FMO DATABASE

FMODB ID: 987Q2

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	OptH
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	-1589060.77401
FMO2-HF: Nuclear repulsion	1526201.417362
FMO2-HF: Total energy	-62859.356648
FMO2-MP2: Total energy	-63043.545905

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.
49.682	59.545	0.432	-5.11	-5.187	0.02

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 : -0.872 / q_NPA : -0.954

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	0.002	0.025	2.828	-24.171	-15.901	0.152	-4.497	-3.926	0.022
4	A	-5	HIS	0	-0.006	-0.006	2.922	6.025	7.618	0.280	-0.613	-1.261	-0.002
5	A	-4	HIS	0	0.004	0.005	5.787	-4.020	-4.020	0.000	0.000	0.000	0.000
6	A	-3	HIS	0	-0.030	-0.016	8.787	0.619	0.619	0.000	0.000	0.000	0.000
7	A	-2	HIS	0	0.047	0.034	11.255	-2.124	-2.124	0.000	0.000	0.000	0.000
8	A	-1	HIS	0	0.003	-0.013	14.168	0.132	0.132	0.000	0.000	0.000	0.000
9	A	0	HIS	0	-0.109	-0.055	17.588	-0.639	-0.639	0.000	0.000	0.000	0.000
10	A	1	MET	0	0.029	0.018	17.061	-0.435	-0.435	0.000	0.000	0.000	0.000
11	A	2	TYR	0	-0.050	-0.045	18.827	0.053	0.053	0.000	0.000	0.000	0.000
12	A	3	ARG	1	0.949	0.980	13.609	-17.453	-17.453	0.000	0.000	0.000	0.000
13	A	4	ILE	0	0.073	0.022	15.673	-1.013	-1.013	0.000	0.000	0.000	0.000
14	A	5	ARG	1	0.776	0.896	15.797	-13.992	-13.992	0.000	0.000	0.000	0.000
15	A	6	VAL	0	0.061	0.033	13.508	-0.191	-0.191	0.000	0.000	0.000	0.000
16	A	7	PHE	0	0.028	0.010	16.901	-0.801	-0.801	0.000	0.000	0.000	0.000
17	A	8	GLY	0	0.013	0.005	17.960	0.674	0.674	0.000	0.000	0.000	0.000
18	A	9	ASP	-1	-0.893	-0.952	18.735	13.825	13.825	0.000	0.000	0.000	0.000
19	A	10	PRO	0	0.009	-0.009	20.432	-0.382	-0.382	0.000	0.000	0.000	0.000
20	A	11	VAL	0	-0.076	-0.031	22.393	-0.637	-0.637	0.000	0.000	0.000	0.000
21	A	12	LEU	0	-0.002	-0.004	20.380	-0.400	-0.400	0.000	0.000	0.000	0.000
22	A	13	ARG	1	0.799	0.868	24.722	-11.458	-11.458	0.000	0.000	0.000	0.000
23	A	14	LYS	1	0.885	0.963	27.696	-10.613	-10.613	0.000	0.000	0.000	0.000
24	A	15	ARG	1	0.976	0.995	29.826	-8.358	-8.358	0.000	0.000	0.000	0.000
25	A	16	ALA	0	-0.006	0.007	30.686	-0.141	-0.141	0.000	0.000	0.000	0.000
26	A	17	LYS	1	0.894	0.935	32.384	-9.093	-9.093	0.000	0.000	0.000	0.000
27	A	18	PRO	0	0.033	0.019	34.827	0.230	0.230	0.000	0.000	0.000	0.000
28	A	19	VAL	0	-0.001	0.017	34.204	0.022	0.022	0.000	0.000	0.000	0.000
