FMO DATABASE

FMODB ID: MN8QZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1850230.586292
FMO2-HF: Nuclear repulsion	1781671.775168
FMO2-HF: Total energy	-68558.811124
FMO2-MP2: Total energy	-68760.13424

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.
-30.523	-28.788	18.025	-9.846	-9.913	-0.102

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 : -0.099 / q_NPA : -0.063

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	-0.032	-0.020	3.831	1.901	3.032	-0.009	-0.440	-0.682	0.002
4	A	4	PRO	0	-0.021	-0.023	6.792	0.077	0.077	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.027	0.011	10.068	-0.172	-0.172	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.810	0.898	12.607	0.642	0.642	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.061	0.041	15.810	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.018	-0.032	18.960	0.002	0.002	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.027	0.009	22.465	0.029	0.029	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.791	-0.867	18.058	-0.336	-0.336	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.011	-0.015	21.490	-0.028	-0.028	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.080	-0.036	17.447	0.001	0.001	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.006	-0.004	18.005	-0.032	-0.032	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.767	0.851	21.323	0.284	0.284	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.887	0.965	21.758	0.340	0.340	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.861	0.934	23.859	0.303	0.303	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.030	-0.009	20.108	0.015	0.015	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.896	0.930	21.309	0.339	0.339	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.044	0.006	20.854	-0.055	-0.055	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.046	-0.011	16.981	0.004	0.004	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.932	-0.961	19.830	-0.276	-0.276	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.849	-0.899	17.697	-0.360	-0.360	0.000	0.000	0.000	0.000
23	A	23	PHE	0	0.006	-0.021	16.037	-0.068	-0.068	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.057	-0.033	14.609	-0.077	-0.077	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.011	0.001	11.105	0.010	0.010	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.027	0.001	9.880	-0.280	-0.280	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.914	0.955	9.013	0.638	0.638	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.860	0.898	2.778	1.972	2.589	0.165	-0.194	-0.587	0.001
29	A	29	LEU	0	0.035	0.035	5.306	-0.910	-0.910	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.021	-0.007	7.337	-0.516	-0.516	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.865	-0.920	4.291	-2.169	-1.991	-0.001	-0.013	-0.164	0.000
32	A	32	ASP	-1	-0.809	-0.905	2.521	-13.806	-10.715	1.523	-1.946	-2.668	-0.026
33	A	33	MET	0	-0.081	-0.022	4.242	0.443	0.472	-0.001	-0.013	-0.015	0.000
34	A	34	LEU	0	0.013	-0.005	7.277	0.445	0.445	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.880	-0.922	1.765	-22.245	-25.556	16.348	-7.240	-5.797	-0.079
