FMO DATABASE

FMODB ID: 877NY

Calculation Name: 4A0C-D-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4A0C

Chain ID: D

ChEMBL ID:

UniProt ID: Q86VP6

Base Structure: X-ray

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	89
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-592876.667268
FMO2-HF: Nuclear repulsion	554387.654195
FMO2-HF: Total energy	-38489.013073
FMO2-MP2: Total energy	-38595.267403

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:20:LYS)

Summations of interaction energy for fragment #1(A:20:LYS)

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.
-144.092	-140.406	21.065	-12.304	-12.446	-0.15

Interaction energy analysis for fragmet #1(A:20:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.737 / q_NPA : 1.857

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

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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	22	PHE	0	0.062	0.038	3.068	8.837	11.415	0.020	-1.197	-1.401	-0.004
4	A	23	GLU	-1	-0.871	-0.939	1.765	-219.801	-218.829	21.046	-11.084	-10.933	-0.146
5	A	24	VAL	0	0.039	0.031	4.550	11.399	11.535	-0.001	-0.023	-0.112	0.000
6	A	25	LYS	1	0.925	0.964	6.669	64.036	64.036	0.000	0.000	0.000	0.000
7	A	26	LYS	1	0.986	0.983	9.417	38.699	38.699	0.000	0.000	0.000	0.000
8	A	27	TRP	0	0.016	0.000	11.033	-2.988	-2.988	0.000	0.000	0.000	0.000
9	A	28	ASN	0	0.004	0.008	13.054	1.185	1.185	0.000	0.000	0.000	0.000
10	A	29	ALA	0	0.008	0.014	15.903	-0.520	-0.520	0.000	0.000	0.000	0.000
11	A	30	VAL	0	0.015	-0.003	17.657	0.936	0.936	0.000	0.000	0.000	0.000
12	A	31	ALA	0	0.003	0.003	21.369	-0.430	-0.430	0.000	0.000	0.000	0.000
13	A	32	LEU	0	0.003	0.007	23.490	0.522	0.522	0.000	0.000	0.000	0.000
14	A	33	TRP	0	-0.009	0.000	27.176	-0.235	-0.235	0.000	0.000	0.000	0.000
15	A	34	ALA	0	0.066	0.035	29.441	0.460	0.460	0.000	0.000	0.000	0.000
16	A	35	TRP	0	-0.078	-0.056	32.433	-0.357	-0.357	0.000	0.000	0.000	0.000
17	A	36	ASP	-1	-0.903	-0.950	32.684	-17.818	-17.818	0.000	0.000	0.000	0.000
18	A	37	ILE	0	-0.044	-0.028	34.511	0.462	0.462	0.000	0.000	0.000	0.000
19	A	38	VAL	0	-0.003	0.001	35.278	0.381	0.381	0.000	0.000	0.000	0.000
20	A	39	VAL	0	-0.041	-0.025	34.599	0.304	0.304	0.000	0.000	0.000	0.000
21	A	40	ASP	-1	-0.860	-0.923	33.722	-17.322	-17.322	0.000	0.000	0.000	0.000
22	A	41	ASN	0	0.072	0.031	36.025	0.406	0.406	0.000	0.000	0.000	0.000
23	A	42	CYS	-1	-0.724	-0.714	39.858	-13.773	-13.773	0.000	0.000	0.000	0.000
24	A	43	ALA	0	0.003	-0.006	42.514	0.336	0.336	0.000	0.000	0.000	0.000
25	A	44	ILE	0	-0.056	-0.017	44.173	0.314	0.314	0.000	0.000	0.000	0.000
26	A	45	CYS	0	-0.077	-0.084	45.898	0.276	0.276	0.000	0.000	0.000	0.000
27	A	46	ARG	1	0.923	0.962	44.502	12.876	12.876	0.000	0.000	0.000	0.000
28	A	47	ASN	0	-0.065	-0.031	44.138	0.270	0.270	0.000	0.000	0.000	0.000
29	A	48	HIS	0	0.058	0.031	35.817	0.197	0.197	0.000	0.000	0.000	0.000
30	A	49	ILE	0	0.013	0.011	35.830	0.352	0.352	0.000	0.000	0.000	0.000
31	A	50	MET	0	-0.041	-0.023	35.317	0.159	0.159	0.000	0.000	0.000	0.000
32	A	51	ASP	-1	-0.894	-0.940	39.639	-15.264	-15.264	0.000	0.000	0.000	0.000
33	A	52	LEU	0	-0.002	0.004	42.112	0.348	0.348	0.000	0.000	0.000	0.000
34	A	53	CYS	0	0.009	0.002	44.910	-0.067	-0.067	0.000	0.000	0.000	0.000
35	A	54	ILE	0	0.055	0.006	47.543	0.192	0.192	0.000	0.000	0.000	0.000
36	A	55	GLU	-1	-0.865	-0.911	50.937	-11.281	-11.281	0.000	0.000	0.000	0.000
37	A	56	CYS	0	-0.041	-0.022	49.153	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	57	GLN	0	-0.008	0.020	47.866	0.161	0.161	0.000	0.000	0.000	0.000
39	A	58	ALA	0	-0.004	0.002	51.062	0.162	0.162	0.000	0.000	0.000	0.000
