FMO DATABASE

FMODB ID: 5R17Z

Calculation Name: 1XFS-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1XFS

Chain ID: A

ChEMBL ID:

UniProt ID: Q82XK1

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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1533474.275157
FMO2-HF: Nuclear repulsion	1470981.628072
FMO2-HF: Total energy	-62492.647085
FMO2-MP2: Total energy	-62672.349809

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:6:ILE)

Summations of interaction energy for fragment #1(A:6:ILE)

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.
-63.464	-56.314	7.591	-5.949	-8.793	-0.056

Interaction energy analysis for fragmet #1(A:6:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.784 / q_NPA : 0.884

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	8	ALA	0	0.001	-0.003	3.648	2.979	4.932	0.002	-0.709	-1.245	-0.003
4	A	9	GLU	-1	-0.850	-0.935	4.730	-21.924	-21.777	-0.001	-0.007	-0.139	0.000
6	A	11	ASP	-1	-0.805	-0.905	2.333	-76.992	-73.483	5.847	-4.594	-4.763	-0.051
7	A	12	LEU	0	-0.035	-0.002	4.123	2.005	2.184	0.001	-0.033	-0.148	0.000
8	A	13	MET	0	-0.024	-0.020	2.624	-4.293	-3.127	0.497	-0.314	-1.349	-0.001
9	A	14	LEU	0	0.009	0.008	4.551	2.558	2.580	-0.001	-0.012	-0.009	0.000
116	A	132	CYS	0	-0.046	-0.029	2.989	-2.786	-2.746	1.247	-0.273	-1.015	-0.001
118	A	134	MET	0	0.015	0.004	4.602	-0.491	-0.357	-0.001	-0.007	-0.125	0.000
5	A	10	LEU	0	-0.022	0.001	6.075	4.213	4.213	0.000	0.000	0.000	0.000
10	A	15	LYS	1	0.877	0.945	8.194	21.027	21.027	0.000	0.000	0.000	0.000
11	A	16	ARG	1	0.857	0.908	9.668	16.995	16.995	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.808	-0.891	13.443	-18.790	-18.790	0.000	0.000	0.000	0.000
13	A	18	LEU	0	0.019	0.018	16.104	0.355	0.355	0.000	0.000	0.000	0.000
14	A	19	ALA	0	-0.012	0.001	19.290	0.012	0.012	0.000	0.000	0.000	0.000
15	A	20	VAL	0	0.008	-0.009	21.563	0.587	0.587	0.000	0.000	0.000	0.000
16	A	21	PRO	0	-0.019	0.016	21.603	-0.561	-0.561	0.000	0.000	0.000	0.000
17	A	22	VAL	0	0.056	0.019	18.253	0.050	0.050	0.000	0.000	0.000	0.000
18	A	23	ASN	0	0.076	0.043	20.750	-0.430	-0.430	0.000	0.000	0.000	0.000
19	A	24	LEU	0	-0.018	-0.009	23.460	0.023	0.023	0.000	0.000	0.000	0.000
20	A	25	VAL	0	0.007	-0.003	17.223	-0.079	-0.079	0.000	0.000	0.000	0.000
21	A	26	TRP	0	-0.023	-0.004	16.187	-0.643	-0.643	0.000	0.000	0.000	0.000
22	A	27	ARG	1	0.865	0.913	20.270	10.449	10.449	0.000	0.000	0.000	0.000
