FMO DATABASE

FMODB ID: 97G12

Calculation Name: 3B5K-B-Xray547

Preferred Name: Interleukin-5

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3B5K

Chain ID: B

ChEMBL ID: CHEMBL1163111

UniProt ID: P04401

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-739024.051661
FMO2-HF: Nuclear repulsion	696564.111341
FMO2-HF: Total energy	-42459.94032
FMO2-MP2: Total energy	-42585.14745

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:5:ILE)

Summations of interaction energy for fragment #1(A:5: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.
76.909	79.723	0.246	-1.4	-1.66	-0.01

Interaction energy analysis for fragmet #1(A:5:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.868 / q_NPA : 0.926

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	7	THR	0	0.009	0.012	2.952	-2.919	-0.105	0.246	-1.400	-1.660	-0.010
4	A	8	SER	0	0.037	0.029	4.886	5.093	5.093	0.000	0.000	0.000	0.000
5	A	9	THR	0	0.011	-0.007	6.565	2.496	2.496	0.000	0.000	0.000	0.000
6	A	10	VAL	0	0.102	0.048	6.160	2.149	2.149	0.000	0.000	0.000	0.000
7	A	11	VAL	0	0.042	0.043	8.724	2.105	2.105	0.000	0.000	0.000	0.000
8	A	12	LYS	1	0.982	0.984	11.274	19.778	19.778	0.000	0.000	0.000	0.000
9	A	13	GLU	-1	-0.805	-0.859	11.422	-20.968	-20.968	0.000	0.000	0.000	0.000
10	A	14	THR	0	-0.019	-0.039	11.658	1.118	1.118	0.000	0.000	0.000	0.000
11	A	15	LEU	0	-0.013	-0.009	14.264	1.104	1.104	0.000	0.000	0.000	0.000
12	A	16	THR	0	-0.002	-0.007	16.704	1.159	1.159	0.000	0.000	0.000	0.000
13	A	17	GLN	0	0.034	0.016	14.217	1.010	1.010	0.000	0.000	0.000	0.000
14	A	18	LEU	0	0.010	0.013	18.376	0.666	0.666	0.000	0.000	0.000	0.000
15	A	19	SER	0	-0.050	-0.023	20.175	0.846	0.846	0.000	0.000	0.000	0.000
16	A	20	ALA	0	0.020	0.007	21.679	0.489	0.489	0.000	0.000	0.000	0.000
17	A	21	HIS	0	0.004	0.003	20.184	0.582	0.582	0.000	0.000	0.000	0.000
18	A	22	ARG	1	0.951	0.986	23.908	12.187	12.187	0.000	0.000	0.000	0.000
19	A	23	ALA	0	0.043	0.013	25.947	0.229	0.229	0.000	0.000	0.000	0.000
20	A	24	LEU	0	0.000	0.008	25.582	0.245	0.245	0.000	0.000	0.000	0.000
21	A	25	LEU	0	-0.032	-0.038	22.253	0.075	0.075	0.000	0.000	0.000	0.000
22	A	26	THR	0	-0.033	-0.014	26.946	0.044	0.044	0.000	0.000	0.000	0.000
23	A	27	SER	0	-0.012	0.011	29.906	0.407	0.407	0.000	0.000	0.000	0.000
24	A	28	ASN	0	0.014	0.010	31.561	0.402	0.402	0.000	0.000	0.000	0.000
25	A	29	GLU	-1	-0.854	-0.924	32.983	-8.539	-8.539	0.000	0.000	0.000	0.000
26	A	30	THR	0	-0.032	-0.012	35.509	0.253	0.253	0.000	0.000	0.000	0.000
27	A	31	LEU	0	-0.024	0.000	28.939	0.019	0.019	0.000	0.000	0.000	0.000
28	A	32	ARG	1	0.823	0.899	32.797	8.913	8.913	0.000	0.000	0.000	0.000
29	A	33	LEU	0	-0.002	0.000	26.484	-0.171	-0.171	0.000	0.000	0.000	0.000
30	A	34	PRO	0	-0.001	0.009	26.411	0.274	0.274	0.000	0.000	0.000	0.000
