FMO DATABASE

FMODB ID: 9LV92

Calculation Name: 1SC0-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1SC0

Chain ID: A

ChEMBL ID:

UniProt ID: P45083

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	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1171143.297348
FMO2-HF: Nuclear repulsion	1118362.382821
FMO2-HF: Total energy	-52780.914527
FMO2-MP2: Total energy	-52933.192447

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-107.297	-101.771	7.892	-5.515	-7.902	-0.061

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.820 / q_NPA : 0.916

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	LYS	1	0.801	0.901	2.467	38.447	40.118	1.846	-1.303	-2.215	-0.013
4	A	5	LYS	1	0.890	0.973	5.308	31.002	31.118	-0.001	-0.006	-0.108	0.000
32	A	33	GLU	-1	-0.938	-0.968	2.338	-40.532	-40.069	0.791	-0.307	-0.947	-0.001
33	A	34	ASP	-1	-0.942	-0.990	2.228	-72.322	-69.625	5.241	-3.697	-4.240	-0.046
34	A	35	TRP	0	0.017	0.009	4.221	4.593	4.665	-0.001	-0.034	-0.037	0.000
72	A	73	CYS	0	-0.065	-0.022	3.972	-12.250	-11.944	0.017	-0.134	-0.189	-0.001
103	A	104	PRO	0	-0.004	0.015	4.031	3.449	3.526	-0.001	-0.009	-0.067	0.000
106	A	107	LEU	0	0.029	0.018	4.054	-0.856	-0.732	0.000	-0.025	-0.099	0.000
5	A	6	THR	0	0.002	0.005	6.961	-2.213	-2.213	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.021	-0.010	6.427	2.432	2.432	0.000	0.000	0.000	0.000
7	A	8	THR	0	0.051	0.020	11.095	-0.146	-0.146	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.053	0.019	12.625	-0.040	-0.040	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.935	-0.948	14.818	-13.840	-13.840	0.000	0.000	0.000	0.000
10	A	11	ASN	0	0.022	0.005	14.850	1.207	1.207	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.013	0.001	11.291	0.299	0.299	0.000	0.000	0.000	0.000
12	A	13	ASN	0	0.008	-0.014	15.973	0.725	0.725	0.000	0.000	0.000	0.000
13	A	14	GLN	0	-0.011	0.001	19.259	0.469	0.469	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.001	0.019	16.071	0.567	0.567	0.000	0.000	0.000	0.000
15	A	16	CYS	0	-0.022	-0.005	17.765	0.053	0.053	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.043	-0.023	20.638	0.860	0.860	0.000	0.000	0.000	0.000
17	A	18	ASN	0	-0.033	-0.022	24.289	0.225	0.225	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.028	0.002	23.013	0.029	0.029	0.000	0.000	0.000	0.000
19	A	20	ALA	0	0.018	-0.009	24.330	0.193	0.193	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.019	0.017	19.456	0.186	0.186	0.000	0.000	0.000	0.000
21	A	22	SER	0	0.016	0.017	22.622	0.320	0.320	0.000	0.000	0.000	0.000
22	A	23	HIS	0	-0.011	0.000	24.884	0.312	0.312	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.029	-0.027	24.450	0.396	0.396	0.000	0.000	0.000	0.000
24	A	25	GLY	0	-0.041	-0.021	25.913	0.045	0.045	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.073	-0.035	19.408	-0.213	-0.213	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.930	-0.954	19.845	-14.133	-14.133	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.023	-0.030	13.872	-0.542	-0.542	0.000	0.000	0.000	0.000
28	A	29	SER	0	0.022	0.010	15.744	0.238	0.238	0.000	0.000	0.000	0.000
29	A	30	ALA	0	-0.011	-0.008	13.403	0.614	0.614	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.018	-0.018	6.778	-0.286	-0.286	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.044	0.040	7.345	2.852	2.852	0.000	0.000	0.000	0.000
35	A	36	ILE	0	-0.012	-0.008	7.422	0.063	0.063	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.834	-0.900	9.670	-19.674	-19.674	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.032	0.026	13.467	0.115	0.115	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.040	-0.009	16.610	0.666	0.666	0.000	0.000	0.000	0.000
39	A	40	MET	0	0.042	0.026	20.237	-0.030	-0.030	0.000	0.000	0.000	0.000
