FMO DATABASE

FMODB ID: J4J29

Calculation Name: 2CB8-A-Xray547

Preferred Name:

Target Type:

Ligand Name: tetradecanoyl-coa | 2-methoxyethanol

Ligand 3-letter code: MYA | MXE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CB8

Chain ID: A

ChEMBL ID:

UniProt ID: P07108

Base Structure: X-ray

Registration Date: 2025-10-03

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-595330.891873
FMO2-HF: Nuclear repulsion	560461.676448
FMO2-HF: Total energy	-34869.215425
FMO2-MP2: Total energy	-34970.706592

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:SER)

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

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.
-125.668	-129.184	35.011	-18.368	-13.125	-0.148

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.779 / q_NPA : 0.854

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	4	ALA	0	0.064	0.044	3.151	2.579	4.773	0.095	-1.023	-1.266	0.002
4	A	5	GLU	-1	-0.816	-0.872	1.654	-146.250	-154.038	34.605	-16.608	-10.209	-0.145
5	A	6	PHE	0	-0.004	-0.003	4.184	7.964	8.450	0.001	-0.165	-0.321	0.000
67	A	68	GLU	-1	-0.874	-0.939	4.306	-63.178	-62.820	-0.001	-0.069	-0.288	0.000
70	A	71	MET	0	0.004	0.005	3.570	-5.146	-4.670	0.039	-0.162	-0.352	-0.002
71	A	72	LYS	1	0.903	0.956	4.560	41.063	41.137	-0.001	-0.014	-0.058	0.000
74	A	75	ILE	0	0.006	-0.003	2.769	-0.229	0.455	0.273	-0.327	-0.631	-0.003
6	A	7	GLU	-1	-0.951	-0.968	5.557	-22.616	-22.616	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.898	0.929	7.339	34.979	34.979	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.006	0.007	7.629	3.370	3.370	0.000	0.000	0.000	0.000
9	A	10	ALA	0	-0.004	-0.013	9.309	3.243	3.243	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.857	-0.926	11.484	-16.741	-16.741	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.783	-0.874	11.155	-26.017	-26.017	0.000	0.000	0.000	0.000
12	A	13	VAL	0	-0.015	-0.009	13.208	1.731	1.731	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.849	0.929	14.987	19.628	19.628	0.000	0.000	0.000	0.000
14	A	15	HIS	1	0.812	0.894	17.071	18.281	18.281	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.017	0.036	16.303	0.235	0.235	0.000	0.000	0.000	0.000
16	A	17	LYS	1	0.832	0.908	19.695	14.337	14.337	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.040	-0.023	22.571	0.907	0.907	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.923	0.978	22.114	12.002	12.002	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.010	0.005	18.374	0.366	0.366	0.000	0.000	0.000	0.000
20	A	21	SER	0	0.011	-0.019	21.264	0.527	0.527	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.864	-0.956	21.793	-12.798	-12.798	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.929	-0.956	20.887	-14.531	-14.531	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.717	-0.797	18.193	-16.114	-16.114	0.000	0.000	0.000	0.000
24	A	25	MET	0	-0.040	-0.025	17.298	-0.848	-0.848	0.000	0.000	0.000	0.000
25	A	26	LEU	0	0.005	0.011	18.181	-0.708	-0.708	0.000	0.000	0.000	0.000
26	A	27	PHE	0	0.039	0.025	12.387	-0.668	-0.668	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.010	0.009	12.434	-1.544	-1.544	0.000	0.000	0.000	0.000
28	A	29	TYR	0	-0.009	-0.018	13.662	-1.244	-1.244	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.056	0.030	15.282	-0.587	-0.587	0.000	0.000	0.000	0.000
30	A	31	HIS	1	0.855	0.915	10.747	21.913	21.913	0.000	0.000	0.000	0.000
31	A	32	TYR	0	0.027	0.020	10.861	-1.359	-1.359	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.871	0.969	11.918	16.931	16.931	0.000	0.000	0.000	0.000
33	A	34	GLN	0	0.006	-0.017	12.856	0.500	0.500	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.015	-0.008	7.977	-0.622	-0.622	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.042	-0.038	9.772	-0.073	-0.073	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.042	-0.015	11.791	0.499	0.499	0.000	0.000	0.000	0.000
37	A	38	GLY	0	-0.014	0.002	13.972	0.107	0.107	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.773	-0.875	14.723	-16.810	-16.810	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.069	-0.022	18.178	0.265	0.265	0.000	0.000	0.000	0.000
40	A	41	ASN	0	0.005	-0.005	20.700	0.427	0.427	0.000	0.000	0.000	0.000
41	A	42	THR	0	-0.015	-0.006	22.899	0.370	0.370	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.848	-0.916	25.365	-10.714	-10.714	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.751	0.857	27.707	10.576	10.576	0.000	0.000	0.000	0.000
44	A	45	PRO	0	-0.029	-0.011	27.285	0.394	0.394	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.054	0.025	30.271	0.083	0.083	0.000	0.000	0.000	0.000
46	A	47	MET	0	-0.006	-0.024	32.967	-0.146	-0.146	0.000	0.000	0.000	0.000
47	A	48	LEU	0	0.020	-0.002	34.490	-0.051	-0.051	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.811	-0.883	29.564	-10.852	-10.852	0.000	0.000	0.000	0.000
49	A	50	PHE	0	-0.010	-0.031	30.298	-0.356	-0.356	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.005	0.011	25.875	-0.345	-0.345	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.015	-0.015	25.763	-0.580	-0.580	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.914	0.968	25.668	9.818	9.818	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.046	0.034	25.512	-0.239	-0.239	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.917	0.953	21.514	13.029	13.029	0.000	0.000	0.000	0.000
55	A	56	TRP	0	-0.018	-0.020	21.228	-0.729	-0.729	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.769	-0.854	22.593	-11.922	-11.922	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.036	0.019	19.623	-0.287	-0.287	0.000	0.000	0.000	0.000
58	A	59	TRP	0	-0.036	-0.037	16.919	-0.628	-0.628	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.024	-0.029	18.953	-0.491	-0.491	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.938	-0.971	20.337	-14.113	-14.113	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.065	-0.024	14.415	-0.644	-0.644	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.933	0.991	16.711	12.313	12.313	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.018	0.007	18.252	0.520	0.520	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.094	-0.043	12.226	-0.487	-0.487	0.000	0.000	0.000	0.000
65	A	66	SER	0	-0.020	-0.037	10.548	-1.156	-1.156	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.907	0.934	8.904	22.112	22.112	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.855	-0.905	6.087	-34.977	-34.977	0.000	0.000	0.000	0.000
69	A	70	ALA	0	-0.019	-0.006	8.672	-0.071	-0.071	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.001	0.002	5.584	2.508	2.508	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.014	-0.009	7.429	2.478	2.478	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.006	-0.001	6.909	1.908	1.908	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.864	0.930	9.468	21.954	21.954	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.002	-0.002	9.966	2.231	2.231	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.854	-0.918	9.391	-26.965	-26.965	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.923	-0.929	12.208	-17.203	-17.203	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.003	-0.014	14.567	1.454	1.454	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.818	0.871	11.361	27.381	27.381	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.890	0.957	14.042	22.505	22.505	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.821	0.918	18.478	15.441	15.441	0.000	0.000	0.000	0.000
84	A	85	TYR	0	-0.055	-0.074	19.569	1.068	1.068	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.022	0.029	20.207	0.683	0.683	0.000	0.000	0.000	0.000
86	A	87	ILE	-1	-0.857	-0.916	15.815	-15.309	-15.309	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:2:SER)