FMO DATABASE

FMODB ID: R8Y38

Calculation Name: 3ERW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ERW

Chain ID: A

ChEMBL ID:

UniProt ID: O31687

Base Structure: X-ray

Registration Date: 2023-09-22

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	OptH
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	133
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1262981.136412
FMO2-HF: Nuclear repulsion	1209438.173605
FMO2-HF: Total energy	-53542.962807
FMO2-MP2: Total energy	-53699.144019

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:31:PRO)

Summations of interaction energy for fragment #1(A:31:PRO)

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.
-14.78	-5.917	8.95	-6.609	-11.204	-0.044

Interaction energy analysis for fragmet #1(A:31:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.015 / q_NPA : -0.016

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	33	VAL	0	-0.041	-0.027	3.651	0.086	1.463	-0.003	-0.558	-0.816	0.003
4	A	34	PRO	0	0.013	0.018	3.266	-1.883	-1.145	0.046	-0.313	-0.471	-0.003
5	A	35	ALA	0	0.001	-0.007	4.806	1.006	1.006	0.000	0.000	0.000	0.000
6	A	36	VAL	0	-0.011	0.013	5.978	-0.205	-0.205	0.000	0.000	0.000	0.000
7	A	37	PHE	0	-0.015	-0.014	4.842	0.322	0.322	0.000	0.000	0.000	0.000
8	A	38	LEU	0	-0.009	-0.009	10.110	0.105	0.105	0.000	0.000	0.000	0.000
9	A	39	MET	0	-0.036	-0.019	11.414	0.029	0.029	0.000	0.000	0.000	0.000
10	A	40	LYS	1	0.913	0.969	15.175	0.165	0.165	0.000	0.000	0.000	0.000
11	A	41	THR	0	-0.037	-0.011	18.299	0.009	0.009	0.000	0.000	0.000	0.000
12	A	42	ILE	0	0.012	-0.002	19.169	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	43	GLU	-1	-0.851	-0.951	21.705	0.020	0.020	0.000	0.000	0.000	0.000
14	A	44	GLY	0	-0.048	-0.027	22.840	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	45	GLU	-1	-0.884	-0.954	20.259	-0.070	-0.070	0.000	0.000	0.000	0.000
16	A	46	ASP	-1	-0.924	-0.953	19.167	-0.186	-0.186	0.000	0.000	0.000	0.000
17	A	47	ILE	0	-0.001	0.010	13.749	0.007	0.007	0.000	0.000	0.000	0.000
18	A	48	SER	0	-0.028	-0.026	12.479	-0.058	-0.058	0.000	0.000	0.000	0.000
19	A	49	ILE	0	-0.038	0.001	7.198	0.135	0.135	0.000	0.000	0.000	0.000
20	A	50	PRO	0	0.093	0.046	6.185	-0.236	-0.236	0.000	0.000	0.000	0.000
21	A	51	ASN	0	-0.028	-0.019	8.759	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	52	LYS	1	0.976	0.976	12.459	0.284	0.284	0.000	0.000	0.000	0.000
23	A	53	GLY	0	-0.057	-0.009	14.192	0.045	0.045	0.000	0.000	0.000	0.000
24	A	54	GLN	0	0.018	-0.009	13.610	0.018	0.018	0.000	0.000	0.000	0.000
25	A	55	LYS	1	0.931	0.994	11.713	-0.275	-0.275	0.000	0.000	0.000	0.000
26	A	56	THR	0	-0.028	-0.003	9.358	-0.067	-0.067	0.000	0.000	0.000	0.000
