FMO DATABASE

FMODB ID: 1N2YZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-985960.261516
FMO2-HF: Nuclear repulsion	939777.354746
FMO2-HF: Total energy	-46182.90677
FMO2-MP2: Total energy	-46319.285582

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.
-11.251	-3.216	4.915	-4.862	-8.089	-0.032

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 : -0.035 / 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

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	3	MET	0	-0.015	0.013	2.977	-1.402	0.423	0.049	-0.812	-1.062	0.001
4	A	4	GLU	-1	-0.823	-0.913	2.435	-7.176	-3.794	1.463	-1.904	-2.941	-0.020
5	A	5	GLY	0	0.044	0.020	5.124	0.074	0.077	-0.001	-0.002	0.000	0.000
6	A	6	PRO	0	-0.045	-0.007	8.850	0.144	0.144	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.002	0.006	10.312	0.034	0.034	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.840	0.891	13.518	0.295	0.295	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.897	0.976	14.866	-0.027	-0.027	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.894	0.955	17.478	0.059	0.059	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.038	-0.024	20.836	0.001	0.001	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.034	-0.023	22.117	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.010	0.002	24.001	0.000	0.000	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.808	0.872	23.629	-0.078	-0.078	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.814	-0.881	25.237	0.081	0.081	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.050	0.027	27.056	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.928	0.980	28.753	-0.044	-0.044	0.000	0.000	0.000	0.000
18	A	18	LYS	1	1.011	1.004	28.385	0.014	0.014	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.045	-0.024	25.539	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.010	0.012	28.607	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.046	0.026	28.831	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.009	-0.017	25.413	0.002	0.002	0.000	0.000	0.000	0.000
23	A	23	SER	0	0.003	0.010	24.280	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.070	0.023	19.988	0.005	0.005	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.034	-0.004	18.192	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.871	0.930	16.895	0.172	0.172	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.024	-0.027	12.292	0.063	0.063	0.000	0.000	0.000	0.000
28	A	28	TRP	0	-0.005	-0.003	5.930	0.144	0.144	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.045	-0.027	7.791	0.149	0.149	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.014	0.008	2.337	-0.815	-0.524	1.541	-0.439	-1.393	0.002
31	A	31	LEU	0	-0.005	0.004	3.145	-0.116	0.383	0.022	-0.144	-0.377	0.000
32	A	32	SER	0	0.016	-0.002	2.630	-1.347	0.620	1.828	-1.619	-2.176	-0.015
33	A	33	GLY	0	0.060	0.029	3.548	-0.872	-0.804	0.013	0.058	-0.140	0.000
34	A	34	ALA	0	0.081	0.053	6.182	-0.446	-0.446	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.059	-0.042	7.389	-0.299	-0.299	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.012	0.025	6.781	0.254	0.254	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.027	-0.025	5.054	-0.009	-0.009	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.024	0.014	8.028	-0.197	-0.197	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.020	0.009	5.856	-0.043	-0.043	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.041	0.018	11.401	-0.064	-0.064	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.023	0.006	14.851	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.839	0.920	14.696	0.249	0.249	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.045	0.019	18.391	0.014	0.014	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.089	0.045	20.666	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.972	1.004	19.521	0.241	0.241	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.013	-0.038	16.857	0.009	0.009	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.019	0.017	15.695	0.013	0.013	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.779	-0.878	13.698	-0.500	-0.500	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.922	0.963	6.598	0.664	0.664	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.923	0.956	10.777	0.475	0.475	0.000	0.000	0.000	0.000
51	A	51	HIS	0	0.003	0.015	13.531	0.057	0.057	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.013	-0.002	11.624	0.069	0.069	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.902	0.944	12.758	0.027	0.027	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.058	0.030	11.114	-0.047	-0.047	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.071	0.040	10.569	0.059	0.059	0.000	0.000	0.000	0.000
