FMO DATABASE

FMODB ID: LZV89

Calculation Name: 1B88-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1B88

Chain ID: A

ChEMBL ID:

UniProt ID: Q5R1B3

Base Structure: X-ray

Registration Date: 2023-06-26

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	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-911074.038196
FMO2-HF: Nuclear repulsion	866686.429977
FMO2-HF: Total energy	-44387.608219
FMO2-MP2: Total energy	-44517.783444

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:1:MET)

Summations of interaction energy for fragment #1(A:1:MET)

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.
-2.33	0.907	5.185	-2.617	-5.804	-0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.039 / q_NPA : 0.024

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	GLN	0	0.021	0.001	3.874	0.323	2.188	-0.012	-0.791	-1.062	0.005
4	A	4	VAL	0	0.047	0.013	5.243	0.512	0.630	-0.001	-0.003	-0.113	0.000
5	A	5	ARG	1	0.910	0.960	8.220	1.076	1.076	0.000	0.000	0.000	0.000
6	A	6	GLN	0	0.052	0.017	9.968	0.098	0.098	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.053	-0.004	13.538	-0.075	-0.075	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.082	0.031	15.531	0.023	0.023	0.000	0.000	0.000	0.000
9	A	9	GLN	0	0.023	-0.007	14.153	-0.040	-0.040	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.052	-0.030	18.213	0.026	0.026	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.003	0.001	21.986	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.062	-0.035	24.542	0.008	0.008	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.025	0.005	28.334	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	14	TRP	0	0.009	-0.001	30.290	0.005	0.005	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.896	-0.971	33.335	-0.097	-0.097	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.008	0.005	35.243	0.004	0.004	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.891	-0.937	30.809	-0.132	-0.132	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.035	-0.016	27.589	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.016	0.028	25.787	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.006	-0.015	20.960	0.003	0.003	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.004	0.012	20.036	-0.023	-0.023	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.032	-0.012	16.070	0.021	0.021	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.019	-0.005	13.000	-0.034	-0.034	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.055	-0.023	9.183	0.069	0.069	0.000	0.000	0.000	0.000
25	A	25	TYR	0	0.052	0.036	7.137	-0.230	-0.230	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.814	-0.882	2.312	-4.291	-3.542	5.195	-1.769	-4.175	-0.010
27	A	27	ASN	0	0.052	0.029	4.442	1.213	1.583	0.004	-0.042	-0.332	0.000
28	A	28	SER	0	0.026	0.000	5.869	-0.605	-0.605	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.039	-0.010	8.119	-0.232	-0.232	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.020	-0.003	7.566	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.758	-0.863	11.417	0.211	0.211	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.009	0.009	15.005	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.003	-0.014	11.265	-0.015	-0.015	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.009	0.003	16.354	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	35	TRP	0	0.026	0.000	16.885	-0.055	-0.055	0.000	0.000	0.000	0.000
36	A	36	TYR	0	-0.001	-0.005	18.604	0.027	0.027	0.000	0.000	0.000	0.000
37	A	37	GLN	0	0.004	-0.006	22.228	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.030	-0.028	24.004	0.017	0.017	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.071	0.043	25.823	-0.011	-0.011	0.000	0.000	0.000	0.000
40	A	40	PRO	0	-0.013	-0.035	28.806	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	41	GLY	0	-0.017	0.006	30.121	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.940	-0.957	29.587	-0.115	-0.115	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.002	0.011	26.776	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	44	PRO	0	-0.040	-0.019	22.353	0.006	0.006	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.073	0.046	24.701	0.008	0.008	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.061	-0.044	22.269	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.022	0.006	24.048	0.008	0.008	0.000	0.000	0.000	0.000