27	A	57	ILE	0	-0.001	0.006	10.080	0.144	0.144	0.000	0.000	0.000	0.000
28	A	58	LEU	0	-0.005	0.023	6.290	-0.090	-0.090	0.000	0.000	0.000	0.000
29	A	59	HIS	1	0.867	0.931	9.983	-0.307	-0.307	0.000	0.000	0.000	0.000
30	A	60	PHE	0	0.059	0.033	7.579	-0.092	-0.092	0.000	0.000	0.000	0.000
31	A	61	TRP	0	-0.053	-0.053	12.920	0.019	0.019	0.000	0.000	0.000	0.000
32	A	62	THR	0	0.051	0.027	16.619	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	63	SER	0	-0.045	-0.048	19.676	0.012	0.012	0.000	0.000	0.000	0.000
34	A	64	TRP	0	-0.067	-0.048	20.653	0.010	0.010	0.000	0.000	0.000	0.000
35	A	65	CYS	0	0.059	0.068	19.279	0.029	0.029	0.000	0.000	0.000	0.000
36	A	66	PRO	0	0.024	0.003	22.395	0.000	0.000	0.000	0.000	0.000	0.000
37	A	67	PRO	0	-0.031	-0.037	20.742	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	69	LYS	1	0.967	0.996	20.764	-0.176	-0.176	0.000	0.000	0.000	0.000
39	A	70	LYS	1	0.932	0.958	24.192	-0.246	-0.246	0.000	0.000	0.000	0.000
40	A	71	GLU	-1	-0.796	-0.908	17.867	0.459	0.459	0.000	0.000	0.000	0.000
41	A	72	LEU	0	0.019	0.009	19.638	0.002	0.002	0.000	0.000	0.000	0.000
42	A	73	PRO	0	-0.007	-0.003	22.283	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	74	GLN	0	-0.038	0.006	21.478	-0.024	-0.024	0.000	0.000	0.000	0.000
44	A	75	PHE	0	0.015	-0.002	15.403	0.000	0.000	0.000	0.000	0.000	0.000
45	A	76	GLN	0	0.005	0.022	20.760	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	77	SER	0	-0.025	-0.011	23.830	-0.013	-0.013	0.000	0.000	0.000	0.000
47	A	78	PHE	0	0.031	0.001	17.599	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	79	TYR	0	0.008	-0.007	20.412	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	80	ASP	-1	-0.877	-0.939	22.447	0.080	0.080	0.000	0.000	0.000	0.000
50	A	81	ALA	0	-0.099	-0.049	25.441	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	82	HIS	0	-0.070	-0.027	22.286	0.004	0.004	0.000	0.000	0.000	0.000
52	A	83	PRO	0	-0.040	-0.020	21.908	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	84	SER	0	0.023	0.004	19.647	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	85	ASP	-1	-0.799	-0.879	21.358	0.019	0.019	0.000	0.000	0.000	0.000
55	A	86	SER	0	-0.065	-0.030	18.205	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	87	VAL	0	-0.035	-0.024	14.483	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	88	LYS	1	0.917	0.970	14.363	0.026	0.026	0.000	0.000	0.000	0.000
58	A	89	LEU	0	-0.029	-0.002	13.757	0.043	0.043	0.000	0.000	0.000	0.000
59	A	90	VAL	0	0.018	-0.003	11.578	-0.050	-0.050	0.000	0.000	0.000	0.000
60	A	91	THR	0	-0.021	0.009	12.589	0.120	0.120	0.000	0.000	0.000	0.000
61	A	92	VAL	0	0.025	0.001	10.342	-0.071	-0.071	0.000	0.000	0.000	0.000