23	A	28	GLY	0	0.015	0.008	21.869	0.138	0.138	0.000	0.000	0.000	0.000
24	A	29	LEU	0	-0.040	-0.022	15.416	-0.232	-0.232	0.000	0.000	0.000	0.000
25	A	30	THR	0	-0.018	-0.026	19.177	-0.178	-0.178	0.000	0.000	0.000	0.000
26	A	31	GLU	-1	-0.782	-0.856	21.706	-10.416	-10.416	0.000	0.000	0.000	0.000
27	A	32	PRO	0	-0.001	-0.022	25.048	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	33	GLU	-1	-0.835	-0.908	26.300	-9.419	-9.419	0.000	0.000	0.000	0.000
29	A	34	LEU	0	0.010	0.009	24.759	0.178	0.178	0.000	0.000	0.000	0.000
30	A	35	LEU	0	0.026	0.007	19.838	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	36	LYS	1	0.788	0.880	23.316	9.542	9.542	0.000	0.000	0.000	0.000
32	A	37	LYS	1	0.876	0.946	25.726	9.810	9.810	0.000	0.000	0.000	0.000
33	A	38	TRP	0	-0.055	-0.030	16.491	-0.161	-0.161	0.000	0.000	0.000	0.000
34	A	39	PHE	0	0.000	0.000	16.518	-0.403	-0.403	0.000	0.000	0.000	0.000
35	A	40	VAL	0	0.024	0.020	18.886	-0.557	-0.557	0.000	0.000	0.000	0.000
36	A	41	PRO	0	-0.010	0.017	18.804	0.336	0.336	0.000	0.000	0.000	0.000
37	A	42	LYS	1	0.980	0.994	21.306	10.804	10.804	0.000	0.000	0.000	0.000
38	A	43	PRO	0	-0.036	-0.022	24.484	-0.181	-0.181	0.000	0.000	0.000	0.000
39	A	44	TRP	0	0.021	0.011	23.370	0.225	0.225	0.000	0.000	0.000	0.000
40	A	45	SER	0	-0.023	-0.016	25.551	0.139	0.139	0.000	0.000	0.000	0.000
41	A	46	ILE	0	0.003	0.001	22.374	-0.236	-0.236	0.000	0.000	0.000	0.000
42	A	47	SER	0	-0.044	-0.022	26.717	0.412	0.412	0.000	0.000	0.000	0.000
43	A	48	ASP	-1	-0.858	-0.935	28.314	-9.580	-9.580	0.000	0.000	0.000	0.000
44	A	49	CYS	0	-0.048	-0.013	24.658	-0.587	-0.587	0.000	0.000	0.000	0.000
45	A	50	ARG	1	0.913	0.966	25.776	10.227	10.227	0.000	0.000	0.000	0.000
46	A	51	VAL	0	0.047	0.022	22.565	-0.454	-0.454	0.000	0.000	0.000	0.000
47	A	52	ASP	-1	-0.877	-0.913	24.391	-10.968	-10.968	0.000	0.000	0.000	0.000
48	A	53	LEU	0	0.035	0.014	20.684	-0.508	-0.508	0.000	0.000	0.000	0.000
49	A	54	ARG	1	0.815	0.898	22.940	12.053	12.053	0.000	0.000	0.000	0.000
50	A	55	PRO	0	0.022	0.008	19.780	-0.206	-0.206	0.000	0.000	0.000	0.000
51	A	56	GLY	0	-0.002	-0.006	20.659	0.711	0.711	0.000	0.000	0.000	0.000
52	A	57	GLY	0	-0.010	-0.007	22.307	0.692	0.692	0.000	0.000	0.000	0.000
53	A	58	GLU	-1	-0.897	-0.961	21.831	-12.086	-12.086	0.000	0.000	0.000	0.000
54	A	59	PHE	0	-0.022	-0.005	17.443	0.250	0.250	0.000	0.000	0.000	0.000
55	A	60	TYR	0	-0.023	-0.019	21.700	-0.208	-0.208	0.000	0.000	0.000	0.000
