FMO DATABASE

FMODB ID: 761LK

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1157401.518445
FMO2-HF: Nuclear repulsion	1106220.354078
FMO2-HF: Total energy	-51181.164367
FMO2-MP2: Total energy	-51330.845006

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.
-33.744	-43.613	34.614	-14.166	-10.579	-0.029

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 : -0.002 / q_NPA : 0.018

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	0.978	0.978	3.864	-4.728	-2.492	-0.028	-1.263	-0.945	0.002
4	A	63	ILE	0	-0.021	0.005	7.187	-0.238	-0.238	0.000	0.000	0.000	0.000
5	A	64	ILE	0	0.005	0.008	6.509	0.026	0.026	0.000	0.000	0.000	0.000
6	A	65	ASP	-1	-0.780	-0.877	9.447	0.060	0.060	0.000	0.000	0.000	0.000
7	A	66	PHE	0	-0.035	-0.031	12.342	-0.071	-0.071	0.000	0.000	0.000	0.000
8	A	67	LYS	1	0.906	0.954	15.103	-0.106	-0.106	0.000	0.000	0.000	0.000
9	A	68	ARG	1	0.811	0.904	14.163	0.284	0.284	0.000	0.000	0.000	0.000
10	A	69	ASP	-1	-0.778	-0.886	17.104	0.092	0.092	0.000	0.000	0.000	0.000
11	A	70	LYS	1	0.779	0.883	15.285	-0.159	-0.159	0.000	0.000	0.000	0.000
12	A	71	ASP	-1	-0.727	-0.829	19.136	-0.078	-0.078	0.000	0.000	0.000	0.000
13	A	72	GLY	0	-0.001	0.003	22.246	0.020	0.020	0.000	0.000	0.000	0.000
14	A	73	ILE	0	-0.056	-0.016	18.826	0.000	0.000	0.000	0.000	0.000	0.000
15	A	74	PRO	0	0.018	0.019	19.030	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	75	GLY	0	0.039	0.004	15.210	0.060	0.060	0.000	0.000	0.000	0.000
17	A	76	ARG	1	0.857	0.938	12.610	0.593	0.593	0.000	0.000	0.000	0.000
18	A	77	VAL	0	-0.008	0.005	9.967	0.026	0.026	0.000	0.000	0.000	0.000
19	A	78	ALA	0	-0.046	-0.021	8.045	0.028	0.028	0.000	0.000	0.000	0.000
20	A	79	THR	0	-0.030	-0.056	4.243	0.599	0.689	-0.001	-0.005	-0.084	0.000
21	A	80	ILE	0	-0.007	-0.018	7.067	0.427	0.427	0.000	0.000	0.000	0.000
22	A	81	GLU	-1	-0.822	-0.871	1.789	-18.986	-22.986	13.307	-5.454	-3.853	-0.052
23	A	82	TYR	0	0.007	0.004	6.346	0.423	0.423	0.000	0.000	0.000	0.000
24	A	83	ASP	-1	-0.807	-0.898	5.555	-2.183	-2.183	0.000	0.000	0.000	0.000
25	A	84	PRO	0	0.033	0.000	6.764	0.398	0.398	0.000	0.000	0.000	0.000
26	A	85	ASN	0	-0.057	-0.022	8.624	0.353	0.353	0.000	0.000	0.000	0.000
27	A	86	ARG	1	0.809	0.885	6.933	1.266	1.266	0.000	0.000	0.000	0.000
28	A	87	SER	0	-0.062	-0.013	11.019	0.125	0.125	0.000	0.000	0.000	0.000
29	A	88	ALA	0	0.028	0.017	10.496	0.082	0.082	0.000	0.000	0.000	0.000
30	A	89	ASN	0	0.031	0.012	8.748	-0.404	-0.404	0.000	0.000	0.000	0.000
31	A	90	ILE	0	-0.033	-0.010	3.054	0.030	0.429	0.055	-0.124	-0.330	-0.001
32	A	91	ALA	0	0.024	0.004	6.405	-0.574	-0.574	0.000	0.000	0.000	0.000
