FMO DATABASE

FMODB ID: Q1RRY

Calculation Name: 2P19-A-Xray372

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: 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	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	148
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1272115.047304
FMO2-HF: Nuclear repulsion	1216270.484129
FMO2-HF: Total energy	-55844.563176
FMO2-MP2: Total energy	-56009.779263

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:LYS)

Summations of interaction energy for fragment #1(A:2:LYS)

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.
-62.587	-57.805	2.518	-3.468	-3.832	-0.02

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.998 / q_NPA : 0.982

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	ALA	0	0.033	0.027	3.268	2.101	4.609	-0.011	-1.158	-1.339	-0.001
4	A	5	ASN	0	-0.036	-0.010	2.433	-1.567	0.698	2.530	-2.301	-2.495	-0.019
5	A	6	LEU	0	0.044	0.021	4.772	0.125	0.134	-0.001	-0.009	0.002	0.000
6	A	7	ASP	-1	-0.859	-0.925	6.554	-33.990	-33.990	0.000	0.000	0.000	0.000
7	A	8	PRO	0	-0.009	0.005	8.718	2.012	2.012	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.866	0.932	10.117	25.695	25.695	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.013	-0.008	14.914	0.678	0.678	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.974	1.009	18.362	12.324	12.324	0.000	0.000	0.000	0.000
11	A	12	VAL	0	0.036	0.016	21.948	0.115	0.115	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.094	-0.036	25.393	-0.010	-0.010	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.807	-0.898	28.118	-8.751	-8.751	0.000	0.000	0.000	0.000
14	A	15	HIS	0	-0.053	-0.035	28.976	-0.155	-0.155	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.894	0.941	31.659	8.627	8.627	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.056	0.043	35.247	-0.094	-0.094	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.086	-0.047	36.902	0.107	0.107	0.000	0.000	0.000	0.000
18	A	19	ALA	0	0.034	0.031	40.276	-0.034	-0.034	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.031	-0.007	40.832	-0.050	-0.050	0.000	0.000	0.000	0.000
20	A	21	SER	0	0.047	0.015	41.324	0.195	0.195	0.000	0.000	0.000	0.000
21	A	22	SER	0	0.035	-0.006	42.573	-0.111	-0.111	0.000	0.000	0.000	0.000
22	A	23	ALA	0	0.042	0.030	41.074	-0.021	-0.021	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.020	-0.005	36.290	-0.143	-0.143	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.016	0.002	39.012	-0.141	-0.141	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.953	-0.972	41.411	-7.144	-7.144	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.832	0.894	35.224	8.465	8.465	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.007	-0.012	34.711	-0.226	-0.226	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.026	0.008	38.108	-0.045	-0.045	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.072	-0.030	40.164	0.054	0.054	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.001	-0.018	42.893	0.168	0.168	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.043	-0.037	44.577	-0.138	-0.138	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.021	-0.012	44.977	0.156	0.156	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.810	-0.900	42.104	-7.209	-7.209	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.904	-0.947	39.846	-7.831	-7.831	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.001	0.011	36.710	-0.165	-0.165	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.017	0.003	31.044	0.077	0.077	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.033	-0.004	31.555	-0.176	-0.176	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.003	-0.007	26.640	-0.133	-0.133	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.819	0.884	27.745	9.524	9.524	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.927	0.948	21.817	12.925	12.925	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.032	0.025	21.482	0.286	0.286	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.851	0.918	15.299	16.832	16.832	0.000	0.000	0.000	0.000
43	A	44	SER	0	0.051	0.026	16.553	0.874	0.874	0.000	0.000	0.000	0.000