48	A	48	ILE	0	0.045	0.021	22.684	0.011	0.011	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.043	-0.025	20.932	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.031	-0.007	18.362	0.010	0.010	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.015	0.007	18.954	0.004	0.004	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.025	-0.054	16.168	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.024	0.001	17.989	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.064	-0.040	20.691	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	55	ASN	0	0.041	0.023	20.052	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.860	0.912	21.069	0.051	0.051	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.904	0.942	23.911	0.058	0.058	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.788	-0.859	25.549	-0.079	-0.079	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.888	-0.953	28.498	-0.084	-0.084	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.017	0.002	30.153	0.008	0.008	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.685	0.819	31.768	0.104	0.104	0.000	0.000	0.000	0.000
62	A	62	PHE	0	0.045	0.032	26.527	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.068	-0.058	25.056	0.016	0.016	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.015	0.019	19.624	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	65	PHE	0	0.000	-0.004	20.953	0.025	0.025	0.000	0.000	0.000	0.000
66	A	66	PHE	0	-0.027	-0.028	13.748	-0.030	-0.030	0.000	0.000	0.000	0.000
67	A	67	ASN	0	-0.032	-0.039	15.275	0.052	0.052	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.871	0.916	12.125	-0.267	-0.267	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.830	0.914	11.588	0.128	0.128	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.816	-0.879	10.527	-0.207	-0.207	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.812	0.902	3.904	-0.135	0.000	-0.001	-0.012	-0.122	0.000
72	A	72	LYS	1	0.896	0.944	9.780	0.504	0.504	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.014	-0.009	13.067	0.071	0.071	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.031	-0.004	15.456	-0.042	-0.042	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.025	0.026	18.507	0.032	0.032	0.000	0.000	0.000	0.000
76	A	76	HIS	0	-0.022	-0.020	21.424	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.016	0.001	24.769	0.009	0.009	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.026	0.007	27.817	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.853	-0.927	30.856	-0.091	-0.091	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.052	0.005	30.023	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	GLN	0	0.067	0.016	32.090	0.004	0.004	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.024	0.007	33.128	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.009	0.016	33.847	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.780	-0.856	29.405	-0.129	-0.129	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.028	-0.018	28.813	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.027	0.024	27.088	0.006	0.006	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.027	-0.018	21.208	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.019	-0.015	21.578	0.010	0.010	0.000	0.000	0.000	0.000
89	A	89	PHE	0	-0.021	-0.009	17.415	-0.043	-0.043	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.013	0.000	13.732	-0.070	-0.070	0.000	0.000	0.000	0.000
91	A	92	ALA	0	0.002	0.005	10.697	0.031	0.031	0.000	0.000	0.000	0.000
92	A	93	SER	0	0.015	-0.004	12.572	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.015	0.004	12.480	0.022	0.022	0.000	0.000	0.000	0.000
94	A	95	SER	0	-0.054	-0.031	13.744	0.001	0.001	0.000	0.000	0.000	0.000
95	A	96	PHE	0	0.049	0.007	17.517	-0.031	-0.031	0.000	0.000	0.000	0.000
96	A	97	GLY	0	-0.007	0.012	20.637	0.014	0.014	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.799	-0.888	19.842	0.124	0.124	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.069	-0.022	21.110	-0.028	-0.028	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.025	-0.020	15.996	0.020	0.020	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.892	0.945	13.322	0.193	0.193	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.025	0.025	13.810	0.015	0.015	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.067	-0.036	8.977	-0.044	-0.044	0.000	0.000	0.000	0.000
103	A	104	TRP	0	0.020	0.002	12.086	0.030	0.030	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.000	0.000	12.172	-0.151	-0.151	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.039	-0.043	12.151	0.045	0.045	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.026	0.028	15.162	0.052	0.052	0.000	0.000	0.000	0.000
107	A	108	THR	0	-0.067	-0.044	17.462	-0.046	-0.046	0.000	0.000	0.000	0.000
108	A	109	SER	0	-0.006	0.002	19.824	0.026	0.026	0.000	0.000	0.000	0.000
109	A	110	LEU	0	-0.015	0.005	23.355	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.008	0.000	25.829	0.009	0.009	0.000	0.000	0.000	0.000
111	A	112	VAL	0	0.016	0.006	29.406	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.042	-0.019	32.003	0.010	0.010	0.000	0.000	0.000	0.000
113	A	114	PRO	0	0.041	0.035	35.537	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:1:MET)