FMO DATABASE

FMODB ID: R9MM8

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

Total energy (hartree)

FMO2-HF: Electronic energy	-901333.337937
FMO2-HF: Nuclear repulsion	857045.453791
FMO2-HF: Total energy	-44287.884145
FMO2-MP2: Total energy	-44417.017927

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.
0.782	2.483	-0.021	-0.785	-0.895	-0.002

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 : -0.027 / q_NPA : -0.028

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	0.015	0.023	3.853	0.275	1.976	-0.021	-0.785	-0.895	-0.002
4	A	1	MET	0	0.041	0.011	6.172	-0.893	-0.893	0.000	0.000	0.000	0.000
5	A	2	ALA	0	0.012	-0.002	9.487	0.064	0.064	0.000	0.000	0.000	0.000
6	A	3	GLU	-1	-0.853	-0.896	12.945	0.421	0.421	0.000	0.000	0.000	0.000
7	A	4	GLU	-1	-0.845	-0.920	8.905	2.096	2.096	0.000	0.000	0.000	0.000
8	A	5	PHE	0	-0.036	-0.009	12.078	-0.034	-0.034	0.000	0.000	0.000	0.000
9	A	6	VAL	0	-0.004	-0.002	13.655	-0.049	-0.049	0.000	0.000	0.000	0.000
10	A	7	GLN	0	0.062	0.016	16.708	-0.012	-0.012	0.000	0.000	0.000	0.000
11	A	8	GLN	0	-0.065	-0.043	12.277	0.007	0.007	0.000	0.000	0.000	0.000
12	A	9	ARG	1	0.747	0.852	15.986	-0.647	-0.647	0.000	0.000	0.000	0.000
13	A	10	LEU	0	-0.052	0.012	20.149	-0.060	-0.060	0.000	0.000	0.000	0.000
14	A	11	ALA	0	0.034	-0.001	22.703	0.028	0.028	0.000	0.000	0.000	0.000
15	A	12	ASN	0	0.005	-0.011	25.460	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	13	ASN	0	-0.046	-0.021	28.900	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	14	LYS	1	0.801	0.884	23.096	-0.419	-0.419	0.000	0.000	0.000	0.000
18	A	15	VAL	0	0.017	0.024	29.078	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	16	THR	0	-0.010	-0.030	22.411	0.012	0.012	0.000	0.000	0.000	0.000
20	A	17	ILE	0	-0.014	0.008	25.486	-0.019	-0.019	0.000	0.000	0.000	0.000
21	A	18	PHE	0	0.039	0.030	18.317	0.009	0.009	0.000	0.000	0.000	0.000
22	A	19	VAL	0	0.012	-0.030	22.525	-0.039	-0.039	0.000	0.000	0.000	0.000
23	A	20	LYS	1	0.838	0.891	20.241	-0.074	-0.074	0.000	0.000	0.000	0.000
24	A	21	TYR	0	0.064	0.024	23.668	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	22	THR	0	0.007	0.002	25.770	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	23	CYS	0	-0.018	0.017	27.372	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	24	PRO	0	0.026	0.000	29.126	0.010	0.010	0.000	0.000	0.000	0.000
28	A	25	PHE	0	0.084	0.032	31.110	0.006	0.006	0.000	0.000	0.000	0.000
29	A	26	CYS	0	-0.031	0.010	27.074	0.010	0.010	0.000	0.000	0.000	0.000
30	A	27	ARG	1	0.910	0.960	29.576	-0.101	-0.101	0.000	0.000	0.000	0.000
31	A	28	ASN	0	0.044	0.017	32.168	0.006	0.006	0.000	0.000	0.000	0.000
32	A	29	ALA	0	0.011	0.003	31.073	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	30	LEU	0	-0.035	-0.020	28.122	0.007	0.007	0.000	0.000	0.000	0.000
34	A	31	ASP	-1	-0.893	-0.954	32.118	0.135	0.135	0.000	0.000	0.000	0.000
