FMO DATABASE

FMODB ID: V52G1

Calculation Name: 1QB3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1QB3

Chain ID: A

ChEMBL ID:

UniProt ID: P20486

Base Structure: X-ray

Registration Date: 2023-06-21

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-832877.293174
FMO2-HF: Nuclear repulsion	786601.191893
FMO2-HF: Total energy	-46276.101281
FMO2-MP2: Total energy	-46411.91127

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:6:HIS)

Summations of interaction energy for fragment #1(A:6:HIS)

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.
-33.657	-26.004	10.138	-6.233	-11.558	-0.019

Interaction energy analysis for fragmet #1(A:6:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : -0.016

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	8	PHE	0	-0.054	-0.009	2.308	-12.926	-8.227	5.115	-3.543	-6.271	0.015
4	A	9	GLN	0	0.007	0.001	3.156	0.767	1.586	0.167	0.132	-1.118	0.003
5	A	10	GLY	0	0.024	0.016	6.881	-0.832	-0.832	0.000	0.000	0.000	0.000
6	A	11	ARG	1	0.694	0.794	8.246	1.359	1.359	0.000	0.000	0.000	0.000
7	A	12	LYS	1	0.804	0.910	5.068	0.282	0.282	0.000	0.000	0.000	0.000
8	A	13	LEU	0	-0.006	0.012	7.512	0.562	0.562	0.000	0.000	0.000	0.000
9	A	14	THR	0	0.011	-0.032	9.458	0.147	0.147	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.832	-0.923	10.054	-0.462	-0.462	0.000	0.000	0.000	0.000
11	A	16	GLN	0	0.034	0.013	12.461	-0.084	-0.084	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.723	-0.796	13.278	-0.824	-0.824	0.000	0.000	0.000	0.000
13	A	18	ARG	1	0.879	0.933	8.453	2.522	2.522	0.000	0.000	0.000	0.000
14	A	19	ALA	0	-0.003	-0.005	12.261	-0.057	-0.057	0.000	0.000	0.000	0.000
15	A	20	ARG	1	0.767	0.835	15.357	0.551	0.551	0.000	0.000	0.000	0.000
16	A	21	VAL	0	0.008	0.001	13.416	0.027	0.027	0.000	0.000	0.000	0.000
17	A	22	LEU	0	-0.011	-0.019	11.622	-0.049	-0.049	0.000	0.000	0.000	0.000
18	A	23	GLU	-1	-0.814	-0.841	15.121	-0.501	-0.501	0.000	0.000	0.000	0.000
19	A	24	PHE	0	0.021	-0.010	17.848	0.086	0.086	0.000	0.000	0.000	0.000
20	A	25	GLN	0	0.006	-0.002	12.250	0.083	0.083	0.000	0.000	0.000	0.000
21	A	26	ASP	-1	-0.919	-0.955	16.761	-0.803	-0.803	0.000	0.000	0.000	0.000
22	A	27	SER	0	-0.096	-0.061	19.762	0.105	0.105	0.000	0.000	0.000	0.000
23	A	28	ILE	0	-0.066	-0.011	14.874	0.026	0.026	0.000	0.000	0.000	0.000
24	A	29	HIS	0	0.008	0.012	19.092	0.000	0.000	0.000	0.000	0.000	0.000
25	A	30	TYR	0	0.040	0.009	15.112	-0.159	-0.159	0.000	0.000	0.000	0.000
26	A	31	SER	0	-0.023	-0.003	20.630	0.053	0.053	0.000	0.000	0.000	0.000
27	A	32	PRO	0	0.023	-0.003	22.489	-0.054	-0.054	0.000	0.000	0.000	0.000
28	A	33	ARG	1	0.846	0.929	20.246	0.750	0.750	0.000	0.000	0.000	0.000
29	A	34	TYR	0	-0.001	0.010	23.815	0.046	0.046	0.000	0.000	0.000	0.000
30	A	35	SER	0	0.018	0.003	24.483	-0.053	-0.053	0.000	0.000	0.000	0.000
31	A	36	ASP	-1	-0.808	-0.870	26.336	-0.523	-0.523	0.000	0.000	0.000	0.000
32	A	37	ASP	-1	-0.947	-0.973	27.693	-0.384	-0.384	0.000	0.000	0.000	0.000
