FMO DATABASE

FMODB ID: MN8ZZ

Calculation Name: 1LME-A-Xray372

Preferred Name:

Target Type:

Ligand Name: cysteinesulfonic acid

ligand 3-letter code: OCS

PDB ID: 1LME

Chain ID: A

ChEMBL ID:

UniProt ID: P96113

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:

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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge	OCS=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1588918.991604
FMO2-HF: Nuclear repulsion	1526058.9129
FMO2-HF: Total energy	-62860.078704
FMO2-MP2: Total energy	-63044.255342

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:-8:ASP)

Summations of interaction energy for fragment #1(A:-8:ASP)

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.
42.922	53.283	0.615	-5.42	-5.556	0.025

Interaction energy analysis for fragmet #1(A:-8:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.862 / q_NPA : -0.944

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	ILE	0	-0.005	0.020	2.690	-26.484	-17.851	0.295	-4.712	-4.216	0.028
4	A	-5	HIS	0	-0.017	-0.018	2.934	3.703	5.431	0.320	-0.708	-1.340	-0.003
5	A	-4	HIS	0	0.005	0.012	5.913	-4.010	-4.010	0.000	0.000	0.000	0.000
6	A	-3	HIS	0	-0.028	-0.016	8.597	0.301	0.301	0.000	0.000	0.000	0.000
7	A	-2	HIS	0	0.043	0.026	11.418	-2.129	-2.129	0.000	0.000	0.000	0.000
8	A	-1	HIS	0	-0.001	-0.013	14.216	0.159	0.159	0.000	0.000	0.000	0.000
9	A	0	HIS	0	-0.106	-0.055	17.643	-0.640	-0.640	0.000	0.000	0.000	0.000
10	A	1	MET	0	0.039	0.032	16.744	-0.454	-0.454	0.000	0.000	0.000	0.000
11	A	2	TYR	0	-0.054	-0.051	18.835	0.143	0.143	0.000	0.000	0.000	0.000
12	A	3	ARG	1	0.959	0.984	13.495	-17.317	-17.317	0.000	0.000	0.000	0.000
13	A	4	ILE	0	0.070	0.021	15.606	-0.982	-0.982	0.000	0.000	0.000	0.000
14	A	5	ARG	1	0.755	0.895	15.857	-13.748	-13.748	0.000	0.000	0.000	0.000
15	A	6	VAL	0	0.059	0.031	13.725	-0.186	-0.186	0.000	0.000	0.000	0.000
16	A	7	PHE	0	0.026	0.008	17.060	-0.749	-0.749	0.000	0.000	0.000	0.000
17	A	8	GLY	0	0.011	0.007	18.101	0.653	0.653	0.000	0.000	0.000	0.000
18	A	9	ASP	-1	-0.892	-0.956	18.905	13.774	13.774	0.000	0.000	0.000	0.000
19	A	10	PRO	0	0.021	-0.006	20.645	-0.371	-0.371	0.000	0.000	0.000	0.000
20	A	11	VAL	0	-0.087	-0.035	22.638	-0.636	-0.636	0.000	0.000	0.000	0.000
21	A	12	LEU	0	0.004	0.000	20.416	-0.406	-0.406	0.000	0.000	0.000	0.000
22	A	13	ARG	1	0.788	0.847	24.904	-11.250	-11.250	0.000	0.000	0.000	0.000
