FMO DATABASE

FMODB ID: JQV49

Calculation Name: 2PN0-A-Xray372

Preferred Name:

Target Type:

Ligand Name: cysteinesulfonic acid

ligand 3-letter code: OCS

PDB ID: 2PN0

Chain ID: A

ChEMBL ID:

UniProt ID: Q82T10

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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge	OCS=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-983405.541777
FMO2-HF: Nuclear repulsion	935889.424716
FMO2-HF: Total energy	-47516.117061
FMO2-MP2: Total energy	-47655.170407

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:4:LYS)

Summations of interaction energy for fragment #1(A:4:LYS)

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.
-155.843	-153.667	0.214	-0.9	-1.491	0.001

Interaction energy analysis for fragmet #1(A:4:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.955 / q_NPA : 0.969

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	6	LYS	1	0.815	0.907	3.888	35.470	36.812	-0.001	-0.620	-0.721	0.001
4	A	7	ILE	0	0.070	0.059	6.842	0.407	0.407	0.000	0.000	0.000	0.000
5	A	8	MET	0	-0.011	-0.002	9.534	-0.228	-0.228	0.000	0.000	0.000	0.000
6	A	9	ILE	0	0.002	0.004	12.984	1.178	1.178	0.000	0.000	0.000	0.000
7	A	10	SER	0	0.040	-0.004	15.735	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	11	SER	0	0.033	-0.009	19.233	-0.173	-0.173	0.000	0.000	0.000	0.000
9	A	12	LEU	0	-0.012	0.005	20.980	0.262	0.262	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.787	-0.864	19.132	-13.267	-13.267	0.000	0.000	0.000	0.000
11	A	14	ALA	0	0.005	0.006	17.558	0.015	0.015	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.961	-0.970	18.764	-11.674	-11.674	0.000	0.000	0.000	0.000
13	A	16	ARG	1	0.858	0.927	22.292	11.750	11.750	0.000	0.000	0.000	0.000
14	A	17	LEU	0	-0.027	-0.021	17.221	0.465	0.465	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.873	-0.922	18.520	-15.042	-15.042	0.000	0.000	0.000	0.000
16	A	19	ILE	0	0.036	0.019	20.755	0.477	0.477	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.074	-0.022	22.229	0.573	0.573	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.010	0.001	17.797	0.427	0.427	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.915	-0.956	22.130	-11.495	-11.495	0.000	0.000	0.000	0.000
20	A	23	THR	0	-0.096	-0.064	24.756	0.542	0.542	0.000	0.000	0.000	0.000
21	A	24	LEU	0	-0.049	-0.020	24.677	0.437	0.437	0.000	0.000	0.000	0.000
22	A	25	SER	0	0.013	0.022	24.299	-0.070	-0.070	0.000	0.000	0.000	0.000
23	A	26	GLN	0	-0.045	-0.020	24.901	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	27	ASN	0	-0.050	-0.027	25.247	0.141	0.141	0.000	0.000	0.000	0.000
25	A	28	ALA	0	0.039	0.027	22.415	-0.429	-0.429	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.004	0.007	18.098	0.308	0.308	0.000	0.000	0.000	0.000
27	A	30	PRO	0	-0.019	-0.024	19.953	-0.362	-0.362	0.000	0.000	0.000	0.000
28	A	31	GLY	0	0.046	0.018	15.585	-0.031	-0.031	0.000	0.000	0.000	0.000
29	A	32	ARG	1	0.694	0.820	15.108	12.235	12.235	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.882	-0.947	15.048	-15.023	-15.023	0.000	0.000	0.000	0.000
31	A	34	ASP	-1	-0.935	-0.971	10.880	-18.686	-18.686	0.000	0.000	0.000	0.000
32	A	35	LEU	0	0.045	0.025	10.814	-1.177	-1.177	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.795	-0.884	12.918	-14.744	-14.744	0.000	0.000	0.000	0.000
34	A	37	ALA	0	-0.047	-0.023	9.916	-0.712	-0.712	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.973	-0.999	7.851	-25.380	-25.380	0.000	0.000	0.000	0.000
