FMO DATABASE

FMODB ID: 981J2

Calculation Name: 1RL2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

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	-1159751.390745
FMO2-HF: Nuclear repulsion	1108571.430177
FMO2-HF: Total energy	-51179.960567
FMO2-MP2: Total energy	-51329.839516

3D Structure Molmil

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.
-12.276	-31.807	45.816	-16.361	-9.924	-0.106

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 : 0.019 / q_NPA : -0.006

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	1.007	1.005	3.691	-6.267	-1.705	-0.081	-2.560	-1.921	-0.005
4	A	63	ILE	0	-0.026	0.005	7.274	-0.029	-0.029	0.000	0.000	0.000	0.000
5	A	64	ILE	0	0.003	0.017	7.708	-0.165	-0.165	0.000	0.000	0.000	0.000
6	A	65	ASP	-1	-0.784	-0.868	10.382	-0.180	-0.180	0.000	0.000	0.000	0.000
7	A	66	PHE	0	-0.042	-0.043	12.984	-0.043	-0.043	0.000	0.000	0.000	0.000
8	A	67	LYS	1	0.971	0.968	16.111	0.115	0.115	0.000	0.000	0.000	0.000
9	A	68	ARG	1	0.784	0.886	14.721	0.473	0.473	0.000	0.000	0.000	0.000
10	A	69	ASP	-1	-0.833	-0.930	17.715	-0.132	-0.132	0.000	0.000	0.000	0.000
11	A	70	LYS	1	0.810	0.924	15.527	0.126	0.126	0.000	0.000	0.000	0.000
12	A	71	ASP	-1	-0.743	-0.854	19.299	-0.181	-0.181	0.000	0.000	0.000	0.000
13	A	72	GLY	0	0.001	0.010	22.508	0.020	0.020	0.000	0.000	0.000	0.000
14	A	73	ILE	0	-0.048	-0.020	18.636	0.005	0.005	0.000	0.000	0.000	0.000
15	A	74	PRO	0	0.019	0.026	18.952	-0.035	-0.035	0.000	0.000	0.000	0.000
16	A	75	GLY	0	0.051	0.018	15.305	0.021	0.021	0.000	0.000	0.000	0.000
17	A	76	ARG	1	0.941	0.996	13.802	0.469	0.469	0.000	0.000	0.000	0.000
18	A	77	VAL	0	-0.008	-0.009	10.285	-0.072	-0.072	0.000	0.000	0.000	0.000
19	A	78	ALA	0	-0.028	-0.017	8.100	0.072	0.072	0.000	0.000	0.000	0.000
20	A	79	THR	0	0.008	-0.005	4.372	0.094	0.157	-0.001	-0.003	-0.059	0.000
21	A	80	ILE	0	-0.014	-0.013	7.228	-0.065	-0.065	0.000	0.000	0.000	0.000
22	A	81	GLU	-1	-0.837	-0.900	1.537	-6.120	-28.824	39.827	-11.846	-5.278	-0.085
23	A	82	TYR	0	0.018	0.021	6.410	0.045	0.045	0.000	0.000	0.000	0.000
24	A	83	ASP	-1	-0.817	-0.914	5.756	-1.362	-1.362	0.000	0.000	0.000	0.000
25	A	84	PRO	0	0.017	-0.009	7.047	0.207	0.207	0.000	0.000	0.000	0.000
26	A	85	ASN	0	-0.016	-0.001	8.961	0.191	0.191	0.000	0.000	0.000	0.000
27	A	86	ARG	1	0.794	0.886	7.304	1.094	1.094	0.000	0.000	0.000	0.000
28	A	87	SER	0	-0.037	-0.007	11.171	0.057	0.057	0.000	0.000	0.000	0.000
29	A	88	ALA	0	-0.009	-0.014	10.543	0.067	0.067	0.000	0.000	0.000	0.000
30	A	89	ASN	0	0.005	0.013	8.905	-0.274	-0.274	0.000	0.000	0.000	0.000
31	A	90	ILE	0	-0.019	-0.003	3.576	0.161	0.367	0.006	-0.043	-0.169	0.000
