FMO DATABASE

FMODB ID: 9LV62

Calculation Name: 1SXR-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1SXR

Chain ID: A

ChEMBL ID:

UniProt ID: Q9VYX7

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	171
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1813954.222902
FMO2-HF: Nuclear repulsion	1746798.912305
FMO2-HF: Total energy	-67155.310597
FMO2-MP2: Total energy	-67352.340243

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:11:CYS)

Summations of interaction energy for fragment #1(A:11:CYS)

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.
-163.955	-146.579	20.19	-15.668	-21.898	-0.058

Interaction energy analysis for fragmet #1(A:11:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.755 / q_NPA : 0.874

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	13	THR	0	-0.016	-0.012	3.571	4.191	5.745	0.004	-0.624	-0.934	0.001
4	A	14	ILE	0	0.035	0.010	4.685	3.363	3.569	-0.002	-0.013	-0.192	0.000
81	A	92	TRP	0	0.017	0.001	3.562	1.216	1.600	0.001	-0.052	-0.333	0.000
119	A	130	ASP	-1	-0.860	-0.926	2.903	-68.780	-67.358	0.060	-0.597	-0.885	-0.005
120	A	131	LEU	0	-0.070	-0.041	2.013	-30.373	-28.409	8.818	-4.812	-5.970	-0.053
121	A	132	LEU	0	0.000	0.008	2.479	-4.520	-0.868	2.251	-2.611	-3.292	-0.028
124	A	136	VAL	0	-0.005	0.006	2.961	2.028	5.547	0.515	-1.974	-2.060	0.011
125	A	137	GLN	0	-0.040	-0.013	2.017	-17.344	-14.546	6.083	-3.573	-5.308	0.027
126	A	138	GLN	0	-0.045	-0.037	3.473	-4.936	-3.059	2.460	-1.412	-2.924	-0.011
5	A	15	LYS	1	0.829	0.929	7.628	31.632	31.632	0.000	0.000	0.000	0.000
6	A	16	LEU	0	0.060	0.012	9.616	0.789	0.789	0.000	0.000	0.000	0.000
7	A	17	LYS	1	0.857	0.950	12.567	16.746	16.746	0.000	0.000	0.000	0.000
8	A	18	ARG	1	0.959	0.973	16.238	15.717	15.717	0.000	0.000	0.000	0.000
9	A	19	GLN	0	-0.042	-0.024	11.912	-0.297	-0.297	0.000	0.000	0.000	0.000
10	A	20	TRP	0	-0.012	0.006	14.880	0.749	0.749	0.000	0.000	0.000	0.000
11	A	21	GLY	0	0.003	0.011	18.019	0.659	0.659	0.000	0.000	0.000	0.000
12	A	22	GLY	0	0.019	0.011	19.530	0.663	0.663	0.000	0.000	0.000	0.000
13	A	23	LYS	1	0.942	0.958	20.820	11.212	11.212	0.000	0.000	0.000	0.000
14	A	24	PRO	0	0.014	-0.013	20.761	-0.644	-0.644	0.000	0.000	0.000	0.000
15	A	25	SER	0	0.048	0.036	19.717	0.424	0.424	0.000	0.000	0.000	0.000
16	A	26	LEU	0	-0.014	-0.012	21.671	0.238	0.238	0.000	0.000	0.000	0.000
17	A	27	GLY	0	0.024	0.000	23.314	0.475	0.475	0.000	0.000	0.000	0.000
18	A	28	LEU	0	-0.044	-0.009	18.301	-0.407	-0.407	0.000	0.000	0.000	0.000
19	A	29	HIS	0	0.036	0.020	19.864	0.474	0.474	0.000	0.000	0.000	0.000
20	A	30	TYR	0	0.002	0.003	16.899	-0.333	-0.333	0.000	0.000	0.000	0.000
