FMO DATABASE

FMODB ID: 43ZKN

Calculation Name: 2QYA-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QYA

Chain ID: A

ChEMBL ID:

UniProt ID: Q8TWR4

Base Structure: X-ray

Registration Date: 2023-06-20

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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-853118.432614
FMO2-HF: Nuclear repulsion	808817.113609
FMO2-HF: Total energy	-44301.319005
FMO2-MP2: Total energy	-44429.847968

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-6.583	-3.37	0.167	-1.527	-1.852	0

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.020 / q_NPA : 0.013

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	4	VAL	0	0.017	0.010	3.856	-0.565	1.617	-0.024	-1.189	-0.968	0.003
4	A	5	LEU	0	-0.011	0.001	7.228	-0.002	-0.002	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.005	-0.013	10.546	0.108	0.108	0.000	0.000	0.000	0.000
6	A	7	ASN	0	-0.037	-0.014	13.253	0.049	0.049	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.005	-0.005	16.825	0.005	0.005	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.018	0.019	19.876	0.004	0.004	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.044	0.023	23.565	-0.002	-0.002	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.066	-0.030	26.988	0.008	0.008	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.006	0.001	30.378	0.003	0.003	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.845	-0.917	32.600	-0.132	-0.132	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.045	-0.014	26.667	0.001	0.001	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.016	0.009	23.300	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	16	VAL	0	-0.040	-0.019	21.303	0.004	0.004	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.023	0.008	17.858	-0.027	-0.027	0.000	0.000	0.000	0.000
17	A	18	ALA	0	-0.019	-0.019	16.771	0.036	0.036	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.006	0.006	10.840	-0.075	-0.075	0.000	0.000	0.000	0.000
19	A	20	CYS	0	-0.003	-0.011	10.864	0.163	0.163	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.747	-0.852	6.844	-0.974	-0.974	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.815	-0.893	5.820	-1.545	-1.545	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.928	-0.964	6.872	0.346	0.346	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.011	-0.006	8.375	0.108	0.108	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.028	-0.007	10.948	0.033	0.033	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.018	-0.010	12.995	0.049	0.049	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.035	-0.001	14.193	0.042	0.042	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.851	-0.920	16.358	-0.053	-0.053	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.039	0.031	15.404	0.024	0.024	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.857	0.888	19.416	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.089	0.039	22.753	0.009	0.009	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.940	0.957	24.688	0.012	0.012	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.013	0.018	28.177	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.914	0.970	26.039	0.071	0.071	0.000	0.000	0.000	0.000
34	A	35	THR	0	-0.010	-0.006	23.438	0.014	0.014	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.015	0.002	19.143	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	37	HIS	0	-0.005	-0.020	20.012	0.001	0.001	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.015	0.022	14.109	-0.015	-0.015	0.000	0.000	0.000	0.000
38	A	39	SER	0	0.004	-0.009	16.599	-0.022	-0.022	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.856	-0.940	17.552	-0.245	-0.245	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.036	-0.014	18.681	-0.030	-0.030	0.000	0.000	0.000	0.000
41	A	42	PHE	0	-0.046	-0.017	20.098	0.005	0.005	0.000	0.000	0.000	0.000
42	A	43	TYR	0	0.012	-0.006	14.788	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.007	0.009	14.320	-0.068	-0.068	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.029	-0.002	14.342	0.020	0.020	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.888	0.941	12.502	0.681	0.681	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.001	-0.020	7.395	-0.165	-0.165	0.000	0.000	0.000	0.000
47	A	48	MET	0	-0.125	-0.066	8.126	0.358	0.358	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.739	-0.849	3.802	-5.251	-5.059	0.001	-0.116	-0.077	-0.001
49	A	50	PRO	0	0.034	0.028	4.128	0.439	0.653	0.000	-0.034	-0.180	0.000
50	A	51	ASP	-1	-0.811	-0.907	6.977	-0.884	-0.884	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.886	0.937	9.200	0.992	0.992	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.013	0.010	9.845	0.182	0.182	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.083	0.048	10.998	0.156	0.156	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.742	0.849	12.864	0.567	0.567	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.871	0.940	14.618	0.498	0.498	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.030	0.009	13.958	0.058	0.058	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.824	0.909	13.440	0.531	0.531	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.839	-0.907	18.727	-0.388	-0.388	0.000	0.000	0.000	0.000
