FMO DATABASE

FMODB ID: 1YK8Z

Calculation Name: 6A2B-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6A2B

Chain ID: B

ChEMBL ID:

UniProt ID: Q9IA97

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	94
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-694033.072388
FMO2-HF: Nuclear repulsion	655446.448897
FMO2-HF: Total energy	-38586.623491
FMO2-MP2: Total energy	-38698.289178

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:ILE)

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

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.
23.128	29.774	4.263	-4.115	-6.796	-0.039

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.843 / q_NPA : 0.912

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	3	PRO	0	0.026	0.021	3.328	0.093	1.883	0.067	-0.484	-1.372	-0.002
4	A	4	PRO	0	0.014	0.004	4.623	1.478	1.517	-0.001	-0.008	-0.031	0.000
30	A	30	HIS	0	0.010	-0.010	3.438	-0.653	-0.120	0.009	-0.122	-0.421	0.000
31	A	31	PRO	0	0.006	-0.011	2.274	-23.565	-20.573	3.944	-3.155	-3.781	-0.036
32	A	32	PRO	0	0.062	0.032	5.277	0.218	0.247	-0.001	-0.002	-0.026	0.000
83	A	83	HIS	0	0.013	-0.003	2.667	-0.427	0.161	0.133	-0.133	-0.588	0.000
84	A	84	ASN	0	-0.032	-0.024	2.864	-0.409	0.266	0.112	-0.211	-0.577	-0.001
5	A	5	VAL	0	-0.030	-0.001	7.836	1.221	1.221	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.010	0.007	11.153	0.428	0.428	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.869	0.928	13.755	17.393	17.393	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.014	0.000	17.550	-0.382	-0.382	0.000	0.000	0.000	0.000
9	A	9	TYR	0	0.028	0.015	19.978	0.059	0.059	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.028	0.017	23.941	-0.023	-0.023	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.023	-0.011	27.286	-0.105	-0.105	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.961	-0.967	28.649	-8.601	-8.601	0.000	0.000	0.000	0.000
13	A	13	PRO	0	-0.024	-0.039	30.618	-0.257	-0.257	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.015	0.012	29.245	0.102	0.102	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.867	-0.926	32.229	-8.008	-8.008	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.067	-0.043	32.043	0.024	0.024	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.013	0.004	36.360	0.211	0.211	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.889	0.960	35.712	8.586	8.586	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.001	-0.014	34.094	-0.162	-0.162	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.016	-0.020	30.555	0.036	0.036	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.853	-0.930	27.780	-10.460	-10.460	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.006	0.003	23.982	-0.220	-0.220	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.000	-0.001	21.404	-0.251	-0.251	0.000	0.000	0.000	0.000
24	A	24	CYS	0	-0.063	-0.021	17.869	-0.425	-0.425	0.000	0.000	0.000	0.000
25	A	25	TYR	0	0.013	0.000	16.721	-0.181	-0.181	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.001	0.001	10.734	-0.560	-0.560	0.000	0.000	0.000	0.000
27	A	27	TYR	0	0.053	0.008	11.773	-0.363	-0.363	0.000	0.000	0.000	0.000
28	A	28	ASN	0	0.009	-0.004	8.642	-0.576	-0.576	0.000	0.000	0.000	0.000
29	A	29	TYR	0	0.028	0.040	5.823	-3.972	-3.972	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.923	0.983	7.655	25.624	25.624	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.002	-0.015	8.136	-2.695	-2.695	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.949	-0.948	10.620	-16.776	-16.776	0.000	0.000	0.000	0.000
36	A	36	MET	0	-0.003	-0.015	13.182	-0.954	-0.954	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.866	0.929	15.733	14.596	14.596	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.066	0.039	19.232	-0.446	-0.446	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.817	-0.918	21.646	-12.818	-12.818	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.893	0.942	24.234	9.065	9.065	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.041	-0.036	27.442	0.167	0.167	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.049	-0.021	24.979	0.174	0.174	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.026	-0.004	26.063	-0.105	-0.105	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.933	-0.969	23.221	-12.265	-12.265	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.001	-0.001	25.035	0.416	0.416	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.036	-0.011	26.640	-0.242	-0.242	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.821	-0.907	27.634	-9.770	-9.770	0.000	0.000	0.000	0.000