21	A	31	GLN	0	-0.057	-0.023	13.480	-0.227	-0.227	0.000	0.000	0.000	0.000
22	A	32	VAL	0	-0.017	-0.010	16.486	-0.101	-0.101	0.000	0.000	0.000	0.000
23	A	33	ARG	1	0.851	0.926	10.657	18.997	18.997	0.000	0.000	0.000	0.000
24	A	34	PRO	0	-0.027	-0.008	10.614	0.835	0.835	0.000	0.000	0.000	0.000
25	A	35	ILE	0	-0.041	-0.021	11.204	0.987	0.987	0.000	0.000	0.000	0.000
26	A	36	ARG	1	0.949	0.970	11.058	14.288	14.288	0.000	0.000	0.000	0.000
27	A	37	TYR	0	0.026	0.026	13.303	0.348	0.348	0.000	0.000	0.000	0.000
28	A	38	VAL	0	0.001	0.004	8.588	-0.935	-0.935	0.000	0.000	0.000	0.000
29	A	39	VAL	0	-0.004	0.004	12.018	0.725	0.725	0.000	0.000	0.000	0.000
30	A	40	ILE	0	0.008	0.004	10.972	-0.779	-0.779	0.000	0.000	0.000	0.000
31	A	41	HIS	0	0.013	-0.005	14.757	1.623	1.623	0.000	0.000	0.000	0.000
32	A	42	HIS	0	0.016	0.016	16.658	-1.221	-1.221	0.000	0.000	0.000	0.000
33	A	43	THR	0	0.032	0.003	18.307	0.232	0.232	0.000	0.000	0.000	0.000
34	A	44	VAL	0	-0.046	0.008	20.840	0.732	0.732	0.000	0.000	0.000	0.000
35	A	45	THR	0	-0.010	-0.024	23.700	0.314	0.314	0.000	0.000	0.000	0.000
36	A	46	GLY	0	0.037	0.018	22.766	-0.537	-0.537	0.000	0.000	0.000	0.000
37	A	47	GLU	-1	-0.781	-0.875	21.494	-14.757	-14.757	0.000	0.000	0.000	0.000
38	A	48	CYS	0	-0.049	-0.006	18.346	0.477	0.477	0.000	0.000	0.000	0.000
39	A	49	SER	0	0.006	0.001	18.958	-0.963	-0.963	0.000	0.000	0.000	0.000
40	A	50	GLY	0	0.069	0.041	17.693	0.795	0.795	0.000	0.000	0.000	0.000
41	A	51	LEU	0	-0.017	-0.013	15.685	0.408	0.408	0.000	0.000	0.000	0.000
42	A	52	LEU	0	-0.019	-0.021	17.891	0.465	0.465	0.000	0.000	0.000	0.000
43	A	53	LYS	1	0.933	0.979	21.297	13.725	13.725	0.000	0.000	0.000	0.000
44	A	55	ALA	0	0.027	0.017	20.008	0.141	0.141	0.000	0.000	0.000	0.000
45	A	56	GLU	-1	-0.898	-0.943	20.834	-11.274	-11.274	0.000	0.000	0.000	0.000
46	A	57	ILE	0	-0.006	0.006	21.884	0.364	0.364	0.000	0.000	0.000	0.000
47	A	58	LEU	0	-0.006	0.000	16.690	0.154	0.154	0.000	0.000	0.000	0.000
48	A	59	GLN	0	-0.040	-0.033	20.610	0.716	0.716	0.000	0.000	0.000	0.000
49	A	60	ASN	0	-0.020	-0.013	23.223	0.683	0.683	0.000	0.000	0.000	0.000
50	A	61	MET	0	-0.017	0.008	20.462	0.068	0.068	0.000	0.000	0.000	0.000
51	A	62	GLN	0	-0.047	-0.036	20.415	0.259	0.259	0.000	0.000	0.000	0.000
52	A	63	ALA	0	-0.025	-0.006	22.679	0.335	0.335	0.000	0.000	0.000	0.000
53	A	64	TYR	0	0.051	0.023	25.885	0.221	0.221	0.000	0.000	0.000	0.000
54	A	65	HIS	0	0.045	0.012	20.800	-0.122	-0.122	0.000	0.000	0.000	0.000
55	A	66	GLN	0	-0.081	-0.058	23.169	0.274	0.274	0.000	0.000	0.000	0.000
56	A	67	ASN	0	-0.114	-0.058	26.276	0.362	0.362	0.000	0.000	0.000	0.000