44	A	45	THR	0	0.013	0.006	11.010	-0.894	-0.894	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.002	0.001	11.898	-0.022	-0.022	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.923	-0.975	12.434	-18.452	-18.452	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.004	0.010	14.765	1.036	1.036	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.006	0.009	16.987	-0.693	-0.693	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.029	-0.015	15.728	0.021	0.021	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.005	-0.013	19.126	0.508	0.508	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.017	0.028	21.625	-0.264	-0.264	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.068	-0.034	19.949	0.040	0.040	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.780	-0.862	24.637	-9.517	-9.517	0.000	0.000	0.000	0.000
54	A	55	ASN	0	-0.058	-0.051	25.783	-0.422	-0.422	0.000	0.000	0.000	0.000
55	A	56	TYR	0	-0.013	-0.020	29.197	0.247	0.247	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.004	0.004	29.201	-0.201	-0.201	0.000	0.000	0.000	0.000
57	A	58	PRO	0	0.056	0.029	33.236	0.234	0.234	0.000	0.000	0.000	0.000
58	A	59	PRO	0	0.046	0.009	35.985	-0.193	-0.193	0.000	0.000	0.000	0.000
59	A	60	ALA	0	-0.043	-0.013	36.571	-0.042	-0.042	0.000	0.000	0.000	0.000
60	A	61	PHE	0	-0.011	-0.011	31.649	-0.186	-0.186	0.000	0.000	0.000	0.000
61	A	62	ASN	0	-0.074	-0.043	32.585	-0.402	-0.402	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.760	-0.867	32.722	-9.729	-9.729	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.073	-0.022	27.221	-0.277	-0.277	0.000	0.000	0.000	0.000
64	A	65	SER	0	0.020	-0.013	28.332	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.008	-0.015	26.947	-0.370	-0.370	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.774	-0.867	25.187	-12.639	-12.639	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.726	-0.817	23.474	-11.960	-11.960	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.052	-0.028	22.054	-0.671	-0.671	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.982	-0.983	21.048	-13.103	-13.103	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.736	0.852	18.796	12.256	12.256	0.000	0.000	0.000	0.000
71	A	72	GLY	0	-0.005	0.005	17.685	-0.897	-0.897	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.019	-0.004	18.768	0.319	0.319	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.031	0.009	19.991	0.295	0.295	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.016	-0.057	21.504	0.294	0.294	0.000	0.000	0.000	0.000
75	A	76	ASP	-1	-0.822	-0.876	18.804	-16.129	-16.129	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.056	0.053	21.853	0.306	0.306	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.018	-0.005	25.125	0.416	0.416	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.848	0.902	19.102	15.316	15.316	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.046	-0.032	24.300	0.182	0.182	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.706	0.798	26.551	10.933	10.933	0.000	0.000	0.000	0.000
81	A	82	GLY	0	-0.017	0.000	28.697	0.371	0.371	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.031	-0.001	28.837	0.181	0.181	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.036	-0.031	25.710	-0.548	-0.548	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.044	-0.017	24.266	0.346	0.346	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.851	0.929	27.561	9.775	9.775	0.000	0.000	0.000	0.000
86	A	87	ILE	0	-0.005	-0.003	29.637	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.029	0.008	26.649	-0.075	-0.075	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.002	0.019	28.569	-0.132	-0.132	0.000	0.000	0.000	0.000
89	A	90	GLN	0	0.010	-0.002	24.181	-0.334	-0.334	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.956	0.981	29.552	8.553	8.553	0.000	0.000	0.000	0.000
91	A	92	ILE	0	0.019	0.015	25.268	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.003	0.002	28.618	0.374	0.374	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.018	0.002	28.590	-0.386	-0.386	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.768	0.845	30.211	9.820	9.820	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.894	0.943	30.893	8.093	8.093	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.023	0.021	29.545	0.021	0.021	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.016	-0.026	31.511	0.314	0.314	0.000	0.000	0.000	0.000