33	A	38	ASN	0	-0.120	-0.058	25.153	0.025	0.025	0.000	0.000	0.000	0.000
34	A	39	TYR	0	-0.050	-0.038	18.329	0.014	0.014	0.000	0.000	0.000	0.000
35	A	40	GLU	-1	-0.864	-0.918	20.498	-0.775	-0.775	0.000	0.000	0.000	0.000
36	A	41	TYR	0	-0.038	-0.056	20.526	-0.096	-0.096	0.000	0.000	0.000	0.000
37	A	42	ARG	1	0.820	0.891	17.221	1.188	1.188	0.000	0.000	0.000	0.000
38	A	43	HIS	0	-0.004	-0.003	19.935	-0.045	-0.045	0.000	0.000	0.000	0.000
39	A	44	VAL	0	0.010	-0.005	16.028	0.015	0.015	0.000	0.000	0.000	0.000
40	A	45	MET	0	-0.052	-0.020	19.160	0.045	0.045	0.000	0.000	0.000	0.000
41	A	46	LEU	0	0.064	0.030	16.061	0.011	0.011	0.000	0.000	0.000	0.000
42	A	47	PRO	0	0.033	0.029	19.775	0.088	0.088	0.000	0.000	0.000	0.000
43	A	48	LYS	1	0.987	0.957	22.148	0.507	0.507	0.000	0.000	0.000	0.000
44	A	49	ALA	0	-0.056	-0.014	23.943	0.033	0.033	0.000	0.000	0.000	0.000
45	A	50	MET	0	0.061	0.053	14.952	0.064	0.064	0.000	0.000	0.000	0.000
46	A	51	LEU	0	0.014	-0.008	19.220	-0.032	-0.032	0.000	0.000	0.000	0.000
47	A	52	LYS	1	0.870	0.935	20.782	0.525	0.525	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.047	-0.014	18.186	0.063	0.063	0.000	0.000	0.000	0.000
49	A	54	ILE	0	-0.014	0.016	14.872	-0.062	-0.062	0.000	0.000	0.000	0.000
50	A	55	PRO	0	0.025	0.013	13.980	0.105	0.105	0.000	0.000	0.000	0.000
51	A	56	SER	0	0.043	0.012	16.952	-0.073	-0.073	0.000	0.000	0.000	0.000
52	A	57	ASP	-1	-0.780	-0.861	14.221	-0.985	-0.985	0.000	0.000	0.000	0.000
53	A	58	TYR	0	-0.022	-0.029	9.422	-0.291	-0.291	0.000	0.000	0.000	0.000
54	A	59	PHE	0	-0.088	-0.036	15.410	-0.061	-0.061	0.000	0.000	0.000	0.000
55	A	60	ASN	0	-0.031	-0.018	19.068	0.072	0.072	0.000	0.000	0.000	0.000
56	A	61	SER	0	-0.023	-0.043	21.439	0.014	0.014	0.000	0.000	0.000	0.000
57	A	62	GLU	-1	-0.894	-0.921	24.361	-0.397	-0.397	0.000	0.000	0.000	0.000
58	A	63	VAL	0	-0.065	-0.030	24.549	0.024	0.024	0.000	0.000	0.000	0.000
59	A	64	GLY	0	-0.025	-0.007	24.650	0.014	0.014	0.000	0.000	0.000	0.000
60	A	65	THR	0	-0.031	-0.013	21.511	0.004	0.004	0.000	0.000	0.000	0.000
61	A	66	LEU	0	-0.010	-0.010	15.533	0.007	0.007	0.000	0.000	0.000	0.000
62	A	67	ARG	1	0.767	0.849	11.942	1.570	1.570	0.000	0.000	0.000	0.000
63	A	68	ILE	0	0.003	0.002	14.257	-0.133	-0.133	0.000	0.000	0.000	0.000
64	A	69	LEU	0	-0.044	-0.006	10.817	-0.015	-0.015	0.000	0.000	0.000	0.000
65	A	70	THR	0	0.009	-0.027	7.407	-0.302	-0.302	0.000	0.000	0.000	0.000
66	A	71	GLU	-1	-0.797	-0.896	5.986	-4.264	-4.264	0.000	0.000	0.000	0.000
67	A	72	ASP	-1	-0.808	-0.912	2.431	-23.461	-21.411	4.857	-2.813	-4.094	-0.037
68	A	73	GLU	-1	-0.738	-0.828	4.274	-1.773	-1.688	-0.001	-0.009	-0.075	0.000
69	A	74	TRP	0	0.014	0.004	7.405	0.234	0.234	0.000	0.000	0.000	0.000
70	A	75	ARG	1	0.773	0.872	5.054	4.784	4.784	0.000	0.000	0.000	0.000
71	A	76	GLY	0	-0.002	0.002	6.307	0.628	0.628	0.000	0.000	0.000	0.000
72	A	77	LEU	0	-0.042	-0.019	7.168	0.857	0.857	0.000	0.000	0.000	0.000
73	A	78	GLY	0	0.003	0.004	9.519	0.423	0.423	0.000	0.000	0.000	0.000
