FMO DATABASE

FMODB ID: 3K5KL

Calculation Name: 2F73-A-Xray547

Preferred Name: Fatty acid-binding protein, liver

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F73

Chain ID: A

ChEMBL ID: CHEMBL5421

UniProt ID: P07148

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	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1195609.499951
FMO2-HF: Nuclear repulsion	1142116.522616
FMO2-HF: Total energy	-53492.977335
FMO2-MP2: Total energy	-53647.991989

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:-7:THR)

Summations of interaction energy for fragment #1(A:-7:THR)

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.
7.091	8.714	-0.031	-0.473	-1.119	-0.001

Interaction energy analysis for fragmet #1(A:-7:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.771 / q_NPA : 0.876

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	-5	ASN	0	-0.018	-0.006	3.753	12.180	13.803	-0.031	-0.473	-1.119	-0.001
4	A	-4	LEU	0	0.011	0.012	6.659	2.395	2.395	0.000	0.000	0.000	0.000
5	A	-3	TYR	0	-0.030	-0.016	7.954	1.400	1.400	0.000	0.000	0.000	0.000
6	A	-2	PHE	0	0.026	0.013	12.091	0.777	0.777	0.000	0.000	0.000	0.000
7	A	-1	GLN	0	-0.040	-0.026	15.384	0.387	0.387	0.000	0.000	0.000	0.000
8	A	0	SER	0	0.021	0.012	18.702	0.082	0.082	0.000	0.000	0.000	0.000
9	A	1	MET	0	-0.025	-0.004	21.669	-0.025	-0.025	0.000	0.000	0.000	0.000
10	A	2	SER	0	0.023	-0.003	24.915	-0.068	-0.068	0.000	0.000	0.000	0.000
11	A	3	PHE	0	0.038	0.008	23.207	0.466	0.466	0.000	0.000	0.000	0.000
12	A	4	SER	0	0.002	0.026	25.826	0.299	0.299	0.000	0.000	0.000	0.000
13	A	5	GLY	0	0.019	0.016	28.063	0.196	0.196	0.000	0.000	0.000	0.000
14	A	6	LYS	1	0.872	0.935	31.771	8.251	8.251	0.000	0.000	0.000	0.000
15	A	7	TYR	0	-0.014	-0.045	30.052	0.114	0.114	0.000	0.000	0.000	0.000
16	A	8	GLN	0	-0.057	-0.028	36.194	0.085	0.085	0.000	0.000	0.000	0.000
17	A	9	LEU	0	0.003	0.005	39.034	-0.033	-0.033	0.000	0.000	0.000	0.000
18	A	10	GLN	0	-0.012	-0.010	40.670	0.312	0.312	0.000	0.000	0.000	0.000
19	A	11	SER	0	-0.012	-0.010	42.169	0.206	0.206	0.000	0.000	0.000	0.000
20	A	12	GLN	0	0.046	0.010	41.334	-0.410	-0.410	0.000	0.000	0.000	0.000
21	A	13	GLU	-1	-0.904	-0.934	42.150	-6.914	-6.914	0.000	0.000	0.000	0.000
22	A	14	ASN	0	0.051	-0.005	42.223	-0.120	-0.120	0.000	0.000	0.000	0.000
23	A	15	PHE	0	-0.024	0.007	42.079	-0.093	-0.093	0.000	0.000	0.000	0.000
24	A	16	GLU	-1	-0.860	-0.945	43.667	-6.440	-6.440	0.000	0.000	0.000	0.000
25	A	17	ALA	0	0.014	0.004	45.257	0.013	0.013	0.000	0.000	0.000	0.000
26	A	18	PHE	0	0.057	0.025	36.043	-0.063	-0.063	0.000	0.000	0.000	0.000
27	A	19	MET	0	-0.006	-0.006	39.131	-0.132	-0.132	0.000	0.000	0.000	0.000