23	A	14	LYS	1	0.859	0.948	27.873	-10.673	-10.673	0.000	0.000	0.000	0.000
24	A	15	ARG	1	0.990	0.998	30.033	-8.269	-8.269	0.000	0.000	0.000	0.000
25	A	16	ALA	0	0.010	0.011	30.824	-0.146	-0.146	0.000	0.000	0.000	0.000
26	A	17	LYS	1	0.853	0.911	32.499	-9.106	-9.106	0.000	0.000	0.000	0.000
27	A	18	PRO	0	0.046	0.023	34.761	0.223	0.223	0.000	0.000	0.000	0.000
28	A	19	VAL	0	-0.012	0.008	34.138	0.020	0.020	0.000	0.000	0.000	0.000
29	A	20	THR	0	-0.006	-0.016	36.758	-0.152	-0.152	0.000	0.000	0.000	0.000
30	A	21	LYS	1	0.926	0.970	37.275	-8.277	-8.277	0.000	0.000	0.000	0.000
31	A	22	PHE	0	0.026	0.022	37.417	0.217	0.217	0.000	0.000	0.000	0.000
32	A	23	ASP	-1	-0.850	-0.933	36.042	8.363	8.363	0.000	0.000	0.000	0.000
33	A	24	GLU	-1	-0.783	-0.898	35.177	8.548	8.548	0.000	0.000	0.000	0.000
34	A	25	ASN	0	-0.011	-0.001	30.891	0.480	0.480	0.000	0.000	0.000	0.000
35	A	26	LEU	0	-0.016	0.013	31.542	0.380	0.380	0.000	0.000	0.000	0.000
36	A	27	LYS	1	0.873	0.913	32.033	-8.011	-8.011	0.000	0.000	0.000	0.000
37	A	28	LYS	1	0.857	0.921	28.631	-10.116	-10.116	0.000	0.000	0.000	0.000
38	A	29	THR	0	-0.055	-0.025	27.250	0.581	0.581	0.000	0.000	0.000	0.000
39	A	30	ILE	0	0.022	0.005	27.336	0.372	0.372	0.000	0.000	0.000	0.000
40	A	31	GLU	-1	-0.808	-0.891	28.185	10.464	10.464	0.000	0.000	0.000	0.000
41	A	32	ARG	1	0.930	0.981	22.855	-12.092	-12.092	0.000	0.000	0.000	0.000
42	A	33	MET	0	-0.081	-0.009	23.376	0.751	0.751	0.000	0.000	0.000	0.000
43	A	34	ILE	0	0.026	0.018	24.135	0.384	0.384	0.000	0.000	0.000	0.000
44	A	35	GLU	-1	-0.840	-0.903	21.201	14.183	14.183	0.000	0.000	0.000	0.000
45	A	36	THR	0	-0.022	-0.039	18.642	0.806	0.806	0.000	0.000	0.000	0.000
46	A	37	MET	0	-0.042	0.002	19.788	0.568	0.568	0.000	0.000	0.000	0.000
47	A	38	TYR	0	-0.035	-0.057	20.985	0.286	0.286	0.000	0.000	0.000	0.000
48	A	39	HIS	0	-0.019	0.002	13.801	0.657	0.657	0.000	0.000	0.000	0.000
49	A	40	TYR	0	-0.104	-0.059	12.976	1.568	1.568	0.000	0.000	0.000	0.000
50	A	41	ASP	-1	-0.895	-0.932	17.196	17.235	17.235	0.000	0.000	0.000	0.000
51	A	42	GLY	0	-0.046	-0.015	19.716	-0.348	-0.348	0.000	0.000	0.000	0.000
52	A	43	VAL	0	0.003	-0.007	21.755	-0.344	-0.344	0.000	0.000	0.000	0.000
53	A	44	GLY	0	0.022	-0.011	24.507	-0.661	-0.661	0.000	0.000	0.000	0.000
54	A	45	LEU	0	-0.032	-0.001	21.197	0.707	0.707	0.000	0.000	0.000	0.000
55	A	46	ALA	0	0.082	0.022	24.906	-0.534	-0.534	0.000	0.000	0.000	0.000
56	A	47	ALA	0	-0.028	-0.016	25.026	0.506	0.506	0.000	0.000	0.000	0.000
