FMO DATABASE

FMODB ID: G74K1

Calculation Name: 1SMB-A-Xray547

Preferred Name:

Target Type:

Ligand Name: cysteinesulfonic acid

Ligand 3-letter code: OCS

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1SMB

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H4G4

Base Structure: X-ray

Registration Date: 2025-10-06

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1426711.288339
FMO2-HF: Nuclear repulsion	1368334.560066
FMO2-HF: Total energy	-58376.728274
FMO2-MP2: Total energy	-58547.816484

3D Structure Molmil

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:SER)

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

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.
119.588	124.797	1.078	-2.334	-3.954	0.012

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.882 / q_NPA : 0.923

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	SER	0	0.088	0.043	3.416	2.198	3.697	-0.001	-0.612	-0.886	-0.002
4	A	7	LYS	1	0.949	0.978	2.687	56.705	59.971	1.080	-1.608	-2.738	0.014
5	A	8	GLN	0	0.016	0.017	3.951	-1.239	-0.795	-0.001	-0.114	-0.330	0.000
6	A	9	PHE	0	0.027	0.013	5.635	5.242	5.242	0.000	0.000	0.000	0.000
7	A	10	HIS	0	-0.014	-0.023	7.838	1.419	1.419	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.001	-0.006	7.638	3.813	3.813	0.000	0.000	0.000	0.000
9	A	12	GLU	-1	-0.852	-0.932	9.670	-22.196	-22.196	0.000	0.000	0.000	0.000
10	A	13	VAL	0	0.028	0.031	11.710	2.056	2.056	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.044	-0.017	12.903	1.622	1.622	0.000	0.000	0.000	0.000
12	A	15	LYS	1	0.856	0.939	13.372	22.798	22.798	0.000	0.000	0.000	0.000
13	A	16	ALA	0	0.057	0.035	15.453	1.170	1.170	0.000	0.000	0.000	0.000
14	A	17	HIS	0	0.016	0.006	17.190	1.720	1.720	0.000	0.000	0.000	0.000
15	A	18	ASN	0	-0.009	-0.010	17.706	1.455	1.455	0.000	0.000	0.000	0.000
16	A	19	GLU	-1	-0.910	-0.954	18.323	-16.178	-16.178	0.000	0.000	0.000	0.000
17	A	20	TYR	0	-0.079	-0.078	21.048	0.988	0.988	0.000	0.000	0.000	0.000
18	A	21	ARG	1	0.780	0.879	22.298	13.268	13.268	0.000	0.000	0.000	0.000
19	A	22	GLN	0	-0.020	-0.010	23.881	0.127	0.127	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.883	0.939	24.454	13.102	13.102	0.000	0.000	0.000	0.000
21	A	24	HIS	0	0.067	0.047	27.807	0.024	0.024	0.000	0.000	0.000	0.000
22	A	25	GLY	0	0.030	0.023	29.280	0.260	0.260	0.000	0.000	0.000	0.000
23	A	26	VAL	0	-0.042	-0.004	26.391	0.199	0.199	0.000	0.000	0.000	0.000
24	A	27	PRO	0	-0.018	-0.015	26.431	-0.363	-0.363	0.000	0.000	0.000	0.000
25	A	28	PRO	0	-0.001	0.016	20.792	-0.183	-0.183	0.000	0.000	0.000	0.000
26	A	29	LEU	0	0.022	0.016	19.454	0.104	0.104	0.000	0.000	0.000	0.000
27	A	30	LYS	1	0.932	0.963	17.622	14.361	14.361	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.000	0.006	11.272	0.055	0.055	0.000	0.000	0.000	0.000
29	A	32	CYS	-1	-0.826	-0.877	15.260	-15.680	-15.680	0.000	0.000	0.000	0.000
30	A	33	LYS	1	0.924	0.949	8.693	26.271	26.271	0.000	0.000	0.000	0.000