28	A	20	LYS	1	0.975	0.985	42.771	6.231	6.231	0.000	0.000	0.000	0.000
29	A	21	ALA	0	-0.028	-0.003	42.079	0.040	0.040	0.000	0.000	0.000	0.000
30	A	22	ILE	0	-0.070	-0.033	37.814	-0.090	-0.090	0.000	0.000	0.000	0.000
31	A	23	GLY	0	0.014	0.019	40.692	-0.064	-0.064	0.000	0.000	0.000	0.000
32	A	24	LEU	0	-0.016	-0.018	41.950	0.034	0.034	0.000	0.000	0.000	0.000
33	A	25	PRO	0	-0.024	-0.016	44.404	0.132	0.132	0.000	0.000	0.000	0.000
34	A	26	GLU	-1	-0.853	-0.930	47.789	-5.986	-5.986	0.000	0.000	0.000	0.000
35	A	27	GLU	-1	-0.890	-0.932	49.971	-5.904	-5.904	0.000	0.000	0.000	0.000
36	A	28	LEU	0	-0.044	-0.037	44.194	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	29	ILE	0	-0.036	0.004	45.623	-0.102	-0.102	0.000	0.000	0.000	0.000
38	A	30	GLN	0	0.019	-0.019	47.352	-0.019	-0.019	0.000	0.000	0.000	0.000
39	A	31	LYS	1	0.938	0.977	48.709	6.193	6.193	0.000	0.000	0.000	0.000
40	A	32	GLY	0	-0.020	-0.027	45.687	-0.053	-0.053	0.000	0.000	0.000	0.000
41	A	33	LYS	1	0.877	0.935	45.791	5.971	5.971	0.000	0.000	0.000	0.000
42	A	34	ASP	-1	-0.886	-0.935	46.569	-6.267	-6.267	0.000	0.000	0.000	0.000
43	A	35	ILE	0	-0.034	-0.006	44.252	0.012	0.012	0.000	0.000	0.000	0.000
44	A	36	LYS	1	0.866	0.936	43.539	6.584	6.584	0.000	0.000	0.000	0.000
45	A	37	GLY	0	0.036	0.032	41.741	0.076	0.076	0.000	0.000	0.000	0.000
46	A	38	VAL	0	0.002	-0.001	37.500	-0.068	-0.068	0.000	0.000	0.000	0.000
47	A	39	SER	0	-0.005	0.005	34.234	-0.035	-0.035	0.000	0.000	0.000	0.000
48	A	40	GLU	-1	-0.943	-0.981	31.068	-9.057	-9.057	0.000	0.000	0.000	0.000
49	A	41	ILE	0	-0.002	0.006	26.574	-0.168	-0.168	0.000	0.000	0.000	0.000
50	A	42	VAL	0	-0.016	-0.008	25.436	0.114	0.114	0.000	0.000	0.000	0.000
51	A	43	GLN	0	0.025	0.013	20.519	0.284	0.284	0.000	0.000	0.000	0.000
52	A	44	ASN	0	-0.030	-0.032	20.056	0.496	0.496	0.000	0.000	0.000	0.000
53	A	45	GLY	0	0.038	0.020	17.223	-0.711	-0.711	0.000	0.000	0.000	0.000
54	A	46	LYS	1	0.926	0.967	11.228	21.315	21.315	0.000	0.000	0.000	0.000
55	A	47	HIS	0	0.040	0.027	14.292	-1.101	-1.101	0.000	0.000	0.000	0.000
56	A	48	PHE	0	0.011	-0.003	18.554	0.422	0.422	0.000	0.000	0.000	0.000
57	A	49	LYS	1	0.993	1.015	22.281	11.469	11.469	0.000	0.000	0.000	0.000
58	A	50	PHE	0	-0.030	-0.028	25.532	0.117	0.117	0.000	0.000	0.000	0.000
59	A	51	THR	0	0.054	0.038	28.646	0.032	0.032	0.000	0.000	0.000	0.000
60	A	52	ILE	0	-0.009	-0.010	31.702	0.122	0.122	0.000	0.000	0.000	0.000
61	A	53	THR	0	0.020	0.020	34.668	0.131	0.131	0.000	0.000	0.000	0.000
62	A	54	ALA	0	0.011	0.001	37.236	0.001	0.001	0.000	0.000	0.000	0.000
63	A	55	GLY	0	0.017	0.013	39.231	0.102	0.102	0.000	0.000	0.000	0.000
64	A	56	SER	0	-0.023	-0.011	43.057	0.000	0.000	0.000	0.000	0.000	0.000
