FMO DATABASE

FMODB ID: 14Y1Z

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	OptHSide
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	-1440381.759963
FMO2-HF: Nuclear repulsion	1382199.778341
FMO2-HF: Total energy	-58181.981622
FMO2-MP2: Total energy	-58353.075328

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.
-2.28	-0.399	6.684	-2.352	-6.212	-0.005

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 : 0.039 / q_NPA : 0.035

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	0.016	2.338	-1.753	0.011	6.680	-2.321	-6.123	-0.005
4	A	9	PHE	0	-0.002	-0.006	4.845	-0.959	-0.842	0.004	-0.031	-0.089	0.000
5	A	10	ASN	0	0.019	0.017	7.548	-0.355	-0.355	0.000	0.000	0.000	0.000
6	A	11	LYS	1	0.924	0.981	7.504	0.308	0.308	0.000	0.000	0.000	0.000
7	A	12	ASN	0	-0.025	-0.012	6.236	0.162	0.162	0.000	0.000	0.000	0.000
8	A	13	LEU	0	-0.022	-0.008	9.357	-0.050	-0.050	0.000	0.000	0.000	0.000
9	A	14	LYS	1	0.968	0.986	6.935	0.472	0.472	0.000	0.000	0.000	0.000
10	A	15	VAL	0	-0.003	0.000	11.107	0.043	0.043	0.000	0.000	0.000	0.000
11	A	16	LEU	0	-0.027	-0.017	12.396	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	17	ALA	0	0.010	0.019	15.959	0.005	0.005	0.000	0.000	0.000	0.000
13	A	18	PRO	0	0.027	0.026	19.466	0.008	0.008	0.000	0.000	0.000	0.000
14	A	19	CYS	0	0.027	0.007	21.829	0.006	0.006	0.000	0.000	0.000	0.000
15	A	20	ASP	-1	-0.768	-0.855	23.319	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	21	GLY	0	0.014	-0.012	25.181	0.000	0.000	0.000	0.000	0.000	0.000
17	A	22	THR	0	-0.081	-0.049	25.137	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	23	ILE	0	-0.007	0.006	21.004	0.000	0.000	0.000	0.000	0.000	0.000
19	A	24	ILE	0	-0.018	-0.014	24.461	0.003	0.003	0.000	0.000	0.000	0.000
20	A	25	THR	0	-0.031	-0.064	26.044	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	26	LEU	0	0.027	0.012	26.515	0.002	0.002	0.000	0.000	0.000	0.000
22	A	27	ASP	-1	-0.781	-0.862	29.324	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	28	GLU	-1	-0.884	-0.907	29.632	-0.022	-0.022	0.000	0.000	0.000	0.000
24	A	29	VAL	0	-0.030	-0.008	30.337	0.001	0.001	0.000	0.000	0.000	0.000
25	A	30	GLU	-1	-0.787	-0.872	33.439	-0.015	-0.015	0.000	0.000	0.000	0.000
26	A	31	ASP	-1	-0.845	-0.957	35.248	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	32	GLU	-1	-0.924	-0.971	35.441	-0.016	-0.016	0.000	0.000	0.000	0.000
28	A	33	VAL	0	0.048	0.028	33.401	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	34	PHE	0	-0.045	-0.036	29.822	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	35	LYS	1	0.834	0.927	31.167	0.013	0.013	0.000	0.000	0.000	0.000
31	A	36	GLU	-1	-0.880	-0.944	32.691	-0.016	-0.016	0.000	0.000	0.000	0.000
32	A	37	ARG	1	0.719	0.830	27.093	0.033	0.033	0.000	0.000	0.000	0.000
33	A	38	MET	0	-0.023	0.017	30.887	0.000	0.000	0.000	0.000	0.000	0.000
34	A	39	LEU	0	-0.019	-0.014	30.256	0.000	0.000	0.000	0.000	0.000	0.000
35	A	40	GLY	0	-0.023	-0.009	26.859	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	41	ASP	-1	-0.845	-0.906	23.960	-0.045	-0.045	0.000	0.000	0.000	0.000