31	A	34	ASN	0	0.012	0.026	13.109	-1.045	-1.045	0.000	0.000	0.000	0.000
32	A	35	LEU	0	0.093	0.058	15.530	-0.342	-0.342	0.000	0.000	0.000	0.000
33	A	36	ASN	0	0.000	-0.015	9.635	1.199	1.199	0.000	0.000	0.000	0.000
34	A	37	ARG	1	0.873	0.945	11.698	18.046	18.046	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.838	-0.924	13.124	-14.782	-14.782	0.000	0.000	0.000	0.000
36	A	39	ALA	0	-0.007	0.000	14.227	0.509	0.509	0.000	0.000	0.000	0.000
37	A	40	GLN	0	-0.072	-0.047	9.990	-0.823	-0.823	0.000	0.000	0.000	0.000
38	A	41	GLN	0	0.038	0.031	12.899	0.307	0.307	0.000	0.000	0.000	0.000
39	A	42	TYR	0	-0.018	-0.036	15.651	0.789	0.789	0.000	0.000	0.000	0.000
40	A	43	SER	0	-0.043	-0.040	13.824	0.122	0.122	0.000	0.000	0.000	0.000
41	A	44	GLU	-1	-0.821	-0.910	11.943	-21.808	-21.808	0.000	0.000	0.000	0.000
42	A	45	ALA	0	-0.006	0.014	16.097	0.730	0.730	0.000	0.000	0.000	0.000
43	A	46	LEU	0	-0.038	-0.010	19.074	0.637	0.637	0.000	0.000	0.000	0.000
44	A	47	ALA	0	-0.007	-0.002	16.599	0.486	0.486	0.000	0.000	0.000	0.000
45	A	48	SER	0	-0.064	-0.044	18.558	0.624	0.624	0.000	0.000	0.000	0.000
46	A	49	THR	0	-0.042	-0.034	20.394	0.626	0.626	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.886	0.932	21.389	13.025	13.025	0.000	0.000	0.000	0.000
48	A	51	ILE	0	-0.027	-0.004	23.099	0.360	0.360	0.000	0.000	0.000	0.000
49	A	52	LEU	0	0.001	0.001	21.978	-0.297	-0.297	0.000	0.000	0.000	0.000
50	A	53	LYS	1	0.983	0.988	24.679	11.338	11.338	0.000	0.000	0.000	0.000
51	A	54	HIS	1	0.875	0.931	24.692	11.559	11.559	0.000	0.000	0.000	0.000
52	A	55	SER	0	-0.022	-0.020	22.823	0.462	0.462	0.000	0.000	0.000	0.000
53	A	56	PRO	0	0.008	-0.002	24.603	0.380	0.380	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.787	-0.897	22.881	-12.416	-12.416	0.000	0.000	0.000	0.000
55	A	58	SER	0	-0.043	-0.006	24.894	0.256	0.256	0.000	0.000	0.000	0.000
56	A	59	SER	0	-0.067	-0.046	26.626	0.417	0.417	0.000	0.000	0.000	0.000
57	A	60	ARG	1	0.936	0.969	28.865	10.439	10.439	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.035	0.028	29.550	0.176	0.176	0.000	0.000	0.000	0.000
59	A	62	GLN	0	-0.012	-0.008	26.562	-0.092	-0.092	0.000	0.000	0.000	0.000
60	A	63	CYS	0	-0.070	-0.040	22.833	-0.560	-0.560	0.000	0.000	0.000	0.000
61	A	64	GLY	0	0.037	0.036	24.705	0.364	0.364	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.742	-0.852	21.221	-13.982	-13.982	0.000	0.000	0.000	0.000
63	A	66	ASN	0	0.006	0.024	21.162	1.028	1.028	0.000	0.000	0.000	0.000
64	A	67	LEU	0	0.004	-0.005	20.454	-0.705	-0.705	0.000	0.000	0.000	0.000
65	A	68	ALA	0	-0.005	0.007	18.774	0.461	0.461	0.000	0.000	0.000	0.000
66	A	69	TRP	0	0.002	0.001	19.021	-0.405	-0.405	0.000	0.000	0.000	0.000
67	A	70	ALA	0	0.017	0.010	18.838	0.372	0.372	0.000	0.000	0.000	0.000
68	A	71	SER	0	0.006	0.003	19.581	-0.540	-0.540	0.000	0.000	0.000	0.000
69	A	72	TYR	0	-0.009	-0.012	16.633	0.356	0.356	0.000	0.000	0.000	0.000
70	A	73	ASP	-1	-0.799	-0.881	10.835	-27.381	-27.381	0.000	0.000	0.000	0.000
