FMO DATABASE

FMODB ID: 1VY5Z

Calculation Name: 7NSO-Z-Other547

Preferred Name:

Target Type:

Ligand Name: erythromycin a

Ligand 3-letter code: ERY

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7NSO

Chain ID: Z

ChEMBL ID:

UniProt ID:

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	58
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-305819.895335
FMO2-HF: Nuclear repulsion	283447.407628
FMO2-HF: Total energy	-22372.487707
FMO2-MP2: Total energy	-22437.775171

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-9.054	-5.618	1.471	-2.365	-2.541	-0.014

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.860 / 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

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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	4	THR	0	-0.014	-0.025	3.520	-4.339	-2.691	0.013	-0.843	-0.818	-0.002
39	A	40	ASP	-1	-0.875	-0.922	2.177	-45.545	-44.676	1.405	-1.086	-1.188	-0.009
40	A	41	THR	0	-0.021	-0.011	3.377	-8.008	-7.089	0.053	-0.436	-0.535	-0.003
4	A	5	ILE	0	-0.021	-0.005	5.273	-0.547	-0.547	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.895	0.964	7.852	21.739	21.739	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.008	-0.005	10.709	0.444	0.444	0.000	0.000	0.000	0.000
7	A	8	THR	0	0.024	0.007	13.711	0.598	0.598	0.000	0.000	0.000	0.000
8	A	9	GLN	0	-0.028	-0.003	17.526	-0.040	-0.040	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.028	-0.002	20.341	0.481	0.481	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.923	0.973	22.767	12.017	12.017	0.000	0.000	0.000	0.000
11	A	12	SER	0	0.065	0.034	25.075	-0.307	-0.307	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.075	0.021	25.474	-0.078	-0.078	0.000	0.000	0.000	0.000
13	A	14	ILE	0	0.042	0.020	27.273	0.021	0.021	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.029	0.022	31.107	0.056	0.056	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.838	0.938	26.222	10.630	10.630	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.095	0.041	26.767	0.203	0.203	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.065	0.023	27.239	-0.377	-0.377	0.000	0.000	0.000	0.000
18	A	19	LYS	1	1.022	1.009	23.373	12.080	12.080	0.000	0.000	0.000	0.000
19	A	20	HIS	0	0.041	0.033	22.701	-0.673	-0.673	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.864	0.928	22.634	9.653	9.653	0.000	0.000	0.000	0.000
21	A	22	ALA	0	0.023	0.008	23.379	-0.285	-0.285	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.008	-0.008	17.704	-0.550	-0.550	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.010	-0.006	18.437	-0.697	-0.697	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.010	-0.005	19.695	-0.383	-0.383	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.003	0.003	18.149	-0.219	-0.219	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.012	0.006	13.444	-0.921	-0.921	0.000	0.000	0.000	0.000
27	A	28	GLY	0	0.014	0.021	15.891	-0.762	-0.762	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.058	-0.020	16.701	0.399	0.399	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.938	0.954	19.963	13.333	13.333	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.942	0.975	23.316	12.363	12.363	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.014	0.000	23.455	-0.499	-0.499	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.031	0.021	23.002	0.295	0.295	0.000	0.000	0.000	0.000
33	A	34	HIS	0	-0.054	-0.012	20.243	0.149	0.149	0.000	0.000	0.000	0.000
34	A	35	THR	0	0.034	0.009	16.726	-0.590	-0.590	0.000	0.000	0.000	0.000
35	A	36	VAL	0	-0.047	-0.034	14.020	0.550	0.550	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.825	-0.881	10.426	-26.581	-26.581	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.811	0.882	9.621	22.071	22.071	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.805	-0.910	5.766	-32.302	-32.302	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.033	0.012	6.184	2.875	2.875	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.023	0.012	8.710	2.135	2.135	0.000	0.000	0.000	0.000
43	A	44	ILE	0	0.050	0.019	8.283	2.090	2.090	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.868	0.920	6.319	34.106	34.106	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.023	0.013	9.924	1.759	1.759	0.000	0.000	0.000	0.000
46	A	47	MET	0	-0.054	-0.029	13.073	1.228	1.228	0.000	0.000	0.000	0.000
47	A	48	ILE	0	0.020	0.003	9.962	1.349	1.349	0.000	0.000	0.000	0.000
48	A	49	ASN	0	-0.014	-0.011	13.876	1.236	1.236	0.000	0.000	0.000	0.000
49	A	50	ALA	0	-0.020	0.005	15.655	1.082	1.082	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.040	-0.037	17.827	1.002	1.002	0.000	0.000	0.000	0.000
51	A	52	SER	0	0.044	0.032	16.995	0.554	0.554	0.000	0.000	0.000	0.000
52	A	53	PHE	0	-0.028	-0.006	18.451	0.320	0.320	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.098	-0.058	20.982	0.892	0.892	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.022	-0.007	16.136	0.229	0.229	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.869	0.928	16.242	16.963	16.963	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.011	-0.007	9.856	0.111	0.111	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.900	-0.960	12.058	-16.263	-16.263	0.000	0.000	0.000	0.000
58	A	59	GLU	-2	-1.657	-1.794	7.641	-54.101	-54.101	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)