FMO DATABASE

FMODB ID: Y7MM2

Calculation Name: 6FAS-A-Xray547

Preferred Name:

Target Type:

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

Ligand 3-letter code: CME

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6FAS

Chain ID: A

ChEMBL ID:

UniProt ID: Q8W4L5

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
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	110
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-847047.249175
FMO2-HF: Nuclear repulsion	803254.24091
FMO2-HF: Total energy	-43793.008265
FMO2-MP2: Total energy	-43917.408222

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:287:MET)

Summations of interaction energy for fragment #1(A:287:MET)

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.
23.529	27.965	1.817	-2.214	-4.038	-0.019

Interaction energy analysis for fragmet #1(A:287:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.841 / 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	289	LEU	0	0.011	0.010	2.669	-6.222	-2.966	0.550	-1.696	-2.110	-0.015
4	A	290	ASN	0	0.020	0.002	4.337	3.775	3.982	-0.001	-0.012	-0.194	0.000
98	A	384	PRO	0	-0.038	-0.031	2.277	-3.195	-2.222	1.269	-0.504	-1.738	-0.004
99	A	385	GLY	0	0.029	-0.004	5.365	-0.073	-0.073	-0.001	-0.002	0.004	0.000
5	A	291	ILE	0	-0.004	0.007	6.090	0.469	0.469	0.000	0.000	0.000	0.000
6	A	292	VAL	0	-0.014	-0.003	7.241	0.001	0.001	0.000	0.000	0.000	0.000
7	A	293	PRO	0	0.020	0.009	9.848	0.725	0.725	0.000	0.000	0.000	0.000
8	A	294	LEU	0	-0.063	-0.021	13.224	-0.317	-0.317	0.000	0.000	0.000	0.000
9	A	295	PHE	0	0.001	-0.011	15.739	0.654	0.654	0.000	0.000	0.000	0.000
10	A	296	GLU	-1	-0.787	-0.859	19.328	-12.520	-12.520	0.000	0.000	0.000	0.000
11	A	297	LYS	1	0.818	0.905	22.176	10.082	10.082	0.000	0.000	0.000	0.000
12	A	298	THR	0	0.012	0.014	25.909	-0.039	-0.039	0.000	0.000	0.000	0.000
13	A	299	LEU	0	-0.066	-0.025	28.674	0.124	0.124	0.000	0.000	0.000	0.000
14	A	300	SER	0	0.042	-0.016	31.193	0.336	0.336	0.000	0.000	0.000	0.000
15	A	301	ALA	0	0.029	-0.012	34.575	-0.071	-0.071	0.000	0.000	0.000	0.000
16	A	302	SER	0	-0.038	-0.018	36.267	0.139	0.139	0.000	0.000	0.000	0.000
17	A	303	ASP	-1	-0.818	-0.879	31.274	-9.393	-9.393	0.000	0.000	0.000	0.000
18	A	304	ALA	0	0.012	0.011	33.007	-0.173	-0.173	0.000	0.000	0.000	0.000
19	A	305	GLY	0	0.048	0.048	34.463	0.154	0.154	0.000	0.000	0.000	0.000
20	A	306	ARG	1	0.951	0.948	37.161	7.167	7.167	0.000	0.000	0.000	0.000
21	A	307	ILE	0	-0.051	-0.021	37.728	0.083	0.083	0.000	0.000	0.000	0.000
22	A	308	GLY	0	0.061	0.038	34.740	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	309	ARG	1	0.885	0.942	32.911	8.037	8.037	0.000	0.000	0.000	0.000
24	A	310	LEU	0	0.021	0.025	26.881	0.166	0.166	0.000	0.000	0.000	0.000
25	A	311	VAL	0	0.008	-0.005	29.782	-0.192	-0.192	0.000	0.000	0.000	0.000
26	A	312	LEU	0	0.008	0.004	24.300	-0.134	-0.134	0.000	0.000	0.000	0.000
27	A	313	PRO	0	0.028	0.008	24.636	0.335	0.335	0.000	0.000	0.000	0.000
28	A	314	LYS	1	0.845	0.913	25.127	9.652	9.652	0.000	0.000	0.000	0.000