56	A	61	THR	0	-0.014	-0.018	22.022	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	62	VAL	0	-0.017	0.001	24.539	0.035	0.035	0.000	0.000	0.000	0.000
58	A	63	MET	0	0.002	0.019	19.972	0.031	0.031	0.000	0.000	0.000	0.000
59	A	64	GLN	0	0.000	0.012	24.976	0.434	0.434	0.000	0.000	0.000	0.000
60	A	65	ASP	-1	-0.688	-0.825	26.197	-10.202	-10.202	0.000	0.000	0.000	0.000
61	A	66	PRO	0	-0.049	-0.048	26.805	0.286	0.286	0.000	0.000	0.000	0.000
62	A	67	GLU	-1	-0.974	-0.977	29.105	-9.344	-9.344	0.000	0.000	0.000	0.000
63	A	68	GLY	0	-0.039	-0.009	30.982	0.319	0.319	0.000	0.000	0.000	0.000
64	A	69	ASN	0	-0.096	-0.057	29.106	0.333	0.333	0.000	0.000	0.000	0.000
65	A	70	LYS	1	0.845	0.894	28.847	8.895	8.895	0.000	0.000	0.000	0.000
66	A	71	PHE	0	0.000	-0.005	24.572	0.029	0.029	0.000	0.000	0.000	0.000
67	A	72	PRO	0	-0.019	-0.002	25.384	-0.224	-0.224	0.000	0.000	0.000	0.000
68	A	73	ASN	0	0.024	0.005	21.032	-0.039	-0.039	0.000	0.000	0.000	0.000
69	A	74	SER	0	-0.022	-0.031	22.367	0.164	0.164	0.000	0.000	0.000	0.000
70	A	75	GLY	0	0.042	0.026	19.022	-0.484	-0.484	0.000	0.000	0.000	0.000
71	A	76	CYS	0	-0.099	-0.020	18.378	0.943	0.943	0.000	0.000	0.000	0.000
72	A	77	PHE	0	0.051	0.020	17.192	-1.249	-1.249	0.000	0.000	0.000	0.000
73	A	78	LEU	0	-0.051	-0.034	13.478	0.484	0.484	0.000	0.000	0.000	0.000
74	A	79	GLU	-1	-0.804	-0.872	13.150	-22.112	-22.112	0.000	0.000	0.000	0.000
75	A	80	VAL	0	-0.003	-0.002	16.392	-0.303	-0.303	0.000	0.000	0.000	0.000
76	A	81	THR	0	-0.038	-0.035	16.001	1.044	1.044	0.000	0.000	0.000	0.000
77	A	82	ASP	-1	-0.820	-0.923	17.872	-13.995	-13.995	0.000	0.000	0.000	0.000
78	A	83	GLU	-1	-0.924	-0.981	19.336	-12.917	-12.917	0.000	0.000	0.000	0.000
79	A	84	LYS	1	0.896	0.963	13.365	20.597	20.597	0.000	0.000	0.000	0.000
80	A	85	ARG	1	0.733	0.814	10.055	24.819	24.819	0.000	0.000	0.000	0.000
81	A	86	LEU	0	0.012	0.029	13.266	1.049	1.049	0.000	0.000	0.000	0.000
82	A	87	ILE	0	-0.019	-0.005	10.851	-1.587	-1.587	0.000	0.000	0.000	0.000
83	A	88	TRP	0	0.049	0.016	12.823	1.334	1.334	0.000	0.000	0.000	0.000
84	A	89	THR	0	-0.032	-0.020	12.819	-1.164	-1.164	0.000	0.000	0.000	0.000
85	A	90	SER	0	0.062	0.028	14.605	0.749	0.749	0.000	0.000	0.000	0.000
86	A	91	ALA	0	0.010	0.007	15.256	0.753	0.753	0.000	0.000	0.000	0.000
87	A	92	LEU	0	-0.048	-0.019	17.124	0.650	0.650	0.000	0.000	0.000	0.000
88	A	93	VAL	0	0.038	0.013	19.394	-0.215	-0.215	0.000	0.000	0.000	0.000
