FMO DATABASE

FMODB ID: YY6G2

Calculation Name: 2P19-A-Xray319

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2P19

Chain ID: A

ChEMBL ID:

UniProt ID: Q8NTZ4

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	149
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1275171.282036
FMO2-HF: Nuclear repulsion	1219176.391945
FMO2-HF: Total energy	-55994.890091
FMO2-MP2: Total energy	-56160.609289

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:ACE )

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

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.
-0.181	1.369	-0.006	-0.68	-0.862	-0.002

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

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 : 0.008

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	ASN	0	0.018	0.002	3.853	-0.141	1.156	-0.006	-0.655	-0.636	-0.002
4	A	4	ALA	0	0.010	0.015	4.549	0.106	0.195	0.000	-0.006	-0.082	0.000
5	A	5	ASN	0	-0.020	0.011	4.730	0.235	0.399	0.000	-0.019	-0.144	0.000
6	A	6	LEU	0	0.025	0.013	6.987	0.116	0.116	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.915	-0.954	10.790	-0.680	-0.680	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.003	0.003	12.896	0.079	0.079	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.928	0.970	15.929	0.317	0.317	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.014	-0.002	19.254	0.014	0.014	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.995	1.020	22.769	0.096	0.096	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.031	0.008	26.295	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.096	-0.047	29.341	0.004	0.004	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.826	-0.925	31.879	-0.050	-0.050	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.043	-0.042	33.746	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.914	0.971	35.928	0.050	0.050	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.049	0.036	39.423	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.075	-0.034	40.092	0.002	0.002	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.032	0.025	43.807	0.000	0.000	0.000	0.000	0.000	0.000
20	A	20	ALA	0	-0.019	-0.002	43.781	0.000	0.000	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.052	0.019	43.626	0.002	0.002	0.000	0.000	0.000	0.000
22	A	22	SER	0	0.048	0.000	45.608	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.014	0.017	43.091	0.000	0.000	0.000	0.000	0.000	0.000
24	A	24	ILE	0	-0.016	-0.003	39.025	0.000	0.000	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.032	0.012	41.688	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.954	-0.968	44.009	-0.027	-0.027	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.900	0.942	37.807	0.037	0.037	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.012	-0.017	37.415	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.009	0.017	40.499	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.072	-0.029	42.934	0.000	0.000	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.012	0.010	45.561	0.002	0.002	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.036	-0.037	47.613	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	GLY	0	-0.041	-0.023	47.835	0.001	0.001	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.829	-0.918	45.695	-0.035	-0.035	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.949	-0.979	43.678	-0.044	-0.044	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.005	0.010	39.892	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.013	-0.001	35.264	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.026	0.003	35.125	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.002	-0.013	30.432	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.926	0.959	31.069	0.062	0.062	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.909	0.953	24.940	0.114	0.114	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.025	0.026	24.343	0.004	0.004	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.864	0.925	18.655	0.178	0.178	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.034	0.004	19.612	0.021	0.021	0.000	0.000	0.000	0.000
45	A	45	THR	0	0.004	-0.001	13.310	-0.035	-0.035	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.013	-0.014	14.852	0.014	0.014	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.924	-0.965	15.422	-0.159	-0.159	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.012	0.001	15.830	0.023	0.023	0.000	0.000	0.000	0.000
49	A	49	PRO	0	0.008	0.019	19.089	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.029	-0.020	17.563	0.005	0.005	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.017	-0.012	20.966	0.013	0.013	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.000	0.016	23.706	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.077	-0.040	23.211	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.870	-0.938	27.536	-0.055	-0.055	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.049	-0.048	28.480	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	56	TYR	0	0.016	0.013	32.147	0.002	0.002	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.009	-0.013	32.340	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.055	0.028	36.175	0.003	0.003	0.000	0.000	0.000	0.000
59	A	59	PRO	0	0.051	0.015	39.296	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.035	-0.010	39.781	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	PHE	0	-0.015	-0.017	35.355	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.053	-0.032	36.472	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.787	-0.903	37.855	-0.064	-0.064	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.069	-0.021	31.490	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.024	0.016	34.027	0.001	0.001	0.000	0.000	0.000	0.000
