FMO DATABASE

FMODB ID: 98VQ2

Calculation Name: 2HLQ-A-Xray372

Preferred Name: Bone morphogenetic protein receptor type-2

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2HLQ

Chain ID: A

ChEMBL ID: CHEMBL5467

UniProt ID: Q13873

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptHSide
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	95
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-715423.283787
FMO2-HF: Nuclear repulsion	674097.473763
FMO2-HF: Total energy	-41325.810024
FMO2-MP2: Total energy	-41438.692597

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:32:ALA)

Summations of interaction energy for fragment #1(A:32: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.
-29.164	-15.259	12.857	-12.498	-14.262	-0.064

Interaction energy analysis for fragmet #1(A:32:ALA)

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 : -0.010

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	34	CYS	0	-0.028	-0.006	3.252	-3.041	-0.349	0.906	-1.413	-2.185	0.003
4	A	35	ALA	0	0.061	0.024	5.261	0.374	0.412	-0.001	-0.004	-0.032	0.000
5	A	36	PHE	0	0.001	-0.018	8.601	-0.245	-0.245	0.000	0.000	0.000	0.000
6	A	37	LYS	1	0.839	0.901	11.032	0.666	0.666	0.000	0.000	0.000	0.000
7	A	38	ASP	-1	-0.741	-0.876	14.363	-0.663	-0.663	0.000	0.000	0.000	0.000
8	A	39	PRO	0	-0.034	-0.012	16.416	0.015	0.015	0.000	0.000	0.000	0.000
9	A	40	TYR	0	-0.031	-0.021	19.431	0.038	0.038	0.000	0.000	0.000	0.000
10	A	41	GLN	0	-0.055	-0.036	15.110	0.058	0.058	0.000	0.000	0.000	0.000
11	A	42	GLN	0	-0.033	-0.032	18.438	0.054	0.054	0.000	0.000	0.000	0.000
12	A	43	ASP	-1	-0.980	-0.965	20.582	-0.251	-0.251	0.000	0.000	0.000	0.000
13	A	44	LEU	0	-0.001	-0.011	20.890	0.020	0.020	0.000	0.000	0.000	0.000
14	A	45	GLY	0	0.035	0.036	18.653	0.014	0.014	0.000	0.000	0.000	0.000
15	A	46	ILE	0	-0.011	-0.014	14.264	-0.028	-0.028	0.000	0.000	0.000	0.000
16	A	47	GLY	0	-0.016	-0.018	12.257	-0.077	-0.077	0.000	0.000	0.000	0.000
17	A	48	GLU	-1	-0.718	-0.829	12.323	-0.608	-0.608	0.000	0.000	0.000	0.000
18	A	49	SER	0	-0.065	-0.033	13.456	-0.045	-0.045	0.000	0.000	0.000	0.000
19	A	50	ARG	1	0.853	0.914	7.186	1.643	1.643	0.000	0.000	0.000	0.000
20	A	51	ILE	0	-0.007	0.012	9.573	-0.308	-0.308	0.000	0.000	0.000	0.000
21	A	52	SER	0	-0.003	0.012	12.073	0.182	0.182	0.000	0.000	0.000	0.000
22	A	53	HIS	0	-0.017	-0.049	14.148	-0.061	-0.061	0.000	0.000	0.000	0.000
23	A	54	GLU	-1	-1.003	-0.986	17.008	-0.257	-0.257	0.000	0.000	0.000	0.000
24	A	55	ASN	0	-0.010	0.000	12.848	-0.095	-0.095	0.000	0.000	0.000	0.000
25	A	56	GLY	0	0.043	0.043	13.625	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	57	THR	0	-0.053	-0.041	8.684	-0.142	-0.142	0.000	0.000	0.000	0.000
