FMO DATABASE

FMODB ID: 1N3RZ

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	OptH
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	-1197591.358456
FMO2-HF: Nuclear repulsion	1144100.445552
FMO2-HF: Total energy	-53490.912904
FMO2-MP2: Total energy	-53646.136188

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.
2.161	3.896	-0.008	-0.67	-1.056	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 : -0.055 / q_NPA : -0.038

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	-0.064	-0.031	3.643	2.134	3.869	-0.008	-0.670	-1.056	0.002
4	A	-4	LEU	0	0.011	0.014	5.917	-0.228	-0.228	0.000	0.000	0.000	0.000
5	A	-3	TYR	0	-0.031	-0.019	7.974	-0.015	-0.015	0.000	0.000	0.000	0.000
6	A	-2	PHE	0	0.017	0.011	11.530	0.006	0.006	0.000	0.000	0.000	0.000
7	A	-1	GLN	0	-0.027	-0.031	15.000	-0.036	-0.036	0.000	0.000	0.000	0.000
8	A	0	SER	0	0.008	0.020	18.077	0.023	0.023	0.000	0.000	0.000	0.000
9	A	1	MET	0	-0.007	-0.005	21.129	-0.018	-0.018	0.000	0.000	0.000	0.000
10	A	2	SER	0	0.021	-0.004	23.979	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	3	PHE	0	0.000	0.000	22.935	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	4	SER	0	0.034	0.018	25.135	0.006	0.006	0.000	0.000	0.000	0.000
13	A	5	GLY	0	0.014	0.017	27.386	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	6	LYS	1	0.943	0.966	31.068	0.007	0.007	0.000	0.000	0.000	0.000
15	A	7	TYR	0	-0.024	-0.037	29.578	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	8	GLN	0	-0.049	-0.025	35.678	0.000	0.000	0.000	0.000	0.000	0.000
17	A	9	LEU	0	-0.006	-0.002	38.630	0.001	0.001	0.000	0.000	0.000	0.000
18	A	10	GLN	0	-0.022	-0.027	40.096	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	11	SER	0	-0.007	-0.003	41.592	0.000	0.000	0.000	0.000	0.000	0.000
20	A	12	GLN	0	0.032	0.004	41.030	0.006	0.006	0.000	0.000	0.000	0.000
21	A	13	GLU	-1	-0.940	-0.974	41.596	0.055	0.055	0.000	0.000	0.000	0.000
22	A	14	ASN	0	0.031	0.002	41.987	0.006	0.006	0.000	0.000	0.000	0.000
23	A	15	PHE	0	0.012	0.012	41.448	0.004	0.004	0.000	0.000	0.000	0.000
24	A	16	GLU	-1	-0.864	-0.945	43.459	0.049	0.049	0.000	0.000	0.000	0.000
25	A	17	ALA	0	0.026	0.021	45.154	0.001	0.001	0.000	0.000	0.000	0.000
26	A	18	PHE	0	0.070	0.032	36.232	0.003	0.003	0.000	0.000	0.000	0.000
27	A	19	MET	0	0.011	0.000	38.680	0.005	0.005	0.000	0.000	0.000	0.000
28	A	20	LYS	1	0.957	0.963	42.485	-0.055	-0.055	0.000	0.000	0.000	0.000
29	A	21	ALA	0	-0.041	-0.009	41.545	0.001	0.001	0.000	0.000	0.000	0.000
30	A	22	ILE	0	-0.094	-0.044	37.596	0.003	0.003	0.000	0.000	0.000	0.000
31	A	23	GLY	0	0.016	0.026	40.418	0.002	0.002	0.000	0.000	0.000	0.000
32	A	24	LEU	0	-0.031	-0.026	41.733	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	25	PRO	0	-0.023	-0.022	44.231	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	26	GLU	-1	-0.904	-0.961	47.496	0.043	0.043	0.000	0.000	0.000	0.000
35	A	27	GLU	-1	-0.820	-0.904	49.594	0.036	0.036	0.000	0.000	0.000	0.000
36	A	28	LEU	0	-0.044	-0.044	44.097	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	29	ILE	0	-0.031	0.009	45.372	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	30	GLN	0	0.054	0.009	46.914	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	31	LYS	1	0.901	0.949	47.828	-0.035	-0.035	0.000	0.000	0.000	0.000
40	A	32	GLY	0	-0.045	-0.036	45.233	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	33	LYS	1	0.935	0.997	45.331	-0.036	-0.036	0.000	0.000	0.000	0.000
42	A	34	ASP	-1	-0.965	-0.986	46.546	0.036	0.036	0.000	0.000	0.000	0.000
