FMO DATABASE

FMODB ID: MNQGZ

Calculation Name: 1RL2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1RL2

Chain ID: A

ChEMBL ID:

UniProt ID: P04257

Base Structure: X-ray

Registration Date: 2023-09-24

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	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	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1159718.391568
FMO2-HF: Nuclear repulsion	1108537.666584
FMO2-HF: Total energy	-51180.724983
FMO2-MP2: Total energy	-51330.494188

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:60:GLN)

Summations of interaction energy for fragment #1(A:60:GLN)

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.
-31.92	-39.63	30.282	-13.513	-9.058	-0.049

Interaction energy analysis for fragmet #1(A:60:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.034 / 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	62	ARG	1	1.018	1.002	3.815	-6.842	-2.644	-0.088	-2.336	-1.773	-0.005
4	A	63	ILE	0	-0.020	0.008	7.274	-0.312	-0.312	0.000	0.000	0.000	0.000
5	A	64	ILE	0	0.004	0.017	7.522	0.090	0.090	0.000	0.000	0.000	0.000
6	A	65	ASP	-1	-0.783	-0.869	10.413	0.189	0.189	0.000	0.000	0.000	0.000
7	A	66	PHE	0	-0.034	-0.038	13.096	-0.096	-0.096	0.000	0.000	0.000	0.000
8	A	67	LYS	1	0.967	0.973	16.034	-0.233	-0.233	0.000	0.000	0.000	0.000
9	A	68	ARG	1	0.793	0.895	14.676	0.126	0.126	0.000	0.000	0.000	0.000
10	A	69	ASP	-1	-0.818	-0.916	17.714	0.173	0.173	0.000	0.000	0.000	0.000
11	A	70	LYS	1	0.780	0.888	15.748	-0.263	-0.263	0.000	0.000	0.000	0.000
12	A	71	ASP	-1	-0.723	-0.828	19.613	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	72	GLY	0	0.000	0.009	22.665	0.019	0.019	0.000	0.000	0.000	0.000
14	A	73	ILE	0	-0.053	-0.019	19.109	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	74	PRO	0	0.021	0.025	19.068	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	75	GLY	0	0.041	0.018	15.324	0.053	0.053	0.000	0.000	0.000	0.000
17	A	76	ARG	1	0.951	0.983	13.262	0.516	0.516	0.000	0.000	0.000	0.000
18	A	77	VAL	0	-0.013	-0.008	10.393	0.016	0.016	0.000	0.000	0.000	0.000
19	A	78	ALA	0	-0.048	-0.024	8.181	-0.061	-0.061	0.000	0.000	0.000	0.000
20	A	79	THR	0	-0.022	-0.038	4.530	0.502	0.573	-0.001	-0.002	-0.068	0.000
21	A	80	ILE	0	-0.019	-0.012	7.232	0.341	0.341	0.000	0.000	0.000	0.000
22	A	81	GLU	-1	-0.801	-0.879	1.757	-16.456	-23.109	16.510	-6.210	-3.648	-0.066
23	A	82	TYR	0	0.022	0.009	6.397	0.443	0.443	0.000	0.000	0.000	0.000
24	A	83	ASP	-1	-0.808	-0.902	5.631	-1.893	-1.893	0.000	0.000	0.000	0.000
25	A	84	PRO	0	0.049	0.008	7.040	0.378	0.378	0.000	0.000	0.000	0.000
26	A	85	ASN	0	-0.047	-0.011	8.984	0.304	0.304	0.000	0.000	0.000	0.000
27	A	86	ARG	1	0.804	0.884	7.133	0.860	0.860	0.000	0.000	0.000	0.000
28	A	87	SER	0	-0.058	-0.013	11.148	0.098	0.098	0.000	0.000	0.000	0.000
29	A	88	ALA	0	0.000	-0.006	10.520	0.124	0.124	0.000	0.000	0.000	0.000
30	A	89	ASN	0	0.009	0.012	8.872	-0.410	-0.410	0.000	0.000	0.000	0.000
31	A	90	ILE	0	-0.022	-0.005	3.736	0.377	0.530	0.002	-0.027	-0.128	0.000
32	A	91	ALA	0	0.002	-0.009	6.090	-0.713	-0.713	0.000	0.000	0.000	0.000
33	A	92	LEU	0	0.004	0.029	4.691	0.327	0.387	-0.001	-0.003	-0.055	0.000
34	A	93	ILE	0	-0.034	-0.027	6.568	-0.288	-0.288	0.000	0.000	0.000	0.000
35	A	94	ASN	0	-0.007	-0.015	10.270	0.442	0.442	0.000	0.000	0.000	0.000
36	A	95	TYR	0	0.031	-0.010	12.227	-0.142	-0.142	0.000	0.000	0.000	0.000
37	A	96	ALA	0	0.008	0.007	15.547	0.042	0.042	0.000	0.000	0.000	0.000
38	A	97	ASP	-1	-0.806	-0.886	17.901	0.274	0.274	0.000	0.000	0.000	0.000
39	A	98	GLY	0	-0.015	-0.005	16.314	0.039	0.039	0.000	0.000	0.000	0.000
40	A	99	GLU	-1	-0.829	-0.873	13.933	0.592	0.592	0.000	0.000	0.000	0.000