98	A	99	GLY	0	0.040	0.028	33.890	-0.090	-0.090	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.862	-0.928	31.943	-9.242	-9.242	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.793	-0.847	29.414	-9.949	-9.949	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.036	-0.026	28.083	-0.428	-0.428	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.011	-0.032	28.058	-0.423	-0.423	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.051	-0.032	26.371	-0.422	-0.422	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.035	-0.020	22.604	-0.628	-0.628	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.933	-0.953	23.021	-12.637	-12.637	0.000	0.000	0.000	0.000
106	A	107	ILE	0	-0.032	-0.007	24.495	-0.153	-0.153	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.907	-0.959	26.926	-9.247	-9.247	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.840	-0.923	30.474	-8.783	-8.783	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.024	-0.002	33.099	0.183	0.183	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.032	0.021	29.984	0.120	0.120	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.059	-0.027	27.315	0.075	0.075	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.035	0.015	25.778	-0.374	-0.374	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.014	0.009	22.148	0.384	0.384	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.048	-0.051	25.879	-0.027	-0.027	0.000	0.000	0.000	0.000
115	A	116	VAL	0	-0.020	-0.025	24.890	-0.034	-0.034	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.808	-0.845	27.730	-9.030	-9.030	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.776	0.853	24.451	11.671	11.671	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.033	0.020	29.754	0.125	0.125	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.014	-0.001	28.197	-0.077	-0.077	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.012	0.006	30.130	0.183	0.183	0.000	0.000	0.000	0.000
121	A	122	ASP	-1	-0.641	-0.793	30.854	-9.317	-9.317	0.000	0.000	0.000	0.000
122	A	123	ASN	0	-0.076	-0.063	32.488	-0.094	-0.094	0.000	0.000	0.000	0.000
123	A	124	SER	0	-0.052	-0.040	34.139	0.197	0.197	0.000	0.000	0.000	0.000
124	A	125	GLY	0	-0.030	-0.004	35.940	0.239	0.239	0.000	0.000	0.000	0.000
125	A	126	GLN	0	-0.035	-0.024	35.983	0.344	0.344	0.000	0.000	0.000	0.000
126	A	127	VAL	0	-0.008	-0.010	33.821	-0.333	-0.333	0.000	0.000	0.000	0.000
127	A	128	ILE	0	-0.041	-0.011	29.043	0.035	0.035	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.759	-0.857	26.766	-11.516	-11.516	0.000	0.000	0.000	0.000
129	A	130	LEU	0	0.002	0.016	30.553	0.082	0.082	0.000	0.000	0.000	0.000
130	A	131	GLY	0	-0.017	-0.016	27.872	-0.305	-0.305	0.000	0.000	0.000	0.000
131	A	132	SER	0	-0.048	-0.050	28.731	0.266	0.266	0.000	0.000	0.000	0.000
132	A	133	HIS	0	0.012	0.032	24.506	-0.030	-0.030	0.000	0.000	0.000	0.000
133	A	134	CYS	0	-0.034	-0.022	25.730	0.279	0.279	0.000	0.000	0.000	0.000
134	A	135	TYR	0	0.029	-0.004	20.142	-0.202	-0.202	0.000	0.000	0.000	0.000
135	A	136	ARG	1	0.866	0.919	20.138	13.485	13.485	0.000	0.000	0.000	0.000
136	A	137	PRO	0	-0.038	-0.013	20.562	-0.524	-0.524	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.842	-0.912	20.349	-13.162	-13.162	0.000	0.000	0.000	0.000
138	A	139	MET	0	-0.028	-0.010	14.306	-0.669	-0.669	0.000	0.000	0.000	0.000
139	A	140	TYR	0	-0.032	-0.018	15.824	-1.212	-1.212	0.000	0.000	0.000	0.000
140	A	141	ASN	0	-0.026	-0.025	17.800	1.134	1.134	0.000	0.000	0.000	0.000
141	A	142	PHE	0	0.000	0.003	18.788	-0.532	-0.532	0.000	0.000	0.000	0.000
142	A	143	GLU	-1	-0.913	-0.938	15.724	-15.502	-15.502	0.000	0.000	0.000	0.000
143	A	144	THR	0	-0.022	-0.017	20.156	0.208	0.208	0.000	0.000	0.000	0.000
144	A	145	THR	0	-0.043	-0.033	22.337	-0.112	-0.112	0.000	0.000	0.000	0.000
145	A	146	LEU	0	-0.007	0.007	24.380	0.096	0.096	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.004	0.002	27.026	-0.005	-0.005	0.000	0.000	0.000	0.000
147	A	148	ALA	0	0.006	0.009	29.690	0.197	0.197	0.000	0.000	0.000	0.000
148	A	149	ARG	1	0.991	0.995	32.888	8.264	8.264	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)