FMO DATABASE

FMODB ID: MV47Z

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	OptHSide
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	-1020537.724317
FMO2-HF: Nuclear repulsion	972072.132685
FMO2-HF: Total energy	-48465.591632
FMO2-MP2: Total energy	-48606.874366

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.
-0.4	0.718	-0.01	-0.555	-0.553	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 : 0.025 / q_NPA : 0.001

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	0.024	-0.001	3.805	-0.827	0.291	-0.010	-0.555	-0.553	0.003
4	A	39	THR	0	-0.037	-0.011	6.538	0.312	0.312	0.000	0.000	0.000	0.000
5	A	40	ASP	-1	-0.888	-0.932	10.255	-0.861	-0.861	0.000	0.000	0.000	0.000
6	A	41	ILE	0	-0.030	-0.008	12.702	0.092	0.092	0.000	0.000	0.000	0.000
7	A	42	TYR	0	0.013	0.000	15.318	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	43	ALA	0	0.016	0.011	18.665	0.023	0.023	0.000	0.000	0.000	0.000
9	A	44	VAL	0	0.002	0.017	21.488	-0.006	-0.006	0.000	0.000	0.000	0.000
10	A	45	ASN	0	0.076	0.047	24.726	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	46	GLY	0	0.029	0.009	25.581	0.017	0.017	0.000	0.000	0.000	0.000
12	A	47	THR	0	-0.123	-0.072	25.227	0.011	0.011	0.000	0.000	0.000	0.000
13	A	48	GLU	-1	-0.847	-0.933	24.079	-0.145	-0.145	0.000	0.000	0.000	0.000
14	A	49	ILE	0	-0.024	-0.012	18.487	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	50	LEU	0	0.002	0.008	19.941	0.003	0.003	0.000	0.000	0.000	0.000
16	A	51	LEU	0	-0.002	-0.005	14.888	-0.027	-0.027	0.000	0.000	0.000	0.000
17	A	52	PRO	0	0.002	-0.010	15.731	0.022	0.022	0.000	0.000	0.000	0.000
18	A	53	CYS	0	-0.012	0.014	15.087	-0.028	-0.028	0.000	0.000	0.000	0.000
19	A	54	THR	0	0.004	-0.013	14.170	0.030	0.030	0.000	0.000	0.000	0.000
20	A	55	PHE	0	0.000	0.013	15.767	0.028	0.028	0.000	0.000	0.000	0.000
21	A	56	SER	0	0.016	0.003	16.765	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	57	SER	0	-0.005	-0.013	19.705	0.016	0.016	0.000	0.000	0.000	0.000
23	A	58	CME	0	-0.020	-0.004	22.372	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	59	PHE	0	0.054	0.012	25.895	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	60	GLY	0	0.053	0.041	24.009	0.002	0.002	0.000	0.000	0.000	0.000
26	A	61	PHE	0	-0.088	-0.035	20.897	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	62	GLU	-1	-0.913	-0.966	24.326	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	63	ASP	-1	-0.950	-0.992	25.476	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	64	LEU	0	-0.063	-0.008	20.621	0.004	0.004	0.000	0.000	0.000	0.000
30	A	65	HIS	0	0.000	-0.013	20.909	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	66	PHE	0	-0.003	-0.010	17.937	0.004	0.004	0.000	0.000	0.000	0.000
32	A	67	ARG	1	0.838	0.894	14.973	0.140	0.140	0.000	0.000	0.000	0.000
33	A	68	TRP	0	-0.021	-0.010	13.008	-0.026	-0.026	0.000	0.000	0.000	0.000
34	A	69	THR	0	-0.053	-0.043	11.321	0.001	0.001	0.000	0.000	0.000	0.000
35	A	70	TYR	0	0.019	0.011	12.406	-0.064	-0.064	0.000	0.000	0.000	0.000
36	A	71	ASN	0	-0.038	-0.024	9.131	0.062	0.062	0.000	0.000	0.000	0.000
37	A	72	SER	0	0.022	-0.001	11.111	-0.085	-0.085	0.000	0.000	0.000	0.000