29	A	315	ALA	0	0.047	0.014	23.851	-0.254	-0.254	0.000	0.000	0.000	0.000
30	A	316	CYS	0	-0.017	-0.001	20.897	-0.470	-0.470	0.000	0.000	0.000	0.000
31	A	317	ALA	0	0.003	-0.002	20.665	-0.568	-0.568	0.000	0.000	0.000	0.000
32	A	318	GLU	-1	-0.786	-0.870	22.015	-10.994	-10.994	0.000	0.000	0.000	0.000
33	A	319	ALA	0	-0.004	0.022	18.309	-0.180	-0.180	0.000	0.000	0.000	0.000
34	A	320	TYR	0	-0.032	-0.023	14.807	-1.076	-1.076	0.000	0.000	0.000	0.000
35	A	321	PHE	0	-0.047	-0.019	17.360	-0.581	-0.581	0.000	0.000	0.000	0.000
36	A	322	PRO	0	0.016	0.006	19.262	0.057	0.057	0.000	0.000	0.000	0.000
37	A	323	PRO	0	0.041	0.027	20.425	0.568	0.568	0.000	0.000	0.000	0.000
38	A	324	ILE	0	0.001	0.013	23.381	0.164	0.164	0.000	0.000	0.000	0.000
39	A	325	SER	0	0.026	0.004	26.808	0.131	0.131	0.000	0.000	0.000	0.000
40	A	326	GLN	0	-0.021	-0.012	30.067	0.227	0.227	0.000	0.000	0.000	0.000
41	A	327	SER	0	0.004	0.010	31.370	-0.160	-0.160	0.000	0.000	0.000	0.000
42	A	328	GLU	-1	-0.810	-0.912	33.474	-8.933	-8.933	0.000	0.000	0.000	0.000
43	A	329	GLY	0	-0.027	-0.010	29.333	-0.097	-0.097	0.000	0.000	0.000	0.000
44	A	330	ILE	0	-0.021	-0.010	23.267	0.032	0.032	0.000	0.000	0.000	0.000
45	A	331	PRO	0	0.016	0.013	26.586	-0.040	-0.040	0.000	0.000	0.000	0.000
46	A	332	LEU	0	-0.033	-0.009	20.520	-0.494	-0.494	0.000	0.000	0.000	0.000
47	A	333	LYS	1	0.880	0.932	20.966	13.977	13.977	0.000	0.000	0.000	0.000
48	A	334	ILE	0	-0.001	0.001	19.149	-0.752	-0.752	0.000	0.000	0.000	0.000
49	A	335	GLN	0	-0.017	-0.012	18.030	-0.291	-0.291	0.000	0.000	0.000	0.000
50	A	336	ASP	-1	-0.728	-0.842	18.875	-13.188	-13.188	0.000	0.000	0.000	0.000
51	A	337	VAL	0	0.041	0.010	18.143	-0.319	-0.319	0.000	0.000	0.000	0.000
52	A	338	ARG	1	0.885	0.949	20.064	11.154	11.154	0.000	0.000	0.000	0.000
53	A	339	GLY	0	0.036	0.026	20.626	0.355	0.355	0.000	0.000	0.000	0.000
54	A	340	ARG	1	0.793	0.895	21.686	11.469	11.469	0.000	0.000	0.000	0.000
55	A	341	GLU	-1	-0.870	-0.938	20.164	-15.334	-15.334	0.000	0.000	0.000	0.000
56	A	342	TRP	0	-0.001	-0.011	23.010	0.801	0.801	0.000	0.000	0.000	0.000
57	A	343	THR	0	-0.013	-0.008	24.046	-0.470	-0.470	0.000	0.000	0.000	0.000
58	A	344	PHE	0	0.003	-0.008	24.423	0.446	0.446	0.000	0.000	0.000	0.000
59	A	345	GLN	0	0.018	0.006	27.191	-0.457	-0.457	0.000	0.000	0.000	0.000
60	A	346	PHE	0	-0.010	-0.001	23.833	0.203	0.203	0.000	0.000	0.000	0.000
61	A	347	ARG	1	0.849	0.902	27.275	9.012	9.012	0.000	0.000	0.000	0.000
62	A	348	TYR	0	-0.032	-0.037	29.668	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	349	TRP	0	0.013	0.019	31.887	0.231	0.231	0.000	0.000	0.000	0.000
64	A	350	PRO	0	0.034	0.008	35.047	-0.155	-0.155	0.000	0.000	0.000	0.000
65	A	351	ASN	0	-0.019	-0.011	36.090	0.188	0.188	0.000	0.000	0.000	0.000
66	A	352	ASN	0	0.017	0.005	37.580	0.058	0.058	0.000	0.000	0.000	0.000
67	A	353	ASN	0	0.007	0.011	38.583	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	354	SER	0	0.020	0.008	33.664	-0.308	-0.308	0.000	0.000	0.000	0.000