40	A	41	PRO	0	0.001	0.016	23.259	0.069	0.069	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.014	0.007	26.978	-0.073	-0.073	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.749	-0.859	29.431	-9.977	-9.977	0.000	0.000	0.000	0.000
43	A	44	HIS	0	0.003	-0.016	32.214	-0.149	-0.149	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.835	0.911	28.911	10.835	10.835	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.018	-0.035	26.926	-0.020	-0.020	0.000	0.000	0.000	0.000
46	A	47	MET	0	-0.042	-0.003	29.541	-0.158	-0.158	0.000	0.000	0.000	0.000
47	A	48	GLN	0	-0.014	-0.009	31.960	0.230	0.230	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.017	-0.010	34.618	0.033	0.033	0.000	0.000	0.000	0.000
49	A	50	PHE	0	-0.023	-0.006	35.701	0.202	0.202	0.000	0.000	0.000	0.000
50	A	51	GLY	0	-0.004	0.009	36.436	0.054	0.054	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.026	-0.029	32.649	-0.071	-0.071	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.003	0.005	25.165	0.099	0.099	0.000	0.000	0.000	0.000
53	A	54	HIS	0	0.040	0.026	29.238	-0.163	-0.163	0.000	0.000	0.000	0.000
54	A	55	GLY	0	0.060	0.024	26.813	-0.447	-0.447	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.009	-0.006	25.636	-0.473	-0.473	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.029	0.013	25.198	-0.403	-0.403	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.025	-0.024	22.939	-0.538	-0.538	0.000	0.000	0.000	0.000
58	A	59	VAL	0	0.011	0.007	21.135	-0.738	-0.738	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.023	0.021	20.406	-0.681	-0.681	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.004	0.008	18.437	-0.616	-0.616	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.004	-0.003	16.719	-1.060	-1.060	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.875	-0.952	15.567	-17.011	-17.011	0.000	0.000	0.000	0.000
63	A	64	THR	0	-0.027	-0.010	15.815	-0.873	-0.873	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.014	-0.011	12.185	-1.055	-1.055	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.035	0.006	11.116	-2.356	-2.356	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.012	-0.021	10.827	-2.110	-2.110	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.014	0.004	11.835	-1.122	-1.122	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.042	0.022	7.311	-1.790	-1.790	0.000	0.000	0.000	0.000
69	A	70	GLY	0	0.076	0.023	7.011	-5.172	-5.172	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.069	-0.048	8.747	-1.030	-1.030	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.032	0.016	7.604	0.506	0.506	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.071	-0.023	5.888	0.906	0.906	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.798	-0.905	8.371	-31.460	-31.460	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.851	-0.950	10.730	-18.621	-18.621	0.000	0.000	0.000	0.000
76	A	77	GLY	0	-0.021	0.000	13.928	0.015	0.015	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.844	0.917	12.808	20.471	20.471	0.000	0.000	0.000	0.000
78	A	79	THR	0	0.022	0.006	13.847	-1.630	-1.630	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.014	-0.007	11.333	-0.213	-0.213	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.019	-0.008	14.429	0.956	0.956	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.046	0.032	17.080	-0.648	-0.648	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.083	-0.034	18.220	0.662	0.662	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.848	-0.916	18.975	-14.823	-14.823	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.032	0.021	17.839	-1.025	-1.025	0.000	0.000	0.000	0.000
85	A	86	ASN	0	-0.049	-0.013	19.250	0.948	0.948	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.048	0.021	20.111	-0.840	-0.840	0.000	0.000	0.000	0.000
87	A	88	ASN	0	-0.036	-0.011	22.241	0.955	0.955	0.000	0.000	0.000	0.000