89	A	94	LYS	1	0.975	0.982	22.238	10.405	10.405	0.000	0.000	0.000	0.000
90	A	95	ASN	0	-0.061	-0.037	24.609	0.144	0.144	0.000	0.000	0.000	0.000
91	A	96	TYR	0	0.049	0.017	19.602	0.028	0.028	0.000	0.000	0.000	0.000
92	A	97	ARG	1	0.951	1.001	22.430	10.870	10.870	0.000	0.000	0.000	0.000
93	A	98	PRO	0	0.000	-0.011	21.654	-0.318	-0.318	0.000	0.000	0.000	0.000
94	A	99	ALA	0	0.002	0.009	20.612	0.673	0.673	0.000	0.000	0.000	0.000
95	A	100	VAL	0	-0.045	-0.028	22.488	0.126	0.126	0.000	0.000	0.000	0.000
96	A	101	PRO	-1	-0.939	-0.952	23.085	-12.319	-12.319	0.000	0.000	0.000	0.000
97	A	113	VAL	0	-0.029	-0.021	14.565	0.046	0.046	0.000	0.000	0.000	0.000
98	A	114	MET	0	-0.023	-0.012	10.363	-1.654	-1.654	0.000	0.000	0.000	0.000
99	A	115	THR	0	-0.004	0.003	9.521	2.442	2.442	0.000	0.000	0.000	0.000
100	A	116	ALA	0	-0.008	0.022	8.539	-2.860	-2.860	0.000	0.000	0.000	0.000
101	A	117	VAL	0	0.022	-0.006	6.936	1.259	1.259	0.000	0.000	0.000	0.000
102	A	118	ILE	0	-0.017	-0.001	7.892	-1.406	-1.406	0.000	0.000	0.000	0.000
103	A	119	GLU	-1	-0.846	-0.905	8.299	-29.911	-29.911	0.000	0.000	0.000	0.000
104	A	120	LEU	0	-0.023	-0.008	10.832	0.525	0.525	0.000	0.000	0.000	0.000
105	A	121	GLN	0	-0.007	-0.016	13.827	-0.128	-0.128	0.000	0.000	0.000	0.000
106	A	122	PRO	0	0.031	0.030	15.659	0.182	0.182	0.000	0.000	0.000	0.000
107	A	123	THR	0	0.008	-0.013	18.006	-0.122	-0.122	0.000	0.000	0.000	0.000
108	A	124	SER	0	-0.008	-0.013	20.620	0.256	0.256	0.000	0.000	0.000	0.000
109	A	125	SER	0	-0.026	-0.015	22.770	0.393	0.393	0.000	0.000	0.000	0.000
110	A	126	GLY	0	-0.006	0.002	21.910	0.328	0.328	0.000	0.000	0.000	0.000
111	A	127	THR	0	-0.029	-0.022	16.334	-0.180	-0.180	0.000	0.000	0.000	0.000
112	A	128	ARG	1	0.852	0.930	12.289	18.579	18.579	0.000	0.000	0.000	0.000
113	A	129	TYR	0	0.050	0.016	11.265	-0.592	-0.592	0.000	0.000	0.000	0.000
114	A	130	THR	0	-0.014	-0.025	6.045	-0.377	-0.377	0.000	0.000	0.000	0.000
115	A	131	ALA	0	0.033	0.036	7.946	-0.304	-0.304	0.000	0.000	0.000	0.000
117	A	133	ALA	0	0.032	0.021	5.262	2.868	2.868	0.000	0.000	0.000	0.000
119	A	135	HIS	1	0.820	0.886	6.505	32.560	32.560	0.000	0.000	0.000	0.000
120	A	136	ASN	0	0.033	0.012	9.474	-2.068	-2.068	0.000	0.000	0.000	0.000
121	A	137	THR	0	0.011	0.006	12.025	0.462	0.462	0.000	0.000	0.000	0.000
122	A	138	PRO	0	0.072	0.032	10.883	-0.304	-0.304	0.000	0.000	0.000	0.000