56	A	56	PRO	0	-0.031	-0.008	9.664	-0.075	-0.075	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.036	0.010	11.635	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.859	0.907	13.149	-0.135	-0.135	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.986	1.003	10.289	-0.827	-0.827	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.005	0.005	11.395	-0.053	-0.053	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.033	0.000	11.430	0.036	0.036	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.024	-0.015	10.118	-0.076	-0.076	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.026	0.030	13.149	-0.062	-0.062	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.006	-0.005	15.095	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	65	TRP	0	-0.076	-0.021	15.915	-0.035	-0.035	0.000	0.000	0.000	0.000
66	A	66	MET	0	0.041	0.015	18.032	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.001	0.008	14.525	0.001	0.001	0.000	0.000	0.000	0.000
68	A	68	GLN	0	0.011	0.003	17.471	0.009	0.009	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.053	0.030	18.021	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	70	PRO	0	-0.048	-0.026	20.532	0.014	0.014	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.831	-0.890	23.365	-0.126	-0.126	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.820	-0.925	25.128	-0.108	-0.108	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.014	-0.003	26.002	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.930	-0.940	28.346	-0.090	-0.090	0.000	0.000	0.000	0.000
75	A	75	HIS	0	-0.137	-0.070	24.030	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.054	0.027	23.124	-0.011	-0.011	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.830	-0.914	18.862	-0.257	-0.257	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.007	-0.002	18.070	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.010	0.011	12.223	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	80	GLN	0	-0.051	-0.047	17.957	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.014	-0.006	13.492	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.015	-0.021	17.578	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ASN	0	0.029	-0.004	19.170	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.020	0.003	19.654	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.819	-0.890	22.459	0.097	0.097	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.910	0.955	23.570	-0.049	-0.049	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.055	0.042	24.614	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.088	-0.057	20.923	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.010	0.016	20.968	0.003	0.003	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.005	-0.017	17.575	0.005	0.005	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.988	1.010	19.019	0.072	0.072	0.000	0.000	0.000	0.000
92	A	92	PHE	0	-0.005	-0.026	12.355	0.019	0.019	0.000	0.000	0.000	0.000
93	A	93	GLN	0	0.041	0.039	16.662	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.020	-0.042	13.785	-0.027	-0.027	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.047	-0.015	15.507	-0.051	-0.051	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.034	0.012	16.756	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.907	0.946	17.694	0.162	0.162	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.027	0.014	13.791	0.007	0.007	0.000	0.000	0.000	0.000
99	A	99	HIS	0	0.014	-0.004	11.476	-0.112	-0.112	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.012	0.005	13.453	-0.033	-0.033	0.000	0.000	0.000	0.000
101	A	101	ILE	0	0.020	0.009	15.251	0.017	0.017	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.009	0.005	10.193	0.010	0.010	0.000	0.000	0.000	0.000
103	A	103	TRP	0	-0.005	-0.023	6.304	-0.065	-0.065	0.000	0.000	0.000	0.000
104	A	104	HIS	0	0.029	0.014	11.295	0.051	0.051	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.873	0.929	10.509	0.563	0.563	0.000	0.000	0.000	0.000
106	A	106	HIS	0	0.070	0.026	8.106	0.207	0.207	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.020	-0.014	9.847	0.154	0.154	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.840	-0.900	11.426	0.054	0.054	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.806	-0.899	11.020	-0.157	-0.157	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.022	-0.006	8.916	0.103	0.103	0.000	0.000	0.000	0.000
111	A	111	CYS	0	-0.095	-0.046	10.842	0.092	0.092	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.824	0.911	14.150	0.001	0.001	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.019	-0.006	11.250	0.060	0.060	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.024	0.005	11.843	-0.018	-0.018	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.908	0.943	12.215	-0.246	-0.246	0.000	0.000	0.000	0.000
116	A	116	PRO	0	0.001	0.013	11.137	-0.054	-0.054	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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