FMO DATABASE

FMODB ID: Z6LLN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-899437.724579
FMO2-HF: Nuclear repulsion	855150.05433
FMO2-HF: Total energy	-44287.670248
FMO2-MP2: Total energy	-44416.797187

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.
-0.359	1.829	-0.031	-1.109	-1.048	-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 : -0.030 / 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	0.032	0.033	3.807	-0.242	1.946	-0.031	-1.109	-1.048	-0.003
4	A	1	MET	0	0.056	0.026	6.074	-0.838	-0.838	0.000	0.000	0.000	0.000
5	A	2	ALA	0	0.022	0.004	9.391	0.110	0.110	0.000	0.000	0.000	0.000
6	A	3	GLU	-1	-0.860	-0.915	12.775	0.283	0.283	0.000	0.000	0.000	0.000
7	A	4	GLU	-1	-0.834	-0.916	9.068	1.698	1.698	0.000	0.000	0.000	0.000
8	A	5	PHE	0	-0.051	-0.014	12.130	-0.006	-0.006	0.000	0.000	0.000	0.000
9	A	6	VAL	0	-0.024	-0.020	13.759	-0.032	-0.032	0.000	0.000	0.000	0.000
10	A	7	GLN	0	0.068	0.031	16.772	0.004	0.004	0.000	0.000	0.000	0.000
11	A	8	GLN	0	-0.078	-0.049	12.163	0.037	0.037	0.000	0.000	0.000	0.000
12	A	9	ARG	1	0.820	0.905	15.110	-0.632	-0.632	0.000	0.000	0.000	0.000
13	A	10	LEU	0	-0.051	0.003	19.900	-0.050	-0.050	0.000	0.000	0.000	0.000
14	A	11	ALA	0	-0.004	-0.017	22.661	0.026	0.026	0.000	0.000	0.000	0.000
15	A	12	ASN	0	0.010	-0.002	25.448	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	13	ASN	0	-0.044	-0.025	28.828	-0.009	-0.009	0.000	0.000	0.000	0.000
17	A	14	LYS	1	0.805	0.881	22.898	-0.384	-0.384	0.000	0.000	0.000	0.000
18	A	15	VAL	0	0.000	0.014	28.881	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	16	THR	0	0.003	-0.008	22.276	0.012	0.012	0.000	0.000	0.000	0.000
20	A	17	ILE	0	-0.017	0.006	25.338	-0.022	-0.022	0.000	0.000	0.000	0.000
21	A	18	PHE	0	0.017	0.022	18.414	0.019	0.019	0.000	0.000	0.000	0.000
22	A	19	VAL	0	0.030	-0.019	22.509	-0.039	-0.039	0.000	0.000	0.000	0.000
23	A	20	LYS	1	0.857	0.917	20.231	-0.053	-0.053	0.000	0.000	0.000	0.000
24	A	21	TYR	0	0.052	0.006	23.317	-0.026	-0.026	0.000	0.000	0.000	0.000
25	A	22	THR	0	-0.007	-0.004	25.614	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	23	CYS	0	-0.023	0.019	27.038	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	24	PRO	0	0.030	-0.004	28.837	0.011	0.011	0.000	0.000	0.000	0.000
28	A	25	PHE	0	0.088	0.038	31.053	0.004	0.004	0.000	0.000	0.000	0.000
29	A	26	CYS	0	-0.011	-0.003	27.025	0.007	0.007	0.000	0.000	0.000	0.000
30	A	27	ARG	1	0.918	0.965	29.581	-0.104	-0.104	0.000	0.000	0.000	0.000
31	A	28	ASN	0	0.044	0.028	31.911	0.005	0.005	0.000	0.000	0.000	0.000
32	A	29	ALA	0	0.020	0.008	30.894	0.000	0.000	0.000	0.000	0.000	0.000
33	A	30	LEU	0	-0.039	-0.028	27.940	0.005	0.005	0.000	0.000	0.000	0.000
34	A	31	ASP	-1	-0.909	-0.945	32.028	0.127	0.127	0.000	0.000	0.000	0.000
