FMO DATABASE

FMODB ID: VQ8N1

Calculation Name: 2DTC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2DTC

Chain ID: A

ChEMBL ID:

UniProt ID: A2AR50

Base Structure: X-ray

Registration Date: 2023-09-20

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-985321.696968
FMO2-HF: Nuclear repulsion	939139.045646
FMO2-HF: Total energy	-46182.651322
FMO2-MP2: Total energy	-46319.054146

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:1:PRO)

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

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.
-11.23	-3.393	5.166	-4.813	-8.188	-0.027

Interaction energy analysis for fragmet #1(A:1:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.029 / q_NPA : -0.035

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

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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	3	MET	0	-0.014	0.007	3.310	-1.658	0.451	0.005	-0.931	-1.183	0.002
4	A	4	GLU	-1	-0.827	-0.912	2.547	-6.868	-3.860	1.132	-1.560	-2.580	-0.017
5	A	5	GLY	0	0.026	0.012	5.220	0.042	0.040	-0.001	0.000	0.004	0.000
6	A	6	PRO	0	-0.046	-0.006	8.889	0.147	0.147	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.012	0.015	10.754	0.033	0.033	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.869	0.924	13.817	0.279	0.279	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.901	0.973	15.057	-0.063	-0.063	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.987	1.003	17.628	0.045	0.045	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.041	-0.028	20.771	0.006	0.006	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.033	-0.018	22.170	-0.007	-0.007	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.008	0.000	23.905	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.854	0.908	23.602	-0.089	-0.089	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.857	-0.921	24.830	0.100	0.100	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.056	0.029	26.697	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.930	0.979	28.517	-0.058	-0.058	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.990	0.998	28.282	0.006	0.006	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.056	-0.029	25.434	0.002	0.002	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.024	0.021	28.616	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.042	0.021	28.824	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.039	-0.029	25.839	0.003	0.003	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.009	-0.008	24.557	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.053	0.026	19.905	0.005	0.005	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.045	-0.016	18.381	0.005	0.005	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.908	0.946	17.109	0.169	0.169	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.008	-0.015	12.538	0.067	0.067	0.000	0.000	0.000	0.000
28	A	28	TRP	0	-0.003	0.004	6.130	0.162	0.162	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.033	-0.034	7.616	0.154	0.154	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.024	0.012	2.375	-0.651	-0.681	2.183	-0.564	-1.589	0.002
31	A	31	LEU	0	0.009	0.015	3.448	-0.056	0.399	0.014	-0.134	-0.334	0.000
32	A	32	SER	0	0.015	-0.006	2.491	-1.171	1.075	1.818	-1.726	-2.338	-0.014
33	A	33	GLY	0	0.056	0.036	3.509	-0.993	-0.942	0.015	0.102	-0.168	0.000
34	A	34	ALA	0	0.066	0.037	5.867	-0.448	-0.448	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.077	-0.047	7.256	-0.384	-0.384	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.006	0.019	6.401	0.253	0.253	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.027	-0.019	5.078	-0.072	-0.072	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.012	0.007	7.961	-0.212	-0.212	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.031	0.016	6.095	-0.026	-0.026	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.041	0.020	11.754	-0.056	-0.056	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.022	0.007	14.926	-0.028	-0.028	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.845	0.920	14.964	0.254	0.254	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.049	0.011	18.506	0.014	0.014	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.078	0.049	21.047	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.963	0.994	20.314	0.237	0.237	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.018	-0.036	17.487	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.012	0.028	16.227	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.768	-0.883	13.874	-0.513	-0.513	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.948	0.976	6.963	0.669	0.669	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.898	0.947	11.150	0.483	0.483	0.000	0.000	0.000	0.000
51	A	51	HIS	0	0.015	0.028	13.791	0.055	0.055	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.030	-0.025	11.854	0.072	0.072	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.890	0.938	13.094	0.025	0.025	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.070	0.030	11.103	-0.043	-0.043	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.063	0.040	10.846	0.064	0.064	0.000	0.000	0.000	0.000
