FMO DATABASE

FMODB ID: Y9G42

Calculation Name: 1S1Q-A-Xray547

Preferred Name: Tumor susceptibility gene 101 protein

Target Type: SINGLE PROTEIN

Ligand Name: acetic acid | copper (ii) ion

Ligand 3-letter code: ACY | CU

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1S1Q

Chain ID: A

ChEMBL ID: CHEMBL6157

UniProt ID: Q99816

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
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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1337612.704824
FMO2-HF: Nuclear repulsion	1280933.978032
FMO2-HF: Total energy	-56678.726791
FMO2-MP2: Total energy	-56843.433307

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:3:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
39.322	43.24	0.888	-1.88	-2.926	-0.018

Interaction energy analysis for fragmet #1(A:3:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.887 / q_NPA : 0.934

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	5	GLU	-1	-0.820	-0.900	3.882	-32.592	-31.228	-0.011	-0.692	-0.662	-0.002
5	A	7	GLN	0	-0.025	-0.018	2.571	-4.520	-3.108	0.874	-0.910	-1.376	-0.014
6	A	8	LEU	0	0.051	0.032	4.703	3.174	3.314	-0.001	-0.012	-0.127	0.000
27	A	29	ILE	0	-0.030	-0.015	3.860	-1.668	-1.494	0.000	-0.040	-0.134	0.000
34	A	36	LYS	1	0.919	0.952	3.643	31.976	32.259	0.001	-0.049	-0.235	0.000
35	A	37	PRO	0	-0.027	-0.004	3.146	3.168	3.675	0.026	-0.175	-0.358	-0.002
36	A	38	VAL	0	-0.041	-0.025	5.067	-9.175	-9.137	-0.001	-0.002	-0.034	0.000
4	A	6	SER	0	0.031	0.013	6.819	3.019	3.019	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.908	0.942	6.270	28.031	28.031	0.000	0.000	0.000	0.000
8	A	10	LYS	1	0.884	0.941	8.452	33.222	33.222	0.000	0.000	0.000	0.000
9	A	11	MET	0	-0.002	0.021	4.873	2.442	2.442	0.000	0.000	0.000	0.000
10	A	12	VAL	0	0.022	0.010	9.365	2.046	2.046	0.000	0.000	0.000	0.000
11	A	13	SER	0	-0.043	-0.027	11.807	2.558	2.558	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.879	0.916	14.521	19.445	19.445	0.000	0.000	0.000	0.000
13	A	15	TYR	0	0.001	0.006	13.844	0.302	0.302	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.902	0.944	16.949	13.116	13.116	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.019	0.011	18.290	0.956	0.956	0.000	0.000	0.000	0.000
16	A	18	ARG	1	0.952	0.992	14.438	16.792	16.792	0.000	0.000	0.000	0.000
17	A	19	ASP	-1	-0.864	-0.931	13.669	-20.738	-20.738	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.006	0.006	14.453	-0.862	-0.862	0.000	0.000	0.000	0.000
19	A	21	THR	0	0.037	0.022	11.564	-0.609	-0.609	0.000	0.000	0.000	0.000
20	A	22	VAL	0	-0.045	-0.021	9.036	-1.937	-1.937	0.000	0.000	0.000	0.000
21	A	23	ARG	1	0.973	0.990	9.963	18.546	18.546	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.742	-0.859	12.177	-18.981	-18.981	0.000	0.000	0.000	0.000
23	A	25	THR	0	-0.007	-0.014	6.473	-0.651	-0.651	0.000	0.000	0.000	0.000
