FMO DATABASE

FMODB ID: YV612

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	OptH
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	-984957.42598
FMO2-HF: Nuclear repulsion	938775.441295
FMO2-HF: Total energy	-46181.984686
FMO2-MP2: Total energy	-46318.388321

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.
-12.767	-5.968	7.352	-5.498	-8.653	-0.036

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 : -0.016 / q_NPA : -0.026

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	-0.017	0.003	3.158	-2.038	0.416	0.023	-1.159	-1.318	0.002
4	A	4	GLU	-1	-0.839	-0.924	2.281	-7.611	-5.332	2.990	-1.981	-3.288	-0.028
5	A	5	GLY	0	0.026	0.010	5.081	0.013	0.015	-0.001	-0.001	0.000	0.000
6	A	6	PRO	0	-0.045	-0.008	8.781	0.182	0.182	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.023	0.020	10.729	0.023	0.023	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.901	0.950	13.863	0.258	0.258	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.911	0.972	15.248	-0.135	-0.135	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.991	1.005	17.719	0.026	0.026	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.039	-0.029	20.871	0.009	0.009	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.054	-0.028	22.259	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.014	0.004	24.002	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.938	0.968	23.502	-0.119	-0.119	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.934	-0.973	24.913	0.137	0.137	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.049	0.027	26.779	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.925	0.977	28.608	-0.084	-0.084	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.983	0.991	28.365	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.053	-0.030	25.500	0.002	0.002	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.031	0.025	28.688	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.038	0.018	28.867	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.052	-0.033	25.929	0.005	0.005	0.000	0.000	0.000	0.000
23	A	23	SER	0	0.005	-0.002	24.632	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.043	0.026	19.589	0.009	0.009	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.046	-0.017	18.231	0.005	0.005	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.903	0.938	17.161	0.127	0.127	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.007	-0.007	12.503	0.076	0.076	0.000	0.000	0.000	0.000
28	A	28	TRP	0	0.006	0.014	5.888	0.162	0.162	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.026	-0.027	7.551	0.188	0.188	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.029	0.012	2.185	-0.527	-0.947	2.798	-0.758	-1.621	0.002
31	A	31	LEU	0	0.012	0.016	3.579	0.008	0.410	0.009	-0.112	-0.299	0.000
32	A	32	SER	0	0.002	-0.011	2.448	-0.917	1.142	1.517	-1.599	-1.976	-0.012
33	A	33	GLY	0	0.064	0.035	3.480	-1.044	-1.021	0.016	0.112	-0.151	0.000
34	A	34	ALA	0	0.078	0.043	5.866	-0.469	-0.469	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.075	-0.044	7.230	-0.400	-0.400	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.000	0.013	6.449	0.342	0.342	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.031	-0.021	5.219	-0.117	-0.117	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.012	0.010	7.978	-0.224	-0.224	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.022	0.017	6.379	-0.060	-0.060	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.026	0.011	12.062	-0.074	-0.074	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.017	0.002	15.108	-0.022	-0.022	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.854	0.924	15.129	0.169	0.169	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.047	0.018	18.615	0.011	0.011	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.081	0.053	21.073	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.973	0.997	20.337	0.211	0.211	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.044	-0.059	17.361	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.023	0.042	16.089	0.017	0.017	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.812	-0.912	13.479	-0.537	-0.537	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.958	0.984	6.973	0.482	0.482	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.961	0.982	10.916	0.449	0.449	0.000	0.000	0.000	0.000
51	A	51	HIS	0	-0.002	0.023	13.637	0.051	0.051	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.037	-0.036	11.804	0.071	0.071	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.911	0.950	13.175	-0.069	-0.069	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.056	0.019	11.361	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.036	0.037	11.220	0.107	0.107	0.000	0.000	0.000	0.000