27	A	58	ILE	0	0.000	-0.010	7.070	0.216	0.216	0.000	0.000	0.000	0.000
28	A	59	LEU	0	-0.001	0.015	4.009	-0.958	-0.886	-0.001	-0.035	-0.036	0.000
29	A	60	CYS	0	-0.056	-0.008	2.804	1.410	2.445	0.089	-0.434	-0.690	0.002
30	A	61	SER	0	0.031	0.022	2.907	-1.750	-0.561	0.197	-0.872	-0.514	-0.009
31	A	62	LYS	1	0.953	0.963	1.962	-14.340	-11.668	3.872	-3.092	-3.452	0.010
32	A	63	GLY	0	0.040	0.007	3.877	-2.706	-2.433	0.005	-0.128	-0.150	0.001
33	A	64	SER	0	-0.030	-0.013	3.098	-0.954	-0.382	0.036	-0.203	-0.404	0.001
34	A	65	THR	0	-0.006	0.006	2.101	-8.043	-6.858	4.053	-2.573	-2.665	-0.035
35	A	67	TYR	0	-0.002	-0.008	5.161	0.614	0.662	-0.001	-0.001	-0.047	0.000
36	A	68	GLY	0	0.035	0.018	8.911	-0.113	-0.113	0.000	0.000	0.000	0.000
37	A	69	LEU	0	-0.040	-0.014	11.803	0.082	0.082	0.000	0.000	0.000	0.000
38	A	70	TRP	0	0.032	0.011	12.459	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	71	GLU	-1	-0.835	-0.905	18.440	-0.302	-0.302	0.000	0.000	0.000	0.000
40	A	72	LYS	1	0.844	0.926	22.149	0.220	0.220	0.000	0.000	0.000	0.000
41	A	73	SER	0	0.015	-0.029	24.794	0.017	0.017	0.000	0.000	0.000	0.000
42	A	74	LYS	1	0.866	0.961	28.565	0.155	0.155	0.000	0.000	0.000	0.000
43	A	75	GLY	0	0.024	0.026	28.647	0.009	0.009	0.000	0.000	0.000	0.000
44	A	76	ASP	-1	-0.888	-0.952	26.992	-0.220	-0.220	0.000	0.000	0.000	0.000
45	A	77	ILE	0	-0.014	-0.014	20.665	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	78	ASN	0	-0.007	-0.004	22.100	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	79	LEU	0	0.026	0.021	14.605	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	80	VAL	0	-0.016	-0.002	17.646	0.014	0.014	0.000	0.000	0.000	0.000
49	A	81	LYS	1	0.835	0.894	14.243	0.621	0.621	0.000	0.000	0.000	0.000
50	A	82	GLN	0	-0.033	-0.018	10.294	0.046	0.046	0.000	0.000	0.000	0.000
51	A	83	GLY	0	0.037	0.023	8.522	0.096	0.096	0.000	0.000	0.000	0.000
52	A	85	TRP	0	-0.005	-0.012	6.400	0.563	0.563	0.000	0.000	0.000	0.000
53	A	86	SER	0	-0.022	0.008	7.906	0.080	0.080	0.000	0.000	0.000	0.000
54	A	87	HIS	0	-0.079	-0.047	6.115	-0.261	-0.261	0.000	0.000	0.000	0.000
55	A	88	ILE	0	0.022	0.010	7.660	0.115	0.115	0.000	0.000	0.000	0.000
56	A	89	GLY	0	-0.054	-0.029	9.747	-0.043	-0.043	0.000	0.000	0.000	0.000
57	A	90	ASP	-1	-0.851	-0.914	11.067	-0.511	-0.511	0.000	0.000	0.000	0.000
58	A	91	PRO	0	-0.070	-0.046	13.432	0.029	0.029	0.000	0.000	0.000	0.000
59	A	92	GLN	0	-0.048	-0.025	14.633	0.008	0.008	0.000	0.000	0.000	0.000
60	A	93	GLU	-1	-0.796	-0.863	11.053	0.086	0.086	0.000	0.000	0.000	0.000
61	A	94	CYS	0	-0.043	-0.022	8.393	-0.060	-0.060	0.000	0.000	0.000	0.000