24	A	26	VAL	0	-0.031	-0.024	7.229	-2.709	-2.709	0.000	0.000	0.000	0.000
25	A	27	ASN	0	-0.005	0.003	8.715	-0.624	-0.624	0.000	0.000	0.000	0.000
26	A	28	VAL	0	0.028	0.024	10.021	0.473	0.473	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.070	-0.038	7.551	-2.103	-2.103	0.000	0.000	0.000	0.000
29	A	31	LEU	0	-0.032	-0.011	9.362	1.207	1.207	0.000	0.000	0.000	0.000
30	A	32	TYR	0	-0.022	-0.035	11.493	0.749	0.749	0.000	0.000	0.000	0.000
31	A	33	LYS	1	0.942	0.961	7.085	28.095	28.095	0.000	0.000	0.000	0.000
32	A	34	ASP	-1	-0.913	-0.931	7.419	-28.929	-28.929	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.028	-0.001	8.578	1.143	1.143	0.000	0.000	0.000	0.000
37	A	39	LEU	0	-0.012	-0.003	7.811	1.786	1.786	0.000	0.000	0.000	0.000
38	A	40	ASP	-1	-0.830	-0.905	10.529	-24.849	-24.849	0.000	0.000	0.000	0.000
39	A	41	SER	0	-0.025	-0.023	13.813	0.565	0.565	0.000	0.000	0.000	0.000
40	A	42	TYR	0	-0.018	0.001	17.582	0.482	0.482	0.000	0.000	0.000	0.000
41	A	43	VAL	0	0.012	0.002	19.239	0.409	0.409	0.000	0.000	0.000	0.000
42	A	44	PHE	0	-0.027	-0.016	21.548	-0.208	-0.208	0.000	0.000	0.000	0.000
43	A	45	ASN	0	0.000	-0.019	25.279	-0.040	-0.040	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.832	-0.883	28.543	-10.796	-10.796	0.000	0.000	0.000	0.000
45	A	47	GLY	0	-0.009	0.006	28.411	0.296	0.296	0.000	0.000	0.000	0.000
46	A	48	SER	0	-0.089	-0.049	26.902	-0.346	-0.346	0.000	0.000	0.000	0.000
47	A	49	SER	0	0.016	-0.016	22.130	-0.574	-0.574	0.000	0.000	0.000	0.000
48	A	50	ARG	1	0.908	0.956	19.692	13.752	13.752	0.000	0.000	0.000	0.000
49	A	51	GLU	-1	-0.863	-0.910	14.891	-20.232	-20.232	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.042	-0.023	14.955	0.424	0.424	0.000	0.000	0.000	0.000
51	A	53	MET	0	-0.025	-0.011	8.517	-2.186	-2.186	0.000	0.000	0.000	0.000
52	A	54	ASN	0	-0.028	-0.029	10.380	1.280	1.280	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.010	0.005	7.363	-4.283	-4.283	0.000	0.000	0.000	0.000
54	A	56	THR	0	0.021	-0.001	8.932	3.245	3.245	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.011	0.003	8.913	-4.079	-4.079	0.000	0.000	0.000	0.000
56	A	58	THR	0	-0.053	-0.022	11.120	2.578	2.578	0.000	0.000	0.000	0.000
57	A	59	ILE	0	0.029	0.012	13.112	-1.354	-1.354	0.000	0.000	0.000	0.000
58	A	60	PRO	0	0.008	0.016	15.422	0.850	0.850	0.000	0.000	0.000	0.000
59	A	61	VAL	0	0.018	-0.002	18.367	0.257	0.257	0.000	0.000	0.000	0.000
60	A	62	PRO	0	-0.007	-0.003	21.920	0.361	0.361	0.000	0.000	0.000	0.000
61	A	63	TYR	0	0.021	0.006	24.757	0.380	0.380	0.000	0.000	0.000	0.000
62	A	64	ARG	1	0.924	0.952	27.962	9.814	9.814	0.000	0.000	0.000	0.000
63	A	65	GLY	0	0.018	0.021	29.451	0.198	0.198	0.000	0.000	0.000	0.000
64	A	66	ASN	0	-0.013	0.010	26.256	-0.159	-0.159	0.000	0.000	0.000	0.000
65	A	67	THR	0	-0.011	-0.015	20.337	-0.113	-0.113	0.000	0.000	0.000	0.000
66	A	68	TYR	0	-0.001	0.005	22.066	0.059	0.059	0.000	0.000	0.000	0.000