123	A	139	GLY	0	-0.014	0.007	11.900	0.423	0.423	0.000	0.000	0.000	0.000
124	A	140	GLN	0	0.044	0.012	13.210	0.206	0.206	0.000	0.000	0.000	0.000
125	A	141	ARG	1	0.757	0.890	6.894	27.844	27.844	0.000	0.000	0.000	0.000
126	A	142	LYS	1	0.881	0.935	10.194	18.853	18.853	0.000	0.000	0.000	0.000
127	A	143	LEU	0	0.049	0.023	12.714	0.542	0.542	0.000	0.000	0.000	0.000
128	A	144	HIS	0	0.018	0.023	10.636	-0.631	-0.631	0.000	0.000	0.000	0.000
129	A	145	GLU	-1	-0.806	-0.905	10.337	-22.212	-22.212	0.000	0.000	0.000	0.000
130	A	146	GLU	-1	-0.936	-0.974	12.480	-15.001	-15.001	0.000	0.000	0.000	0.000
131	A	147	MET	0	-0.045	-0.014	15.430	1.023	1.023	0.000	0.000	0.000	0.000
132	A	148	GLY	0	0.053	0.036	15.598	0.347	0.347	0.000	0.000	0.000	0.000
133	A	149	PHE	0	-0.067	-0.029	7.434	-0.117	-0.117	0.000	0.000	0.000	0.000
134	A	150	HIS	0	-0.006	-0.011	10.123	0.683	0.683	0.000	0.000	0.000	0.000
135	A	151	GLU	-1	-0.877	-0.933	12.171	-13.309	-13.309	0.000	0.000	0.000	0.000
136	A	152	GLY	0	0.048	0.033	15.626	0.523	0.523	0.000	0.000	0.000	0.000
137	A	153	TRP	0	0.024	-0.001	10.326	-0.248	-0.248	0.000	0.000	0.000	0.000
138	A	154	GLY	0	0.025	0.011	13.893	0.260	0.260	0.000	0.000	0.000	0.000
139	A	155	THR	0	-0.025	-0.015	14.960	0.747	0.747	0.000	0.000	0.000	0.000
140	A	156	THR	0	-0.051	-0.026	15.793	0.228	0.228	0.000	0.000	0.000	0.000
141	A	157	ILE	0	-0.003	-0.014	13.576	0.434	0.434	0.000	0.000	0.000	0.000
142	A	158	THR	0	0.015	0.009	17.051	0.150	0.150	0.000	0.000	0.000	0.000
143	A	159	GLN	0	-0.029	-0.015	20.206	0.835	0.835	0.000	0.000	0.000	0.000
144	A	160	LEU	0	0.009	0.016	17.259	0.455	0.455	0.000	0.000	0.000	0.000
145	A	161	GLU	-1	-0.830	-0.926	20.277	-12.398	-12.398	0.000	0.000	0.000	0.000
146	A	162	GLU	-1	-0.980	-0.990	22.031	-10.107	-10.107	0.000	0.000	0.000	0.000
147	A	163	LEU	0	-0.010	-0.004	24.143	0.400	0.400	0.000	0.000	0.000	0.000
148	A	164	LEU	0	-0.012	-0.011	21.459	0.353	0.353	0.000	0.000	0.000	0.000
149	A	165	LYS	1	0.834	0.930	23.780	11.810	11.810	0.000	0.000	0.000	0.000
150	A	166	GLN	0	-0.053	-0.027	27.539	0.202	0.202	0.000	0.000	0.000	0.000
151	A	167	GLU	-1	-0.879	-0.945	28.724	-9.044	-9.044	0.000	0.000	0.000	0.000
152	A	168	LYS	1	0.894	0.954	28.088	10.012	10.012	0.000	0.000	0.000	0.000
153	A	169	ALA	0	-0.069	-0.042	30.082	0.010	0.010	0.000	0.000	0.000	0.000
154	A	170	TYR	-1	-0.948	-0.949	32.055	-8.804	-8.804	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ILE)