57	A	48	PRO	0	0.016	0.002	25.056	0.385	0.385	0.000	0.000	0.000	0.000
58	A	49	GLN	0	0.098	0.068	21.359	0.107	0.107	0.000	0.000	0.000	0.000
59	A	50	VAL	0	0.003	0.021	20.344	0.921	0.921	0.000	0.000	0.000	0.000
60	A	51	GLY	0	-0.076	-0.055	21.669	0.034	0.034	0.000	0.000	0.000	0.000
61	A	52	ILE	0	-0.012	0.001	23.194	-0.447	-0.447	0.000	0.000	0.000	0.000
62	A	53	SER	0	0.008	0.001	26.731	-0.091	-0.091	0.000	0.000	0.000	0.000
63	A	54	GLN	0	-0.035	-0.026	29.350	-0.323	-0.323	0.000	0.000	0.000	0.000
64	A	55	ARG	1	0.856	0.910	30.997	-8.439	-8.439	0.000	0.000	0.000	0.000
65	A	56	PHE	0	0.028	0.015	28.342	-0.275	-0.275	0.000	0.000	0.000	0.000
66	A	57	PHE	0	0.040	0.025	28.871	0.344	0.344	0.000	0.000	0.000	0.000
67	A	58	VAL	0	-0.036	-0.006	26.958	-0.396	-0.396	0.000	0.000	0.000	0.000
68	A	59	MET	0	0.022	0.004	28.269	0.240	0.240	0.000	0.000	0.000	0.000
69	A	60	ASP	-1	-0.779	-0.857	27.886	10.275	10.275	0.000	0.000	0.000	0.000
70	A	61	VAL	0	-0.029	-0.020	28.741	0.275	0.275	0.000	0.000	0.000	0.000
71	A	62	GLY	0	0.006	0.002	30.723	-0.200	-0.200	0.000	0.000	0.000	0.000
72	A	63	ASN	0	-0.072	-0.026	31.895	-0.213	-0.213	0.000	0.000	0.000	0.000
73	A	64	GLY	0	0.031	0.025	31.576	-0.219	-0.219	0.000	0.000	0.000	0.000
74	A	65	PRO	0	-0.075	-0.034	29.224	-0.058	-0.058	0.000	0.000	0.000	0.000
75	A	66	VAL	0	0.005	0.006	31.143	-0.305	-0.305	0.000	0.000	0.000	0.000
76	A	67	ALA	0	-0.034	-0.027	32.116	0.302	0.302	0.000	0.000	0.000	0.000
77	A	68	VAL	0	-0.012	0.006	32.918	-0.328	-0.328	0.000	0.000	0.000	0.000
78	A	69	ILE	0	-0.021	-0.022	33.798	0.251	0.251	0.000	0.000	0.000	0.000
79	A	70	ASN	0	-0.051	-0.036	35.911	-0.038	-0.038	0.000	0.000	0.000	0.000
80	A	71	PRO	0	0.029	0.020	34.947	-0.178	-0.178	0.000	0.000	0.000	0.000
81	A	72	GLU	-1	-0.894	-0.923	38.202	7.188	7.188	0.000	0.000	0.000	0.000
82	A	73	ILE	0	-0.011	-0.009	36.898	0.022	0.022	0.000	0.000	0.000	0.000
83	A	74	LEU	0	-0.068	-0.037	41.306	-0.075	-0.075	0.000	0.000	0.000	0.000
84	A	75	GLU	-1	-0.915	-0.953	44.356	6.320	6.320	0.000	0.000	0.000	0.000
85	A	76	ILE	0	-0.043	-0.029	40.654	0.216	0.216	0.000	0.000	0.000	0.000
86	A	77	ASP	-1	-0.786	-0.860	43.736	6.727	6.727	0.000	0.000	0.000	0.000
87	A	78	PRO	0	0.001	0.003	43.948	0.146	0.146	0.000	0.000	0.000	0.000
88	A	79	GLU	-1	-0.841	-0.890	44.214	7.217	7.217	0.000	0.000	0.000	0.000
89	A	80	THR	0	-0.042	-0.052	39.761	0.100	0.100	0.000	0.000	0.000	0.000
