FMO DATABASE

FMODB ID: QVY5Y

Calculation Name: 2QZJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QZJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q180B0

Base Structure: X-ray

Registration Date: 2023-09-21

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	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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1065413.302694
FMO2-HF: Nuclear repulsion	1016831.727953
FMO2-HF: Total energy	-48581.574741
FMO2-MP2: Total energy	-48721.532324

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:4:GLN)

Summations of interaction energy for fragment #1(A:4:GLN)

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.
-30.06	-24.105	9.971	-7.099	-8.827	-0.045

Interaction energy analysis for fragmet #1(A:4:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.036 / 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	6	LYS	1	0.886	0.943	2.631	-6.447	-2.772	0.680	-2.045	-2.311	-0.008
4	A	7	ILE	0	-0.012	-0.004	5.199	0.328	0.392	-0.001	-0.004	-0.059	0.000
5	A	8	LEU	0	-0.007	0.014	8.324	0.274	0.274	0.000	0.000	0.000	0.000
6	A	9	ILE	0	-0.033	-0.026	11.558	-0.075	-0.075	0.000	0.000	0.000	0.000
7	A	10	ILE	0	-0.009	-0.008	14.264	0.109	0.109	0.000	0.000	0.000	0.000
8	A	11	ASP	-1	-0.730	-0.871	17.815	-0.472	-0.472	0.000	0.000	0.000	0.000
9	A	12	GLY	0	0.065	0.045	20.372	0.029	0.029	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.888	-0.936	22.539	-0.376	-0.376	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.917	0.943	19.717	0.101	0.101	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.846	-0.908	18.979	-0.376	-0.376	0.000	0.000	0.000	0.000
13	A	16	ASN	0	-0.140	-0.081	19.043	-0.114	-0.114	0.000	0.000	0.000	0.000
14	A	17	CYS	0	-0.017	-0.003	16.155	-0.098	-0.098	0.000	0.000	0.000	0.000
15	A	18	GLN	0	0.002	-0.001	14.240	-0.155	-0.155	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.878	0.938	14.438	0.471	0.471	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.026	-0.023	12.994	-0.155	-0.155	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.904	0.969	8.952	0.157	0.157	0.000	0.000	0.000	0.000
19	A	22	GLY	0	0.056	0.028	9.656	-0.380	-0.380	0.000	0.000	0.000	0.000
20	A	23	PHE	0	-0.014	-0.015	10.310	-0.298	-0.298	0.000	0.000	0.000	0.000
21	A	24	LEU	0	-0.004	-0.011	8.262	-0.188	-0.188	0.000	0.000	0.000	0.000
22	A	25	GLU	-1	-0.861	-0.938	5.727	-2.228	-2.228	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.919	-0.938	5.802	-2.852	-2.852	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.757	0.883	7.372	2.027	2.027	0.000	0.000	0.000	0.000
25	A	28	GLY	0	-0.008	-0.001	3.588	0.332	0.794	0.002	-0.218	-0.246	-0.001
26	A	29	ILE	0	-0.060	-0.026	1.878	-17.391	-18.098	7.989	-3.551	-3.731	-0.048
27	A	30	SER	0	0.007	0.025	2.651	-0.978	1.248	1.286	-1.185	-2.327	0.011
28	A	31	ILE	0	-0.002	-0.016	4.241	-0.565	-0.330	0.015	-0.096	-0.153	0.001
29	A	32	ASP	-1	-0.801	-0.871	7.924	1.033	1.033	0.000	0.000	0.000	0.000
30	A	33	LEU	0	-0.022	-0.024	10.808	-0.217	-0.217	0.000	0.000	0.000	0.000
31	A	34	ALA	0	0.020	0.001	14.346	0.119	0.119	0.000	0.000	0.000	0.000
32	A	35	TYR	0	0.006	-0.012	17.400	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	36	ASN	0	-0.026	-0.011	21.102	0.007	0.007	0.000	0.000	0.000	0.000
