FMO DATABASE

FMODB ID: 76N1K

Calculation Name: 1V3Y-A-Xray372

Preferred Name:

Target Type:

Ligand Name: cysteinesulfonic acid

ligand 3-letter code: OCS

PDB ID: 1V3Y

Chain ID: A

ChEMBL ID:

UniProt ID: P43522

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	170
LigandResidueName
LigandFragmentNumber	0
LigandCharge	OCS=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1852106.381959
FMO2-HF: Nuclear repulsion	1783547.162276
FMO2-HF: Total energy	-68559.219683
FMO2-MP2: Total energy	-68760.496492

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:1:MET)

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

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.
-24.558	-23.422	16.272	-7.841	-9.569	-0.088

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.077 / q_NPA : -0.054

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	3	TYR	0	-0.024	-0.019	3.877	1.979	3.200	-0.008	-0.489	-0.725	0.002
4	A	4	PRO	0	-0.028	-0.029	6.715	0.121	0.121	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.013	0.011	10.077	-0.103	-0.103	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.818	0.914	12.652	0.591	0.591	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.044	0.031	15.892	-0.038	-0.038	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.042	-0.040	19.087	0.001	0.001	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.031	0.004	22.522	0.030	0.030	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.797	-0.872	17.851	-0.293	-0.293	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.001	-0.015	21.272	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.059	-0.026	17.246	0.000	0.000	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.006	0.011	18.016	-0.024	-0.024	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.765	0.846	21.338	0.258	0.258	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.855	0.937	21.905	0.306	0.306	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.839	0.912	22.858	0.273	0.273	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.010	0.012	20.036	0.019	0.019	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.886	0.928	21.441	0.300	0.300	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.023	0.000	20.900	-0.050	-0.050	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.037	-0.003	16.622	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.927	-0.960	19.431	-0.262	-0.262	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.798	-0.875	17.081	-0.360	-0.360	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.002	-0.026	15.597	-0.059	-0.059	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.093	-0.059	13.954	-0.107	-0.107	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.027	0.018	10.448	0.015	0.015	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.041	-0.012	9.397	-0.286	-0.286	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.828	0.895	9.257	0.608	0.608	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.833	0.884	2.434	3.525	3.861	1.447	-0.411	-1.373	-0.001
29	A	29	LEU	0	0.036	0.028	5.286	-0.920	-0.920	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.014	-0.002	7.433	-0.391	-0.391	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.848	-0.912	4.438	-2.618	-2.429	-0.001	-0.013	-0.175	0.000
32	A	32	ASP	-1	-0.787	-0.884	2.475	-11.663	-9.370	1.896	-1.532	-2.657	-0.021
33	A	33	MET	0	-0.061	-0.011	4.056	0.200	0.235	-0.001	-0.010	-0.024	0.000
