FMO DATABASE

FMODB ID: 3MJ4L

Calculation Name: 1XTD-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1XTD

Chain ID: A

ChEMBL ID:

UniProt ID: E9AXF0

Base Structure: X-ray

Registration Date: 2025-10-05

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1178384.443054
FMO2-HF: Nuclear repulsion	1121670.472699
FMO2-HF: Total energy	-56713.970355
FMO2-MP2: Total energy	-56877.032311

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:24:ASN)

Summations of interaction energy for fragment #1(A:24:ASN)

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.
-50.823	-47.818	3.827	-3.1	-3.732	0.015

Interaction energy analysis for fragmet #1(A:24:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.857 / 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	26	SER	0	0.005	0.019	2.047	-0.921	1.954	3.825	-3.088	-3.613	0.015
4	A	27	LYS	1	0.958	0.968	3.982	29.650	29.780	0.002	-0.012	-0.119	0.000
5	A	28	THR	0	-0.056	-0.041	6.950	1.622	1.622	0.000	0.000	0.000	0.000
6	A	29	TYR	0	-0.021	0.001	6.994	-2.366	-2.366	0.000	0.000	0.000	0.000
7	A	30	PRO	0	0.057	0.038	8.501	1.479	1.479	0.000	0.000	0.000	0.000
8	A	31	MET	0	-0.034	-0.019	11.751	0.270	0.270	0.000	0.000	0.000	0.000
9	A	32	ALA	0	0.043	0.031	15.187	0.337	0.337	0.000	0.000	0.000	0.000
10	A	33	ALA	0	0.054	0.018	18.612	0.250	0.250	0.000	0.000	0.000	0.000
11	A	34	GLY	0	-0.043	-0.033	21.016	0.341	0.341	0.000	0.000	0.000	0.000
12	A	35	ALA	0	-0.029	-0.002	19.750	0.375	0.375	0.000	0.000	0.000	0.000
13	A	36	LEU	0	-0.005	0.007	19.050	-0.033	-0.033	0.000	0.000	0.000	0.000
14	A	37	LYS	1	0.896	0.937	22.002	12.230	12.230	0.000	0.000	0.000	0.000
15	A	38	LYS	1	0.900	0.944	23.896	8.761	8.761	0.000	0.000	0.000	0.000
16	A	39	GLY	0	0.016	0.015	25.192	0.110	0.110	0.000	0.000	0.000	0.000
17	A	40	GLY	0	-0.018	-0.002	21.137	-0.296	-0.296	0.000	0.000	0.000	0.000
18	A	41	TYR	0	0.002	-0.007	16.990	0.407	0.407	0.000	0.000	0.000	0.000
19	A	42	VAL	0	-0.001	-0.008	17.200	-0.155	-0.155	0.000	0.000	0.000	0.000
20	A	43	CYS	0	-0.038	-0.010	14.025	-0.216	-0.216	0.000	0.000	0.000	0.000
21	A	44	ILE	0	0.030	0.016	16.745	0.225	0.225	0.000	0.000	0.000	0.000
22	A	45	ASN	0	-0.008	-0.010	19.670	-0.217	-0.217	0.000	0.000	0.000	0.000
23	A	46	GLY	0	0.017	0.013	15.640	-0.053	-0.053	0.000	0.000	0.000	0.000
24	A	47	ARG	1	0.874	0.912	15.771	13.318	13.318	0.000	0.000	0.000	0.000
25	A	48	PRO	0	0.010	0.017	15.391	0.052	0.052	0.000	0.000	0.000	0.000
26	A	49	CYS	0	-0.002	0.003	17.184	0.747	0.747	0.000	0.000	0.000	0.000
27	A	50	LYS	1	0.931	0.963	19.840	11.450	11.450	0.000	0.000	0.000	0.000
28	A	51	VAL	0	-0.015	-0.008	21.955	0.395	0.395	0.000	0.000	0.000	0.000
29	A	52	ILE	0	-0.012	-0.007	24.472	0.132	0.132	0.000	0.000	0.000	0.000
30	A	53	ASP	-1	-0.901	-0.951	28.180	-8.633	-8.633	0.000	0.000	0.000	0.000
31	A	54	LEU	0	-0.008	-0.002	25.135	-0.313	-0.313	0.000	0.000	0.000	0.000
32	A	55	SER	0	-0.018	0.000	28.724	0.345	0.345	0.000	0.000	0.000	0.000