29	A	20	THR	0	-0.016	-0.022	36.809	-0.155	-0.155	0.000	0.000	0.000	0.000
30	A	21	LYS	1	0.922	0.966	37.320	-8.289	-8.289	0.000	0.000	0.000	0.000
31	A	22	PHE	0	0.024	0.028	37.441	0.214	0.214	0.000	0.000	0.000	0.000
32	A	23	ASP	-1	-0.849	-0.935	36.090	8.361	8.361	0.000	0.000	0.000	0.000
33	A	24	GLU	-1	-0.903	-0.970	34.720	8.857	8.857	0.000	0.000	0.000	0.000
34	A	25	ASN	0	-0.003	0.003	31.037	0.461	0.461	0.000	0.000	0.000	0.000
35	A	26	LEU	0	-0.012	0.019	31.545	0.372	0.372	0.000	0.000	0.000	0.000
36	A	27	LYS	1	0.979	0.979	32.050	-8.028	-8.028	0.000	0.000	0.000	0.000
37	A	28	LYS	1	0.939	0.977	28.358	-10.193	-10.193	0.000	0.000	0.000	0.000
38	A	29	THR	0	-0.049	-0.032	27.151	0.489	0.489	0.000	0.000	0.000	0.000
39	A	30	ILE	0	0.008	-0.003	27.359	0.373	0.373	0.000	0.000	0.000	0.000
40	A	31	GLU	-1	-0.867	-0.936	28.213	10.440	10.440	0.000	0.000	0.000	0.000
41	A	32	ARG	1	0.908	0.965	22.478	-12.257	-12.257	0.000	0.000	0.000	0.000
42	A	33	MET	0	-0.079	-0.015	23.397	0.759	0.759	0.000	0.000	0.000	0.000
43	A	34	ILE	0	0.021	0.021	24.181	0.399	0.399	0.000	0.000	0.000	0.000
44	A	35	GLU	-1	-0.814	-0.884	21.155	14.398	14.398	0.000	0.000	0.000	0.000
45	A	36	THR	0	-0.018	-0.029	18.683	0.839	0.839	0.000	0.000	0.000	0.000
46	A	37	MET	0	-0.040	0.004	19.866	0.604	0.604	0.000	0.000	0.000	0.000
47	A	38	TYR	0	-0.034	-0.067	21.047	0.268	0.268	0.000	0.000	0.000	0.000
48	A	39	HIS	0	-0.033	-0.002	14.070	0.447	0.447	0.000	0.000	0.000	0.000
49	A	40	TYR	0	-0.090	-0.051	13.135	1.629	1.629	0.000	0.000	0.000	0.000
50	A	41	ASP	-1	-0.888	-0.932	17.029	17.809	17.809	0.000	0.000	0.000	0.000
51	A	42	GLY	0	-0.052	-0.017	19.780	-0.348	-0.348	0.000	0.000	0.000	0.000
52	A	43	VAL	0	0.005	-0.007	21.749	-0.370	-0.370	0.000	0.000	0.000	0.000
53	A	44	GLY	0	0.019	-0.014	24.465	-0.675	-0.675	0.000	0.000	0.000	0.000
54	A	45	LEU	0	-0.023	0.005	21.284	0.725	0.725	0.000	0.000	0.000	0.000
55	A	46	ALA	0	0.078	0.022	24.857	-0.541	-0.541	0.000	0.000	0.000	0.000
56	A	47	ALA	0	-0.039	-0.018	25.051	0.517	0.517	0.000	0.000	0.000	0.000
57	A	48	PRO	0	0.018	0.001	25.125	0.399	0.399	0.000	0.000	0.000	0.000
58	A	49	GLN	0	0.096	0.056	21.352	0.028	0.028	0.000	0.000	0.000	0.000
59	A	50	VAL	0	-0.003	0.019	20.356	0.945	0.945	0.000	0.000	0.000	0.000
60	A	51	GLY	0	-0.091	-0.055	21.731	0.011	0.011	0.000	0.000	0.000	0.000