66	A	66	LEU	0	0.015	-0.017	32.431	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.774	-0.864	31.075	-0.106	-0.106	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.807	-0.896	29.687	-0.097	-0.097	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.088	-0.045	27.788	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.971	-0.976	26.533	-0.114	-0.114	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.787	0.880	25.273	0.094	0.094	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.012	0.018	23.271	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	73	GLY	0	-0.051	-0.016	23.623	0.006	0.006	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.025	0.003	24.512	0.006	0.006	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.015	-0.062	24.569	0.005	0.005	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.833	-0.883	23.024	-0.171	-0.171	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.047	0.031	26.030	0.007	0.007	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.007	-0.006	29.328	0.007	0.007	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.928	0.940	22.969	0.144	0.144	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.052	-0.009	29.464	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.753	0.870	31.540	0.082	0.082	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.023	-0.002	32.913	0.005	0.005	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.021	0.007	31.690	0.004	0.004	0.000	0.000	0.000	0.000
84	A	84	VAL	0	-0.040	-0.037	27.749	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.036	-0.018	25.792	0.005	0.005	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.888	0.962	28.876	0.048	0.048	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.008	-0.009	30.171	0.002	0.002	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.018	0.008	27.510	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	89	ASN	0	-0.027	0.008	29.432	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	GLN	0	0.035	0.000	24.395	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.959	0.986	29.765	0.033	0.033	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.016	0.012	25.422	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.002	0.000	29.223	0.006	0.006	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.018	-0.006	29.245	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.778	0.862	30.949	0.045	0.045	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.913	0.953	31.686	0.014	0.014	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.004	0.013	30.829	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	98	VAL	0	0.005	-0.010	32.809	0.004	0.004	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.010	0.000	35.049	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.854	-0.940	34.156	-0.042	-0.042	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.797	-0.853	30.987	-0.050	-0.050	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.008	-0.004	29.773	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	103	THR	0	0.032	0.018	29.620	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.074	-0.041	28.695	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.058	-0.045	24.306	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.934	-0.956	24.864	-0.060	-0.060	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.045	-0.017	25.387	0.003	0.003	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.913	-0.961	27.844	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.901	-0.963	31.175	-0.029	-0.029	0.000	0.000	0.000	0.000
110	A	110	GLY	0	-0.033	-0.005	34.163	0.003	0.003	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.031	0.012	30.493	0.003	0.003	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.054	-0.023	27.581	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	113	LEU	0	0.017	0.008	27.218	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.011	0.007	23.102	0.005	0.005	0.000	0.000	0.000	0.000
115	A	115	THR	0	-0.044	-0.034	26.810	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	116	VAL	0	0.002	-0.013	25.866	0.003	0.003	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.887	-0.901	28.641	-0.049	-0.049	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.847	0.908	25.187	0.086	0.086	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.024	0.020	30.823	0.000	0.000	0.000	0.000	0.000	0.000
120	A	120	ALA	0	-0.011	-0.001	29.858	0.000	0.000	0.000	0.000	0.000	0.000
121	A	121	LEU	0	0.004	0.006	31.773	0.002	0.002	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.692	-0.836	32.522	-0.054	-0.054	0.000	0.000	0.000	0.000
123	A	123	ASN	0	-0.044	-0.053	34.346	0.003	0.003	0.000	0.000	0.000	0.000
124	A	124	SER	0	-0.081	-0.041	35.721	0.003	0.003	0.000	0.000	0.000	0.000
125	A	125	GLY	0	-0.026	-0.012	37.564	0.003	0.003	0.000	0.000	0.000	0.000
126	A	126	GLN	0	-0.027	-0.013	38.154	0.004	0.004	0.000	0.000	0.000	0.000
127	A	127	VAL	0	0.004	-0.001	35.857	-0.004	-0.004	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.038	-0.017	31.777	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.795	-0.889	29.350	-0.083	-0.083	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.042	-0.008	33.240	0.003	0.003	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.011	0.002	29.842	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	132	SER	0	-0.058	-0.040	30.857	0.005	0.005	0.000	0.000	0.000	0.000
133	A	133	HIS	0	0.011	0.008	26.125	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	134	CYS	0	-0.038	-0.017	27.469	0.006	0.006	0.000	0.000	0.000	0.000
135	A	135	TYR	0	0.020	-0.006	21.488	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.898	0.940	21.537	0.074	0.074	0.000	0.000	0.000	0.000
137	A	137	PRO	0	-0.031	-0.012	21.500	-0.007	-0.007	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.839	-0.904	20.153	-0.042	-0.042	0.000	0.000	0.000	0.000
139	A	139	MET	0	-0.028	-0.005	15.426	0.004	0.004	0.000	0.000	0.000	0.000
140	A	140	TYR	0	-0.019	-0.009	16.827	-0.031	-0.031	0.000	0.000	0.000	0.000
141	A	141	ASN	0	-0.044	-0.028	18.254	0.033	0.033	0.000	0.000	0.000	0.000
142	A	142	PHE	0	-0.001	-0.006	18.957	-0.015	-0.015	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.919	-0.942	15.424	-0.027	-0.027	0.000	0.000	0.000	0.000
144	A	144	THR	0	-0.046	-0.033	19.685	-0.008	-0.008	0.000	0.000	0.000	0.000
145	A	145	THR	0	0.003	-0.003	20.513	0.013	0.013	0.000	0.000	0.000	0.000
146	A	146	LEU	0	-0.023	-0.002	22.807	-0.007	-0.007	0.000	0.000	0.000	0.000
147	A	147	VAL	0	-0.004	-0.008	24.992	0.006	0.006	0.000	0.000	0.000	0.000
148	A	148	ALA	0	-0.045	-0.017	27.607	-0.004	-0.004	0.000	0.000	0.000	0.000
149	A	149	ARG	0	0.057	0.031	30.926	0.014	0.014	0.000	0.000	0.000	0.000

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