69	A	355	ARG	1	0.848	0.927	28.782	10.083	10.083	0.000	0.000	0.000	0.000
70	A	356	MET	0	-0.020	-0.001	32.037	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	357	TYR	0	-0.007	-0.022	27.289	0.049	0.049	0.000	0.000	0.000	0.000
72	A	358	VAL	0	-0.022	-0.015	29.585	0.070	0.070	0.000	0.000	0.000	0.000
73	A	359	LEU	0	0.007	0.020	24.369	-0.281	-0.281	0.000	0.000	0.000	0.000
74	A	360	GLU	-1	-0.848	-0.933	28.811	-8.629	-8.629	0.000	0.000	0.000	0.000
75	A	361	GLY	0	0.047	0.016	30.706	-0.259	-0.259	0.000	0.000	0.000	0.000
76	A	362	VAL	0	-0.006	-0.007	28.596	-0.087	-0.087	0.000	0.000	0.000	0.000
77	A	363	THR	0	0.024	0.011	30.894	-0.176	-0.176	0.000	0.000	0.000	0.000
78	A	364	PRO	0	0.006	0.006	31.618	0.038	0.038	0.000	0.000	0.000	0.000
79	A	365	CYS	0	-0.003	0.030	26.385	-0.087	-0.087	0.000	0.000	0.000	0.000
80	A	366	ILE	0	0.043	0.011	29.036	-0.076	-0.076	0.000	0.000	0.000	0.000
81	A	367	GLN	0	0.031	0.019	30.986	0.122	0.122	0.000	0.000	0.000	0.000
82	A	368	SER	0	-0.043	-0.029	30.128	0.127	0.127	0.000	0.000	0.000	0.000
83	A	369	MET	0	-0.074	-0.024	24.080	-0.282	-0.282	0.000	0.000	0.000	0.000
84	A	370	MET	0	-0.026	-0.001	29.599	0.090	0.090	0.000	0.000	0.000	0.000
85	A	371	LEU	0	-0.026	-0.002	27.535	0.085	0.085	0.000	0.000	0.000	0.000
86	A	372	GLN	0	0.016	-0.003	32.100	0.159	0.159	0.000	0.000	0.000	0.000
87	A	373	ALA	0	-0.015	-0.019	33.068	-0.230	-0.230	0.000	0.000	0.000	0.000
88	A	374	GLY	0	0.023	0.014	33.143	0.178	0.178	0.000	0.000	0.000	0.000
89	A	375	ASP	-1	-0.730	-0.833	29.691	-9.331	-9.331	0.000	0.000	0.000	0.000
90	A	376	THR	0	-0.036	-0.020	24.228	0.033	0.033	0.000	0.000	0.000	0.000
91	A	377	VAL	0	-0.009	0.002	23.257	-0.211	-0.211	0.000	0.000	0.000	0.000
92	A	378	THR	0	-0.040	-0.034	19.096	-0.166	-0.166	0.000	0.000	0.000	0.000
93	A	379	PHE	0	0.009	-0.009	18.743	-0.025	-0.025	0.000	0.000	0.000	0.000
94	A	380	SER	0	0.027	0.001	13.621	-0.279	-0.279	0.000	0.000	0.000	0.000
95	A	381	ARG	1	0.874	0.937	9.642	23.984	23.984	0.000	0.000	0.000	0.000
96	A	382	VAL	0	-0.005	0.007	8.296	-0.558	-0.558	0.000	0.000	0.000	0.000
97	A	383	ASP	-1	-0.780	-0.881	5.751	-29.277	-29.277	0.000	0.000	0.000	0.000
100	A	386	GLY	0	0.008	0.014	8.780	2.342	2.342	0.000	0.000	0.000	0.000
101	A	387	LYS	1	0.896	0.959	11.322	20.501	20.501	0.000	0.000	0.000	0.000
102	A	388	LEU	0	0.028	0.018	13.237	-0.430	-0.430	0.000	0.000	0.000	0.000
103	A	389	ILE	0	-0.029	-0.022	13.201	0.334	0.334	0.000	0.000	0.000	0.000
104	A	390	MET	0	-0.013	-0.011	16.900	0.316	0.316	0.000	0.000	0.000	0.000
105	A	391	GLY	0	0.029	0.018	19.468	-0.115	-0.115	0.000	0.000	0.000	0.000
106	A	392	SER	0	-0.036	-0.023	21.035	0.110	0.110	0.000	0.000	0.000	0.000
107	A	393	ARG	1	0.833	0.887	22.181	11.601	11.601	0.000	0.000	0.000	0.000
108	A	394	LYS	1	0.804	0.878	26.098	9.074	9.074	0.000	0.000	0.000	0.000
109	A	395	ALA	0	-0.020	-0.014	29.173	-0.219	-0.219	0.000	0.000	0.000	0.000
110	A	396	ALA	-1	-0.940	-0.950	30.762	-8.473	-8.473	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:287:MET)