32	A	91	ALA	0	0.002	-0.010	6.125	-0.409	-0.409	0.000	0.000	0.000	0.000
33	A	92	LEU	0	-0.009	0.020	4.739	0.054	0.120	-0.001	-0.002	-0.062	0.000
34	A	93	ILE	0	-0.036	-0.025	6.552	0.252	0.252	0.000	0.000	0.000	0.000
35	A	94	ASN	0	0.004	-0.009	10.001	0.135	0.135	0.000	0.000	0.000	0.000
36	A	95	TYR	0	0.023	-0.009	11.950	-0.028	-0.028	0.000	0.000	0.000	0.000
37	A	96	ALA	0	0.009	0.007	15.190	0.048	0.048	0.000	0.000	0.000	0.000
38	A	97	ASP	-1	-0.812	-0.881	17.057	-0.031	-0.031	0.000	0.000	0.000	0.000
39	A	98	GLY	0	-0.010	-0.010	15.540	0.044	0.044	0.000	0.000	0.000	0.000
40	A	99	GLU	-1	-0.845	-0.900	13.078	0.008	0.008	0.000	0.000	0.000	0.000
41	A	100	LYS	1	0.906	0.950	7.328	-0.478	-0.478	0.000	0.000	0.000	0.000
42	A	101	ARG	1	0.775	0.857	8.984	0.269	0.269	0.000	0.000	0.000	0.000
43	A	102	TYR	0	0.061	0.035	2.129	-1.547	-3.271	6.066	-1.907	-2.435	-0.016
44	A	103	ILE	0	0.002	0.004	7.823	0.325	0.325	0.000	0.000	0.000	0.000
45	A	104	ILE	0	0.007	0.012	9.005	-0.280	-0.280	0.000	0.000	0.000	0.000
46	A	105	ALA	0	-0.025	-0.027	9.840	0.095	0.095	0.000	0.000	0.000	0.000
47	A	106	PRO	0	-0.012	-0.004	11.714	0.041	0.041	0.000	0.000	0.000	0.000
48	A	107	LYS	1	1.003	0.994	15.004	0.380	0.380	0.000	0.000	0.000	0.000
49	A	108	ASN	0	-0.059	-0.045	16.930	0.019	0.019	0.000	0.000	0.000	0.000
50	A	109	LEU	0	0.035	0.026	11.773	0.029	0.029	0.000	0.000	0.000	0.000
51	A	110	LYS	1	0.937	0.934	13.927	0.550	0.550	0.000	0.000	0.000	0.000
52	A	111	VAL	0	0.038	0.018	10.407	0.026	0.026	0.000	0.000	0.000	0.000
53	A	112	GLY	0	-0.050	-0.044	12.977	0.078	0.078	0.000	0.000	0.000	0.000
54	A	113	MET	0	-0.030	0.009	15.392	0.053	0.053	0.000	0.000	0.000	0.000
55	A	114	GLU	-1	-0.897	-0.941	15.600	-0.326	-0.326	0.000	0.000	0.000	0.000
56	A	115	ILE	0	-0.057	-0.029	14.229	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	116	MET	0	0.023	0.010	17.351	0.037	0.037	0.000	0.000	0.000	0.000
58	A	117	SER	0	-0.023	-0.036	19.238	-0.042	-0.042	0.000	0.000	0.000	0.000
59	A	118	GLY	0	0.059	0.014	21.118	0.022	0.022	0.000	0.000	0.000	0.000
60	A	119	PRO	0	-0.084	-0.065	24.670	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	120	ASP	-1	-0.908	-0.944	27.262	-0.123	-0.123	0.000	0.000	0.000	0.000
62	A	121	ALA	0	-0.039	-0.002	22.842	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	122	ASP	-1	-0.807	-0.909	23.878	-0.252	-0.252	0.000	0.000	0.000	0.000
64	A	123	ILE	0	-0.028	-0.016	24.158	-0.021	-0.021	0.000	0.000	0.000	0.000
65	A	124	LYS	1	0.891	0.956	19.536	0.375	0.375	0.000	0.000	0.000	0.000
66	A	125	ILE	0	-0.008	-0.005	17.304	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	126	GLY	0	0.013	0.015	16.317	-0.031	-0.031	0.000	0.000	0.000	0.000