61	A	52	ILE	0	-0.013	0.003	23.255	-0.444	-0.444	0.000	0.000	0.000	0.000
62	A	53	SER	0	0.014	0.002	26.786	-0.078	-0.078	0.000	0.000	0.000	0.000
63	A	54	GLN	0	-0.042	-0.034	29.364	-0.258	-0.258	0.000	0.000	0.000	0.000
64	A	55	ARG	1	0.841	0.880	31.043	-8.530	-8.530	0.000	0.000	0.000	0.000
65	A	56	PHE	0	0.039	0.013	28.384	-0.303	-0.303	0.000	0.000	0.000	0.000
66	A	57	PHE	0	0.036	0.024	28.900	0.344	0.344	0.000	0.000	0.000	0.000
67	A	58	VAL	0	-0.032	-0.001	26.957	-0.410	-0.410	0.000	0.000	0.000	0.000
68	A	59	MET	0	0.016	-0.001	28.266	0.259	0.259	0.000	0.000	0.000	0.000
69	A	60	ASP	-1	-0.780	-0.847	27.912	10.354	10.354	0.000	0.000	0.000	0.000
70	A	61	VAL	0	-0.038	-0.019	28.761	0.286	0.286	0.000	0.000	0.000	0.000
71	A	62	GLY	0	0.009	-0.002	30.762	-0.202	-0.202	0.000	0.000	0.000	0.000
72	A	63	ASN	0	-0.067	-0.024	31.958	-0.197	-0.197	0.000	0.000	0.000	0.000
73	A	64	GLY	0	0.026	0.023	31.696	-0.225	-0.225	0.000	0.000	0.000	0.000
74	A	65	PRO	0	-0.089	-0.038	29.378	-0.073	-0.073	0.000	0.000	0.000	0.000
75	A	66	VAL	0	0.020	0.012	31.229	-0.313	-0.313	0.000	0.000	0.000	0.000
76	A	67	ALA	0	-0.034	-0.028	32.138	0.303	0.303	0.000	0.000	0.000	0.000
77	A	68	VAL	0	-0.010	0.009	32.984	-0.339	-0.339	0.000	0.000	0.000	0.000
78	A	69	ILE	0	-0.022	-0.023	33.869	0.254	0.254	0.000	0.000	0.000	0.000
79	A	70	ASN	0	-0.058	-0.043	35.982	-0.033	-0.033	0.000	0.000	0.000	0.000
80	A	71	PRO	0	0.010	0.008	34.940	-0.175	-0.175	0.000	0.000	0.000	0.000
81	A	72	GLU	-1	-0.973	-0.988	38.165	7.244	7.244	0.000	0.000	0.000	0.000
82	A	73	ILE	0	-0.013	-0.010	36.916	0.024	0.024	0.000	0.000	0.000	0.000
83	A	74	LEU	0	-0.068	-0.038	41.198	-0.085	-0.085	0.000	0.000	0.000	0.000
84	A	75	GLU	-1	-0.913	-0.960	44.209	6.369	6.369	0.000	0.000	0.000	0.000
85	A	76	ILE	0	-0.040	-0.023	40.844	0.214	0.214	0.000	0.000	0.000	0.000
86	A	77	ASP	-1	-0.823	-0.893	43.596	6.765	6.765	0.000	0.000	0.000	0.000
87	A	78	PRO	0	-0.008	-0.010	43.753	0.149	0.149	0.000	0.000	0.000	0.000
88	A	79	GLU	-1	-0.896	-0.938	43.421	7.137	7.137	0.000	0.000	0.000	0.000
89	A	80	THR	0	-0.065	-0.046	39.431	0.116	0.116	0.000	0.000	0.000	0.000
90	A	81	GLU	-1	-0.931	-0.984	36.823	8.241	8.241	0.000	0.000	0.000	0.000
91	A	82	VAL	0	-0.012	0.015	33.528	0.165	0.165	0.000	0.000	0.000	0.000
92	A	83	ALA	0	-0.013	-0.006	31.565	-0.059	-0.059	0.000	0.000	0.000	0.000
