FMO DATABASE

FMODB ID: G5LG1

Calculation Name: 2PPI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PPI

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H2C0

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:

Apendix: None

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	125
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1000531.326578
FMO2-HF: Nuclear repulsion	950274.885661
FMO2-HF: Total energy	-50256.440917
FMO2-MP2: Total energy	-50400.806072

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:TYR)

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

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.
-0.739	1.573	0.032	-0.857	-1.488	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.019

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].
3	A	3	GLN	0	-0.037	-0.028	3.454	-0.907	1.405	0.032	-0.857	-1.488
4	A	4	SER	0	-0.009	0.006	5.682	0.166	0.166	0.000	0.000	0.000
5	A	5	MET	0	0.017	0.010	9.262	0.014	0.014	0.000	0.000	0.000
6	A	6	ALA	0	0.029	0.007	11.913	0.036	0.036	0.000	0.000	0.000
7	A	7	VAL	0	-0.016	-0.009	15.402	0.010	0.010	0.000	0.000	0.000
8	A	8	SER	0	0.000	0.000	17.847	0.019	0.019	0.000	0.000	0.000
9	A	9	ASP	-1	-0.814	-0.907	21.288	-0.130	-0.130	0.000	0.000	0.000
10	A	10	PRO	0	0.006	-0.003	24.600	0.009	0.009	0.000	0.000	0.000
11	A	11	GLN	0	0.003	-0.005	27.088	0.013	0.013	0.000	0.000	0.000
12	A	12	HIS	0	-0.024	-0.002	27.627	0.003	0.003	0.000	0.000	0.000
13	A	13	ALA	0	0.050	0.018	29.622	0.004	0.004	0.000	0.000	0.000
14	A	14	ALA	0	0.031	0.024	31.816	0.004	0.004	0.000	0.000	0.000
15	A	15	ARG	1	0.871	0.920	28.611	0.108	0.108	0.000	0.000	0.000
16	A	16	LEU	0	-0.004	-0.004	32.190	0.002	0.002	0.000	0.000	0.000
17	A	17	LEU	0	0.018	0.021	34.738	0.003	0.003	0.000	0.000	0.000
18	A	18	ARG	1	0.996	0.994	35.238	0.069	0.069	0.000	0.000	0.000
19	A	19	ALA	0	-0.025	-0.008	37.452	0.003	0.003	0.000	0.000	0.000
20	A	20	LEU	0	0.011	0.000	37.319	0.002	0.002	0.000	0.000	0.000
21	A	21	SER	0	-0.008	-0.007	40.526	0.004	0.004	0.000	0.000	0.000
22	A	22	SER	0	-0.041	-0.022	42.455	0.002	0.002	0.000	0.000	0.000
23	A	23	PHE	0	-0.041	-0.023	39.956	0.001	0.001	0.000	0.000	0.000
24	A	24	ARG	1	0.803	0.899	45.196	0.037	0.037	0.000	0.000	0.000
25	A	25	GLU	-1	-0.899	-0.911	47.742	-0.028	-0.028	0.000	0.000	0.000
26	A	26	GLU	-1	-0.909	-0.965	47.182	-0.039	-0.039	0.000	0.000	0.000
27	A	27	SER	0	0.014	-0.001	49.805	0.001	0.001	0.000	0.000	0.000
28	A	28	ARG	1	0.815	0.899	45.861	0.038	0.038	0.000	0.000	0.000
29	A	29	PHE	0	0.006	-0.005	41.913	-0.001	-0.001	0.000	0.000	0.000
30	A	30	CYS	0	-0.022	0.018	45.913	0.000	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.844	-0.914	45.119	-0.034	-0.034	0.000	0.000	0.000
32	A	32	ALA	0	-0.069	-0.045	48.442	0.001	0.001	0.000	0.000	0.000
33	A	33	HIS	0	0.064	0.045	51.047	-0.001	-0.001	0.000	0.000	0.000
34	A	34	LEU	0	-0.026	-0.018	50.483	0.000	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.025	0.009	53.988	0.000	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.011	0.004	54.371	0.000	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.881	-0.937	58.732	-0.017	-0.017	0.000	0.000	0.000
