0	-0.031	0.004	12.550	-2.041	-2.041	0.000	0.000	0.000	0.000
63	A	116	LYS	1	0.903	0.944	8.880	30.055	30.055	0.000	0.000	0.000	0.000
64	A	117	ALA	0	0.014	0.001	12.706	1.419	1.419	0.000	0.000	0.000	0.000
65	A	118	ILE	0	0.002	0.004	15.653	-0.649	-0.649	0.000	0.000	0.000	0.000
66	A	119	LYS	1	0.868	0.944	18.504	17.205	17.205	0.000	0.000	0.000	0.000
67	A	120	THR	0	-0.015	-0.015	20.549	-0.090	-0.090	0.000	0.000	0.000	0.000
68	A	121	ASP	-1	-0.775	-0.875	24.251	-10.980	-10.980	0.000	0.000	0.000	0.000
69	A	122	ASN	0	0.017	-0.002	27.546	-0.271	-0.271	0.000	0.000	0.000	0.000
70	A	123	GLY	0	0.060	0.040	29.986	0.360	0.360	0.000	0.000	0.000	0.000
71	A	124	SER	0	0.015	0.004	30.948	-0.304	-0.304	0.000	0.000	0.000	0.000
72	A	125	CYS	0	-0.044	-0.013	29.984	0.024	0.024	0.000	0.000	0.000	0.000
73	A	126	PHE	0	0.037	0.021	26.725	-0.254	-0.254	0.000	0.000	0.000	0.000
74	A	127	THR	0	0.026	0.012	27.863	-0.148	-0.148	0.000	0.000	0.000	0.000
75	A	128	SER	0	0.002	0.021	29.930	0.244	0.244	0.000	0.000	0.000	0.000
76	A	129	LYS	1	0.992	0.991	30.451	9.531	9.531	0.000	0.000	0.000	0.000
77	A	130	SER	0	-0.058	-0.049	30.877	-0.126	-0.126	0.000	0.000	0.000	0.000
78	A	131	THR	0	0.025	-0.003	26.499	-0.083	-0.083	0.000	0.000	0.000	0.000
79	A	132	ARG	1	0.923	0.960	26.104	10.212	10.212	0.000	0.000	0.000	0.000
80	A	133	GLU	-1	-0.923	-0.955	25.935	-11.328	-11.328	0.000	0.000	0.000	0.000
81	A	134	TRP	0	-0.023	-0.014	22.365	-0.286	-0.286	0.000	0.000	0.000	0.000
82	A	135	LEU	0	0.015	-0.005	21.059	-0.388	-0.388	0.000	0.000	0.000	0.000
83	A	136	ALA	0	0.008	0.013	21.576	-0.710	-0.710	0.000	0.000	0.000	0.000
84	A	137	ARG	1	0.936	0.971	22.662	10.976	10.976	0.000	0.000	0.000	0.000
85	A	138	TRP	0	0.024	0.007	19.395	-0.529	-0.529	0.000	0.000	0.000	0.000
86	A	139	GLY	0	-0.045	-0.007	18.680	-1.056	-1.056	0.000	0.000	0.000	0.000
87	A	140	ILE	0	-0.064	-0.020	16.738	-1.108	-1.108	0.000	0.000	0.000	0.000
88	A	141	ALA	0	0.007	0.003	16.685	1.004	1.004	0.000	0.000	0.000	0.000
89	A	142	HIS	0	-0.027	-0.024	18.470	-0.228	-0.228	0.000	0.000	0.000	0.000
90	A	143	THR	0	-0.009	-0.014	19.158	0.129	0.129	0.000	0.000	0.000	0.000
91	A	144	THR	0	0.000	-0.013	22.003	-0.080	-0.080	0.000	0.000	0.000	0.000
92	A	145	GLY	0	-0.049	-0.011	22.465	0.175	0.175	0.000	0.000	0.000	0.000
93	A	146	ILE	0	0.032	0.018	23.406	0.164	0.164	0.000	0.000	0.000	0.000
94	A	147	PRO	0	0.012	0.000	26.307	0.120	0.120	0.000	0.000	0.000	0.000
95	A	148	GLY	0	0.041	0.014	29.696	0.307	0.307	0.000	0.000	0.000	0.000
96	A	149	ASN	0	-0.033	-0.028	23.471	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	150	SER	0	0.009	0.030	27.614	-0.077	-0.077	0.000	0.000	0.000	0.000
98	A	151	GLN	0	0.038	0.015	25.882	0.110	0.110	0.000	0.000	0.000	0.000
99	A	152	GLY	0	0.003	0.010	22.461	-0.076	-0.076	0.000	0.000	0.000	0.000
100	A	153	GLN	0	0.006	-0.023	21.347	-1.396	-1.396	0.000	0.000	0.000	0.000
101	A	154	ALA	0	0.081	0.037	22.872	0.186	0.186	0.000	0.000	0.000	0.000
102	A	155	MET	0	-0.052	-0.011	16.290	0.095	0.095	0.000	0.000	0.000	0.000
103	A	156	VAL	0	0.037	0.022	21.683	0.273	0.273	0.000	0.000	0.000	0.000
104	A	157	GLU	-1	-0.881	-0.937	23.478	-11.146	-11.146	0.000	0.000	0.000	0.000
