FMO DATABASE

FMODB ID: 3MRML

Calculation Name: 4JGX-A-Xray547

Preferred Name:

Target Type:

Ligand Name: citric acid | palmitic acid

Ligand 3-letter code: CIT | PLM

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4JGX

Chain ID: A

ChEMBL ID:

UniProt ID: P80547

Base Structure: X-ray

Registration Date: 2025-10-05

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	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-920334.332037
FMO2-HF: Nuclear repulsion	875539.569005
FMO2-HF: Total energy	-44794.763032
FMO2-MP2: Total energy	-44926.982243

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:SER)

Summations of interaction energy for fragment #1(A:1: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.
-10.012	-0.27800000000001	7.612	-8.732	-8.613	-0.084

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.790 / q_NPA : 0.890

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	3	LYS	1	0.963	1.004	2.224	51.156	54.412	1.795	-2.111	-2.940	-0.003
4	A	4	VAL	0	-0.008	-0.009	3.061	-9.933	-8.624	0.033	-0.884	-0.458	-0.008
14	A	14	ASP	-1	-0.780	-0.889	2.340	-97.916	-93.066	5.756	-5.618	-4.987	-0.073
17	A	17	ARG	1	0.909	0.956	2.894	53.986	54.305	0.028	-0.119	-0.228	0.000
5	A	5	ASP	-1	-0.867	-0.927	5.760	-30.379	-30.379	0.000	0.000	0.000	0.000
6	A	6	GLY	0	-0.020	-0.023	8.021	1.642	1.642	0.000	0.000	0.000	0.000
7	A	7	PHE	0	-0.061	-0.027	8.971	2.518	2.518	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.050	0.045	8.894	-3.193	-3.193	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.017	-0.034	9.718	-1.416	-1.416	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.007	-0.023	6.997	-2.683	-2.683	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.003	-0.010	4.918	-5.240	-5.240	0.000	0.000	0.000	0.000
12	A	12	ILE	0	0.014	0.005	5.998	-1.451	-1.451	0.000	0.000	0.000	0.000
13	A	13	PHE	0	0.020	0.005	6.464	1.711	1.711	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.026	0.015	5.416	2.917	2.917	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.004	0.001	8.886	2.197	2.197	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.912	-0.955	7.532	-34.427	-34.427	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.020	-0.015	9.762	2.171	2.171	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.050	-0.021	12.329	1.796	1.796	0.000	0.000	0.000	0.000
21	A	21	ASN	0	-0.001	-0.023	10.276	2.692	2.692	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.811	-0.872	13.523	-16.921	-16.921	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.013	-0.002	15.298	0.875	0.875	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.050	-0.035	18.649	1.123	1.123	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.020	-0.008	17.248	1.158	1.158	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.017	0.021	19.473	0.018	0.018	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.923	0.974	20.535	11.073	11.073	0.000	0.000	0.000	0.000
28	A	28	GLN	0	0.045	0.014	20.697	0.485	0.485	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.857	0.954	14.875	19.687	19.687	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.001	-0.003	19.636	0.054	0.054	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.918	-0.978	22.717	-11.258	-11.258	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.011	-0.023	20.169	0.240	0.240	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.046	-0.009	18.960	0.082	0.082	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.913	0.962	22.193	10.786	10.786	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.790	0.885	23.786	13.124	13.124	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.014	0.015	22.257	0.262	0.262	0.000	0.000	0.000	0.000
37	A	37	ASN	0	0.011	-0.010	23.998	0.151	0.151	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.036	-0.036	22.371	0.450	0.450	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.029	0.009	17.616	-0.754	-0.754	0.000	0.000	0.000	0.000
40	A	40	ILE	0	0.009	0.002	17.373	0.784	0.784	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.025	-0.017	16.083	-1.207	-1.207	0.000	0.000	0.000	0.000
42	A	42	PHE	0	0.017	0.006	13.415	1.157	1.157	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.037	-0.014	14.114	-2.222	-2.222	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.019	0.015	11.096	1.080	1.080	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.907	0.938	15.096	15.434	15.434	0.000	0.000	0.000	0.000
46	A	46	ASN	0	0.030	0.001	13.375	1.068	1.068	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.914	0.938	16.729	15.054	15.054	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.004	0.023	16.877	0.651	0.651	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.013	0.013	18.943	0.082	0.082	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.940	0.981	13.835	18.772	18.772	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.016	-0.022	16.111	0.733	0.733	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.824	-0.877	10.575	-26.495	-26.495	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.037	-0.032	12.939	0.774	0.774	0.000	0.000	0.000	0.000
54	A	54	TRP	0	-0.021	-0.015	6.404	-0.219	-0.219	0.000	0.000	0.000	0.000