59	A	60	ALA	0	-0.003	-0.002	19.794	0.031	0.031	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.006	0.004	20.505	0.024	0.024	0.000	0.000	0.000	0.000
61	A	62	GLN	0	-0.062	-0.036	23.006	0.015	0.015	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.925	-0.952	23.026	-0.304	-0.304	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.027	-0.040	24.356	0.017	0.017	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.807	-0.879	27.399	-0.168	-0.168	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.803	-0.864	28.945	-0.130	-0.130	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.990	-0.997	31.326	-0.149	-0.149	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.779	0.875	28.762	0.155	0.155	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.008	0.010	27.574	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.026	0.011	22.261	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.008	0.003	23.743	0.004	0.004	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.005	-0.006	17.514	-0.031	-0.031	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.035	-0.018	18.019	0.064	0.064	0.000	0.000	0.000	0.000
73	A	74	ALA	0	0.025	0.015	12.935	-0.065	-0.065	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.035	-0.016	13.192	0.078	0.078	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.062	0.015	10.088	-0.076	-0.076	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.920	-0.953	7.880	0.160	0.160	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.034	-0.011	2.830	-0.816	-0.191	0.190	-0.188	-0.627	-0.002
78	A	79	ALA	0	0.004	-0.002	6.401	-0.042	-0.042	0.000	0.000	0.000	0.000
79	A	80	CYS	0	-0.038	-0.013	9.540	0.065	0.065	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.034	-0.030	7.574	0.005	0.005	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.021	-0.010	7.987	0.005	0.005	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.007	-0.005	10.525	0.059	0.059	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.002	0.009	12.935	0.043	0.043	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.840	-0.917	11.496	-0.500	-0.500	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.078	-0.048	13.496	0.035	0.035	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.025	-0.004	15.777	0.032	0.032	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.072	-0.037	17.511	0.025	0.025	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.013	0.008	17.849	0.021	0.021	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.756	0.844	17.859	0.094	0.094	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.898	-0.963	14.914	-0.093	-0.093	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.908	-0.934	17.250	-0.083	-0.083	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.845	-0.911	19.690	-0.130	-0.130	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.066	-0.015	14.464	-0.019	-0.019	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.017	0.015	17.778	0.029	0.029	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.882	-0.943	17.267	-0.022	-0.022	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.042	-0.022	17.968	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.069	-0.045	19.342	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	99	GLY	0	-0.034	-0.016	18.313	0.019	0.019	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.032	-0.007	12.695	0.029	0.029	0.000	0.000	0.000	0.000
100	A	101	PRO	0	0.031	0.014	11.979	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	102	HIS	0	0.003	-0.019	14.033	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	103	VAL	0	0.050	0.026	15.449	0.024	0.024	0.000	0.000	0.000	0.000
103	A	104	GLN	0	-0.047	-0.023	17.882	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.015	0.003	19.990	0.010	0.010	0.000	0.000	0.000	0.000
105	A	106	TYR	0	-0.020	-0.034	22.593	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.006	0.015	21.968	0.014	0.014	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.015	-0.011	26.159	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.011	0.013	29.619	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.761	0.834	30.599	0.157	0.157	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.923	-0.962	33.389	-0.091	-0.091	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.039	-0.020	37.121	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	113	PHE	0	-0.062	-0.009	35.397	0.007	0.007	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.036	-0.024	40.693	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.872	-0.932	38.714	-0.101	-0.101	0.000	0.000	0.000	0.000
115	A	116	GLY	0	-0.099	-0.052	43.289	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)