62	A	93	ASN	0	-0.023	-0.022	13.704	0.050	0.050	0.000	0.000	0.000	0.000
63	A	94	LEU	0	0.017	0.003	12.240	-0.041	-0.041	0.000	0.000	0.000	0.000
64	A	95	VAL	0	0.076	0.025	16.020	0.002	0.002	0.000	0.000	0.000	0.000
65	A	96	ASN	0	-0.039	-0.029	16.619	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	97	SER	0	-0.056	-0.017	17.375	0.020	0.020	0.000	0.000	0.000	0.000
67	A	98	GLU	-1	-0.769	-0.853	19.767	0.179	0.179	0.000	0.000	0.000	0.000
68	A	99	GLN	0	-0.048	-0.012	22.734	-0.020	-0.020	0.000	0.000	0.000	0.000
69	A	100	ASN	0	0.027	-0.002	24.945	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	101	GLN	0	0.025	-0.005	23.142	0.005	0.005	0.000	0.000	0.000	0.000
71	A	102	GLN	0	-0.038	-0.018	24.418	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	103	VAL	0	0.010	0.003	26.238	0.005	0.005	0.000	0.000	0.000	0.000
73	A	104	VAL	0	-0.020	-0.001	21.207	0.010	0.010	0.000	0.000	0.000	0.000
74	A	105	GLU	-1	-0.791	-0.901	24.445	0.014	0.014	0.000	0.000	0.000	0.000
75	A	106	ASP	-1	-0.896	-0.930	26.341	0.043	0.043	0.000	0.000	0.000	0.000
76	A	107	PHE	0	-0.039	-0.013	23.747	0.007	0.007	0.000	0.000	0.000	0.000
77	A	108	ILE	0	0.047	0.024	21.918	0.010	0.010	0.000	0.000	0.000	0.000
78	A	109	LYS	1	0.950	0.984	25.925	-0.029	-0.029	0.000	0.000	0.000	0.000
79	A	110	ALA	0	-0.048	-0.034	29.332	0.000	0.000	0.000	0.000	0.000	0.000
80	A	111	ASN	0	-0.145	-0.088	27.150	0.007	0.007	0.000	0.000	0.000	0.000
81	A	112	LYS	1	0.909	0.954	28.387	-0.064	-0.064	0.000	0.000	0.000	0.000
82	A	113	LEU	0	-0.034	-0.004	23.204	0.005	0.005	0.000	0.000	0.000	0.000
83	A	114	THR	0	-0.026	-0.026	24.785	-0.015	-0.015	0.000	0.000	0.000	0.000
84	A	115	PHE	0	-0.026	0.008	18.985	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	116	PRO	0	0.041	0.022	17.011	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	117	ILE	0	-0.043	-0.022	17.394	0.043	0.043	0.000	0.000	0.000	0.000
87	A	118	VAL	0	0.048	0.024	12.957	-0.035	-0.035	0.000	0.000	0.000	0.000
88	A	119	LEU	0	0.016	0.013	15.584	0.051	0.051	0.000	0.000	0.000	0.000
89	A	120	ASP	-1	-0.766	-0.899	11.685	-0.092	-0.092	0.000	0.000	0.000	0.000
90	A	121	SER	0	-0.031	-0.033	14.111	0.015	0.015	0.000	0.000	0.000	0.000
91	A	122	LYS	1	0.898	0.944	14.070	0.199	0.199	0.000	0.000	0.000	0.000
92	A	123	GLY	0	0.021	0.031	12.781	-0.025	-0.025	0.000	0.000	0.000	0.000
93	A	124	GLU	-1	-0.903	-0.965	8.630	-0.977	-0.977	0.000	0.000	0.000	0.000
94	A	125	LEU	0	0.022	0.030	7.025	-0.138	-0.138	0.000	0.000	0.000	0.000
95	A	126	MET	0	-0.008	-0.013	6.756	0.228	0.228	0.000	0.000	0.000	0.000
96	A	127	LYS	1	0.883	0.956	7.726	1.030	1.030	0.000	0.000	0.000	0.000
97	A	128	GLU	-1	-0.860	-0.945	2.371	-7.957	-6.141	2.617	-1.928	-2.506	-0.018
