FMO DATABASE

FMODB ID: 6649Z

Calculation Name: 4B0E-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B0E

Chain ID: A

ChEMBL ID:

UniProt ID: P26949

Base Structure: X-ray

Registration Date: 2023-03-14

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	95
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-713406.371141
FMO2-HF: Nuclear repulsion	675604.509535
FMO2-HF: Total energy	-37801.861606
FMO2-MP2: Total energy	-37913.712362

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:28:LEU)

Summations of interaction energy for fragment #1(A:28:LEU)

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.
-6.836	-1.094	0.824	-2.667	-3.901	-0.004

Interaction energy analysis for fragmet #1(A:28:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : -0.009

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	30	GLY	0	0.024	0.027	3.442	-3.000	-1.349	0.024	-0.832	-0.844	-0.001
4	A	31	ASN	0	-0.006	-0.001	6.037	0.579	0.579	0.000	0.000	0.000	0.000
5	A	32	TYR	0	0.003	-0.016	2.437	-1.327	0.825	0.405	-1.050	-1.507	-0.009
6	A	33	PHE	0	-0.005	0.011	8.877	0.211	0.211	0.000	0.000	0.000	0.000
7	A	34	VAL	0	-0.011	-0.014	10.393	0.015	0.015	0.000	0.000	0.000	0.000
8	A	35	ASN	0	0.008	-0.006	13.086	0.009	0.009	0.000	0.000	0.000	0.000
9	A	36	VAL	0	0.035	0.022	15.661	0.038	0.038	0.000	0.000	0.000	0.000
10	A	37	PHE	0	-0.033	-0.034	17.520	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	38	VAL	0	0.078	0.042	19.662	0.023	0.023	0.000	0.000	0.000	0.000
12	A	39	ASN	0	0.010	0.002	22.442	0.000	0.000	0.000	0.000	0.000	0.000
13	A	40	GLY	0	-0.005	-0.006	23.029	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	41	ARG	1	0.893	0.950	24.170	-0.052	-0.052	0.000	0.000	0.000	0.000
15	A	42	LYS	1	0.853	0.935	20.012	0.096	0.096	0.000	0.000	0.000	0.000
16	A	43	VAL	0	-0.011	-0.014	21.386	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	44	ASP	-1	-0.766	-0.878	19.599	-0.140	-0.140	0.000	0.000	0.000	0.000
18	A	45	SER	0	-0.071	-0.032	17.635	0.025	0.025	0.000	0.000	0.000	0.000
19	A	46	GLY	0	0.008	0.017	16.166	0.004	0.004	0.000	0.000	0.000	0.000
20	A	47	ASN	0	-0.020	0.000	12.996	0.043	0.043	0.000	0.000	0.000	0.000
21	A	48	ILE	0	-0.021	0.000	11.776	0.075	0.075	0.000	0.000	0.000	0.000
22	A	49	ASP	-1	-0.902	-0.953	9.612	-1.007	-1.007	0.000	0.000	0.000	0.000
23	A	50	PHE	0	-0.002	-0.005	6.597	0.335	0.335	0.000	0.000	0.000	0.000
24	A	51	ARG	1	0.897	0.923	7.103	-0.651	-0.651	0.000	0.000	0.000	0.000
25	A	52	LEU	0	-0.020	-0.021	4.503	0.208	0.356	-0.001	-0.009	-0.139	0.000
26	A	53	GLU	-1	-0.827	-0.886	7.779	0.048	0.048	0.000	0.000	0.000	0.000
27	A	54	LYS	1	0.884	0.930	11.376	-0.558	-0.558	0.000	0.000	0.000	0.000
28	A	55	HIS	0	0.056	0.026	13.523	-0.110	-0.110	0.000	0.000	0.000	0.000
29	A	56	ASN	0	-0.023	-0.024	16.331	0.014	0.014	0.000	0.000	0.000	0.000
30	A	57	GLY	0	-0.009	-0.008	17.021	0.003	0.003	0.000	0.000	0.000	0.000
31	A	58	LYS	1	0.925	0.968	14.077	-0.504	-0.504	0.000	0.000	0.000	0.000
32	A	59	GLU	-1	-0.824	-0.896	8.593	0.875	0.875	0.000	0.000	0.000	0.000
33	A	60	LEU	0	-0.047	-0.016	8.742	0.182	0.182	0.000	0.000	0.000	0.000
34	A	61	LEU	0	0.006	0.008	3.033	-2.057	-0.854	0.322	-0.595	-0.930	0.007
35	A	62	TRP	0	0.057	0.017	7.594	-0.224	-0.224	0.000	0.000	0.000	0.000
36	A	63	PRO	0	-0.010	0.004	10.545	-0.128	-0.128	0.000	0.000	0.000	0.000
37	A	64	CYS	0	-0.090	-0.049	12.111	0.006	0.006	0.000	0.000	0.000	0.000
38	A	65	LEU	0	-0.036	-0.013	14.487	-0.054	-0.054	0.000	0.000	0.000	0.000
39	A	66	SER	0	0.086	0.024	17.509	0.023	0.023	0.000	0.000	0.000	0.000
40	A	67	SER	0	0.016	-0.017	20.838	0.008	0.008	0.000	0.000	0.000	0.000
41	A	68	LEU	0	0.008	0.018	23.945	0.005	0.005	0.000	0.000	0.000	0.000
42	A	69	GLN	0	0.031	0.033	16.584	0.007	0.007	0.000	0.000	0.000	0.000
43	A	70	LEU	0	0.040	0.013	20.215	0.007	0.007	0.000	0.000	0.000	0.000
44	A	71	THR	0	0.022	0.012	22.874	0.008	0.008	0.000	0.000	0.000	0.000