65	A	57	LYS	1	0.916	0.964	39.445	7.535	7.535	0.000	0.000	0.000	0.000
66	A	58	VAL	0	0.007	0.002	36.419	-0.067	-0.067	0.000	0.000	0.000	0.000
67	A	59	ILE	0	-0.004	0.015	32.548	0.035	0.035	0.000	0.000	0.000	0.000
68	A	60	GLN	0	-0.050	-0.042	30.043	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	61	ASN	0	0.012	0.023	27.064	-0.120	-0.120	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.897	-0.954	22.944	-11.661	-11.661	0.000	0.000	0.000	0.000
71	A	63	PHE	0	-0.017	-0.031	20.246	0.035	0.035	0.000	0.000	0.000	0.000
72	A	64	THR	0	-0.034	-0.048	14.309	-0.024	-0.024	0.000	0.000	0.000	0.000
73	A	65	VAL	0	-0.037	-0.022	16.162	0.120	0.120	0.000	0.000	0.000	0.000
74	A	66	GLY	0	-0.027	-0.015	14.373	-1.145	-1.145	0.000	0.000	0.000	0.000
75	A	67	GLU	-1	-0.886	-0.931	14.749	-17.912	-17.912	0.000	0.000	0.000	0.000
76	A	68	GLU	-1	-0.894	-0.950	15.995	-13.193	-13.193	0.000	0.000	0.000	0.000
77	A	69	CYS	0	-0.026	0.034	18.937	0.069	0.069	0.000	0.000	0.000	0.000
78	A	70	GLU	-1	-0.925	-0.980	20.996	-10.658	-10.658	0.000	0.000	0.000	0.000
79	A	71	LEU	0	-0.022	-0.010	24.700	0.023	0.023	0.000	0.000	0.000	0.000
80	A	72	GLU	-1	-0.860	-0.919	27.534	-8.646	-8.646	0.000	0.000	0.000	0.000
81	A	73	THR	0	-0.042	-0.041	31.259	-0.056	-0.056	0.000	0.000	0.000	0.000
82	A	74	MET	0	0.021	0.000	33.359	0.154	0.154	0.000	0.000	0.000	0.000
83	A	75	THR	0	-0.018	-0.003	36.601	0.209	0.209	0.000	0.000	0.000	0.000
84	A	76	GLY	0	-0.007	-0.002	36.794	-0.127	-0.127	0.000	0.000	0.000	0.000
85	A	77	GLU	-1	-0.820	-0.882	33.751	-8.613	-8.613	0.000	0.000	0.000	0.000
86	A	78	LYS	1	0.845	0.910	29.429	9.414	9.414	0.000	0.000	0.000	0.000
87	A	79	VAL	0	-0.020	-0.005	28.096	0.116	0.116	0.000	0.000	0.000	0.000
88	A	80	LYS	1	0.927	0.963	22.198	12.724	12.724	0.000	0.000	0.000	0.000
89	A	81	THR	0	-0.042	-0.032	23.478	0.149	0.149	0.000	0.000	0.000	0.000
90	A	82	VAL	0	0.034	0.040	17.712	-0.280	-0.280	0.000	0.000	0.000	0.000
91	A	83	VAL	0	-0.016	0.018	20.008	0.639	0.639	0.000	0.000	0.000	0.000
92	A	84	GLN	0	0.011	-0.006	16.241	-1.317	-1.317	0.000	0.000	0.000	0.000
93	A	85	LEU	0	-0.002	0.004	17.826	0.702	0.702	0.000	0.000	0.000	0.000
94	A	86	GLU	-1	-0.893	-0.959	20.107	-12.371	-12.371	0.000	0.000	0.000	0.000
95	A	87	GLY	0	-0.020	-0.012	22.422	0.444	0.444	0.000	0.000	0.000	0.000
96	A	88	ASP	-1	-0.865	-0.931	21.668	-12.699	-12.699	0.000	0.000	0.000	0.000
97	A	89	ASN	0	-0.029	-0.017	23.523	-0.270	-0.270	0.000	0.000	0.000	0.000
98	A	90	LYS	1	0.890	0.953	24.926	11.458	11.458	0.000	0.000	0.000	0.000
99	A	91	LEU	0	-0.017	0.006	22.180	-0.621	-0.621	0.000	0.000	0.000	0.000
100	A	92	VAL	0	-0.031	-0.021	23.447	0.661	0.661	0.000	0.000	0.000	0.000
