FMO DATABASE

FMODB ID: 3MJZL

Calculation Name: 1XAX-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1XAX

Chain ID: A

ChEMBL ID:

UniProt ID: P71335

Base Structure: SolutionNMR

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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1316998.555599
FMO2-HF: Nuclear repulsion	1258998.637251
FMO2-HF: Total energy	-57999.918349
FMO2-MP2: Total energy	-58165.938378

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:SER)

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

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.
-544.14	-544.527	39.996	-22.208	-17.401	-0.202

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.725 / q_NPA : 0.821

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	LEU	0	-0.036	-0.012	2.738	5.398	7.119	0.490	-0.715	-1.495	-0.004
35	A	37	ASN	0	0.007	-0.005	1.784	-26.716	-30.394	19.713	-9.407	-6.628	-0.075
36	A	38	GLU	-1	-0.919	-0.937	2.001	-150.186	-149.097	19.759	-12.042	-8.806	-0.122
37	A	39	VAL	0	0.091	0.044	3.135	15.237	15.718	0.034	-0.044	-0.472	-0.001
4	A	6	VAL	0	0.013	-0.001	5.597	2.182	2.182	0.000	0.000	0.000	0.000
5	A	7	ASP	-1	-0.909	-0.929	9.074	-20.928	-20.928	0.000	0.000	0.000	0.000
6	A	8	LEU	0	-0.005	-0.009	12.206	0.706	0.706	0.000	0.000	0.000	0.000
7	A	9	GLN	0	0.000	-0.005	14.953	2.024	2.024	0.000	0.000	0.000	0.000
8	A	10	ILE	0	-0.022	-0.016	17.842	0.605	0.605	0.000	0.000	0.000	0.000
9	A	11	ALA	0	-0.001	0.012	20.983	0.120	0.120	0.000	0.000	0.000	0.000
10	A	12	THR	0	-0.069	-0.033	24.467	0.398	0.398	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.907	-0.956	25.284	-11.170	-11.170	0.000	0.000	0.000	0.000
12	A	14	ASN	0	-0.086	-0.047	26.661	-0.014	-0.014	0.000	0.000	0.000	0.000
13	A	15	ILE	0	-0.001	-0.019	25.015	0.163	0.163	0.000	0.000	0.000	0.000
14	A	16	GLU	-1	-0.939	-0.965	28.854	-9.331	-9.331	0.000	0.000	0.000	0.000
15	A	17	GLY	0	-0.005	0.003	26.307	0.014	0.014	0.000	0.000	0.000	0.000
16	A	18	LEU	0	-0.041	-0.010	22.054	-0.251	-0.251	0.000	0.000	0.000	0.000
17	A	19	PRO	0	-0.004	0.012	18.705	-0.079	-0.079	0.000	0.000	0.000	0.000
18	A	20	THR	0	-0.015	-0.030	17.330	-0.230	-0.230	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.806	-0.910	12.140	-18.610	-18.610	0.000	0.000	0.000	0.000
20	A	22	GLU	-1	-0.941	-0.968	12.822	-18.315	-18.315	0.000	0.000	0.000	0.000
21	A	23	GLN	0	-0.042	-0.036	13.522	-0.821	-0.821	0.000	0.000	0.000	0.000
22	A	24	ILE	0	-0.020	-0.006	14.361	-0.358	-0.358	0.000	0.000	0.000	0.000
23	A	25	VAL	0	0.016	0.015	8.414	-0.692	-0.692	0.000	0.000	0.000	0.000
24	A	26	GLN	0	-0.014	-0.001	10.250	-2.254	-2.254	0.000	0.000	0.000	0.000
25	A	27	TRP	0	-0.058	-0.033	11.629	0.000	0.000	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.017	0.005	13.023	0.219	0.219	0.000	0.000	0.000	0.000
27	A	29	THR	0	0.039	-0.017	7.770	0.228	0.228	0.000	0.000	0.000	0.000
