FMO DATABASE

FMODB ID: 896LY

Calculation Name: 2F73-A-Xray372

Preferred Name: Fatty acid-binding protein, liver

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2F73

Chain ID: A

ChEMBL ID: CHEMBL5421

UniProt ID: P07148

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1198775.29606
FMO2-HF: Nuclear repulsion	1145281.733835
FMO2-HF: Total energy	-53493.562224
FMO2-MP2: Total energy	-53648.642583

3D Structure

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.
-0.612	2.932	0.09	-1.938	-1.696	-0.002

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 : 0 / q_Mulliken : 0.014 / q_NPA : 0.007

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	-0.055	-0.019	2.981	-2.413	1.131	0.090	-1.938	-1.696	-0.002
4	A	-4	LEU	0	0.002	0.015	5.402	0.896	0.896	0.000	0.000	0.000	0.000
5	A	-3	TYR	0	-0.050	-0.030	7.167	0.457	0.457	0.000	0.000	0.000	0.000
6	A	-2	PHE	0	0.018	0.004	10.675	0.099	0.099	0.000	0.000	0.000	0.000
7	A	-1	GLN	0	-0.035	-0.020	14.032	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	0	SER	0	0.024	0.006	17.359	0.033	0.033	0.000	0.000	0.000	0.000
9	A	1	MET	0	-0.014	0.004	20.545	-0.002	-0.002	0.000	0.000	0.000	0.000
10	A	2	SER	0	0.004	0.000	23.314	0.004	0.004	0.000	0.000	0.000	0.000
11	A	3	PHE	0	0.039	0.004	22.527	0.013	0.013	0.000	0.000	0.000	0.000
12	A	4	SER	0	-0.011	0.021	24.685	0.021	0.021	0.000	0.000	0.000	0.000
13	A	5	GLY	0	0.030	0.017	26.874	-0.010	-0.010	0.000	0.000	0.000	0.000
14	A	6	LYS	1	0.842	0.908	30.639	0.020	0.020	0.000	0.000	0.000	0.000
15	A	7	TYR	0	-0.030	-0.045	28.859	-0.010	-0.010	0.000	0.000	0.000	0.000
16	A	8	GLN	0	-0.048	-0.028	35.192	0.008	0.008	0.000	0.000	0.000	0.000
17	A	9	LEU	0	0.014	0.014	37.950	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	10	GLN	0	0.000	0.003	39.538	0.000	0.000	0.000	0.000	0.000	0.000
19	A	11	SER	0	0.002	0.004	40.917	0.004	0.004	0.000	0.000	0.000	0.000
20	A	12	GLN	0	0.071	0.024	40.366	0.002	0.002	0.000	0.000	0.000	0.000
21	A	13	GLU	-1	-0.824	-0.877	41.124	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	14	ASN	0	0.032	-0.015	41.288	0.005	0.005	0.000	0.000	0.000	0.000
23	A	15	PHE	0	0.009	0.015	40.784	0.004	0.004	0.000	0.000	0.000	0.000
24	A	16	GLU	-1	-0.873	-0.949	42.507	0.018	0.018	0.000	0.000	0.000	0.000
25	A	17	ALA	0	0.016	0.010	44.329	0.004	0.004	0.000	0.000	0.000	0.000
26	A	18	PHE	0	0.045	0.017	35.026	0.004	0.004	0.000	0.000	0.000	0.000
27	A	19	MET	0	-0.010	-0.009	37.824	0.008	0.008	0.000	0.000	0.000	0.000
28	A	20	LYS	1	0.887	0.923	41.686	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	21	ALA	0	-0.024	0.000	41.428	0.003	0.003	0.000	0.000	0.000	0.000
30	A	22	ILE	0	-0.059	-0.027	36.902	0.005	0.005	0.000	0.000	0.000	0.000
31	A	23	GLY	0	0.001	0.011	39.757	0.006	0.006	0.000	0.000	0.000	0.000
32	A	24	LEU	0	-0.035	-0.020	40.084	0.002	0.002	0.000	0.000	0.000	0.000
33	A	25	PRO	0	0.017	-0.002	43.512	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	26	GLU	-1	-0.785	-0.883	46.956	0.025	0.025	0.000	0.000	0.000	0.000
35	A	27	GLU	-1	-0.796	-0.865	48.976	0.030	0.030	0.000	0.000	0.000	0.000
36	A	28	LEU	0	-0.002	-0.005	43.441	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	29	ILE	0	-0.009	0.019	44.516	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	30	GLN	0	0.012	-0.018	46.373	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	31	LYS	1	0.807	0.884	47.902	-0.032	-0.032	0.000	0.000	0.000	0.000
40	A	32	GLY	0	-0.008	-0.013	44.621	0.000	0.000	0.000	0.000	0.000	0.000
41	A	33	LYS	1	0.805	0.901	44.606	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	34	ASP	-1	-0.841	-0.908	45.653	0.004	0.004	0.000	0.000	0.000	0.000