34	A	37	CYS	0	0.010	-0.007	21.578	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.963	-0.966	22.065	0.003	0.003	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.814	-0.912	19.611	-0.056	-0.056	0.000	0.000	0.000	0.000
37	A	40	ALA	0	-0.043	-0.026	17.971	0.024	0.024	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.012	-0.023	17.990	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.034	0.036	19.462	0.023	0.023	0.000	0.000	0.000	0.000
40	A	43	LYS	1	0.874	0.942	13.273	-0.046	-0.046	0.000	0.000	0.000	0.000
41	A	44	ILE	0	-0.006	-0.011	14.445	0.017	0.017	0.000	0.000	0.000	0.000
42	A	45	PHE	0	-0.048	-0.026	16.103	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	46	SER	0	-0.067	-0.034	14.919	0.054	0.054	0.000	0.000	0.000	0.000
44	A	47	ASN	0	-0.070	-0.024	10.202	0.437	0.437	0.000	0.000	0.000	0.000
45	A	48	LYS	1	0.945	0.977	9.184	0.011	0.011	0.000	0.000	0.000	0.000
46	A	49	TYR	0	-0.035	-0.045	8.671	-0.070	-0.070	0.000	0.000	0.000	0.000
47	A	50	ASP	-1	-0.829	-0.920	6.235	-3.990	-3.990	0.000	0.000	0.000	0.000
48	A	51	LEU	0	-0.066	-0.054	9.428	0.209	0.209	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.011	0.006	11.028	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	53	PHE	0	0.003	0.000	11.982	0.025	0.025	0.000	0.000	0.000	0.000
51	A	54	LEU	0	-0.023	-0.017	15.754	0.057	0.057	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.716	-0.801	19.142	-0.389	-0.389	0.000	0.000	0.000	0.000
53	A	56	ILE	0	-0.016	-0.016	22.202	0.020	0.020	0.000	0.000	0.000	0.000
54	A	57	ILE	0	-0.001	0.006	25.639	0.029	0.029	0.000	0.000	0.000	0.000
55	A	58	LEU	0	0.006	-0.005	22.399	-0.018	-0.018	0.000	0.000	0.000	0.000
56	A	59	SER	0	-0.011	-0.013	26.421	0.011	0.011	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.783	-0.878	26.118	-0.128	-0.128	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.021	0.011	28.302	0.013	0.013	0.000	0.000	0.000	0.000
59	A	62	ASP	-1	-0.791	-0.864	27.748	-0.218	-0.218	0.000	0.000	0.000	0.000
60	A	63	GLY	0	0.036	-0.005	24.184	0.001	0.001	0.000	0.000	0.000	0.000
61	A	64	TRP	0	-0.012	-0.017	24.423	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	65	THR	0	-0.088	-0.076	26.780	0.003	0.003	0.000	0.000	0.000	0.000
63	A	66	LEU	0	0.003	0.002	20.993	0.011	0.011	0.000	0.000	0.000	0.000
64	A	67	CYS	0	-0.027	0.007	22.008	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	68	LYS	1	0.906	0.949	22.915	0.226	0.226	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.940	0.977	24.173	0.105	0.105	0.000	0.000	0.000	0.000
67	A	70	ILE	0	0.022	0.014	18.082	0.021	0.021	0.000	0.000	0.000	0.000
68	A	71	ARG	1	0.795	0.895	17.984	0.504	0.504	0.000	0.000	0.000	0.000
69	A	72	ASN	0	-0.075	-0.021	21.897	0.001	0.001	0.000	0.000	0.000	0.000
70	A	73	VAL	0	-0.069	-0.033	17.650	0.035	0.035	0.000	0.000	0.000	0.000
71	A	74	THR	0	-0.015	-0.016	14.406	-0.023	-0.023	0.000	0.000	0.000	0.000
72	A	75	THR	0	0.030	0.015	17.015	0.015	0.015	0.000	0.000	0.000	0.000
73	A	76	CYS	0	-0.061	0.001	12.366	-0.029	-0.029	0.000	0.000	0.000	0.000
74	A	77	PRO	0	0.046	0.026	13.178	0.078	0.078	0.000	0.000	0.000	0.000
75	A	78	ILE	0	0.005	-0.001	14.969	-0.079	-0.079	0.000	0.000	0.000	0.000
76	A	79	VAL	0	-0.034	-0.030	16.411	0.039	0.039	0.000	0.000	0.000	0.000
77	A	80	TYR	0	0.059	0.012	18.140	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	81	MET	0	-0.057	-0.009	17.686	-0.072	-0.072	0.000	0.000	0.000	0.000