33	A	92	LEU	0	-0.005	0.021	4.578	0.279	0.361	-0.001	-0.008	-0.073	0.000
34	A	93	ILE	0	-0.018	-0.009	6.266	-0.214	-0.214	0.000	0.000	0.000	0.000
35	A	94	ASN	0	0.027	0.021	9.979	0.449	0.449	0.000	0.000	0.000	0.000
36	A	95	TYR	0	0.037	-0.005	11.925	-0.150	-0.150	0.000	0.000	0.000	0.000
37	A	96	ALA	0	0.002	0.000	15.354	0.047	0.047	0.000	0.000	0.000	0.000
38	A	97	ASP	-1	-0.795	-0.880	17.780	0.192	0.192	0.000	0.000	0.000	0.000
39	A	98	GLY	0	-0.006	0.002	16.491	0.036	0.036	0.000	0.000	0.000	0.000
40	A	99	GLU	-1	-0.828	-0.873	13.624	0.443	0.443	0.000	0.000	0.000	0.000
41	A	100	LYS	1	0.894	0.930	8.912	-0.755	-0.755	0.000	0.000	0.000	0.000
42	A	101	ARG	1	0.763	0.845	8.898	-0.076	-0.076	0.000	0.000	0.000	0.000
43	A	102	TYR	0	0.025	-0.011	1.842	-12.263	-20.939	21.282	-7.312	-5.294	0.022
44	A	103	ILE	0	-0.018	-0.005	6.837	0.138	0.138	0.000	0.000	0.000	0.000
45	A	104	ILE	0	0.035	0.010	8.155	-0.338	-0.338	0.000	0.000	0.000	0.000
46	A	105	ALA	0	-0.016	-0.005	9.319	0.136	0.136	0.000	0.000	0.000	0.000
47	A	106	PRO	0	-0.020	-0.011	11.114	0.017	0.017	0.000	0.000	0.000	0.000
48	A	107	LYS	1	0.839	0.896	14.900	0.399	0.399	0.000	0.000	0.000	0.000
49	A	108	ASN	0	0.018	-0.007	16.929	0.023	0.023	0.000	0.000	0.000	0.000
50	A	109	LEU	0	0.011	0.031	11.691	0.038	0.038	0.000	0.000	0.000	0.000
51	A	110	LYS	1	0.893	0.910	13.856	0.641	0.641	0.000	0.000	0.000	0.000
52	A	111	VAL	0	0.027	0.008	9.937	0.065	0.065	0.000	0.000	0.000	0.000
53	A	112	GLY	0	-0.015	-0.004	12.604	0.084	0.084	0.000	0.000	0.000	0.000
54	A	113	MET	0	-0.034	0.002	15.214	0.075	0.075	0.000	0.000	0.000	0.000
55	A	114	GLU	-1	-0.863	-0.928	15.284	-0.292	-0.292	0.000	0.000	0.000	0.000
56	A	115	ILE	0	-0.075	-0.041	13.534	-0.048	-0.048	0.000	0.000	0.000	0.000
57	A	116	MET	0	0.026	0.031	16.852	0.051	0.051	0.000	0.000	0.000	0.000
58	A	117	SER	0	-0.040	-0.046	18.683	-0.035	-0.035	0.000	0.000	0.000	0.000
59	A	118	GLY	0	0.070	0.044	20.494	0.023	0.023	0.000	0.000	0.000	0.000
60	A	119	PRO	0	-0.064	-0.057	24.107	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	120	ASP	-1	-0.894	-0.947	26.891	-0.079	-0.079	0.000	0.000	0.000	0.000
62	A	121	ALA	0	-0.032	-0.001	22.468	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	122	ASP	-1	-0.806	-0.906	23.140	-0.255	-0.255	0.000	0.000	0.000	0.000
64	A	123	ILE	0	-0.031	-0.023	23.614	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	124	LYS	1	0.821	0.912	17.870	0.389	0.389	0.000	0.000	0.000	0.000
66	A	125	ILE	0	0.010	-0.008	17.766	0.007	0.007	0.000	0.000	0.000	0.000
67	A	126	GLY	0	0.016	0.015	15.762	-0.025	-0.025	0.000	0.000	0.000	0.000