43	A	35	ILE	0	-0.050	-0.011	43.096	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	36	LYS	1	0.867	0.924	42.605	0.008	0.008	0.000	0.000	0.000	0.000
45	A	37	GLY	0	0.046	0.032	40.867	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	38	VAL	0	0.012	0.006	36.710	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	39	SER	0	-0.007	0.018	33.319	0.009	0.009	0.000	0.000	0.000	0.000
48	A	40	GLU	-1	-0.827	-0.908	29.984	-0.013	-0.013	0.000	0.000	0.000	0.000
49	A	41	ILE	0	0.008	0.014	25.355	0.012	0.012	0.000	0.000	0.000	0.000
50	A	42	VAL	0	-0.009	-0.005	24.503	-0.013	-0.013	0.000	0.000	0.000	0.000
51	A	43	GLN	0	0.034	0.016	19.014	0.030	0.030	0.000	0.000	0.000	0.000
52	A	44	ASN	0	-0.022	-0.021	19.105	0.009	0.009	0.000	0.000	0.000	0.000
53	A	45	GLY	0	0.051	0.025	15.942	0.016	0.016	0.000	0.000	0.000	0.000
54	A	46	LYS	1	0.890	0.954	10.864	-0.352	-0.352	0.000	0.000	0.000	0.000
55	A	47	HIS	0	0.042	0.034	14.031	0.055	0.055	0.000	0.000	0.000	0.000
56	A	48	PHE	0	-0.004	-0.016	17.603	-0.051	-0.051	0.000	0.000	0.000	0.000
57	A	49	LYS	1	0.940	0.991	21.339	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	50	PHE	0	-0.023	-0.027	24.750	-0.023	-0.023	0.000	0.000	0.000	0.000
59	A	51	THR	0	0.033	0.025	27.756	0.016	0.016	0.000	0.000	0.000	0.000
60	A	52	ILE	0	-0.005	-0.010	30.838	-0.012	-0.012	0.000	0.000	0.000	0.000
61	A	53	THR	0	0.036	0.001	33.848	0.005	0.005	0.000	0.000	0.000	0.000
62	A	54	ALA	0	0.003	0.006	36.260	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	55	GLY	0	-0.009	-0.005	38.137	0.003	0.003	0.000	0.000	0.000	0.000
64	A	56	SER	0	-0.038	-0.026	41.910	0.000	0.000	0.000	0.000	0.000	0.000
65	A	57	LYS	1	0.858	0.935	38.118	-0.061	-0.061	0.000	0.000	0.000	0.000
66	A	58	VAL	0	0.003	0.000	35.957	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	59	ILE	0	-0.022	0.003	32.008	0.005	0.005	0.000	0.000	0.000	0.000
68	A	60	GLN	0	-0.037	-0.034	29.481	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	61	ASN	0	-0.003	0.018	26.251	0.024	0.024	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.884	-0.951	22.391	0.129	0.129	0.000	0.000	0.000	0.000
71	A	63	PHE	0	-0.026	-0.035	19.575	0.015	0.015	0.000	0.000	0.000	0.000
72	A	64	THR	0	-0.040	-0.043	14.235	-0.049	-0.049	0.000	0.000	0.000	0.000
73	A	65	VAL	0	-0.019	-0.004	15.007	0.025	0.025	0.000	0.000	0.000	0.000
74	A	66	GLY	0	-0.018	-0.010	13.355	0.007	0.007	0.000	0.000	0.000	0.000
75	A	67	GLU	-1	-0.817	-0.910	12.816	0.615	0.615	0.000	0.000	0.000	0.000
76	A	68	GLU	-1	-0.841	-0.904	15.111	0.309	0.309	0.000	0.000	0.000	0.000
77	A	69	CYS	0	-0.034	0.013	18.095	0.009	0.009	0.000	0.000	0.000	0.000
78	A	70	GLU	-1	-0.897	-0.963	20.360	0.216	0.216	0.000	0.000	0.000	0.000
79	A	71	LEU	0	-0.041	-0.020	23.942	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	72	GLU	-1	-0.857	-0.917	26.808	0.109	0.109	0.000	0.000	0.000	0.000
81	A	73	THR	0	-0.041	-0.050	30.559	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	74	MET	0	0.016	-0.017	32.553	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	75	THR	0	-0.001	0.009	35.783	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	76	GLY	0	0.021	0.001	37.084	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	77	GLU	-1	-0.804	-0.838	32.819	0.102	0.102	0.000	0.000	0.000	0.000
86	A	78	LYS	1	0.850	0.914	28.363	-0.147	-0.147	0.000	0.000	0.000	0.000
87	A	79	VAL	0	-0.036	-0.008	27.280	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	80	LYS	1	0.860	0.907	21.259	-0.342	-0.342	0.000	0.000	0.000	0.000
89	A	81	THR	0	-0.022	-0.026	22.567	-0.012	-0.012	0.000	0.000	0.000	0.000