93	A	84	GLU	-1	-0.900	-0.939	24.392	12.455	12.455	0.000	0.000	0.000	0.000
94	A	85	GLU	-1	-0.740	-0.824	26.244	10.622	10.622	0.000	0.000	0.000	0.000
95	A	86	GLY	0	0.091	0.050	21.927	0.222	0.222	0.000	0.000	0.000	0.000
96	A	87	OCS	-1	-0.881	-0.940	20.567	13.201	13.201	0.000	0.000	0.000	0.000
97	A	88	LEU	0	0.081	0.045	17.240	0.657	0.657	0.000	0.000	0.000	0.000
98	A	89	SER	0	-0.061	-0.036	16.812	0.833	0.833	0.000	0.000	0.000	0.000
99	A	90	PHE	0	-0.060	-0.040	17.796	0.061	0.061	0.000	0.000	0.000	0.000
100	A	91	PRO	0	-0.014	-0.009	13.021	-0.283	-0.283	0.000	0.000	0.000	0.000
101	A	92	GLU	-1	-0.920	-0.968	12.829	23.073	23.073	0.000	0.000	0.000	0.000
102	A	93	ILE	0	-0.042	0.002	16.263	-0.615	-0.615	0.000	0.000	0.000	0.000
103	A	94	PHE	0	-0.001	-0.006	18.428	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	95	VAL	0	-0.031	-0.011	22.868	-0.162	-0.162	0.000	0.000	0.000	0.000
105	A	96	GLU	-1	-0.897	-0.943	26.390	10.142	10.142	0.000	0.000	0.000	0.000
106	A	97	ILE	0	-0.033	-0.018	28.387	-0.137	-0.137	0.000	0.000	0.000	0.000
107	A	98	GLU	-1	-0.867	-0.922	31.924	8.051	8.051	0.000	0.000	0.000	0.000
108	A	99	ARG	1	0.727	0.821	29.743	-9.931	-9.931	0.000	0.000	0.000	0.000
109	A	100	SER	0	0.016	0.008	36.344	-0.107	-0.107	0.000	0.000	0.000	0.000
110	A	101	LYS	1	0.889	0.941	38.430	-7.520	-7.520	0.000	0.000	0.000	0.000
111	A	102	ARG	1	0.842	0.909	40.379	-7.056	-7.056	0.000	0.000	0.000	0.000
112	A	103	ILE	0	-0.027	0.006	37.833	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	104	LYS	1	0.963	1.021	42.069	-6.725	-6.725	0.000	0.000	0.000	0.000
114	A	105	VAL	0	-0.020	-0.025	38.674	0.046	0.046	0.000	0.000	0.000	0.000
115	A	106	LYS	1	0.987	0.988	41.571	-7.017	-7.017	0.000	0.000	0.000	0.000
116	A	107	TYR	0	-0.077	-0.040	38.381	0.207	0.207	0.000	0.000	0.000	0.000
117	A	108	GLN	0	0.015	0.005	39.374	-0.090	-0.090	0.000	0.000	0.000	0.000
118	A	109	ASN	0	0.072	0.040	38.143	0.278	0.278	0.000	0.000	0.000	0.000
119	A	110	THR	0	0.027	-0.022	34.692	-0.150	-0.150	0.000	0.000	0.000	0.000
120	A	111	ARG	1	0.854	0.921	37.605	-7.367	-7.367	0.000	0.000	0.000	0.000
121	A	112	GLY	0	0.004	0.011	40.604	-0.171	-0.171	0.000	0.000	0.000	0.000
122	A	113	GLU	-1	-0.890	-0.939	42.226	6.974	6.974	0.000	0.000	0.000	0.000
123	A	114	TYR	0	-0.014	-0.018	42.709	0.150	0.150	0.000	0.000	0.000	0.000