38	A	73	SER	0	-0.037	-0.023	12.372	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	74	ASP	-1	-0.938	-0.963	13.398	-0.276	-0.276	0.000	0.000	0.000	0.000
40	A	75	ALA	0	0.001	0.015	14.325	0.049	0.049	0.000	0.000	0.000	0.000
41	A	76	PHE	0	0.005	-0.007	12.139	-0.053	-0.053	0.000	0.000	0.000	0.000
42	A	77	LYS	1	0.859	0.922	14.737	0.277	0.277	0.000	0.000	0.000	0.000
43	A	78	ILE	0	-0.013	-0.011	15.325	-0.036	-0.036	0.000	0.000	0.000	0.000
44	A	79	LEU	0	0.016	0.012	15.858	0.014	0.014	0.000	0.000	0.000	0.000
45	A	80	ILE	0	0.010	0.001	18.346	0.020	0.020	0.000	0.000	0.000	0.000
46	A	81	GLU	-1	-0.837	-0.895	18.785	-0.121	-0.121	0.000	0.000	0.000	0.000
47	A	82	GLY	0	0.042	0.026	20.873	0.005	0.005	0.000	0.000	0.000	0.000
48	A	83	THR	0	-0.014	-0.002	22.512	0.005	0.005	0.000	0.000	0.000	0.000
49	A	84	VAL	0	-0.025	-0.009	23.286	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	85	LYS	1	0.987	1.005	25.912	0.026	0.026	0.000	0.000	0.000	0.000
51	A	86	ASN	0	0.063	0.022	27.274	0.003	0.003	0.000	0.000	0.000	0.000
52	A	87	GLU	-1	-0.843	-0.930	25.781	-0.031	-0.031	0.000	0.000	0.000	0.000
53	A	88	LYS	1	0.905	0.942	26.897	0.029	0.029	0.000	0.000	0.000	0.000
54	A	89	SER	0	-0.077	-0.009	28.628	0.001	0.001	0.000	0.000	0.000	0.000
55	A	90	ASP	-1	-0.873	-0.949	28.993	-0.069	-0.069	0.000	0.000	0.000	0.000
56	A	91	PRO	0	-0.047	-0.021	25.105	0.004	0.004	0.000	0.000	0.000	0.000
57	A	92	LYS	1	0.958	0.993	27.113	0.047	0.047	0.000	0.000	0.000	0.000
58	A	93	VAL	0	0.008	-0.005	24.357	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	94	THR	0	-0.047	-0.039	24.402	0.007	0.007	0.000	0.000	0.000	0.000
60	A	95	LEU	0	-0.021	-0.002	20.972	0.003	0.003	0.000	0.000	0.000	0.000
61	A	96	LYS	1	0.828	0.882	23.034	0.118	0.118	0.000	0.000	0.000	0.000
62	A	97	ASP	-1	-0.853	-0.905	21.286	-0.190	-0.190	0.000	0.000	0.000	0.000
63	A	98	ASP	-1	-0.761	-0.876	23.003	-0.170	-0.170	0.000	0.000	0.000	0.000
64	A	99	ASP	-1	-0.904	-0.943	24.801	-0.113	-0.113	0.000	0.000	0.000	0.000
65	A	100	ARG	1	0.777	0.865	21.884	0.207	0.207	0.000	0.000	0.000	0.000
66	A	101	ILE	0	-0.012	0.006	19.681	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	102	THR	0	-0.006	0.010	23.474	0.018	0.018	0.000	0.000	0.000	0.000
68	A	103	LEU	0	0.000	-0.006	21.698	-0.012	-0.012	0.000	0.000	0.000	0.000
69	A	104	VAL	0	-0.022	-0.021	22.342	0.007	0.007	0.000	0.000	0.000	0.000
70	A	105	GLY	0	0.007	0.016	24.981	0.007	0.007	0.000	0.000	0.000	0.000
71	A	106	SER	0	-0.041	-0.027	26.497	0.007	0.007	0.000	0.000	0.000	0.000
72	A	107	THR	0	-0.016	-0.003	25.001	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	108	LYS	1	0.902	0.930	24.676	0.060	0.060	0.000	0.000	0.000	0.000
74	A	109	GLU	-1	-0.853	-0.915	23.754	-0.055	-0.055	0.000	0.000	0.000	0.000
75	A	110	LYS	1	0.871	0.928	17.371	0.056	0.056	0.000	0.000	0.000	0.000
76	A	111	MET	0	-0.015	0.032	19.437	-0.014	-0.014	0.000	0.000	0.000	0.000
77	A	112	ASN	0	0.060	-0.003	18.397	0.004	0.004	0.000	0.000	0.000	0.000
78	A	113	ASN	0	0.019	0.002	21.938	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	114	ILE	0	0.005	0.011	18.212	0.000	0.000	0.000	0.000	0.000	0.000
