FMO DATABASE

FMODB ID: G8251

Calculation Name: 1QU9-A-Xray547

Preferred Name:

Target Type:

Ligand Name: s-phosphocysteine

Ligand 3-letter code: CSP

Ligand of Interest (LOI):

PDB ID: 1QU9

Chain ID: A

ChEMBL ID:

UniProt ID: P0AF93

Base Structure: X-ray

Registration Date: 2025-10-03

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1011863.902267
FMO2-HF: Nuclear repulsion	965094.159505
FMO2-HF: Total energy	-46769.742762
FMO2-MP2: Total energy	-46908.010906

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:2:SER)

Summations of interaction energy for fragment #1(A:2: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.
-114.008	-109.593	8.128	-6.447	-6.096	-0.053

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.825 / q_NPA : 0.909

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	4	THR	0	0.054	0.023	3.852	-2.400	-0.489	-0.016	-0.971	-0.924	-0.002
20	A	21	VAL	0	-0.065	-0.016	3.348	-2.708	-2.481	0.010	-0.071	-0.166	0.000
21	A	22	ASP	-1	-0.730	-0.846	4.171	-41.816	-41.599	-0.001	-0.091	-0.126	0.000
22	A	23	LEU	0	-0.030	-0.047	2.221	-31.996	-29.546	8.130	-5.884	-4.695	-0.049
23	A	24	GLY	0	-0.018	0.002	3.257	-3.132	-3.484	0.006	0.573	-0.228	-0.002
24	A	25	ASN	0	-0.033	-0.029	5.259	4.100	4.062	-0.001	-0.003	0.043	0.000
4	A	5	ILE	0	-0.045	-0.001	6.278	-0.173	-0.173	0.000	0.000	0.000	0.000
5	A	6	ALA	0	-0.023	-0.022	8.807	1.156	1.156	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.007	-0.009	12.316	0.418	0.418	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.856	-0.917	15.591	-15.847	-15.847	0.000	0.000	0.000	0.000
8	A	9	ASN	0	-0.089	-0.047	18.569	1.433	1.433	0.000	0.000	0.000	0.000
9	A	10	ALA	0	0.045	0.022	16.609	0.301	0.301	0.000	0.000	0.000	0.000
10	A	11	PRO	0	-0.030	-0.013	18.772	-0.061	-0.061	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.025	0.029	17.480	-0.900	-0.900	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.029	-0.023	14.063	0.317	0.317	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.027	-0.001	16.094	0.102	0.102	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.011	0.009	18.354	0.426	0.426	0.000	0.000	0.000	0.000
15	A	16	PRO	0	-0.019	-0.011	15.454	-0.745	-0.745	0.000	0.000	0.000	0.000
16	A	17	TYR	0	-0.016	-0.004	12.527	-0.138	-0.138	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.035	0.014	7.533	0.026	0.026	0.000	0.000	0.000	0.000
18	A	19	GLN	0	0.026	0.005	11.019	-0.740	-0.740	0.000	0.000	0.000	0.000
19	A	20	GLY	0	0.089	0.039	8.951	1.452	1.452	0.000	0.000	0.000	0.000
25	A	26	MET	0	0.015	0.027	7.179	2.530	2.530	0.000	0.000	0.000	0.000
26	A	27	ILE	0	0.013	0.004	6.424	-6.500	-6.500	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.013	-0.006	7.443	2.728	2.728	0.000	0.000	0.000	0.000
28	A	29	THR	0	-0.006	-0.011	8.564	-1.744	-1.744	0.000	0.000	0.000	0.000
29	A	30	SER	0	-0.008	-0.020	11.305	-0.068	-0.068	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.007	0.022	12.910	0.411	0.411	0.000	0.000	0.000	0.000
31	A	32	GLN	0	-0.052	-0.041	14.817	0.596	0.596	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.063	0.027	18.476	0.645	0.645	0.000	0.000	0.000	0.000
33	A	34	PRO	0	-0.019	0.008	21.978	-0.245	-0.245	0.000	0.000	0.000	0.000
34	A	35	VAL	0	-0.051	-0.037	22.868	0.503	0.503	0.000	0.000	0.000	0.000
35	A	36	ASN	0	0.071	0.031	23.552	-0.763	-0.763	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.019	-0.001	21.502	0.191	0.191	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.914	0.960	23.458	11.189	11.189	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.032	-0.039	26.808	0.085	0.085	0.000	0.000	0.000	0.000
