FMO DATABASE

FMODB ID: 3G4QL

Calculation Name: 1OCS-A-Xray547

Preferred Name:

Target Type:

Ligand Name: s,s-(2-hydroxyethyl)thiocysteine | glycerol

Ligand 3-letter code: CME | GOL

Ligand of Interest (LOI):

PDB ID: 1OCS

Chain ID: A

ChEMBL ID:

UniProt ID: Q08826

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1213396.268538
FMO2-HF: Nuclear repulsion	1158832.883363
FMO2-HF: Total energy	-54563.385175
FMO2-MP2: Total energy	-54720.62152

3D Structure

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:30:ALA)

Summations of interaction energy for fragment #1(A:30: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.
76.616	77.922	0.001	-0.483	-0.824	0

Interaction energy analysis for fragmet #1(A:30:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.828 / q_NPA : 0.904

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].
3	A	32	PRO	0	0.008	0.008	3.704	-1.974	-0.813	0.003	-0.458	-0.706
38	A	67	ASN	0	-0.018	-0.030	4.012	3.358	3.429	-0.001	-0.015	-0.055
45	A	74	ARG	1	0.837	0.901	4.031	46.423	46.497	-0.001	-0.010	-0.063
4	A	33	GLU	-1	-0.902	-0.939	6.139	-21.888	-21.888	0.000	0.000	0.000
5	A	34	ASN	0	-0.029	-0.009	7.021	-4.903	-4.903	0.000	0.000	0.000
6	A	35	PHE	0	0.011	0.010	5.694	1.751	1.751	0.000	0.000	0.000
7	A	36	LEU	0	-0.008	0.000	10.125	-0.623	-0.623	0.000	0.000	0.000
8	A	37	GLU	-1	-0.791	-0.833	11.389	-23.678	-23.678	0.000	0.000	0.000
9	A	38	ILE	0	-0.026	-0.030	14.349	-0.036	-0.036	0.000	0.000	0.000
10	A	39	GLU	-1	-0.887	-0.927	17.641	-13.353	-13.353	0.000	0.000	0.000
11	A	40	VAL	0	-0.068	-0.028	20.844	-0.035	-0.035	0.000	0.000	0.000
12	A	41	HIS	0	0.052	-0.006	22.290	0.822	0.822	0.000	0.000	0.000
13	A	42	ASN	0	-0.029	-0.007	25.751	0.154	0.154	0.000	0.000	0.000
14	A	43	PRO	0	0.055	0.035	27.723	-0.023	-0.023	0.000	0.000	0.000
15	A	44	LYS	1	0.943	0.973	30.166	10.162	10.162	0.000	0.000	0.000
16	A	45	THR	0	0.038	0.006	33.060	-0.066	-0.066	0.000	0.000	0.000
17	A	46	HIS	0	-0.087	-0.056	32.102	0.163	0.163	0.000	0.000	0.000
18	A	47	ILE	0	0.042	0.004	37.298	0.124	0.124	0.000	0.000	0.000
19	A	48	PRO	0	-0.028	0.002	40.946	-0.092	-0.092	0.000	0.000	0.000
20	A	49	ASN	0	0.010	-0.011	40.866	0.169	0.169	0.000	0.000	0.000
21	A	50	GLY	0	0.034	0.019	44.618	0.122	0.122	0.000	0.000	0.000
22	A	51	MET	0	-0.011	0.006	46.782	-0.074	-0.074	0.000	0.000	0.000
23	A	52	ASP	-1	-0.860	-0.919	47.599	-6.392	-6.392	0.000	0.000	0.000