35	A	32	ILE	0	-0.036	-0.011	35.513	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	33	LEU	0	0.003	-0.008	30.724	0.001	0.001	0.000	0.000	0.000	0.000
37	A	34	ASN	0	-0.043	-0.028	34.243	0.012	0.012	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.791	0.897	35.543	-0.102	-0.102	0.000	0.000	0.000	0.000
39	A	36	PHE	0	-0.015	0.000	36.682	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	37	SER	0	-0.005	0.011	36.747	0.006	0.006	0.000	0.000	0.000	0.000
41	A	38	PHE	0	0.070	0.024	32.901	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	39	LYS	1	0.828	0.908	33.764	-0.166	-0.166	0.000	0.000	0.000	0.000
43	A	40	ARG	1	0.988	0.979	29.499	-0.276	-0.276	0.000	0.000	0.000	0.000
44	A	41	GLY	0	-0.003	-0.004	27.609	0.002	0.002	0.000	0.000	0.000	0.000
45	A	42	ALA	0	0.005	0.015	27.535	0.014	0.014	0.000	0.000	0.000	0.000
46	A	43	TYR	0	0.031	0.016	28.667	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	44	GLU	-1	-0.827	-0.892	20.536	0.485	0.485	0.000	0.000	0.000	0.000
48	A	45	ILE	0	0.001	0.003	24.624	-0.016	-0.016	0.000	0.000	0.000	0.000
49	A	46	VAL	0	0.005	0.007	18.532	0.024	0.024	0.000	0.000	0.000	0.000
50	A	47	ASP	-1	-0.785	-0.884	19.495	0.239	0.239	0.000	0.000	0.000	0.000
51	A	48	ILE	0	0.042	0.004	17.337	0.040	0.040	0.000	0.000	0.000	0.000
52	A	49	LYS	1	0.775	0.871	16.291	-0.283	-0.283	0.000	0.000	0.000	0.000
53	A	50	GLU	-1	-0.885	-0.919	13.762	0.612	0.612	0.000	0.000	0.000	0.000
54	A	51	PHE	0	-0.055	-0.014	10.227	0.079	0.079	0.000	0.000	0.000	0.000
55	A	52	LYS	1	0.895	0.968	9.990	-0.233	-0.233	0.000	0.000	0.000	0.000
56	A	53	PRO	0	0.097	0.052	8.689	0.002	0.002	0.000	0.000	0.000	0.000
57	A	54	GLU	-1	-0.762	-0.898	11.589	0.073	0.073	0.000	0.000	0.000	0.000
58	A	55	ASN	0	-0.042	-0.037	13.943	0.036	0.036	0.000	0.000	0.000	0.000
59	A	56	GLU	-1	-0.746	-0.860	9.820	-0.643	-0.643	0.000	0.000	0.000	0.000
60	A	57	LEU	0	-0.022	-0.004	14.035	0.053	0.053	0.000	0.000	0.000	0.000
61	A	58	ARG	1	0.879	0.944	15.855	0.070	0.070	0.000	0.000	0.000	0.000
62	A	59	ASP	-1	-0.830	-0.909	16.930	-0.176	-0.176	0.000	0.000	0.000	0.000
63	A	60	TYR	0	-0.029	-0.039	16.023	0.023	0.023	0.000	0.000	0.000	0.000
64	A	61	PHE	0	0.003	-0.017	18.138	0.019	0.019	0.000	0.000	0.000	0.000
65	A	62	GLU	-1	-0.865	-0.909	21.100	-0.081	-0.081	0.000	0.000	0.000	0.000
66	A	63	GLN	0	-0.023	-0.004	20.049	0.003	0.003	0.000	0.000	0.000	0.000
67	A	64	ILE	0	-0.001	0.004	20.688	0.007	0.007	0.000	0.000	0.000	0.000
68	A	65	THR	0	-0.099	-0.062	23.424	0.012	0.012	0.000	0.000	0.000	0.000
69	A	66	GLY	0	0.030	0.026	25.573	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	67	GLY	0	-0.023	-0.010	26.076	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	68	LYS	1	0.797	0.887	21.061	0.122	0.122	0.000	0.000	0.000	0.000
72	A	69	THR	0	-0.051	-0.028	22.589	0.005	0.005	0.000	0.000	0.000	0.000
73	A	70	VAL	0	-0.028	0.016	22.268	0.007	0.007	0.000	0.000	0.000	0.000