38	A	38	GLY	0	-0.056	-0.029	62.477	0.000	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.904	-0.935	58.819	-0.021	-0.021	0.000	0.000	0.000
40	A	40	GLU	-1	-0.850	-0.915	57.818	-0.020	-0.020	0.000	0.000	0.000
41	A	41	ILE	0	-0.051	-0.025	52.403	0.000	0.000	0.000	0.000	0.000
42	A	42	PRO	0	0.010	0.001	52.159	0.000	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.004	-0.009	47.777	-0.001	-0.001	0.000	0.000	0.000
44	A	44	GLN	0	0.016	0.008	43.000	-0.001	-0.001	0.000	0.000	0.000
45	A	45	LYS	1	0.900	0.953	44.895	0.028	0.028	0.000	0.000	0.000
46	A	46	ASN	0	0.012	-0.006	38.728	0.002	0.002	0.000	0.000	0.000
47	A	47	ILE	0	0.029	0.012	39.804	0.000	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.053	0.025	41.466	0.000	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.002	0.007	42.264	0.001	0.001	0.000	0.000	0.000
50	A	50	ALA	0	-0.035	-0.005	38.056	0.001	0.001	0.000	0.000	0.000
51	A	51	ALA	0	0.000	0.005	39.379	0.000	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.005	-0.015	41.499	0.001	0.001	0.000	0.000	0.000
53	A	53	PRO	0	0.011	-0.004	41.800	0.000	0.000	0.000	0.000	0.000
54	A	54	TYR	0	0.035	0.035	43.897	0.001	0.001	0.000	0.000	0.000
55	A	55	ILE	0	0.034	0.020	46.381	0.001	0.001	0.000	0.000	0.000
56	A	56	ARG	1	0.840	0.908	38.617	0.032	0.032	0.000	0.000	0.000
57	A	57	THR	0	-0.042	-0.022	44.664	0.001	0.001	0.000	0.000	0.000
58	A	58	LYS	1	0.897	0.950	46.940	0.019	0.019	0.000	0.000	0.000
59	A	59	LEU	0	0.012	0.010	44.774	0.000	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.051	-0.025	43.758	0.000	0.000	0.000	0.000	0.000
61	A	61	TYR	0	-0.047	-0.023	47.706	0.001	0.001	0.000	0.000	0.000
62	A	62	ASN	0	-0.020	0.006	51.207	0.002	0.002	0.000	0.000	0.000
63	A	63	PRO	0	0.056	0.109	49.902	-0.001	-0.001	0.000	0.000	0.000
64	A	64	PRO	0	-0.076	-0.041	51.707	0.000	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.800	0.895	55.211	0.019	0.019	0.000	0.000	0.000
66	A	66	ASP	-1	-0.853	-0.934	54.477	-0.021	-0.021	0.000	0.000	0.000
67	A	67	ASP	-1	-0.871	-0.934	57.845	-0.017	-0.017	0.000	0.000	0.000
68	A	68	GLY	0	0.026	0.031	59.457	-0.001	-0.001	0.000	0.000	0.000
69	A	69	SER	0	-0.108	-0.055	56.451	0.000	0.000	0.000	0.000	0.000
70	A	70	THR	0	0.011	0.004	54.976	-0.001	-0.001	0.000	0.000	0.000
71	A	71	TYR	0	-0.065	-0.099	50.084	0.000	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.802	0.880	53.462	0.018	0.018	0.000	0.000	0.000
73	A	73	ILE	0	-0.013	-0.015	49.079	0.000	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.789	-0.905	53.472	-0.019	-0.019	0.000	0.000	0.000
75	A	75	LEU	0	-0.045	-0.046	51.922	0.000	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.864	-0.928	56.466	-0.017	-0.017	0.000	0.000	0.000
77	A	77	GLY	0	-0.022	0.000	58.295	0.000	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.027	-0.024	53.341	0.000	0.000	0.000	0.000	0.000
79	A	79	SER	0	0.060	0.039	57.596	0.000	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.049	0.013	57.243	-0.001	-0.001	0.000	0.000	0.000
81	A	81	MET	0	-0.026	-0.008	56.700	-0.001	-0.001	0.000	0.000	0.000