41	A	100	LYS	1	0.934	0.967	8.829	-0.907	-0.907	0.000	0.000	0.000	0.000
42	A	101	ARG	1	0.771	0.851	9.581	-0.228	-0.228	0.000	0.000	0.000	0.000
43	A	102	TYR	0	0.026	-0.006	1.881	-9.971	-15.510	13.860	-4.935	-3.386	0.022
44	A	103	ILE	0	-0.018	-0.002	7.777	0.051	0.051	0.000	0.000	0.000	0.000
45	A	104	ILE	0	0.022	0.016	8.944	-0.252	-0.252	0.000	0.000	0.000	0.000
46	A	105	ALA	0	-0.026	-0.024	9.784	0.106	0.106	0.000	0.000	0.000	0.000
47	A	106	PRO	0	-0.014	-0.007	11.669	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	107	LYS	1	0.864	0.917	14.973	0.354	0.354	0.000	0.000	0.000	0.000
49	A	108	ASN	0	-0.033	-0.036	16.910	0.020	0.020	0.000	0.000	0.000	0.000
50	A	109	LEU	0	0.048	0.040	12.037	0.034	0.034	0.000	0.000	0.000	0.000
51	A	110	LYS	1	0.903	0.921	13.950	0.612	0.612	0.000	0.000	0.000	0.000
52	A	111	VAL	0	0.026	0.011	10.449	0.082	0.082	0.000	0.000	0.000	0.000
53	A	112	GLY	0	-0.047	-0.026	13.025	0.074	0.074	0.000	0.000	0.000	0.000
54	A	113	MET	0	-0.031	0.009	15.453	0.071	0.071	0.000	0.000	0.000	0.000
55	A	114	GLU	-1	-0.884	-0.933	15.641	-0.241	-0.241	0.000	0.000	0.000	0.000
56	A	115	ILE	0	-0.073	-0.032	14.067	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	116	MET	0	0.031	0.020	17.357	0.047	0.047	0.000	0.000	0.000	0.000
58	A	117	SER	0	-0.027	-0.044	19.228	-0.025	-0.025	0.000	0.000	0.000	0.000
59	A	118	GLY	0	0.063	0.040	21.095	0.018	0.018	0.000	0.000	0.000	0.000
60	A	119	PRO	0	-0.076	-0.066	24.644	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	120	ASP	-1	-0.912	-0.951	27.273	-0.038	-0.038	0.000	0.000	0.000	0.000
62	A	121	ALA	0	-0.033	0.003	22.834	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	122	ASP	-1	-0.829	-0.919	23.619	-0.203	-0.203	0.000	0.000	0.000	0.000
64	A	123	ILE	0	-0.019	-0.019	24.144	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	124	LYS	1	0.842	0.923	18.463	0.311	0.311	0.000	0.000	0.000	0.000
66	A	125	ILE	0	-0.005	-0.009	17.816	0.013	0.013	0.000	0.000	0.000	0.000
67	A	126	GLY	0	0.023	0.010	16.288	-0.032	-0.032	0.000	0.000	0.000	0.000
68	A	127	ASN	0	0.011	0.013	16.865	0.008	0.008	0.000	0.000	0.000	0.000
69	A	128	ALA	0	-0.047	-0.017	18.882	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	129	LEU	0	0.055	0.027	20.753	0.021	0.021	0.000	0.000	0.000	0.000
71	A	130	PRO	0	0.029	0.019	24.439	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	131	LEU	0	0.079	0.018	27.224	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	132	GLU	-1	-0.826	-0.884	28.817	-0.037	-0.037	0.000	0.000	0.000	0.000
74	A	133	ASN	0	-0.017	-0.006	28.642	0.005	0.005	0.000	0.000	0.000	0.000
75	A	134	ILE	0	-0.018	-0.015	25.022	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	135	PRO	0	-0.018	-0.005	28.804	0.008	0.008	0.000	0.000	0.000	0.000
77	A	136	VAL	0	0.032	0.035	30.765	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	137	GLY	0	0.020	0.007	31.974	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	138	THR	0	-0.047	-0.033	25.689	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	139	LEU	0	0.012	0.010	24.623	0.010	0.010	0.000	0.000	0.000	0.000
81	A	140	VAL	0	-0.002	-0.021	22.921	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	141	HIS	0	-0.040	-0.032	17.307	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	142	ASN	0	-0.027	-0.028	17.692	0.015	0.015	0.000	0.000	0.000	0.000
84	A	143	ILE	0	-0.002	-0.001	19.796	0.023	0.023	0.000	0.000	0.000	0.000
85	A	144	GLU	-1	-0.745	-0.853	23.224	0.012	0.012	0.000	0.000	0.000	0.000
86	A	145	LEU	0	-0.038	-0.029	24.837	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	146	LYS	1	0.943	0.959	27.625	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	147	PRO	0	-0.007	-0.015	27.573	0.006	0.006	0.000	0.000	0.000	0.000