28	A	30	GLY	0	-0.032	-0.011	8.179	-3.493	-3.493	0.000	0.000	0.000	0.000
29	A	31	ALA	0	-0.021	-0.010	9.337	-0.542	-0.542	0.000	0.000	0.000	0.000
30	A	32	VAL	0	-0.045	0.010	8.980	0.409	0.409	0.000	0.000	0.000	0.000
31	A	33	GLN	0	-0.007	-0.010	5.329	-7.604	-7.604	0.000	0.000	0.000	0.000
32	A	34	PRO	0	-0.029	-0.009	6.630	-3.358	-3.358	0.000	0.000	0.000	0.000
33	A	35	GLU	-1	-1.014	-1.005	8.415	-22.260	-22.260	0.000	0.000	0.000	0.000
34	A	36	GLY	0	0.005	0.007	6.329	-2.039	-2.039	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.960	-0.967	5.239	-40.420	-40.420	0.000	0.000	0.000	0.000
39	A	41	MET	0	-0.007	-0.010	7.618	3.567	3.567	0.000	0.000	0.000	0.000
40	A	42	THR	0	0.046	0.005	10.934	0.069	0.069	0.000	0.000	0.000	0.000
41	A	43	VAL	0	-0.015	-0.008	13.280	1.441	1.441	0.000	0.000	0.000	0.000
42	A	44	ARG	1	0.762	0.885	15.983	16.827	16.827	0.000	0.000	0.000	0.000
43	A	45	ILE	0	-0.023	0.005	19.205	0.557	0.557	0.000	0.000	0.000	0.000
44	A	46	VAL	0	0.039	0.002	21.511	0.288	0.288	0.000	0.000	0.000	0.000
45	A	47	ASP	-1	-0.812	-0.902	24.938	-10.105	-10.105	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.884	-0.947	28.289	-9.895	-9.895	0.000	0.000	0.000	0.000
47	A	49	ALA	0	-0.060	-0.032	30.406	-0.075	-0.075	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.877	-0.950	27.630	-11.052	-11.052	0.000	0.000	0.000	0.000
49	A	51	SER	0	0.003	0.007	26.228	-0.383	-0.383	0.000	0.000	0.000	0.000
50	A	52	HIS	0	-0.026	-0.023	27.305	-0.179	-0.179	0.000	0.000	0.000	0.000
51	A	53	GLU	-1	-0.876	-0.937	30.298	-9.575	-9.575	0.000	0.000	0.000	0.000
52	A	54	LEU	0	0.008	0.030	23.691	0.044	0.044	0.000	0.000	0.000	0.000
53	A	55	ASN	0	0.046	-0.008	25.887	-0.539	-0.539	0.000	0.000	0.000	0.000
54	A	56	LEU	0	-0.114	-0.055	27.831	0.079	0.079	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.035	-0.016	29.200	0.170	0.170	0.000	0.000	0.000	0.000
56	A	58	TYR	0	-0.026	-0.013	22.599	0.161	0.161	0.000	0.000	0.000	0.000
57	A	59	ARG	1	0.874	0.945	25.835	11.647	11.647	0.000	0.000	0.000	0.000
58	A	60	GLY	0	-0.032	0.003	29.420	0.079	0.079	0.000	0.000	0.000	0.000
59	A	61	LYS	1	0.777	0.888	23.455	13.489	13.489	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.842	-0.906	29.735	-9.825	-9.825	0.000	0.000	0.000	0.000
61	A	63	ARG	1	0.866	0.912	31.631	9.226	9.226	0.000	0.000	0.000	0.000
62	A	64	PRO	0	-0.023	-0.027	32.053	-0.257	-0.257	0.000	0.000	0.000	0.000
63	A	65	THR	0	0.026	0.034	28.358	0.183	0.183	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.026	0.002	28.102	0.039	0.039	0.000	0.000	0.000	0.000
65	A	67	VAL	0	0.012	0.017	22.798	-0.174	-0.174	0.000	0.000	0.000	0.000
66	A	68	LEU	0	-0.039	-0.010	24.318	0.210	0.210	0.000	0.000	0.000	0.000
67	A	69	SER	0	0.076	0.012	19.275	-0.092	-0.092	0.000	0.000	0.000	0.000
68	A	70	PHE	0	-0.078	-0.060	19.373	1.342	1.342	0.000	0.000	0.000	0.000
69	A	71	PRO	0	0.050	0.041	17.608	-0.908	-0.908	0.000	0.000	0.000	0.000
