FMO DATABASE

FMODB ID: 94LN2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-826812.485262
FMO2-HF: Nuclear repulsion	783385.651701
FMO2-HF: Total energy	-43426.833561
FMO2-MP2: Total energy	-43555.374013

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.
-10.87	-4.929	5.556	-3.581	-7.914	0.011

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 : 0.025 / q_NPA : 0.004

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	0.046	0.001	2.954	-3.794	1.533	1.467	-2.313	-4.481	-0.009
4	A	12	LYS	1	0.834	0.924	3.549	2.390	2.547	0.016	0.038	-0.210	0.000
5	A	13	SER	0	-0.014	-0.044	6.443	0.576	0.576	0.000	0.000	0.000	0.000
6	A	14	LYS	1	0.877	0.940	2.093	-8.086	-7.629	4.073	-1.306	-3.223	0.020
7	A	15	TYR	0	0.066	0.014	6.204	0.207	0.207	0.000	0.000	0.000	0.000
8	A	16	LEU	0	-0.014	-0.004	8.353	0.153	0.153	0.000	0.000	0.000	0.000
9	A	17	ARG	1	0.799	0.890	7.193	-0.759	-0.759	0.000	0.000	0.000	0.000
10	A	18	GLU	-1	-0.837	-0.912	7.968	0.772	0.772	0.000	0.000	0.000	0.000
11	A	19	ALA	0	0.047	0.021	11.822	0.017	0.017	0.000	0.000	0.000	0.000
12	A	20	ALA	0	0.001	0.000	13.977	0.014	0.014	0.000	0.000	0.000	0.000
13	A	21	LEU	0	-0.018	0.005	15.033	0.013	0.013	0.000	0.000	0.000	0.000
14	A	22	GLU	-1	-0.784	-0.887	16.059	-0.041	-0.041	0.000	0.000	0.000	0.000
15	A	23	ALA	0	-0.007	0.000	17.857	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	24	ASN	0	-0.098	-0.067	19.357	0.002	0.002	0.000	0.000	0.000	0.000
17	A	25	LEU	0	-0.016	0.009	19.056	0.009	0.009	0.000	0.000	0.000	0.000
18	A	26	SER	0	-0.056	-0.019	21.284	0.004	0.004	0.000	0.000	0.000	0.000
19	A	27	HIS	0	-0.012	-0.001	23.783	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	28	PRO	0	0.043	0.007	26.694	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	29	GLU	-1	-0.742	-0.862	28.133	-0.034	-0.034	0.000	0.000	0.000	0.000
22	A	30	THR	0	-0.068	-0.022	24.443	0.000	0.000	0.000	0.000	0.000	0.000
23	A	31	THR	0	0.005	-0.011	23.087	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	32	PRO	0	-0.014	0.003	19.355	0.004	0.004	0.000	0.000	0.000	0.000
25	A	33	THR	0	0.077	0.031	17.287	-0.025	-0.025	0.000	0.000	0.000	0.000
26	A	34	MET	0	-0.051	-0.001	10.498	-0.014	-0.014	0.000	0.000	0.000	0.000
27	A	35	LEU	0	-0.039	-0.011	15.194	-0.075	-0.075	0.000	0.000	0.000	0.000
28	A	36	THR	0	-0.058	-0.048	17.873	0.000	0.000	0.000	0.000	0.000	0.000
29	A	37	CSD	-1	-0.804	-0.917	17.809	-0.345	-0.345	0.000	0.000	0.000	0.000
30	A	38	PRO	0	0.002	0.029	15.641	0.033	0.033	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.049	-0.030	18.780	0.028	0.028	0.000	0.000	0.000	0.000
32	A	40	ASP	-1	-0.903	-0.937	21.693	-0.196	-0.196	0.000	0.000	0.000	0.000
33	A	41	SER	0	-0.095	-0.045	22.581	0.021	0.021	0.000	0.000	0.000	0.000
