FMO DATABASE

FMODB ID: 9Q582

Calculation Name: 2D9I-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2D9I

Chain ID: A

ChEMBL ID:

UniProt ID: Q86UW6

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	96
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-620171.081037
FMO2-HF: Nuclear repulsion	583967.699828
FMO2-HF: Total energy	-36203.381209
FMO2-MP2: Total energy	-36308.796598

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.
51.491	54.11	0.252	-1.645	-1.227	-0.018

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 : 0.839 / 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	3	SER	0	0.001	-0.004	2.689	-18.060	-15.441	0.252	-1.645	-1.227	-0.018
4	A	4	GLY	0	0.007	-0.011	5.472	0.916	0.916	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.013	0.017	8.235	0.582	0.582	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.012	0.008	11.052	-1.365	-1.365	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.084	0.048	13.148	0.848	0.848	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.003	-0.003	13.603	-1.372	-1.372	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.006	-0.006	11.697	-0.040	-0.040	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.033	-0.019	13.751	0.051	0.051	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.019	0.019	15.666	0.262	0.262	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.923	-0.958	19.400	-14.888	-14.888	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.041	0.009	21.051	0.468	0.468	0.000	0.000	0.000	0.000
14	A	14	HIS	0	-0.104	-0.057	21.834	0.474	0.474	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.021	0.009	25.600	-0.167	-0.167	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.001	0.026	26.601	0.341	0.341	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.034	0.013	29.792	-0.066	-0.066	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.021	-0.024	31.820	-0.253	-0.253	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.885	-0.944	32.297	-8.950	-8.950	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.810	-0.904	30.804	-10.370	-10.370	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.032	-0.022	28.066	-0.381	-0.381	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.049	-0.025	27.939	-0.424	-0.424	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.880	-0.941	29.589	-9.789	-9.789	0.000	0.000	0.000	0.000
24	A	24	HIS	0	-0.043	-0.034	25.823	-0.596	-0.596	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.035	-0.017	23.839	-0.544	-0.544	0.000	0.000	0.000	0.000
26	A	26	MET	0	-0.011	-0.006	25.604	-0.259	-0.259	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.958	0.977	27.489	10.501	10.501	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.064	-0.034	21.681	-0.351	-0.351	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.042	-0.017	22.455	-0.619	-0.619	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.864	-0.932	23.450	-11.923	-11.923	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.964	0.983	23.011	11.684	11.684	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.818	0.902	17.926	16.153	16.153	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.021	-0.009	19.677	-0.836	-0.836	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.879	-0.941	21.672	-12.379	-12.379	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.880	-0.950	18.368	-15.243	-15.243	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.124	-0.058	16.648	-0.687	-0.687	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.860	0.926	18.330	12.135	12.135	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.027	0.001	21.496	0.494	0.494	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.023	-0.001	15.615	0.171	0.171	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.061	0.043	16.408	-0.128	-0.128	0.000	0.000	0.000	0.000
41	A	41	GLY	0	-0.040	-0.026	13.260	-1.527	-1.527	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.876	0.938	7.608	33.167	33.167	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.070	0.043	13.351	0.739	0.739	0.000	0.000	0.000	0.000
44	A	44	TYR	0	-0.037	-0.043	10.597	-0.296	-0.296	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.032	0.030	15.242	-1.198	-1.198	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.086	-0.053	14.326	0.189	0.189	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.082	0.024	16.287	0.272	0.272	0.000	0.000	0.000	0.000
48	A	48	ILE	0	0.000	0.003	16.352	0.296	0.296	0.000	0.000	0.000	0.000
49	A	49	THR	0	0.004	-0.002	20.539	0.664	0.664	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.052	0.022	23.255	0.538	0.538	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.971	0.982	19.259	15.236	15.236	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.015	0.000	24.443	-0.084	-0.084	0.000	0.000	0.000	0.000
53	A	53	ASN	0	0.063	0.024	26.309	0.660	0.660	0.000	0.000	0.000	0.000
54	A	54	HIS	0	0.063	0.021	26.716	0.161	0.161	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.059	-0.032	29.114	0.248	0.248	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.016	-0.004	31.783	0.013	0.013	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.048	0.019	33.300	0.333	0.333	0.000	0.000	0.000	0.000
58	A	58	GLY	0	-0.054	-0.013	31.245	0.012	0.012	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.017	-0.010	32.051	-0.156	-0.156	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.024	0.012	30.351	0.139	0.139	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.948	0.971	32.376	8.646	8.646	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.071	0.045	27.087	0.065	0.065	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.868	0.910	24.526	12.523	12.523	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.015	-0.017	28.164	-0.024	-0.024	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.030	0.029	31.587	0.127	0.127	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.046	0.023	25.093	0.024	0.024	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.003	-0.001	27.400	-0.077	-0.077	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.979	0.993	29.097	8.623	8.623	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.060	0.035	28.061	0.058	0.058	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.011	-0.014	24.595	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	71	ILE	0	0.002	-0.002	28.506	0.009	0.009	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.040	-0.024	31.080	0.260	0.260	0.000	0.000	0.000	0.000
73	A	73	HIS	0	-0.016	0.006	29.896	0.328	0.328	0.000	0.000	0.000	0.000
74	A	74	SER	0	0.012	0.003	30.057	-0.190	-0.190	0.000	0.000	0.000	0.000
75	A	75	PHE	0	-0.019	-0.011	24.620	-0.305	-0.305	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.974	0.979	21.973	13.550	13.550	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.022	0.004	21.487	-0.616	-0.616	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.041	-0.027	18.987	0.267	0.267	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.825	-0.883	19.470	-13.756	-13.756	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.002	-0.002	13.445	-0.129	-0.129	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.860	0.884	13.255	21.027	21.027	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.068	0.040	18.055	0.294	0.294	0.000	0.000	0.000	0.000
83	A	83	GLY	0	-0.053	-0.046	20.338	0.579	0.579	0.000	0.000	0.000	0.000
84	A	84	CYS	-1	-0.880	-0.863	16.096	-20.359	-20.359	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.004	0.015	18.698	0.368	0.368	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.936	0.980	12.174	23.005	23.005	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.040	0.011	17.871	0.654	0.654	0.000	0.000	0.000	0.000
88	A	88	MET	0	-0.049	-0.017	18.432	-0.604	-0.604	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.001	0.003	18.108	0.745	0.745	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.844	0.923	21.205	11.544	11.544	0.000	0.000	0.000	0.000
91	A	91	SER	0	0.007	0.006	23.470	-0.036	-0.036	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.016	-0.003	24.788	0.374	0.374	0.000	0.000	0.000	0.000
93	A	93	PRO	0	0.011	0.009	27.149	-0.372	-0.372	0.000	0.000	0.000	0.000
94	A	94	SER	0	0.045	0.019	26.565	-0.503	-0.503	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.016	-0.023	28.479	0.206	0.206	0.000	0.000	0.000	0.000
96	A	96	GLY	-1	-0.931	-0.935	30.583	-9.601	-9.601	0.000	0.000	0.000	0.000

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