FMO DATABASE

FMODB ID: K3K53

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1628953.247786
FMO2-HF: Nuclear repulsion	1564503.113221
FMO2-HF: Total energy	-64450.134566
FMO2-MP2: Total energy	-64638.746261

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.
-4.414	-7.199	11.161	-3.954	-4.422	-0.036

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 : 0.030 / q_NPA : 0.007

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	0.027	0.026	3.914	0.194	1.587	-0.006	-0.666	-0.721	0.004
4	A	4	ARG	1	0.919	0.947	4.547	2.706	2.856	-0.001	-0.011	-0.138	0.000
5	A	5	LEU	0	0.054	0.011	8.286	0.000	0.000	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.014	0.013	11.211	0.116	0.116	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.067	-0.019	6.926	-0.611	-0.611	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.830	-0.898	10.121	-0.293	-0.293	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.002	-0.031	11.963	0.054	0.054	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.818	0.883	14.569	0.278	0.278	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.001	0.011	14.565	0.034	0.034	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.009	0.006	15.651	0.031	0.031	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.844	-0.903	17.525	-0.201	-0.201	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.898	0.930	20.059	0.284	0.284	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.003	-0.010	19.457	0.025	0.025	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.035	-0.007	20.266	0.020	0.020	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.004	0.002	23.736	0.023	0.023	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.758	-0.846	25.996	-0.196	-0.196	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.010	0.002	26.674	0.014	0.014	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.828	0.893	27.770	0.155	0.155	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.786	-0.866	29.515	-0.104	-0.104	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.043	0.017	31.544	0.010	0.010	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.858	-0.890	31.608	-0.135	-0.135	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.833	0.901	33.702	0.116	0.116	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.005	0.009	35.632	0.009	0.009	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.014	-0.024	36.485	0.005	0.005	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.050	-0.048	37.566	0.005	0.005	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.017	-0.001	40.130	0.004	0.004	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.034	-0.004	41.891	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.019	0.001	43.991	0.002	0.002	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.815	-0.918	46.390	-0.074	-0.074	0.000	0.000	0.000	0.000
32	A	32	HIS	0	-0.088	-0.037	46.225	0.001	0.001	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.027	0.016	42.690	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.035	-0.024	38.553	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.058	-0.032	42.895	0.003	0.003	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.783	-0.879	41.607	-0.107	-0.107	0.000	0.000	0.000	0.000
37	A	38	LYN	0	-0.002	-0.005	41.889	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.009	0.024	36.135	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.022	-0.001	34.637	0.001	0.001	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.020	-0.005	32.541	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.017	0.019	27.828	0.006	0.006	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.740	-0.850	29.556	-0.156	-0.156	0.000	0.000	0.000	0.000
43	A	44	THR	0	0.027	0.011	27.033	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.820	0.918	26.677	0.151	0.151	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.060	0.014	22.812	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	47	ASN	0	0.025	0.025	25.993	0.011	0.011	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.079	0.014	21.718	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.013	0.013	23.870	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.034	0.001	25.228	0.002	0.002	0.000	0.000	0.000	0.000
