FMO DATABASE

FMODB ID: 94Z62

Calculation Name: 4MZ3-A-Xray372

Preferred Name:

Target Type:

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

ligand 3-letter code: CME

PDB ID: 4MZ3

Chain ID: A

ChEMBL ID:

UniProt ID: Q8IWT1

Base Structure: X-ray

Registration Date: 2023-09-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1020640.6731
FMO2-HF: Nuclear repulsion	972175.700161
FMO2-HF: Total energy	-48464.972939
FMO2-MP2: Total energy	-48606.290826

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:36:GLY)

Summations of interaction energy for fragment #1(A:36: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.
0.344	1.422	-0.009	-0.53	-0.539	0.003

Interaction energy analysis for fragmet #1(A:36:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.030 / q_NPA : 0.002

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

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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	38	ALA	0	0.018	-0.003	3.805	-0.761	0.317	-0.009	-0.530	-0.539	0.003
4	A	39	THR	0	-0.041	-0.011	6.538	0.353	0.353	0.000	0.000	0.000	0.000
5	A	40	ASP	-1	-0.852	-0.913	10.255	-0.871	-0.871	0.000	0.000	0.000	0.000
6	A	41	ILE	0	-0.044	-0.020	12.702	0.093	0.093	0.000	0.000	0.000	0.000
7	A	42	TYR	0	0.030	0.010	15.645	-0.020	-0.020	0.000	0.000	0.000	0.000
8	A	43	ALA	0	0.014	0.010	18.669	0.023	0.023	0.000	0.000	0.000	0.000
9	A	44	VAL	0	0.000	0.018	21.493	-0.006	-0.006	0.000	0.000	0.000	0.000
10	A	45	ASN	0	0.076	0.045	24.734	-0.007	-0.007	0.000	0.000	0.000	0.000
11	A	46	GLY	0	0.020	0.008	25.586	0.016	0.016	0.000	0.000	0.000	0.000
12	A	47	THR	0	-0.122	-0.067	25.153	0.010	0.010	0.000	0.000	0.000	0.000
13	A	48	GLU	-1	-0.878	-0.945	24.093	-0.143	-0.143	0.000	0.000	0.000	0.000
14	A	49	ILE	0	-0.027	-0.012	18.369	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	50	LEU	0	0.008	0.009	19.827	0.004	0.004	0.000	0.000	0.000	0.000
16	A	51	LEU	0	-0.011	-0.013	14.990	-0.029	-0.029	0.000	0.000	0.000	0.000
17	A	52	PRO	0	0.001	-0.006	15.689	0.024	0.024	0.000	0.000	0.000	0.000
18	A	53	CYS	0	-0.012	0.016	15.087	-0.028	-0.028	0.000	0.000	0.000	0.000
19	A	54	THR	0	-0.017	-0.025	14.029	0.031	0.031	0.000	0.000	0.000	0.000
20	A	55	PHE	0	-0.001	0.003	15.823	0.027	0.027	0.000	0.000	0.000	0.000
21	A	56	SER	0	0.020	-0.003	16.767	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	57	SER	0	-0.011	-0.008	19.707	0.017	0.017	0.000	0.000	0.000	0.000
23	A	58	CME	0	0.008	0.006	22.373	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	59	PHE	0	0.028	0.002	25.908	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	60	GLY	0	0.044	0.031	24.020	0.002	0.002	0.000	0.000	0.000	0.000
26	A	61	PHE	0	-0.094	-0.039	20.920	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	62	GLU	-1	-0.923	-0.972	24.329	0.000	0.000	0.000	0.000	0.000	0.000
28	A	63	ASP	-1	-0.963	-0.989	25.479	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	64	LEU	0	-0.071	-0.011	20.464	0.005	0.005	0.000	0.000	0.000	0.000
30	A	65	HIS	0	-0.003	-0.016	20.909	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	66	PHE	0	-0.011	-0.011	17.936	0.005	0.005	0.000	0.000	0.000	0.000
32	A	67	ARG	1	0.876	0.924	14.979	0.129	0.129	0.000	0.000	0.000	0.000
33	A	68	TRP	0	-0.027	-0.010	12.992	-0.024	-0.024	0.000	0.000	0.000	0.000