36	A	36	THR	0	0.028	-0.005	5.818	1.157	1.157	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.076	-0.012	6.963	0.831	0.831	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.024	-0.007	8.303	0.516	0.516	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.913	-0.953	6.431	0.346	0.346	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.008	-0.004	8.791	0.371	0.371	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.783	0.888	10.921	0.942	0.942	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.013	0.025	13.147	0.113	0.113	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.026	-0.029	14.656	-0.059	-0.059	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.037	-0.001	15.726	0.010	0.010	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.031	-0.003	10.383	-0.025	-0.025	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.072	0.030	14.079	-0.073	-0.073	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.019	0.004	12.991	-0.051	-0.051	0.000	0.000	0.000	0.000
48	A	48	PRO	0	-0.018	-0.018	13.974	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.057	0.027	14.400	-0.025	-0.025	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.022	0.032	8.733	0.045	0.045	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.041	-0.020	11.849	0.012	0.012	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.014	0.018	10.695	0.122	0.122	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.012	-0.008	15.014	0.007	0.007	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.001	-0.011	14.834	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.848	0.908	17.628	0.375	0.375	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.035	0.012	12.244	0.038	0.038	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.020	-0.004	14.771	-0.014	-0.014	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.015	0.024	10.717	0.030	0.030	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.021	-0.006	13.906	0.070	0.070	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.046	-0.018	13.343	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.842	-0.891	16.411	-0.353	-0.353	0.000	0.000	0.000	0.000
62	A	74	LEU	0	0.010	-0.005	10.943	-0.039	-0.039	0.000	0.000	0.000	0.000
63	A	75	ARG	1	0.892	0.926	8.315	0.793	0.793	0.000	0.000	0.000	0.000
64	A	76	GLU	-1	-0.865	-0.915	11.806	-0.284	-0.284	0.000	0.000	0.000	0.000
65	A	77	LEU	0	-0.034	-0.015	14.890	0.075	0.075	0.000	0.000	0.000	0.000
66	A	78	VAL	0	-0.061	-0.008	13.881	0.036	0.036	0.000	0.000	0.000	0.000
67	A	79	ARG	1	0.917	0.936	16.982	0.397	0.397	0.000	0.000	0.000	0.000
68	A	80	ARG	1	0.883	0.928	18.416	0.455	0.455	0.000	0.000	0.000	0.000
69	A	81	VAL	0	0.040	0.026	11.976	-0.033	-0.033	0.000	0.000	0.000	0.000
70	A	82	TYR	0	-0.035	-0.015	15.349	0.093	0.093	0.000	0.000	0.000	0.000
71	A	83	VAL	0	0.064	0.031	12.033	-0.136	-0.136	0.000	0.000	0.000	0.000
72	A	84	VAL	0	-0.041	-0.017	14.833	0.124	0.124	0.000	0.000	0.000	0.000
73	A	85	ALA	0	0.044	0.024	17.103	-0.042	-0.042	0.000	0.000	0.000	0.000
74	A	86	ASN	0	-0.050	-0.049	18.750	0.040	0.040	0.000	0.000	0.000	0.000
75	A	87	PRO	0	0.001	0.004	20.834	0.037	0.037	0.000	0.000	0.000	0.000
76	A	88	VAL	0	-0.022	-0.014	23.690	0.017	0.017	0.000	0.000	0.000	0.000
77	A	89	ILE	0	-0.023	-0.013	27.360	0.001	0.001	0.000	0.000	0.000	0.000
78	A	90	THR	0	-0.058	-0.053	29.414	0.016	0.016	0.000	0.000	0.000	0.000
79	A	91	TYR	0	-0.091	-0.058	32.175	0.021	0.021	0.000	0.000	0.000	0.000
80	A	92	ARG	1	0.932	0.966	31.279	0.240	0.240	0.000	0.000	0.000	0.000
81	A	93	GLU	-1	-0.801	-0.864	34.384	-0.175	-0.175	0.000	0.000	0.000	0.000
