FMO DATABASE

FMODB ID: 72QRK

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	OptAll
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	-1022286.726537
FMO2-HF: Nuclear repulsion	973820.896819
FMO2-HF: Total energy	-48465.829718
FMO2-MP2: Total energy	-48607.158595

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.
-0.445	0.499	-0.005	-0.429	-0.511	0.001

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 : 0.026 / 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

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	38	ALA	0	0.027	0.015	3.854	-0.594	0.350	-0.005	-0.429	-0.511	0.001
4	A	39	THR	0	-0.025	-0.021	6.444	0.278	0.278	0.000	0.000	0.000	0.000
5	A	40	ASP	-1	-0.871	-0.939	10.154	-0.829	-0.829	0.000	0.000	0.000	0.000
6	A	41	ILE	0	-0.026	-0.007	12.118	0.103	0.103	0.000	0.000	0.000	0.000
7	A	42	TYR	0	0.003	-0.009	15.143	-0.019	-0.019	0.000	0.000	0.000	0.000
8	A	43	ALA	0	0.014	0.013	18.590	0.025	0.025	0.000	0.000	0.000	0.000
9	A	44	VAL	0	0.003	0.016	21.545	-0.010	-0.010	0.000	0.000	0.000	0.000
10	A	45	ASN	0	0.062	0.043	24.765	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	46	GLY	0	0.028	0.014	25.607	0.015	0.015	0.000	0.000	0.000	0.000
12	A	47	THR	0	-0.087	-0.065	25.317	0.012	0.012	0.000	0.000	0.000	0.000
13	A	48	GLU	-1	-0.777	-0.865	24.244	-0.104	-0.104	0.000	0.000	0.000	0.000
14	A	49	ILE	0	-0.011	-0.005	18.823	0.002	0.002	0.000	0.000	0.000	0.000
15	A	50	LEU	0	0.004	0.004	19.756	0.001	0.001	0.000	0.000	0.000	0.000
16	A	51	LEU	0	-0.005	0.002	15.025	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	52	PRO	0	0.009	-0.008	15.557	0.020	0.020	0.000	0.000	0.000	0.000
18	A	53	CYS	0	-0.022	0.013	14.812	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	54	THR	0	0.007	-0.007	13.756	0.022	0.022	0.000	0.000	0.000	0.000
20	A	55	PHE	0	0.011	0.018	15.423	0.032	0.032	0.000	0.000	0.000	0.000
21	A	56	SER	0	0.012	-0.005	16.503	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	57	SER	0	0.008	0.001	19.870	0.019	0.019	0.000	0.000	0.000	0.000
23	A	58	CME	0	-0.001	-0.007	22.448	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	59	PHE	0	0.017	0.007	25.842	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	60	GLY	0	0.065	0.037	24.211	0.002	0.002	0.000	0.000	0.000	0.000
26	A	61	PHE	0	-0.106	-0.032	20.292	0.006	0.006	0.000	0.000	0.000	0.000
27	A	62	GLU	-1	-0.890	-0.953	23.897	0.035	0.035	0.000	0.000	0.000	0.000
28	A	63	ASP	-1	-0.908	-0.952	24.562	0.032	0.032	0.000	0.000	0.000	0.000
29	A	64	LEU	0	-0.025	0.005	20.252	0.004	0.004	0.000	0.000	0.000	0.000
30	A	65	HIS	0	0.000	-0.005	20.919	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	66	PHE	0	-0.019	-0.017	17.897	0.012	0.012	0.000	0.000	0.000	0.000
32	A	67	ARG	1	0.851	0.895	15.136	0.081	0.081	0.000	0.000	0.000	0.000
33	A	68	TRP	0	-0.001	-0.006	13.295	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	69	THR	0	-0.041	-0.033	11.671	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	70	TYR	0	0.024	0.018	12.615	-0.054	-0.054	0.000	0.000	0.000	0.000
36	A	71	ASN	0	-0.031	-0.017	9.041	0.074	0.074	0.000	0.000	0.000	0.000
37	A	72	SER	0	0.003	-0.019	10.906	-0.092	-0.092	0.000	0.000	0.000	0.000