88	A	89	HIS	0	0.013	0.010	23.752	-0.208	-0.208	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.021	-0.011	23.143	0.377	0.377	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.913	0.956	27.094	11.474	11.474	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.012	0.020	28.339	-0.297	-0.297	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.009	-0.007	26.413	-0.095	-0.095	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.942	0.963	29.901	8.838	8.838	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.014	0.019	31.069	0.348	0.348	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.073	0.054	29.068	-0.290	-0.290	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.885	0.935	22.993	13.381	13.381	0.000	0.000	0.000	0.000
97	A	98	VAL	0	0.001	-0.003	22.315	0.011	0.011	0.000	0.000	0.000	0.000
98	A	99	THR	0	0.024	0.001	16.979	-0.077	-0.077	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.016	-0.006	16.636	0.303	0.303	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.846	0.903	11.484	22.955	22.955	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.018	0.017	9.779	0.615	0.615	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.004	-0.022	7.418	-1.928	-1.928	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.027	-0.014	7.224	1.126	1.126	0.000	0.000	0.000	0.000
105	A	106	ASN	0	-0.064	-0.047	9.341	0.575	0.575	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.050	0.034	8.162	-0.218	-0.218	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.895	0.936	11.287	17.086	17.086	0.000	0.000	0.000	0.000
109	A	110	ASN	0	0.019	-0.001	13.241	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	111	ILE	0	0.035	0.026	13.839	0.885	0.885	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.007	0.019	8.761	-2.126	-2.126	0.000	0.000	0.000	0.000
112	A	113	VAL	0	-0.002	0.001	10.756	2.199	2.199	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.038	0.001	4.805	-3.860	-3.860	0.000	0.000	0.000	0.000
114	A	115	GLN	0	0.000	-0.003	10.832	2.652	2.652	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.047	-0.030	11.688	-1.737	-1.737	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.869	-0.913	14.290	-17.597	-17.597	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.014	-0.015	16.526	-0.369	-0.369	0.000	0.000	0.000	0.000
118	A	119	ARG	1	0.940	0.960	17.985	16.979	16.979	0.000	0.000	0.000	0.000
119	A	120	THR	0	0.036	0.003	21.481	-0.111	-0.111	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.802	-0.905	23.730	-11.330	-11.330	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.917	-0.965	25.402	-10.894	-10.894	0.000	0.000	0.000	0.000
122	A	123	ASN	0	-0.021	-0.017	21.526	-0.433	-0.433	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.845	0.944	22.866	10.669	10.669	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.017	0.013	19.113	-0.055	-0.055	0.000	0.000	0.000	0.000
125	A	126	CYS	0	-0.084	-0.036	22.922	0.517	0.517	0.000	0.000	0.000	0.000
126	A	127	CYS	0	-0.048	-0.025	21.769	0.415	0.415	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.028	0.034	18.951	-0.599	-0.599	0.000	0.000	0.000	0.000
128	A	129	SER	0	-0.016	-0.034	17.664	0.774	0.774	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.956	0.988	14.883	15.804	15.804	0.000	0.000	0.000	0.000
130	A	131	LEU	0	0.003	0.018	13.218	1.062	1.062	0.000	0.000	0.000	0.000
131	A	132	THR	0	-0.061	-0.045	14.088	-2.187	-2.187	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.010	0.006	11.312	0.691	0.691	0.000	0.000	0.000	0.000
133	A	134	SER	0	0.022	0.003	14.983	-0.122	-0.122	0.000	0.000	0.000	0.000
134	A	135	VAL	0	-0.055	-0.022	11.851	-0.656	-0.656	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.033	-0.018	14.871	1.079	1.079	0.000	0.000	0.000	0.000
136	A	137	ASN	0	-0.018	-0.018	16.783	-1.746	-1.746	0.000	0.000	0.000	0.000
137	A	138	LEU	-1	-0.898	-0.924	17.812	-14.043	-14.043	0.000	0.000	0.000	0.000

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