31	A	35	VAL	0	0.002	-0.009	27.048	-0.488	-0.488	0.000	0.000	0.000	0.000
32	A	36	PRO	0	-0.012	-0.005	24.775	0.363	0.363	0.000	0.000	0.000	0.000
33	A	37	THR	0	0.002	0.006	28.120	0.028	0.028	0.000	0.000	0.000	0.000
34	A	38	HIS	0	0.057	0.036	25.970	0.149	0.149	0.000	0.000	0.000	0.000
35	A	39	LYS	1	0.950	0.958	24.803	11.035	11.035	0.000	0.000	0.000	0.000
36	A	40	ASN	0	0.063	0.048	23.610	-1.111	-1.111	0.000	0.000	0.000	0.000
37	A	41	HIS	0	0.035	-0.010	19.869	-0.141	-0.141	0.000	0.000	0.000	0.000
38	A	42	GLN	0	0.004	-0.010	16.126	-0.808	-0.808	0.000	0.000	0.000	0.000
39	A	43	LEU	0	-0.004	0.010	19.506	-0.301	-0.301	0.000	0.000	0.000	0.000
40	A	44	CYS	0	-0.023	0.006	21.792	0.594	0.594	0.000	0.000	0.000	0.000
41	A	45	ILE	0	-0.006	-0.005	16.218	-0.205	-0.205	0.000	0.000	0.000	0.000
42	A	46	GLY	0	0.016	0.015	19.356	-0.486	-0.486	0.000	0.000	0.000	0.000
43	A	47	GLU	-1	-0.824	-0.927	21.465	-13.129	-13.129	0.000	0.000	0.000	0.000
44	A	48	ILE	0	-0.004	0.000	19.248	0.161	0.161	0.000	0.000	0.000	0.000
45	A	49	PHE	0	-0.040	-0.036	14.750	-0.307	-0.307	0.000	0.000	0.000	0.000
46	A	50	GLN	0	0.009	0.009	19.954	-0.115	-0.115	0.000	0.000	0.000	0.000
47	A	51	GLY	0	0.023	0.009	23.323	0.426	0.426	0.000	0.000	0.000	0.000
48	A	52	LEU	0	-0.027	-0.015	17.830	0.173	0.173	0.000	0.000	0.000	0.000
49	A	53	ASP	-1	-0.826	-0.904	20.668	-14.835	-14.835	0.000	0.000	0.000	0.000
50	A	54	ILE	0	0.013	0.009	22.819	0.344	0.344	0.000	0.000	0.000	0.000
51	A	55	LEU	0	0.003	0.018	23.261	0.328	0.328	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.834	0.892	18.333	16.379	16.379	0.000	0.000	0.000	0.000
53	A	57	ASN	0	-0.070	-0.040	23.849	0.016	0.016	0.000	0.000	0.000	0.000
54	A	58	GLN	0	-0.020	-0.004	26.468	0.701	0.701	0.000	0.000	0.000	0.000
55	A	59	THR	0	-0.042	-0.005	24.724	0.269	0.269	0.000	0.000	0.000	0.000
56	A	60	VAL	0	0.004	-0.008	27.010	-0.200	-0.200	0.000	0.000	0.000	0.000
57	A	61	ARG	1	0.793	0.861	20.610	13.723	13.723	0.000	0.000	0.000	0.000
58	A	62	GLY	0	0.001	-0.007	23.223	0.400	0.400	0.000	0.000	0.000	0.000
59	A	63	GLY	0	0.023	0.021	23.896	0.051	0.051	0.000	0.000	0.000	0.000
60	A	64	THR	0	-0.012	-0.036	21.159	-0.763	-0.763	0.000	0.000	0.000	0.000
61	A	65	VAL	0	0.028	0.016	19.862	-0.732	-0.732	0.000	0.000	0.000	0.000
62	A	66	GLU	-1	-0.711	-0.817	18.582	-15.324	-15.324	0.000	0.000	0.000	0.000
63	A	67	ARG	1	0.844	0.915	15.054	17.029	17.029	0.000	0.000	0.000	0.000
64	A	68	LEU	0	-0.032	-0.008	14.621	-1.431	-1.431	0.000	0.000	0.000	0.000
65	A	69	PHE	0	0.043	0.003	15.357	-1.108	-1.108	0.000	0.000	0.000	0.000
66	A	70	GLN	0	-0.007	-0.002	12.716	-0.344	-0.344	0.000	0.000	0.000	0.000
67	A	71	ASN	0	-0.028	-0.025	10.532	-2.651	-2.651	0.000	0.000	0.000	0.000
68	A	72	LEU	0	0.001	0.001	10.752	-2.122	-2.122	0.000	0.000	0.000	0.000
69	A	73	SER	0	0.021	0.021	12.667	-1.174	-1.174	0.000	0.000	0.000	0.000