55	A	55	TYR	0	0.026	0.016	11.683	1.858	1.858	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.018	0.007	11.945	-2.245	-2.245	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.772	-0.855	14.285	-15.724	-15.724	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.001	0.000	16.636	-0.129	-0.129	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.821	0.903	19.231	14.418	14.418	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.040	-0.038	19.114	1.205	1.205	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.808	-0.891	17.059	-16.099	-16.099	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.010	0.000	16.510	-0.432	-0.432	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.853	-0.911	12.508	-23.343	-23.343	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.011	-0.018	8.940	0.910	0.910	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.010	-0.001	8.082	-3.204	-3.204	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.779	0.888	7.351	32.926	32.926	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.024	0.005	9.427	1.411	1.411	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.031	-0.038	13.152	-0.041	-0.041	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.964	0.981	15.979	16.729	16.729	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.015	0.011	15.486	-1.837	-1.837	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.034	-0.020	14.012	0.980	0.980	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.794	0.877	16.082	19.694	19.694	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.039	0.018	19.605	0.786	0.786	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.911	-0.960	20.005	-14.625	-14.625	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.026	-0.026	19.891	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.818	-0.870	21.511	-12.673	-12.673	0.000	0.000	0.000	0.000
77	A	77	ILE	0	-0.048	-0.022	21.336	0.648	0.648	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.010	0.002	19.700	-0.318	-0.318	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.023	0.021	18.587	0.858	0.858	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.048	-0.033	18.557	-0.961	-0.961	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.047	0.030	16.575	0.923	0.923	0.000	0.000	0.000	0.000
82	A	82	SER	0	0.013	0.001	17.971	-0.724	-0.724	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.760	-0.861	12.251	-22.593	-22.593	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.851	-0.918	15.010	-15.018	-15.018	0.000	0.000	0.000	0.000
85	A	85	HIS	0	0.011	-0.024	17.569	0.613	0.613	0.000	0.000	0.000	0.000
86	A	86	PHE	0	0.019	0.017	11.631	0.574	0.574	0.000	0.000	0.000	0.000
87	A	87	GLN	0	0.007	-0.010	14.049	-0.611	-0.611	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.016	-0.006	15.319	0.787	0.787	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.033	-0.015	18.202	0.524	0.524	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.012	-0.004	13.034	0.260	0.260	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.856	-0.911	15.695	-16.938	-16.938	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.016	0.015	18.096	0.651	0.651	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.829	0.906	19.368	15.168	15.168	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.022	-0.006	21.737	0.491	0.491	0.000	0.000	0.000	0.000
95	A	95	ASN	0	0.063	0.023	22.982	-0.078	-0.078	0.000	0.000	0.000	0.000
96	A	96	ALA	0	0.052	0.026	22.909	0.094	0.094	0.000	0.000	0.000	0.000
97	A	97	GLN	0	0.032	-0.001	24.288	0.366	0.366	0.000	0.000	0.000	0.000
98	A	98	ARG	1	0.921	0.960	27.695	9.842	9.842	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.009	0.008	21.566	0.183	0.183	0.000	0.000	0.000	0.000
100	A	100	PHE	0	-0.028	-0.004	25.747	0.075	0.075	0.000	0.000	0.000	0.000
101	A	101	MET	0	0.017	0.007	27.461	0.345	0.345	0.000	0.000	0.000	0.000
102	A	102	THR	0	-0.072	-0.044	28.254	0.184	0.184	0.000	0.000	0.000	0.000
103	A	103	GLY	0	-0.013	0.000	28.356	-0.032	-0.032	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.843	0.932	23.752	11.330	11.330	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.037	-0.007	20.859	-0.746	-0.746	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.923	0.953	22.956	12.218	12.218	0.000	0.000	0.000	0.000
107	A	107	VAL	0	0.054	0.023	23.053	-0.648	-0.648	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.938	0.970	24.369	12.873	12.873	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.038	0.031	24.877	-0.528	-0.528	0.000	0.000	0.000	0.000
110	A	110	ASN	0	0.034	0.005	27.021	0.634	0.634	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.075	0.028	28.124	-0.315	-0.315	0.000	0.000	0.000	0.000
112	A	112	MET	0	0.015	0.010	29.855	0.046	0.046	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.823	0.916	25.057	11.854	11.854	0.000	0.000	0.000	0.000
114	A	114	ALA	0	-0.005	-0.009	25.498	-0.344	-0.344	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.010	0.005	26.449	-0.166	-0.166	0.000	0.000	0.000	0.000
116	A	116	ALA	0	0.008	0.018	26.778	-0.023	-0.023	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.057	-0.038	21.689	-0.321	-0.321	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.925	-0.944	23.235	-11.889	-11.889	0.000	0.000	0.000	0.000
119	A	119	GLY	-1	-0.857	-0.897	24.633	-12.095	-12.095	0.000	0.000	0.000	0.000

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