34	A	34	LEU	0	0.011	-0.003	7.510	0.439	0.439	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.880	-0.933	1.814	-19.017	-21.955	12.939	-5.386	-4.615	-0.068
36	A	36	THR	0	0.011	-0.010	5.825	1.058	1.058	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.074	-0.009	7.199	0.760	0.760	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.025	-0.007	8.605	0.457	0.457	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.910	-0.959	6.862	0.277	0.277	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.001	-0.002	8.923	0.346	0.346	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.769	0.879	11.392	0.862	0.862	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.017	0.026	13.423	0.111	0.111	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.009	-0.022	14.990	-0.049	-0.049	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.004	-0.014	15.912	0.022	0.022	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.002	0.010	10.164	-0.024	-0.024	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.070	0.029	13.687	-0.087	-0.087	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.015	0.002	12.878	-0.041	-0.041	0.000	0.000	0.000	0.000
48	A	48	PRO	0	-0.016	-0.018	13.900	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.055	0.020	14.375	-0.028	-0.028	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.041	0.037	8.844	0.029	0.029	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.036	-0.023	11.976	0.080	0.080	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.002	0.008	10.772	0.109	0.109	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.001	0.008	15.026	0.012	0.012	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.006	-0.008	15.048	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.817	0.905	17.682	0.352	0.352	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.044	0.013	12.113	0.031	0.031	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.009	0.002	14.627	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.004	0.020	10.625	0.026	0.026	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.013	-0.004	13.856	0.057	0.057	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.053	-0.025	13.566	-0.024	-0.024	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.876	-0.925	16.566	-0.328	-0.328	0.000	0.000	0.000	0.000
62	A	74	LEU	0	0.028	0.003	11.190	-0.027	-0.027	0.000	0.000	0.000	0.000
63	A	75	ARG	1	0.863	0.916	8.506	0.842	0.842	0.000	0.000	0.000	0.000
64	A	76	GLU	-1	-0.870	-0.915	12.161	-0.374	-0.374	0.000	0.000	0.000	0.000
65	A	77	LEU	0	-0.045	-0.021	15.318	0.079	0.079	0.000	0.000	0.000	0.000
66	A	78	VAL	0	-0.012	0.012	14.111	0.025	0.025	0.000	0.000	0.000	0.000
67	A	79	ARG	1	0.886	0.936	17.495	0.360	0.360	0.000	0.000	0.000	0.000
68	A	80	ARG	1	0.887	0.933	18.533	0.442	0.442	0.000	0.000	0.000	0.000
69	A	81	VAL	0	0.048	0.035	12.101	-0.020	-0.020	0.000	0.000	0.000	0.000
70	A	82	TYR	0	-0.020	-0.011	15.151	0.098	0.098	0.000	0.000	0.000	0.000
71	A	83	VAL	0	0.054	0.029	12.130	-0.134	-0.134	0.000	0.000	0.000	0.000
72	A	84	VAL	0	-0.035	-0.016	14.893	0.114	0.114	0.000	0.000	0.000	0.000
73	A	85	ALA	0	0.052	0.031	16.834	-0.025	-0.025	0.000	0.000	0.000	0.000
74	A	86	ASN	0	-0.045	-0.048	18.467	0.040	0.040	0.000	0.000	0.000	0.000
75	A	87	PRO	0	-0.001	0.010	20.517	0.038	0.038	0.000	0.000	0.000	0.000
76	A	88	VAL	0	-0.003	-0.008	23.453	0.016	0.016	0.000	0.000	0.000	0.000
77	A	89	ILE	0	-0.021	-0.006	26.940	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	90	THR	0	-0.090	-0.077	29.136	0.014	0.014	0.000	0.000	0.000	0.000