38	A	73	SER	0	-0.029	-0.026	12.221	0.010	0.010	0.000	0.000	0.000	0.000
39	A	74	ASP	-1	-0.922	-0.946	13.263	-0.271	-0.271	0.000	0.000	0.000	0.000
40	A	75	ALA	0	-0.006	0.014	14.164	0.046	0.046	0.000	0.000	0.000	0.000
41	A	76	PHE	0	-0.007	-0.009	12.230	-0.046	-0.046	0.000	0.000	0.000	0.000
42	A	77	LYS	1	0.854	0.920	14.725	0.230	0.230	0.000	0.000	0.000	0.000
43	A	78	ILE	0	-0.014	-0.005	15.388	-0.024	-0.024	0.000	0.000	0.000	0.000
44	A	79	LEU	0	0.001	0.008	15.697	0.007	0.007	0.000	0.000	0.000	0.000
45	A	80	ILE	0	0.013	-0.009	18.847	0.016	0.016	0.000	0.000	0.000	0.000
46	A	81	GLU	-1	-0.834	-0.890	19.058	-0.072	-0.072	0.000	0.000	0.000	0.000
47	A	82	GLY	0	0.036	0.032	21.025	0.001	0.001	0.000	0.000	0.000	0.000
48	A	83	THR	0	-0.049	-0.018	22.420	0.007	0.007	0.000	0.000	0.000	0.000
49	A	84	VAL	0	-0.002	-0.010	22.757	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	85	LYS	1	0.962	0.998	25.338	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	86	ASN	0	0.029	-0.017	26.575	0.004	0.004	0.000	0.000	0.000	0.000
52	A	87	GLU	-1	-0.828	-0.895	25.121	0.016	0.016	0.000	0.000	0.000	0.000
53	A	88	LYS	1	0.928	0.956	26.112	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	89	SER	0	-0.085	-0.025	27.949	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	90	ASP	-1	-0.860	-0.946	28.311	-0.033	-0.033	0.000	0.000	0.000	0.000
56	A	91	PRO	0	-0.046	-0.026	24.595	0.004	0.004	0.000	0.000	0.000	0.000
57	A	92	LYS	1	0.977	1.006	26.776	0.013	0.013	0.000	0.000	0.000	0.000
58	A	93	VAL	0	-0.009	-0.005	24.648	0.001	0.001	0.000	0.000	0.000	0.000
59	A	94	THR	0	-0.064	-0.050	24.931	0.007	0.007	0.000	0.000	0.000	0.000
60	A	95	LEU	0	-0.019	0.005	21.476	0.001	0.001	0.000	0.000	0.000	0.000
61	A	96	LYS	1	0.808	0.872	23.392	0.089	0.089	0.000	0.000	0.000	0.000
62	A	97	ASP	-1	-0.833	-0.900	21.057	-0.165	-0.165	0.000	0.000	0.000	0.000
63	A	98	ASP	-1	-0.785	-0.877	22.761	-0.149	-0.149	0.000	0.000	0.000	0.000
64	A	99	ASP	-1	-0.871	-0.928	24.599	-0.083	-0.083	0.000	0.000	0.000	0.000
65	A	100	ARG	1	0.761	0.846	22.073	0.176	0.176	0.000	0.000	0.000	0.000
66	A	101	ILE	0	-0.019	0.001	19.724	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	102	THR	0	-0.006	-0.003	23.635	0.014	0.014	0.000	0.000	0.000	0.000
68	A	103	LEU	0	-0.006	-0.005	21.358	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	104	VAL	0	-0.003	-0.013	22.113	0.004	0.004	0.000	0.000	0.000	0.000
70	A	105	GLY	0	0.004	0.017	24.855	0.005	0.005	0.000	0.000	0.000	0.000
71	A	106	SER	0	-0.056	-0.025	26.348	0.005	0.005	0.000	0.000	0.000	0.000
72	A	107	THR	0	-0.012	-0.013	24.453	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	108	LYS	1	0.882	0.928	24.196	0.003	0.003	0.000	0.000	0.000	0.000
74	A	109	GLU	-1	-0.841	-0.913	23.262	0.010	0.010	0.000	0.000	0.000	0.000
75	A	110	LYS	1	0.871	0.928	17.374	-0.071	-0.071	0.000	0.000	0.000	0.000
76	A	111	MET	0	-0.012	0.029	19.051	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	112	ASN	0	0.046	-0.006	17.854	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	113	ASN	0	0.036	0.012	21.448	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	114	ILE	0	0.010	0.010	17.831	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	115	SER	0	-0.041	-0.024	18.453	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	116	ILE	0	-0.015	0.004	17.188	0.013	0.013	0.000	0.000	0.000	0.000