71	A	74	GLN	0	-0.008	0.019	14.160	0.420	0.420	0.000	0.000	0.000	0.000
72	A	75	THR	0	-0.021	-0.037	12.250	-2.525	-2.525	0.000	0.000	0.000	0.000
73	A	76	GLY	0	0.010	-0.022	11.874	0.748	0.748	0.000	0.000	0.000	0.000
74	A	77	LYS	1	0.901	0.938	13.058	17.480	17.480	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.711	-0.816	15.818	-17.350	-17.350	0.000	0.000	0.000	0.000
76	A	79	VAL	0	-0.005	0.003	16.357	0.948	0.948	0.000	0.000	0.000	0.000
77	A	80	ALA	0	0.013	0.012	17.885	0.817	0.817	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.772	-0.870	19.589	-14.847	-14.847	0.000	0.000	0.000	0.000
79	A	82	ARG	1	0.822	0.911	19.461	16.148	16.148	0.000	0.000	0.000	0.000
80	A	83	TRP	0	-0.007	-0.021	18.137	0.208	0.208	0.000	0.000	0.000	0.000
81	A	84	TYR	0	0.047	-0.009	23.638	0.485	0.485	0.000	0.000	0.000	0.000
82	A	85	SER	0	-0.067	-0.043	25.447	0.660	0.660	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.774	-0.880	27.736	-10.916	-10.916	0.000	0.000	0.000	0.000
84	A	87	ILE	0	0.008	0.016	29.593	0.460	0.460	0.000	0.000	0.000	0.000
85	A	88	LYS	1	0.907	0.962	31.464	9.354	9.354	0.000	0.000	0.000	0.000
86	A	89	ASN	0	-0.067	-0.041	33.805	0.486	0.486	0.000	0.000	0.000	0.000
87	A	90	TYR	0	0.031	0.012	33.696	0.150	0.150	0.000	0.000	0.000	0.000
88	A	91	ASN	0	-0.010	-0.011	35.720	-0.036	-0.036	0.000	0.000	0.000	0.000
89	A	92	PHE	0	0.045	0.004	32.942	0.065	0.065	0.000	0.000	0.000	0.000
90	A	93	GLN	0	-0.021	-0.001	38.846	-0.048	-0.048	0.000	0.000	0.000	0.000
91	A	94	GLN	0	-0.045	-0.011	41.440	0.166	0.166	0.000	0.000	0.000	0.000
92	A	95	PRO	0	0.017	0.027	38.798	-0.156	-0.156	0.000	0.000	0.000	0.000
93	A	96	GLY	0	0.045	0.006	37.834	0.193	0.193	0.000	0.000	0.000	0.000
94	A	97	PHE	0	-0.032	-0.013	31.782	-0.252	-0.252	0.000	0.000	0.000	0.000
95	A	98	THR	0	0.059	0.028	34.986	0.149	0.149	0.000	0.000	0.000	0.000
96	A	99	SER	0	0.019	-0.008	33.133	-0.248	-0.248	0.000	0.000	0.000	0.000
97	A	100	GLY	0	-0.026	-0.002	31.875	-0.301	-0.301	0.000	0.000	0.000	0.000
98	A	101	THR	0	-0.038	-0.021	31.392	-0.061	-0.061	0.000	0.000	0.000	0.000
99	A	102	GLY	0	0.038	0.038	30.080	-0.166	-0.166	0.000	0.000	0.000	0.000
100	A	103	HIS	0	-0.090	-0.062	24.767	-0.505	-0.505	0.000	0.000	0.000	0.000
101	A	104	PHE	0	0.032	0.014	25.662	-0.439	-0.439	0.000	0.000	0.000	0.000
102	A	105	THR	0	-0.012	-0.033	27.285	-0.153	-0.153	0.000	0.000	0.000	0.000
103	A	106	ALA	0	-0.037	-0.008	25.233	0.028	0.028	0.000	0.000	0.000	0.000
104	A	107	MET	0	-0.096	-0.034	20.833	-0.314	-0.314	0.000	0.000	0.000	0.000
105	A	108	VAL	0	0.004	-0.002	24.255	-0.332	-0.332	0.000	0.000	0.000	0.000
106	A	109	TRP	0	0.047	0.055	26.889	0.243	0.243	0.000	0.000	0.000	0.000
107	A	110	LYS	1	0.981	1.004	27.540	8.886	8.886	0.000	0.000	0.000	0.000
108	A	111	ASN	0	-0.031	-0.025	28.782	-0.265	-0.265	0.000	0.000	0.000	0.000
109	A	112	THR	0	-0.042	-0.016	23.457	-0.022	-0.022	0.000	0.000	0.000	0.000
110	A	113	LYS	1	0.899	0.952	24.085	10.761	10.761	0.000	0.000	0.000	0.000