33	A	56	VAL	0	0.037	0.007	28.492	-0.331	-0.331	0.000	0.000	0.000	0.000
34	A	57	SER	0	-0.032	0.002	31.020	0.220	0.220	0.000	0.000	0.000	0.000
35	A	58	LYS	1	0.962	0.963	32.590	7.479	7.479	0.000	0.000	0.000	0.000
36	A	59	THR	0	0.023	0.007	32.931	-0.061	-0.061	0.000	0.000	0.000	0.000
37	A	60	GLY	0	0.072	0.028	33.770	-0.097	-0.097	0.000	0.000	0.000	0.000
38	A	61	LYS	1	0.915	0.959	34.553	7.583	7.583	0.000	0.000	0.000	0.000
39	A	62	HIS	0	0.047	0.028	32.025	0.278	0.278	0.000	0.000	0.000	0.000
40	A	63	GLY	0	0.039	0.025	31.942	-0.269	-0.269	0.000	0.000	0.000	0.000
41	A	64	HIS	0	-0.034	-0.022	27.034	-0.378	-0.378	0.000	0.000	0.000	0.000
42	A	65	ALA	0	0.034	0.042	29.227	0.192	0.192	0.000	0.000	0.000	0.000
43	A	66	LYS	1	0.932	0.973	27.977	9.088	9.088	0.000	0.000	0.000	0.000
44	A	67	VAL	0	0.023	0.016	24.764	0.357	0.357	0.000	0.000	0.000	0.000
45	A	68	SER	0	-0.044	-0.033	26.975	-0.075	-0.075	0.000	0.000	0.000	0.000
46	A	69	ILE	0	-0.004	0.000	22.338	0.178	0.178	0.000	0.000	0.000	0.000
47	A	70	VAL	0	0.048	0.028	26.622	0.060	0.060	0.000	0.000	0.000	0.000
48	A	71	ALA	0	-0.001	-0.008	23.152	-0.080	-0.080	0.000	0.000	0.000	0.000
49	A	72	THR	0	0.012	0.010	24.666	0.378	0.378	0.000	0.000	0.000	0.000
50	A	73	ASP	-1	-0.736	-0.832	21.254	-13.485	-13.485	0.000	0.000	0.000	0.000
51	A	74	ILE	0	-0.057	-0.039	17.840	0.383	0.383	0.000	0.000	0.000	0.000
52	A	75	PHE	0	-0.004	0.002	16.987	0.014	0.014	0.000	0.000	0.000	0.000
53	A	76	THR	0	-0.017	-0.025	22.739	0.397	0.397	0.000	0.000	0.000	0.000
54	A	77	GLY	0	0.043	0.035	25.415	0.385	0.385	0.000	0.000	0.000	0.000
55	A	78	ASN	0	-0.035	-0.018	25.729	0.633	0.633	0.000	0.000	0.000	0.000
56	A	79	ARG	1	0.863	0.924	26.142	8.790	8.790	0.000	0.000	0.000	0.000
57	A	80	LEU	0	-0.006	-0.012	22.654	-0.028	-0.028	0.000	0.000	0.000	0.000
58	A	81	GLU	-1	-0.861	-0.923	26.267	-9.135	-9.135	0.000	0.000	0.000	0.000
59	A	82	ASP	-1	-0.850	-0.926	22.054	-12.600	-12.600	0.000	0.000	0.000	0.000
60	A	83	GLN	0	-0.096	-0.058	25.252	0.467	0.467	0.000	0.000	0.000	0.000
61	A	84	ALA	0	0.053	0.041	22.310	-0.237	-0.237	0.000	0.000	0.000	0.000
62	A	85	PRO	0	-0.015	-0.017	23.617	0.388	0.388	0.000	0.000	0.000	0.000
63	A	86	SER	0	-0.010	-0.020	23.377	-0.428	-0.428	0.000	0.000	0.000	0.000
64	A	87	THR	0	-0.013	-0.018	22.325	-0.304	-0.304	0.000	0.000	0.000	0.000
65	A	88	HIS	0	0.003	0.014	18.373	-0.152	-0.152	0.000	0.000	0.000	0.000
66	A	89	ASN	0	-0.037	-0.022	14.849	0.009	0.009	0.000	0.000	0.000	0.000
67	A	90	VAL	0	0.023	0.016	16.296	-0.191	-0.191	0.000	0.000	0.000	0.000
68	A	91	GLU	-1	-0.779	-0.879	10.081	-22.400	-22.400	0.000	0.000	0.000	0.000
69	A	92	VAL	0	-0.019	-0.005	12.486	1.116	1.116	0.000	0.000	0.000	0.000
70	A	93	PRO	0	0.022	0.001	11.556	-1.414	-1.414	0.000	0.000	0.000	0.000
71	A	94	PHE	0	-0.051	-0.035	6.074	0.670	0.670	0.000	0.000	0.000	0.000
72	A	95	VAL	0	-0.030	-0.005	11.127	-0.250	-0.250	0.000	0.000	0.000	0.000