70	A	74	LEU	0	-0.036	-0.020	4.976	-1.679	-1.679	0.000	0.000	0.000	0.000
71	A	75	ILE	0	-0.002	-0.012	8.147	-2.900	-2.900	0.000	0.000	0.000	0.000
72	A	76	LYS	1	0.832	0.917	9.844	19.584	19.584	0.000	0.000	0.000	0.000
73	A	77	LYS	1	0.965	0.974	8.029	28.048	28.048	0.000	0.000	0.000	0.000
74	A	78	TYR	0	-0.021	-0.006	4.851	-1.628	-1.628	0.000	0.000	0.000	0.000
75	A	79	ILE	0	0.020	0.001	7.520	0.862	0.862	0.000	0.000	0.000	0.000
76	A	80	ASP	-1	-0.800	-0.883	11.157	-20.675	-20.675	0.000	0.000	0.000	0.000
77	A	81	ARG	1	0.771	0.839	6.631	28.874	28.874	0.000	0.000	0.000	0.000
78	A	82	GLN	0	-0.004	-0.006	9.202	-1.797	-1.797	0.000	0.000	0.000	0.000
79	A	83	LYS	1	0.968	0.984	11.237	18.053	18.053	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.848	-0.915	11.705	-23.433	-23.433	0.000	0.000	0.000	0.000
81	A	85	LYS	1	0.877	0.927	7.622	34.158	34.158	0.000	0.000	0.000	0.000
82	A	86	CYS	0	-0.082	-0.019	13.927	0.966	0.966	0.000	0.000	0.000	0.000
83	A	87	GLY	0	-0.002	0.000	17.199	0.976	0.976	0.000	0.000	0.000	0.000
84	A	88	GLU	-1	-0.851	-0.886	12.785	-23.097	-23.097	0.000	0.000	0.000	0.000
85	A	89	GLU	-1	-0.911	-0.947	17.003	-15.982	-15.982	0.000	0.000	0.000	0.000
86	A	90	ARG	1	0.938	0.968	19.186	12.582	12.582	0.000	0.000	0.000	0.000
87	A	91	ARG	1	0.920	0.961	20.693	14.291	14.291	0.000	0.000	0.000	0.000
88	A	92	ARG	1	0.978	0.984	24.903	10.375	10.375	0.000	0.000	0.000	0.000
89	A	93	THR	0	0.062	0.014	28.149	-0.255	-0.255	0.000	0.000	0.000	0.000
90	A	94	ARG	1	0.937	0.982	28.268	10.361	10.361	0.000	0.000	0.000	0.000
91	A	95	GLN	0	0.037	0.013	24.391	0.067	0.067	0.000	0.000	0.000	0.000
92	A	96	PHE	0	-0.006	0.012	25.239	-0.373	-0.373	0.000	0.000	0.000	0.000
93	A	97	LEU	0	0.008	-0.010	26.546	-0.066	-0.066	0.000	0.000	0.000	0.000
94	A	98	ASP	-1	-0.847	-0.927	26.164	-11.020	-11.020	0.000	0.000	0.000	0.000
95	A	99	TYR	0	0.014	0.004	19.170	0.016	0.016	0.000	0.000	0.000	0.000
96	A	100	LEU	0	-0.015	-0.009	24.583	-0.105	-0.105	0.000	0.000	0.000	0.000
97	A	101	GLN	0	-0.003	0.001	27.316	0.346	0.346	0.000	0.000	0.000	0.000
98	A	102	GLU	-1	-0.947	-0.972	22.139	-13.721	-13.721	0.000	0.000	0.000	0.000
99	A	103	PHE	0	-0.036	-0.011	23.595	-0.055	-0.055	0.000	0.000	0.000	0.000
100	A	104	LEU	0	-0.011	-0.025	25.662	0.131	0.131	0.000	0.000	0.000	0.000
101	A	105	GLY	0	0.014	0.020	28.586	0.285	0.285	0.000	0.000	0.000	0.000
102	A	106	VAL	0	-0.036	-0.023	23.583	0.156	0.156	0.000	0.000	0.000	0.000
103	A	107	LEU	0	-0.046	-0.018	26.866	0.039	0.039	0.000	0.000	0.000	0.000
104	A	108	SER	0	-0.069	-0.033	28.984	0.329	0.329	0.000	0.000	0.000	0.000
105	A	109	THR	0	-0.092	-0.040	28.041	0.242	0.242	0.000	0.000	0.000	0.000
106	A	110	GLU	-2	-1.926	-1.949	29.358	-20.486	-20.486	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:5:ILE)