124	A	115	VAL	0	-0.014	0.013	41.561	-0.126	-0.126	0.000	0.000	0.000	0.000
125	A	116	GLU	-1	-0.928	-0.986	43.456	6.758	6.758	0.000	0.000	0.000	0.000
126	A	117	GLU	-1	-0.897	-0.949	39.495	7.943	7.943	0.000	0.000	0.000	0.000
127	A	118	GLU	-1	-0.868	-0.929	42.989	7.087	7.087	0.000	0.000	0.000	0.000
128	A	119	LEU	0	-0.043	-0.012	36.859	0.141	0.141	0.000	0.000	0.000	0.000
129	A	120	GLU	-1	-0.857	-0.957	39.622	7.213	7.213	0.000	0.000	0.000	0.000
130	A	121	GLY	0	0.001	0.006	37.668	0.189	0.189	0.000	0.000	0.000	0.000
131	A	122	TYR	0	0.034	-0.001	27.397	0.103	0.103	0.000	0.000	0.000	0.000
132	A	123	ALA	0	0.052	0.024	33.239	0.225	0.225	0.000	0.000	0.000	0.000
133	A	124	ALA	0	0.048	0.031	34.511	0.142	0.142	0.000	0.000	0.000	0.000
134	A	125	ARG	1	0.828	0.911	30.751	-9.601	-9.601	0.000	0.000	0.000	0.000
135	A	126	VAL	0	0.015	0.003	28.808	0.179	0.179	0.000	0.000	0.000	0.000
136	A	127	PHE	0	0.053	0.023	30.809	0.184	0.184	0.000	0.000	0.000	0.000
137	A	128	GLN	0	-0.055	-0.046	33.123	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	129	HIS	1	0.810	0.897	24.948	-11.892	-11.892	0.000	0.000	0.000	0.000
139	A	130	GLU	-1	-0.855	-0.945	26.699	12.092	12.092	0.000	0.000	0.000	0.000
140	A	131	PHE	0	-0.028	-0.025	29.668	-0.054	-0.054	0.000	0.000	0.000	0.000
141	A	132	ASP	-1	-0.803	-0.889	30.585	9.480	9.480	0.000	0.000	0.000	0.000
142	A	133	HIS	0	0.067	0.037	23.971	-0.296	-0.296	0.000	0.000	0.000	0.000
143	A	134	LEU	0	-0.093	-0.017	28.786	-0.021	-0.021	0.000	0.000	0.000	0.000
144	A	135	ASN	0	-0.109	-0.059	31.438	-0.393	-0.393	0.000	0.000	0.000	0.000
145	A	136	GLY	0	-0.026	0.004	28.919	-0.180	-0.180	0.000	0.000	0.000	0.000
146	A	137	VAL	0	-0.038	-0.012	29.459	0.053	0.053	0.000	0.000	0.000	0.000
147	A	138	LEU	0	0.004	-0.009	23.828	0.309	0.309	0.000	0.000	0.000	0.000
148	A	139	ILE	0	0.069	0.019	22.880	-0.361	-0.361	0.000	0.000	0.000	0.000
149	A	140	ILE	0	-0.004	0.008	23.993	-0.267	-0.267	0.000	0.000	0.000	0.000
150	A	141	ASP	-1	-0.818	-0.865	26.955	10.525	10.525	0.000	0.000	0.000	0.000
151	A	142	ARG	1	0.788	0.861	29.854	-9.679	-9.679	0.000	0.000	0.000	0.000
152	A	143	ILE	0	0.005	0.023	27.311	-0.041	-0.041	0.000	0.000	0.000	0.000
153	A	144	SER	0	0.030	0.015	30.937	-0.382	-0.382	0.000	0.000	0.000	0.000
154	A	145	PRO	0	-0.057	-0.017	33.386	0.105	0.105	0.000	0.000	0.000	0.000

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