70	A	72	PHE	0	0.036	0.012	14.707	0.501	0.501	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.999	-1.003	16.854	-14.351	-14.351	0.000	0.000	0.000	0.000
72	A	74	CYS	0	0.006	-0.001	18.144	-0.815	-0.815	0.000	0.000	0.000	0.000
73	A	75	PRO	0	-0.066	-0.024	19.236	0.777	0.777	0.000	0.000	0.000	0.000
74	A	76	ASP	-1	-0.956	-0.975	21.780	-12.389	-12.389	0.000	0.000	0.000	0.000
75	A	77	GLU	-1	-0.930	-0.965	19.314	-14.186	-14.186	0.000	0.000	0.000	0.000
76	A	78	VAL	0	-0.096	-0.069	15.835	-0.725	-0.725	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.822	-0.915	14.004	-19.470	-19.470	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.065	-0.039	9.696	-0.602	-0.602	0.000	0.000	0.000	0.000
79	A	81	PRO	0	0.073	0.055	6.393	0.718	0.718	0.000	0.000	0.000	0.000
80	A	82	LEU	0	-0.125	-0.059	7.998	-3.104	-3.104	0.000	0.000	0.000	0.000
81	A	83	LEU	0	-0.035	-0.019	10.176	2.194	2.194	0.000	0.000	0.000	0.000
82	A	84	GLY	0	-0.021	0.003	12.085	2.215	2.215	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.772	-0.867	13.998	-19.448	-19.448	0.000	0.000	0.000	0.000
84	A	86	LEU	0	-0.020	-0.002	16.395	1.301	1.301	0.000	0.000	0.000	0.000
85	A	87	VAL	0	-0.034	-0.025	18.776	-0.045	-0.045	0.000	0.000	0.000	0.000
86	A	88	ILE	0	-0.019	-0.005	19.937	0.491	0.491	0.000	0.000	0.000	0.000
87	A	89	CYS	0	0.022	0.016	23.478	0.088	0.088	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.887	0.934	24.601	10.825	10.825	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.115	-0.071	25.910	0.180	0.180	0.000	0.000	0.000	0.000
90	A	92	VAL	0	0.013	0.016	28.436	0.310	0.310	0.000	0.000	0.000	0.000
91	A	93	VAL	0	0.032	0.001	23.392	0.186	0.186	0.000	0.000	0.000	0.000
92	A	94	GLU	-1	-0.861	-0.918	26.455	-10.725	-10.725	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.899	0.954	27.176	9.139	9.139	0.000	0.000	0.000	0.000
94	A	96	GLU	-1	-0.879	-0.955	28.621	-10.791	-10.791	0.000	0.000	0.000	0.000
95	A	97	ALA	0	0.010	0.005	25.883	0.112	0.112	0.000	0.000	0.000	0.000
96	A	98	SER	0	-0.046	-0.020	27.873	0.210	0.210	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.902	-0.958	30.591	-8.541	-8.541	0.000	0.000	0.000	0.000
98	A	100	GLN	0	-0.080	-0.035	28.542	0.306	0.306	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.990	-0.982	31.890	-8.965	-8.965	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.874	0.932	27.016	10.199	10.199	0.000	0.000	0.000	0.000
101	A	103	PRO	0	-0.014	-0.010	23.955	-0.077	-0.077	0.000	0.000	0.000	0.000
102	A	104	LEU	0	0.056	0.019	22.984	-0.415	-0.415	0.000	0.000	0.000	0.000
103	A	105	MET	0	-0.013	0.016	19.063	-0.513	-0.513	0.000	0.000	0.000	0.000
104	A	106	ALA	0	0.038	0.032	18.917	-0.791	-0.791	0.000	0.000	0.000	0.000
105	A	107	HIS	0	0.002	0.004	20.672	-0.510	-0.510	0.000	0.000	0.000	0.000
106	A	108	TRP	0	0.031	-0.008	17.476	-0.268	-0.268	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.053	0.034	16.348	-0.570	-0.570	0.000	0.000	0.000	0.000