34	A	42	GLY	0	0.028	0.023	23.143	0.017	0.017	0.000	0.000	0.000	0.000
35	A	43	PHE	0	0.023	0.005	21.770	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	44	LEU	0	-0.039	-0.010	16.010	-0.013	-0.013	0.000	0.000	0.000	0.000
37	A	45	LYS	1	0.914	0.949	20.273	0.211	0.211	0.000	0.000	0.000	0.000
38	A	46	ASP	-1	-0.894	-0.964	20.398	-0.429	-0.429	0.000	0.000	0.000	0.000
39	A	47	PRO	0	0.004	0.014	15.058	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	48	VAL	0	-0.021	-0.016	14.475	-0.035	-0.035	0.000	0.000	0.000	0.000
41	A	49	ILE	0	-0.005	-0.010	7.125	0.042	0.042	0.000	0.000	0.000	0.000
42	A	50	THR	0	0.015	0.015	10.287	-0.125	-0.125	0.000	0.000	0.000	0.000
43	A	51	PRO	0	0.021	-0.003	7.119	-0.353	-0.353	0.000	0.000	0.000	0.000
44	A	52	GLU	-1	-0.813	-0.877	5.559	-1.240	-1.240	0.000	0.000	0.000	0.000
45	A	53	GLY	0	-0.013	0.002	5.913	0.075	0.075	0.000	0.000	0.000	0.000
46	A	54	PHE	0	-0.055	-0.017	6.661	0.333	0.333	0.000	0.000	0.000	0.000
47	A	55	VAL	0	0.009	-0.006	10.297	-0.160	-0.160	0.000	0.000	0.000	0.000
48	A	56	TYR	0	-0.005	-0.026	12.670	0.123	0.123	0.000	0.000	0.000	0.000
49	A	57	ASN	0	0.067	0.020	16.364	-0.061	-0.061	0.000	0.000	0.000	0.000
50	A	58	LYS	1	0.922	0.972	19.296	0.392	0.392	0.000	0.000	0.000	0.000
51	A	59	SER	0	-0.019	-0.027	20.164	0.001	0.001	0.000	0.000	0.000	0.000
52	A	60	SER	0	-0.013	-0.017	21.291	0.010	0.010	0.000	0.000	0.000	0.000
53	A	61	ILE	0	0.019	0.009	16.833	0.018	0.018	0.000	0.000	0.000	0.000
54	A	62	LEU	0	-0.038	-0.028	20.148	0.003	0.003	0.000	0.000	0.000	0.000
55	A	63	LYS	1	1.009	1.018	22.427	0.199	0.199	0.000	0.000	0.000	0.000
56	A	64	TRP	0	-0.001	0.000	20.154	0.048	0.048	0.000	0.000	0.000	0.000
57	A	65	LEU	0	-0.050	-0.038	18.178	0.012	0.012	0.000	0.000	0.000	0.000
58	A	66	GLU	-1	-0.979	-0.974	22.411	-0.220	-0.220	0.000	0.000	0.000	0.000
59	A	67	THR	0	-0.084	-0.032	25.861	0.021	0.021	0.000	0.000	0.000	0.000
60	A	68	LYS	1	0.887	0.947	22.785	0.201	0.201	0.000	0.000	0.000	0.000
61	A	69	LYS	1	0.949	0.987	20.840	0.275	0.275	0.000	0.000	0.000	0.000
62	A	70	GLU	-1	-0.830	-0.912	17.582	-0.198	-0.198	0.000	0.000	0.000	0.000
63	A	71	ASP	-1	-0.728	-0.849	14.007	-0.482	-0.482	0.000	0.000	0.000	0.000
64	A	72	PRO	0	-0.040	-0.023	16.121	0.053	0.053	0.000	0.000	0.000	0.000
65	A	73	GLN	0	-0.021	-0.019	13.690	0.101	0.101	0.000	0.000	0.000	0.000
66	A	74	SER	0	-0.068	-0.064	12.059	0.070	0.070	0.000	0.000	0.000	0.000
67	A	75	ARG	1	0.824	0.902	14.423	0.187	0.187	0.000	0.000	0.000	0.000
68	A	76	LYS	1	0.872	0.943	9.287	0.221	0.221	0.000	0.000	0.000	0.000
69	A	77	PRO	0	-0.015	-0.017	14.572	-0.039	-0.039	0.000	0.000	0.000	0.000
70	A	78	LEU	0	0.002	0.018	13.103	-0.091	-0.091	0.000	0.000	0.000	0.000
71	A	79	THR	0	-0.084	-0.077	15.897	0.089	0.089	0.000	0.000	0.000	0.000