73	A	96	LYS	1	0.896	0.949	11.628	20.889	20.889	0.000	0.000	0.000	0.000
74	A	97	THR	0	-0.004	-0.010	15.228	0.545	0.545	0.000	0.000	0.000	0.000
75	A	98	PHE	0	0.043	0.027	15.520	-0.528	-0.528	0.000	0.000	0.000	0.000
76	A	99	THR	0	-0.038	-0.032	20.938	0.466	0.466	0.000	0.000	0.000	0.000
77	A	100	TYR	0	0.057	0.035	20.834	-0.463	-0.463	0.000	0.000	0.000	0.000
78	A	101	SER	0	-0.045	-0.044	26.598	0.297	0.297	0.000	0.000	0.000	0.000
79	A	102	VAL	0	-0.034	-0.025	29.949	-0.272	-0.272	0.000	0.000	0.000	0.000
80	A	103	LEU	0	-0.018	-0.004	30.809	0.325	0.325	0.000	0.000	0.000	0.000
81	A	104	ASP	-1	-0.820	-0.913	33.326	-8.182	-8.182	0.000	0.000	0.000	0.000
82	A	105	ILE	0	-0.055	-0.026	33.317	-0.345	-0.345	0.000	0.000	0.000	0.000
83	A	106	GLN	0	-0.048	-0.027	34.371	0.360	0.360	0.000	0.000	0.000	0.000
84	A	107	PRO	0	-0.016	-0.007	34.915	-0.228	-0.228	0.000	0.000	0.000	0.000
85	A	108	ASN	0	-0.053	-0.038	32.041	-0.109	-0.109	0.000	0.000	0.000	0.000
86	A	109	GLU	-1	-0.934	-0.963	35.780	-8.021	-8.021	0.000	0.000	0.000	0.000
87	A	110	ASP	-1	-0.853	-0.906	36.546	-8.050	-8.050	0.000	0.000	0.000	0.000
88	A	111	PRO	0	-0.039	-0.042	37.281	-0.147	-0.147	0.000	0.000	0.000	0.000
89	A	112	SER	0	-0.121	-0.066	37.774	0.027	0.027	0.000	0.000	0.000	0.000
90	A	113	LEU	0	-0.011	0.000	31.516	-0.205	-0.205	0.000	0.000	0.000	0.000
91	A	114	PRO	0	-0.015	-0.001	29.692	0.188	0.188	0.000	0.000	0.000	0.000
92	A	115	SER	0	0.009	0.000	32.327	0.026	0.026	0.000	0.000	0.000	0.000
93	A	116	HIS	1	0.869	0.918	30.010	9.791	9.791	0.000	0.000	0.000	0.000
94	A	117	LEU	0	-0.038	-0.023	27.946	0.392	0.392	0.000	0.000	0.000	0.000
95	A	118	SER	0	-0.028	-0.012	28.850	-0.267	-0.267	0.000	0.000	0.000	0.000
96	A	119	LEU	0	-0.051	-0.035	25.422	0.235	0.235	0.000	0.000	0.000	0.000
97	A	120	MET	0	0.050	0.030	27.724	-0.223	-0.223	0.000	0.000	0.000	0.000
98	A	121	ASP	-1	-0.865	-0.943	23.164	-12.919	-12.919	0.000	0.000	0.000	0.000
99	A	122	ASP	-1	-0.971	-0.999	24.587	-12.016	-12.016	0.000	0.000	0.000	0.000
100	A	123	GLU	-1	-1.002	-0.997	21.637	-13.708	-13.708	0.000	0.000	0.000	0.000
101	A	124	GLY	0	-0.074	-0.026	25.928	0.307	0.307	0.000	0.000	0.000	0.000
102	A	125	GLU	-1	-0.955	-0.963	23.204	-12.460	-12.460	0.000	0.000	0.000	0.000
103	A	126	SER	0	-0.062	-0.061	25.997	0.090	0.090	0.000	0.000	0.000	0.000
104	A	127	ARG	1	0.670	0.766	19.240	14.313	14.313	0.000	0.000	0.000	0.000
105	A	128	GLU	-1	-0.792	-0.863	25.295	-10.444	-10.444	0.000	0.000	0.000	0.000
106	A	129	ASP	-1	-0.856	-0.897	21.416	-14.039	-14.039	0.000	0.000	0.000	0.000
107	A	130	LEU	0	-0.034	-0.007	21.215	-0.271	-0.271	0.000	0.000	0.000	0.000
108	A	131	ASP	-1	-0.806	-0.882	25.055	-10.505	-10.505	0.000	0.000	0.000	0.000
109	A	132	MET	0	-0.061	-0.032	27.062	-0.095	-0.095	0.000	0.000	0.000	0.000
110	A	133	PRO	0	-0.048	-0.015	26.808	-0.178	-0.178	0.000	0.000	0.000	0.000
111	A	134	PRO	0	0.014	-0.013	26.320	0.318	0.318	0.000	0.000	0.000	0.000