105	A	158	ARG	1	0.906	0.956	21.677	14.099	14.099	0.000	0.000	0.000	0.000
106	A	159	ALA	0	0.032	0.018	22.941	0.336	0.336	0.000	0.000	0.000	0.000
107	A	160	ASN	0	-0.009	-0.035	25.045	0.262	0.262	0.000	0.000	0.000	0.000
108	A	161	ARG	1	0.903	0.956	28.328	11.336	11.336	0.000	0.000	0.000	0.000
109	A	162	LEU	0	0.017	0.001	25.070	0.323	0.323	0.000	0.000	0.000	0.000
110	A	163	LEU	0	0.024	0.021	27.600	0.260	0.260	0.000	0.000	0.000	0.000
111	A	164	LYS	1	0.864	0.931	29.289	9.588	9.588	0.000	0.000	0.000	0.000
112	A	165	ASP	-1	-0.828	-0.890	32.433	-8.860	-8.860	0.000	0.000	0.000	0.000
113	A	166	LYS	1	0.951	0.989	29.299	10.693	10.693	0.000	0.000	0.000	0.000
114	A	167	ILE	0	0.011	-0.012	31.747	0.233	0.233	0.000	0.000	0.000	0.000
115	A	168	ARG	1	0.775	0.874	34.425	8.674	8.674	0.000	0.000	0.000	0.000
116	A	169	VAL	0	0.003	-0.005	34.678	0.229	0.229	0.000	0.000	0.000	0.000
117	A	170	LEU	0	-0.011	-0.001	32.410	0.141	0.141	0.000	0.000	0.000	0.000
118	A	171	ALA	0	-0.026	-0.009	36.917	0.180	0.180	0.000	0.000	0.000	0.000
119	A	172	GLU	-1	-0.821	-0.917	39.644	-7.574	-7.574	0.000	0.000	0.000	0.000
120	A	173	GLY	0	-0.013	0.003	40.243	0.190	0.190	0.000	0.000	0.000	0.000
121	A	174	ASP	-1	-0.900	-0.947	39.146	-8.098	-8.098	0.000	0.000	0.000	0.000
122	A	175	GLY	0	0.023	0.014	42.194	0.163	0.163	0.000	0.000	0.000	0.000
123	A	176	PHE	0	-0.036	-0.037	41.052	0.168	0.168	0.000	0.000	0.000	0.000
124	A	177	MET	0	0.029	0.020	43.049	-0.195	-0.195	0.000	0.000	0.000	0.000
125	A	178	LYS	1	0.918	0.950	45.010	6.658	6.658	0.000	0.000	0.000	0.000
126	A	179	ARG	1	0.839	0.918	42.696	7.094	7.094	0.000	0.000	0.000	0.000
127	A	180	ILE	0	0.023	0.024	37.724	0.142	0.142	0.000	0.000	0.000	0.000
128	A	181	PRO	0	0.013	0.012	41.890	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	182	THR	0	0.055	0.010	41.643	-0.136	-0.136	0.000	0.000	0.000	0.000
130	A	183	SER	0	-0.013	0.002	40.696	-0.205	-0.205	0.000	0.000	0.000	0.000
131	A	184	LYS	1	0.982	0.994	39.781	7.449	7.449	0.000	0.000	0.000	0.000
132	A	185	GLN	0	-0.051	-0.021	37.123	-0.326	-0.326	0.000	0.000	0.000	0.000
133	A	186	GLY	0	0.030	0.016	34.183	-0.233	-0.233	0.000	0.000	0.000	0.000
134	A	187	GLU	-1	-0.875	-0.939	33.172	-8.897	-8.897	0.000	0.000	0.000	0.000
135	A	188	LEU	0	-0.033	-0.009	33.677	-0.223	-0.223	0.000	0.000	0.000	0.000
136	A	189	LEU	0	0.004	-0.009	29.887	-0.179	-0.179	0.000	0.000	0.000	0.000
137	A	190	ALA	0	0.018	0.012	29.174	-0.397	-0.397	0.000	0.000	0.000	0.000
138	A	191	LYS	1	0.904	0.959	28.941	8.413	8.413	0.000	0.000	0.000	0.000
139	A	192	ALA	0	-0.015	-0.024	29.988	-0.184	-0.184	0.000	0.000	0.000	0.000
140	A	193	MET	0	-0.009	-0.002	22.673	-0.148	-0.148	0.000	0.000	0.000	0.000
141	A	194	TYR	0	0.032	0.029	24.847	-0.574	-0.574	0.000	0.000	0.000	0.000
142	A	195	ALA	0	-0.004	-0.007	25.222	-0.368	-0.368	0.000	0.000	0.000	0.000
143	A	196	LEU	0	-0.087	-0.042	24.469	0.105	0.105	0.000	0.000	0.000	0.000
144	A	197	ASN	0	-0.093	-0.054	20.275	-1.240	-1.240	0.000	0.000	0.000	0.000
145	A	198	HIS	0	-0.035	-0.020	20.462	-0.272	-0.272	0.000	0.000	0.000	0.000
146	A	199	PHE	-1	-0.928	-0.941	21.474	-12.868	-12.868	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:54:GLY)