FMO DATABASE

FMODB ID: GNR31

Calculation Name: 2GPR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2GPR

Chain ID: A

ChEMBL ID:

UniProt ID: P45618

Base Structure: X-ray

Registration Date: 2023-03-13

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	154
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1438467.413415
FMO2-HF: Nuclear repulsion	1380284.003445
FMO2-HF: Total energy	-58183.40997
FMO2-MP2: Total energy	-58354.411372

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:6:MET)

Summations of interaction energy for fragment #1(A:6:MET)

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.
-2.81	1.06	2.956	-2.014	-4.812	-0.003

Interaction energy analysis for fragmet #1(A:6:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.029

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	8	PHE	0	0.045	0.014	2.438	-2.466	1.328	2.955	-1.994	-4.755	-0.003
4	A	9	PHE	0	-0.014	-0.009	5.135	-0.813	-0.737	0.001	-0.020	-0.057	0.000
5	A	10	ASN	0	0.004	-0.002	7.759	-0.342	-0.342	0.000	0.000	0.000	0.000
6	A	11	LYS	1	0.893	0.952	7.315	0.310	0.310	0.000	0.000	0.000	0.000
7	A	12	ASN	0	0.002	0.010	5.687	0.263	0.263	0.000	0.000	0.000	0.000
8	A	13	LEU	0	0.002	0.001	9.008	0.000	0.000	0.000	0.000	0.000	0.000
9	A	14	LYS	1	0.942	0.985	6.916	0.263	0.263	0.000	0.000	0.000	0.000
10	A	15	VAL	0	0.016	0.017	10.653	0.051	0.051	0.000	0.000	0.000	0.000
11	A	16	LEU	0	-0.044	-0.026	12.297	-0.016	-0.016	0.000	0.000	0.000	0.000
12	A	17	ALA	0	0.019	0.012	15.885	0.001	0.001	0.000	0.000	0.000	0.000
13	A	18	PRO	0	0.009	0.023	19.376	0.012	0.012	0.000	0.000	0.000	0.000
14	A	19	CYS	0	0.005	-0.006	21.493	0.007	0.007	0.000	0.000	0.000	0.000
15	A	20	ASP	-1	-0.770	-0.863	23.205	0.021	0.021	0.000	0.000	0.000	0.000
16	A	21	GLY	0	0.027	-0.007	24.975	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	22	THR	0	-0.070	-0.048	25.330	0.001	0.001	0.000	0.000	0.000	0.000
18	A	23	ILE	0	-0.033	-0.006	20.573	0.001	0.001	0.000	0.000	0.000	0.000
19	A	24	ILE	0	0.001	-0.005	23.996	0.001	0.001	0.000	0.000	0.000	0.000
20	A	25	THR	0	-0.025	-0.055	25.553	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	26	LEU	0	0.006	0.003	26.108	0.003	0.003	0.000	0.000	0.000	0.000
22	A	27	ASP	-1	-0.778	-0.869	28.649	-0.030	-0.030	0.000	0.000	0.000	0.000
23	A	28	GLU	-1	-0.854	-0.888	29.199	-0.024	-0.024	0.000	0.000	0.000	0.000
24	A	29	VAL	0	-0.026	-0.003	30.216	0.003	0.003	0.000	0.000	0.000	0.000
25	A	30	GLU	-1	-0.808	-0.873	33.313	-0.011	-0.011	0.000	0.000	0.000	0.000
26	A	31	ASP	-1	-0.847	-0.942	34.777	-0.011	-0.011	0.000	0.000	0.000	0.000
27	A	32	GLU	-1	-0.913	-0.971	35.235	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	33	VAL	0	0.036	0.018	32.938	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	34	PHE	0	-0.017	-0.026	29.092	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	35	LYS	1	0.821	0.925	30.669	0.012	0.012	0.000	0.000	0.000	0.000
31	A	36	GLU	-1	-0.884	-0.951	32.098	-0.017	-0.017	0.000	0.000	0.000	0.000
32	A	37	ARG	1	0.739	0.833	26.639	0.038	0.038	0.000	0.000	0.000	0.000