45	A	72	LYS	1	0.819	0.902	21.512	0.125	0.125	0.000	0.000	0.000	0.000
46	A	73	TYR	0	-0.044	-0.036	18.122	0.000	0.000	0.000	0.000	0.000	0.000
47	A	74	GLY	0	-0.006	-0.004	23.634	0.010	0.010	0.000	0.000	0.000	0.000
48	A	75	ILE	0	-0.023	-0.005	22.551	0.009	0.009	0.000	0.000	0.000	0.000
49	A	76	ASP	-1	-0.838	-0.931	26.706	0.014	0.014	0.000	0.000	0.000	0.000
50	A	77	ILE	0	0.006	-0.015	25.903	0.009	0.009	0.000	0.000	0.000	0.000
51	A	78	ASP	-1	-0.868	-0.924	28.475	0.015	0.015	0.000	0.000	0.000	0.000
52	A	79	LYS	1	0.764	0.881	31.441	-0.031	-0.031	0.000	0.000	0.000	0.000
53	A	80	TYR	0	-0.015	-0.016	27.833	0.010	0.010	0.000	0.000	0.000	0.000
54	A	81	PRO	0	0.071	0.027	28.476	0.001	0.001	0.000	0.000	0.000	0.000
55	A	82	ASP	-1	-0.854	-0.918	27.485	0.067	0.067	0.000	0.000	0.000	0.000
56	A	83	LEU	0	-0.046	-0.001	23.120	0.006	0.006	0.000	0.000	0.000	0.000
57	A	84	ILE	0	0.020	0.004	23.793	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	85	LYS	1	0.860	0.916	25.694	-0.053	-0.053	0.000	0.000	0.000	0.000
59	A	86	SER	0	-0.008	0.001	24.275	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	87	GLY	0	0.001	0.005	21.744	0.020	0.020	0.000	0.000	0.000	0.000
61	A	88	THR	0	-0.048	-0.012	20.765	-0.022	-0.022	0.000	0.000	0.000	0.000
62	A	89	GLU	-1	-0.832	-0.914	22.573	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	90	GLN	0	-0.013	-0.012	19.768	0.004	0.004	0.000	0.000	0.000	0.000
64	A	92	VAL	0	-0.014	0.003	18.772	0.021	0.021	0.000	0.000	0.000	0.000
65	A	93	ASP	-1	-0.853	-0.941	19.101	0.197	0.197	0.000	0.000	0.000	0.000
66	A	94	LEU	0	-0.030	-0.034	16.255	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	95	LEU	0	-0.027	-0.007	18.347	0.005	0.005	0.000	0.000	0.000	0.000
68	A	96	ALA	0	-0.009	0.015	21.483	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	97	ILE	0	-0.050	-0.014	23.267	-0.017	-0.017	0.000	0.000	0.000	0.000
70	A	98	PRO	0	-0.005	0.009	24.727	0.019	0.019	0.000	0.000	0.000	0.000
71	A	99	HIS	0	-0.037	-0.031	26.116	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	100	SER	0	-0.023	-0.020	22.436	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	101	ASP	-1	-0.927	-0.951	19.232	0.295	0.295	0.000	0.000	0.000	0.000
74	A	102	VAL	0	-0.018	-0.014	14.195	-0.038	-0.038	0.000	0.000	0.000	0.000
75	A	103	GLN	0	0.001	-0.011	13.379	0.153	0.153	0.000	0.000	0.000	0.000
76	A	104	PHE	0	0.021	0.014	5.613	-0.105	-0.105	0.000	0.000	0.000	0.000
77	A	105	TYR	0	-0.025	-0.022	10.218	0.186	0.186	0.000	0.000	0.000	0.000
78	A	106	PHE	0	0.033	0.011	2.893	-0.304	0.284	0.074	-0.181	-0.481	-0.001
79	A	107	ASN	0	0.018	-0.010	8.123	-0.185	-0.185	0.000	0.000	0.000	0.000
80	A	108	GLN	0	-0.041	-0.009	10.506	-0.084	-0.084	0.000	0.000	0.000	0.000
81	A	109	GLN	0	-0.039	-0.012	9.776	-0.035	-0.035	0.000	0.000	0.000	0.000
82	A	110	LYS	1	0.935	0.976	11.480	-0.133	-0.133	0.000	0.000	0.000	0.000
83	A	111	LEU	0	0.027	0.033	12.451	0.096	0.096	0.000	0.000	0.000	0.000
84	A	112	SER	0	-0.044	-0.034	13.899	-0.063	-0.063	0.000	0.000	0.000	0.000
85	A	113	LEU	0	0.004	0.013	16.642	0.047	0.047	0.000	0.000	0.000	0.000
86	A	114	ILE	0	-0.004	-0.005	19.266	-0.029	-0.029	0.000	0.000	0.000	0.000
87	A	115	VAL	0	0.052	0.021	22.328	0.014	0.014	0.000	0.000	0.000	0.000
88	A	116	PRO	0	0.052	0.047	25.072	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	117	PRO	0	0.017	-0.004	28.665	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	118	GLN	0	0.046	0.012	31.148	-0.008	-0.008	0.000	0.000	0.000	0.000
91	A	119	ALA	0	-0.045	-0.017	27.473	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	120	LEU	0	-0.027	0.007	26.970	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	121	LEU	0	-0.018	-0.011	29.155	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	122	PRO	0	-0.005	-0.007	31.908	0.000	0.000	0.000	0.000	0.000	0.000
95	A	123	ARG	1	0.861	0.949	27.489	0.017	0.017	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:LEU)