90	A	81	GLU	-1	-0.872	-0.932	36.170	8.449	8.449	0.000	0.000	0.000	0.000
91	A	82	VAL	0	-0.002	0.016	33.701	0.151	0.151	0.000	0.000	0.000	0.000
92	A	83	ALA	0	0.001	0.002	31.733	-0.054	-0.054	0.000	0.000	0.000	0.000
93	A	84	GLU	-1	-0.916	-0.947	24.647	12.300	12.300	0.000	0.000	0.000	0.000
94	A	85	GLU	-1	-0.741	-0.840	26.422	10.437	10.437	0.000	0.000	0.000	0.000
95	A	86	GLY	0	0.101	0.053	22.118	0.213	0.213	0.000	0.000	0.000	0.000
96	A	87	OCS	-1	-0.890	-0.947	20.769	12.730	12.730	0.000	0.000	0.000	0.000
97	A	88	LEU	0	0.074	0.046	17.428	0.614	0.614	0.000	0.000	0.000	0.000
98	A	89	SER	0	-0.041	-0.029	16.897	0.817	0.817	0.000	0.000	0.000	0.000
99	A	90	PHE	0	-0.061	-0.046	17.826	0.075	0.075	0.000	0.000	0.000	0.000
100	A	91	PRO	0	-0.005	-0.003	13.131	-0.247	-0.247	0.000	0.000	0.000	0.000
101	A	92	GLU	-1	-0.939	-0.975	13.460	21.779	21.779	0.000	0.000	0.000	0.000
102	A	93	ILE	0	-0.044	-0.003	16.543	-0.610	-0.610	0.000	0.000	0.000	0.000
103	A	94	PHE	0	0.012	0.001	18.611	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	95	VAL	0	-0.026	-0.011	23.139	-0.155	-0.155	0.000	0.000	0.000	0.000
105	A	96	GLU	-1	-0.897	-0.941	26.682	9.902	9.902	0.000	0.000	0.000	0.000
106	A	97	ILE	0	-0.050	-0.027	28.340	-0.120	-0.120	0.000	0.000	0.000	0.000
107	A	98	GLU	-1	-0.858	-0.895	32.184	7.951	7.951	0.000	0.000	0.000	0.000
108	A	99	ARG	1	0.740	0.839	30.015	-9.817	-9.817	0.000	0.000	0.000	0.000
109	A	100	SER	0	0.013	-0.014	36.553	-0.120	-0.120	0.000	0.000	0.000	0.000
110	A	101	LYS	1	0.798	0.877	38.593	-7.394	-7.394	0.000	0.000	0.000	0.000
111	A	102	ARG	1	0.811	0.877	40.502	-7.018	-7.018	0.000	0.000	0.000	0.000
112	A	103	ILE	0	-0.058	-0.016	37.858	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	104	LYS	1	0.914	0.984	42.196	-6.640	-6.640	0.000	0.000	0.000	0.000
114	A	105	VAL	0	-0.038	-0.038	38.788	0.050	0.050	0.000	0.000	0.000	0.000
115	A	106	LYS	1	0.857	0.908	41.651	-7.150	-7.150	0.000	0.000	0.000	0.000
116	A	107	TYR	0	-0.088	-0.072	38.290	0.209	0.209	0.000	0.000	0.000	0.000
117	A	108	GLN	0	0.010	-0.007	39.307	-0.086	-0.086	0.000	0.000	0.000	0.000
118	A	109	ASN	0	0.084	0.028	38.085	0.267	0.267	0.000	0.000	0.000	0.000
119	A	110	THR	0	0.015	-0.023	34.680	-0.119	-0.119	0.000	0.000	0.000	0.000
120	A	111	ARG	1	0.786	0.853	37.574	-7.321	-7.321	0.000	0.000	0.000	0.000
121	A	112	GLY	0	0.000	0.011	40.561	-0.173	-0.173	0.000	0.000	0.000	0.000
122	A	113	GLU	-1	-0.826	-0.854	42.187	7.030	7.030	0.000	0.000	0.000	0.000
