FMO DATABASE

FMODB ID: LZQM9

Calculation Name: 4WZ0-A-Xray372

Preferred Name:

Target Type:

Ligand Name: 3-sulfinoalanine

ligand 3-letter code: CSD

PDB ID: 4WZ0

Chain ID: A

ChEMBL ID:

UniProt ID: Q5X159

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	109
LigandCharge	CSD=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-826040.525847
FMO2-HF: Nuclear repulsion	782614.246112
FMO2-HF: Total energy	-43426.279735
FMO2-MP2: Total energy	-43554.793239

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:9:ILE)

Summations of interaction energy for fragment #1(A:9:ILE)

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.
-10.541	-4.395	3.897	-2.741	-7.302	-0.002

Interaction energy analysis for fragmet #1(A:9:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : -0.029

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	11	HIS	0	0.056	0.007	2.778	-3.257	1.487	1.578	-1.874	-4.448	-0.015
4	A	12	LYS	1	0.923	0.989	3.621	1.777	1.949	0.011	0.025	-0.208	0.000
5	A	13	SER	0	-0.003	-0.025	6.281	0.300	0.300	0.000	0.000	0.000	0.000
6	A	14	LYS	1	0.871	0.929	2.351	-6.421	-5.191	2.308	-0.892	-2.646	0.013
7	A	15	TYR	0	0.089	0.026	6.092	0.156	0.156	0.000	0.000	0.000	0.000
8	A	16	LEU	0	-0.011	-0.003	8.349	0.143	0.143	0.000	0.000	0.000	0.000
9	A	17	ARG	1	0.919	0.962	6.477	-0.769	-0.769	0.000	0.000	0.000	0.000
10	A	18	GLU	-1	-0.948	-0.973	7.898	0.080	0.080	0.000	0.000	0.000	0.000
11	A	19	ALA	0	0.050	0.020	11.754	0.014	0.014	0.000	0.000	0.000	0.000
12	A	20	ALA	0	-0.002	-0.004	13.912	0.021	0.021	0.000	0.000	0.000	0.000
13	A	21	LEU	0	-0.025	0.006	15.000	0.016	0.016	0.000	0.000	0.000	0.000
14	A	22	GLU	-1	-0.811	-0.918	16.000	-0.160	-0.160	0.000	0.000	0.000	0.000
15	A	23	ALA	0	-0.013	0.011	17.816	0.001	0.001	0.000	0.000	0.000	0.000
16	A	24	ASN	0	-0.090	-0.066	19.091	0.008	0.008	0.000	0.000	0.000	0.000
17	A	25	LEU	0	-0.033	0.002	19.097	0.009	0.009	0.000	0.000	0.000	0.000
18	A	26	SER	0	-0.064	-0.036	21.201	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	27	HIS	0	-0.002	0.004	23.752	0.000	0.000	0.000	0.000	0.000	0.000
20	A	28	PRO	0	0.028	0.001	26.680	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	29	GLU	-1	-0.785	-0.907	28.110	-0.053	-0.053	0.000	0.000	0.000	0.000
22	A	30	THR	0	-0.075	-0.027	24.749	-0.004	-0.004	0.000	0.000	0.000	0.000
23	A	31	THR	0	0.008	-0.011	23.051	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	32	PRO	0	0.003	0.010	19.383	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	33	THR	0	0.101	0.054	17.180	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	34	MET	0	-0.034	0.024	10.482	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	35	LEU	0	-0.049	-0.015	15.252	-0.049	-0.049	0.000	0.000	0.000	0.000
28	A	36	THR	0	-0.068	-0.062	17.933	0.014	0.014	0.000	0.000	0.000	0.000
29	A	37	CSD	-1	-0.783	-0.918	17.933	-0.402	-0.402	0.000	0.000	0.000	0.000