74	A	71	PRO	0	0.000	-0.036	25.056	-0.014	-0.014	0.000	0.000	0.000	0.000
75	A	72	ARG	1	0.855	0.936	22.780	-0.103	-0.103	0.000	0.000	0.000	0.000
76	A	73	ILE	0	0.012	0.005	25.279	0.029	0.029	0.000	0.000	0.000	0.000
77	A	74	PHE	0	0.023	0.012	22.717	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	75	PHE	0	0.032	0.013	27.390	0.010	0.010	0.000	0.000	0.000	0.000
79	A	76	GLY	0	0.047	0.021	28.661	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	77	LYS	1	0.836	0.901	21.312	-0.345	-0.345	0.000	0.000	0.000	0.000
81	A	78	THR	0	0.006	0.008	25.702	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	79	SER	0	0.013	0.012	26.041	0.006	0.006	0.000	0.000	0.000	0.000
83	A	80	ILE	0	-0.011	-0.013	27.907	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	81	GLY	0	0.048	0.048	29.071	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	82	GLY	0	-0.058	-0.067	28.828	0.015	0.015	0.000	0.000	0.000	0.000
86	A	83	TYR	0	-0.001	-0.008	30.412	0.000	0.000	0.000	0.000	0.000	0.000
87	A	84	SER	0	0.009	-0.008	32.890	0.003	0.003	0.000	0.000	0.000	0.000
88	A	85	ASP	-1	-0.773	-0.865	33.026	0.063	0.063	0.000	0.000	0.000	0.000
89	A	86	LEU	0	-0.018	-0.010	32.856	0.003	0.003	0.000	0.000	0.000	0.000
90	A	87	LEU	0	-0.023	-0.014	35.455	0.000	0.000	0.000	0.000	0.000	0.000
91	A	88	GLU	-1	-0.944	-0.955	38.446	0.048	0.048	0.000	0.000	0.000	0.000
92	A	89	ILE	0	0.002	-0.002	36.056	0.000	0.000	0.000	0.000	0.000	0.000
93	A	90	ASP	-1	-0.834	-0.922	39.037	0.096	0.096	0.000	0.000	0.000	0.000
94	A	91	ASN	0	-0.021	-0.017	40.882	0.000	0.000	0.000	0.000	0.000	0.000
95	A	92	MET	0	-0.111	-0.050	41.983	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	93	ASP	-1	-0.937	-0.953	44.456	0.079	0.079	0.000	0.000	0.000	0.000
97	A	94	ALA	0	0.042	0.028	41.993	0.001	0.001	0.000	0.000	0.000	0.000
98	A	95	LEU	0	-0.027	-0.011	36.030	0.007	0.007	0.000	0.000	0.000	0.000
99	A	96	GLY	0	0.053	0.018	39.369	0.008	0.008	0.000	0.000	0.000	0.000
100	A	97	ASP	-1	-0.817	-0.896	41.239	0.093	0.093	0.000	0.000	0.000	0.000
101	A	98	ILE	0	-0.039	-0.013	36.322	0.006	0.006	0.000	0.000	0.000	0.000
102	A	99	LEU	0	-0.019	-0.025	34.623	0.011	0.011	0.000	0.000	0.000	0.000
103	A	100	SER	0	-0.026	-0.032	37.440	0.009	0.009	0.000	0.000	0.000	0.000
104	A	101	SER	0	-0.051	-0.024	38.654	0.003	0.003	0.000	0.000	0.000	0.000
105	A	102	ILE	0	-0.034	-0.006	32.431	0.005	0.005	0.000	0.000	0.000	0.000
106	A	103	GLY	0	0.000	0.017	34.248	0.015	0.015	0.000	0.000	0.000	0.000
107	A	104	VAL	0	-0.010	-0.008	32.099	0.011	0.011	0.000	0.000	0.000	0.000
108	A	105	LEU	0	0.044	0.042	34.594	0.008	0.008	0.000	0.000	0.000	0.000
109	A	106	ARG	1	0.800	0.892	35.253	-0.180	-0.180	0.000	0.000	0.000	0.000
110	A	107	THR	0	0.054	0.034	38.911	-0.006	-0.006	0.000	0.000	0.000	0.000

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