89	A	148	GLY	0	0.085	0.062	25.224	0.012	0.012	0.000	0.000	0.000	0.000
90	A	149	ARG	1	0.771	0.884	23.886	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	150	GLY	0	0.061	0.037	20.957	0.004	0.004	0.000	0.000	0.000	0.000
92	A	151	GLY	0	-0.005	0.008	19.797	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	152	GLN	0	-0.038	-0.037	20.659	0.028	0.028	0.000	0.000	0.000	0.000
94	A	153	LEU	0	-0.004	-0.004	22.651	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	154	VAL	0	0.006	0.011	20.642	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	155	ARG	1	0.943	0.974	16.523	0.057	0.057	0.000	0.000	0.000	0.000
97	A	156	ALA	0	0.015	-0.002	13.578	-0.026	-0.026	0.000	0.000	0.000	0.000
98	A	157	ALA	0	0.028	0.026	15.408	-0.071	-0.071	0.000	0.000	0.000	0.000
99	A	158	GLY	0	0.021	0.021	18.020	0.054	0.054	0.000	0.000	0.000	0.000
100	A	159	THR	0	-0.010	-0.020	21.548	-0.022	-0.022	0.000	0.000	0.000	0.000
101	A	160	SER	0	-0.004	-0.023	21.605	0.013	0.013	0.000	0.000	0.000	0.000
102	A	161	ALA	0	-0.022	0.013	23.723	0.010	0.010	0.000	0.000	0.000	0.000
103	A	162	GLN	0	-0.015	-0.006	26.476	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	163	VAL	0	-0.008	0.012	28.606	0.015	0.015	0.000	0.000	0.000	0.000
105	A	164	LEU	0	-0.003	-0.010	31.065	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	165	GLY	0	0.046	0.008	34.748	0.002	0.002	0.000	0.000	0.000	0.000
107	A	166	LYS	1	0.818	0.919	32.361	0.095	0.095	0.000	0.000	0.000	0.000
108	A	167	GLU	-1	-0.904	-0.945	36.959	-0.054	-0.054	0.000	0.000	0.000	0.000
109	A	168	GLY	0	0.037	0.023	39.440	0.004	0.004	0.000	0.000	0.000	0.000
110	A	169	LYS	1	0.920	0.963	37.581	0.010	0.010	0.000	0.000	0.000	0.000
111	A	170	TYR	0	-0.012	-0.030	35.478	0.007	0.007	0.000	0.000	0.000	0.000
112	A	171	VAL	0	0.027	0.020	31.412	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	172	ILE	0	0.001	0.007	33.945	0.002	0.002	0.000	0.000	0.000	0.000
114	A	173	VAL	0	0.006	-0.006	28.604	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	174	ARG	1	0.971	1.002	31.557	0.168	0.168	0.000	0.000	0.000	0.000
116	A	175	LEU	0	-0.010	-0.011	27.606	-0.018	-0.018	0.000	0.000	0.000	0.000
117	A	176	ALA	0	0.055	0.018	26.927	0.004	0.004	0.000	0.000	0.000	0.000
118	A	177	SER	0	0.006	0.001	29.046	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	178	GLY	0	-0.016	-0.012	31.634	0.005	0.005	0.000	0.000	0.000	0.000
120	A	179	GLU	-1	-0.875	-0.920	32.367	-0.092	-0.092	0.000	0.000	0.000	0.000
121	A	180	VAL	0	0.009	0.002	33.308	-0.009	-0.009	0.000	0.000	0.000	0.000
122	A	181	ARG	1	0.857	0.920	30.932	0.086	0.086	0.000	0.000	0.000	0.000
123	A	182	MET	0	0.027	0.021	34.014	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	183	ILE	0	-0.035	-0.031	29.216	0.007	0.007	0.000	0.000	0.000	0.000
125	A	184	LEU	0	0.027	0.011	32.356	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	185	GLY	0	0.050	0.031	31.294	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	186	LYS	1	0.858	0.893	30.591	0.013	0.013	0.000	0.000	0.000	0.000
128	A	187	CYS	0	-0.094	-0.022	27.647	0.013	0.013	0.000	0.000	0.000	0.000
129	A	188	ARG	1	0.811	0.877	21.904	-0.021	-0.021	0.000	0.000	0.000	0.000
130	A	189	ALA	0	-0.017	-0.006	22.607	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	190	THR	0	-0.014	-0.006	16.923	0.014	0.014	0.000	0.000	0.000	0.000
132	A	191	VAL	0	0.052	0.033	20.378	-0.016	-0.016	0.000	0.000	0.000	0.000
133	A	192	GLY	0	0.031	0.002	19.612	-0.043	-0.043	0.000	0.000	0.000	0.000
134	A	193	GLU	-1	-0.838	-0.882	19.901	-0.373	-0.373	0.000	0.000	0.000	0.000
135	A	194	VAL	0	0.003	-0.009	16.410	-0.058	-0.058	0.000	0.000	0.000	0.000
136	A	195	GLY	0	0.003	0.024	16.878	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:60:GLN)