33	A	38	MET	0	-0.018	0.015	30.285	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	39	LEU	0	-0.008	0.002	30.104	0.001	0.001	0.000	0.000	0.000	0.000
35	A	40	GLY	0	-0.021	-0.019	26.284	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	41	ASP	-1	-0.817	-0.889	23.978	-0.054	-0.054	0.000	0.000	0.000	0.000
37	A	42	GLY	0	-0.047	-0.040	21.947	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	43	PHE	0	-0.025	-0.010	18.829	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	44	ALA	0	0.056	0.027	23.967	0.004	0.004	0.000	0.000	0.000	0.000
40	A	45	ILE	0	-0.027	-0.011	22.972	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	46	ASN	0	0.024	0.009	26.068	0.004	0.004	0.000	0.000	0.000	0.000
42	A	47	PRO	0	-0.007	0.005	27.989	0.001	0.001	0.000	0.000	0.000	0.000
43	A	48	LYS	1	0.806	0.897	27.927	0.002	0.002	0.000	0.000	0.000	0.000
44	A	49	SER	0	-0.040	0.000	26.833	0.002	0.002	0.000	0.000	0.000	0.000
45	A	50	ASN	0	0.019	-0.002	29.200	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	51	ASP	-1	-0.850	-0.901	26.965	0.026	0.026	0.000	0.000	0.000	0.000
47	A	52	PHE	0	0.046	0.010	25.122	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	53	HIS	0	-0.048	-0.046	20.788	0.002	0.002	0.000	0.000	0.000	0.000
49	A	54	ALA	0	0.039	0.018	19.268	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	55	PRO	0	0.001	0.014	17.637	0.004	0.004	0.000	0.000	0.000	0.000
51	A	56	VAL	0	0.021	-0.011	14.421	-0.030	-0.030	0.000	0.000	0.000	0.000
52	A	57	SER	0	-0.003	-0.005	13.704	0.013	0.013	0.000	0.000	0.000	0.000
53	A	58	GLY	0	-0.055	-0.030	15.513	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	59	LYS	1	0.889	0.963	18.240	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	60	LEU	0	-0.010	0.007	21.998	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	61	VAL	0	0.000	-0.006	24.595	0.002	0.002	0.000	0.000	0.000	0.000
57	A	62	THR	0	-0.008	0.018	26.671	0.000	0.000	0.000	0.000	0.000	0.000
58	A	63	ALA	0	0.044	0.021	28.083	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	64	PHE	0	0.033	0.016	30.562	0.000	0.000	0.000	0.000	0.000	0.000
60	A	65	PRO	0	0.012	0.009	34.216	0.001	0.001	0.000	0.000	0.000	0.000
61	A	66	THR	0	0.008	-0.034	35.692	0.001	0.001	0.000	0.000	0.000	0.000
62	A	67	LYS	1	0.798	0.893	33.072	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	68	HIS	0	0.074	0.069	32.393	0.002	0.002	0.000	0.000	0.000	0.000
64	A	69	ALA	0	-0.022	-0.013	29.304	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	70	PHE	0	-0.005	-0.010	25.789	0.003	0.003	0.000	0.000	0.000	0.000
66	A	71	GLY	0	0.001	0.001	24.566	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	72	ILE	0	-0.034	-0.019	19.284	0.005	0.005	0.000	0.000	0.000	0.000
68	A	73	GLN	0	-0.002	-0.012	20.681	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	74	THR	0	-0.009	-0.012	15.458	0.004	0.004	0.000	0.000	0.000	0.000
70	A	75	LYS	1	0.873	0.901	14.218	-0.045	-0.045	0.000	0.000	0.000	0.000
71	A	76	SER	0	-0.071	-0.034	14.456	0.001	0.001	0.000	0.000	0.000	0.000
72	A	77	GLY	0	-0.003	0.005	16.415	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	78	VAL	0	-0.049	-0.009	16.462	0.000	0.000	0.000	0.000	0.000	0.000
