FMO DATABASE

FMODB ID: YQK62

Calculation Name: 1EER-A-Xray308

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	164
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1624490.572537
FMO2-HF: Nuclear repulsion	1560042.591549
FMO2-HF: Total energy	-64447.980988
FMO2-MP2: Total energy	-64636.753081

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.
-3.016	-0.77399999999998	8.176	-5.997	-4.42	-0.075

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 : 1 / q_Mulliken : 0.831 / q_NPA : 0.904

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	0.080	0.065	3.854	5.134	6.118	0.000	-0.323	-0.661	0.001
4	A	4	ARG	1	0.914	0.937	5.229	46.714	46.714	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.039	0.011	7.749	0.606	0.606	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.073	0.056	10.803	1.670	1.670	0.000	0.000	0.000	0.000
7	A	161	CYS	0	-0.120	-0.042	6.745	-5.133	-5.133	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.865	-0.914	9.613	-22.632	-22.632	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.018	-0.029	11.515	2.159	2.159	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.898	0.957	14.413	17.564	17.564	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.000	0.021	13.597	1.243	1.243	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.010	-0.007	15.574	0.995	0.995	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.916	-0.982	17.236	-14.112	-14.112	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.946	0.992	19.767	14.246	14.246	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.035	0.010	18.919	0.531	0.531	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.038	-0.011	19.955	0.652	0.652	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.010	-0.008	23.491	0.702	0.702	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.878	-0.944	25.631	-11.708	-11.708	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.003	-0.004	26.557	0.531	0.531	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.936	0.981	27.790	11.035	11.035	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.796	-0.875	29.526	-9.054	-9.054	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.031	0.014	31.209	0.379	0.379	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.980	-0.996	31.851	-9.442	-9.442	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.872	0.926	33.402	9.493	9.493	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.008	0.035	35.352	0.381	0.381	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.040	-0.033	36.048	0.260	0.260	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.101	-0.093	37.254	0.256	0.256	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.001	0.007	40.051	0.205	0.205	0.000	0.000	0.000	0.000
29	A	33	CYS	0	-0.105	-0.051	41.499	-0.083	-0.083	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.004	0.003	43.561	0.144	0.144	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.904	-0.955	46.644	-6.564	-6.564	0.000	0.000	0.000	0.000
32	A	32	HIS	0	-0.039	-0.034	46.392	0.161	0.161	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.060	0.035	42.660	-0.266	-0.266	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.046	-0.023	38.270	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.049	-0.030	42.804	0.149	0.149	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.782	-0.895	41.582	-7.677	-7.677	0.000	0.000	0.000	0.000
37	A	38	LYN	0	-0.019	-0.009	41.415	-0.175	-0.175	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.015	0.021	35.660	-0.093	-0.093	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.007	-0.018	33.913	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.036	-0.007	32.099	-0.209	-0.209	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.034	0.021	27.610	0.112	0.112	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.792	-0.905	29.061	-10.249	-10.249	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.065	-0.041	26.870	-0.435	-0.435	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.871	0.945	26.776	9.723	9.723	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.056	0.019	22.794	-0.229	-0.229	0.000	0.000	0.000	0.000
46	A	47	ASN	0	0.003	0.013	25.949	0.098	0.098	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.080	0.014	21.119	-0.224	-0.224	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.021	0.005	23.942	-0.524	-0.524	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.037	-0.008	25.358	-0.215	-0.215	0.000	0.000	0.000	0.000