39	A	40	GLY	0	0.000	0.009	25.907	0.179	0.179	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.926	-0.944	26.976	-9.427	-9.427	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.006	-0.002	27.025	-0.425	-0.425	0.000	0.000	0.000	0.000
42	A	43	PRO	0	-0.012	0.019	28.746	0.400	0.400	0.000	0.000	0.000	0.000
43	A	44	ALA	0	0.063	0.019	31.757	-0.105	-0.105	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.830	-0.921	34.235	-8.876	-8.876	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.001	0.004	31.162	-0.321	-0.321	0.000	0.000	0.000	0.000
46	A	47	ALA	0	0.057	0.034	30.555	-0.348	-0.348	0.000	0.000	0.000	0.000
47	A	48	ALA	0	-0.026	-0.019	29.955	-0.371	-0.371	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.004	-0.015	27.827	-0.612	-0.612	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.033	0.013	26.099	-0.532	-0.532	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.818	0.871	25.209	10.234	10.234	0.000	0.000	0.000	0.000
51	A	52	GLN	0	0.012	0.011	23.172	-0.048	-0.048	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.014	-0.018	21.744	-0.580	-0.580	0.000	0.000	0.000	0.000
53	A	54	LEU	0	-0.007	0.003	20.316	-0.816	-0.816	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.863	-0.946	20.471	-13.060	-13.060	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.047	-0.030	18.747	-0.523	-0.523	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.010	-0.010	15.998	-1.036	-1.036	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.832	0.927	15.701	12.208	12.208	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.026	0.017	16.795	-0.812	-0.812	0.000	0.000	0.000	0.000
59	A	60	ILE	0	-0.055	-0.021	11.368	-0.949	-0.949	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.005	-0.010	12.224	-2.061	-2.061	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.878	-0.947	13.189	-16.196	-16.196	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.049	-0.013	13.104	-0.249	-0.249	0.000	0.000	0.000	0.000
63	A	64	ALA	0	-0.039	-0.010	8.917	-1.782	-1.782	0.000	0.000	0.000	0.000
64	A	65	GLY	0	-0.021	-0.014	10.450	-1.440	-1.440	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.086	-0.032	11.199	0.157	0.157	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.977	0.968	14.441	15.616	15.616	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.046	0.012	17.289	-0.612	-0.612	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.011	-0.017	19.686	0.071	0.071	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.825	-0.891	15.241	-17.482	-17.482	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.053	-0.027	15.624	-1.333	-1.333	0.000	0.000	0.000	0.000
71	A	72	VAL	0	0.018	0.009	14.719	0.950	0.950	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.831	0.916	15.666	16.504	16.504	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.020	0.018	16.458	-0.452	-0.452	0.000	0.000	0.000	0.000
74	A	75	THR	0	-0.079	-0.067	18.009	0.713	0.713	0.000	0.000	0.000	0.000
75	A	76	VAL	0	-0.005	0.000	20.068	-0.274	-0.274	0.000	0.000	0.000	0.000
76	A	77	PHE	0	0.035	0.019	18.936	0.533	0.533	0.000	0.000	0.000	0.000
77	A	78	VAL	0	0.010	-0.011	24.354	-0.043	-0.043	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.895	0.955	27.802	9.263	9.263	0.000	0.000	0.000	0.000
79	A	80	ASP	-1	-0.825	-0.910	30.653	-8.224	-8.224	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.002	-0.005	30.389	-0.181	-0.181	0.000	0.000	0.000	0.000
81	A	82	ASN	0	-0.086	-0.044	33.552	0.173	0.173	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.857	-0.927	33.455	-8.644	-8.644	0.000	0.000	0.000	0.000