62	A	95	HIS	0	-0.017	-0.037	8.735	0.051	0.051	0.000	0.000	0.000	0.000
63	A	96	TYR	0	0.008	0.021	10.050	0.088	0.088	0.000	0.000	0.000	0.000
64	A	97	GLU	-1	-0.859	-0.934	8.091	0.024	0.024	0.000	0.000	0.000	0.000
65	A	98	GLU	-1	-0.902	-0.945	8.020	-0.293	-0.293	0.000	0.000	0.000	0.000
66	A	99	CYS	0	-0.084	-0.032	9.970	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	100	VAL	0	0.010	0.000	11.379	0.056	0.056	0.000	0.000	0.000	0.000
68	A	101	VAL	0	-0.043	-0.015	14.946	-0.026	-0.026	0.000	0.000	0.000	0.000
69	A	102	THR	0	0.039	0.009	17.456	0.030	0.030	0.000	0.000	0.000	0.000
70	A	103	THR	0	0.000	-0.010	20.085	-0.017	-0.017	0.000	0.000	0.000	0.000
71	A	104	THR	0	0.015	0.003	19.377	0.024	0.024	0.000	0.000	0.000	0.000
72	A	105	PRO	0	-0.012	0.012	22.100	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	106	PRO	0	0.076	0.023	19.108	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	107	SER	0	0.027	0.009	21.652	0.018	0.018	0.000	0.000	0.000	0.000
75	A	108	ILE	0	-0.051	-0.031	23.389	0.014	0.014	0.000	0.000	0.000	0.000
76	A	109	GLN	0	-0.034	0.011	25.622	0.017	0.017	0.000	0.000	0.000	0.000
77	A	110	ASN	0	0.024	0.015	25.939	0.015	0.015	0.000	0.000	0.000	0.000
78	A	111	GLY	0	0.044	0.024	25.208	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	112	THR	0	-0.046	-0.025	25.462	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	113	TYR	0	-0.018	-0.010	20.128	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	114	ARG	1	0.730	0.850	18.278	0.271	0.271	0.000	0.000	0.000	0.000
82	A	115	PHE	0	0.031	0.010	12.347	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	118	CYS	0	-0.030	0.013	5.049	0.228	0.228	0.000	0.000	0.000	0.000
84	A	119	SER	0	0.037	0.003	4.660	-0.699	-0.639	-0.001	-0.012	-0.046	0.000
85	A	120	THR	0	-0.005	0.003	3.070	-1.061	0.128	0.141	-0.566	-0.764	-0.005
86	A	121	ASP	-1	-0.818	-0.933	2.373	0.256	3.320	3.543	-3.502	-3.105	-0.032
87	A	122	LEU	0	-0.044	-0.030	3.269	0.573	0.389	0.019	0.337	-0.172	0.000
88	A	124	ASN	0	-0.011	-0.023	6.854	0.035	0.035	0.000	0.000	0.000	0.000
89	A	125	VAL	0	0.000	0.003	8.793	0.052	0.052	0.000	0.000	0.000	0.000
90	A	126	ASN	0	-0.042	-0.031	11.062	0.071	0.071	0.000	0.000	0.000	0.000
91	A	127	PHE	0	0.006	0.012	12.634	-0.022	-0.022	0.000	0.000	0.000	0.000
92	A	128	THR	0	0.019	0.017	15.023	0.055	0.055	0.000	0.000	0.000	0.000
93	A	129	GLU	-1	-0.833	-0.910	17.167	-0.219	-0.219	0.000	0.000	0.000	0.000
94	A	130	ASN	0	0.010	0.004	19.249	0.033	0.033	0.000	0.000	0.000	0.000
95	A	131	PHE	0	-0.031	-0.005	21.065	0.011	0.011	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:32:ALA)