74	A	79	GLU	-1	-0.867	-0.919	19.249	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	80	ILE	0	-0.033	-0.012	18.217	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	81	LEU	0	0.010	0.003	21.386	0.008	0.008	0.000	0.000	0.000	0.000
77	A	82	LEU	0	-0.002	0.005	23.344	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	83	HIS	0	0.000	-0.022	25.133	0.005	0.005	0.000	0.000	0.000	0.000
79	A	84	ILE	0	0.006	0.005	27.954	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	85	GLY	0	0.002	0.011	30.334	0.002	0.002	0.000	0.000	0.000	0.000
81	A	86	LEU	0	-0.012	0.001	32.750	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	87	ASP	-1	-0.855	-0.949	35.367	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	88	THR	0	-0.052	-0.026	33.916	0.001	0.001	0.000	0.000	0.000	0.000
84	A	89	VAL	0	-0.021	0.002	36.666	0.001	0.001	0.000	0.000	0.000	0.000
85	A	90	SER	0	-0.026	-0.025	37.864	0.001	0.001	0.000	0.000	0.000	0.000
86	A	91	LEU	0	-0.024	-0.014	38.260	0.001	0.001	0.000	0.000	0.000	0.000
87	A	92	ASP	-1	-0.896	-0.945	40.476	0.005	0.005	0.000	0.000	0.000	0.000
88	A	93	GLY	0	0.024	0.020	37.461	0.001	0.001	0.000	0.000	0.000	0.000
89	A	94	ASN	0	-0.050	-0.027	38.498	0.001	0.001	0.000	0.000	0.000	0.000
90	A	95	GLY	0	0.009	-0.009	38.548	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	96	PHE	0	-0.007	0.011	32.785	0.000	0.000	0.000	0.000	0.000	0.000
92	A	97	GLU	-1	-0.869	-0.930	33.819	0.017	0.017	0.000	0.000	0.000	0.000
93	A	98	SER	0	0.006	0.003	30.683	0.000	0.000	0.000	0.000	0.000	0.000
94	A	99	PHE	0	-0.041	-0.035	28.002	0.001	0.001	0.000	0.000	0.000	0.000
95	A	100	VAL	0	-0.033	-0.005	25.171	0.003	0.003	0.000	0.000	0.000	0.000
96	A	101	THR	0	-0.016	-0.009	28.397	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	102	GLN	0	-0.009	-0.019	28.120	0.001	0.001	0.000	0.000	0.000	0.000
98	A	103	ASP	-1	-0.872	-0.951	26.846	0.015	0.015	0.000	0.000	0.000	0.000
99	A	104	GLN	0	0.032	0.034	24.576	0.000	0.000	0.000	0.000	0.000	0.000
100	A	105	GLU	-1	-0.847	-0.921	18.861	0.041	0.041	0.000	0.000	0.000	0.000
101	A	106	VAL	0	-0.016	0.000	19.997	0.005	0.005	0.000	0.000	0.000	0.000
102	A	107	ASN	0	-0.015	-0.028	15.425	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	108	ALA	0	-0.023	-0.005	13.476	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	109	GLY	0	0.034	0.021	15.487	0.023	0.023	0.000	0.000	0.000	0.000
105	A	110	ASP	-1	-0.832	-0.895	18.077	0.073	0.073	0.000	0.000	0.000	0.000
106	A	111	LYS	1	0.768	0.891	20.905	-0.042	-0.042	0.000	0.000	0.000	0.000
107	A	112	LEU	0	0.015	0.011	22.933	0.001	0.001	0.000	0.000	0.000	0.000
108	A	113	VAL	0	-0.010	-0.011	25.856	0.000	0.000	0.000	0.000	0.000	0.000
109	A	114	THR	0	-0.036	-0.021	28.388	0.002	0.002	0.000	0.000	0.000	0.000
110	A	115	VAL	0	0.005	0.002	31.053	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	116	ASP	-1	-0.802	-0.872	33.496	0.010	0.010	0.000	0.000	0.000	0.000
