FMO DATABASE

FMODB ID: R5Q28

Calculation Name: 1EER-A-Xray372

Preferred Name: Erythropoietin receptor

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1EER

Chain ID: A

ChEMBL ID: CHEMBL1817

UniProt ID: P19235

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	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	164
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1624468.2251
FMO2-HF: Nuclear repulsion	1560020.041836
FMO2-HF: Total energy	-64448.183265
FMO2-MP2: Total energy	-64636.963925

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:1:ALA)

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

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.
-7.093	-7.541	9.208	-4.543	-4.218	-0.025

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.048 / q_NPA : 0.022

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	3	PRO	0	0.071	0.059	3.836	-0.170	1.470	-0.006	-0.757	-0.877	0.005
4	A	4	ARG	1	0.899	0.928	5.219	2.641	2.641	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.033	0.006	7.749	-0.005	-0.005	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.068	0.052	10.803	0.160	0.160	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.114	-0.038	6.673	-0.626	-0.626	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.863	-0.913	9.613	-0.237	-0.237	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.017	-0.030	11.528	0.039	0.039	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.893	0.955	14.430	0.211	0.211	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.003	0.022	13.611	0.034	0.034	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.010	-0.006	15.574	0.028	0.028	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.917	-0.983	17.236	-0.165	-0.165	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.944	0.991	19.781	0.270	0.270	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.035	0.010	18.935	0.016	0.016	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.037	-0.010	19.973	0.022	0.022	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.012	-0.009	23.491	0.023	0.023	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.876	-0.944	25.631	-0.197	-0.197	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.008	-0.006	26.557	0.015	0.015	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.945	0.984	27.795	0.134	0.134	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.801	-0.876	29.543	-0.097	-0.097	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.033	0.015	31.209	0.009	0.009	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.983	-0.998	31.863	-0.115	-0.115	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.872	0.927	33.419	0.107	0.107	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.006	0.036	35.369	0.009	0.009	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.040	-0.032	36.048	0.005	0.005	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.103	-0.094	37.269	0.005	0.005	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.000	0.007	40.069	0.005	0.005	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.100	-0.050	41.499	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.006	0.003	43.561	0.002	0.002	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.905	-0.956	46.563	-0.069	-0.069	0.000	0.000	0.000	0.000
32	A	32	HIS	0	-0.039	-0.034	46.391	0.002	0.002	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.059	0.035	42.561	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.046	-0.023	38.165	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.050	-0.031	42.693	0.003	0.003	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.783	-0.894	41.456	-0.108	-0.108	0.000	0.000	0.000	0.000
37	A	38	LYN	0	-0.023	-0.010	41.308	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.015	0.022	35.543	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.010	-0.017	33.800	0.002	0.002	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.036	-0.007	31.999	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.035	0.021	27.511	0.006	0.006	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.794	-0.905	28.970	-0.150	-0.150	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.065	-0.042	26.796	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.873	0.946	26.717	0.131	0.131	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.058	0.020	22.765	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	47	ASN	0	0.005	0.014	25.911	0.015	0.015	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.080	0.014	21.118	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.024	0.003	23.947	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.037	-0.008	25.362	0.001	0.001	0.000	0.000	0.000	0.000