79	A	82	THR	0	0.007	-0.018	21.327	0.039	0.039	0.000	0.000	0.000	0.000
80	A	83	TYR	0	0.027	0.001	24.990	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.016	0.009	28.130	0.016	0.016	0.000	0.000	0.000	0.000
82	A	85	ASN	0	0.020	0.025	29.069	-0.039	-0.039	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.834	-0.933	30.997	-0.233	-0.233	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.903	-0.950	32.160	-0.259	-0.259	0.000	0.000	0.000	0.000
85	A	88	GLN	0	-0.018	-0.026	32.941	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	89	SER	0	0.003	-0.004	29.263	0.005	0.005	0.000	0.000	0.000	0.000
87	A	90	ILE	0	0.028	0.009	27.422	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	91	LEU	0	0.020	0.013	28.437	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	92	ASN	0	0.011	0.017	30.239	0.002	0.002	0.000	0.000	0.000	0.000
90	A	93	ALA	0	-0.013	0.005	25.109	0.000	0.000	0.000	0.000	0.000	0.000
91	A	94	LEU	0	-0.008	-0.013	24.185	-0.014	-0.014	0.000	0.000	0.000	0.000
92	A	95	ASN	0	-0.033	-0.019	26.241	0.007	0.007	0.000	0.000	0.000	0.000
93	A	96	SER	0	-0.116	-0.054	26.213	0.025	0.025	0.000	0.000	0.000	0.000
94	A	97	GLY	0	0.010	0.004	23.942	0.007	0.007	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.003	0.013	21.579	-0.041	-0.041	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.854	-0.913	19.017	-0.611	-0.611	0.000	0.000	0.000	0.000
97	A	100	ASP	-1	-0.820	-0.909	19.678	-0.628	-0.628	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.023	-0.029	21.302	0.005	0.005	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.039	-0.020	18.253	0.002	0.002	0.000	0.000	0.000	0.000
100	A	103	ILE	0	0.027	0.007	22.502	0.015	0.015	0.000	0.000	0.000	0.000
101	A	104	LYS	1	0.697	0.849	21.942	0.420	0.420	0.000	0.000	0.000	0.000
102	A	105	PRO	0	0.018	-0.007	24.275	0.032	0.032	0.000	0.000	0.000	0.000
103	A	106	LEU	0	0.028	0.002	18.282	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	107	ASN	0	0.016	0.018	21.221	-0.051	-0.051	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.041	-0.008	15.531	-0.019	-0.019	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.864	-0.925	16.216	-1.177	-1.177	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.015	-0.013	17.633	-0.063	-0.063	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.012	0.012	14.030	-0.031	-0.031	0.000	0.000	0.000	0.000
109	A	112	TYR	0	0.128	0.041	9.477	0.131	0.131	0.000	0.000	0.000	0.000
110	A	113	ALA	0	-0.044	-0.020	14.060	-0.099	-0.099	0.000	0.000	0.000	0.000
111	A	114	LYS	1	0.852	0.908	16.250	0.658	0.658	0.000	0.000	0.000	0.000
112	A	115	VAL	0	0.015	0.018	10.128	0.005	0.005	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.909	0.968	11.367	1.326	1.326	0.000	0.000	0.000	0.000
114	A	117	ALA	0	-0.071	-0.035	12.747	0.086	0.086	0.000	0.000	0.000	0.000
115	A	118	ILE	0	0.011	-0.005	13.310	0.094	0.094	0.000	0.000	0.000	0.000
116	A	119	LEU	0	0.042	0.032	7.732	0.095	0.095	0.000	0.000	0.000	0.000
117	A	120	ARG	1	0.976	0.994	11.250	0.912	0.912	0.000	0.000	0.000	0.000
118	A	121	ARG	1	0.928	0.972	13.198	0.641	0.641	0.000	0.000	0.000	0.000
119	A	122	MET	0	-0.005	-0.001	11.112	0.125	0.125	0.000	0.000	0.000	0.000
120	A	123	ASN	0	-0.060	-0.023	8.022	0.087	0.087	0.000	0.000	0.000	0.000
121	A	124	SER	0	-0.084	-0.041	11.256	0.192	0.192	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:4:GLN)