68	A	127	ASN	0	0.006	0.013	16.893	-0.050	-0.050	0.000	0.000	0.000	0.000
69	A	128	ALA	0	-0.049	-0.018	18.960	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	129	LEU	0	0.043	0.018	20.792	0.017	0.017	0.000	0.000	0.000	0.000
71	A	130	PRO	0	0.017	0.020	24.479	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	131	LEU	0	0.086	0.017	27.258	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	132	GLU	-1	-0.869	-0.914	28.872	-0.106	-0.106	0.000	0.000	0.000	0.000
74	A	133	ASN	0	-0.038	-0.033	28.735	0.006	0.006	0.000	0.000	0.000	0.000
75	A	134	ILE	0	-0.022	-0.014	25.286	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	135	PRO	0	-0.025	-0.010	28.885	0.011	0.011	0.000	0.000	0.000	0.000
77	A	136	VAL	0	0.044	0.044	30.808	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	137	GLY	0	0.012	0.002	32.020	0.000	0.000	0.000	0.000	0.000	0.000
79	A	138	THR	0	-0.048	-0.039	25.706	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	139	LEU	0	0.014	0.013	24.710	0.008	0.008	0.000	0.000	0.000	0.000
81	A	140	VAL	0	-0.001	-0.020	22.992	-0.017	-0.017	0.000	0.000	0.000	0.000
82	A	141	HIS	0	-0.037	-0.029	17.361	-0.035	-0.035	0.000	0.000	0.000	0.000
83	A	142	ASN	0	-0.025	-0.021	17.845	0.004	0.004	0.000	0.000	0.000	0.000
84	A	143	ILE	0	-0.011	-0.001	19.875	0.013	0.013	0.000	0.000	0.000	0.000
85	A	144	GLU	-1	-0.748	-0.865	23.047	-0.148	-0.148	0.000	0.000	0.000	0.000
86	A	145	LEU	0	-0.062	-0.032	24.916	0.009	0.009	0.000	0.000	0.000	0.000
87	A	146	LYS	1	0.938	0.956	27.708	0.077	0.077	0.000	0.000	0.000	0.000
88	A	147	PRO	0	-0.019	-0.028	27.597	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	148	GLY	0	0.093	0.071	25.079	0.016	0.016	0.000	0.000	0.000	0.000
90	A	149	ARG	1	0.783	0.898	23.715	0.080	0.080	0.000	0.000	0.000	0.000
91	A	150	GLY	0	0.052	0.020	20.959	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	151	GLY	0	0.004	0.006	19.899	0.011	0.011	0.000	0.000	0.000	0.000
93	A	152	GLN	0	-0.059	-0.061	20.752	0.015	0.015	0.000	0.000	0.000	0.000
94	A	153	LEU	0	0.003	-0.001	22.705	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	154	VAL	0	0.032	0.021	20.185	-0.020	-0.020	0.000	0.000	0.000	0.000
96	A	155	ARG	1	0.956	0.988	16.484	0.277	0.277	0.000	0.000	0.000	0.000
97	A	156	ALA	0	0.023	-0.002	13.602	-0.056	-0.056	0.000	0.000	0.000	0.000
98	A	157	ALA	0	0.024	0.022	15.451	-0.038	-0.038	0.000	0.000	0.000	0.000
99	A	158	GLY	0	0.006	0.016	18.061	0.037	0.037	0.000	0.000	0.000	0.000
100	A	159	THR	0	0.008	-0.010	21.588	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	160	SER	0	-0.020	-0.044	21.718	0.004	0.004	0.000	0.000	0.000	0.000