57	A	68	GLU	-1	-0.918	-0.950	29.201	-8.825	-8.825	0.000	0.000	0.000	0.000
58	A	69	LEU	0	-0.098	-0.037	25.392	0.087	0.087	0.000	0.000	0.000	0.000
59	A	70	ASP	-1	-0.913	-0.933	27.937	-9.510	-9.510	0.000	0.000	0.000	0.000
60	A	71	PHE	0	-0.027	-0.020	22.732	-0.294	-0.294	0.000	0.000	0.000	0.000
61	A	72	ASN	0	0.003	-0.005	22.191	0.343	0.343	0.000	0.000	0.000	0.000
62	A	73	ASP	-1	-0.783	-0.881	18.595	-15.035	-15.035	0.000	0.000	0.000	0.000
63	A	74	ILE	0	-0.028	0.005	16.850	0.157	0.157	0.000	0.000	0.000	0.000
64	A	75	SER	0	0.027	0.010	17.797	-0.607	-0.607	0.000	0.000	0.000	0.000
65	A	76	TYR	0	0.006	-0.003	14.423	0.065	0.065	0.000	0.000	0.000	0.000
66	A	77	ASN	0	-0.013	0.006	10.824	0.514	0.514	0.000	0.000	0.000	0.000
67	A	78	PHE	0	0.000	-0.008	7.539	-1.089	-1.089	0.000	0.000	0.000	0.000
68	A	79	LEU	0	0.026	0.018	10.994	1.309	1.309	0.000	0.000	0.000	0.000
69	A	80	ILE	0	-0.022	-0.004	9.092	-1.880	-1.880	0.000	0.000	0.000	0.000
70	A	81	GLY	0	0.054	0.034	12.785	1.699	1.699	0.000	0.000	0.000	0.000
71	A	82	ASN	0	0.005	-0.010	14.724	-1.853	-1.853	0.000	0.000	0.000	0.000
72	A	83	ASP	-1	-0.880	-0.940	15.199	-19.119	-19.119	0.000	0.000	0.000	0.000
73	A	84	GLY	0	0.010	0.011	11.389	-1.252	-1.252	0.000	0.000	0.000	0.000
74	A	85	ILE	0	-0.091	-0.044	9.935	-3.370	-3.370	0.000	0.000	0.000	0.000
75	A	86	VAL	0	0.052	0.030	6.843	1.718	1.718	0.000	0.000	0.000	0.000
76	A	87	TYR	0	0.013	-0.015	9.960	0.216	0.216	0.000	0.000	0.000	0.000
77	A	88	GLU	-1	-0.860	-0.929	11.040	-21.635	-21.635	0.000	0.000	0.000	0.000
78	A	89	GLY	0	0.010	-0.008	11.864	1.332	1.332	0.000	0.000	0.000	0.000
79	A	90	THR	0	-0.011	-0.035	14.477	0.808	0.808	0.000	0.000	0.000	0.000
80	A	91	GLY	0	0.022	0.013	11.077	0.341	0.341	0.000	0.000	0.000	0.000
82	A	93	GLY	0	0.032	0.017	10.018	1.132	1.132	0.000	0.000	0.000	0.000
83	A	94	LEU	0	-0.030	-0.001	12.732	1.418	1.418	0.000	0.000	0.000	0.000
84	A	95	ARG	1	0.873	0.930	15.092	11.650	11.650	0.000	0.000	0.000	0.000
85	A	96	GLY	0	0.008	0.021	16.872	0.309	0.309	0.000	0.000	0.000	0.000
86	A	97	ALA	0	-0.036	-0.031	17.965	0.562	0.562	0.000	0.000	0.000	0.000
87	A	98	HIS	0	-0.005	0.035	15.308	0.702	0.702	0.000	0.000	0.000	0.000
88	A	99	THR	0	0.020	-0.020	18.140	0.252	0.252	0.000	0.000	0.000	0.000
89	A	100	TYR	0	-0.013	-0.008	20.751	-0.228	-0.228	0.000	0.000	0.000	0.000
90	A	101	GLY	0	0.016	0.012	22.977	-0.179	-0.179	0.000	0.000	0.000	0.000
91	A	102	TYR	0	-0.025	-0.059	17.745	-0.369	-0.369	0.000	0.000	0.000	0.000
92	A	103	ASN	0	-0.005	0.019	17.507	-1.171	-1.171	0.000	0.000	0.000	0.000
93	A	104	ALA	0	-0.008	-0.020	17.484	-0.486	-0.486	0.000	0.000	0.000	0.000
