FMO DATABASE

FMODB ID: 3MNGL

Calculation Name: 1M5T-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1M5T

Chain ID: A

ChEMBL ID:

UniProt ID: Q9A5I4

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1082858.876329
FMO2-HF: Nuclear repulsion	1033934.60034
FMO2-HF: Total energy	-48924.275989
FMO2-MP2: Total energy	-49067.057123

3D Structure

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:THR)

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

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.
-280.825	-277.907	27.818	-16.096	-14.64	-0.185

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.730 / q_NPA : 0.851

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	0.895	0.949	2.947	61.593	64.580	0.297	-1.317	-1.966	-0.010
25	A	26	GLY	0	-0.008	0.010	4.658	-0.428	-0.351	-0.001	-0.015	-0.061	0.000
26	A	27	TYR	0	-0.112	-0.094	2.538	-10.772	-9.148	1.264	-1.000	-1.888	-0.012
27	A	28	GLU	-1	-0.805	-0.888	1.770	-151.944	-153.782	26.258	-13.742	-10.679	-0.163
28	A	29	THR	0	-0.017	-0.029	4.149	3.024	3.092	0.000	-0.022	-0.046	0.000
4	A	5	VAL	0	0.028	0.021	5.574	5.021	5.021	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.018	-0.008	8.671	-0.904	-0.904	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.006	-0.005	11.637	1.808	1.808	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.022	0.007	13.991	0.152	0.152	0.000	0.000	0.000	0.000
8	A	9	GLU	0	-0.037	-0.068	17.591	1.118	1.118	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.753	-0.859	19.674	-12.898	-12.898	0.000	0.000	0.000	0.000
10	A	11	ASN	0	-0.013	0.001	22.640	-0.182	-0.182	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.820	-0.909	20.860	-14.072	-14.072	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.002	0.000	20.136	-0.648	-0.648	0.000	0.000	0.000	0.000
13	A	14	ASN	0	-0.010	-0.005	20.117	-0.322	-0.322	0.000	0.000	0.000	0.000
14	A	15	MET	0	-0.026	0.004	15.543	-1.337	-1.337	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.855	0.918	15.491	13.429	13.429	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.026	0.025	15.676	-0.894	-0.894	0.000	0.000	0.000	0.000
17	A	18	PHE	0	0.006	-0.016	13.812	-0.470	-0.470	0.000	0.000	0.000	0.000
18	A	19	HIS	1	0.820	0.894	10.105	23.565	23.565	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.866	-0.918	10.991	-20.740	-20.740	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.044	-0.030	12.143	-0.466	-0.466	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.016	-0.007	7.949	-0.271	-0.271	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.846	-0.912	7.223	-28.982	-28.982	0.000	0.000	0.000	0.000
23	A	24	ALA	0	-0.025	-0.012	7.804	-0.743	-0.743	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.062	-0.026	7.929	1.522	1.522	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.023	0.004	7.807	0.435	0.435	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.009	-0.002	10.144	-0.088	-0.088	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.005	-0.005	13.568	0.862	0.862	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.853	0.900	17.270	13.198	13.198	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.857	-0.905	20.705	-13.007	-13.007	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.023	-0.006	20.710	-0.835	-0.835	0.000	0.000	0.000	0.000
35	A	36	LEU	0	0.001	-0.007	21.399	-0.486	-0.486	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.004	-0.016	19.610	-0.360	-0.360	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.003	-0.003	16.955	-1.008	-1.008	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.000	0.000	16.796	-1.077	-1.077	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.040	-0.007	18.245	0.050	0.050	0.000	0.000	0.000	0.000
40	A	41	ILE	0	-0.009	-0.010	12.390	-0.698	-0.698	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.008	-0.007	12.897	-2.003	-2.003	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.837	0.904	13.640	14.538	14.538	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.943	-0.959	13.113	-21.448	-21.448	0.000	0.000	0.000	0.000
44	A	45	ASN	0	-0.071	-0.057	9.046	-0.171	-0.171	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.916	0.977	8.394	18.547	18.547	0.000	0.000	0.000	0.000
46	A	47	PRO	0	-0.036	-0.007	8.367	-3.781	-3.781	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.791	-0.893	6.441	-43.343	-43.343	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.007	-0.004	9.440	2.696	2.696	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.005	0.007	11.232	-1.669	-1.669	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.025	-0.004	13.322	0.975	0.975	0.000	0.000	0.000	0.000
51	A	52	MET	0	-0.003	0.001	15.162	0.073	0.073	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.777	-0.843	18.733	-12.711	-12.711	0.000	0.000	0.000	0.000
53	A	54	ILE	0	0.004	-0.010	21.692	0.122	0.122	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.029	-0.016	24.876	0.277	0.277	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.013	0.011	21.866	-0.142	-0.142	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.041	-0.026	25.942	0.430	0.430	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.818	-0.917	25.170	-12.356	-12.356	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.026	-0.008	25.759	0.199	0.199	0.000	0.000	0.000	0.000