36	A	39	LEU	0	0.007	-0.010	9.381	-1.295	-1.295	0.000	0.000	0.000	0.000
37	A	40	ALA	0	0.007	0.013	12.203	-0.522	-0.522	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.781	0.890	3.189	38.819	39.653	0.215	-0.280	-0.770	0.000
39	A	42	ALA	0	0.048	0.038	8.536	-4.011	-4.011	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.968	-0.993	8.858	-32.030	-32.030	0.000	0.000	0.000	0.000
41	A	44	VAL	0	-0.001	0.012	12.011	1.068	1.068	0.000	0.000	0.000	0.000
42	A	45	VAL	0	-0.015	-0.008	14.620	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.871	-0.954	17.451	-12.551	-12.551	0.000	0.000	0.000	0.000
44	A	47	PRO	0	-0.012	-0.033	19.938	-0.574	-0.574	0.000	0.000	0.000	0.000
45	A	48	GLU	-1	-0.949	-0.963	21.463	-12.205	-12.205	0.000	0.000	0.000	0.000
46	A	49	GLU	-1	-1.008	-0.989	17.303	-15.733	-15.733	0.000	0.000	0.000	0.000
47	A	50	ILE	0	-0.037	-0.014	16.499	-1.380	-1.380	0.000	0.000	0.000	0.000
48	A	51	PRO	0	-0.011	-0.010	15.195	0.855	0.855	0.000	0.000	0.000	0.000
49	A	52	PRO	0	0.022	0.005	18.329	-0.151	-0.151	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.026	-0.011	17.393	0.366	0.366	0.000	0.000	0.000	0.000
51	A	54	VAL	0	0.000	0.003	13.997	-0.334	-0.334	0.000	0.000	0.000	0.000
52	A	55	VAL	0	-0.011	-0.004	15.894	0.907	0.907	0.000	0.000	0.000	0.000
53	A	56	THR	0	0.031	0.013	16.138	-0.695	-0.695	0.000	0.000	0.000	0.000
54	A	57	MET	0	0.004	0.000	18.428	0.252	0.252	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.058	-0.031	20.709	0.094	0.094	0.000	0.000	0.000	0.000
56	A	59	SER	0	0.035	0.031	20.397	0.263	0.263	0.000	0.000	0.000	0.000
57	A	60	THR	0	-0.049	-0.032	22.515	0.035	0.035	0.000	0.000	0.000	0.000
58	A	61	VAL	0	-0.007	-0.005	19.511	-0.267	-0.267	0.000	0.000	0.000	0.000
59	A	62	ARG	1	0.850	0.922	22.545	10.292	10.292	0.000	0.000	0.000	0.000
60	A	63	PHE	0	0.024	-0.013	19.141	-0.585	-0.585	0.000	0.000	0.000	0.000
61	A	64	ARG	1	0.817	0.891	23.662	10.935	10.935	0.000	0.000	0.000	0.000
62	A	65	VAL	0	-0.003	0.007	24.020	-0.506	-0.506	0.000	0.000	0.000	0.000
63	A	66	GLU	-1	-0.900	-0.967	22.650	-11.611	-11.611	0.000	0.000	0.000	0.000
64	A	67	SER	0	-0.047	-0.028	26.008	0.193	0.193	0.000	0.000	0.000	0.000
65	A	68	SER	0	-0.090	-0.092	29.024	0.218	0.218	0.000	0.000	0.000	0.000
66	A	69	ALA	0	-0.042	-0.012	29.017	0.219	0.219	0.000	0.000	0.000	0.000
67	A	70	GLU	-1	-0.885	-0.893	29.910	-8.910	-8.910	0.000	0.000	0.000	0.000
68	A	71	GLU	-1	-0.768	-0.872	28.185	-10.389	-10.389	0.000	0.000	0.000	0.000
69	A	72	PHE	0	-0.055	-0.012	24.174	0.345	0.345	0.000	0.000	0.000	0.000
70	A	73	OCS	-1	-0.882	-0.944	26.135	-10.219	-10.219	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.013	-0.008	22.694	0.217	0.217	0.000	0.000	0.000	0.000
72	A	75	THR	0	0.002	0.000	23.635	-0.442	-0.442	0.000	0.000	0.000	0.000
73	A	76	LEU	0	-0.014	0.017	17.731	0.288	0.288	0.000	0.000	0.000	0.000
74	A	77	VAL	0	-0.017	-0.011	22.039	0.001	0.001	0.000	0.000	0.000	0.000
75	A	78	TYR	0	0.031	-0.026	22.269	-0.108	-0.108	0.000	0.000	0.000	0.000
76	A	79	PRO	0	0.013	-0.009	24.213	0.348	0.348	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.758	0.861	27.125	10.006	10.006	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.790	-0.871	28.015	-9.605	-9.605	0.000	0.000	0.000	0.000
79	A	82	VAL	0	0.002	0.005	27.338	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	83	ASP	-1	-0.781	-0.857	29.930	-8.472	-8.472	0.000	0.000	0.000	0.000