30	A	38	PRO	0	-0.018	0.014	16.002	0.034	0.034	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.068	-0.045	18.864	0.013	0.013	0.000	0.000	0.000	0.000
32	A	40	ASP	-1	-0.895	-0.937	21.794	-0.244	-0.244	0.000	0.000	0.000	0.000
33	A	41	SER	0	-0.107	-0.049	22.742	0.026	0.026	0.000	0.000	0.000	0.000
34	A	42	GLY	0	0.022	0.018	23.289	0.024	0.024	0.000	0.000	0.000	0.000
35	A	43	PHE	0	0.022	0.006	21.896	-0.026	-0.026	0.000	0.000	0.000	0.000
36	A	44	LEU	0	-0.033	-0.011	16.125	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	45	LYS	1	0.901	0.945	20.377	0.218	0.218	0.000	0.000	0.000	0.000
38	A	46	ASP	-1	-0.897	-0.966	20.517	-0.323	-0.323	0.000	0.000	0.000	0.000
39	A	47	PRO	0	-0.001	0.021	15.181	-0.024	-0.024	0.000	0.000	0.000	0.000
40	A	48	VAL	0	-0.021	-0.021	14.624	0.003	0.003	0.000	0.000	0.000	0.000
41	A	49	ILE	0	-0.002	-0.013	7.167	0.008	0.008	0.000	0.000	0.000	0.000
42	A	50	THR	0	0.019	0.015	10.205	-0.084	-0.084	0.000	0.000	0.000	0.000
43	A	51	PRO	0	0.008	-0.010	7.091	-0.358	-0.358	0.000	0.000	0.000	0.000
44	A	52	GLU	-1	-0.892	-0.940	5.540	-2.155	-2.155	0.000	0.000	0.000	0.000
45	A	53	GLY	0	-0.015	-0.001	6.130	-0.171	-0.171	0.000	0.000	0.000	0.000
46	A	54	PHE	0	-0.054	-0.016	6.877	0.375	0.375	0.000	0.000	0.000	0.000
47	A	55	VAL	0	0.016	-0.003	10.436	-0.081	-0.081	0.000	0.000	0.000	0.000
48	A	56	TYR	0	-0.011	-0.022	12.838	0.119	0.119	0.000	0.000	0.000	0.000
49	A	57	ASN	0	0.071	0.040	16.542	-0.023	-0.023	0.000	0.000	0.000	0.000
50	A	58	LYS	1	0.951	0.984	19.477	0.314	0.314	0.000	0.000	0.000	0.000
51	A	59	SER	0	-0.034	-0.041	20.340	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	60	SER	0	-0.002	0.002	21.450	0.011	0.011	0.000	0.000	0.000	0.000
53	A	61	ILE	0	0.024	0.015	16.946	0.009	0.009	0.000	0.000	0.000	0.000
54	A	62	LEU	0	-0.029	-0.026	20.294	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	63	LYS	1	1.015	1.018	22.365	0.231	0.231	0.000	0.000	0.000	0.000
56	A	64	TRP	0	-0.030	-0.022	19.932	0.049	0.049	0.000	0.000	0.000	0.000
57	A	65	LEU	0	-0.052	-0.040	18.229	0.007	0.007	0.000	0.000	0.000	0.000
58	A	66	GLU	-1	-0.999	-0.983	22.374	-0.238	-0.238	0.000	0.000	0.000	0.000
59	A	67	THR	0	-0.072	-0.021	25.824	0.021	0.021	0.000	0.000	0.000	0.000
60	A	68	LYS	1	0.912	0.952	22.782	0.299	0.299	0.000	0.000	0.000	0.000
61	A	69	LYS	1	0.947	0.990	20.806	0.353	0.353	0.000	0.000	0.000	0.000
62	A	70	GLU	-1	-0.837	-0.925	17.609	-0.404	-0.404	0.000	0.000	0.000	0.000
63	A	71	ASP	-1	-0.720	-0.836	13.838	-0.764	-0.764	0.000	0.000	0.000	0.000
64	A	72	PRO	0	-0.059	-0.035	16.056	0.041	0.041	0.000	0.000	0.000	0.000
65	A	73	GLN	0	-0.016	-0.016	14.001	0.103	0.103	0.000	0.000	0.000	0.000
66	A	74	SER	0	-0.047	-0.042	11.792	0.083	0.083	0.000	0.000	0.000	0.000
67	A	75	ARG	1	0.818	0.910	14.338	0.382	0.382	0.000	0.000	0.000	0.000
68	A	76	LYS	1	0.941	0.992	9.450	0.948	0.948	0.000	0.000	0.000	0.000
69	A	77	PRO	0	-0.008	-0.012	14.696	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	78	LEU	0	0.028	0.034	13.155	-0.102	-0.102	0.000	0.000	0.000	0.000
