FMO DATABASE

FMODB ID: K35Z3

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

Total energy (hartree)

FMO2-HF: Electronic energy	-854667.630093
FMO2-HF: Nuclear repulsion	810366.87992
FMO2-HF: Total energy	-44300.750173
FMO2-MP2: Total energy	-44429.339762

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.
-8.632	-4.377	0.157	-2.255	-2.157	-0.003

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 : 0.028 / q_NPA : 0.019

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	0.038	0.014	3.831	-0.940	1.755	-0.032	-1.532	-1.132	0.003
4	A	5	LEU	0	-0.032	-0.015	7.169	0.019	0.019	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.006	0.003	10.517	0.110	0.110	0.000	0.000	0.000	0.000
6	A	7	ASN	0	-0.040	-0.018	13.430	0.025	0.025	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.005	0.005	16.900	0.015	0.015	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.009	0.012	19.881	0.000	0.000	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.053	0.033	23.446	0.004	0.004	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.059	-0.034	26.756	0.009	0.009	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.003	-0.001	29.955	0.002	0.002	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.855	-0.929	32.551	-0.128	-0.128	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.023	-0.003	26.783	0.000	0.000	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.022	0.012	23.161	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	16	VAL	0	-0.018	-0.001	20.981	0.003	0.003	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.004	-0.003	17.941	-0.030	-0.030	0.000	0.000	0.000	0.000
17	A	18	ALA	0	-0.012	-0.013	17.038	0.021	0.021	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.004	-0.008	11.040	-0.071	-0.071	0.000	0.000	0.000	0.000
19	A	20	CYS	0	-0.021	-0.025	10.896	0.152	0.152	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.752	-0.856	6.908	-0.813	-0.813	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.836	-0.903	5.584	-1.373	-1.373	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.942	-0.975	6.340	0.725	0.725	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.006	-0.002	7.917	0.079	0.079	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.036	-0.015	10.750	0.007	0.007	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.022	-0.011	12.824	0.058	0.058	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.012	0.012	14.087	0.039	0.039	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.871	-0.959	16.242	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.006	0.014	15.586	0.024	0.024	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.862	0.927	19.654	-0.053	-0.053	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.087	0.025	22.588	0.007	0.007	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.950	0.967	24.571	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.009	0.014	28.158	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.916	0.972	25.887	0.040	0.040	0.000	0.000	0.000	0.000
34	A	35	THR	0	0.004	-0.005	23.663	0.016	0.016	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.041	-0.005	18.926	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	37	HIS	0	0.009	-0.002	20.372	0.012	0.012	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.007	0.020	14.001	-0.023	-0.023	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.020	-0.018	16.704	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.865	-0.946	17.191	-0.192	-0.192	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.034	-0.014	18.350	-0.022	-0.022	0.000	0.000	0.000	0.000
41	A	42	PHE	0	-0.032	-0.011	20.232	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	43	TYR	0	-0.025	-0.012	14.708	-0.025	-0.025	0.000	0.000	0.000	0.000
43	A	44	SER	0	0.078	0.006	14.646	0.025	0.025	0.000	0.000	0.000	0.000
44	A	45	GLY	0	-0.019	0.016	13.555	0.036	0.036	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.925	0.957	12.404	0.716	0.716	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.030	-0.029	6.985	-0.228	-0.228	0.000	0.000	0.000	0.000
47	A	48	MET	0	-0.125	-0.074	8.191	0.270	0.270	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.804	-0.898	3.468	-7.834	-7.011	0.021	-0.530	-0.314	-0.004
49	A	50	PRO	0	0.063	0.034	4.110	0.582	0.796	0.000	-0.034	-0.180	0.000
50	A	51	ASP	-1	-0.824	-0.902	6.962	-0.904	-0.904	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.871	0.920	9.082	1.094	1.094	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.018	-0.009	9.776	0.203	0.203	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.106	0.054	11.043	0.166	0.166	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.782	0.880	12.972	0.601	0.601	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.914	0.948	14.653	0.590	0.590	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.016	0.016	13.923	0.060	0.060	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.877	0.938	14.359	0.560	0.560	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.865	-0.929	18.758	-0.424	-0.424	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.026	0.024	20.149	0.030	0.030	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.006	-0.016	20.639	0.029	0.029	0.000	0.000	0.000	0.000