108	A	110	HIS	1	0.871	0.907	17.284	14.112	14.112	0.000	0.000	0.000	0.000
109	A	111	MET	0	-0.059	-0.012	19.863	0.160	0.160	0.000	0.000	0.000	0.000
110	A	112	VAL	0	0.024	0.006	14.959	0.232	0.232	0.000	0.000	0.000	0.000
111	A	113	VAL	0	0.084	0.065	15.465	-0.220	-0.220	0.000	0.000	0.000	0.000
112	A	114	HIS	0	-0.021	-0.010	17.783	0.540	0.540	0.000	0.000	0.000	0.000
113	A	115	GLY	0	0.002	-0.030	20.791	0.397	0.397	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.001	0.006	16.419	-0.188	-0.188	0.000	0.000	0.000	0.000
115	A	117	LEU	0	0.015	0.006	18.395	0.241	0.241	0.000	0.000	0.000	0.000
116	A	118	HIS	0	-0.050	-0.026	20.274	0.412	0.412	0.000	0.000	0.000	0.000
117	A	119	LEU	0	-0.112	-0.030	20.946	0.698	0.698	0.000	0.000	0.000	0.000
118	A	120	LEU	0	-0.034	-0.034	16.797	0.570	0.570	0.000	0.000	0.000	0.000
119	A	121	GLY	0	-0.004	0.016	20.680	0.074	0.074	0.000	0.000	0.000	0.000
120	A	122	TYR	0	-0.038	-0.056	13.625	0.872	0.872	0.000	0.000	0.000	0.000
121	A	123	ASP	-1	-0.882	-0.926	15.587	-18.218	-18.218	0.000	0.000	0.000	0.000
122	A	124	HIS	1	0.848	0.923	14.654	20.734	20.734	0.000	0.000	0.000	0.000
123	A	125	ILE	0	-0.002	-0.003	15.391	-0.309	-0.309	0.000	0.000	0.000	0.000
124	A	126	GLU	-1	-0.966	-0.976	17.505	-13.998	-13.998	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.957	-0.977	18.455	-14.713	-14.713	0.000	0.000	0.000	0.000
126	A	128	ASP	-1	-0.930	-0.960	12.991	-21.407	-21.407	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.848	-0.963	11.314	-28.811	-28.811	0.000	0.000	0.000	0.000
128	A	130	ALA	0	0.016	0.041	13.355	-0.433	-0.433	0.000	0.000	0.000	0.000
129	A	131	GLU	-1	-0.946	-0.973	13.011	-21.660	-21.660	0.000	0.000	0.000	0.000
130	A	132	GLU	-1	-0.922	-0.959	9.206	-31.156	-31.156	0.000	0.000	0.000	0.000
131	A	133	MET	0	-0.023	-0.003	11.124	-1.409	-1.409	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.891	-0.945	12.892	-16.958	-16.958	0.000	0.000	0.000	0.000
133	A	135	SER	0	-0.043	-0.011	12.230	0.624	0.624	0.000	0.000	0.000	0.000
134	A	136	LEU	0	0.002	0.009	8.532	0.221	0.221	0.000	0.000	0.000	0.000
135	A	137	GLU	-1	-0.907	-0.983	11.332	-16.758	-16.758	0.000	0.000	0.000	0.000
136	A	138	THR	0	0.019	0.000	14.633	1.238	1.238	0.000	0.000	0.000	0.000
137	A	139	GLN	0	-0.078	-0.048	11.440	0.990	0.990	0.000	0.000	0.000	0.000
138	A	140	ILE	0	-0.026	-0.009	11.904	0.813	0.813	0.000	0.000	0.000	0.000
139	A	141	MET	0	-0.098	-0.026	14.614	1.775	1.775	0.000	0.000	0.000	0.000
140	A	142	GLN	0	-0.045	-0.037	18.019	0.943	0.943	0.000	0.000	0.000	0.000
141	A	143	GLY	0	-0.034	-0.011	16.601	0.739	0.739	0.000	0.000	0.000	0.000
142	A	144	LEU	0	-0.049	-0.021	15.064	0.366	0.366	0.000	0.000	0.000	0.000
143	A	145	GLY	0	-0.061	-0.018	19.103	0.747	0.747	0.000	0.000	0.000	0.000
144	A	146	PHE	-1	-0.883	-0.935	17.395	-12.242	-12.242	0.000	0.000	0.000	0.000

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