79	A	91	TYR	0	-0.079	-0.057	32.046	0.020	0.020	0.000	0.000	0.000	0.000
80	A	92	ARG	1	0.903	0.948	31.032	0.226	0.226	0.000	0.000	0.000	0.000
81	A	93	GLU	-1	-0.785	-0.853	34.385	-0.170	-0.170	0.000	0.000	0.000	0.000
82	A	94	GLY	0	0.094	0.046	35.459	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	95	LEU	0	-0.070	-0.048	36.068	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	96	VAL	0	0.030	0.019	33.799	0.010	0.010	0.000	0.000	0.000	0.000
85	A	97	GLU	-1	-0.862	-0.916	33.495	-0.177	-0.177	0.000	0.000	0.000	0.000
86	A	98	GLY	0	0.001	-0.013	31.726	0.002	0.002	0.000	0.000	0.000	0.000
87	A	99	THR	0	-0.027	-0.029	27.321	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	100	GLU	-1	-0.773	-0.829	25.529	-0.363	-0.363	0.000	0.000	0.000	0.000
89	A	101	GLY	0	0.089	0.035	23.740	0.033	0.033	0.000	0.000	0.000	0.000
90	A	102	OCS	-1	-0.925	-0.941	19.168	-0.548	-0.548	0.000	0.000	0.000	0.000
91	A	103	LEU	0	0.069	0.042	13.764	0.042	0.042	0.000	0.000	0.000	0.000
92	A	104	SER	0	0.014	-0.008	17.362	0.015	0.015	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.087	-0.051	18.726	0.053	0.053	0.000	0.000	0.000	0.000
94	A	106	PRO	0	0.027	0.027	18.444	0.004	0.004	0.000	0.000	0.000	0.000
95	A	107	GLY	0	0.035	0.012	20.485	0.035	0.035	0.000	0.000	0.000	0.000
96	A	108	LEU	0	-0.055	-0.015	23.318	0.019	0.019	0.000	0.000	0.000	0.000
97	A	109	TYR	0	0.014	-0.014	22.046	-0.026	-0.026	0.000	0.000	0.000	0.000
98	A	110	SER	0	-0.030	-0.020	27.368	0.019	0.019	0.000	0.000	0.000	0.000
99	A	111	GLU	-1	-0.833	-0.908	29.932	-0.209	-0.209	0.000	0.000	0.000	0.000
100	A	112	GLU	-1	-0.851	-0.923	32.136	-0.152	-0.152	0.000	0.000	0.000	0.000
101	A	113	VAL	0	-0.009	0.004	28.794	0.006	0.006	0.000	0.000	0.000	0.000
102	A	114	PRO	0	-0.015	0.016	31.811	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	115	ARG	1	0.706	0.809	26.370	0.311	0.311	0.000	0.000	0.000	0.000
104	A	116	ALA	0	-0.050	-0.026	31.593	0.015	0.015	0.000	0.000	0.000	0.000
105	A	117	GLU	-1	-0.931	-0.956	31.449	-0.210	-0.210	0.000	0.000	0.000	0.000
106	A	118	ARG	1	0.887	0.914	31.684	0.196	0.196	0.000	0.000	0.000	0.000
107	A	119	ILE	0	-0.052	-0.032	26.397	0.008	0.008	0.000	0.000	0.000	0.000
108	A	120	ARG	1	0.860	0.933	29.380	0.230	0.230	0.000	0.000	0.000	0.000
109	A	121	VAL	0	-0.005	-0.009	23.880	0.000	0.000	0.000	0.000	0.000	0.000
110	A	122	GLU	-1	-0.830	-0.887	26.536	-0.259	-0.259	0.000	0.000	0.000	0.000
111	A	123	TYR	0	-0.005	-0.014	19.852	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	124	GLN	0	-0.023	-0.006	20.236	0.037	0.037	0.000	0.000	0.000	0.000
113	A	125	ASP	-1	-0.736	-0.848	17.354	-0.557	-0.557	0.000	0.000	0.000	0.000
114	A	126	GLU	-1	-0.804	-0.910	12.469	-0.859	-0.859	0.000	0.000	0.000	0.000
115	A	127	GLU	-1	-0.836	-0.899	14.202	-0.531	-0.531	0.000	0.000	0.000	0.000
116	A	128	GLY	0	0.013	0.022	16.646	0.065	0.065	0.000	0.000	0.000	0.000
117	A	129	ARG	1	0.733	0.834	16.914	0.511	0.511	0.000	0.000	0.000	0.000
118	A	130	GLY	0	0.036	0.019	21.749	-0.030	-0.030	0.000	0.000	0.000	0.000
119	A	131	ARG	1	0.828	0.911	21.268	0.387	0.387	0.000	0.000	0.000	0.000
120	A	132	VAL	0	0.039	0.015	24.544	0.003	0.003	0.000	0.000	0.000	0.000
121	A	133	LEU	0	-0.039	-0.009	22.736	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	134	GLU	-1	-0.815	-0.890	26.584	-0.231	-0.231	0.000	0.000	0.000	0.000
123	A	135	LEU	0	-0.034	-0.013	23.283	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	136	GLU	-1	-0.877	-0.954	27.908	-0.221	-0.221	0.000	0.000	0.000	0.000
