FMO DATABASE

FMODB ID: 6N77Z

Calculation Name: 2HZE-A-Xray372

Preferred Name:

Target Type:

Ligand Name: s-(dimethylarsenic)cysteine

ligand 3-letter code: CAS

PDB ID: 2HZE

Chain ID: A

ChEMBL ID:

UniProt ID: Q8JLF5

Base Structure: X-ray

Registration Date: 2023-06-22

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	110
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-898410.823335
FMO2-HF: Nuclear repulsion	854123.844213
FMO2-HF: Total energy	-44286.979122
FMO2-MP2: Total energy	-44416.074139

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:-2:HIS)

Summations of interaction energy for fragment #1(A:-2:HIS)

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.
-0.987	1.389	-0.034	-1.216	-1.126	-0.003

Interaction energy analysis for fragmet #1(A:-2:HIS)

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 : -0.030

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	0	GLN	0	0.027	0.028	3.807	-0.541	1.835	-0.034	-1.216	-1.126	-0.003
4	A	1	MET	0	0.065	0.040	6.414	-0.734	-0.734	0.000	0.000	0.000	0.000
5	A	2	ALA	0	0.027	0.005	9.427	0.123	0.123	0.000	0.000	0.000	0.000
6	A	3	GLU	-1	-0.942	-0.973	12.810	0.171	0.171	0.000	0.000	0.000	0.000
7	A	4	GLU	-1	-0.852	-0.930	9.020	1.291	1.291	0.000	0.000	0.000	0.000
8	A	5	PHE	0	-0.059	-0.030	12.191	0.017	0.017	0.000	0.000	0.000	0.000
9	A	6	VAL	0	-0.025	-0.025	13.759	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	7	GLN	0	0.021	0.005	16.785	0.011	0.011	0.000	0.000	0.000	0.000
11	A	8	GLN	0	-0.035	-0.014	12.663	0.050	0.050	0.000	0.000	0.000	0.000
12	A	9	ARG	1	0.882	0.964	14.146	-0.551	-0.551	0.000	0.000	0.000	0.000
13	A	10	LEU	0	-0.039	0.007	19.903	-0.038	-0.038	0.000	0.000	0.000	0.000
14	A	11	ALA	0	0.001	-0.012	22.661	0.021	0.021	0.000	0.000	0.000	0.000
15	A	12	ASN	0	-0.009	-0.015	25.448	-0.015	-0.015	0.000	0.000	0.000	0.000
16	A	13	ASN	0	-0.039	-0.010	28.828	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	14	LYS	1	0.815	0.885	22.835	-0.296	-0.296	0.000	0.000	0.000	0.000
18	A	15	VAL	0	-0.006	0.015	28.881	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	16	THR	0	0.000	-0.009	22.288	0.013	0.013	0.000	0.000	0.000	0.000
20	A	17	ILE	0	-0.018	0.004	25.320	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	18	PHE	0	0.013	0.019	18.427	0.017	0.017	0.000	0.000	0.000	0.000
22	A	19	VAL	0	0.029	-0.019	22.498	-0.032	-0.032	0.000	0.000	0.000	0.000
23	A	20	LYS	1	0.910	0.961	20.428	-0.032	-0.032	0.000	0.000	0.000	0.000
24	A	21	TYR	0	0.071	0.010	23.452	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	22	THR	0	-0.005	-0.006	25.355	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	23	CYS	0	-0.046	0.023	27.003	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	24	PRO	0	0.048	0.002	28.823	0.009	0.009	0.000	0.000	0.000	0.000
28	A	25	PHE	0	0.077	0.031	31.110	0.004	0.004	0.000	0.000	0.000	0.000
29	A	26	CYS	0	-0.012	-0.008	26.927	0.004	0.004	0.000	0.000	0.000	0.000
30	A	27	ARG	1	0.924	0.972	29.567	-0.087	-0.087	0.000	0.000	0.000	0.000