80	A	115	SER	0	-0.031	-0.013	18.585	-0.028	-0.028	0.000	0.000	0.000	0.000
81	A	116	ILE	0	-0.005	0.008	16.970	0.021	0.021	0.000	0.000	0.000	0.000
82	A	117	VAL	0	-0.031	-0.013	20.154	-0.016	-0.016	0.000	0.000	0.000	0.000
83	A	118	LEU	0	-0.002	0.010	18.859	0.006	0.006	0.000	0.000	0.000	0.000
84	A	119	ARG	1	0.915	0.929	21.977	0.132	0.132	0.000	0.000	0.000	0.000
85	A	120	ASP	-1	-0.918	-0.960	24.909	-0.141	-0.141	0.000	0.000	0.000	0.000
86	A	121	LEU	0	-0.040	-0.015	20.456	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	122	GLU	-1	-0.857	-0.925	22.768	-0.166	-0.166	0.000	0.000	0.000	0.000
88	A	123	PHE	0	-0.003	-0.021	21.638	-0.023	-0.023	0.000	0.000	0.000	0.000
89	A	124	SER	0	0.001	-0.002	20.067	-0.029	-0.029	0.000	0.000	0.000	0.000
90	A	125	ASP	-1	-0.788	-0.851	18.557	-0.277	-0.277	0.000	0.000	0.000	0.000
91	A	126	THR	0	-0.007	0.010	15.274	-0.049	-0.049	0.000	0.000	0.000	0.000
92	A	127	GLY	0	0.000	0.002	12.519	0.012	0.012	0.000	0.000	0.000	0.000
93	A	128	LYS	1	0.863	0.936	6.008	2.005	2.005	0.000	0.000	0.000	0.000
94	A	129	TYR	0	0.002	-0.007	9.883	0.105	0.105	0.000	0.000	0.000	0.000
95	A	130	THR	0	-0.007	-0.002	7.602	-0.179	-0.179	0.000	0.000	0.000	0.000
96	A	131	TRP	0	0.059	0.051	9.999	0.117	0.117	0.000	0.000	0.000	0.000
97	A	132	HIS	0	-0.010	-0.017	9.637	-0.054	-0.054	0.000	0.000	0.000	0.000
98	A	133	VAL	0	0.013	0.003	13.396	0.000	0.000	0.000	0.000	0.000	0.000
99	A	134	LYS	1	0.901	0.936	15.818	-0.030	-0.030	0.000	0.000	0.000	0.000
100	A	135	ASN	0	0.065	0.042	18.329	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	136	PRO	0	-0.023	-0.025	21.801	0.012	0.012	0.000	0.000	0.000	0.000
102	A	137	LYS	1	0.901	0.965	23.002	0.000	0.000	0.000	0.000	0.000	0.000
103	A	138	GLU	-1	-0.892	-0.906	21.691	0.071	0.071	0.000	0.000	0.000	0.000
104	A	139	ASN	0	-0.032	-0.045	22.069	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	140	ASN	0	-0.030	-0.005	17.585	0.026	0.026	0.000	0.000	0.000	0.000
106	A	141	LEU	0	0.025	0.012	12.597	-0.018	-0.018	0.000	0.000	0.000	0.000
107	A	142	GLN	0	-0.013	0.000	11.733	-0.043	-0.043	0.000	0.000	0.000	0.000
108	A	143	HIS	0	0.025	0.008	12.030	0.045	0.045	0.000	0.000	0.000	0.000
109	A	144	HIS	0	-0.017	-0.019	5.712	-0.170	-0.170	0.000	0.000	0.000	0.000
110	A	145	ALA	0	0.001	0.011	7.603	0.065	0.065	0.000	0.000	0.000	0.000
111	A	146	THR	0	-0.015	-0.017	5.510	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	147	ILE	0	-0.007	-0.001	7.546	-0.124	-0.124	0.000	0.000	0.000	0.000
113	A	148	PHE	0	-0.053	-0.039	8.943	-0.124	-0.124	0.000	0.000	0.000	0.000
114	A	149	LEU	0	0.031	0.029	10.573	0.089	0.089	0.000	0.000	0.000	0.000
115	A	150	GLN	0	-0.004	-0.012	14.282	-0.024	-0.024	0.000	0.000	0.000	0.000
116	A	151	VAL	0	0.028	0.022	16.632	0.029	0.029	0.000	0.000	0.000	0.000
117	A	152	VAL	0	-0.021	-0.015	20.185	0.002	0.002	0.000	0.000	0.000	0.000
118	A	153	ASP	-1	-0.864	-0.937	22.899	-0.160	-0.160	0.000	0.000	0.000	0.000
119	A	154	ARG	1	0.801	0.894	26.623	0.133	0.133	0.000	0.000	0.000	0.000
120	A	155	LEU	0	0.001	0.008	29.140	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)