74	A	79	ILE	0	-0.017	0.010	10.950	0.331	0.331	0.000	0.000	0.000	0.000
75	A	80	THR	0	-0.026	-0.028	10.389	-0.488	-0.488	0.000	0.000	0.000	0.000
76	A	81	GLN	0	0.020	0.025	12.027	0.568	0.568	0.000	0.000	0.000	0.000
77	A	82	SER	0	0.039	0.016	11.996	-0.229	-0.229	0.000	0.000	0.000	0.000
78	A	83	LEU	0	0.024	0.000	8.503	-0.246	-0.246	0.000	0.000	0.000	0.000
79	A	84	GLY	0	0.035	0.016	10.470	0.273	0.273	0.000	0.000	0.000	0.000
80	A	85	TRP	0	-0.045	-0.009	12.026	0.177	0.177	0.000	0.000	0.000	0.000
81	A	86	GLU	-1	-0.821	-0.891	12.110	-1.571	-1.571	0.000	0.000	0.000	0.000
82	A	87	HIS	0	-0.043	-0.014	13.378	0.006	0.006	0.000	0.000	0.000	0.000
83	A	88	TYR	0	-0.026	-0.044	15.037	0.047	0.047	0.000	0.000	0.000	0.000
84	A	89	GLU	-1	-0.835	-0.921	18.437	-0.841	-0.841	0.000	0.000	0.000	0.000
85	A	90	CYS	0	-0.093	-0.045	20.699	0.065	0.065	0.000	0.000	0.000	0.000
86	A	91	HIS	0	0.054	0.050	23.974	-0.067	-0.067	0.000	0.000	0.000	0.000
87	A	92	ALA	0	-0.003	0.006	25.882	0.033	0.033	0.000	0.000	0.000	0.000
88	A	93	PRO	0	-0.017	-0.007	29.309	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	94	GLU	-1	-0.827	-0.929	32.133	-0.346	-0.346	0.000	0.000	0.000	0.000
90	A	95	PRO	0	0.021	-0.003	33.977	0.012	0.012	0.000	0.000	0.000	0.000
91	A	96	HIS	0	-0.053	-0.014	36.477	0.020	0.020	0.000	0.000	0.000	0.000
92	A	97	ILE	0	-0.072	-0.028	35.935	0.014	0.014	0.000	0.000	0.000	0.000
93	A	98	LEU	0	0.013	0.009	36.709	-0.015	-0.015	0.000	0.000	0.000	0.000
94	A	99	LEU	0	-0.008	0.003	33.245	0.004	0.004	0.000	0.000	0.000	0.000
95	A	100	PHE	0	-0.001	-0.007	37.408	0.007	0.007	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.949	0.968	34.681	0.320	0.320	0.000	0.000	0.000	0.000
97	A	102	ARG	1	0.898	0.961	39.616	0.213	0.213	0.000	0.000	0.000	0.000
98	A	103	PRO	0	0.065	0.038	40.584	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	104	LEU	0	0.032	0.006	40.759	0.010	0.010	0.000	0.000	0.000	0.000
100	A	105	ASN	0	-0.031	-0.016	42.744	0.001	0.001	0.000	0.000	0.000	0.000
101	A	106	TYR	0	0.007	-0.025	45.221	0.007	0.007	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.785	-0.862	46.395	-0.150	-0.150	0.000	0.000	0.000	0.000
103	A	108	ALA	0	-0.030	-0.014	47.773	0.008	0.008	0.000	0.000	0.000	0.000
104	A	109	GLU	-1	-0.837	-0.917	43.481	-0.199	-0.199	0.000	0.000	0.000	0.000
105	A	110	LEU	0	0.028	0.008	48.315	0.007	0.007	0.000	0.000	0.000	0.000
106	A	111	ARG	1	0.846	0.926	51.075	0.150	0.150	0.000	0.000	0.000	0.000
107	A	112	ALA	0	0.010	0.005	50.692	0.007	0.007	0.000	0.000	0.000	0.000
108	A	113	ALA	0	0.007	-0.006	51.081	0.006	0.006	0.000	0.000	0.000	0.000
109	A	114	THR	0	-0.056	-0.045	53.063	0.005	0.005	0.000	0.000	0.000	0.000
110	A	115	ALA	0	-0.009	0.003	56.303	0.005	0.005	0.000	0.000	0.000	0.000
111	A	116	ALA	0	0.008	0.004	54.277	0.005	0.005	0.000	0.000	0.000	0.000
112	A	117	ALA	0	-0.024	0.004	56.304	0.004	0.004	0.000	0.000	0.000	0.000
113	A	118	GLN	0	-0.119	-0.053	58.117	0.010	0.010	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:HIS)