71	A	79	THR	0	-0.099	-0.058	15.870	0.122	0.122	0.000	0.000	0.000	0.000
72	A	80	ALA	0	0.093	0.020	16.574	-0.060	-0.060	0.000	0.000	0.000	0.000
73	A	81	LYS	1	0.895	0.951	14.558	0.653	0.653	0.000	0.000	0.000	0.000
74	A	82	ASP	-1	-0.859	-0.925	12.272	-0.907	-0.907	0.000	0.000	0.000	0.000
75	A	83	LEU	0	-0.023	-0.004	12.298	-0.166	-0.166	0.000	0.000	0.000	0.000
76	A	84	GLN	0	0.031	0.019	9.926	-0.088	-0.088	0.000	0.000	0.000	0.000
77	A	85	PRO	0	0.015	0.003	13.524	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	86	PHE	0	-0.022	-0.017	10.118	-0.092	-0.092	0.000	0.000	0.000	0.000
79	A	87	PRO	0	0.060	0.031	14.084	0.039	0.039	0.000	0.000	0.000	0.000
80	A	88	GLU	-1	-0.837	-0.942	13.620	-0.400	-0.400	0.000	0.000	0.000	0.000
81	A	89	LEU	0	0.010	0.013	13.066	0.054	0.054	0.000	0.000	0.000	0.000
82	A	90	LEU	0	0.012	-0.004	15.260	0.039	0.039	0.000	0.000	0.000	0.000
83	A	91	ILE	0	-0.056	-0.009	18.120	0.036	0.036	0.000	0.000	0.000	0.000
84	A	92	ILE	0	0.007	-0.003	14.596	0.028	0.028	0.000	0.000	0.000	0.000
85	A	93	VAL	0	0.000	0.007	17.972	0.021	0.021	0.000	0.000	0.000	0.000
86	A	94	ASN	0	-0.005	-0.017	20.383	0.015	0.015	0.000	0.000	0.000	0.000
87	A	95	ARG	1	0.867	0.947	22.297	0.106	0.106	0.000	0.000	0.000	0.000
88	A	96	PHE	0	0.040	0.047	22.012	0.010	0.010	0.000	0.000	0.000	0.000
89	A	97	VAL	0	0.046	0.028	24.020	0.011	0.011	0.000	0.000	0.000	0.000
90	A	98	GLU	-1	-0.882	-0.949	26.307	-0.074	-0.074	0.000	0.000	0.000	0.000
91	A	99	THR	0	-0.058	-0.046	26.581	0.013	0.013	0.000	0.000	0.000	0.000
92	A	100	GLN	0	-0.033	-0.008	27.481	0.003	0.003	0.000	0.000	0.000	0.000
93	A	101	THR	0	0.022	0.013	29.388	0.005	0.005	0.000	0.000	0.000	0.000
94	A	102	ASN	0	-0.045	-0.032	31.962	0.006	0.006	0.000	0.000	0.000	0.000
95	A	103	TYR	0	0.001	-0.003	31.806	0.007	0.007	0.000	0.000	0.000	0.000
96	A	104	GLU	-1	-0.870	-0.929	32.412	-0.066	-0.066	0.000	0.000	0.000	0.000
97	A	105	LYS	1	0.917	0.966	35.264	0.039	0.039	0.000	0.000	0.000	0.000
98	A	106	LEU	0	-0.074	-0.043	35.985	0.004	0.004	0.000	0.000	0.000	0.000
99	A	107	LYS	1	0.895	0.942	35.346	0.043	0.043	0.000	0.000	0.000	0.000
100	A	108	ASN	0	0.020	0.004	38.533	0.004	0.004	0.000	0.000	0.000	0.000
101	A	109	ARG	1	0.923	0.968	40.437	0.024	0.024	0.000	0.000	0.000	0.000
102	A	110	LEU	0	-0.018	-0.012	39.766	0.002	0.002	0.000	0.000	0.000	0.000
103	A	111	VAL	0	0.014	0.010	41.422	0.002	0.002	0.000	0.000	0.000	0.000
104	A	112	GLN	0	-0.015	-0.029	44.175	0.003	0.003	0.000	0.000	0.000	0.000
105	A	113	ASN	0	0.011	-0.002	46.490	0.000	0.000	0.000	0.000	0.000	0.000
106	A	114	ALA	0	-0.002	0.004	47.023	0.002	0.002	0.000	0.000	0.000	0.000
107	A	115	ARG	1	0.867	0.953	45.178	0.030	0.030	0.000	0.000	0.000	0.000
108	A	116	VAL	0	-0.002	0.003	50.460	0.000	0.000	0.000	0.000	0.000	0.000
109	A	117	ALA	0	-0.029	0.013	51.809	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ILE)