68	A	127	ASN	0	0.017	0.015	16.298	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	128	ALA	0	-0.041	-0.020	18.090	-0.018	-0.018	0.000	0.000	0.000	0.000
70	A	129	LEU	0	0.040	0.026	20.058	0.025	0.025	0.000	0.000	0.000	0.000
71	A	130	PRO	0	0.035	0.019	23.731	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	131	LEU	0	0.031	0.011	26.425	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	132	GLU	-1	-0.794	-0.883	28.261	-0.072	-0.072	0.000	0.000	0.000	0.000
74	A	133	ASN	0	0.019	0.029	27.834	0.006	0.006	0.000	0.000	0.000	0.000
75	A	134	ILE	0	-0.017	0.003	24.104	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	135	PRO	0	0.019	0.013	28.155	0.011	0.011	0.000	0.000	0.000	0.000
77	A	136	VAL	0	0.031	0.028	30.026	-0.012	-0.012	0.000	0.000	0.000	0.000
78	A	137	GLY	0	0.016	0.015	31.371	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	138	THR	0	-0.047	-0.035	25.040	-0.020	-0.020	0.000	0.000	0.000	0.000
80	A	139	LEU	0	0.020	0.010	24.097	0.009	0.009	0.000	0.000	0.000	0.000
81	A	140	VAL	0	-0.006	-0.011	22.287	-0.017	-0.017	0.000	0.000	0.000	0.000
82	A	141	HIS	0	-0.025	-0.028	16.607	-0.026	-0.026	0.000	0.000	0.000	0.000
83	A	142	ASN	0	-0.026	-0.039	16.865	0.013	0.013	0.000	0.000	0.000	0.000
84	A	143	ILE	0	0.012	0.025	19.000	0.026	0.026	0.000	0.000	0.000	0.000
85	A	144	GLU	-1	-0.761	-0.870	22.413	-0.064	-0.064	0.000	0.000	0.000	0.000
86	A	145	LEU	0	-0.018	-0.024	24.139	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	146	LYS	1	0.924	0.947	26.810	0.029	0.029	0.000	0.000	0.000	0.000
88	A	147	PRO	0	0.020	0.006	26.577	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	148	GLY	0	0.023	0.026	24.073	0.015	0.015	0.000	0.000	0.000	0.000
90	A	149	ARG	1	0.802	0.901	23.356	0.046	0.046	0.000	0.000	0.000	0.000
91	A	150	GLY	0	0.048	0.031	19.861	0.006	0.006	0.000	0.000	0.000	0.000
92	A	151	GLY	0	0.005	0.011	19.073	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	152	GLN	0	-0.057	-0.040	20.059	0.028	0.028	0.000	0.000	0.000	0.000
94	A	153	LEU	0	0.016	0.009	21.752	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	154	VAL	0	0.005	0.003	20.005	-0.013	-0.013	0.000	0.000	0.000	0.000
96	A	155	ARG	1	0.911	0.949	15.868	0.180	0.180	0.000	0.000	0.000	0.000
97	A	156	ALA	0	0.014	0.009	13.316	-0.040	-0.040	0.000	0.000	0.000	0.000
98	A	157	ALA	0	0.051	0.031	14.987	-0.073	-0.073	0.000	0.000	0.000	0.000
99	A	158	GLY	0	0.012	0.012	17.625	0.055	0.055	0.000	0.000	0.000	0.000
100	A	159	THR	0	-0.003	-0.019	21.263	-0.021	-0.021	0.000	0.000	0.000	0.000
101	A	160	SER	0	-0.023	-0.031	21.117	0.014	0.014	0.000	0.000	0.000	0.000
102	A	161	ALA	0	-0.007	0.014	23.101	0.015	0.015	0.000	0.000	0.000	0.000