94	A	105	ILE	0	0.003	0.008	17.132	-0.175	-0.175	0.000	0.000	0.000	0.000
95	A	106	GLY	0	0.031	0.009	14.047	-0.405	-0.405	0.000	0.000	0.000	0.000
96	A	107	THR	0	-0.013	0.000	8.376	0.168	0.168	0.000	0.000	0.000	0.000
97	A	108	GLY	0	-0.008	0.005	11.759	-0.341	-0.341	0.000	0.000	0.000	0.000
98	A	109	ILE	0	-0.011	-0.025	7.995	-0.933	-0.933	0.000	0.000	0.000	0.000
99	A	110	ALA	0	-0.008	0.005	12.053	0.723	0.723	0.000	0.000	0.000	0.000
100	A	111	PHE	0	0.011	-0.001	11.883	-1.013	-1.013	0.000	0.000	0.000	0.000
101	A	112	ILE	0	-0.009	-0.024	15.705	1.205	1.205	0.000	0.000	0.000	0.000
102	A	113	GLY	0	0.030	0.003	18.204	-0.046	-0.046	0.000	0.000	0.000	0.000
103	A	114	ASN	0	-0.043	-0.018	21.611	-0.154	-0.154	0.000	0.000	0.000	0.000
104	A	115	PHE	0	0.026	-0.005	19.051	-0.046	-0.046	0.000	0.000	0.000	0.000
105	A	116	VAL	0	0.000	0.008	22.418	-0.186	-0.186	0.000	0.000	0.000	0.000
106	A	117	ASP	-1	-0.888	-0.925	25.373	-11.092	-11.092	0.000	0.000	0.000	0.000
107	A	118	LYS	1	0.806	0.894	23.092	14.056	14.056	0.000	0.000	0.000	0.000
108	A	119	LEU	0	0.053	0.027	18.348	-0.201	-0.201	0.000	0.000	0.000	0.000
109	A	120	PRO	0	-0.030	-0.012	16.059	0.422	0.422	0.000	0.000	0.000	0.000
110	A	121	SER	0	-0.003	-0.021	15.841	-0.156	-0.156	0.000	0.000	0.000	0.000
111	A	122	ASP	-1	-0.833	-0.922	14.751	-20.505	-20.505	0.000	0.000	0.000	0.000
112	A	123	ALA	0	-0.026	-0.011	11.813	-2.097	-2.097	0.000	0.000	0.000	0.000
113	A	124	ALA	0	-0.002	-0.006	10.784	-3.287	-3.287	0.000	0.000	0.000	0.000
114	A	125	LEU	0	0.011	0.001	11.085	-2.278	-2.278	0.000	0.000	0.000	0.000
115	A	126	GLN	0	-0.060	-0.028	6.543	2.810	2.810	0.000	0.000	0.000	0.000
116	A	127	ALA	0	0.021	0.012	6.791	-5.619	-5.619	0.000	0.000	0.000	0.000
117	A	128	ALA	0	0.002	-0.007	6.396	-5.888	-5.888	0.000	0.000	0.000	0.000
118	A	129	LYS	1	0.925	0.982	5.813	23.045	23.045	0.000	0.000	0.000	0.000
127	A	139	GLY	0	0.020	0.026	5.776	1.131	1.131	0.000	0.000	0.000	0.000
128	A	140	GLU	-1	-0.853	-0.912	6.299	-21.628	-21.628	0.000	0.000	0.000	0.000
129	A	141	LEU	0	-0.057	-0.025	5.547	0.960	0.960	0.000	0.000	0.000	0.000
130	A	142	SER	0	-0.031	-0.040	7.611	0.403	0.403	0.000	0.000	0.000	0.000
131	A	143	GLU	-1	-0.903	-0.973	7.476	-19.667	-19.667	0.000	0.000	0.000	0.000
132	A	144	ASP	-1	-0.899	-0.933	8.661	-17.222	-17.222	0.000	0.000	0.000	0.000
133	A	145	TYR	0	-0.051	-0.010	5.472	-0.840	-0.840	0.000	0.000	0.000	0.000
134	A	146	ALA	0	0.038	0.022	10.868	-0.425	-0.425	0.000	0.000	0.000	0.000
135	A	147	LEU	0	-0.020	-0.024	9.957	-0.858	-0.858	0.000	0.000	0.000	0.000
136	A	148	ILE	0	0.001	0.001	12.478	1.035	1.035	0.000	0.000	0.000	0.000
