FMO DATABASE

FMODB ID: 65R7Z

Calculation Name: 2QPF-A-Xray547

Preferred Name:

Target Type:

Ligand Name: cysteinesulfonic acid

Ligand 3-letter code: OCS

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2QPF

Chain ID: A

ChEMBL ID:

UniProt ID: P07309

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	117
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-897898.175309
FMO2-HF: Nuclear repulsion	853556.706168
FMO2-HF: Total energy	-44341.469141
FMO2-MP2: Total energy	-44472.470051

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:8:SER)

Summations of interaction energy for fragment #1(A:8: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.
-46.159	-41.216	0.361	-2.416	-2.887	0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.871 / q_NPA : 0.921

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	10	CYS	0	0.017	0.045	2.714	4.429	9.080	0.364	-2.322	-2.693	0.003
4	A	11	PRO	0	0.010	0.020	4.483	-4.065	-4.022	-0.001	-0.026	-0.016	0.000
6	A	13	MET	0	-0.072	-0.022	4.999	-3.515	-3.393	-0.001	-0.017	-0.104	0.000
97	A	104	HIS	1	0.795	0.896	3.880	46.061	46.188	-0.001	-0.051	-0.074	0.000
5	A	12	LEU	0	0.049	0.021	7.334	2.595	2.595	0.000	0.000	0.000	0.000
7	A	14	VAL	0	-0.001	0.007	8.447	1.145	1.145	0.000	0.000	0.000	0.000
8	A	15	LYS	1	0.825	0.897	7.840	29.283	29.283	0.000	0.000	0.000	0.000
9	A	16	VAL	0	0.006	0.003	12.827	0.764	0.764	0.000	0.000	0.000	0.000
10	A	17	LEU	0	0.026	0.022	16.452	-0.058	-0.058	0.000	0.000	0.000	0.000
11	A	18	ASP	-1	-0.738	-0.852	19.130	-11.391	-11.391	0.000	0.000	0.000	0.000
12	A	19	ALA	0	-0.003	-0.013	22.873	0.026	0.026	0.000	0.000	0.000	0.000
13	A	20	VAL	0	-0.051	-0.019	25.500	0.382	0.382	0.000	0.000	0.000	0.000
14	A	21	ARG	1	0.899	0.944	24.408	12.022	12.022	0.000	0.000	0.000	0.000
15	A	22	GLY	0	-0.003	0.019	24.639	0.073	0.073	0.000	0.000	0.000	0.000
16	A	23	SER	0	-0.043	-0.027	21.743	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	24	PRO	0	0.023	0.006	16.683	-0.082	-0.082	0.000	0.000	0.000	0.000
18	A	25	ALA	0	-0.017	0.013	18.334	0.782	0.782	0.000	0.000	0.000	0.000
19	A	26	VAL	0	-0.021	0.017	18.141	-0.842	-0.842	0.000	0.000	0.000	0.000
20	A	27	ASP	-1	-0.874	-0.948	18.676	-13.193	-13.193	0.000	0.000	0.000	0.000
21	A	28	VAL	0	-0.040	-0.013	18.414	0.599	0.599	0.000	0.000	0.000	0.000
22	A	29	ALA	0	-0.041	-0.024	18.345	-0.774	-0.774	0.000	0.000	0.000	0.000
23	A	30	VAL	0	-0.002	-0.002	15.118	0.176	0.176	0.000	0.000	0.000	0.000
24	A	31	LYS	1	0.866	0.925	18.141	12.040	12.040	0.000	0.000	0.000	0.000
25	A	32	VAL	0	0.001	0.000	14.574	-0.243	-0.243	0.000	0.000	0.000	0.000
26	A	33	PHE	0	0.007	-0.001	18.065	0.370	0.370	0.000	0.000	0.000	0.000
27	A	34	LYS	1	0.903	0.959	19.600	14.183	14.183	0.000	0.000	0.000	0.000
28	A	35	LYS	1	0.915	0.975	21.524	11.675	11.675	0.000	0.000	0.000	0.000
29	A	36	THR	0	0.016	0.001	24.813	-0.189	-0.189	0.000	0.000	0.000	0.000
30	A	37	SER	0	0.008	-0.018	27.357	-0.045	-0.045	0.000	0.000	0.000	0.000
31	A	38	GLU	-1	-0.883	-0.889	29.982	-9.324	-9.324	0.000	0.000	0.000	0.000
32	A	39	GLY	0	-0.043	-0.023	29.755	0.224	0.224	0.000	0.000	0.000	0.000