103	A	162	GLN	0	-0.030	-0.023	25.831	-0.013	-0.013	0.000	0.000	0.000	0.000
104	A	163	VAL	0	0.004	0.013	27.823	0.017	0.017	0.000	0.000	0.000	0.000
105	A	164	LEU	0	-0.004	-0.017	30.374	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	165	GLY	0	0.037	0.016	34.147	0.006	0.006	0.000	0.000	0.000	0.000
107	A	166	LYS	1	0.773	0.875	31.336	0.130	0.130	0.000	0.000	0.000	0.000
108	A	167	GLU	-1	-0.893	-0.938	36.460	-0.076	-0.076	0.000	0.000	0.000	0.000
109	A	168	GLY	0	0.037	0.015	38.922	0.003	0.003	0.000	0.000	0.000	0.000
110	A	169	LYS	1	0.920	0.972	36.981	0.044	0.044	0.000	0.000	0.000	0.000
111	A	170	TYR	0	-0.010	-0.017	34.808	0.004	0.004	0.000	0.000	0.000	0.000
112	A	171	VAL	0	0.025	0.012	30.760	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	172	ILE	0	0.010	0.016	33.009	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	173	VAL	0	0.007	-0.007	28.003	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	174	ARG	1	0.926	0.976	31.051	0.205	0.205	0.000	0.000	0.000	0.000
116	A	175	LEU	0	0.008	-0.003	26.936	-0.022	-0.022	0.000	0.000	0.000	0.000
117	A	176	ALA	0	0.053	0.016	26.174	0.008	0.008	0.000	0.000	0.000	0.000
118	A	177	SER	0	0.010	0.003	28.244	0.003	0.003	0.000	0.000	0.000	0.000
119	A	178	GLY	0	0.002	0.005	30.853	0.007	0.007	0.000	0.000	0.000	0.000
120	A	179	GLU	-1	-0.861	-0.915	31.539	-0.133	-0.133	0.000	0.000	0.000	0.000
121	A	180	VAL	0	-0.007	-0.005	32.553	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	181	ARG	1	0.861	0.923	30.507	0.129	0.129	0.000	0.000	0.000	0.000
123	A	182	MET	0	0.028	0.016	33.698	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	183	ILE	0	-0.030	-0.015	28.164	0.007	0.007	0.000	0.000	0.000	0.000
125	A	184	LEU	0	0.015	-0.001	31.725	0.001	0.001	0.000	0.000	0.000	0.000
126	A	185	GLY	0	0.027	0.011	30.579	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	186	LYS	1	0.856	0.888	29.640	0.048	0.048	0.000	0.000	0.000	0.000
128	A	187	CYS	0	-0.087	-0.017	26.740	0.010	0.010	0.000	0.000	0.000	0.000
129	A	188	ARG	1	0.812	0.865	21.211	0.054	0.054	0.000	0.000	0.000	0.000
130	A	189	ALA	0	-0.002	0.000	21.572	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	190	THR	0	-0.022	-0.011	16.062	0.009	0.009	0.000	0.000	0.000	0.000
132	A	191	VAL	0	0.047	0.035	19.473	-0.009	-0.009	0.000	0.000	0.000	0.000
133	A	192	GLY	0	0.033	0.000	19.056	-0.054	-0.054	0.000	0.000	0.000	0.000
134	A	193	GLU	-1	-0.825	-0.868	19.922	-0.416	-0.416	0.000	0.000	0.000	0.000
135	A	194	VAL	0	-0.003	-0.001	15.468	-0.065	-0.065	0.000	0.000	0.000	0.000
136	A	195	GLY	0	0.002	0.019	16.087	0.052	0.052	0.000	0.000	0.000	0.000

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