101	A	93	THR	0	0.026	-0.001	23.368	-0.411	-0.411	0.000	0.000	0.000	0.000
102	A	94	THR	0	-0.059	-0.053	25.329	0.481	0.481	0.000	0.000	0.000	0.000
103	A	95	PHE	0	0.056	0.040	26.844	-0.228	-0.228	0.000	0.000	0.000	0.000
104	A	96	LYS	1	0.860	0.913	29.348	9.077	9.077	0.000	0.000	0.000	0.000
105	A	97	ASN	0	-0.014	-0.010	31.889	0.104	0.104	0.000	0.000	0.000	0.000
106	A	98	ILE	0	-0.005	0.013	32.715	0.208	0.208	0.000	0.000	0.000	0.000
107	A	99	LYS	1	0.948	0.992	26.916	10.696	10.696	0.000	0.000	0.000	0.000
108	A	100	SER	0	-0.022	-0.012	28.924	0.335	0.335	0.000	0.000	0.000	0.000
109	A	101	VAL	0	0.034	0.005	28.262	-0.471	-0.471	0.000	0.000	0.000	0.000
110	A	102	THR	0	-0.002	-0.001	28.072	0.550	0.550	0.000	0.000	0.000	0.000
111	A	103	GLU	-1	-0.836	-0.907	27.979	-10.490	-10.490	0.000	0.000	0.000	0.000
112	A	104	LEU	0	-0.011	0.002	28.264	0.373	0.373	0.000	0.000	0.000	0.000
113	A	105	ASN	0	-0.048	-0.027	30.253	-0.147	-0.147	0.000	0.000	0.000	0.000
114	A	106	GLY	0	0.046	0.019	31.843	0.324	0.324	0.000	0.000	0.000	0.000
115	A	107	ASP	-1	-0.810	-0.898	32.569	-8.953	-8.953	0.000	0.000	0.000	0.000
116	A	108	ILE	0	-0.082	-0.027	35.201	0.137	0.137	0.000	0.000	0.000	0.000
117	A	109	ILE	0	0.008	0.001	29.871	-0.268	-0.268	0.000	0.000	0.000	0.000
118	A	110	THR	0	0.003	-0.008	33.276	0.442	0.442	0.000	0.000	0.000	0.000
119	A	111	ASN	0	-0.043	-0.028	31.246	-0.082	-0.082	0.000	0.000	0.000	0.000
120	A	112	THR	0	0.009	-0.014	32.900	0.443	0.443	0.000	0.000	0.000	0.000
121	A	113	MET	0	-0.045	-0.015	32.488	-0.318	-0.318	0.000	0.000	0.000	0.000
122	A	114	THR	0	0.000	-0.004	34.238	0.229	0.229	0.000	0.000	0.000	0.000
123	A	115	LEU	0	0.002	0.007	35.031	-0.272	-0.272	0.000	0.000	0.000	0.000
124	A	116	GLY	0	0.016	0.007	37.004	0.243	0.243	0.000	0.000	0.000	0.000
125	A	117	ASP	-1	-0.899	-0.952	38.854	-7.492	-7.492	0.000	0.000	0.000	0.000
126	A	118	ILE	0	-0.064	-0.018	40.950	0.119	0.119	0.000	0.000	0.000	0.000
127	A	119	VAL	0	0.012	-0.007	38.040	-0.267	-0.267	0.000	0.000	0.000	0.000
128	A	120	PHE	0	-0.004	0.012	37.442	0.186	0.186	0.000	0.000	0.000	0.000
129	A	121	LYS	1	0.943	0.970	37.517	7.497	7.497	0.000	0.000	0.000	0.000
130	A	122	ARG	1	0.868	0.932	36.140	8.400	8.400	0.000	0.000	0.000	0.000
131	A	123	ILE	0	-0.008	0.001	36.991	-0.218	-0.218	0.000	0.000	0.000	0.000
132	A	124	SER	0	0.010	0.001	36.378	0.289	0.289	0.000	0.000	0.000	0.000
133	A	125	LYS	1	0.891	0.955	37.324	7.093	7.093	0.000	0.000	0.000	0.000
134	A	126	ARG	1	0.850	0.913	30.318	9.713	9.713	0.000	0.000	0.000	0.000
135	A	127	ILE	-1	-0.885	-0.927	36.222	-8.006	-8.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-7:THR)