83	A	84	PHE	0	-0.038	-0.038	27.189	-0.211	-0.211	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.000	0.004	32.403	-0.179	-0.179	0.000	0.000	0.000	0.000
85	A	86	THR	0	0.028	0.012	33.524	-0.031	-0.031	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.003	0.013	27.773	-0.215	-0.215	0.000	0.000	0.000	0.000
87	A	88	ASN	0	0.035	0.014	29.351	-0.670	-0.670	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.038	0.028	30.555	-0.186	-0.186	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.036	-0.023	28.264	0.004	0.004	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.015	-0.024	21.960	-0.188	-0.188	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.940	-0.969	27.007	-9.883	-9.883	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.001	0.020	29.389	-0.088	-0.088	0.000	0.000	0.000	0.000
93	A	94	PHE	0	0.038	0.018	21.774	-0.126	-0.126	0.000	0.000	0.000	0.000
94	A	95	PHE	0	0.003	-0.013	20.502	-0.385	-0.385	0.000	0.000	0.000	0.000
95	A	96	THR	0	-0.004	-0.010	25.644	-0.087	-0.087	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.828	-0.882	27.834	-10.577	-10.577	0.000	0.000	0.000	0.000
97	A	98	HIS	0	-0.030	-0.016	23.469	-0.254	-0.254	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.086	-0.040	24.752	-0.141	-0.141	0.000	0.000	0.000	0.000
99	A	100	ALA	0	0.000	0.013	22.978	-0.238	-0.238	0.000	0.000	0.000	0.000
100	A	101	THR	0	-0.020	-0.004	23.685	0.604	0.604	0.000	0.000	0.000	0.000
101	A	102	PHE	0	-0.015	-0.012	23.452	-0.543	-0.543	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.010	0.015	19.509	-0.028	-0.028	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.006	0.019	20.007	0.649	0.649	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.875	0.927	20.678	10.914	10.914	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.018	-0.009	22.015	0.118	0.118	0.000	0.000	0.000	0.000
106	A	107	CYS	0	-0.030	-0.008	23.361	-0.427	-0.427	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.011	0.008	24.719	0.266	0.266	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.858	-0.923	27.318	-9.305	-9.305	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.020	-0.011	25.141	-0.067	-0.067	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.006	-0.007	28.587	0.237	0.237	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.767	0.827	28.908	10.080	10.080	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.028	0.037	23.729	-0.339	-0.339	0.000	0.000	0.000	0.000
113	A	114	PRO	0	0.032	0.008	21.695	0.486	0.486	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.922	0.950	24.534	11.734	11.734	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.806	-0.849	27.661	-9.515	-9.515	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.036	0.001	24.900	0.288	0.288	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.932	0.946	28.387	9.010	9.010	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.029	-0.016	24.470	0.107	0.107	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.874	-0.948	19.245	-14.676	-14.676	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.027	-0.014	18.975	0.202	0.202	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.848	-0.873	14.785	-18.450	-18.450	0.000	0.000	0.000	0.000
122	A	123	ALA	0	0.009	-0.017	14.330	1.005	1.005	0.000	0.000	0.000	0.000
123	A	124	ILE	0	-0.013	-0.001	10.859	-1.751	-1.751	0.000	0.000	0.000	0.000
124	A	125	ALA	0	0.032	0.015	11.621	1.815	1.815	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.037	-0.023	11.135	-2.722	-2.722	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.799	0.878	7.065	32.932	32.932	0.000	0.000	0.000	0.000
127	A	128	ARG	0	0.075	0.068	12.684	-0.997	-0.997	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)