24	A	53	SER	0	-0.105	-0.050	42.587	-0.222	-0.222	0.000	0.000	0.000
25	A	54	LYS	1	0.942	0.950	35.340	8.716	8.716	0.000	0.000	0.000
26	A	55	GLY	0	0.060	0.037	41.642	0.000	0.000	0.000	0.000	0.000
27	A	56	MET	0	-0.017	0.001	40.797	-0.212	-0.212	0.000	0.000	0.000
28	A	57	PHE	0	-0.061	-0.039	33.477	0.048	0.048	0.000	0.000	0.000
29	A	58	THR	0	0.004	-0.002	35.029	-0.030	-0.030	0.000	0.000	0.000
30	A	59	ASP	-1	-0.854	-0.907	30.245	-10.124	-10.124	0.000	0.000	0.000
31	A	60	TYR	0	0.028	0.005	27.869	0.137	0.137	0.000	0.000	0.000
32	A	61	GLU	-1	-0.831	-0.900	22.462	-13.357	-13.357	0.000	0.000	0.000
33	A	62	ILE	0	0.007	0.009	20.017	-0.019	-0.019	0.000	0.000	0.000
34	A	63	ILE	0	0.002	0.004	16.909	-0.267	-0.267	0.000	0.000	0.000
35	A	64	CYS	0	-0.042	-0.034	15.020	-0.055	-0.055	0.000	0.000	0.000
36	A	65	ARG	1	0.826	0.870	9.859	25.724	25.724	0.000	0.000	0.000
37	A	66	THR	0	-0.003	-0.020	9.497	0.660	0.660	0.000	0.000	0.000
39	A	68	LEU	0	0.015	0.024	6.346	-0.547	-0.547	0.000	0.000	0.000
40	A	69	PRO	0	0.011	0.001	8.780	0.678	0.678	0.000	0.000	0.000
41	A	70	SER	0	-0.044	-0.021	10.163	0.883	0.883	0.000	0.000	0.000
42	A	71	PHE	0	-0.027	-0.025	11.229	1.696	1.696	0.000	0.000	0.000
43	A	72	HIS	1	0.827	0.882	11.910	17.507	17.507	0.000	0.000	0.000
44	A	73	LYS	1	0.897	0.950	11.072	17.606	17.606	0.000	0.000	0.000
46	A	75	VAL	0	0.013	0.009	9.587	0.078	0.078	0.000	0.000	0.000
47	A	76	SER	0	-0.012	-0.010	12.666	0.801	0.801	0.000	0.000	0.000
48	A	77	LYS	1	0.889	0.936	16.299	13.749	13.749	0.000	0.000	0.000
49	A	78	VAL	0	0.010	0.031	19.420	0.366	0.366	0.000	0.000	0.000
50	A	79	ARG	1	0.800	0.889	22.598	11.246	11.246	0.000	0.000	0.000
51	A	80	ARG	1	0.760	0.874	22.949	12.541	12.541	0.000	0.000	0.000
52	A	81	ARG	1	0.941	0.973	28.156	8.901	8.901	0.000	0.000	0.000
53	A	82	TYR	0	-0.026	-0.036	30.857	-0.139	-0.139	0.000	0.000	0.000
54	A	83	SER	0	0.049	0.018	32.456	-0.051	-0.051	0.000	0.000	0.000
55	A	84	ASP	-1	-0.842	-0.912	28.885	-9.984	-9.984	0.000	0.000	0.000
56	A	85	PHE	0	0.052	0.011	25.420	-0.210	-0.210	0.000	0.000	0.000
57	A	86	GLU	-1	-0.912	-0.968	29.365	-8.605	-8.605	0.000	0.000	0.000
58	A	87	PHE	0	-0.030	-0.017	30.489	0.146	0.146	0.000	0.000	0.000
59	A	88	PHE	0	0.066	0.040	22.922	-0.015	-0.015	0.000	0.000	0.000
60	A	89	ARG	1	0.856	0.911	28.151	9.351	9.351	0.000	0.000	0.000
61	A	90	LYS	1	0.915	0.954	29.646	8.457	8.457	0.000	0.000	0.000
62	A	91	CYS	0	-0.021	-0.007	28.457	0.147	0.147	0.000	0.000	0.000