123	A	114	TYR	0	-0.008	-0.013	42.657	0.138	0.138	0.000	0.000	0.000	0.000
124	A	115	VAL	0	-0.014	0.008	41.579	-0.124	-0.124	0.000	0.000	0.000	0.000
125	A	116	GLU	-1	-0.872	-0.938	43.450	6.712	6.712	0.000	0.000	0.000	0.000
126	A	117	GLU	-1	-0.870	-0.910	39.408	7.923	7.923	0.000	0.000	0.000	0.000
127	A	118	GLU	-1	-0.862	-0.934	43.053	7.006	7.006	0.000	0.000	0.000	0.000
128	A	119	LEU	0	-0.049	-0.011	37.036	0.136	0.136	0.000	0.000	0.000	0.000
129	A	120	GLU	-1	-0.834	-0.949	39.676	7.189	7.189	0.000	0.000	0.000	0.000
130	A	121	GLY	0	0.022	0.022	37.763	0.187	0.187	0.000	0.000	0.000	0.000
131	A	122	TYR	0	0.039	0.001	27.510	0.102	0.102	0.000	0.000	0.000	0.000
132	A	123	ALA	0	0.043	0.023	33.327	0.220	0.220	0.000	0.000	0.000	0.000
133	A	124	ALA	0	0.039	0.027	34.591	0.136	0.136	0.000	0.000	0.000	0.000
134	A	125	ARG	1	0.778	0.874	31.077	-9.383	-9.383	0.000	0.000	0.000	0.000
135	A	126	VAL	0	0.024	0.004	28.721	0.175	0.175	0.000	0.000	0.000	0.000
136	A	127	PHE	0	0.058	0.023	30.924	0.178	0.178	0.000	0.000	0.000	0.000
137	A	128	GLN	0	-0.055	-0.040	33.252	0.006	0.006	0.000	0.000	0.000	0.000
138	A	129	HIS	1	0.793	0.884	25.136	-11.662	-11.662	0.000	0.000	0.000	0.000
139	A	130	GLU	-1	-0.858	-0.947	26.896	11.946	11.946	0.000	0.000	0.000	0.000
140	A	131	PHE	0	-0.011	-0.021	29.776	-0.056	-0.056	0.000	0.000	0.000	0.000
141	A	132	ASP	-1	-0.803	-0.877	30.630	9.354	9.354	0.000	0.000	0.000	0.000
142	A	133	HIS	0	0.083	0.038	23.739	-0.220	-0.220	0.000	0.000	0.000	0.000
143	A	134	LEU	0	-0.090	-0.022	28.923	-0.020	-0.020	0.000	0.000	0.000	0.000
144	A	135	ASN	0	-0.117	-0.068	31.602	-0.422	-0.422	0.000	0.000	0.000	0.000
145	A	136	GLY	0	-0.022	0.009	29.080	-0.179	-0.179	0.000	0.000	0.000	0.000
146	A	137	VAL	0	-0.041	-0.013	29.599	0.059	0.059	0.000	0.000	0.000	0.000
147	A	138	LEU	0	0.011	-0.007	23.815	0.307	0.307	0.000	0.000	0.000	0.000
148	A	139	ILE	0	0.070	0.024	22.770	-0.370	-0.370	0.000	0.000	0.000	0.000
149	A	140	ILE	0	-0.004	0.006	23.906	-0.260	-0.260	0.000	0.000	0.000	0.000
150	A	141	ASP	-1	-0.814	-0.848	26.991	10.361	10.361	0.000	0.000	0.000	0.000
151	A	142	ARG	1	0.763	0.839	29.891	-9.574	-9.574	0.000	0.000	0.000	0.000
152	A	143	ILE	0	0.007	0.023	27.199	-0.038	-0.038	0.000	0.000	0.000	0.000
153	A	144	SER	0	0.034	0.020	31.045	-0.366	-0.366	0.000	0.000	0.000	0.000
154	A	145	PRO	0	-0.058	-0.020	33.670	0.103	0.103	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-8:ASP)