61	A	62	GLN	0	-0.076	-0.044	22.990	0.013	0.013	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.933	-0.943	24.419	-0.267	-0.267	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.054	-0.060	24.625	0.019	0.019	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.810	-0.878	27.621	-0.173	-0.173	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.810	-0.860	28.995	-0.134	-0.134	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.996	-1.006	31.145	-0.152	-0.152	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.771	0.879	28.781	0.154	0.154	0.000	0.000	0.000	0.000
68	A	69	THR	0	-0.002	0.009	27.822	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.010	0.003	22.403	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.021	-0.007	23.696	0.010	0.010	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.005	-0.005	17.494	-0.028	-0.028	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.001	0.002	18.486	0.060	0.060	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.006	0.010	13.244	-0.053	-0.053	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.010	-0.005	13.595	0.066	0.066	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.051	0.007	10.386	-0.067	-0.067	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.918	-0.949	8.347	0.171	0.171	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.020	-0.003	2.858	-0.776	-0.253	0.168	-0.159	-0.531	-0.002
78	A	79	ALA	0	0.009	-0.005	6.708	-0.110	-0.110	0.000	0.000	0.000	0.000
79	A	80	CYS	0	-0.046	-0.021	9.625	0.036	0.036	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.028	-0.019	7.985	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	VAL	0	0.002	-0.002	8.104	-0.027	-0.027	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.009	-0.005	10.690	0.050	0.050	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.005	0.000	13.449	0.033	0.033	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.900	-0.946	11.750	-0.526	-0.526	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.061	-0.029	13.740	0.008	0.008	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.044	-0.018	15.940	0.032	0.032	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.068	-0.031	17.708	0.027	0.027	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.009	0.003	17.729	0.023	0.023	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.779	0.856	18.248	0.096	0.096	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.905	-0.966	15.358	-0.115	-0.115	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.902	-0.935	17.625	-0.085	-0.085	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.853	-0.916	20.184	-0.130	-0.130	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.089	-0.025	14.916	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.019	0.015	18.273	0.025	0.025	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.885	-0.965	17.846	0.016	0.016	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.048	-0.033	18.192	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.029	-0.018	18.529	0.000	0.000	0.000	0.000	0.000	0.000
98	A	99	GLY	0	-0.061	-0.027	18.473	0.022	0.022	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.031	-0.004	12.951	0.028	0.028	0.000	0.000	0.000	0.000
100	A	101	PRO	0	0.039	0.030	12.412	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	102	HIS	0	0.006	-0.012	14.533	-0.020	-0.020	0.000	0.000	0.000	0.000
102	A	103	VAL	0	0.052	0.028	15.764	0.018	0.018	0.000	0.000	0.000	0.000
103	A	104	GLN	0	-0.045	-0.032	18.292	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.022	0.005	19.995	0.008	0.008	0.000	0.000	0.000	0.000
105	A	106	TYR	0	-0.017	-0.012	22.781	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.009	0.009	22.100	0.010	0.010	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.021	-0.015	26.489	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.011	0.014	29.997	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.750	0.834	30.957	0.162	0.162	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.933	-0.970	33.625	-0.092	-0.092	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.019	-0.007	37.309	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	113	PHE	0	-0.062	-0.015	35.617	0.007	0.007	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.035	-0.017	40.881	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.864	-0.932	38.699	-0.109	-0.109	0.000	0.000	0.000	0.000
115	A	116	GLY	0	-0.099	-0.053	43.248	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)