33	A	40	SER	0	-0.040	-0.043	29.822	-0.166	-0.166	0.000	0.000	0.000	0.000
34	A	41	TRP	0	-0.019	-0.023	22.645	-0.451	-0.451	0.000	0.000	0.000	0.000
35	A	42	GLU	-1	-0.884	-0.936	23.405	-12.177	-12.177	0.000	0.000	0.000	0.000
36	A	43	PRO	0	-0.036	-0.036	22.211	-0.629	-0.629	0.000	0.000	0.000	0.000
37	A	44	PHE	0	0.027	0.020	14.232	-0.126	-0.126	0.000	0.000	0.000	0.000
38	A	45	ALA	0	-0.022	-0.019	14.794	-0.844	-0.844	0.000	0.000	0.000	0.000
39	A	46	SER	0	-0.037	-0.013	16.442	0.929	0.929	0.000	0.000	0.000	0.000
40	A	47	GLY	0	0.034	0.011	15.111	-0.841	-0.841	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.935	0.966	15.563	14.538	14.538	0.000	0.000	0.000	0.000
42	A	49	THR	0	-0.035	-0.021	14.270	-0.808	-0.808	0.000	0.000	0.000	0.000
43	A	50	ALA	0	0.048	0.029	13.216	0.976	0.976	0.000	0.000	0.000	0.000
44	A	51	GLU	-1	-0.831	-0.941	15.151	-14.228	-14.228	0.000	0.000	0.000	0.000
45	A	52	SER	0	-0.039	-0.016	11.330	0.665	0.665	0.000	0.000	0.000	0.000
46	A	53	GLY	0	0.033	0.018	14.117	-0.324	-0.324	0.000	0.000	0.000	0.000
47	A	54	GLU	-1	-0.864	-0.917	8.226	-30.404	-30.404	0.000	0.000	0.000	0.000
48	A	55	LEU	0	0.004	0.010	10.391	1.130	1.130	0.000	0.000	0.000	0.000
49	A	56	HIS	0	-0.016	-0.030	5.553	-1.323	-1.323	0.000	0.000	0.000	0.000
50	A	57	GLY	0	0.018	-0.010	6.925	1.985	1.985	0.000	0.000	0.000	0.000
51	A	58	LEU	0	0.010	0.020	8.661	1.689	1.689	0.000	0.000	0.000	0.000
52	A	59	THR	0	-0.026	-0.032	10.019	2.799	2.799	0.000	0.000	0.000	0.000
53	A	60	THR	0	-0.047	-0.031	9.160	-2.799	-2.799	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.799	-0.929	8.267	-34.457	-34.457	0.000	0.000	0.000	0.000
55	A	62	GLU	-1	-0.870	-0.908	11.301	-23.126	-23.126	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.841	0.931	13.878	20.422	20.422	0.000	0.000	0.000	0.000
57	A	64	PHE	0	-0.042	-0.009	11.433	0.989	0.989	0.000	0.000	0.000	0.000
58	A	65	VAL	0	0.033	0.015	14.339	-0.542	-0.542	0.000	0.000	0.000	0.000
59	A	66	GLU	-1	-0.874	-0.918	17.406	-14.517	-14.517	0.000	0.000	0.000	0.000
60	A	67	GLY	0	0.010	0.004	19.321	0.726	0.726	0.000	0.000	0.000	0.000
61	A	68	VAL	0	-0.028	-0.006	20.025	-0.579	-0.579	0.000	0.000	0.000	0.000
62	A	69	TYR	0	-0.004	-0.034	17.190	0.212	0.212	0.000	0.000	0.000	0.000
63	A	70	ARG	1	0.777	0.875	19.895	12.553	12.553	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.025	-0.012	15.388	-0.393	-0.393	0.000	0.000	0.000	0.000
65	A	72	GLU	-1	-0.800	-0.885	18.538	-11.591	-11.591	0.000	0.000	0.000	0.000
66	A	73	LEU	0	0.008	-0.003	16.936	-0.607	-0.607	0.000	0.000	0.000	0.000
67	A	74	ASP	-1	-0.791	-0.874	20.687	-10.767	-10.767	0.000	0.000	0.000	0.000
68	A	75	THR	0	0.028	-0.005	23.398	-0.072	-0.072	0.000	0.000	0.000	0.000
69	A	76	LYS	1	0.792	0.888	25.003	9.507	9.507	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.038	-0.062	25.819	0.471	0.471	0.000	0.000	0.000	0.000
71	A	78	TYR	0	-0.059	-0.037	22.577	0.072	0.072	0.000	0.000	0.000	0.000
72	A	79	TRP	0	0.036	0.003	25.447	0.254	0.254	0.000	0.000	0.000	0.000
73	A	80	LYS	1	0.957	0.981	28.443	9.288	9.288	0.000	0.000	0.000	0.000
74	A	81	THR	0	-0.051	-0.027	26.797	0.320	0.320	0.000	0.000	0.000	0.000
