FMO DATABASE

FMODB ID: G5411

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	OptHSide
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	-1198120.385016
FMO2-HF: Nuclear repulsion	1144627.67745
FMO2-HF: Total energy	-53492.707566
FMO2-MP2: Total energy	-53647.805029

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.
1.677	4.673	-0.002	-1.493	-1.501	0.003

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 : 0.004 / q_NPA : 0.000

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	-0.074	-0.027	3.381	0.506	3.454	-0.001	-1.489	-1.457	0.003
4	A	-4	LEU	0	0.019	0.013	5.286	0.501	0.549	-0.001	-0.004	-0.044	0.000
5	A	-3	TYR	0	-0.051	-0.030	7.500	0.283	0.283	0.000	0.000	0.000	0.000
6	A	-2	PHE	0	0.023	0.013	11.034	0.053	0.053	0.000	0.000	0.000	0.000
7	A	-1	GLN	0	-0.022	-0.024	14.410	0.007	0.007	0.000	0.000	0.000	0.000
8	A	0	SER	0	0.024	0.018	17.545	0.027	0.027	0.000	0.000	0.000	0.000
9	A	1	MET	0	-0.030	-0.014	20.650	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	2	SER	0	0.020	0.000	23.736	0.001	0.001	0.000	0.000	0.000	0.000
11	A	3	PHE	0	0.014	0.000	22.801	0.006	0.006	0.000	0.000	0.000	0.000
12	A	4	SER	0	0.012	0.028	25.045	0.018	0.018	0.000	0.000	0.000	0.000
13	A	5	GLY	0	0.031	0.025	27.299	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	6	LYS	1	0.840	0.912	31.008	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	7	TYR	0	-0.033	-0.062	29.160	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	8	GLN	0	-0.058	-0.037	35.506	0.007	0.007	0.000	0.000	0.000	0.000
17	A	9	LEU	0	-0.002	0.002	38.464	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	10	GLN	0	0.016	-0.001	39.842	0.000	0.000	0.000	0.000	0.000	0.000
19	A	11	SER	0	0.000	0.008	41.221	0.003	0.003	0.000	0.000	0.000	0.000
20	A	12	GLN	0	0.076	0.029	40.681	0.004	0.004	0.000	0.000	0.000	0.000
21	A	13	GLU	-1	-0.846	-0.909	41.232	0.002	0.002	0.000	0.000	0.000	0.000
22	A	14	ASN	0	0.013	-0.015	41.648	0.006	0.006	0.000	0.000	0.000	0.000
23	A	15	PHE	0	0.011	0.003	41.194	0.003	0.003	0.000	0.000	0.000	0.000
24	A	16	GLU	-1	-0.869	-0.945	43.169	0.030	0.030	0.000	0.000	0.000	0.000
25	A	17	ALA	0	0.049	0.029	44.970	0.004	0.004	0.000	0.000	0.000	0.000
26	A	18	PHE	0	0.048	0.030	35.692	0.003	0.003	0.000	0.000	0.000	0.000
27	A	19	MET	0	-0.012	-0.011	38.330	0.008	0.008	0.000	0.000	0.000	0.000
28	A	20	LYS	1	0.880	0.909	42.273	-0.033	-0.033	0.000	0.000	0.000	0.000
29	A	21	ALA	0	-0.021	0.003	41.491	0.003	0.003	0.000	0.000	0.000	0.000
30	A	22	ILE	0	-0.086	-0.042	37.298	0.005	0.005	0.000	0.000	0.000	0.000
31	A	23	GLY	0	0.011	0.023	40.204	0.006	0.006	0.000	0.000	0.000	0.000
32	A	24	LEU	0	-0.028	-0.021	40.865	0.003	0.003	0.000	0.000	0.000	0.000
33	A	25	PRO	0	-0.021	-0.020	44.020	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	26	GLU	-1	-0.781	-0.888	47.300	0.035	0.035	0.000	0.000	0.000	0.000
35	A	27	GLU	-1	-0.838	-0.910	49.633	0.041	0.041	0.000	0.000	0.000	0.000
36	A	28	LEU	0	0.014	-0.012	43.609	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	29	ILE	0	-0.017	0.017	44.913	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	30	GLN	0	0.016	-0.017	46.704	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	31	LYS	1	0.837	0.911	47.846	-0.046	-0.046	0.000	0.000	0.000	0.000
40	A	32	GLY	0	-0.048	-0.026	45.084	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	33	LYS	1	0.837	0.928	45.125	-0.023	-0.023	0.000	0.000	0.000	0.000
42	A	34	ASP	-1	-0.886	-0.930	46.264	0.018	0.018	0.000	0.000	0.000	0.000