82	A	94	GLY	0	0.081	0.041	35.544	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	95	LEU	0	-0.064	-0.047	36.041	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	96	VAL	0	0.034	0.022	33.778	0.011	0.011	0.000	0.000	0.000	0.000
85	A	97	GLU	-1	-0.892	-0.945	33.701	-0.192	-0.192	0.000	0.000	0.000	0.000
86	A	98	GLY	0	-0.002	-0.011	30.856	0.003	0.003	0.000	0.000	0.000	0.000
87	A	99	THR	0	0.014	0.011	26.941	0.001	0.001	0.000	0.000	0.000	0.000
88	A	100	GLU	-1	-0.770	-0.825	24.863	-0.392	-0.392	0.000	0.000	0.000	0.000
89	A	101	GLY	0	0.096	0.045	22.952	0.037	0.037	0.000	0.000	0.000	0.000
90	A	102	OCS	-1	-0.908	-0.943	19.280	-0.596	-0.596	0.000	0.000	0.000	0.000
91	A	103	LEU	0	0.065	0.036	13.330	0.052	0.052	0.000	0.000	0.000	0.000
92	A	104	SER	0	0.008	0.001	17.094	0.014	0.014	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.093	-0.052	18.655	0.057	0.057	0.000	0.000	0.000	0.000
94	A	106	PRO	0	0.029	0.026	18.406	0.004	0.004	0.000	0.000	0.000	0.000
95	A	107	GLY	0	0.033	0.006	20.428	0.035	0.035	0.000	0.000	0.000	0.000
96	A	108	LEU	0	-0.047	-0.005	23.177	0.021	0.021	0.000	0.000	0.000	0.000
97	A	109	TYR	0	0.013	-0.007	21.583	-0.027	-0.027	0.000	0.000	0.000	0.000
98	A	110	SER	0	-0.041	-0.020	26.994	0.025	0.025	0.000	0.000	0.000	0.000
99	A	111	GLU	-1	-0.888	-0.959	29.304	-0.210	-0.210	0.000	0.000	0.000	0.000
100	A	112	GLU	-1	-0.853	-0.915	31.739	-0.161	-0.161	0.000	0.000	0.000	0.000
101	A	113	VAL	0	-0.008	-0.008	28.576	0.006	0.006	0.000	0.000	0.000	0.000
102	A	114	PRO	0	-0.001	0.021	31.724	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	115	ARG	1	0.725	0.809	26.376	0.335	0.335	0.000	0.000	0.000	0.000
104	A	116	ALA	0	-0.042	-0.019	31.761	0.016	0.016	0.000	0.000	0.000	0.000
105	A	117	GLU	-1	-0.951	-0.956	31.482	-0.225	-0.225	0.000	0.000	0.000	0.000
106	A	118	ARG	1	0.898	0.922	31.546	0.202	0.202	0.000	0.000	0.000	0.000
107	A	119	ILE	0	-0.053	-0.029	26.260	0.007	0.007	0.000	0.000	0.000	0.000
108	A	120	ARG	1	0.885	0.945	29.633	0.233	0.233	0.000	0.000	0.000	0.000
109	A	121	VAL	0	-0.006	-0.012	24.273	0.000	0.000	0.000	0.000	0.000	0.000
110	A	122	GLU	-1	-0.851	-0.900	26.805	-0.272	-0.272	0.000	0.000	0.000	0.000
111	A	123	TYR	0	-0.013	-0.016	19.967	-0.025	-0.025	0.000	0.000	0.000	0.000
112	A	124	GLN	0	-0.012	0.000	20.620	0.035	0.035	0.000	0.000	0.000	0.000
113	A	125	ASP	-1	-0.740	-0.855	17.722	-0.558	-0.558	0.000	0.000	0.000	0.000
114	A	126	GLU	-1	-0.820	-0.926	12.554	-0.826	-0.826	0.000	0.000	0.000	0.000
115	A	127	GLU	-1	-0.901	-0.946	14.953	-0.434	-0.434	0.000	0.000	0.000	0.000
116	A	128	GLY	0	0.003	0.013	17.284	0.058	0.058	0.000	0.000	0.000	0.000
117	A	129	ARG	1	0.743	0.850	17.566	0.493	0.493	0.000	0.000	0.000	0.000
118	A	130	GLY	0	0.027	0.020	22.095	-0.032	-0.032	0.000	0.000	0.000	0.000
119	A	131	ARG	1	0.832	0.912	21.702	0.383	0.383	0.000	0.000	0.000	0.000
120	A	132	VAL	0	0.049	0.021	25.034	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	133	LEU	0	-0.043	-0.009	22.749	0.002	0.002	0.000	0.000	0.000	0.000
122	A	134	GLU	-1	-0.815	-0.895	26.710	-0.238	-0.238	0.000	0.000	0.000	0.000
123	A	135	LEU	0	-0.057	-0.017	23.375	-0.011	-0.011	0.000	0.000	0.000	0.000
124	A	136	GLU	-1	-0.884	-0.955	27.907	-0.230	-0.230	0.000	0.000	0.000	0.000
125	A	137	GLY	0	0.019	0.013	28.496	-0.018	-0.018	0.000	0.000	0.000	0.000