34	A	69	THR	0	-0.059	-0.043	11.303	0.000	0.000	0.000	0.000	0.000	0.000
35	A	70	TYR	0	-0.001	-0.018	12.408	-0.058	-0.058	0.000	0.000	0.000	0.000
36	A	71	ASN	0	-0.030	-0.018	9.149	0.074	0.074	0.000	0.000	0.000	0.000
37	A	72	SER	0	0.021	0.008	11.115	-0.091	-0.091	0.000	0.000	0.000	0.000
38	A	73	SER	0	-0.027	-0.024	12.376	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	74	ASP	-1	-0.945	-0.965	13.436	-0.270	-0.270	0.000	0.000	0.000	0.000
40	A	75	ALA	0	0.007	0.016	14.325	0.048	0.048	0.000	0.000	0.000	0.000
41	A	76	PHE	0	0.000	-0.006	11.940	-0.051	-0.051	0.000	0.000	0.000	0.000
42	A	77	LYS	1	0.906	0.963	14.736	0.276	0.276	0.000	0.000	0.000	0.000
43	A	78	ILE	0	-0.016	-0.009	15.326	-0.034	-0.034	0.000	0.000	0.000	0.000
44	A	79	LEU	0	0.000	0.005	15.394	0.013	0.013	0.000	0.000	0.000	0.000
45	A	80	ILE	0	0.012	0.001	18.346	0.018	0.018	0.000	0.000	0.000	0.000
46	A	81	GLU	-1	-0.861	-0.921	18.784	-0.111	-0.111	0.000	0.000	0.000	0.000
47	A	82	GLY	0	0.048	0.027	20.872	0.004	0.004	0.000	0.000	0.000	0.000
48	A	83	THR	0	-0.018	-0.004	22.510	0.005	0.005	0.000	0.000	0.000	0.000
49	A	84	VAL	0	-0.021	-0.010	23.272	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	85	LYS	1	0.986	1.007	25.909	0.025	0.025	0.000	0.000	0.000	0.000
51	A	86	ASN	0	0.053	0.025	27.313	0.003	0.003	0.000	0.000	0.000	0.000
52	A	87	GLU	-1	-0.828	-0.931	25.745	-0.026	-0.026	0.000	0.000	0.000	0.000
53	A	88	LYS	1	0.891	0.936	26.900	0.027	0.027	0.000	0.000	0.000	0.000
54	A	89	SER	0	-0.075	-0.015	28.800	0.002	0.002	0.000	0.000	0.000	0.000
55	A	90	ASP	-1	-0.882	-0.950	28.991	-0.066	-0.066	0.000	0.000	0.000	0.000
56	A	91	PRO	0	-0.047	-0.019	25.113	0.004	0.004	0.000	0.000	0.000	0.000
57	A	92	LYS	1	0.964	0.995	27.104	0.043	0.043	0.000	0.000	0.000	0.000
58	A	93	VAL	0	0.002	-0.009	24.283	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	94	THR	0	-0.050	-0.040	24.498	0.006	0.006	0.000	0.000	0.000	0.000
60	A	95	LEU	0	-0.014	0.005	21.195	0.003	0.003	0.000	0.000	0.000	0.000
61	A	96	LYS	1	0.896	0.928	23.025	0.115	0.115	0.000	0.000	0.000	0.000
62	A	97	ASP	-1	-0.891	-0.946	21.375	-0.173	-0.173	0.000	0.000	0.000	0.000
63	A	98	ASP	-1	-0.786	-0.900	23.029	-0.165	-0.165	0.000	0.000	0.000	0.000
64	A	99	ASP	-1	-0.973	-0.980	24.802	-0.110	-0.110	0.000	0.000	0.000	0.000
65	A	100	ARG	1	0.813	0.895	21.881	0.203	0.203	0.000	0.000	0.000	0.000
66	A	101	ILE	0	-0.007	0.005	19.722	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	102	THR	0	-0.010	0.008	23.475	0.017	0.017	0.000	0.000	0.000	0.000
68	A	103	LEU	0	0.001	-0.003	21.770	-0.012	-0.012	0.000	0.000	0.000	0.000
69	A	104	VAL	0	-0.025	-0.021	22.254	0.007	0.007	0.000	0.000	0.000	0.000
70	A	105	GLY	0	0.003	0.016	24.982	0.007	0.007	0.000	0.000	0.000	0.000
71	A	106	SER	0	-0.049	-0.031	26.497	0.008	0.008	0.000	0.000	0.000	0.000
72	A	107	THR	0	-0.001	0.005	25.141	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	108	LYS	1	0.969	0.976	24.677	0.060	0.060	0.000	0.000	0.000	0.000
74	A	109	GLU	-1	-0.918	-0.961	23.612	-0.053	-0.053	0.000	0.000	0.000	0.000
75	A	110	LYS	1	0.901	0.953	16.679	0.058	0.058	0.000	0.000	0.000	0.000
76	A	111	MET	0	-0.023	0.031	19.439	-0.014	-0.014	0.000	0.000	0.000	0.000
77	A	112	ASN	0	0.051	-0.005	18.392	0.003	0.003	0.000	0.000	0.000	0.000