43	A	35	ILE	0	-0.016	0.021	43.742	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	36	LYS	1	0.850	0.905	42.705	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	37	GLY	0	0.042	0.038	41.404	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	38	VAL	0	0.000	-0.010	36.540	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	39	SER	0	0.004	0.027	33.280	0.009	0.009	0.000	0.000	0.000	0.000
48	A	40	GLU	-1	-0.844	-0.922	30.392	0.025	0.025	0.000	0.000	0.000	0.000
49	A	41	ILE	0	0.014	0.017	25.767	0.013	0.013	0.000	0.000	0.000	0.000
50	A	42	VAL	0	-0.016	-0.004	24.615	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	43	GLN	0	0.027	0.013	19.455	0.017	0.017	0.000	0.000	0.000	0.000
52	A	44	ASN	0	-0.002	-0.008	19.480	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	45	GLY	0	0.037	0.024	16.137	0.028	0.028	0.000	0.000	0.000	0.000
54	A	46	LYS	1	0.924	0.953	11.189	-0.483	-0.483	0.000	0.000	0.000	0.000
55	A	47	HIS	0	0.038	0.035	14.427	0.061	0.061	0.000	0.000	0.000	0.000
56	A	48	PHE	0	-0.004	-0.020	18.221	-0.050	-0.050	0.000	0.000	0.000	0.000
57	A	49	LYS	1	0.955	1.004	21.708	-0.091	-0.091	0.000	0.000	0.000	0.000
58	A	50	PHE	0	-0.015	-0.022	25.028	-0.024	-0.024	0.000	0.000	0.000	0.000
59	A	51	THR	0	0.025	0.030	28.037	0.013	0.013	0.000	0.000	0.000	0.000
60	A	52	ILE	0	-0.009	-0.013	31.125	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	53	THR	0	0.021	0.026	34.032	0.004	0.004	0.000	0.000	0.000	0.000
62	A	54	ALA	0	-0.011	-0.026	36.667	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	55	GLY	0	0.007	0.010	38.630	0.003	0.003	0.000	0.000	0.000	0.000
64	A	56	SER	0	-0.017	-0.018	42.403	0.000	0.000	0.000	0.000	0.000	0.000
65	A	57	LYS	1	0.932	0.970	39.179	-0.077	-0.077	0.000	0.000	0.000	0.000
66	A	58	VAL	0	0.011	0.006	35.795	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	59	ILE	0	-0.022	0.016	31.931	0.004	0.004	0.000	0.000	0.000	0.000
68	A	60	GLN	0	-0.031	-0.041	29.691	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	61	ASN	0	0.000	0.027	26.491	0.023	0.023	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.886	-0.964	22.706	0.195	0.195	0.000	0.000	0.000	0.000
71	A	63	PHE	0	-0.024	-0.022	19.705	0.013	0.013	0.000	0.000	0.000	0.000
72	A	64	THR	0	-0.015	-0.021	14.282	-0.052	-0.052	0.000	0.000	0.000	0.000
73	A	65	VAL	0	-0.007	-0.019	15.439	0.022	0.022	0.000	0.000	0.000	0.000
74	A	66	GLY	0	-0.058	-0.033	14.155	0.042	0.042	0.000	0.000	0.000	0.000
75	A	67	GLU	-1	-0.891	-0.936	13.776	0.731	0.731	0.000	0.000	0.000	0.000
76	A	68	GLU	-1	-0.906	-0.960	15.378	0.338	0.338	0.000	0.000	0.000	0.000
77	A	69	CYS	0	-0.030	0.019	18.356	0.019	0.019	0.000	0.000	0.000	0.000
78	A	70	GLU	-1	-0.905	-0.978	20.683	0.240	0.240	0.000	0.000	0.000	0.000
79	A	71	LEU	0	-0.054	-0.016	23.655	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	72	GLU	-1	-0.838	-0.920	26.964	0.137	0.137	0.000	0.000	0.000	0.000
81	A	73	THR	0	-0.063	-0.076	30.702	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	74	MET	0	0.011	-0.012	32.780	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	75	THR	0	-0.044	-0.015	35.856	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	76	GLY	0	0.008	0.019	36.179	0.005	0.005	0.000	0.000	0.000	0.000
85	A	77	GLU	-1	-0.790	-0.869	33.147	0.119	0.119	0.000	0.000	0.000	0.000
86	A	78	LYS	1	0.810	0.893	28.939	-0.178	-0.178	0.000	0.000	0.000	0.000
87	A	79	VAL	0	-0.003	0.018	27.428	0.001	0.001	0.000	0.000	0.000	0.000
88	A	80	LYS	1	0.938	0.968	21.840	-0.372	-0.372	0.000	0.000	0.000	0.000
89	A	81	THR	0	-0.034	-0.034	23.158	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	82	VAL	0	0.041	0.045	17.330	0.016	0.016	0.000	0.000	0.000	0.000