137	A	149	ALA	0	0.050	0.030	15.498	-0.989	-0.989	0.000	0.000	0.000	0.000
138	A	150	GLY	0	0.014	0.000	18.074	0.507	0.507	0.000	0.000	0.000	0.000
139	A	151	SER	0	-0.022	-0.024	20.377	0.546	0.546	0.000	0.000	0.000	0.000
140	A	152	GLN	0	-0.016	0.007	18.667	-0.191	-0.191	0.000	0.000	0.000	0.000
141	A	153	VAL	0	-0.045	-0.021	20.436	0.316	0.316	0.000	0.000	0.000	0.000
142	A	154	ILE	0	-0.030	-0.007	22.608	0.351	0.351	0.000	0.000	0.000	0.000
143	A	155	SER	0	0.024	0.003	25.576	-0.092	-0.092	0.000	0.000	0.000	0.000
144	A	156	THR	0	-0.031	-0.004	23.195	-0.009	-0.009	0.000	0.000	0.000	0.000
145	A	157	GLN	0	0.048	0.017	25.817	-0.136	-0.136	0.000	0.000	0.000	0.000
146	A	158	SER	0	-0.017	0.001	20.224	-0.523	-0.523	0.000	0.000	0.000	0.000
147	A	159	PRO	0	-0.004	-0.003	17.605	0.295	0.295	0.000	0.000	0.000	0.000
148	A	160	GLY	0	0.062	0.016	19.904	-0.216	-0.216	0.000	0.000	0.000	0.000
149	A	161	LEU	0	0.016	0.003	21.727	-0.462	-0.462	0.000	0.000	0.000	0.000
150	A	162	THR	0	-0.025	-0.028	22.079	-0.161	-0.161	0.000	0.000	0.000	0.000
151	A	163	LEU	0	-0.003	-0.004	15.448	-0.521	-0.521	0.000	0.000	0.000	0.000
152	A	164	TYR	0	-0.013	-0.022	17.678	-0.870	-0.870	0.000	0.000	0.000	0.000
153	A	165	ASN	0	-0.008	-0.007	18.925	-0.070	-0.070	0.000	0.000	0.000	0.000
154	A	166	GLU	-1	-0.820	-0.893	14.691	-19.922	-19.922	0.000	0.000	0.000	0.000
155	A	167	ILE	0	-0.045	-0.040	13.455	-0.690	-0.690	0.000	0.000	0.000	0.000
156	A	168	GLN	0	-0.048	-0.026	14.536	0.013	0.013	0.000	0.000	0.000	0.000
157	A	169	GLU	-1	-0.922	-0.949	16.281	-14.468	-14.468	0.000	0.000	0.000	0.000
158	A	170	TRP	0	-0.141	-0.077	9.244	-2.597	-2.597	0.000	0.000	0.000	0.000
159	A	171	PRO	0	0.008	-0.010	9.093	0.767	0.767	0.000	0.000	0.000	0.000
160	A	172	HIS	1	0.812	0.891	6.787	22.223	22.223	0.000	0.000	0.000	0.000
161	A	173	TRP	0	-0.008	0.027	11.277	0.735	0.735	0.000	0.000	0.000	0.000
162	A	174	LEU	0	0.004	0.010	14.218	0.643	0.643	0.000	0.000	0.000	0.000
163	A	175	SER	0	0.032	0.016	17.062	0.117	0.117	0.000	0.000	0.000	0.000
164	A	176	ASN	0	-0.028	-0.024	20.518	-0.052	-0.052	0.000	0.000	0.000	0.000
165	A	177	PRO	0	-0.012	0.009	19.240	0.095	0.095	0.000	0.000	0.000	0.000
166	A	178	HIS	0	0.017	0.011	21.158	0.526	0.526	0.000	0.000	0.000	0.000
167	A	179	HIS	0	0.012	0.014	23.131	-0.336	-0.336	0.000	0.000	0.000	0.000
168	A	180	HIS	0	0.002	0.004	25.721	0.483	0.483	0.000	0.000	0.000	0.000
169	A	181	HIS	0	0.047	0.026	28.741	-0.240	-0.240	0.000	0.000	0.000	0.000
170	A	182	HIS	0	-0.032	-0.024	28.356	-0.055	-0.055	0.000	0.000	0.000	0.000
171	A	183	HIS	-1	-0.931	-0.947	31.991	-8.134	-8.134	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:11:CYS)