82	A	117	VAL	0	-0.030	-0.017	20.310	-0.009	-0.009	0.000	0.000	0.000	0.000
83	A	118	LEU	0	0.005	0.022	19.097	0.006	0.006	0.000	0.000	0.000	0.000
84	A	119	ARG	1	0.824	0.860	22.065	0.096	0.096	0.000	0.000	0.000	0.000
85	A	120	ASP	-1	-0.899	-0.961	24.686	-0.119	-0.119	0.000	0.000	0.000	0.000
86	A	121	LEU	0	-0.054	-0.009	20.458	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	122	GLU	-1	-0.817	-0.880	23.048	-0.156	-0.156	0.000	0.000	0.000	0.000
88	A	123	PHE	0	0.000	-0.023	21.518	-0.019	-0.019	0.000	0.000	0.000	0.000
89	A	124	SER	0	-0.016	-0.035	19.807	-0.034	-0.034	0.000	0.000	0.000	0.000
90	A	125	ASP	-1	-0.783	-0.833	18.471	-0.239	-0.239	0.000	0.000	0.000	0.000
91	A	126	THR	0	-0.007	0.002	15.157	-0.039	-0.039	0.000	0.000	0.000	0.000
92	A	127	GLY	0	-0.009	-0.001	12.399	0.007	0.007	0.000	0.000	0.000	0.000
93	A	128	LYS	1	0.821	0.914	5.890	1.735	1.735	0.000	0.000	0.000	0.000
94	A	129	TYR	0	0.011	-0.006	9.602	0.072	0.072	0.000	0.000	0.000	0.000
95	A	130	THR	0	-0.016	-0.006	7.906	-0.187	-0.187	0.000	0.000	0.000	0.000
96	A	131	TRP	0	0.065	0.058	10.139	0.090	0.090	0.000	0.000	0.000	0.000
97	A	132	HIS	0	-0.002	-0.020	9.869	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	133	VAL	0	0.015	0.003	13.193	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	134	LYS	1	0.835	0.908	15.608	-0.077	-0.077	0.000	0.000	0.000	0.000
100	A	135	ASN	0	0.037	0.029	18.220	-0.016	-0.016	0.000	0.000	0.000	0.000
101	A	136	PRO	0	-0.009	-0.020	21.737	0.012	0.012	0.000	0.000	0.000	0.000
102	A	137	LYS	1	0.845	0.922	23.094	-0.041	-0.041	0.000	0.000	0.000	0.000
103	A	138	GLU	-1	-0.841	-0.905	21.495	0.125	0.125	0.000	0.000	0.000	0.000
104	A	139	ASN	0	0.014	-0.002	21.965	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	140	ASN	0	-0.046	-0.023	17.904	0.030	0.030	0.000	0.000	0.000	0.000
106	A	141	LEU	0	0.032	0.021	12.701	-0.023	-0.023	0.000	0.000	0.000	0.000
107	A	142	GLN	0	0.003	0.007	11.397	-0.035	-0.035	0.000	0.000	0.000	0.000
108	A	143	HIS	0	0.014	0.006	12.121	0.070	0.070	0.000	0.000	0.000	0.000
109	A	144	HIS	0	-0.023	-0.024	5.635	-0.184	-0.184	0.000	0.000	0.000	0.000
110	A	145	ALA	0	0.011	0.013	7.124	0.128	0.128	0.000	0.000	0.000	0.000
111	A	146	THR	0	-0.020	-0.016	5.606	-0.099	-0.099	0.000	0.000	0.000	0.000
112	A	147	ILE	0	-0.011	-0.005	7.481	-0.025	-0.025	0.000	0.000	0.000	0.000
113	A	148	PHE	0	-0.034	-0.034	8.768	-0.132	-0.132	0.000	0.000	0.000	0.000
114	A	149	LEU	0	0.043	0.040	10.592	0.076	0.076	0.000	0.000	0.000	0.000
115	A	150	GLN	0	-0.001	-0.004	14.078	-0.040	-0.040	0.000	0.000	0.000	0.000
116	A	151	VAL	0	0.022	0.019	16.419	0.032	0.032	0.000	0.000	0.000	0.000
117	A	152	VAL	0	-0.016	-0.014	20.043	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	153	ASP	-1	-0.866	-0.941	22.711	-0.150	-0.150	0.000	0.000	0.000	0.000
119	A	154	ARG	1	0.780	0.885	26.474	0.113	0.113	0.000	0.000	0.000	0.000
120	A	155	LEU	0	0.006	0.011	28.845	0.008	0.008	0.000	0.000	0.000	0.000

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