112	A	135	ASP	-1	-0.905	-0.933	29.259	-9.032	-9.032	0.000	0.000	0.000	0.000
113	A	136	ALA	0	0.084	0.029	31.067	0.039	0.039	0.000	0.000	0.000	0.000
114	A	137	ALA	0	-0.014	0.013	34.460	0.196	0.196	0.000	0.000	0.000	0.000
115	A	138	LEU	0	-0.029	-0.014	28.355	0.120	0.120	0.000	0.000	0.000	0.000
116	A	139	ALA	0	0.011	-0.005	32.131	0.026	0.026	0.000	0.000	0.000	0.000
117	A	140	THR	0	-0.020	-0.019	33.364	0.137	0.137	0.000	0.000	0.000	0.000
118	A	141	GLN	0	-0.021	-0.012	35.332	0.038	0.038	0.000	0.000	0.000	0.000
119	A	142	ILE	0	-0.028	-0.012	30.221	0.060	0.060	0.000	0.000	0.000	0.000
120	A	143	LYS	1	0.911	0.942	34.609	7.855	7.855	0.000	0.000	0.000	0.000
121	A	144	GLU	-1	-0.921	-0.970	37.341	-7.295	-7.295	0.000	0.000	0.000	0.000
122	A	145	GLN	0	-0.045	-0.018	36.799	0.200	0.200	0.000	0.000	0.000	0.000
123	A	146	PHE	0	0.051	0.038	36.212	0.139	0.139	0.000	0.000	0.000	0.000
124	A	147	ASP	-1	-0.824	-0.899	38.431	-7.508	-7.508	0.000	0.000	0.000	0.000
125	A	148	SER	0	-0.163	-0.088	41.319	0.232	0.232	0.000	0.000	0.000	0.000
126	A	149	GLY	0	-0.004	-0.004	41.862	0.151	0.151	0.000	0.000	0.000	0.000
127	A	150	LYS	1	0.862	0.940	38.905	7.385	7.385	0.000	0.000	0.000	0.000
128	A	151	GLU	-1	-0.829	-0.886	33.997	-9.226	-9.226	0.000	0.000	0.000	0.000
129	A	152	VAL	0	-0.013	-0.007	32.512	-0.026	-0.026	0.000	0.000	0.000	0.000
130	A	153	LEU	0	0.006	-0.001	29.880	-0.305	-0.305	0.000	0.000	0.000	0.000
131	A	154	VAL	0	0.021	0.010	26.962	0.023	0.023	0.000	0.000	0.000	0.000
132	A	155	VAL	0	-0.060	-0.040	23.135	-0.303	-0.303	0.000	0.000	0.000	0.000
133	A	156	VAL	0	0.049	0.033	19.686	0.161	0.161	0.000	0.000	0.000	0.000
134	A	157	VAL	0	-0.032	-0.018	18.279	-0.435	-0.435	0.000	0.000	0.000	0.000
135	A	158	SER	0	0.041	0.020	14.425	-0.461	-0.461	0.000	0.000	0.000	0.000
136	A	159	ALA	0	0.008	-0.011	13.141	-0.338	-0.338	0.000	0.000	0.000	0.000
137	A	160	MET	0	-0.048	-0.031	11.385	-0.244	-0.244	0.000	0.000	0.000	0.000
138	A	161	GLY	0	-0.028	-0.015	12.377	-0.521	-0.521	0.000	0.000	0.000	0.000
139	A	162	THR	0	-0.039	0.001	12.931	0.683	0.683	0.000	0.000	0.000	0.000
140	A	163	GLU	-1	-0.803	-0.881	16.312	-16.897	-16.897	0.000	0.000	0.000	0.000
141	A	164	GLN	0	-0.011	-0.023	18.524	0.329	0.329	0.000	0.000	0.000	0.000
142	A	165	VAL	0	0.046	0.032	22.051	-0.216	-0.216	0.000	0.000	0.000	0.000
143	A	166	LEU	0	-0.054	-0.029	21.591	0.207	0.207	0.000	0.000	0.000	0.000
144	A	167	GLN	0	-0.031	-0.023	25.425	0.276	0.276	0.000	0.000	0.000	0.000
145	A	168	THR	0	0.038	0.020	27.970	-0.225	-0.225	0.000	0.000	0.000	0.000
146	A	169	LYS	1	0.889	0.966	27.496	10.591	10.591	0.000	0.000	0.000	0.000
147	A	170	ASN	0	0.005	-0.001	33.039	-0.173	-0.173	0.000	0.000	0.000	0.000
148	A	171	ALA	0	0.016	0.018	34.621	-0.142	-0.142	0.000	0.000	0.000	0.000
149	A	172	ALA	-1	-0.979	-0.980	35.798	-7.661	-7.661	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:ASN)