112	A	117	LEU	0	0.061	0.013	31.668	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	118	LYS	1	0.916	0.977	35.902	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.088	-0.083	39.395	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	120	VAL	0	0.014	-0.005	36.070	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	121	ALA	0	0.006	0.001	37.878	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.877	0.953	39.267	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.785	0.888	41.061	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	124	VAL	0	0.028	0.029	37.428	0.000	0.000	0.000	0.000	0.000	0.000
120	A	125	PRO	0	0.014	0.008	39.184	0.000	0.000	0.000	0.000	0.000	0.000
121	A	126	SER	0	-0.012	-0.021	35.275	0.000	0.000	0.000	0.000	0.000	0.000
122	A	127	ILE	0	0.020	0.006	33.652	0.001	0.001	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.795	0.877	30.890	0.013	0.013	0.000	0.000	0.000	0.000
124	A	129	SER	0	-0.009	-0.004	27.777	0.002	0.002	0.000	0.000	0.000	0.000
125	A	130	PRO	0	-0.005	0.006	26.776	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	131	ILE	0	-0.031	-0.009	20.753	0.003	0.003	0.000	0.000	0.000	0.000
127	A	132	ILE	0	0.020	0.021	23.121	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	133	PHE	0	-0.001	-0.020	16.698	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	134	THR	0	0.018	0.008	22.157	0.000	0.000	0.000	0.000	0.000	0.000
130	A	135	ASN	0	-0.017	-0.006	22.680	0.002	0.002	0.000	0.000	0.000	0.000
131	A	136	ASN	0	0.009	-0.001	19.488	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	137	GLY	0	0.044	0.031	18.934	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	138	GLY	0	-0.007	-0.005	16.872	0.006	0.006	0.000	0.000	0.000	0.000
134	A	139	LYS	1	0.863	0.929	17.421	0.021	0.021	0.000	0.000	0.000	0.000
135	A	140	THR	0	0.032	-0.002	16.413	0.016	0.016	0.000	0.000	0.000	0.000
136	A	141	LEU	0	0.008	0.009	15.993	-0.034	-0.034	0.000	0.000	0.000	0.000
137	A	142	GLU	-1	-0.818	-0.871	11.855	-0.277	-0.277	0.000	0.000	0.000	0.000
138	A	143	ILE	0	-0.008	-0.012	11.892	0.007	0.007	0.000	0.000	0.000	0.000
139	A	144	VAL	0	0.036	0.007	15.593	-0.016	-0.016	0.000	0.000	0.000	0.000
140	A	145	LYS	1	0.779	0.898	16.326	0.048	0.048	0.000	0.000	0.000	0.000
141	A	146	MET	0	0.011	0.008	18.271	0.009	0.009	0.000	0.000	0.000	0.000
142	A	147	GLY	0	0.008	0.013	21.858	0.001	0.001	0.000	0.000	0.000	0.000
143	A	148	GLU	-1	-0.806	-0.884	23.718	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	149	VAL	0	-0.055	-0.025	19.926	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	150	LYS	1	0.844	0.896	20.190	-0.026	-0.026	0.000	0.000	0.000	0.000
146	A	151	GLN	0	0.010	-0.002	19.993	-0.010	-0.010	0.000	0.000	0.000	0.000
147	A	152	GLY	0	0.028	0.017	16.991	0.015	0.015	0.000	0.000	0.000	0.000
148	A	153	ASP	-1	-0.803	-0.897	15.310	-0.004	-0.004	0.000	0.000	0.000	0.000
149	A	154	VAL	0	-0.059	-0.036	10.406	-0.022	-0.022	0.000	0.000	0.000	0.000
150	A	155	VAL	0	0.002	0.008	13.647	0.005	0.005	0.000	0.000	0.000	0.000
151	A	156	ALA	0	0.014	0.013	14.726	0.007	0.007	0.000	0.000	0.000	0.000
152	A	157	ILE	0	-0.038	-0.014	9.150	-0.065	-0.065	0.000	0.000	0.000	0.000
153	A	158	LEU	0	0.035	0.032	12.476	0.037	0.037	0.000	0.000	0.000	0.000
154	A	159	LYS	1	0.788	0.865	9.246	0.272	0.272	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:MET)