48	A	48	CYS	0	-0.097	-0.060	24.480	-0.137	-0.137	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.990	0.996	23.758	10.446	10.446	0.000	0.000	0.000	0.000
50	A	50	GLN	0	0.007	-0.009	15.900	0.224	0.224	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.002	-0.001	19.950	0.092	0.092	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.871	-0.935	18.670	-14.854	-14.854	0.000	0.000	0.000	0.000
53	A	53	PRO	0	-0.062	-0.025	13.545	-0.393	-0.393	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.043	0.041	15.141	-0.451	-0.451	0.000	0.000	0.000	0.000
55	A	55	PHE	0	-0.019	-0.034	11.869	-1.903	-1.903	0.000	0.000	0.000	0.000
56	A	56	GLN	0	0.014	0.021	12.977	1.788	1.788	0.000	0.000	0.000	0.000
57	A	57	HIS	0	0.060	0.015	13.471	-1.974	-1.974	0.000	0.000	0.000	0.000
58	A	58	ASN	0	-0.016	-0.003	11.157	-0.783	-0.783	0.000	0.000	0.000	0.000
59	A	59	TRP	0	0.008	0.000	8.712	-3.611	-3.611	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.844	0.950	5.828	36.167	36.167	0.000	0.000	0.000	0.000
61	A	61	TYR	0	0.028	0.001	7.865	1.913	1.913	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.034	-0.031	10.676	-0.818	-0.818	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.004	0.011	13.430	0.649	0.649	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.032	0.014	15.884	-0.322	-0.322	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.862	0.928	18.670	14.268	14.268	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.024	0.018	20.609	-0.043	-0.043	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.022	-0.026	24.222	-0.039	-0.039	0.000	0.000	0.000	0.000
68	A	68	HIS	0	-0.003	0.016	27.050	0.195	0.195	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.013	-0.014	27.986	0.143	0.143	0.000	0.000	0.000	0.000
70	A	70	HIS	0	-0.055	-0.025	31.067	-0.029	-0.029	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.022	0.002	29.374	-0.206	-0.206	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.831	-0.895	33.276	-7.731	-7.731	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.970	0.962	34.610	7.485	7.485	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.023	-0.002	33.362	0.116	0.116	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.844	-0.925	31.579	-9.288	-9.288	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.804	0.916	24.751	11.082	11.082	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.104	0.041	24.508	0.022	0.022	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.845	-0.917	21.263	-12.014	-12.014	0.000	0.000	0.000	0.000
79	A	79	CYS	0	0.013	0.014	17.331	-0.161	-0.161	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.051	-0.024	16.481	-0.606	-0.606	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.020	0.002	10.768	-0.149	-0.149	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.010	-0.019	10.466	-0.858	-0.858	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.012	0.003	6.737	2.230	2.230	0.000	0.000	0.000	0.000
86	A	86	ASN	0	-0.053	-0.014	5.427	2.027	2.027	0.000	0.000	0.000	0.000
87	A	87	PRO	0	0.046	0.023	9.614	0.840	0.840	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.001	0.004	11.570	-1.273	-1.273	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.917	0.968	8.907	24.957	24.957	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.938	0.974	14.254	13.411	13.411	0.000	0.000	0.000	0.000
91	A	91	TYR	0	-0.018	-0.013	11.849	-0.507	-0.507	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.941	0.962	18.160	11.931	11.931	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.013	0.013	21.684	-0.498	-0.498	0.000	0.000	0.000	0.000
94	A	94	ASP	-2	-1.851	-1.918	24.162	-22.430	-22.430	0.000	0.000	0.000	0.000

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