56	A	56	PRO	0	-0.040	-0.014	9.749	-0.065	-0.065	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.014	-0.011	11.804	0.004	0.004	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.880	0.929	13.189	-0.121	-0.121	0.000	0.000	0.000	0.000
59	A	59	LYS	1	1.010	1.006	10.076	-0.935	-0.935	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.028	-0.014	11.052	-0.049	-0.049	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.008	0.024	11.163	0.037	0.037	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.031	-0.018	10.266	-0.093	-0.093	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.051	0.025	12.862	-0.056	-0.056	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.020	-0.017	14.738	-0.022	-0.022	0.000	0.000	0.000	0.000
65	A	65	TRP	0	-0.080	-0.010	15.527	-0.041	-0.041	0.000	0.000	0.000	0.000
66	A	66	MET	0	0.047	0.016	17.613	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.000	0.007	14.703	0.001	0.001	0.000	0.000	0.000	0.000
68	A	68	GLN	0	-0.004	0.003	17.398	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.039	0.005	18.234	-0.015	-0.015	0.000	0.000	0.000	0.000
70	A	70	PRO	0	-0.057	-0.040	20.935	0.007	0.007	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.828	-0.872	23.748	-0.127	-0.127	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.766	-0.881	25.388	-0.087	-0.087	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.028	-0.028	26.609	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.922	-0.942	28.637	-0.086	-0.086	0.000	0.000	0.000	0.000
75	A	75	HIS	0	-0.151	-0.079	24.432	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.030	0.016	23.593	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.880	-0.934	19.055	-0.238	-0.238	0.000	0.000	0.000	0.000
78	A	78	ILE	0	0.014	-0.009	18.592	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.022	0.016	12.505	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	80	GLN	0	-0.057	-0.043	18.335	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.020	-0.006	13.478	0.001	0.001	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.016	-0.029	17.508	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	83	ASN	0	0.028	-0.006	18.864	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.027	-0.002	19.219	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.835	-0.892	22.099	0.115	0.115	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.907	0.953	23.608	-0.070	-0.070	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.075	0.058	24.617	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.063	-0.035	20.218	-0.018	-0.018	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.001	0.008	20.951	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.032	-0.031	17.546	0.005	0.005	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.996	1.013	19.303	0.053	0.053	0.000	0.000	0.000	0.000
92	A	92	PHE	0	0.000	-0.026	12.814	0.020	0.020	0.000	0.000	0.000	0.000
93	A	93	GLN	0	0.059	0.056	17.136	-0.019	-0.019	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.020	-0.036	14.506	-0.026	-0.026	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.055	-0.030	15.845	-0.049	-0.049	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.022	0.013	17.015	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.918	0.947	18.167	0.169	0.169	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.018	0.004	14.339	0.003	0.003	0.000	0.000	0.000	0.000
99	A	99	HIS	0	0.020	-0.008	11.849	-0.113	-0.113	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.011	0.011	13.888	-0.026	-0.026	0.000	0.000	0.000	0.000
101	A	101	ILE	0	0.013	0.002	15.699	0.020	0.020	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.007	0.007	10.513	0.009	0.009	0.000	0.000	0.000	0.000
103	A	103	TRP	0	-0.001	-0.027	6.757	-0.055	-0.055	0.000	0.000	0.000	0.000
104	A	104	HIS	0	0.031	0.015	11.747	0.061	0.061	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.874	0.943	10.707	0.549	0.549	0.000	0.000	0.000	0.000
106	A	106	HIS	0	0.071	0.025	8.303	0.189	0.189	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.020	-0.013	9.682	0.171	0.171	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.827	-0.900	11.346	0.096	0.096	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.834	-0.916	10.886	-0.129	-0.129	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.016	-0.010	8.876	0.111	0.111	0.000	0.000	0.000	0.000
111	A	111	CYS	0	-0.103	-0.031	10.720	0.094	0.094	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.841	0.920	14.117	-0.026	-0.026	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.037	-0.021	10.900	0.073	0.073	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.031	0.014	11.693	-0.035	-0.035	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.899	0.942	12.050	-0.293	-0.293	0.000	0.000	0.000	0.000
116	A	116	PRO	0	0.010	0.016	11.074	-0.065	-0.065	0.000	0.000	0.000	0.000

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