75	A	82	LEU	0	-0.056	-0.019	25.991	0.104	0.104	0.000	0.000	0.000	0.000
76	A	83	GLY	0	-0.011	0.003	30.022	0.214	0.214	0.000	0.000	0.000	0.000
77	A	84	ILE	0	-0.040	-0.021	30.450	0.269	0.269	0.000	0.000	0.000	0.000
78	A	85	SER	0	-0.015	-0.020	32.352	-0.122	-0.122	0.000	0.000	0.000	0.000
79	A	86	PRO	0	-0.074	-0.026	29.680	0.126	0.126	0.000	0.000	0.000	0.000
80	A	87	PHE	0	-0.026	-0.011	32.041	0.237	0.237	0.000	0.000	0.000	0.000
81	A	88	HIS	0	-0.002	0.002	28.310	0.085	0.085	0.000	0.000	0.000	0.000
82	A	89	GLU	-1	-0.795	-0.884	29.408	-9.367	-9.367	0.000	0.000	0.000	0.000
83	A	90	PHE	0	-0.026	-0.019	24.589	-0.132	-0.132	0.000	0.000	0.000	0.000
84	A	91	ALA	0	0.015	0.023	22.430	0.255	0.255	0.000	0.000	0.000	0.000
85	A	92	ASP	-1	-0.863	-0.927	21.505	-12.605	-12.605	0.000	0.000	0.000	0.000
86	A	93	VAL	0	-0.001	0.006	18.150	0.117	0.117	0.000	0.000	0.000	0.000
87	A	94	VAL	0	-0.007	-0.010	20.210	-0.306	-0.306	0.000	0.000	0.000	0.000
88	A	95	PHE	0	-0.035	-0.014	14.684	0.016	0.016	0.000	0.000	0.000	0.000
89	A	96	THR	0	0.031	0.012	20.007	0.126	0.126	0.000	0.000	0.000	0.000
90	A	97	ALA	0	-0.027	-0.011	15.008	-0.672	-0.672	0.000	0.000	0.000	0.000
91	A	98	ASN	0	0.013	-0.025	13.208	-0.125	-0.125	0.000	0.000	0.000	0.000
92	A	99	ASP	-1	-0.838	-0.909	16.253	-15.616	-15.616	0.000	0.000	0.000	0.000
93	A	100	SER	0	-0.043	-0.004	17.941	0.342	0.342	0.000	0.000	0.000	0.000
94	A	101	GLY	0	0.041	0.023	16.199	-0.561	-0.561	0.000	0.000	0.000	0.000
95	A	102	HIS	0	-0.048	-0.037	11.223	0.127	0.127	0.000	0.000	0.000	0.000
96	A	103	ARG	1	0.859	0.951	10.230	21.466	21.466	0.000	0.000	0.000	0.000
98	A	105	TYR	0	0.053	0.030	7.885	1.113	1.113	0.000	0.000	0.000	0.000
99	A	106	THR	0	-0.019	-0.014	8.086	-2.371	-2.371	0.000	0.000	0.000	0.000
100	A	107	ILE	0	-0.003	0.001	10.039	1.574	1.574	0.000	0.000	0.000	0.000
101	A	108	ALA	0	0.029	0.016	13.396	-0.226	-0.226	0.000	0.000	0.000	0.000
102	A	109	ALA	0	0.007	-0.004	14.766	0.959	0.959	0.000	0.000	0.000	0.000
103	A	110	LEU	0	-0.015	0.011	18.158	-0.338	-0.338	0.000	0.000	0.000	0.000
104	A	111	LEU	0	0.017	0.003	20.978	0.507	0.507	0.000	0.000	0.000	0.000
105	A	112	SER	0	-0.012	-0.016	23.710	0.244	0.244	0.000	0.000	0.000	0.000
106	A	113	PRO	0	0.008	0.007	27.468	-0.045	-0.045	0.000	0.000	0.000	0.000
107	A	114	TYR	0	0.046	0.011	30.129	0.133	0.133	0.000	0.000	0.000	0.000
108	A	115	SER	0	-0.033	-0.013	28.784	0.043	0.043	0.000	0.000	0.000	0.000
109	A	116	TYR	0	0.032	0.018	22.957	-0.082	-0.082	0.000	0.000	0.000	0.000
110	A	117	SER	0	0.000	0.017	22.495	0.083	0.083	0.000	0.000	0.000	0.000
111	A	118	THR	0	0.002	-0.020	18.001	-0.451	-0.451	0.000	0.000	0.000	0.000
112	A	119	THR	0	-0.024	-0.024	16.521	0.600	0.600	0.000	0.000	0.000	0.000
113	A	120	ALA	0	0.017	0.025	14.755	-0.917	-0.917	0.000	0.000	0.000	0.000
114	A	121	VAL	0	0.001	0.000	10.554	0.589	0.589	0.000	0.000	0.000	0.000
115	A	122	VAL	0	-0.017	-0.012	10.992	-1.810	-1.810	0.000	0.000	0.000	0.000
116	A	123	SER	0	-0.051	-0.028	7.258	-1.610	-1.610	0.000	0.000	0.000	0.000
117	A	124	ASN	-1	-0.887	-0.942	7.178	-38.977	-38.977	0.000	0.000	0.000	0.000

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