35	A	32	ILE	0	-0.027	-0.005	35.829	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	33	LEU	0	0.000	-0.011	30.968	0.002	0.002	0.000	0.000	0.000	0.000
37	A	34	ASN	0	-0.051	-0.029	34.748	0.011	0.011	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.778	0.890	35.907	-0.115	-0.115	0.000	0.000	0.000	0.000
39	A	36	PHE	0	0.009	0.012	36.720	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	37	SER	0	-0.011	0.003	36.505	0.007	0.007	0.000	0.000	0.000	0.000
41	A	38	PHE	0	0.085	0.041	33.052	0.000	0.000	0.000	0.000	0.000	0.000
42	A	39	LYS	1	0.850	0.922	33.822	-0.192	-0.192	0.000	0.000	0.000	0.000
43	A	40	ARG	1	0.963	0.967	29.442	-0.293	-0.293	0.000	0.000	0.000	0.000
44	A	41	GLY	0	0.016	0.010	27.758	0.007	0.007	0.000	0.000	0.000	0.000
45	A	42	ALA	0	-0.001	0.007	27.728	0.016	0.016	0.000	0.000	0.000	0.000
46	A	43	TYR	0	0.022	0.007	28.808	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	44	GLU	-1	-0.805	-0.874	20.707	0.515	0.515	0.000	0.000	0.000	0.000
48	A	45	ILE	0	0.010	0.010	24.805	-0.018	-0.018	0.000	0.000	0.000	0.000
49	A	46	VAL	0	-0.004	0.007	18.520	0.018	0.018	0.000	0.000	0.000	0.000
50	A	47	ASP	-1	-0.792	-0.880	19.865	0.219	0.219	0.000	0.000	0.000	0.000
51	A	48	ILE	0	0.033	0.000	17.603	0.034	0.034	0.000	0.000	0.000	0.000
52	A	49	LYS	1	0.787	0.871	16.445	-0.255	-0.255	0.000	0.000	0.000	0.000
53	A	50	GLU	-1	-0.849	-0.894	14.174	0.597	0.597	0.000	0.000	0.000	0.000
54	A	51	PHE	0	-0.035	-0.002	10.128	0.066	0.066	0.000	0.000	0.000	0.000
55	A	52	LYS	1	0.880	0.946	10.078	-0.197	-0.197	0.000	0.000	0.000	0.000
56	A	53	PRO	0	0.102	0.065	8.862	0.004	0.004	0.000	0.000	0.000	0.000
57	A	54	GLU	-1	-0.781	-0.899	11.799	0.118	0.118	0.000	0.000	0.000	0.000
58	A	55	ASN	0	-0.057	-0.033	14.434	0.012	0.012	0.000	0.000	0.000	0.000
59	A	56	GLU	-1	-0.740	-0.864	10.016	-0.272	-0.272	0.000	0.000	0.000	0.000
60	A	57	LEU	0	-0.009	0.005	14.369	0.056	0.056	0.000	0.000	0.000	0.000
61	A	58	ARG	1	0.895	0.955	16.180	0.016	0.016	0.000	0.000	0.000	0.000
62	A	59	ASP	-1	-0.813	-0.911	17.203	-0.086	-0.086	0.000	0.000	0.000	0.000
63	A	60	TYR	0	-0.023	-0.049	16.276	0.014	0.014	0.000	0.000	0.000	0.000
64	A	61	PHE	0	0.016	-0.011	18.388	0.012	0.012	0.000	0.000	0.000	0.000
65	A	62	GLU	-1	-0.860	-0.906	21.452	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	63	GLN	0	-0.037	-0.020	20.109	0.005	0.005	0.000	0.000	0.000	0.000
67	A	64	ILE	0	-0.010	0.009	20.467	0.006	0.006	0.000	0.000	0.000	0.000
68	A	65	THR	0	-0.089	-0.059	23.415	0.009	0.009	0.000	0.000	0.000	0.000
69	A	66	GLY	0	0.039	0.029	25.932	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	67	GLY	0	-0.015	-0.015	26.127	-0.016	-0.016	0.000	0.000	0.000	0.000
71	A	68	LYS	1	0.778	0.879	21.173	0.049	0.049	0.000	0.000	0.000	0.000
72	A	69	THR	0	-0.056	-0.024	22.776	0.001	0.001	0.000	0.000	0.000	0.000