50	A	51	TRP	0	0.003	-0.008	17.785	0.008	0.008	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.933	0.963	19.781	0.090	0.090	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.911	0.960	20.485	0.106	0.106	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.059	0.006	20.748	0.008	0.008	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.864	-0.933	18.452	-0.275	-0.275	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.023	-0.003	13.148	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.071	0.053	15.848	-0.045	-0.045	0.000	0.000	0.000	0.000
57	A	58	GLN	0	0.074	0.030	16.762	-0.018	-0.018	0.000	0.000	0.000	0.000
58	A	59	GLN	0	-0.072	-0.044	15.606	-0.048	-0.048	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.011	0.011	15.460	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.003	0.010	17.101	0.006	0.006	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.905	-0.957	20.704	-0.239	-0.239	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.055	-0.027	17.826	0.023	0.023	0.000	0.000	0.000	0.000
63	A	64	TRP	0	0.024	0.013	18.413	0.000	0.000	0.000	0.000	0.000	0.000
64	A	65	GLN	0	0.044	0.013	20.450	0.017	0.017	0.000	0.000	0.000	0.000
65	A	66	GLY	0	-0.013	-0.008	23.684	0.022	0.022	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.003	-0.010	20.212	0.021	0.021	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.000	0.010	23.915	0.015	0.015	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.055	0.032	25.809	0.017	0.017	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.018	-0.026	25.507	0.018	0.018	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.024	-0.014	25.790	0.011	0.011	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.931	-0.957	28.435	-0.188	-0.188	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.007	-0.004	31.378	0.015	0.015	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.045	-0.031	29.650	0.012	0.012	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.013	0.003	30.409	0.010	0.010	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.881	0.934	33.814	0.128	0.128	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.034	0.013	35.903	0.009	0.009	0.000	0.000	0.000	0.000
77	A	78	GLN	0	-0.006	-0.010	34.402	0.003	0.003	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.033	-0.021	37.357	0.007	0.007	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.063	-0.044	40.006	0.006	0.006	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.018	-0.005	39.365	0.005	0.005	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.019	0.004	41.248	0.004	0.004	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.867	0.951	42.989	0.099	0.099	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.014	0.006	46.152	0.001	0.001	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.016	0.014	47.853	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.014	-0.016	46.834	0.004	0.004	0.000	0.000	0.000	0.000
86	A	87	PRO	0	-0.007	0.022	47.458	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	TRP	0	-0.004	-0.026	41.113	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.836	-0.907	43.146	-0.081	-0.081	0.000	0.000	0.000	0.000
89	A	90	PRO	0	-0.037	-0.019	39.977	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.019	-0.006	38.303	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	92	GLN	0	0.061	0.044	37.150	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.090	0.035	34.729	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	94	HIS	0	-0.047	-0.028	32.931	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.023	0.010	32.118	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.860	-0.924	32.312	-0.150	-0.150	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.883	0.933	28.946	0.141	0.141	0.000	0.000	0.000	0.000
97	A	98	ALA	0	0.021	0.034	27.858	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	99	VAL	0	0.026	0.020	27.670	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.087	-0.042	26.864	-0.025	-0.025	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.036	-0.004	24.089	-0.023	-0.023	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.007	-0.005	22.926	-0.040	-0.040	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.976	1.017	23.135	0.203	0.203	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.020	-0.012	20.245	-0.027	-0.027	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.007	0.001	18.631	-0.063	-0.063	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.010	-0.006	18.170	-0.064	-0.064	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.056	-0.027	16.984	-0.032	-0.032	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.012	-0.027	14.301	-0.067	-0.067	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.027	0.003	13.714	-0.143	-0.143	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.922	0.978	13.882	0.395	0.395	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.046	-0.005	11.573	-0.043	-0.043	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.003	-0.009	8.503	-0.241	-0.241	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.007	0.008	10.151	-0.126	-0.126	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.008	0.005	12.342	0.138	0.138	0.000	0.000	0.000	0.000
