FMO DATABASE

FMODB ID: RLQN8

Calculation Name: 2DMX-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DMX

Chain ID: A

ChEMBL ID:

UniProt ID: Q8NHS0

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	92
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-541357.768254
FMO2-HF: Nuclear repulsion	506449.369407
FMO2-HF: Total energy	-34908.398847
FMO2-MP2: Total energy	-35010.173458

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.
13.484	14.518	-0.015	-0.439	-0.58	-0.001

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 : 0.861 / q_NPA : 0.919

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	SER	0	0.065	0.038	3.842	2.771	3.805	-0.015	-0.439	-0.580	-0.001
4	A	4	GLY	0	0.027	0.020	6.930	-2.497	-2.497	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.009	-0.010	8.995	1.076	1.076	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.033	0.001	11.628	0.693	0.693	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.024	0.000	14.795	1.118	1.118	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.036	-0.030	16.562	0.177	0.177	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.035	0.035	19.665	0.429	0.429	0.000	0.000	0.000	0.000
10	A	10	ASN	0	0.027	0.008	21.524	-0.028	-0.028	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.029	0.007	23.111	0.029	0.029	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.046	0.013	26.585	0.186	0.186	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.879	-0.931	26.629	-10.407	-10.407	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.089	-0.040	23.252	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.043	-0.029	26.077	0.083	0.083	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.004	0.022	29.469	0.284	0.284	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.074	-0.040	31.572	0.409	0.409	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.052	0.013	33.246	-0.058	-0.058	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.075	0.027	35.153	0.065	0.065	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.000	0.003	36.139	0.104	0.104	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.018	0.013	36.970	0.216	0.216	0.000	0.000	0.000	0.000
22	A	22	SER	0	0.058	0.027	39.080	-0.021	-0.021	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.039	0.011	37.912	-0.214	-0.214	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.886	-0.935	38.055	-7.511	-7.511	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.835	-0.936	38.096	-8.002	-8.002	0.000	0.000	0.000	0.000
26	A	26	ILE	0	0.048	0.035	32.602	-0.182	-0.182	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.910	0.959	33.790	7.552	7.552	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.825	0.898	35.126	7.925	7.925	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.004	0.009	33.212	-0.038	-0.038	0.000	0.000	0.000	0.000
30	A	30	TYR	0	0.070	0.030	27.801	-0.255	-0.255	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.936	0.971	30.652	8.511	8.511	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.923	0.966	32.450	8.320	8.320	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.019	0.013	28.615	-0.104	-0.104	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.003	0.009	27.330	-0.353	-0.353	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.022	-0.009	27.845	-0.205	-0.205	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.951	0.968	28.946	10.115	10.115	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.040	0.009	23.321	-0.259	-0.259	0.000	0.000	0.000	0.000
38	A	38	HIS	0	0.059	0.035	24.264	-0.650	-0.650	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.038	0.022	21.799	0.196	0.196	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.913	-0.967	23.799	-10.658	-10.658	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.815	0.914	26.983	10.538	10.538	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.059	-0.023	24.618	0.398	0.398	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.003	-0.006	24.485	-0.506	-0.506	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.894	-0.929	23.379	-13.716	-13.716	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.031	-0.037	19.960	-0.662	-0.662	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.929	0.979	20.243	13.720	13.720	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.845	-0.926	13.785	-19.667	-19.667	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.922	-0.963	17.140	-16.067	-16.067	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.006	0.004	18.011	0.255	0.255	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.871	-0.946	18.219	-15.352	-15.352	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.917	0.965	13.331	20.701	20.701	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.870	0.944	17.867	15.614	15.614	0.000	0.000	0.000	0.000
53	A	53	PHE	0	0.015	0.013	21.269	0.652	0.652	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.879	0.941	18.947	14.253	14.253	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.000	0.009	18.414	0.382	0.382	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.016	0.009	21.762	0.508	0.508	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.042	-0.041	23.622	0.420	0.420	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.911	-0.953	21.733	-13.196	-13.196	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.007	-0.010	24.523	0.361	0.361	0.000	0.000	0.000	0.000
60	A	60	TYR	0	-0.015	-0.004	26.618	0.548	0.548	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.845	-0.941	28.184	-9.474	-9.474	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.119	-0.067	25.636	0.239	0.239	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.005	-0.009	28.989	0.232	0.232	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.069	-0.015	32.078	0.447	0.447	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.819	-0.919	32.939	-8.730	-8.730	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.013	0.014	34.444	-0.076	-0.076	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.948	0.979	32.750	9.262	9.262	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.900	0.961	26.243	11.152	11.152	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.891	0.949	31.065	8.459	8.459	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.003	-0.006	33.114	-0.013	-0.013	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.077	-0.049	30.771	0.013	0.013	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.005	0.001	26.357	-0.145	-0.145	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.921	-0.964	30.191	-9.012	-9.012	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.933	0.965	31.518	9.585	9.585	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.077	-0.024	29.100	0.059	0.059	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.039	0.034	31.074	0.018	0.018	0.000	0.000	0.000	0.000
77	A	77	CYS	0	-0.065	-0.049	28.378	-0.193	-0.193	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.798	-0.889	25.091	-13.330	-13.330	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.045	-0.042	24.047	0.292	0.292	0.000	0.000	0.000	0.000
80	A	80	TRP	0	-0.044	-0.010	18.319	0.185	0.185	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.865	0.928	24.518	12.193	12.193	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.085	0.044	27.805	0.164	0.164	0.000	0.000	0.000	0.000
83	A	83	GLY	0	-0.037	-0.009	30.791	0.329	0.329	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.006	-0.007	32.497	-0.051	-0.051	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.007	0.009	33.306	0.054	0.054	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.000	-0.002	37.020	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.024	-0.016	39.636	-0.034	-0.034	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.042	0.019	40.936	0.179	0.179	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.056	-0.021	41.530	0.033	0.033	0.000	0.000	0.000	0.000
90	A	90	SER	0	0.003	-0.003	43.297	0.175	0.175	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.072	-0.051	45.532	-0.194	-0.194	0.000	0.000	0.000	0.000
92	A	92	GLY	-1	-0.910	-0.929	47.831	-6.290	-6.290	0.000	0.000	0.000	0.000

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