40	A	59	ASN	0	-0.026	-0.012	53.324	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	60	GLN	0	-0.027	-0.022	56.965	0.072	0.072	0.000	0.000	0.000	0.000
42	A	61	ALA	0	0.013	0.005	60.424	0.140	0.140	0.000	0.000	0.000	0.000
43	A	62	SER	0	-0.044	-0.020	57.824	0.016	0.016	0.000	0.000	0.000	0.000
44	A	63	ALA	0	0.052	0.020	55.679	-0.039	-0.039	0.000	0.000	0.000	0.000
45	A	64	THR	0	-0.013	-0.006	52.998	-0.018	-0.018	0.000	0.000	0.000	0.000
46	A	65	SER	0	0.010	-0.008	49.304	-0.111	-0.111	0.000	0.000	0.000	0.000
47	A	66	GLU	-1	-0.906	-0.948	48.140	-13.149	-13.149	0.000	0.000	0.000	0.000
48	A	67	GLU	-1	-0.961	-0.966	47.043	-12.578	-12.578	0.000	0.000	0.000	0.000
49	A	68	CYS	0	-0.051	-0.013	46.409	-0.055	-0.055	0.000	0.000	0.000	0.000
50	A	69	THR	0	0.005	0.008	41.821	-0.342	-0.342	0.000	0.000	0.000	0.000
51	A	70	VAL	0	0.002	0.005	38.405	0.316	0.316	0.000	0.000	0.000	0.000
52	A	71	ALA	0	-0.008	-0.003	41.509	0.115	0.115	0.000	0.000	0.000	0.000
53	A	72	TRP	0	0.001	0.000	33.951	-0.120	-0.120	0.000	0.000	0.000	0.000
54	A	73	GLY	0	0.089	0.052	40.812	0.270	0.270	0.000	0.000	0.000	0.000
55	A	74	VAL	0	0.005	-0.006	40.314	-0.398	-0.398	0.000	0.000	0.000	0.000
56	A	75	CYS	0	-0.068	-0.030	39.854	-0.301	-0.301	0.000	0.000	0.000	0.000
57	A	76	ASN	0	-0.029	-0.021	33.249	-0.077	-0.077	0.000	0.000	0.000	0.000
58	A	77	HIS	1	0.838	0.929	36.980	14.787	14.787	0.000	0.000	0.000	0.000
59	A	78	ALA	0	0.050	0.029	37.828	0.149	0.149	0.000	0.000	0.000	0.000
60	A	79	PHE	0	0.009	-0.007	39.790	0.063	0.063	0.000	0.000	0.000	0.000
61	A	80	HIS	1	0.804	0.811	42.650	14.052	14.052	0.000	0.000	0.000	0.000
62	A	81	PHE	0	0.028	0.006	44.506	0.182	0.182	0.000	0.000	0.000	0.000
63	A	82	HIS	0	0.030	0.014	46.493	0.347	0.347	0.000	0.000	0.000	0.000
64	A	83	CYS	0	-0.041	-0.032	47.368	0.265	0.265	0.000	0.000	0.000	0.000
65	A	84	ILE	0	0.010	0.012	46.219	0.241	0.241	0.000	0.000	0.000	0.000
66	A	85	SER	0	0.021	-0.003	48.821	0.223	0.223	0.000	0.000	0.000	0.000
67	A	86	ARG	1	0.780	0.864	51.539	11.701	11.701	0.000	0.000	0.000	0.000
68	A	87	TRP	0	-0.028	-0.024	50.840	0.240	0.240	0.000	0.000	0.000	0.000
69	A	88	LEU	0	0.002	0.000	50.180	0.134	0.134	0.000	0.000	0.000	0.000
70	A	89	LYS	1	0.904	0.974	54.025	10.796	10.796	0.000	0.000	0.000	0.000
71	A	90	THR	0	-0.040	-0.018	57.177	0.104	0.104	0.000	0.000	0.000	0.000
72	A	91	ARG	1	0.911	0.965	53.933	11.164	11.164	0.000	0.000	0.000	0.000
73	A	92	GLN	0	-0.002	-0.021	52.843	0.097	0.097	0.000	0.000	0.000	0.000
74	A	93	VAL	0	0.021	0.016	50.757	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	94	CYS	0	-0.012	-0.007	44.620	-0.191	-0.191	0.000	0.000	0.000	0.000
76	A	95	PRO	0	0.010	0.012	46.886	-0.068	-0.068	0.000	0.000	0.000	0.000
77	A	96	LEU	0	-0.003	-0.005	41.280	-0.044	-0.044	0.000	0.000	0.000	0.000
78	A	97	ASP	-1	-0.750	-0.898	43.218	-14.317	-14.317	0.000	0.000	0.000	0.000
79	A	98	ASN	0	-0.118	-0.041	45.274	0.281	0.281	0.000	0.000	0.000	0.000
80	A	99	ARG	1	0.902	0.951	44.006	13.870	13.870	0.000	0.000	0.000	0.000
81	A	100	GLU	-1	-0.851	-0.925	47.814	-11.683	-11.683	0.000	0.000	0.000	0.000
82	A	101	TRP	0	-0.076	-0.028	42.911	-0.168	-0.168	0.000	0.000	0.000	0.000
83	A	102	GLU	-1	-0.875	-0.940	44.762	-12.930	-12.930	0.000	0.000	0.000	0.000
84	A	103	PHE	0	-0.001	-0.011	44.773	-0.068	-0.068	0.000	0.000	0.000	0.000
85	A	104	GLN	0	-0.029	-0.023	39.640	-0.067	-0.067	0.000	0.000	0.000	0.000
86	A	105	LYS	1	0.880	0.947	34.767	16.837	16.837	0.000	0.000	0.000	0.000
87	A	106	TYR	0	0.026	0.016	40.617	0.270	0.270	0.000	0.000	0.000	0.000
88	A	107	GLY	0	0.005	0.008	39.344	-0.185	-0.185	0.000	0.000	0.000	0.000
89	A	108	HIS	-1	-0.913	-0.963	31.771	-17.265	-17.265	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:20:LYS)