90	A	82	VAL	0	0.017	0.033	16.847	0.016	0.016	0.000	0.000	0.000	0.000
91	A	83	VAL	0	-0.010	0.019	19.277	-0.039	-0.039	0.000	0.000	0.000	0.000
92	A	84	GLN	0	0.028	0.004	15.204	-0.016	-0.016	0.000	0.000	0.000	0.000
93	A	85	LEU	0	-0.010	-0.004	16.722	0.003	0.003	0.000	0.000	0.000	0.000
94	A	86	GLU	-1	-0.883	-0.946	19.010	-0.084	-0.084	0.000	0.000	0.000	0.000
95	A	87	GLY	0	-0.010	-0.014	21.195	0.007	0.007	0.000	0.000	0.000	0.000
96	A	88	ASP	-1	-0.873	-0.938	20.524	-0.230	-0.230	0.000	0.000	0.000	0.000
97	A	89	ASN	0	-0.048	-0.046	22.100	0.005	0.005	0.000	0.000	0.000	0.000
98	A	90	LYS	1	0.854	0.913	23.575	0.125	0.125	0.000	0.000	0.000	0.000
99	A	91	LEU	0	-0.008	0.023	20.948	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	92	VAL	0	-0.046	-0.031	22.399	0.009	0.009	0.000	0.000	0.000	0.000
101	A	93	THR	0	0.034	0.000	22.369	0.015	0.015	0.000	0.000	0.000	0.000
102	A	94	THR	0	-0.039	-0.037	24.324	-0.020	-0.020	0.000	0.000	0.000	0.000
103	A	95	PHE	0	0.045	0.035	26.106	0.020	0.020	0.000	0.000	0.000	0.000
104	A	96	LYS	1	0.876	0.915	28.693	-0.103	-0.103	0.000	0.000	0.000	0.000
105	A	97	ASN	0	-0.003	-0.003	31.509	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	98	ILE	0	0.001	0.013	31.770	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	99	LYS	1	0.894	0.973	25.847	0.017	0.017	0.000	0.000	0.000	0.000
108	A	100	SER	0	-0.031	-0.022	28.009	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	101	VAL	0	0.059	0.020	27.201	0.000	0.000	0.000	0.000	0.000	0.000
110	A	102	THR	0	-0.007	-0.011	27.007	0.007	0.007	0.000	0.000	0.000	0.000
111	A	103	GLU	-1	-0.753	-0.837	26.742	-0.100	-0.100	0.000	0.000	0.000	0.000
112	A	104	LEU	0	-0.026	0.000	27.221	0.010	0.010	0.000	0.000	0.000	0.000
113	A	105	ASN	0	-0.041	-0.038	28.983	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	106	GLY	0	0.063	0.030	30.595	0.006	0.006	0.000	0.000	0.000	0.000
115	A	107	ASP	-1	-0.812	-0.895	31.351	-0.088	-0.088	0.000	0.000	0.000	0.000
116	A	108	ILE	0	-0.072	-0.019	34.054	0.011	0.011	0.000	0.000	0.000	0.000
117	A	109	ILE	0	0.000	0.001	28.925	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	110	THR	0	0.014	0.001	31.987	0.010	0.010	0.000	0.000	0.000	0.000
119	A	111	ASN	0	-0.030	-0.016	30.666	0.001	0.001	0.000	0.000	0.000	0.000
120	A	112	THR	0	-0.002	-0.015	31.849	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	113	MET	0	-0.068	-0.028	31.549	0.006	0.006	0.000	0.000	0.000	0.000
122	A	114	THR	0	0.008	0.009	33.291	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	115	LEU	0	-0.001	0.001	34.204	0.006	0.006	0.000	0.000	0.000	0.000
124	A	116	GLY	0	0.029	0.012	36.510	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	117	ASP	-1	-0.911	-0.957	38.305	0.012	0.012	0.000	0.000	0.000	0.000
126	A	118	ILE	0	-0.042	-0.010	40.055	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	119	VAL	0	0.015	-0.005	37.134	0.002	0.002	0.000	0.000	0.000	0.000
128	A	120	PHE	0	-0.009	0.012	36.319	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	121	LYS	1	0.864	0.914	36.568	0.015	0.015	0.000	0.000	0.000	0.000
130	A	122	ARG	1	0.830	0.912	35.663	-0.011	-0.011	0.000	0.000	0.000	0.000
131	A	123	ILE	0	0.003	0.009	35.852	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	124	SER	0	0.002	-0.002	35.270	0.006	0.006	0.000	0.000	0.000	0.000
133	A	125	LYS	1	0.906	0.957	36.231	0.030	0.030	0.000	0.000	0.000	0.000
134	A	126	ARG	1	0.845	0.910	28.716	0.096	0.096	0.000	0.000	0.000	0.000
135	A	127	ILE	0	-0.055	-0.024	35.035	0.000	0.000	0.000	0.000	0.000	0.000

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