37	A	42	GLY	0	-0.035	-0.025	22.195	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	43	PHE	0	-0.021	-0.013	19.150	0.000	0.000	0.000	0.000	0.000	0.000
39	A	44	ALA	0	0.040	0.022	24.473	0.002	0.002	0.000	0.000	0.000	0.000
40	A	45	ILE	0	0.004	-0.004	23.242	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	46	ASN	0	0.008	0.022	26.638	0.004	0.004	0.000	0.000	0.000	0.000
42	A	47	PRO	0	-0.012	-0.002	28.210	0.001	0.001	0.000	0.000	0.000	0.000
43	A	48	LYS	1	0.859	0.921	28.028	0.011	0.011	0.000	0.000	0.000	0.000
44	A	49	SER	0	-0.033	-0.003	27.139	0.002	0.002	0.000	0.000	0.000	0.000
45	A	50	ASN	0	0.007	-0.011	29.487	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	51	ASP	-1	-0.849	-0.919	26.925	0.002	0.002	0.000	0.000	0.000	0.000
47	A	52	PHE	0	0.067	0.038	25.371	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	53	HIS	0	-0.055	-0.050	20.985	0.004	0.004	0.000	0.000	0.000	0.000
49	A	54	ALA	0	0.021	0.006	19.560	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	55	PRO	0	0.020	0.026	17.841	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	56	VAL	0	0.024	-0.012	14.638	-0.029	-0.029	0.000	0.000	0.000	0.000
52	A	57	SER	0	0.014	0.013	14.637	0.014	0.014	0.000	0.000	0.000	0.000
53	A	58	GLY	0	-0.028	-0.032	16.334	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	59	LYS	1	0.871	0.955	19.013	0.031	0.031	0.000	0.000	0.000	0.000
55	A	60	LEU	0	0.013	0.016	22.765	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	61	VAL	0	-0.007	-0.006	24.932	0.004	0.004	0.000	0.000	0.000	0.000
57	A	62	THR	0	-0.005	0.022	27.066	0.003	0.003	0.000	0.000	0.000	0.000
58	A	63	ALA	0	0.048	0.031	28.647	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	64	PHE	0	0.035	0.008	30.868	0.000	0.000	0.000	0.000	0.000	0.000
60	A	65	PRO	0	0.013	0.012	34.420	0.000	0.000	0.000	0.000	0.000	0.000
61	A	66	THR	0	0.035	-0.017	36.109	0.001	0.001	0.000	0.000	0.000	0.000
62	A	67	LYS	1	0.781	0.888	33.058	0.006	0.006	0.000	0.000	0.000	0.000
63	A	68	HIS	0	0.090	0.075	32.565	0.001	0.001	0.000	0.000	0.000	0.000
64	A	69	ALA	0	-0.019	-0.008	29.762	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	70	PHE	0	-0.025	-0.021	26.022	0.002	0.002	0.000	0.000	0.000	0.000
66	A	71	GLY	0	0.016	0.002	25.340	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	72	ILE	0	-0.017	-0.005	19.612	0.002	0.002	0.000	0.000	0.000	0.000
68	A	73	GLN	0	-0.029	-0.016	21.237	-0.005	-0.005	0.000	0.000	0.000	0.000
69	A	74	THR	0	0.021	0.031	15.805	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	75	LYS	1	1.012	0.982	13.574	0.063	0.063	0.000	0.000	0.000	0.000
71	A	76	SER	0	-0.077	-0.042	15.463	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	77	GLY	0	-0.008	0.004	17.421	0.004	0.004	0.000	0.000	0.000	0.000
73	A	78	VAL	0	-0.050	-0.029	17.058	0.002	0.002	0.000	0.000	0.000	0.000
74	A	79	GLU	-1	-0.872	-0.932	19.981	-0.041	-0.041	0.000	0.000	0.000	0.000
75	A	80	ILE	0	-0.046	-0.024	18.610	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	81	LEU	0	0.005	-0.008	21.937	0.004	0.004	0.000	0.000	0.000	0.000