56	A	56	PRO	0	-0.010	-0.009	9.926	-0.085	-0.085	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.006	-0.005	11.995	-0.015	-0.015	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.860	0.919	13.164	-0.235	-0.235	0.000	0.000	0.000	0.000
59	A	59	LYS	1	1.012	1.006	10.340	-1.214	-1.214	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.025	-0.013	11.078	-0.071	-0.071	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.007	0.025	11.213	0.047	0.047	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.027	-0.017	10.459	-0.102	-0.102	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.043	0.023	13.011	-0.062	-0.062	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.024	-0.021	14.716	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	65	TRP	0	-0.069	-0.013	15.623	-0.037	-0.037	0.000	0.000	0.000	0.000
66	A	66	MET	0	0.033	0.009	17.726	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.000	0.001	15.015	0.009	0.009	0.000	0.000	0.000	0.000
68	A	68	GLN	0	-0.010	-0.003	17.546	0.004	0.004	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.019	-0.011	17.868	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	70	PRO	0	-0.052	-0.037	21.040	0.005	0.005	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.979	-0.976	23.678	-0.125	-0.125	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.764	-0.874	25.270	-0.083	-0.083	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.019	-0.027	26.395	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.941	-0.955	28.393	-0.082	-0.082	0.000	0.000	0.000	0.000
75	A	75	HIS	0	-0.131	-0.054	24.308	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.039	0.022	23.402	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.907	-0.951	18.780	-0.232	-0.232	0.000	0.000	0.000	0.000
78	A	78	ILE	0	0.013	-0.003	18.422	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.008	0.011	12.566	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	80	GLN	0	-0.065	-0.044	18.475	0.001	0.001	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.021	-0.004	13.698	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	82	ASN	0	0.017	-0.007	17.639	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	83	ASN	0	0.044	0.018	18.966	0.001	0.001	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.023	-0.008	19.351	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.854	-0.919	22.199	0.136	0.136	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.907	0.953	23.718	-0.085	-0.085	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.072	0.057	24.726	-0.015	-0.015	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.059	-0.033	20.374	-0.017	-0.017	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.005	0.015	21.087	0.005	0.005	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.030	-0.031	17.639	0.009	0.009	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.997	1.011	19.427	0.033	0.033	0.000	0.000	0.000	0.000
92	A	92	PHE	0	-0.005	-0.027	13.176	0.028	0.028	0.000	0.000	0.000	0.000
93	A	93	GLN	0	0.051	0.032	17.259	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.025	-0.033	14.233	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.033	-0.013	15.665	-0.053	-0.053	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.019	0.004	16.746	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	97	ARG	1	1.060	1.035	17.929	0.187	0.187	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.011	0.002	14.086	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	99	HIS	0	0.015	-0.012	11.762	-0.121	-0.121	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.003	0.020	13.620	-0.027	-0.027	0.000	0.000	0.000	0.000
101	A	101	ILE	0	0.025	0.009	15.458	0.020	0.020	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.036	-0.008	10.375	0.006	0.006	0.000	0.000	0.000	0.000
103	A	103	TRP	0	0.003	-0.025	7.110	-0.067	-0.067	0.000	0.000	0.000	0.000
104	A	104	HIS	0	0.039	0.018	11.550	0.072	0.072	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.967	0.991	11.586	0.817	0.817	0.000	0.000	0.000	0.000
106	A	106	HIS	0	0.067	0.021	8.341	0.140	0.140	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.036	-0.025	9.648	0.186	0.186	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.872	-0.935	11.500	0.081	0.081	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.893	-0.941	10.968	-0.160	-0.160	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.033	-0.018	8.869	0.122	0.122	0.000	0.000	0.000	0.000
111	A	111	CYS	0	-0.101	-0.022	10.701	0.110	0.110	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.894	0.960	14.108	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.039	-0.028	11.009	0.065	0.065	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.016	0.001	12.057	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.943	0.970	12.051	-0.327	-0.327	0.000	0.000	0.000	0.000
116	A	116	PRO	0	0.007	0.014	11.146	-0.079	-0.079	0.000	0.000	0.000	0.000

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