67	A	69	ASN	0	0.038	0.012	16.448	-0.029	-0.029	0.000	0.000	0.000	0.000
68	A	70	ILE	0	0.018	0.020	18.393	-0.048	-0.048	0.000	0.000	0.000	0.000
69	A	71	PRO	0	0.022	0.005	15.751	-1.124	-1.124	0.000	0.000	0.000	0.000
70	A	72	ILE	0	-0.023	-0.012	14.069	1.199	1.199	0.000	0.000	0.000	0.000
71	A	73	CYS	0	-0.073	-0.032	13.185	-1.431	-1.431	0.000	0.000	0.000	0.000
72	A	74	LEU	0	0.009	0.007	13.229	1.630	1.630	0.000	0.000	0.000	0.000
73	A	75	TRP	0	0.026	0.009	13.213	-1.985	-1.985	0.000	0.000	0.000	0.000
74	A	76	LEU	0	0.012	0.008	11.500	1.288	1.288	0.000	0.000	0.000	0.000
75	A	77	LEU	0	0.088	0.052	15.259	-0.269	-0.269	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.841	-0.927	17.418	-15.469	-15.469	0.000	0.000	0.000	0.000
77	A	79	THR	0	-0.038	-0.043	18.510	-0.250	-0.250	0.000	0.000	0.000	0.000
78	A	80	TYR	0	-0.066	-0.035	15.214	0.503	0.503	0.000	0.000	0.000	0.000
79	A	81	PRO	0	0.023	-0.011	17.643	-0.250	-0.250	0.000	0.000	0.000	0.000
80	A	82	TYR	0	-0.021	-0.029	18.940	0.751	0.751	0.000	0.000	0.000	0.000
81	A	83	ASN	0	-0.024	0.010	21.226	0.579	0.579	0.000	0.000	0.000	0.000
82	A	84	PRO	0	0.049	0.035	20.341	-0.736	-0.736	0.000	0.000	0.000	0.000
83	A	85	PRO	0	-0.003	0.001	16.231	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	86	ILE	0	-0.023	0.004	18.335	0.837	0.837	0.000	0.000	0.000	0.000
85	A	87	CYS	0	-0.039	-0.010	18.105	-1.192	-1.192	0.000	0.000	0.000	0.000
86	A	88	PHE	0	-0.010	-0.019	18.296	1.057	1.057	0.000	0.000	0.000	0.000
87	A	89	VAL	0	0.051	0.024	18.338	-1.023	-1.023	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.852	0.924	16.436	16.245	16.245	0.000	0.000	0.000	0.000
89	A	91	PRO	0	0.057	0.032	19.276	-0.448	-0.448	0.000	0.000	0.000	0.000
90	A	92	THR	0	0.036	-0.004	19.345	-0.039	-0.039	0.000	0.000	0.000	0.000
91	A	93	SER	0	-0.005	-0.015	21.906	0.277	0.277	0.000	0.000	0.000	0.000
92	A	94	SER	0	-0.047	-0.020	23.365	0.417	0.417	0.000	0.000	0.000	0.000
93	A	95	MET	0	-0.017	0.014	20.112	-0.232	-0.232	0.000	0.000	0.000	0.000
94	A	96	THR	0	0.031	0.032	25.737	0.048	0.048	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.023	-0.018	25.020	-0.211	-0.211	0.000	0.000	0.000	0.000
96	A	98	LYS	1	0.924	0.961	27.683	10.113	10.113	0.000	0.000	0.000	0.000
97	A	99	THR	0	-0.004	-0.003	29.649	-0.109	-0.109	0.000	0.000	0.000	0.000
98	A	100	GLY	0	0.006	-0.001	31.130	0.299	0.299	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.835	0.899	31.472	9.054	9.054	0.000	0.000	0.000	0.000
100	A	102	HIS	1	0.900	0.959	26.861	10.751	10.751	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.017	0.029	24.905	-0.548	-0.548	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.755	-0.847	27.290	-10.979	-10.979	0.000	0.000	0.000	0.000
103	A	105	ALA	0	0.053	0.000	27.736	-0.325	-0.325	0.000	0.000	0.000	0.000