59	A	60	SER	0	0.050	0.036	27.329	-0.349	-0.349	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.057	0.020	24.126	-0.216	-0.216	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.004	-0.007	24.095	-0.420	-0.420	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.949	-0.966	26.441	-10.368	-10.368	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.016	-0.003	21.526	-0.176	-0.176	0.000	0.000	0.000	0.000
64	A	65	THR	0	0.000	-0.027	21.571	-0.678	-0.678	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.853	0.918	23.153	10.494	10.494	0.000	0.000	0.000	0.000
66	A	67	TRP	0	0.011	-0.016	24.156	-0.043	-0.043	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.048	-0.019	18.177	-0.285	-0.285	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.796	0.890	19.046	15.557	15.557	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.883	-0.913	23.779	-10.619	-10.619	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.779	-0.870	21.765	-14.581	-14.581	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.880	-0.946	21.694	-13.534	-13.534	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.959	-0.968	18.049	-16.595	-16.595	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.097	-0.063	16.422	-1.644	-1.644	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.009	0.019	18.248	-0.592	-0.592	0.000	0.000	0.000	0.000
75	A	76	HIS	0	-0.059	-0.026	13.832	0.019	0.019	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.012	0.022	13.329	-0.583	-0.583	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.007	0.004	13.116	1.522	1.522	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.032	0.005	14.880	-1.155	-1.155	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.022	-0.014	15.154	0.826	0.826	0.000	0.000	0.000	0.000
80	A	81	ALA	0	0.047	0.023	17.616	-0.348	-0.348	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.007	-0.012	18.466	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.006	-0.013	21.377	0.338	0.338	0.000	0.000	0.000	0.000
83	A	84	ALA	0	-0.021	-0.028	25.193	0.020	0.020	0.000	0.000	0.000	0.000
84	A	85	PHE	0	-0.064	-0.015	28.288	0.366	0.366	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.075	0.030	27.555	-0.366	-0.366	0.000	0.000	0.000	0.000
86	A	87	MET	0	-0.025	-0.010	29.405	0.228	0.228	0.000	0.000	0.000	0.000
87	A	88	LYS	1	0.987	0.975	31.713	8.329	8.329	0.000	0.000	0.000	0.000
88	A	89	GLY	0	-0.009	0.011	32.956	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.833	-0.917	29.556	-9.784	-9.784	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.864	-0.913	27.921	-10.253	-10.253	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.838	-0.903	28.139	-10.166	-10.166	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.892	0.951	29.783	9.932	9.932	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.001	-0.015	24.176	-0.237	-0.237	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.761	0.858	25.616	10.156	10.156	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.907	-0.963	26.711	-9.708	-9.708	0.000	0.000	0.000	0.000
96	A	97	GLY	0	-0.089	-0.043	26.964	0.087	0.087	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.011	0.013	24.532	-0.307	-0.307	0.000	0.000	0.000	0.000
98	A	99	CYS	0	-0.080	-0.029	21.056	-0.838	-0.838	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.833	-0.901	17.577	-14.678	-14.678	0.000	0.000	0.000	0.000
100	A	101	ALA	0	-0.066	-0.041	18.318	0.257	0.257	0.000	0.000	0.000	0.000
101	A	102	TYR	-1	-0.909	-0.960	20.365	-11.920	-11.920	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.022	0.003	17.604	-0.099	-0.099	0.000	0.000	0.000	0.000
103	A	104	SER	0	0.038	0.020	21.337	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.831	0.912	23.618	12.194	12.194	0.000	0.000	0.000	0.000
105	A	106	PRO	0	-0.014	-0.022	25.650	0.380	0.380	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.037	0.019	19.007	0.080	0.080	0.000	0.000	0.000	0.000
107	A	108	SER	0	0.010	0.015	22.189	-0.056	-0.056	0.000	0.000	0.000	0.000
108	A	109	VAL	0	0.041	0.008	17.066	-0.469	-0.469	0.000	0.000	0.000	0.000
109	A	110	VAL	0	0.011	0.006	17.320	-0.780	-0.780	0.000	0.000	0.000	0.000
110	A	111	HIS	0	0.033	0.022	17.885	-0.499	-0.499	0.000	0.000	0.000	0.000
111	A	112	PHE	0	0.037	0.009	12.745	-0.396	-0.396	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.007	-0.008	12.242	-0.957	-0.957	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.969	-0.980	13.277	-15.061	-15.061	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.033	-0.026	15.007	-0.348	-0.348	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.010	-0.003	9.777	-0.410	-0.410	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.894	0.948	9.448	22.105	22.105	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.943	0.975	11.202	14.896	14.896	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.047	-0.028	13.256	0.490	0.490	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.024	-0.001	6.441	-0.594	-0.594	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.802	-0.891	6.903	-33.725	-33.725	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.776	0.903	10.737	18.220	18.220	0.000	0.000	0.000	0.000
122	A	123	GLN	0	-0.071	-0.052	11.554	-0.821	-0.821	0.000	0.000	0.000	0.000
123	A	124	PRO	-1	-0.932	-0.949	14.917	-14.984	-14.984	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:2:THR)