77	A	82	LEU	0	0.003	0.013	23.771	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	83	HIS	0	-0.015	-0.016	25.521	0.005	0.005	0.000	0.000	0.000	0.000
79	A	84	ILE	0	-0.002	-0.003	28.635	0.000	0.000	0.000	0.000	0.000	0.000
80	A	85	GLY	0	-0.014	-0.013	30.731	0.002	0.002	0.000	0.000	0.000	0.000
81	A	86	LEU	0	0.012	0.014	33.085	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	87	ASP	-1	-0.842	-0.949	35.816	-0.009	-0.009	0.000	0.000	0.000	0.000
83	A	88	THR	0	-0.045	-0.007	34.339	0.001	0.001	0.000	0.000	0.000	0.000
84	A	89	VAL	0	-0.015	0.009	37.424	0.001	0.001	0.000	0.000	0.000	0.000
85	A	90	SER	0	0.005	-0.020	38.580	0.001	0.001	0.000	0.000	0.000	0.000
86	A	91	LEU	0	-0.095	-0.044	38.727	0.001	0.001	0.000	0.000	0.000	0.000
87	A	92	ASP	-1	-0.890	-0.951	41.220	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	93	GLY	0	0.026	0.017	37.994	0.000	0.000	0.000	0.000	0.000	0.000
89	A	94	ASN	0	-0.111	-0.058	38.971	0.001	0.001	0.000	0.000	0.000	0.000
90	A	95	GLY	0	0.044	0.008	38.677	0.000	0.000	0.000	0.000	0.000	0.000
91	A	96	PHE	0	0.003	0.015	33.056	0.000	0.000	0.000	0.000	0.000	0.000
92	A	97	GLU	-1	-0.897	-0.931	34.096	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	98	SER	0	0.005	-0.002	31.383	0.000	0.000	0.000	0.000	0.000	0.000
94	A	99	PHE	0	-0.028	-0.030	28.483	0.002	0.002	0.000	0.000	0.000	0.000
95	A	100	VAL	0	-0.059	-0.016	25.728	0.001	0.001	0.000	0.000	0.000	0.000
96	A	101	THR	0	-0.012	-0.001	29.058	0.000	0.000	0.000	0.000	0.000	0.000
97	A	102	GLN	0	0.005	-0.031	28.921	0.000	0.000	0.000	0.000	0.000	0.000
98	A	103	ASP	-1	-0.892	-0.955	27.810	-0.017	-0.017	0.000	0.000	0.000	0.000
99	A	104	GLN	0	0.026	0.032	25.289	0.000	0.000	0.000	0.000	0.000	0.000
100	A	105	GLU	-1	-0.954	-0.974	19.539	-0.031	-0.031	0.000	0.000	0.000	0.000
101	A	106	VAL	0	-0.071	-0.039	20.180	0.005	0.005	0.000	0.000	0.000	0.000
102	A	107	ASN	0	-0.009	-0.025	16.259	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	108	ALA	0	-0.026	0.001	14.324	0.001	0.001	0.000	0.000	0.000	0.000
104	A	109	GLY	0	0.034	0.003	16.294	0.012	0.012	0.000	0.000	0.000	0.000
105	A	110	ASP	-1	-0.858	-0.902	18.323	0.013	0.013	0.000	0.000	0.000	0.000
106	A	111	LYS	1	0.789	0.917	21.227	-0.010	-0.010	0.000	0.000	0.000	0.000
107	A	112	LEU	0	-0.033	-0.021	23.286	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	113	VAL	0	0.009	-0.010	26.327	0.002	0.002	0.000	0.000	0.000	0.000
109	A	114	THR	0	-0.034	-0.019	28.993	0.000	0.000	0.000	0.000	0.000	0.000
110	A	115	VAL	0	0.016	0.009	31.236	0.000	0.000	0.000	0.000	0.000	0.000
111	A	116	ASP	-1	-0.835	-0.874	33.714	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	117	LEU	0	0.065	0.001	32.178	0.000	0.000	0.000	0.000	0.000	0.000
113	A	118	LYS	1	0.924	0.976	35.949	0.000	0.000	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.090	-0.078	39.317	0.000	0.000	0.000	0.000	0.000	0.000
115	A	120	VAL	0	0.007	-0.014	36.295	0.000	0.000	0.000	0.000	0.000	0.000