63	A	92	LEU	0	0.004	0.009	23.763	-0.009	-0.009	0.000	0.000	0.000
64	A	93	ILE	0	0.004	0.000	27.227	-0.044	-0.044	0.000	0.000	0.000
65	A	94	LYS	1	0.968	0.993	30.128	8.907	8.907	0.000	0.000	0.000
66	A	95	GLU	-1	-0.698	-0.807	23.657	-12.496	-12.496	0.000	0.000	0.000
67	A	96	ILE	0	0.010	0.002	25.755	-0.095	-0.095	0.000	0.000	0.000
68	A	97	SER	0	-0.087	-0.051	27.613	0.139	0.139	0.000	0.000	0.000
69	A	98	MET	0	-0.007	-0.011	28.958	0.144	0.144	0.000	0.000	0.000
70	A	99	LEU	0	-0.048	-0.021	23.108	-0.065	-0.065	0.000	0.000	0.000
71	A	100	ASN	0	-0.035	-0.009	26.782	0.093	0.093	0.000	0.000	0.000
72	A	101	HIS	0	0.054	0.034	24.050	0.183	0.183	0.000	0.000	0.000
73	A	102	PRO	0	0.022	0.002	28.683	0.005	0.005	0.000	0.000	0.000
74	A	103	LYS	1	0.928	0.952	30.723	9.308	9.308	0.000	0.000	0.000
75	A	104	VAL	0	-0.014	0.011	25.491	-0.035	-0.035	0.000	0.000	0.000
76	A	105	MET	0	-0.001	0.000	28.739	0.250	0.250	0.000	0.000	0.000
77	A	106	VAL	0	0.046	0.025	27.088	-0.242	-0.242	0.000	0.000	0.000
78	A	107	PRO	0	0.075	0.047	27.795	0.465	0.465	0.000	0.000	0.000
79	A	108	HIS	0	0.006	0.006	30.741	-0.150	-0.150	0.000	0.000	0.000
80	A	109	LEU	0	0.026	0.027	29.538	-0.135	-0.135	0.000	0.000	0.000
81	A	110	PRO	0	0.029	0.017	31.255	0.366	0.366	0.000	0.000	0.000
82	A	111	GLY	0	0.076	0.053	34.160	-0.087	-0.087	0.000	0.000	0.000
83	A	112	LYS	1	0.902	0.972	35.909	8.488	8.488	0.000	0.000	0.000
84	A	113	ILE	0	0.003	-0.001	38.103	0.097	0.097	0.000	0.000	0.000
85	A	114	LEU	0	-0.014	-0.011	39.661	-0.146	-0.146	0.000	0.000	0.000
86	A	115	LEU	0	0.018	0.012	43.211	0.129	0.129	0.000	0.000	0.000
87	A	116	SER	0	0.029	0.008	43.695	0.158	0.158	0.000	0.000	0.000
88	A	117	ASN	0	0.035	0.010	44.373	-0.158	-0.158	0.000	0.000	0.000
89	A	118	ARG	1	0.974	0.986	40.176	7.403	7.403	0.000	0.000	0.000
90	A	119	PHE	0	-0.042	-0.026	39.470	-0.222	-0.222	0.000	0.000	0.000
91	A	120	SER	0	0.014	0.013	41.190	-0.018	-0.018	0.000	0.000	0.000
92	A	121	ASN	0	0.032	-0.011	38.356	-0.190	-0.190	0.000	0.000	0.000
93	A	122	GLU	-1	-0.854	-0.891	37.780	-7.400	-7.400	0.000	0.000	0.000
94	A	123	VAL	0	0.054	0.027	37.910	-0.243	-0.243	0.000	0.000	0.000
95	A	124	ILE	0	-0.036	-0.013	34.217	-0.273	-0.273	0.000	0.000	0.000
96	A	125	GLU	-1	-0.762	-0.859	32.469	-10.161	-10.161	0.000	0.000	0.000
97	A	126	GLU	-1	-0.930	-0.963	33.125	-8.343	-8.343	0.000	0.000	0.000
98	A	127	ARG	1	0.808	0.903	33.287	8.311	8.311	0.000	0.000	0.000