111	A	114	LYS	1	0.812	0.858	18.717	14.620	14.620	0.000	0.000	0.000	0.000
112	A	115	MET	0	0.025	0.028	15.551	0.564	0.564	0.000	0.000	0.000	0.000
113	A	116	GLY	0	-0.021	-0.013	14.806	-0.628	-0.628	0.000	0.000	0.000	0.000
114	A	117	VAL	0	0.007	-0.014	11.856	0.494	0.494	0.000	0.000	0.000	0.000
115	A	118	GLY	0	-0.012	-0.007	11.256	-1.563	-1.563	0.000	0.000	0.000	0.000
116	A	119	LYS	1	0.780	0.867	9.645	29.724	29.724	0.000	0.000	0.000	0.000
117	A	120	ALA	0	0.027	0.037	10.607	-2.032	-2.032	0.000	0.000	0.000	0.000
118	A	121	SER	0	0.027	0.001	12.509	1.067	1.067	0.000	0.000	0.000	0.000
119	A	122	ALA	0	0.005	0.016	14.421	-0.065	-0.065	0.000	0.000	0.000	0.000
120	A	123	SER	0	-0.021	-0.028	17.443	-0.623	-0.623	0.000	0.000	0.000	0.000
121	A	124	ASP	-1	-0.812	-0.863	19.387	-13.947	-13.947	0.000	0.000	0.000	0.000
122	A	125	GLY	0	-0.006	0.004	16.806	0.192	0.192	0.000	0.000	0.000	0.000
123	A	126	SER	0	-0.071	-0.044	17.154	-0.579	-0.579	0.000	0.000	0.000	0.000
124	A	127	SER	0	-0.009	-0.018	14.356	-0.614	-0.614	0.000	0.000	0.000	0.000
125	A	128	PHE	0	0.002	-0.001	15.691	1.016	1.016	0.000	0.000	0.000	0.000
126	A	129	VAL	0	-0.021	-0.016	14.039	-1.485	-1.485	0.000	0.000	0.000	0.000
127	A	130	VAL	0	-0.002	0.001	15.582	1.353	1.353	0.000	0.000	0.000	0.000
128	A	131	ALA	0	-0.007	0.003	15.657	-1.418	-1.418	0.000	0.000	0.000	0.000
129	A	132	ARG	1	0.810	0.897	17.606	15.132	15.132	0.000	0.000	0.000	0.000
130	A	133	TYR	0	0.001	-0.023	19.122	-0.597	-0.597	0.000	0.000	0.000	0.000
131	A	134	PHE	0	0.042	0.024	21.864	0.506	0.506	0.000	0.000	0.000	0.000
132	A	135	PRO	0	0.025	-0.001	23.709	-0.324	-0.324	0.000	0.000	0.000	0.000
133	A	136	ALA	0	-0.001	0.010	26.309	-0.299	-0.299	0.000	0.000	0.000	0.000
134	A	137	GLY	0	0.057	0.022	27.065	0.252	0.252	0.000	0.000	0.000	0.000
135	A	138	ASN	0	-0.068	-0.028	28.734	0.152	0.152	0.000	0.000	0.000	0.000
136	A	139	VAL	0	0.008	0.010	31.618	0.206	0.206	0.000	0.000	0.000	0.000
137	A	140	VAL	0	0.016	-0.011	34.295	0.104	0.104	0.000	0.000	0.000	0.000
138	A	141	ASN	0	-0.030	0.004	37.266	0.204	0.204	0.000	0.000	0.000	0.000
139	A	142	GLU	-1	-0.886	-0.950	39.689	-7.090	-7.090	0.000	0.000	0.000	0.000
140	A	143	GLY	0	0.045	0.031	41.243	-0.035	-0.035	0.000	0.000	0.000	0.000
141	A	144	PHE	0	-0.012	-0.011	35.500	-0.201	-0.201	0.000	0.000	0.000	0.000
142	A	145	PHE	0	0.046	0.001	33.476	-0.308	-0.308	0.000	0.000	0.000	0.000
143	A	146	GLU	-1	-0.965	-0.964	36.013	-7.778	-7.778	0.000	0.000	0.000	0.000
144	A	147	GLU	-1	-0.936	-0.959	35.816	-8.817	-8.817	0.000	0.000	0.000	0.000
145	A	148	ASN	0	-0.097	-0.076	31.872	-0.545	-0.545	0.000	0.000	0.000	0.000
146	A	149	VAL	0	-0.022	-0.004	31.429	-0.473	-0.473	0.000	0.000	0.000	0.000
147	A	150	LEU	0	0.016	0.021	32.353	0.262	0.262	0.000	0.000	0.000	0.000
148	A	151	PRO	0	0.003	0.003	32.813	-0.282	-0.282	0.000	0.000	0.000	0.000
149	A	152	PRO	-1	-0.955	-0.963	31.148	-9.484	-9.484	0.000	0.000	0.000	0.000

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