50	A	51	TRP	0	0.031	0.006	17.814	0.011	0.011	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.906	0.955	19.889	0.116	0.116	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.906	0.948	20.956	0.123	0.123	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.062	0.004	20.432	0.006	0.006	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.836	-0.898	18.174	-0.283	-0.283	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.012	-0.008	12.919	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.088	0.043	16.308	-0.043	-0.043	0.000	0.000	0.000	0.000
57	A	58	GLN	0	0.015	0.003	17.334	0.011	0.011	0.000	0.000	0.000	0.000
58	A	59	GLN	0	-0.026	-0.040	15.984	-0.046	-0.046	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.013	0.015	15.725	0.001	0.001	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.004	0.011	17.535	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.892	-0.929	21.207	-0.234	-0.234	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.050	-0.028	18.024	0.020	0.020	0.000	0.000	0.000	0.000
63	A	64	TRP	0	0.020	0.003	18.482	0.002	0.002	0.000	0.000	0.000	0.000
64	A	65	GLN	0	0.037	0.017	20.852	0.011	0.011	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.005	0.005	24.093	0.024	0.024	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.006	-0.004	20.644	0.020	0.020	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.002	0.014	24.328	0.015	0.015	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.065	0.039	26.256	0.015	0.015	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.035	-0.032	26.400	0.016	0.016	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.032	-0.023	26.343	0.009	0.009	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.925	-0.956	28.966	-0.175	-0.175	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.006	-0.002	32.015	0.013	0.013	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.018	-0.020	30.665	0.012	0.012	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.011	0.000	30.818	0.009	0.009	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.836	0.910	34.334	0.128	0.128	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.050	0.019	36.484	0.008	0.008	0.000	0.000	0.000	0.000
77	A	78	GLN	0	-0.038	-0.036	34.405	0.004	0.004	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.018	-0.013	37.715	0.008	0.008	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.079	-0.029	40.198	0.007	0.007	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.004	0.003	39.217	0.004	0.004	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.035	0.001	41.408	0.004	0.004	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.866	0.924	43.305	0.101	0.101	0.000	0.000	0.000	0.000
83	A	84	SER	0	-0.006	0.002	46.636	0.001	0.001	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.017	0.006	48.748	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	86	GLN	0	0.006	0.008	46.778	0.004	0.004	0.000	0.000	0.000	0.000
86	A	87	PRO	0	0.003	0.011	47.819	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	TRP	0	0.009	-0.015	41.379	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.826	-0.911	43.078	-0.085	-0.085	0.000	0.000	0.000	0.000
89	A	90	PRO	0	-0.045	-0.024	39.921	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	91	LEU	0	0.011	0.011	38.461	-0.008	-0.008	0.000	0.000	0.000	0.000
91	A	92	GLN	0	0.017	0.000	37.328	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.048	0.016	35.251	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	94	HIS	0	-0.041	-0.036	32.906	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.010	0.007	32.504	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.807	-0.878	32.456	-0.151	-0.151	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.841	0.907	29.257	0.149	0.149	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.004	0.010	28.143	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	99	VAL	0	0.023	0.016	27.906	-0.021	-0.021	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.022	-0.024	26.346	-0.015	-0.015	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.007	0.011	24.214	-0.023	-0.023	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.011	0.003	23.140	-0.039	-0.039	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.979	1.013	23.445	0.190	0.190	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.026	-0.014	20.617	-0.022	-0.022	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.001	-0.004	18.623	-0.056	-0.056	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.004	-0.011	18.560	-0.063	-0.063	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.060	-0.034	17.764	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.011	-0.021	14.597	-0.057	-0.057	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.010	0.006	13.991	-0.144	-0.144	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.886	0.942	14.637	0.394	0.394	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.037	-0.012	11.921	-0.035	-0.035	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.026	-0.010	8.842	-0.210	-0.210	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.042	0.027	10.432	-0.127	-0.127	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.024	0.017	12.421	0.142	0.142	0.000	0.000	0.000	0.000