104	A	106	ASN	0	-0.064	-0.028	26.393	0.020	0.020	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.017	0.012	23.493	-0.596	-0.596	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.895	0.971	22.979	11.985	11.985	0.000	0.000	0.000	0.000
107	A	109	ILE	0	-0.008	-0.015	19.782	0.499	0.499	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.075	-0.051	23.777	0.013	0.013	0.000	0.000	0.000	0.000
109	A	111	LEU	0	0.036	-0.008	22.278	0.120	0.120	0.000	0.000	0.000	0.000
110	A	112	PRO	0	0.050	0.026	26.342	-0.112	-0.112	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.058	0.035	20.685	-0.148	-0.148	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.030	-0.021	20.595	-0.382	-0.382	0.000	0.000	0.000	0.000
113	A	115	HIS	0	-0.071	-0.022	24.512	0.149	0.149	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.938	-0.978	28.088	-10.110	-10.110	0.000	0.000	0.000	0.000
115	A	117	TRP	0	-0.040	-0.019	18.391	-0.147	-0.147	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.944	0.961	25.052	11.060	11.060	0.000	0.000	0.000	0.000
117	A	119	HIS	0	0.024	0.049	19.885	0.201	0.201	0.000	0.000	0.000	0.000
118	A	120	PRO	0	-0.029	-0.037	22.666	0.535	0.535	0.000	0.000	0.000	0.000
119	A	121	GLN	0	0.003	-0.017	22.932	-0.309	-0.309	0.000	0.000	0.000	0.000
120	A	122	SER	0	-0.018	0.002	21.927	0.139	0.139	0.000	0.000	0.000	0.000
121	A	123	ASP	-1	-0.834	-0.910	17.230	-17.246	-17.246	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.005	-0.026	11.912	0.161	0.161	0.000	0.000	0.000	0.000
123	A	125	LEU	0	-0.010	-0.001	14.514	-0.435	-0.435	0.000	0.000	0.000	0.000
124	A	126	GLY	0	0.011	0.001	16.241	0.484	0.484	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.012	0.001	16.952	0.575	0.575	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.002	-0.002	13.325	0.387	0.387	0.000	0.000	0.000	0.000
127	A	129	GLN	0	0.009	0.019	17.652	-0.108	-0.108	0.000	0.000	0.000	0.000
128	A	130	VAL	0	0.003	0.004	20.282	0.649	0.649	0.000	0.000	0.000	0.000
129	A	131	MET	0	-0.034	-0.011	18.546	0.262	0.262	0.000	0.000	0.000	0.000
130	A	132	ILE	0	0.005	0.003	17.321	0.361	0.361	0.000	0.000	0.000	0.000
131	A	133	VAL	0	-0.004	0.005	21.695	0.461	0.461	0.000	0.000	0.000	0.000
132	A	134	VAL	0	-0.015	-0.013	25.049	0.459	0.459	0.000	0.000	0.000	0.000
133	A	135	PHE	0	-0.038	-0.037	20.652	0.294	0.294	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.039	0.025	25.264	0.056	0.056	0.000	0.000	0.000	0.000
135	A	137	ASP	-1	-0.925	-0.956	26.838	-9.995	-9.995	0.000	0.000	0.000	0.000
136	A	138	GLU	-1	-0.929	-0.971	28.863	-9.525	-9.525	0.000	0.000	0.000	0.000
137	A	139	PRO	0	0.005	0.016	26.573	-0.353	-0.353	0.000	0.000	0.000	0.000
138	A	140	PRO	0	-0.006	-0.004	23.504	0.361	0.361	0.000	0.000	0.000	0.000
139	A	141	VAL	0	-0.023	-0.022	23.362	-0.096	-0.096	0.000	0.000	0.000	0.000
140	A	142	PHE	0	-0.068	-0.028	26.480	0.228	0.228	0.000	0.000	0.000	0.000
141	A	143	SER	-1	-0.869	-0.924	27.338	-10.802	-10.802	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:VAL)