98	A	129	TYR	0	-0.003	0.003	2.313	-3.701	-1.312	4.458	-2.873	-3.974	-0.025
99	A	130	HIS	0	-0.034	-0.010	3.444	1.551	2.220	0.040	-0.149	-0.559	0.000
100	A	131	ILE	0	-0.015	-0.001	6.150	0.058	0.058	0.000	0.000	0.000	0.000
101	A	132	ILE	0	-0.015	-0.005	8.969	-0.265	-0.265	0.000	0.000	0.000	0.000
102	A	133	THR	0	-0.038	-0.021	11.984	-0.156	-0.156	0.000	0.000	0.000	0.000
103	A	134	ILE	0	-0.008	0.036	12.943	0.093	0.093	0.000	0.000	0.000	0.000
104	A	135	PRO	0	0.013	-0.018	15.457	-0.063	-0.063	0.000	0.000	0.000	0.000
105	A	136	THR	0	-0.037	-0.034	9.456	0.049	0.049	0.000	0.000	0.000	0.000
106	A	137	SER	0	-0.025	-0.013	10.815	-0.115	-0.115	0.000	0.000	0.000	0.000
107	A	138	PHE	0	0.044	0.019	6.241	0.236	0.236	0.000	0.000	0.000	0.000
108	A	139	LEU	0	-0.007	0.006	8.401	-0.262	-0.262	0.000	0.000	0.000	0.000
109	A	140	LEU	0	0.006	0.005	4.364	0.111	0.241	-0.001	-0.012	-0.117	0.000
110	A	141	ASN	0	0.015	-0.012	7.690	-0.224	-0.224	0.000	0.000	0.000	0.000
111	A	142	GLU	-1	-0.921	-0.970	8.490	-0.311	-0.311	0.000	0.000	0.000	0.000
112	A	143	LYS	1	0.887	0.941	8.301	0.308	0.308	0.000	0.000	0.000	0.000
113	A	144	GLY	0	0.010	-0.010	4.932	-0.385	-0.385	0.000	0.000	0.000	0.000
114	A	145	GLU	-1	-0.920	-0.944	3.082	-1.937	-0.964	0.101	-0.367	-0.707	-0.004
115	A	146	ILE	0	-0.005	-0.015	2.307	-1.139	-0.379	1.693	-0.405	-2.048	0.003
116	A	147	GLU	-1	-0.861	-0.937	4.907	0.268	0.279	-0.001	-0.004	-0.006	0.000
117	A	148	LYS	1	0.908	0.957	8.546	-0.678	-0.678	0.000	0.000	0.000	0.000
118	A	149	THR	0	0.048	0.023	7.431	0.444	0.444	0.000	0.000	0.000	0.000
119	A	150	LYS	1	0.886	0.948	9.517	-0.811	-0.811	0.000	0.000	0.000	0.000
120	A	151	ILE	0	0.051	0.034	11.719	0.011	0.011	0.000	0.000	0.000	0.000
121	A	152	GLY	0	-0.033	-0.022	14.237	-0.095	-0.095	0.000	0.000	0.000	0.000
122	A	153	PRO	0	-0.056	-0.039	16.725	0.026	0.026	0.000	0.000	0.000	0.000
123	A	154	MET	0	-0.028	0.005	15.353	0.045	0.045	0.000	0.000	0.000	0.000
124	A	155	THR	0	0.000	-0.029	19.186	-0.035	-0.035	0.000	0.000	0.000	0.000
125	A	156	ALA	0	0.071	0.017	20.723	0.020	0.020	0.000	0.000	0.000	0.000
126	A	157	GLU	-1	-0.922	-0.956	22.222	0.194	0.194	0.000	0.000	0.000	0.000
127	A	158	GLN	0	-0.023	-0.020	18.847	0.013	0.013	0.000	0.000	0.000	0.000
128	A	159	LEU	0	-0.021	-0.002	16.061	0.030	0.030	0.000	0.000	0.000	0.000
129	A	160	LYS	1	0.975	0.989	18.249	-0.161	-0.161	0.000	0.000	0.000	0.000
130	A	161	GLU	-1	-0.891	-0.944	18.297	0.373	0.373	0.000	0.000	0.000	0.000
131	A	162	TRP	0	-0.072	-0.040	11.876	0.065	0.065	0.000	0.000	0.000	0.000
132	A	163	THR	0	-0.063	-0.030	16.112	-0.016	-0.016	0.000	0.000	0.000	0.000
133	A	164	GLU	-1	-1.011	-0.993	18.359	0.182	0.182	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:PRO)