50	A	51	TRP	0	0.002	-0.008	17.832	0.085	0.085	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.930	0.962	19.781	13.338	13.338	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.910	0.961	20.475	11.473	11.473	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.055	0.007	20.785	0.203	0.203	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.859	-0.932	18.497	-16.462	-16.462	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.022	-0.003	13.183	0.199	0.199	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.072	0.053	15.929	-0.303	-0.303	0.000	0.000	0.000	0.000
57	A	58	GLN	0	0.074	0.030	16.838	0.202	0.202	0.000	0.000	0.000	0.000
58	A	59	GLN	0	-0.068	-0.042	15.650	-0.329	-0.329	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.004	0.009	15.561	0.352	0.352	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.004	0.010	17.203	0.449	0.449	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.899	-0.954	20.811	-12.886	-12.886	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.058	-0.029	17.927	0.609	0.609	0.000	0.000	0.000	0.000
63	A	64	TRP	0	0.018	0.011	18.437	0.181	0.181	0.000	0.000	0.000	0.000
64	A	65	GLN	0	0.046	0.014	20.576	0.363	0.363	0.000	0.000	0.000	0.000
65	A	66	GLY	0	-0.007	-0.006	23.797	0.553	0.553	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.001	-0.011	20.336	0.469	0.469	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.000	0.010	24.036	0.368	0.368	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.054	0.033	25.943	0.405	0.405	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.019	-0.027	25.614	0.445	0.445	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.021	-0.014	25.899	0.255	0.255	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.930	-0.956	28.549	-10.124	-10.124	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.010	-0.005	31.504	0.409	0.409	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.048	-0.032	29.767	0.322	0.322	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.008	0.004	30.297	0.275	0.275	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.882	0.935	33.823	8.321	8.321	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.034	0.013	36.028	0.282	0.282	0.000	0.000	0.000	0.000
77	A	78	GLN	0	-0.005	-0.010	34.411	0.135	0.135	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.034	-0.021	37.382	0.233	0.233	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.064	-0.043	39.967	0.235	0.235	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.019	-0.006	39.364	0.168	0.168	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.019	0.005	41.258	0.146	0.146	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.865	0.950	42.998	7.415	7.415	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.015	0.006	46.132	0.030	0.030	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.016	0.015	47.853	-0.056	-0.056	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.015	-0.016	46.834	0.131	0.131	0.000	0.000	0.000	0.000
86	A	87	PRO	0	-0.007	0.022	47.458	-0.059	-0.059	0.000	0.000	0.000	0.000
87	A	88	TRP	0	-0.006	-0.028	41.112	-0.113	-0.113	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.831	-0.906	43.131	-7.308	-7.308	0.000	0.000	0.000	0.000
89	A	90	PRO	0	-0.038	-0.020	39.971	-0.194	-0.194	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.027	-0.009	38.303	-0.310	-0.310	0.000	0.000	0.000	0.000
91	A	92	GLN	0	0.071	0.047	37.150	-0.069	-0.069	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.092	0.035	34.713	-0.317	-0.317	0.000	0.000	0.000	0.000
93	A	94	HIS	0	-0.050	-0.029	32.931	-0.551	-0.551	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.025	0.010	32.118	-0.427	-0.427	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.859	-0.923	32.312	-9.500	-9.500	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.883	0.932	28.930	10.110	10.110	0.000	0.000	0.000	0.000
97	A	98	ALA	0	0.021	0.035	27.858	-0.555	-0.555	0.000	0.000	0.000	0.000
98	A	99	VAL	0	0.017	0.017	27.670	-0.519	-0.519	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.077	-0.038	26.847	-0.592	-0.592	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.034	-0.006	24.080	-0.574	-0.574	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.010	-0.004	22.926	-0.864	-0.864	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.975	1.017	23.110	11.090	11.090	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.019	-0.012	20.253	-0.591	-0.591	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.004	-0.001	18.631	-1.156	-1.156	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.006	-0.005	18.177	-0.969	-0.969	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.059	-0.027	16.992	-0.482	-0.482	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.014	-0.028	14.310	-1.103	-1.103	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.028	0.002	13.593	-1.848	-1.848	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.922	0.979	13.880	15.312	15.312	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.045	-0.004	11.556	-0.796	-0.796	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.013	-0.014	8.639	-2.768	-2.768	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.010	0.008	10.265	-1.544	-1.544	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.008	0.006	12.274	1.497	1.497	0.000	0.000	0.000	0.000