72	A	80	ALA	0	0.093	0.019	16.600	-0.065	-0.065	0.000	0.000	0.000	0.000
73	A	81	LYS	1	0.838	0.916	14.834	0.668	0.668	0.000	0.000	0.000	0.000
74	A	82	ASP	-1	-0.820	-0.874	12.266	-0.867	-0.867	0.000	0.000	0.000	0.000
75	A	83	LEU	0	-0.012	0.010	12.329	-0.172	-0.172	0.000	0.000	0.000	0.000
76	A	84	GLN	0	0.034	0.023	10.414	-0.081	-0.081	0.000	0.000	0.000	0.000
77	A	85	PRO	0	0.021	0.006	13.385	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	86	PHE	0	-0.005	-0.006	10.046	-0.171	-0.171	0.000	0.000	0.000	0.000
79	A	87	PRO	0	0.058	0.027	14.004	0.071	0.071	0.000	0.000	0.000	0.000
80	A	88	GLU	-1	-0.777	-0.893	13.619	-0.831	-0.831	0.000	0.000	0.000	0.000
81	A	89	LEU	0	0.018	0.016	13.059	0.071	0.071	0.000	0.000	0.000	0.000
82	A	90	LEU	0	0.018	0.000	15.245	0.065	0.065	0.000	0.000	0.000	0.000
83	A	91	ILE	0	-0.052	-0.006	17.918	0.051	0.051	0.000	0.000	0.000	0.000
84	A	92	ILE	0	0.008	-0.001	14.553	0.038	0.038	0.000	0.000	0.000	0.000
85	A	93	VAL	0	-0.004	0.004	17.931	0.036	0.036	0.000	0.000	0.000	0.000
86	A	94	ASN	0	-0.027	-0.027	20.369	0.038	0.038	0.000	0.000	0.000	0.000
87	A	95	ARG	1	0.802	0.874	22.346	0.189	0.189	0.000	0.000	0.000	0.000
88	A	96	PHE	0	0.029	0.038	22.007	0.014	0.014	0.000	0.000	0.000	0.000
89	A	97	VAL	0	0.060	0.035	24.039	0.016	0.016	0.000	0.000	0.000	0.000
90	A	98	GLU	-1	-0.800	-0.860	26.295	-0.135	-0.135	0.000	0.000	0.000	0.000
91	A	99	THR	0	-0.053	-0.047	26.617	0.015	0.015	0.000	0.000	0.000	0.000
92	A	100	GLN	0	-0.049	-0.017	27.047	0.002	0.002	0.000	0.000	0.000	0.000
93	A	101	THR	0	0.013	0.001	29.395	0.008	0.008	0.000	0.000	0.000	0.000
94	A	102	ASN	0	-0.046	-0.031	31.976	0.008	0.008	0.000	0.000	0.000	0.000
95	A	103	TYR	0	0.001	0.001	31.806	0.008	0.008	0.000	0.000	0.000	0.000
96	A	104	GLU	-1	-0.854	-0.925	31.985	-0.054	-0.054	0.000	0.000	0.000	0.000
97	A	105	LYS	1	0.923	0.972	35.269	0.055	0.055	0.000	0.000	0.000	0.000
98	A	106	LEU	0	-0.059	-0.037	36.126	0.004	0.004	0.000	0.000	0.000	0.000
99	A	107	LYS	1	0.846	0.900	35.308	0.024	0.024	0.000	0.000	0.000	0.000
100	A	108	ASN	0	-0.011	-0.020	38.539	0.006	0.006	0.000	0.000	0.000	0.000
101	A	109	ARG	1	0.921	0.973	40.547	0.032	0.032	0.000	0.000	0.000	0.000
102	A	110	LEU	0	-0.012	-0.008	39.757	0.002	0.002	0.000	0.000	0.000	0.000
103	A	111	VAL	0	0.015	0.010	41.466	0.003	0.003	0.000	0.000	0.000	0.000
104	A	112	GLN	0	0.020	0.004	44.196	0.004	0.004	0.000	0.000	0.000	0.000
105	A	113	ASN	0	-0.006	-0.011	46.639	0.000	0.000	0.000	0.000	0.000	0.000
106	A	114	ALA	0	0.002	0.005	47.014	0.001	0.001	0.000	0.000	0.000	0.000
107	A	115	ARG	1	0.858	0.934	45.163	0.019	0.019	0.000	0.000	0.000	0.000
108	A	116	VAL	0	-0.016	-0.004	50.477	0.001	0.001	0.000	0.000	0.000	0.000
109	A	117	ALA	0	-0.027	0.015	51.801	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)