73	A	70	VAL	0	-0.007	0.019	22.388	0.007	0.007	0.000	0.000	0.000	0.000
74	A	71	PRO	0	-0.015	-0.032	25.258	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	72	ARG	1	0.848	0.930	23.096	-0.144	-0.144	0.000	0.000	0.000	0.000
76	A	73	ILE	0	-0.005	0.003	25.202	0.029	0.029	0.000	0.000	0.000	0.000
77	A	74	PHE	0	0.041	0.018	22.675	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	75	PHE	0	0.024	0.009	27.440	0.006	0.006	0.000	0.000	0.000	0.000
79	A	76	GLY	0	0.038	0.019	28.719	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	77	LYS	1	0.822	0.897	21.073	-0.439	-0.439	0.000	0.000	0.000	0.000
81	A	78	THR	0	-0.010	0.009	25.572	0.006	0.006	0.000	0.000	0.000	0.000
82	A	79	SER	0	0.031	0.014	25.945	0.003	0.003	0.000	0.000	0.000	0.000
83	A	80	ILE	0	-0.035	-0.025	27.692	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	81	GLY	0	0.053	0.042	29.144	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	82	GLY	0	-0.052	-0.052	28.473	0.015	0.015	0.000	0.000	0.000	0.000
86	A	83	TYR	0	0.007	-0.006	30.375	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	84	SER	0	0.016	0.006	33.135	0.001	0.001	0.000	0.000	0.000	0.000
88	A	85	ASP	-1	-0.770	-0.870	32.868	0.096	0.096	0.000	0.000	0.000	0.000
89	A	86	LEU	0	-0.015	-0.007	32.985	0.002	0.002	0.000	0.000	0.000	0.000
90	A	87	LEU	0	-0.015	-0.012	35.499	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	88	GLU	-1	-0.948	-0.961	38.461	0.069	0.069	0.000	0.000	0.000	0.000
92	A	89	ILE	0	-0.001	-0.015	35.972	0.000	0.000	0.000	0.000	0.000	0.000
93	A	90	ASP	-1	-0.828	-0.905	39.113	0.110	0.110	0.000	0.000	0.000	0.000
94	A	91	ASN	0	-0.057	-0.038	40.974	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	92	MET	0	-0.062	-0.007	41.909	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	93	ASP	-1	-0.909	-0.952	44.261	0.095	0.095	0.000	0.000	0.000	0.000
97	A	94	ALA	0	0.015	0.006	42.343	0.005	0.005	0.000	0.000	0.000	0.000
98	A	95	LEU	0	-0.013	-0.003	36.189	0.008	0.008	0.000	0.000	0.000	0.000
99	A	96	GLY	0	0.038	0.020	39.505	0.009	0.009	0.000	0.000	0.000	0.000
100	A	97	ASP	-1	-0.852	-0.912	41.477	0.113	0.113	0.000	0.000	0.000	0.000
101	A	98	ILE	0	-0.031	-0.001	36.424	0.008	0.008	0.000	0.000	0.000	0.000
102	A	99	LEU	0	-0.013	-0.018	34.729	0.013	0.013	0.000	0.000	0.000	0.000
103	A	100	SER	0	-0.029	-0.034	37.423	0.011	0.011	0.000	0.000	0.000	0.000
104	A	101	SER	0	-0.052	-0.033	38.913	0.004	0.004	0.000	0.000	0.000	0.000
105	A	102	ILE	0	-0.055	-0.017	32.566	0.006	0.006	0.000	0.000	0.000	0.000
106	A	103	GLY	0	0.018	0.021	34.428	0.016	0.016	0.000	0.000	0.000	0.000
107	A	104	VAL	0	-0.016	-0.005	32.072	0.010	0.010	0.000	0.000	0.000	0.000
108	A	105	LEU	0	0.037	0.032	34.710	0.008	0.008	0.000	0.000	0.000	0.000
109	A	106	ARG	1	0.833	0.909	35.456	-0.188	-0.188	0.000	0.000	0.000	0.000
110	A	107	THR	0	-0.002	0.002	39.039	-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:-2:HIS)