114	A	115	GLN	0	0.025	-0.002	15.164	0.554	0.554	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.952	0.981	14.649	20.762	20.762	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.883	-0.966	13.675	-22.008	-22.008	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.032	-0.010	16.520	0.989	0.989	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.009	-0.011	19.550	0.786	0.786	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.020	-0.015	19.145	0.214	0.214	0.000	0.000	0.000	0.000
120	A	121	ASN	0	-0.035	-0.008	19.258	0.441	0.441	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.032	-0.017	21.258	0.497	0.497	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.945	-0.957	24.197	-12.692	-12.692	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.002	0.013	26.109	0.481	0.481	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.032	-0.017	28.762	0.010	0.010	0.000	0.000	0.000	0.000
125	A	126	SER	0	0.025	0.003	29.730	-0.165	-0.165	0.000	0.000	0.000	0.000
126	A	127	ALA	0	-0.039	-0.014	31.867	0.340	0.340	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.027	0.003	33.142	-0.200	-0.200	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.035	0.011	32.666	-0.081	-0.081	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.034	-0.002	33.496	-0.035	-0.035	0.000	0.000	0.000	0.000
130	A	131	ARG	1	0.900	0.928	32.569	9.224	9.224	0.000	0.000	0.000	0.000
131	A	132	THR	0	-0.008	0.007	34.730	0.097	0.097	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.015	0.020	32.523	0.248	0.248	0.000	0.000	0.000	0.000
133	A	134	THR	0	0.049	0.017	35.647	-0.123	-0.123	0.000	0.000	0.000	0.000
134	A	135	ALA	0	-0.052	-0.048	36.752	-0.010	-0.010	0.000	0.000	0.000	0.000
135	A	136	ASP	-1	-0.811	-0.888	38.578	-7.562	-7.562	0.000	0.000	0.000	0.000
136	A	137	THR	0	0.006	0.006	40.128	0.083	0.083	0.000	0.000	0.000	0.000
137	A	138	PHE	0	0.074	0.015	37.194	-0.295	-0.295	0.000	0.000	0.000	0.000
138	A	139	ARG	1	0.993	1.003	36.726	7.441	7.441	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.822	0.926	35.979	8.432	8.432	0.000	0.000	0.000	0.000
140	A	141	LEU	0	0.040	0.031	32.938	-0.311	-0.311	0.000	0.000	0.000	0.000
141	A	142	PHE	0	0.054	0.003	31.897	-0.465	-0.465	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.976	1.000	31.391	8.604	8.604	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.057	-0.027	29.851	-0.363	-0.363	0.000	0.000	0.000	0.000
144	A	145	TYR	0	0.066	0.026	25.949	-0.611	-0.611	0.000	0.000	0.000	0.000
145	A	146	SER	0	0.035	0.010	26.602	-0.751	-0.751	0.000	0.000	0.000	0.000
146	A	147	ASN	0	0.007	-0.017	26.023	-0.614	-0.614	0.000	0.000	0.000	0.000
147	A	148	PHE	0	0.004	0.009	22.032	-0.335	-0.335	0.000	0.000	0.000	0.000
148	A	149	LEU	0	-0.026	-0.016	21.922	-0.758	-0.758	0.000	0.000	0.000	0.000
149	A	150	ARG	1	0.912	0.949	20.967	10.756	10.756	0.000	0.000	0.000	0.000
150	A	151	GLY	0	0.015	0.019	22.236	-0.171	-0.171	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.910	0.952	20.518	12.298	12.298	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.008	0.044	17.556	-0.875	-0.875	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.960	0.989	14.978	18.437	18.437	0.000	0.000	0.000	0.000
154	A	155	LEU	0	-0.050	-0.036	15.863	-1.249	-1.249	0.000	0.000	0.000	0.000
155	A	156	TYR	0	0.049	0.026	12.840	-1.081	-1.081	0.000	0.000	0.000	0.000
156	A	157	THR	0	-0.014	-0.016	12.018	-1.871	-1.871	0.000	0.000	0.000	0.000
157	A	158	GLY	0	-0.056	-0.032	11.082	-2.436	-2.436	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.954	-0.984	10.685	-24.556	-24.556	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.069	0.037	9.274	-2.701	-2.701	0.000	0.000	0.000	0.000
160	A	162	ARG	1	0.883	0.958	5.166	17.087	17.048	0.000	-0.007	0.046	0.000
161	A	163	THR	0	0.017	-0.004	4.031	6.373	6.901	0.001	-0.238	-0.290	-0.001
162	A	164	GLY	0	-0.109	-0.055	1.984	-41.334	-40.016	8.164	-6.096	-3.386	-0.074
163	A	165	ASP	-1	-0.878	-0.948	3.130	-51.056	-51.605	0.011	0.667	-0.129	-0.001
164	A	166	ARG	0	0.014	0.024	5.853	8.770	8.770	0.000	0.000	0.000	0.000

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