31	A	28	ASN	0	0.057	0.035	31.896	0.005	0.005	0.000	0.000	0.000	0.000
32	A	29	ALA	0	0.019	0.012	30.850	0.000	0.000	0.000	0.000	0.000	0.000
33	A	30	LEU	0	-0.048	-0.039	27.952	0.004	0.004	0.000	0.000	0.000	0.000
34	A	31	ASP	-1	-0.908	-0.939	32.018	0.101	0.101	0.000	0.000	0.000	0.000
35	A	32	ILE	0	-0.026	-0.012	35.516	0.000	0.000	0.000	0.000	0.000	0.000
36	A	33	LEU	0	-0.011	-0.014	30.794	0.002	0.002	0.000	0.000	0.000	0.000
37	A	34	ASN	0	-0.029	-0.018	34.352	0.010	0.010	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.849	0.940	35.536	-0.076	-0.076	0.000	0.000	0.000	0.000
39	A	36	PHE	0	-0.012	0.006	36.701	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	37	SER	0	-0.013	0.004	36.742	0.006	0.006	0.000	0.000	0.000	0.000
41	A	38	PHE	0	0.063	0.024	32.838	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	39	LYS	1	0.889	0.937	33.878	-0.126	-0.126	0.000	0.000	0.000	0.000
43	A	40	ARG	1	0.982	0.980	29.429	-0.222	-0.222	0.000	0.000	0.000	0.000
44	A	41	GLY	0	-0.002	-0.005	27.612	0.001	0.001	0.000	0.000	0.000	0.000
45	A	42	ALA	0	0.002	0.016	27.539	0.010	0.010	0.000	0.000	0.000	0.000
46	A	43	TYR	0	0.022	0.013	28.686	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	44	GLU	-1	-0.865	-0.923	20.758	0.382	0.382	0.000	0.000	0.000	0.000
48	A	45	ILE	0	-0.014	-0.005	24.590	-0.017	-0.017	0.000	0.000	0.000	0.000
49	A	46	VAL	0	0.020	0.012	18.492	0.022	0.022	0.000	0.000	0.000	0.000
50	A	47	ASP	-1	-0.804	-0.906	19.475	0.198	0.198	0.000	0.000	0.000	0.000
51	A	48	ILE	0	0.025	-0.002	17.324	0.031	0.031	0.000	0.000	0.000	0.000
52	A	49	LYS	1	0.798	0.900	16.275	-0.246	-0.246	0.000	0.000	0.000	0.000
53	A	50	GLU	-1	-0.929	-0.967	13.758	0.488	0.488	0.000	0.000	0.000	0.000
54	A	51	PHE	0	-0.064	-0.016	10.130	0.069	0.069	0.000	0.000	0.000	0.000
55	A	52	LYS	1	0.903	0.971	9.907	-0.168	-0.168	0.000	0.000	0.000	0.000
56	A	53	PRO	0	0.079	0.047	8.578	-0.029	-0.029	0.000	0.000	0.000	0.000
57	A	54	GLU	-1	-0.815	-0.941	11.424	0.015	0.015	0.000	0.000	0.000	0.000
58	A	55	ASN	0	-0.029	-0.032	14.082	0.048	0.048	0.000	0.000	0.000	0.000
59	A	56	GLU	-1	-0.760	-0.874	9.745	-0.785	-0.785	0.000	0.000	0.000	0.000
60	A	57	LEU	0	-0.012	-0.001	13.943	0.046	0.046	0.000	0.000	0.000	0.000
61	A	58	ARG	1	0.868	0.943	15.778	0.098	0.098	0.000	0.000	0.000	0.000
62	A	59	ASP	-1	-0.877	-0.947	16.817	-0.222	-0.222	0.000	0.000	0.000	0.000
63	A	60	TYR	0	0.042	0.019	16.096	0.030	0.030	0.000	0.000	0.000	0.000
64	A	61	PHE	0	0.001	-0.015	18.170	0.021	0.021	0.000	0.000	0.000	0.000
65	A	62	GLU	-1	-0.919	-0.940	21.133	-0.103	-0.103	0.000	0.000	0.000	0.000
66	A	63	GLN	0	-0.011	0.003	20.004	0.014	0.014	0.000	0.000	0.000	0.000
67	A	64	ILE	0	-0.009	-0.006	20.780	0.010	0.010	0.000	0.000	0.000	0.000
68	A	65	THR	0	-0.102	-0.057	23.459	0.015	0.015	0.000	0.000	0.000	0.000
69	A	66	GLY	0	0.034	0.027	25.607	0.003	0.003	0.000	0.000	0.000	0.000
70	A	67	GLY	0	-0.024	-0.013	26.084	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	68	LYS	1	0.916	0.966	21.518	0.145	0.145	0.000	0.000	0.000	0.000