43	A	35	ILE	0	-0.028	0.022	43.810	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	36	LYS	1	0.884	0.927	42.892	-0.034	-0.034	0.000	0.000	0.000	0.000
45	A	37	GLY	0	0.034	0.031	41.485	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	38	VAL	0	-0.023	-0.018	36.471	0.001	0.001	0.000	0.000	0.000	0.000
47	A	39	SER	0	0.020	0.020	33.298	0.004	0.004	0.000	0.000	0.000	0.000
48	A	40	GLU	-1	-0.938	-0.981	30.415	0.004	0.004	0.000	0.000	0.000	0.000
49	A	41	ILE	0	0.023	0.028	25.875	0.008	0.008	0.000	0.000	0.000	0.000
50	A	42	VAL	0	-0.034	-0.019	24.631	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	43	GLN	0	0.025	0.008	20.005	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	44	ASN	0	-0.001	-0.005	19.147	-0.008	-0.008	0.000	0.000	0.000	0.000
53	A	45	GLY	0	0.023	0.010	16.151	0.004	0.004	0.000	0.000	0.000	0.000
54	A	46	LYS	1	0.980	0.977	9.814	-0.272	-0.272	0.000	0.000	0.000	0.000
55	A	47	HIS	0	-0.011	0.011	13.973	0.011	0.011	0.000	0.000	0.000	0.000
56	A	48	PHE	0	-0.001	-0.019	18.155	-0.029	-0.029	0.000	0.000	0.000	0.000
57	A	49	LYS	1	1.013	1.030	21.711	0.002	0.002	0.000	0.000	0.000	0.000
58	A	50	PHE	0	-0.034	-0.026	24.938	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	51	THR	0	0.046	0.030	28.042	0.005	0.005	0.000	0.000	0.000	0.000
60	A	52	ILE	0	-0.021	-0.019	30.969	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	53	THR	0	0.005	0.021	34.105	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	54	ALA	0	-0.020	-0.020	36.859	0.001	0.001	0.000	0.000	0.000	0.000
63	A	55	GLY	0	0.021	0.019	38.777	0.000	0.000	0.000	0.000	0.000	0.000
64	A	56	SER	0	-0.018	-0.021	42.556	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	57	LYS	1	0.939	0.965	39.484	-0.059	-0.059	0.000	0.000	0.000	0.000
66	A	58	VAL	0	0.010	0.011	35.956	0.002	0.002	0.000	0.000	0.000	0.000
67	A	59	ILE	0	-0.003	0.030	31.842	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	60	GLN	0	-0.008	-0.022	29.739	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	61	ASN	0	-0.018	0.035	26.382	0.011	0.011	0.000	0.000	0.000	0.000
70	A	62	GLU	-1	-0.898	-0.969	22.433	0.052	0.052	0.000	0.000	0.000	0.000
71	A	63	PHE	0	-0.032	-0.029	20.192	0.013	0.013	0.000	0.000	0.000	0.000
72	A	64	THR	0	0.022	0.013	14.165	-0.051	-0.051	0.000	0.000	0.000	0.000
73	A	65	VAL	0	-0.023	-0.027	15.720	0.024	0.024	0.000	0.000	0.000	0.000
74	A	66	GLY	0	-0.064	-0.039	14.409	0.042	0.042	0.000	0.000	0.000	0.000
75	A	67	GLU	-1	-0.902	-0.956	14.379	0.399	0.399	0.000	0.000	0.000	0.000
76	A	68	GLU	-1	-0.963	-0.994	15.602	0.316	0.316	0.000	0.000	0.000	0.000
77	A	69	CYS	0	-0.040	0.018	18.622	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	70	GLU	-1	-0.898	-0.987	20.914	0.149	0.149	0.000	0.000	0.000	0.000
79	A	71	LEU	0	-0.032	-0.016	23.914	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	72	GLU	-1	-0.916	-0.984	27.146	0.078	0.078	0.000	0.000	0.000	0.000
81	A	73	THR	0	-0.039	-0.028	30.866	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	74	MET	0	0.020	-0.013	32.990	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	75	THR	0	-0.045	-0.011	36.036	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	76	GLY	0	0.009	0.024	36.373	0.001	0.001	0.000	0.000	0.000	0.000
85	A	77	GLU	-1	-0.936	-1.010	33.721	0.113	0.113	0.000	0.000	0.000	0.000
86	A	78	LYS	1	0.878	0.958	29.512	-0.102	-0.102	0.000	0.000	0.000	0.000
87	A	79	VAL	0	0.010	0.025	27.822	0.004	0.004	0.000	0.000	0.000	0.000
88	A	80	LYS	1	0.988	1.003	22.846	-0.254	-0.254	0.000	0.000	0.000	0.000
89	A	81	THR	0	-0.043	-0.041	23.384	0.009	0.009	0.000	0.000	0.000	0.000