114	A	115	GLN	0	0.047	0.031	15.149	0.059	0.059	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.891	0.946	14.959	0.474	0.474	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.841	-0.912	13.628	-0.700	-0.700	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.013	-0.014	16.372	0.063	0.063	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.015	-0.021	19.569	0.039	0.039	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.004	-0.010	19.546	0.014	0.014	0.000	0.000	0.000	0.000
120	A	121	ASN	0	-0.082	-0.049	19.507	0.028	0.028	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.047	-0.032	21.631	0.024	0.024	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.909	-0.936	23.614	-0.216	-0.216	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.005	0.015	26.083	0.019	0.019	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.024	-0.017	28.504	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	126	SER	0	0.003	0.000	29.678	0.003	0.003	0.000	0.000	0.000	0.000
126	A	127	ALA	0	-0.012	-0.007	31.827	0.007	0.007	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.034	0.017	33.150	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.018	-0.013	32.842	0.000	0.000	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.039	-0.007	33.701	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	131	ARG	1	0.854	0.914	32.796	0.137	0.137	0.000	0.000	0.000	0.000
131	A	132	THR	0	-0.004	-0.009	35.333	0.001	0.001	0.000	0.000	0.000	0.000
132	A	133	ILE	0	0.004	0.027	33.001	0.007	0.007	0.000	0.000	0.000	0.000
133	A	134	THR	0	0.046	0.025	36.024	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	135	ALA	0	-0.053	-0.037	36.532	0.002	0.002	0.000	0.000	0.000	0.000
135	A	136	ASP	-1	-0.734	-0.850	38.572	-0.104	-0.104	0.000	0.000	0.000	0.000
136	A	137	THR	0	0.003	-0.008	40.405	0.004	0.004	0.000	0.000	0.000	0.000
137	A	138	PHE	0	0.070	0.029	37.206	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	139	ARG	1	0.881	0.961	36.902	0.082	0.082	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.739	0.863	36.807	0.110	0.110	0.000	0.000	0.000	0.000
140	A	141	LEU	0	0.050	0.028	33.262	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	142	PHE	0	0.042	0.004	32.161	-0.015	-0.015	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.934	0.978	31.565	0.112	0.112	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.007	-0.005	29.833	-0.008	-0.008	0.000	0.000	0.000	0.000
144	A	145	TYR	0	0.057	0.022	25.710	-0.021	-0.021	0.000	0.000	0.000	0.000
145	A	146	SER	0	-0.024	-0.035	26.804	-0.024	-0.024	0.000	0.000	0.000	0.000
146	A	147	ASN	0	0.009	-0.012	26.427	-0.014	-0.014	0.000	0.000	0.000	0.000
147	A	148	PHE	0	-0.003	0.006	22.344	-0.006	-0.006	0.000	0.000	0.000	0.000
148	A	149	LEU	0	-0.035	-0.008	22.103	-0.031	-0.031	0.000	0.000	0.000	0.000
149	A	150	ARG	1	0.898	0.934	21.211	0.151	0.151	0.000	0.000	0.000	0.000
150	A	151	GLY	0	0.011	0.024	22.433	0.007	0.007	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.802	0.869	20.595	0.217	0.217	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.029	0.030	17.918	-0.038	-0.038	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.955	0.995	15.192	0.395	0.395	0.000	0.000	0.000	0.000
154	A	155	LEU	0	-0.034	-0.018	15.950	-0.047	-0.047	0.000	0.000	0.000	0.000
155	A	156	TYR	0	0.017	-0.011	13.364	-0.058	-0.058	0.000	0.000	0.000	0.000
156	A	157	THR	0	-0.046	-0.032	12.346	-0.127	-0.127	0.000	0.000	0.000	0.000
157	A	158	GLY	0	-0.020	-0.018	11.098	-0.189	-0.189	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.835	-0.895	11.248	-0.460	-0.460	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.064	0.032	9.352	-0.112	-0.112	0.000	0.000	0.000	0.000
160	A	162	ARG	1	0.794	0.908	5.629	-0.165	-0.165	0.000	0.000	0.000	0.000
161	A	163	THR	0	-0.010	-0.016	4.064	0.647	1.269	0.000	-0.335	-0.287	-0.001
162	A	164	GLY	0	0.041	0.002	1.916	-8.786	-11.816	10.884	-4.881	-2.973	-0.039
163	A	165	ASP	-1	-0.918	-0.944	2.814	2.284	0.364	0.284	1.939	-0.303	0.000
164	A	166	ARG	1	0.853	0.938	5.477	-0.112	-0.112	0.000	0.000	0.000	0.000

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