126	A	138	TYR	0	0.007	-0.013	21.533	0.003	0.003	0.000	0.000	0.000	0.000
127	A	139	MET	0	0.067	0.033	19.868	-0.018	-0.018	0.000	0.000	0.000	0.000
128	A	140	ALA	0	0.037	0.028	24.005	-0.032	-0.032	0.000	0.000	0.000	0.000
129	A	141	ARG	1	0.813	0.904	25.741	0.295	0.295	0.000	0.000	0.000	0.000
130	A	142	VAL	0	0.001	-0.001	19.686	-0.009	-0.009	0.000	0.000	0.000	0.000
131	A	143	PHE	0	0.067	0.020	20.141	-0.035	-0.035	0.000	0.000	0.000	0.000
132	A	144	GLN	0	-0.061	-0.038	22.889	0.016	0.016	0.000	0.000	0.000	0.000
133	A	145	HIS	1	0.789	0.874	20.799	0.514	0.514	0.000	0.000	0.000	0.000
134	A	146	GLU	-1	-0.851	-0.935	17.557	-0.789	-0.789	0.000	0.000	0.000	0.000
135	A	147	ILE	0	-0.010	-0.017	20.560	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	148	ASP	-1	-0.762	-0.830	22.778	-0.332	-0.332	0.000	0.000	0.000	0.000
137	A	149	HIS	0	0.047	0.016	19.429	0.039	0.039	0.000	0.000	0.000	0.000
138	A	150	LEU	0	-0.073	-0.018	18.197	0.011	0.011	0.000	0.000	0.000	0.000
139	A	151	ASP	-1	-0.855	-0.919	21.735	-0.327	-0.327	0.000	0.000	0.000	0.000
140	A	152	GLY	0	0.002	0.033	23.700	0.035	0.035	0.000	0.000	0.000	0.000
141	A	153	ILE	0	-0.072	-0.036	24.850	0.036	0.036	0.000	0.000	0.000	0.000
142	A	154	LEU	0	0.060	0.030	22.519	-0.033	-0.033	0.000	0.000	0.000	0.000
143	A	155	PHE	0	0.030	0.006	24.028	0.025	0.025	0.000	0.000	0.000	0.000
144	A	156	PHE	0	0.048	0.020	26.424	0.020	0.020	0.000	0.000	0.000	0.000
145	A	157	GLU	-1	-0.816	-0.891	28.679	-0.244	-0.244	0.000	0.000	0.000	0.000
146	A	158	ARG	1	0.757	0.852	28.711	0.307	0.307	0.000	0.000	0.000	0.000
147	A	159	LEU	0	-0.008	0.019	31.640	0.009	0.009	0.000	0.000	0.000	0.000
148	A	160	PRO	0	0.023	0.002	34.385	0.005	0.005	0.000	0.000	0.000	0.000
149	A	161	LYS	1	0.851	0.907	37.732	0.122	0.122	0.000	0.000	0.000	0.000
150	A	162	PRO	0	0.045	0.015	38.773	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	163	LYS	1	0.838	0.916	36.277	0.169	0.169	0.000	0.000	0.000	0.000
152	A	164	ARG	1	0.927	0.978	33.277	0.180	0.180	0.000	0.000	0.000	0.000
153	A	165	GLU	-1	-0.838	-0.910	34.782	-0.128	-0.128	0.000	0.000	0.000	0.000
154	A	166	ALA	0	0.019	0.015	36.953	0.004	0.004	0.000	0.000	0.000	0.000
155	A	167	PHE	0	0.004	0.005	27.446	0.003	0.003	0.000	0.000	0.000	0.000
156	A	168	LEU	0	-0.004	-0.009	30.946	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	169	GLU	-1	-0.847	-0.922	33.337	-0.093	-0.093	0.000	0.000	0.000	0.000
158	A	170	ALA	0	-0.032	-0.011	34.164	0.007	0.007	0.000	0.000	0.000	0.000
159	A	171	ASN	0	-0.017	-0.011	29.428	0.008	0.008	0.000	0.000	0.000	0.000
160	A	172	ARG	1	0.852	0.930	30.339	0.092	0.092	0.000	0.000	0.000	0.000
161	A	173	ALA	0	-0.013	-0.011	31.350	0.000	0.000	0.000	0.000	0.000	0.000
162	A	174	GLU	-1	-0.773	-0.894	25.249	-0.118	-0.118	0.000	0.000	0.000	0.000
163	A	175	LEU	0	-0.020	-0.001	26.427	-0.008	-0.008	0.000	0.000	0.000	0.000
164	A	176	VAL	0	-0.021	-0.023	27.158	-0.002	-0.002	0.000	0.000	0.000	0.000
165	A	177	ARG	1	0.782	0.880	20.788	0.121	0.121	0.000	0.000	0.000	0.000
166	A	178	PHE	0	0.019	0.005	22.645	0.000	0.000	0.000	0.000	0.000	0.000
167	A	179	GLN	0	0.009	-0.002	22.931	0.000	0.000	0.000	0.000	0.000	0.000
168	A	180	LYS	1	0.840	0.926	24.666	0.081	0.081	0.000	0.000	0.000	0.000
169	A	181	GLU	-1	-0.865	-0.907	19.348	-0.080	-0.080	0.000	0.000	0.000	0.000
170	A	182	ALA	0	-0.066	-0.019	19.807	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)