90	A	82	VAL	0	0.050	0.044	17.393	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	83	VAL	0	-0.008	0.018	19.789	-0.021	-0.021	0.000	0.000	0.000	0.000
92	A	84	GLN	0	0.011	0.007	16.302	0.053	0.053	0.000	0.000	0.000	0.000
93	A	85	LEU	0	0.008	-0.001	17.097	-0.037	-0.037	0.000	0.000	0.000	0.000
94	A	86	GLU	-1	-0.949	-0.976	19.407	0.211	0.211	0.000	0.000	0.000	0.000
95	A	87	GLY	0	-0.018	-0.008	21.728	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	88	ASP	-1	-0.860	-0.934	21.140	0.071	0.071	0.000	0.000	0.000	0.000
97	A	89	ASN	0	-0.039	-0.025	22.967	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	90	LYS	1	0.962	0.983	24.042	-0.125	-0.125	0.000	0.000	0.000	0.000
99	A	91	LEU	0	-0.020	0.012	21.775	0.017	0.017	0.000	0.000	0.000	0.000
100	A	92	VAL	0	-0.028	-0.030	22.965	-0.016	-0.016	0.000	0.000	0.000	0.000
101	A	93	THR	0	0.025	0.004	23.138	0.020	0.020	0.000	0.000	0.000	0.000
102	A	94	THR	0	0.005	-0.007	25.094	-0.025	-0.025	0.000	0.000	0.000	0.000
103	A	95	PHE	0	0.004	0.010	26.408	0.014	0.014	0.000	0.000	0.000	0.000
104	A	96	LYS	1	0.988	1.006	28.778	-0.132	-0.132	0.000	0.000	0.000	0.000
105	A	97	ASN	0	-0.017	-0.006	31.348	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	98	ILE	0	-0.027	0.001	32.228	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	99	LYS	1	0.987	1.008	27.553	-0.163	-0.163	0.000	0.000	0.000	0.000
108	A	100	SER	0	-0.036	-0.022	28.385	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	101	VAL	0	0.052	0.030	27.813	0.014	0.014	0.000	0.000	0.000	0.000
110	A	102	THR	0	-0.025	-0.019	27.366	-0.015	-0.015	0.000	0.000	0.000	0.000
111	A	103	GLU	-1	-0.892	-0.940	27.609	0.092	0.092	0.000	0.000	0.000	0.000
112	A	104	LEU	0	-0.017	-0.002	27.339	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	105	ASN	0	0.007	0.002	29.767	0.004	0.004	0.000	0.000	0.000	0.000
114	A	106	GLY	0	0.042	0.015	31.501	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	107	ASP	-1	-0.853	-0.933	32.190	0.006	0.006	0.000	0.000	0.000	0.000
116	A	108	ILE	0	-0.082	-0.027	34.655	0.000	0.000	0.000	0.000	0.000	0.000
117	A	109	ILE	0	-0.001	-0.003	29.427	0.003	0.003	0.000	0.000	0.000	0.000
118	A	110	THR	0	0.000	-0.007	32.885	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	111	ASN	0	-0.058	-0.034	30.818	0.005	0.005	0.000	0.000	0.000	0.000
120	A	112	THR	0	0.011	-0.007	32.541	-0.008	-0.008	0.000	0.000	0.000	0.000
121	A	113	MET	0	-0.009	0.004	32.500	0.010	0.010	0.000	0.000	0.000	0.000
122	A	114	THR	0	-0.014	-0.035	34.054	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	115	LEU	0	-0.020	0.018	35.179	0.010	0.010	0.000	0.000	0.000	0.000
124	A	116	GLY	0	0.001	-0.003	36.992	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	117	ASP	-1	-0.882	-0.935	38.963	0.089	0.089	0.000	0.000	0.000	0.000
126	A	118	ILE	0	-0.067	-0.024	40.633	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	119	VAL	0	-0.001	-0.022	37.638	0.007	0.007	0.000	0.000	0.000	0.000
128	A	120	PHE	0	-0.022	0.015	37.630	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	121	LYS	1	0.990	0.988	37.234	-0.056	-0.056	0.000	0.000	0.000	0.000
130	A	122	ARG	1	0.900	0.960	35.336	-0.067	-0.067	0.000	0.000	0.000	0.000
131	A	123	ILE	0	0.007	0.005	36.604	0.003	0.003	0.000	0.000	0.000	0.000
132	A	124	SER	0	0.015	0.008	35.715	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	125	LYS	1	0.919	0.984	36.518	-0.014	-0.014	0.000	0.000	0.000	0.000
134	A	126	ARG	1	0.922	0.973	29.241	-0.014	-0.014	0.000	0.000	0.000	0.000
135	A	127	ILE	0	-0.044	-0.022	35.524	-0.002	-0.002	0.000	0.000	0.000	0.000

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