99	A	128	ARG	1	0.871	0.937	28.140	10.211	10.211	0.000	0.000	0.000
100	A	129	GLN	0	-0.050	-0.036	28.633	-0.429	-0.429	0.000	0.000	0.000
101	A	130	GLY	0	0.017	0.006	29.061	-0.297	-0.297	0.000	0.000	0.000
102	A	131	LEU	0	-0.050	-0.034	27.884	-0.210	-0.210	0.000	0.000	0.000
103	A	132	ASN	0	0.044	0.035	23.463	-0.793	-0.793	0.000	0.000	0.000
104	A	133	THR	0	0.009	-0.002	24.510	-0.495	-0.495	0.000	0.000	0.000
105	A	134	TRP	0	-0.051	-0.048	25.727	-0.312	-0.312	0.000	0.000	0.000
106	A	135	MET	0	-0.005	-0.001	20.713	0.025	0.025	0.000	0.000	0.000
107	A	136	GLN	0	-0.013	-0.014	20.432	-0.111	-0.111	0.000	0.000	0.000
108	A	137	SER	0	-0.036	-0.007	21.026	-0.475	-0.475	0.000	0.000	0.000
109	A	138	VAL	0	-0.022	-0.022	22.506	-0.186	-0.186	0.000	0.000	0.000
110	A	139	ALA	0	-0.015	-0.015	17.885	-0.224	-0.224	0.000	0.000	0.000
111	A	140	GLY	0	0.061	0.045	17.380	-1.057	-1.057	0.000	0.000	0.000
112	A	141	HIS	0	0.030	0.014	18.620	-0.592	-0.592	0.000	0.000	0.000
113	A	142	PRO	0	0.060	0.026	16.970	-0.206	-0.206	0.000	0.000	0.000
114	A	143	LEU	0	0.006	0.011	17.568	-0.400	-0.400	0.000	0.000	0.000
115	A	144	LEU	0	-0.057	-0.017	20.103	0.205	0.205	0.000	0.000	0.000
116	A	145	GLN	0	-0.001	-0.014	14.424	-0.785	-0.785	0.000	0.000	0.000
117	A	146	SER	0	-0.044	-0.014	15.071	-0.542	-0.542	0.000	0.000	0.000
118	A	147	GLY	0	0.013	0.005	16.329	0.016	0.016	0.000	0.000	0.000
119	A	148	SER	0	-0.105	-0.081	19.531	0.338	0.338	0.000	0.000	0.000
120	A	149	LYS	1	0.910	0.940	18.422	14.041	14.041	0.000	0.000	0.000
121	A	150	VAL	0	-0.022	-0.012	20.821	-0.158	-0.158	0.000	0.000	0.000
122	A	151	LEU	0	0.003	-0.008	17.988	0.075	0.075	0.000	0.000	0.000
123	A	152	VAL	0	0.009	0.015	15.820	-0.073	-0.073	0.000	0.000	0.000
124	A	153	ARG	0	0.003	0.005	18.213	-0.243	-0.243	0.000	0.000	0.000
125	A	154	PHE	0	-0.001	-0.016	21.115	0.184	0.184	0.000	0.000	0.000
126	A	155	ILE	0	0.002	0.004	16.384	0.220	0.220	0.000	0.000	0.000
127	A	156	GLU	-1	-0.793	-0.891	14.331	-19.258	-19.258	0.000	0.000	0.000
128	A	157	ALA	0	-0.025	0.007	18.544	-0.042	-0.042	0.000	0.000	0.000
129	A	158	GLU	-1	-0.901	-0.940	22.022	-11.525	-11.525	0.000	0.000	0.000
130	A	159	LYS	1	0.915	0.954	24.278	10.005	10.005	0.000	0.000	0.000
131	A	160	PHE	0	-0.016	-0.002	24.886	-0.124	-0.124	0.000	0.000	0.000
132	A	161	VAL	-1	-0.891	-0.950	27.089	-9.813	-9.813	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:30:ALA)