102	A	161	ALA	0	-0.014	0.018	23.794	0.018	0.018	0.000	0.000	0.000	0.000
103	A	162	GLN	0	0.001	0.005	26.540	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	163	VAL	0	-0.011	0.013	28.674	0.015	0.015	0.000	0.000	0.000	0.000
105	A	164	LEU	0	-0.005	-0.014	31.124	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	165	GLY	0	0.050	0.008	34.808	0.005	0.005	0.000	0.000	0.000	0.000
107	A	166	LYS	1	0.838	0.944	32.698	0.138	0.138	0.000	0.000	0.000	0.000
108	A	167	GLU	-1	-0.894	-0.941	37.015	-0.082	-0.082	0.000	0.000	0.000	0.000
109	A	168	GLY	0	0.027	0.019	39.502	0.002	0.002	0.000	0.000	0.000	0.000
110	A	169	LYS	1	0.931	0.968	37.646	0.062	0.062	0.000	0.000	0.000	0.000
111	A	170	TYR	0	-0.014	-0.032	35.542	0.002	0.002	0.000	0.000	0.000	0.000
112	A	171	VAL	0	0.029	0.026	31.342	0.001	0.001	0.000	0.000	0.000	0.000
113	A	172	ILE	0	-0.012	0.000	34.015	0.000	0.000	0.000	0.000	0.000	0.000
114	A	173	VAL	0	0.012	-0.002	28.767	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	174	ARG	1	0.988	1.016	31.628	0.172	0.172	0.000	0.000	0.000	0.000
116	A	175	LEU	0	-0.023	-0.019	27.894	-0.018	-0.018	0.000	0.000	0.000	0.000
117	A	176	ALA	0	0.054	0.021	27.006	0.008	0.008	0.000	0.000	0.000	0.000
118	A	177	SER	0	-0.019	-0.006	29.104	0.004	0.004	0.000	0.000	0.000	0.000
119	A	178	GLY	0	-0.021	-0.026	31.678	0.009	0.009	0.000	0.000	0.000	0.000
120	A	179	GLU	-1	-0.892	-0.938	32.440	-0.126	-0.126	0.000	0.000	0.000	0.000
121	A	180	VAL	0	0.019	0.007	33.391	-0.010	-0.010	0.000	0.000	0.000	0.000
122	A	181	ARG	1	0.876	0.940	30.735	0.134	0.134	0.000	0.000	0.000	0.000
123	A	182	MET	0	0.023	0.020	34.091	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	183	ILE	0	-0.031	-0.025	29.264	0.005	0.005	0.000	0.000	0.000	0.000
125	A	184	LEU	0	0.026	0.011	32.433	0.002	0.002	0.000	0.000	0.000	0.000
126	A	185	GLY	0	0.060	0.034	31.360	-0.009	-0.009	0.000	0.000	0.000	0.000
127	A	186	LYS	1	0.889	0.920	30.646	0.085	0.085	0.000	0.000	0.000	0.000
128	A	187	CYS	0	-0.082	-0.013	27.770	0.003	0.003	0.000	0.000	0.000	0.000
129	A	188	ARG	1	0.839	0.923	21.893	0.176	0.176	0.000	0.000	0.000	0.000
130	A	189	ALA	0	0.001	0.005	22.686	0.000	0.000	0.000	0.000	0.000	0.000
131	A	190	THR	0	-0.009	-0.005	17.065	-0.008	-0.008	0.000	0.000	0.000	0.000
132	A	191	VAL	0	0.042	0.028	20.431	0.002	0.002	0.000	0.000	0.000	0.000
133	A	192	GLY	0	0.021	-0.003	19.653	-0.049	-0.049	0.000	0.000	0.000	0.000
134	A	193	GLU	-1	-0.951	-0.948	19.958	-0.327	-0.327	0.000	0.000	0.000	0.000
135	A	194	VAL	0	0.006	0.002	16.736	-0.057	-0.057	0.000	0.000	0.000	0.000
136	A	195	GLY	0	-0.021	0.006	16.913	0.025	0.025	0.000	0.000	0.000	0.000

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