125	A	137	GLY	0	0.034	0.019	28.334	-0.020	-0.020	0.000	0.000	0.000	0.000
126	A	138	TYR	0	0.002	-0.006	21.805	0.005	0.005	0.000	0.000	0.000	0.000
127	A	139	MET	0	0.049	0.024	20.242	-0.022	-0.022	0.000	0.000	0.000	0.000
128	A	140	ALA	0	0.028	0.027	24.327	-0.028	-0.028	0.000	0.000	0.000	0.000
129	A	141	ARG	1	0.826	0.910	25.782	0.274	0.274	0.000	0.000	0.000	0.000
130	A	142	VAL	0	0.013	0.006	19.933	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	143	PHE	0	0.047	0.006	20.144	-0.031	-0.031	0.000	0.000	0.000	0.000
132	A	144	GLN	0	-0.052	-0.037	22.947	0.019	0.019	0.000	0.000	0.000	0.000
133	A	145	HIS	1	0.783	0.884	20.566	0.470	0.470	0.000	0.000	0.000	0.000
134	A	146	GLU	-1	-0.852	-0.944	17.373	-0.727	-0.727	0.000	0.000	0.000	0.000
135	A	147	ILE	0	-0.014	-0.015	20.220	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	148	ASP	-1	-0.780	-0.846	22.699	-0.309	-0.309	0.000	0.000	0.000	0.000
137	A	149	HIS	0	0.061	0.021	19.325	0.024	0.024	0.000	0.000	0.000	0.000
138	A	150	LEU	0	-0.072	-0.016	17.825	0.018	0.018	0.000	0.000	0.000	0.000
139	A	151	ASP	-1	-0.813	-0.906	21.539	-0.300	-0.300	0.000	0.000	0.000	0.000
140	A	152	GLY	0	-0.029	0.021	23.714	0.032	0.032	0.000	0.000	0.000	0.000
141	A	153	ILE	0	-0.044	-0.027	24.893	0.032	0.032	0.000	0.000	0.000	0.000
142	A	154	LEU	0	0.058	0.026	22.785	-0.029	-0.029	0.000	0.000	0.000	0.000
143	A	155	PHE	0	0.024	0.001	24.444	0.020	0.020	0.000	0.000	0.000	0.000
144	A	156	PHE	0	0.054	0.028	26.366	0.017	0.017	0.000	0.000	0.000	0.000
145	A	157	GLU	-1	-0.827	-0.903	28.641	-0.220	-0.220	0.000	0.000	0.000	0.000
146	A	158	ARG	1	0.804	0.884	28.152	0.292	0.292	0.000	0.000	0.000	0.000
147	A	159	LEU	0	0.000	0.028	31.913	0.008	0.008	0.000	0.000	0.000	0.000
148	A	160	PRO	0	0.021	0.001	34.371	0.005	0.005	0.000	0.000	0.000	0.000
149	A	161	LYS	1	0.829	0.896	37.941	0.112	0.112	0.000	0.000	0.000	0.000
150	A	162	PRO	0	0.036	0.009	38.829	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	163	LYS	1	0.833	0.905	36.461	0.155	0.155	0.000	0.000	0.000	0.000
152	A	164	ARG	1	0.934	0.986	33.452	0.166	0.166	0.000	0.000	0.000	0.000
153	A	165	GLU	-1	-0.840	-0.906	34.886	-0.117	-0.117	0.000	0.000	0.000	0.000
154	A	166	ALA	0	0.019	0.014	37.253	0.004	0.004	0.000	0.000	0.000	0.000
155	A	167	PHE	0	0.004	0.005	27.764	0.003	0.003	0.000	0.000	0.000	0.000
156	A	168	LEU	0	-0.013	-0.007	31.331	0.001	0.001	0.000	0.000	0.000	0.000
157	A	169	GLU	-1	-0.820	-0.905	33.731	-0.082	-0.082	0.000	0.000	0.000	0.000
158	A	170	ALA	0	-0.038	-0.016	34.584	0.006	0.006	0.000	0.000	0.000	0.000
159	A	171	ASN	0	-0.007	-0.012	29.695	0.005	0.005	0.000	0.000	0.000	0.000
160	A	172	ARG	1	0.807	0.896	30.504	0.084	0.084	0.000	0.000	0.000	0.000
161	A	173	ALA	0	-0.002	-0.001	31.552	0.002	0.002	0.000	0.000	0.000	0.000
162	A	174	GLU	-1	-0.765	-0.884	25.387	-0.098	-0.098	0.000	0.000	0.000	0.000
163	A	175	LEU	0	-0.028	0.004	26.562	-0.008	-0.008	0.000	0.000	0.000	0.000
164	A	176	VAL	0	0.007	-0.011	27.366	0.000	0.000	0.000	0.000	0.000	0.000
165	A	177	ARG	1	0.796	0.884	20.802	0.106	0.106	0.000	0.000	0.000	0.000
166	A	178	PHE	0	0.047	0.014	22.852	0.002	0.002	0.000	0.000	0.000	0.000
167	A	179	GLN	0	-0.011	-0.015	23.237	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	180	LYS	1	0.772	0.884	25.407	0.073	0.073	0.000	0.000	0.000	0.000
169	A	181	GLU	-1	-0.853	-0.880	19.886	-0.053	-0.053	0.000	0.000	0.000	0.000
170	A	182	ALA	0	-0.058	-0.019	19.557	0.012	0.012	0.000	0.000	0.000	0.000

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