81	A	84	THR	0	-0.023	-0.032	32.207	-0.122	-0.122	0.000	0.000	0.000	0.000
82	A	85	SER	0	-0.089	-0.064	32.472	0.045	0.045	0.000	0.000	0.000	0.000
83	A	86	GLY	0	-0.014	-0.006	30.270	0.078	0.078	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.803	-0.865	28.354	-10.007	-10.007	0.000	0.000	0.000	0.000
85	A	88	LYS	1	0.789	0.893	27.142	8.879	8.879	0.000	0.000	0.000	0.000
86	A	89	ILE	0	0.011	0.009	21.539	0.118	0.118	0.000	0.000	0.000	0.000
87	A	90	SER	0	0.011	0.008	23.296	-0.377	-0.377	0.000	0.000	0.000	0.000
88	A	91	ILE	0	0.056	0.018	16.535	-0.064	-0.064	0.000	0.000	0.000	0.000
89	A	92	LEU	0	-0.013	-0.006	19.031	-0.357	-0.357	0.000	0.000	0.000	0.000
90	A	93	ALA	0	-0.047	-0.013	21.392	0.258	0.258	0.000	0.000	0.000	0.000
91	A	94	PRO	0	0.015	-0.009	19.884	-0.455	-0.455	0.000	0.000	0.000	0.000
92	A	95	VAL	0	0.021	0.021	17.940	0.348	0.348	0.000	0.000	0.000	0.000
93	A	96	GLY	0	0.047	0.016	17.443	-0.551	-0.551	0.000	0.000	0.000	0.000
94	A	97	SER	0	-0.046	-0.029	16.537	-0.453	-0.453	0.000	0.000	0.000	0.000
95	A	98	ALA	0	-0.024	-0.010	13.195	-0.708	-0.708	0.000	0.000	0.000	0.000
96	A	99	LEU	0	-0.010	-0.012	13.594	-0.435	-0.435	0.000	0.000	0.000	0.000
97	A	100	LEU	0	-0.003	-0.008	13.862	-0.015	-0.015	0.000	0.000	0.000	0.000
98	A	101	GLY	0	-0.023	-0.013	11.571	-0.937	-0.937	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.026	0.010	10.937	-1.183	-1.183	0.000	0.000	0.000	0.000
100	A	103	ALA	0	0.006	-0.005	12.826	0.586	0.586	0.000	0.000	0.000	0.000
101	A	104	GLN	0	-0.092	-0.063	15.070	-0.040	-0.040	0.000	0.000	0.000	0.000
102	A	105	GLY	0	-0.043	-0.015	17.155	-0.535	-0.535	0.000	0.000	0.000	0.000
103	A	106	ASP	-1	-0.844	-0.910	12.507	-20.198	-20.198	0.000	0.000	0.000	0.000
104	A	107	GLU	-1	-0.848	-0.903	14.740	-13.004	-13.004	0.000	0.000	0.000	0.000
105	A	108	ILE	0	-0.014	0.007	14.129	-0.771	-0.771	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.865	-0.934	16.653	-12.617	-12.617	0.000	0.000	0.000	0.000
107	A	110	TRP	0	0.043	0.023	18.734	-0.406	-0.406	0.000	0.000	0.000	0.000
108	A	111	PRO	0	-0.003	-0.010	21.447	0.306	0.306	0.000	0.000	0.000	0.000
109	A	112	LYS	1	0.916	0.964	24.744	9.365	9.365	0.000	0.000	0.000	0.000
110	A	113	PRO	0	0.025	-0.002	28.052	0.114	0.114	0.000	0.000	0.000	0.000
111	A	114	GLY	0	-0.034	-0.010	31.294	0.059	0.059	0.000	0.000	0.000	0.000
112	A	115	GLY	0	0.018	0.011	29.843	0.114	0.114	0.000	0.000	0.000	0.000
113	A	116	GLY	0	-0.023	-0.005	27.165	0.098	0.098	0.000	0.000	0.000	0.000
114	A	117	VAL	0	-0.002	0.003	21.965	0.102	0.102	0.000	0.000	0.000	0.000
115	A	118	LEU	0	-0.017	-0.012	24.108	0.329	0.329	0.000	0.000	0.000	0.000
116	A	119	ARG	1	0.840	0.909	16.481	13.955	13.955	0.000	0.000	0.000	0.000
117	A	120	VAL	0	-0.012	-0.016	20.018	0.532	0.532	0.000	0.000	0.000	0.000
118	A	121	ARG	1	0.835	0.903	19.138	12.544	12.544	0.000	0.000	0.000	0.000
119	A	122	ILE	0	0.043	0.031	16.187	0.761	0.761	0.000	0.000	0.000	0.000
120	A	123	VAL	0	-0.060	-0.029	19.934	-0.325	-0.325	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.950	-0.982	22.761	-10.684	-10.684	0.000	0.000	0.000	0.000
122	A	125	VAL	0	0.003	0.007	18.686	-0.086	-0.086	0.000	0.000	0.000	0.000
123	A	126	THR	0	0.014	0.020	22.170	0.190	0.190	0.000	0.000	0.000	0.000
124	A	127	TYR	0	-0.019	-0.005	23.015	0.477	0.477	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LYS)