72	A	69	THR	0	-0.067	-0.040	22.466	0.003	0.003	0.000	0.000	0.000	0.000
73	A	70	VAL	0	-0.022	0.023	22.374	0.005	0.005	0.000	0.000	0.000	0.000
74	A	71	PRO	0	0.009	-0.040	25.056	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	72	ARG	1	0.862	0.939	23.000	-0.052	-0.052	0.000	0.000	0.000	0.000
76	A	73	ILE	0	0.004	-0.002	25.279	0.025	0.025	0.000	0.000	0.000	0.000
77	A	74	PHE	0	0.030	0.020	22.748	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	75	PHE	0	0.027	0.010	27.390	0.011	0.011	0.000	0.000	0.000	0.000
79	A	76	GLY	0	0.042	0.018	28.660	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	77	LYS	1	0.900	0.932	22.722	-0.210	-0.210	0.000	0.000	0.000	0.000
81	A	78	THR	0	0.003	0.006	25.740	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	79	SER	0	0.019	0.017	26.115	0.008	0.008	0.000	0.000	0.000	0.000
83	A	80	ILE	0	-0.011	-0.011	27.943	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	81	GLY	0	0.044	0.046	29.076	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	82	GLY	0	-0.061	-0.064	28.828	0.012	0.012	0.000	0.000	0.000	0.000
86	A	83	TYR	0	-0.002	-0.010	30.412	0.003	0.003	0.000	0.000	0.000	0.000
87	A	84	SER	0	0.018	-0.010	32.890	0.003	0.003	0.000	0.000	0.000	0.000
88	A	85	ASP	-1	-0.764	-0.859	32.939	0.031	0.031	0.000	0.000	0.000	0.000
89	A	86	LEU	0	-0.032	-0.019	32.660	0.003	0.003	0.000	0.000	0.000	0.000
90	A	87	LEU	0	-0.022	-0.012	35.455	0.001	0.001	0.000	0.000	0.000	0.000
91	A	88	GLU	-1	-0.935	-0.951	38.446	0.026	0.026	0.000	0.000	0.000	0.000
92	A	89	ILE	0	-0.015	-0.007	36.087	0.001	0.001	0.000	0.000	0.000	0.000
93	A	90	ASP	-1	-0.885	-0.965	39.107	0.069	0.069	0.000	0.000	0.000	0.000
94	A	91	ASN	0	-0.022	-0.018	40.882	0.002	0.002	0.000	0.000	0.000	0.000
95	A	92	MET	0	-0.112	-0.052	41.893	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	93	ASP	-1	-0.927	-0.948	44.533	0.055	0.055	0.000	0.000	0.000	0.000
97	A	94	ALA	0	0.043	0.027	42.025	0.001	0.001	0.000	0.000	0.000	0.000
98	A	95	LEU	0	-0.031	-0.016	36.106	0.005	0.005	0.000	0.000	0.000	0.000
99	A	96	GLY	0	0.043	0.016	39.369	0.006	0.006	0.000	0.000	0.000	0.000
100	A	97	ASP	-1	-0.831	-0.914	41.238	0.065	0.065	0.000	0.000	0.000	0.000
101	A	98	ILE	0	-0.037	-0.021	36.296	0.004	0.004	0.000	0.000	0.000	0.000
102	A	99	LEU	0	-0.028	-0.032	34.620	0.008	0.008	0.000	0.000	0.000	0.000
103	A	100	SER	0	-0.007	-0.008	37.441	0.008	0.008	0.000	0.000	0.000	0.000
104	A	101	SER	0	-0.038	-0.011	38.976	0.003	0.003	0.000	0.000	0.000	0.000
105	A	102	ILE	0	-0.046	-0.012	32.442	0.003	0.003	0.000	0.000	0.000	0.000
106	A	103	GLY	0	-0.007	0.011	34.248	0.011	0.011	0.000	0.000	0.000	0.000
107	A	104	VAL	0	-0.018	-0.012	32.007	0.010	0.010	0.000	0.000	0.000	0.000
108	A	105	LEU	0	0.030	0.031	34.597	0.008	0.008	0.000	0.000	0.000	0.000
109	A	106	ARG	1	0.809	0.894	35.478	-0.142	-0.142	0.000	0.000	0.000	0.000
110	A	107	THR	0	0.034	0.027	38.912	-0.005	-0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:HIS)