91	A	83	VAL	0	-0.012	0.017	19.592	-0.042	-0.042	0.000	0.000	0.000	0.000
92	A	84	GLN	0	0.023	0.014	15.734	0.001	0.001	0.000	0.000	0.000	0.000
93	A	85	LEU	0	0.005	-0.003	16.614	0.000	0.000	0.000	0.000	0.000	0.000
94	A	86	GLU	-1	-0.932	-0.966	18.950	-0.072	-0.072	0.000	0.000	0.000	0.000
95	A	87	GLY	0	-0.023	-0.013	21.234	0.008	0.008	0.000	0.000	0.000	0.000
96	A	88	ASP	-1	-0.870	-0.938	20.599	-0.184	-0.184	0.000	0.000	0.000	0.000
97	A	89	ASN	0	-0.070	-0.046	22.409	0.008	0.008	0.000	0.000	0.000	0.000
98	A	90	LYS	1	0.901	0.939	23.534	0.090	0.090	0.000	0.000	0.000	0.000
99	A	91	LEU	0	-0.018	0.013	21.285	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	92	VAL	0	-0.029	-0.025	22.601	0.004	0.004	0.000	0.000	0.000	0.000
101	A	93	THR	0	0.010	-0.011	22.837	0.015	0.015	0.000	0.000	0.000	0.000
102	A	94	THR	0	0.004	-0.003	24.838	-0.024	-0.024	0.000	0.000	0.000	0.000
103	A	95	PHE	0	0.021	0.012	26.334	0.021	0.021	0.000	0.000	0.000	0.000
104	A	96	LYS	1	0.901	0.930	28.663	-0.121	-0.121	0.000	0.000	0.000	0.000
105	A	97	ASN	0	-0.024	-0.008	31.377	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	98	ILE	0	-0.007	0.010	32.181	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	99	LYS	1	0.969	0.999	26.713	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	100	SER	0	-0.032	-0.021	28.081	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	101	VAL	0	0.057	0.028	27.494	0.001	0.001	0.000	0.000	0.000	0.000
110	A	102	THR	0	-0.009	-0.009	27.103	0.004	0.004	0.000	0.000	0.000	0.000
111	A	103	GLU	-1	-0.781	-0.862	27.178	-0.070	-0.070	0.000	0.000	0.000	0.000
112	A	104	LEU	0	-0.005	0.008	27.563	0.008	0.008	0.000	0.000	0.000	0.000
113	A	105	ASN	0	-0.037	-0.025	29.242	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	106	GLY	0	0.067	0.029	31.018	0.005	0.005	0.000	0.000	0.000	0.000
115	A	107	ASP	-1	-0.827	-0.915	31.806	-0.051	-0.051	0.000	0.000	0.000	0.000
116	A	108	ILE	0	-0.076	-0.019	34.303	0.010	0.010	0.000	0.000	0.000	0.000
117	A	109	ILE	0	-0.001	-0.004	28.995	-0.005	-0.005	0.000	0.000	0.000	0.000
118	A	110	THR	0	0.000	0.000	32.433	0.008	0.008	0.000	0.000	0.000	0.000
119	A	111	ASN	0	-0.059	-0.039	30.609	0.002	0.002	0.000	0.000	0.000	0.000
120	A	112	THR	0	0.010	-0.010	32.173	0.000	0.000	0.000	0.000	0.000	0.000
121	A	113	MET	0	-0.012	0.007	31.673	0.006	0.006	0.000	0.000	0.000	0.000
122	A	114	THR	0	-0.012	-0.018	33.766	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	115	LEU	0	-0.015	0.006	35.040	0.005	0.005	0.000	0.000	0.000	0.000
124	A	116	GLY	0	0.003	-0.002	37.008	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	117	ASP	-1	-0.893	-0.941	38.980	0.019	0.019	0.000	0.000	0.000	0.000
126	A	118	ILE	0	-0.065	-0.028	40.639	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	119	VAL	0	0.006	-0.017	37.500	0.003	0.003	0.000	0.000	0.000	0.000
128	A	120	PHE	0	-0.008	0.020	36.777	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	121	LYS	1	0.898	0.936	36.873	0.004	0.004	0.000	0.000	0.000	0.000
130	A	122	ARG	1	0.862	0.942	35.637	-0.036	-0.036	0.000	0.000	0.000	0.000
131	A	123	ILE	0	0.004	0.004	36.203	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	124	SER	0	0.024	0.011	35.458	0.004	0.004	0.000	0.000	0.000	0.000
133	A	125	LYS	1	0.912	0.969	36.169	0.008	0.008	0.000	0.000	0.000	0.000
134	A	126	ARG	1	0.860	0.925	28.967	0.054	0.054	0.000	0.000	0.000	0.000
135	A	127	ILE	0	-0.039	-0.013	35.311	-0.003	-0.003	0.000	0.000	0.000	0.000

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