82	A	82	VAL	0	0.094	0.040	54.215	-0.001	-0.001	0.000	0.000	0.000
83	A	83	MET	0	0.005	0.011	51.836	-0.002	-0.002	0.000	0.000	0.000
84	A	84	ARG	1	0.857	0.905	51.619	0.023	0.023	0.000	0.000	0.000
85	A	85	GLU	-1	-0.812	-0.893	51.355	-0.028	-0.028	0.000	0.000	0.000
86	A	86	ILE	0	-0.030	-0.006	47.953	-0.002	-0.002	0.000	0.000	0.000
87	A	87	LEU	0	-0.039	-0.029	47.203	-0.002	-0.002	0.000	0.000	0.000
88	A	88	ASP	-1	-0.781	-0.881	46.447	-0.034	-0.034	0.000	0.000	0.000
89	A	89	TYR	0	0.004	0.027	41.735	-0.002	-0.002	0.000	0.000	0.000
90	A	90	ILE	0	-0.030	-0.010	42.457	-0.003	-0.003	0.000	0.000	0.000
91	A	91	PHE	0	-0.042	-0.030	41.494	-0.003	-0.003	0.000	0.000	0.000
92	A	92	SER	0	-0.071	-0.065	41.232	-0.002	-0.002	0.000	0.000	0.000
93	A	93	GLY	0	-0.027	-0.010	40.418	-0.003	-0.003	0.000	0.000	0.000
94	A	94	GLN	0	-0.068	-0.030	41.379	0.002	0.002	0.000	0.000	0.000
95	A	95	ILE	0	0.020	0.007	44.587	0.000	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.814	0.902	47.841	0.030	0.030	0.000	0.000	0.000
97	A	97	LEU	0	-0.020	-0.006	50.404	0.001	0.001	0.000	0.000	0.000
98	A	98	ASN	0	0.002	0.011	53.494	-0.001	-0.001	0.000	0.000	0.000
99	A	99	GLU	-1	-0.909	-0.964	57.119	-0.017	-0.017	0.000	0.000	0.000
100	A	100	ASP	-1	-0.910	-0.959	59.519	-0.019	-0.019	0.000	0.000	0.000
101	A	101	THR	0	-0.004	0.004	55.468	0.000	0.000	0.000	0.000	0.000
102	A	102	ILE	0	0.013	0.009	51.639	0.000	0.000	0.000	0.000	0.000
103	A	103	GLN	0	0.032	-0.004	54.488	-0.001	-0.001	0.000	0.000	0.000
104	A	104	ASP	-1	-0.886	-0.940	56.374	-0.017	-0.017	0.000	0.000	0.000
105	A	105	VAL	0	-0.020	-0.016	50.925	0.000	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.011	-0.002	51.394	-0.001	-0.001	0.000	0.000	0.000
107	A	107	GLN	0	-0.016	-0.005	52.168	0.000	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.027	0.012	52.851	0.000	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.010	-0.018	48.092	0.000	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.912	-0.934	48.658	-0.018	-0.018	0.000	0.000	0.000
111	A	111	LEU	0	0.034	0.028	50.370	0.000	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.048	-0.028	48.228	0.000	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.011	0.001	45.755	-0.001	-0.001	0.000	0.000	0.000
114	A	114	LEU	0	-0.035	-0.004	44.192	-0.001	-0.001	0.000	0.000	0.000
115	A	115	THR	0	0.008	-0.016	41.158	0.001	0.001	0.000	0.000	0.000
116	A	116	ASP	-1	-0.877	-0.950	39.098	-0.032	-0.032	0.000	0.000	0.000
117	A	117	LEU	0	-0.019	0.010	42.119	0.000	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.913	0.934	44.954	0.019	0.019	0.000	0.000	0.000
119	A	119	THR	0	-0.026	-0.018	42.605	0.002	0.002	0.000	0.000	0.000
120	A	120	LEU	0	-0.009	0.001	42.732	0.000	0.000	0.000	0.000	0.000
121	A	121	CYS	0	-0.048	-0.022	45.259	0.000	0.000	0.000	0.000	0.000
122	A	122	CYS	0	-0.029	-0.035	48.524	0.001	0.001	0.000	0.000	0.000
123	A	123	GLU	-1	-0.980	-0.970	43.995	-0.026	-0.026	0.000	0.000	0.000
124	A	124	PHE	0	-0.071	-0.029	46.059	0.000	0.000	0.000	0.000	0.000
125	A	125	LEU	0	-0.032	0.002	50.846	0.001	0.001	0.000	0.000	0.000

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