78	A	113	ASN	0	0.012	-0.005	21.938	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	114	ILE	0	0.019	0.017	17.986	0.000	0.000	0.000	0.000	0.000	0.000
80	A	115	SER	0	-0.022	-0.006	18.584	-0.028	-0.028	0.000	0.000	0.000	0.000
81	A	116	ILE	0	-0.010	0.006	17.060	0.020	0.020	0.000	0.000	0.000	0.000
82	A	117	VAL	0	-0.013	-0.006	20.156	-0.017	-0.017	0.000	0.000	0.000	0.000
83	A	118	LEU	0	-0.009	0.005	18.791	0.007	0.007	0.000	0.000	0.000	0.000
84	A	119	ARG	1	0.914	0.917	21.980	0.131	0.131	0.000	0.000	0.000	0.000
85	A	120	ASP	-1	-0.914	-0.956	24.912	-0.139	-0.139	0.000	0.000	0.000	0.000
86	A	121	LEU	0	-0.043	-0.011	20.477	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	122	GLU	-1	-0.854	-0.933	22.789	-0.161	-0.161	0.000	0.000	0.000	0.000
88	A	123	PHE	0	-0.004	-0.019	21.642	-0.023	-0.023	0.000	0.000	0.000	0.000
89	A	124	SER	0	-0.005	-0.005	20.072	-0.024	-0.024	0.000	0.000	0.000	0.000
90	A	125	ASP	-1	-0.783	-0.848	18.561	-0.274	-0.274	0.000	0.000	0.000	0.000
91	A	126	THR	0	0.012	0.024	15.232	-0.048	-0.048	0.000	0.000	0.000	0.000
92	A	127	GLY	0	-0.003	0.011	12.522	0.014	0.014	0.000	0.000	0.000	0.000
93	A	128	LYS	1	0.898	0.947	5.219	2.580	2.580	0.000	0.000	0.000	0.000
94	A	129	TYR	0	0.006	-0.010	9.887	0.107	0.107	0.000	0.000	0.000	0.000
95	A	130	THR	0	-0.004	0.002	7.646	-0.184	-0.184	0.000	0.000	0.000	0.000
96	A	131	TRP	0	0.052	0.046	9.999	0.115	0.115	0.000	0.000	0.000	0.000
97	A	132	HIS	0	-0.024	-0.025	9.745	-0.047	-0.047	0.000	0.000	0.000	0.000
98	A	133	VAL	0	0.017	0.008	13.394	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	134	LYS	1	0.942	0.962	15.822	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	135	ASN	0	0.093	0.049	18.332	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	136	PRO	0	-0.032	-0.022	21.804	0.012	0.012	0.000	0.000	0.000	0.000
102	A	137	LYS	1	0.952	0.981	23.005	-0.012	-0.012	0.000	0.000	0.000	0.000
103	A	138	GLU	-1	-0.922	-0.937	22.030	0.073	0.073	0.000	0.000	0.000	0.000
104	A	139	ASN	0	-0.018	-0.023	22.072	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	140	ASN	0	-0.030	-0.005	17.655	0.022	0.022	0.000	0.000	0.000	0.000
106	A	141	LEU	0	0.003	-0.003	12.643	-0.014	-0.014	0.000	0.000	0.000	0.000
107	A	142	GLN	0	-0.017	-0.003	11.805	-0.045	-0.045	0.000	0.000	0.000	0.000
108	A	143	HIS	0	0.031	0.012	12.027	0.058	0.058	0.000	0.000	0.000	0.000
109	A	144	HIS	0	-0.010	-0.013	5.433	-0.189	-0.189	0.000	0.000	0.000	0.000
110	A	145	ALA	0	-0.001	0.006	7.610	0.063	0.063	0.000	0.000	0.000	0.000
111	A	146	THR	0	-0.015	-0.016	5.479	0.013	0.013	0.000	0.000	0.000	0.000
112	A	147	ILE	0	-0.011	-0.003	7.548	-0.135	-0.135	0.000	0.000	0.000	0.000
113	A	148	PHE	0	-0.083	-0.043	8.991	-0.091	-0.091	0.000	0.000	0.000	0.000
114	A	149	LEU	0	0.031	0.025	10.577	0.089	0.089	0.000	0.000	0.000	0.000
115	A	150	GLN	0	-0.006	-0.017	14.287	-0.033	-0.033	0.000	0.000	0.000	0.000
116	A	151	VAL	0	0.016	0.014	16.637	0.030	0.030	0.000	0.000	0.000	0.000
117	A	152	VAL	0	-0.020	-0.014	20.190	0.001	0.001	0.000	0.000	0.000	0.000
118	A	153	ASP	-1	-0.858	-0.937	22.905	-0.162	-0.162	0.000	0.000	0.000	0.000
119	A	154	ARG	1	0.801	0.894	26.629	0.134	0.134	0.000	0.000	0.000	0.000
120	A	155	LEU	0	0.000	0.007	29.220	0.007	0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:36:GLY)