116	A	121	ALA	0	0.011	0.003	37.844	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.869	0.936	39.219	0.003	0.003	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.836	0.934	41.615	0.004	0.004	0.000	0.000	0.000	0.000
119	A	124	VAL	0	-0.013	0.010	37.476	0.000	0.000	0.000	0.000	0.000	0.000
120	A	125	PRO	0	0.030	0.028	39.378	0.000	0.000	0.000	0.000	0.000	0.000
121	A	126	SER	0	0.002	-0.015	35.358	0.000	0.000	0.000	0.000	0.000	0.000
122	A	127	ILE	0	0.034	0.017	33.573	0.000	0.000	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.771	0.867	31.120	0.015	0.015	0.000	0.000	0.000	0.000
124	A	129	SER	0	-0.022	-0.018	27.846	0.001	0.001	0.000	0.000	0.000	0.000
125	A	130	PRO	0	-0.002	0.013	27.142	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	131	ILE	0	-0.035	-0.017	20.861	0.000	0.000	0.000	0.000	0.000	0.000
127	A	132	ILE	0	0.033	0.016	23.641	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	133	PHE	0	-0.005	-0.021	17.369	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	134	THR	0	0.020	0.016	22.792	0.004	0.004	0.000	0.000	0.000	0.000
130	A	135	ASN	0	-0.003	-0.012	23.450	0.005	0.005	0.000	0.000	0.000	0.000
131	A	136	ASN	0	0.083	0.054	19.928	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	137	GLY	0	0.035	0.029	20.235	0.000	0.000	0.000	0.000	0.000	0.000
133	A	138	GLY	0	-0.028	-0.016	17.130	0.008	0.008	0.000	0.000	0.000	0.000
134	A	139	LYS	1	0.890	0.936	17.732	0.022	0.022	0.000	0.000	0.000	0.000
135	A	140	THR	0	-0.029	-0.003	16.719	0.010	0.010	0.000	0.000	0.000	0.000
136	A	141	LEU	0	0.067	0.013	16.834	-0.023	-0.023	0.000	0.000	0.000	0.000
137	A	142	GLU	-1	-0.932	-0.964	12.361	-0.157	-0.157	0.000	0.000	0.000	0.000
138	A	143	ILE	0	-0.009	-0.020	12.509	0.013	0.013	0.000	0.000	0.000	0.000
139	A	144	VAL	0	0.046	0.031	15.886	-0.024	-0.024	0.000	0.000	0.000	0.000
140	A	145	LYS	1	0.851	0.948	16.213	0.073	0.073	0.000	0.000	0.000	0.000
141	A	146	MET	0	0.011	0.012	18.405	0.003	0.003	0.000	0.000	0.000	0.000
142	A	147	GLY	0	0.012	0.010	22.062	0.002	0.002	0.000	0.000	0.000	0.000
143	A	148	GLU	-1	-0.807	-0.885	24.114	-0.013	-0.013	0.000	0.000	0.000	0.000
144	A	149	VAL	0	-0.084	-0.043	20.173	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	150	LYS	1	0.830	0.895	20.133	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	151	GLN	0	0.007	-0.007	19.601	-0.013	-0.013	0.000	0.000	0.000	0.000
147	A	152	GLY	0	0.022	0.006	16.891	0.010	0.010	0.000	0.000	0.000	0.000
148	A	153	ASP	-1	-0.890	-0.929	15.217	-0.025	-0.025	0.000	0.000	0.000	0.000
149	A	154	VAL	0	-0.072	-0.064	10.496	-0.023	-0.023	0.000	0.000	0.000	0.000
150	A	155	VAL	0	0.027	0.002	13.886	0.017	0.017	0.000	0.000	0.000	0.000
151	A	156	ALA	0	0.041	0.009	14.739	0.016	0.016	0.000	0.000	0.000	0.000
152	A	157	ILE	0	-0.057	-0.003	9.769	-0.058	-0.058	0.000	0.000	0.000	0.000
153	A	158	LEU	0	0.018	0.036	13.152	0.048	0.048	0.000	0.000	0.000	0.000
154	A	159	LYS	1	0.873	0.934	9.776	0.074	0.074	0.000	0.000	0.000	0.000

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