114	A	115	GLN	0	0.025	-0.001	15.028	0.050	0.050	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.953	0.981	14.726	0.586	0.586	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.888	-0.969	13.572	-0.669	-0.669	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.036	-0.011	16.395	0.065	0.065	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.005	-0.009	19.426	0.041	0.041	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.020	-0.015	19.028	0.013	0.013	0.000	0.000	0.000	0.000
120	A	121	ASN	0	-0.034	-0.009	19.180	0.023	0.023	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.031	-0.017	21.156	0.025	0.025	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.950	-0.958	24.085	-0.218	-0.218	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.004	0.014	25.992	0.019	0.019	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.030	-0.017	28.658	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	126	SER	0	0.023	0.002	29.634	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	127	ALA	0	-0.038	-0.012	31.773	0.008	0.008	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.027	0.004	33.046	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.035	0.010	32.566	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.034	-0.003	33.405	0.000	0.000	0.000	0.000	0.000	0.000
130	A	131	ARG	1	0.898	0.927	32.486	0.129	0.129	0.000	0.000	0.000	0.000
131	A	132	THR	0	-0.006	0.008	34.633	0.002	0.002	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.016	0.020	32.439	0.009	0.009	0.000	0.000	0.000	0.000
133	A	134	THR	0	0.050	0.017	35.545	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	135	ALA	0	-0.053	-0.048	36.658	0.002	0.002	0.000	0.000	0.000	0.000
135	A	136	ASP	-1	-0.811	-0.889	38.480	-0.095	-0.095	0.000	0.000	0.000	0.000
136	A	137	THR	0	0.004	0.006	40.030	0.003	0.003	0.000	0.000	0.000	0.000
137	A	138	PHE	0	0.078	0.017	37.129	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	139	ARG	1	0.989	1.001	36.634	0.082	0.082	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.824	0.926	35.893	0.114	0.114	0.000	0.000	0.000	0.000
140	A	141	LEU	0	0.037	0.030	32.834	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	142	PHE	0	0.058	0.004	31.897	-0.014	-0.014	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.972	0.999	31.310	0.108	0.108	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.056	-0.027	29.761	-0.007	-0.007	0.000	0.000	0.000	0.000
144	A	145	TYR	0	0.067	0.027	25.884	-0.021	-0.021	0.000	0.000	0.000	0.000
145	A	146	SER	0	0.036	0.011	26.517	-0.025	-0.025	0.000	0.000	0.000	0.000
146	A	147	ASN	0	0.009	-0.017	25.958	-0.012	-0.012	0.000	0.000	0.000	0.000
147	A	148	PHE	0	0.004	0.010	21.929	-0.004	-0.004	0.000	0.000	0.000	0.000
148	A	149	LEU	0	-0.025	-0.015	21.839	-0.029	-0.029	0.000	0.000	0.000	0.000
149	A	150	ARG	1	0.914	0.949	20.900	0.135	0.135	0.000	0.000	0.000	0.000
150	A	151	GLY	0	0.010	0.018	22.197	0.008	0.008	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.909	0.952	20.469	0.231	0.231	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.007	0.043	17.474	-0.039	-0.039	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.961	0.988	14.995	0.351	0.351	0.000	0.000	0.000	0.000
154	A	155	LEU	0	-0.051	-0.036	15.820	-0.045	-0.045	0.000	0.000	0.000	0.000
155	A	156	TYR	0	0.049	0.026	12.729	-0.047	-0.047	0.000	0.000	0.000	0.000
156	A	157	THR	0	-0.017	-0.017	11.939	-0.111	-0.111	0.000	0.000	0.000	0.000
157	A	158	GLY	0	-0.054	-0.030	11.028	-0.158	-0.158	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.959	-0.987	10.681	-0.429	-0.429	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.066	0.033	9.216	-0.075	-0.075	0.000	0.000	0.000	0.000
160	A	162	ARG	1	0.881	0.957	5.152	-0.410	-0.445	-0.001	-0.005	0.041	0.000
161	A	163	THR	0	-0.024	-0.027	4.017	0.879	1.353	0.000	-0.200	-0.274	-0.001
162	A	164	GLY	0	-0.025	0.000	1.956	-8.458	-10.334	9.215	-4.369	-2.971	-0.030
163	A	165	ASP	-1	-0.871	-0.943	3.244	-0.110	-0.761	0.000	0.788	-0.137	0.001
164	A	166	ARG	1	0.929	0.972	6.332	-0.360	-0.360	0.000	0.000	0.000	0.000

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