FMO DATABASE

FMODB ID: Y16V2

Calculation Name: 2MP1-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2MP1

Chain ID: A

ChEMBL ID:

UniProt ID: Q99731

Base Structure: SolutionNMR

Registration Date: 2025-10-04

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	75
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-481251.071702
FMO2-HF: Nuclear repulsion	449806.513275
FMO2-HF: Total energy	-31444.558427
FMO2-MP2: Total energy	-31533.719591

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:1:GLY)

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

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.
-69.795	-74.955	32.366	-15.802	-11.403	-0.183

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.724 / q_NPA : 0.835

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	3	ASN	0	0.018	0.009	3.821	2.432	3.405	-0.015	-0.358	-0.599	-0.001
4	A	4	ASP	-1	-0.818	-0.881	1.818	-147.702	-151.051	22.494	-12.060	-7.086	-0.144
5	A	5	ALA	0	0.005	0.002	4.594	5.058	5.184	-0.001	-0.074	-0.051	0.000
47	A	48	GLN	0	0.062	0.044	1.850	-17.088	-20.158	9.889	-3.302	-3.516	-0.038
48	A	49	LEU	0	-0.008	-0.003	4.777	-3.838	-3.678	-0.001	-0.008	-0.151	0.000
6	A	6	GLU	-1	-0.964	-0.977	6.834	-28.747	-28.747	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.881	-0.940	6.415	-33.998	-33.998	0.000	0.000	0.000	0.000
8	A	8	CYS	0	-0.056	-0.004	7.623	-2.128	-2.128	0.000	0.000	0.000	0.000
9	A	9	CYS	0	-0.035	-0.013	6.209	-6.632	-6.632	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.053	0.036	7.210	3.420	3.420	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.046	-0.002	9.150	3.245	3.245	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.031	0.000	10.656	-2.029	-2.029	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.015	0.011	12.827	1.475	1.475	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.018	0.004	15.261	-0.247	-0.247	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.957	0.963	17.314	15.211	15.211	0.000	0.000	0.000	0.000
16	A	16	PRO	0	-0.040	0.002	12.119	0.269	0.269	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.027	0.010	11.465	-0.065	-0.065	0.000	0.000	0.000	0.000
18	A	18	PRO	0	0.022	0.007	14.576	0.559	0.559	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.061	0.011	15.819	-0.776	-0.776	0.000	0.000	0.000	0.000
20	A	20	TYR	0	-0.023	-0.026	16.886	0.316	0.316	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.019	0.003	13.751	0.358	0.358	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.005	0.004	11.674	-1.589	-1.589	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.921	0.959	12.170	20.737	20.737	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.016	-0.018	10.969	-0.070	-0.070	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.006	-0.008	10.635	-1.575	-1.575	0.000	0.000	0.000	0.000
26	A	26	HIS	0	0.053	0.049	7.630	1.998	1.998	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.030	-0.036	10.590	-0.736	-0.736	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.060	0.059	8.921	1.269	1.269	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.037	-0.041	12.537	0.861	0.861	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.017	0.004	15.784	-0.338	-0.338	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.885	0.946	18.087	15.348	15.348	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.853	-0.920	14.863	-19.111	-19.111	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.036	0.026	16.282	0.286	0.286	0.000	0.000	0.000	0.000
34	A	35	ARG	1	0.965	0.969	14.633	17.871	17.871	0.000	0.000	0.000	0.000
35	A	36	VAL	0	-0.002	-0.006	11.686	1.418	1.418	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.015	0.006	13.201	-1.219	-1.219	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.001	-0.020	10.565	0.434	0.434	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.024	0.009	11.073	-1.038	-1.038	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.005	0.001	6.153	-0.976	-0.976	0.000	0.000	0.000	0.000
40	A	41	PHE	0	0.005	-0.020	8.312	1.063	1.063	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.018	0.001	6.633	-3.881	-3.881	0.000	0.000	0.000	0.000
42	A	43	THR	0	-0.012	-0.033	8.426	4.662	4.662	0.000	0.000	0.000	0.000
43	A	44	LEU	0	0.003	-0.011	10.383	-0.978	-0.978	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.925	0.975	9.433	25.358	25.358	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.041	0.021	8.061	-0.633	-0.633	0.000	0.000	0.000	0.000
46	A	47	ARG	1	0.965	0.995	4.872	30.476	30.476	0.000	0.000	0.000	0.000
49	A	51	ALA	0	-0.012	-0.014	8.900	2.188	2.188	0.000	0.000	0.000	0.000
50	A	52	PRO	0	0.054	0.027	12.543	-0.430	-0.430	0.000	0.000	0.000	0.000
51	A	53	PRO	0	-0.023	-0.016	14.743	0.662	0.662	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.915	-0.944	16.809	-13.164	-13.164	0.000	0.000	0.000	0.000
53	A	55	GLN	0	0.067	0.039	19.602	0.063	0.063	0.000	0.000	0.000	0.000
54	A	56	PRO	0	0.095	0.026	20.907	-0.484	-0.484	0.000	0.000	0.000	0.000
55	A	57	TRP	0	-0.060	-0.050	15.271	-0.097	-0.097	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.003	-0.001	15.964	-0.449	-0.449	0.000	0.000	0.000	0.000
57	A	59	GLU	-1	-0.822	-0.916	18.551	-13.222	-13.222	0.000	0.000	0.000	0.000
58	A	60	ARG	1	0.915	0.960	20.903	12.106	12.106	0.000	0.000	0.000	0.000
59	A	61	ILE	0	-0.048	-0.003	16.187	0.168	0.168	0.000	0.000	0.000	0.000
60	A	62	ILE	0	0.020	0.026	16.044	-0.430	-0.430	0.000	0.000	0.000	0.000
61	A	63	GLN	0	0.003	0.008	18.327	0.377	0.377	0.000	0.000	0.000	0.000
62	A	64	ARG	1	0.936	0.984	19.457	15.394	15.394	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.005	0.014	14.348	0.188	0.188	0.000	0.000	0.000	0.000
64	A	66	GLN	0	0.024	0.031	18.447	0.505	0.505	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.945	0.967	20.289	12.308	12.308	0.000	0.000	0.000	0.000
66	A	68	THR	0	-0.064	-0.043	19.974	0.120	0.120	0.000	0.000	0.000	0.000
67	A	69	SER	0	-0.057	-0.043	17.654	0.107	0.107	0.000	0.000	0.000	0.000
68	A	70	ALA	0	0.031	0.012	19.738	0.208	0.208	0.000	0.000	0.000	0.000
69	A	71	LYS	1	0.941	0.975	22.763	12.367	12.367	0.000	0.000	0.000	0.000
70	A	72	MET	0	-0.063	-0.020	20.329	0.858	0.858	0.000	0.000	0.000	0.000
71	A	73	LYS	1	1.001	0.989	21.544	10.555	10.555	0.000	0.000	0.000	0.000
72	A	74	ARG	1	0.950	0.977	23.225	12.365	12.365	0.000	0.000	0.000	0.000
73	A	75	ARG	1	0.860	0.899	14.107	19.930	19.930	0.000	0.000	0.000	0.000
74	A	76	SER	0	0.010	0.000	18.531	0.804	0.804	0.000	0.000	0.000	0.000
75	A	77	SER	-1	-0.828	-0.865	13.302	-21.522	-21.522	0.000	0.000	0.000	0.000

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