FMO DATABASE

FMODB ID: MN1ZZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-715362.112991
FMO2-HF: Nuclear repulsion	674036.121316
FMO2-HF: Total energy	-41325.991675
FMO2-MP2: Total energy	-41438.901564

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.
-30.794	-17.374	13.697	-12.084	-15.035	-0.058

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 : 0.000 / q_NPA : -0.001

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	-0.019	0.005	3.214	-2.803	-0.438	0.830	-1.215	-1.979	0.003
4	A	35	ALA	0	0.055	0.016	5.156	0.414	0.456	-0.001	-0.005	-0.036	0.000
5	A	36	PHE	0	-0.030	-0.038	8.520	-0.239	-0.239	0.000	0.000	0.000	0.000
6	A	37	LYS	1	0.855	0.912	11.047	0.674	0.674	0.000	0.000	0.000	0.000
7	A	38	ASP	-1	-0.743	-0.870	14.484	-0.644	-0.644	0.000	0.000	0.000	0.000
8	A	39	PRO	0	-0.028	-0.012	16.349	0.011	0.011	0.000	0.000	0.000	0.000
9	A	40	TYR	0	-0.020	-0.017	19.443	0.038	0.038	0.000	0.000	0.000	0.000
10	A	41	GLN	0	-0.054	-0.032	14.983	0.074	0.074	0.000	0.000	0.000	0.000
11	A	42	GLN	0	-0.033	-0.039	18.320	0.054	0.054	0.000	0.000	0.000	0.000
12	A	43	ASP	-1	-0.971	-0.964	20.557	-0.264	-0.264	0.000	0.000	0.000	0.000
13	A	44	LEU	0	-0.018	-0.015	20.854	0.027	0.027	0.000	0.000	0.000	0.000
14	A	45	GLY	0	0.014	0.024	18.733	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	46	ILE	0	-0.004	-0.006	14.528	-0.036	-0.036	0.000	0.000	0.000	0.000
16	A	47	GLY	0	-0.005	-0.008	12.362	-0.107	-0.107	0.000	0.000	0.000	0.000
17	A	48	GLU	-1	-0.734	-0.846	12.242	-0.709	-0.709	0.000	0.000	0.000	0.000
18	A	49	SER	0	-0.071	-0.034	13.532	-0.061	-0.061	0.000	0.000	0.000	0.000
19	A	50	ARG	1	0.864	0.925	7.015	1.812	1.812	0.000	0.000	0.000	0.000
20	A	51	ILE	0	-0.011	0.005	9.340	-0.403	-0.403	0.000	0.000	0.000	0.000
21	A	52	SER	0	0.000	-0.001	11.932	0.193	0.193	0.000	0.000	0.000	0.000
22	A	53	HIS	0	-0.025	-0.048	14.173	-0.053	-0.053	0.000	0.000	0.000	0.000
23	A	54	GLU	-1	-0.950	-0.950	17.011	-0.357	-0.357	0.000	0.000	0.000	0.000
24	A	55	ASN	0	-0.043	-0.024	13.101	-0.087	-0.087	0.000	0.000	0.000	0.000
25	A	56	GLY	0	0.032	0.042	13.617	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	57	THR	0	-0.030	-0.024	8.869	-0.161	-0.161	0.000	0.000	0.000	0.000
27	A	58	ILE	0	-0.007	-0.013	6.959	0.243	0.243	0.000	0.000	0.000	0.000
28	A	59	LEU	0	0.019	0.021	3.972	-1.180	-1.107	-0.001	-0.041	-0.031	0.000
29	A	60	CYS	0	-0.061	-0.013	2.740	1.399	2.583	0.169	-0.505	-0.848	0.004
30	A	61	SER	0	0.020	0.012	2.262	-4.593	-3.453	2.245	-1.822	-1.564	-0.025
31	A	62	LYS	1	0.854	0.902	2.141	-13.467	-10.298	4.547	-3.709	-4.008	0.016
32	A	63	GLY	0	0.044	0.016	3.504	-3.887	-3.903	0.027	0.360	-0.371	0.004
33	A	64	SER	0	-0.055	-0.008	3.089	-0.882	-0.420	0.035	-0.162	-0.335	0.001
34	A	65	THR	0	0.018	0.004	2.196	-7.599	-5.958	2.966	-2.214	-2.393	-0.032
35	A	67	TYR	0	-0.010	-0.013	5.148	0.669	0.716	-0.001	-0.001	-0.044	0.000
36	A	68	GLY	0	0.039	0.019	8.948	-0.164	-0.164	0.000	0.000	0.000	0.000
37	A	69	LEU	0	-0.029	-0.014	11.945	0.089	0.089	0.000	0.000	0.000	0.000
38	A	70	TRP	0	0.024	0.011	12.685	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	71	GLU	-1	-0.840	-0.894	18.769	-0.277	-0.277	0.000	0.000	0.000	0.000
40	A	72	LYS	1	0.837	0.921	22.552	0.197	0.197	0.000	0.000	0.000	0.000
41	A	73	SER	0	-0.018	-0.042	24.944	0.018	0.018	0.000	0.000	0.000	0.000
42	A	74	LYS	1	0.858	0.942	28.728	0.156	0.156	0.000	0.000	0.000	0.000
43	A	75	GLY	0	0.022	0.004	29.252	0.008	0.008	0.000	0.000	0.000	0.000
44	A	76	ASP	-1	-0.860	-0.918	26.681	-0.228	-0.228	0.000	0.000	0.000	0.000
45	A	77	ILE	0	-0.010	-0.019	20.927	0.002	0.002	0.000	0.000	0.000	0.000
46	A	78	ASN	0	-0.011	0.006	22.268	-0.022	-0.022	0.000	0.000	0.000	0.000
47	A	79	LEU	0	0.031	0.018	14.595	0.004	0.004	0.000	0.000	0.000	0.000
48	A	80	VAL	0	-0.010	0.002	18.246	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	81	LYS	1	0.809	0.883	14.404	0.606	0.606	0.000	0.000	0.000	0.000
50	A	82	GLN	0	-0.012	-0.005	10.621	0.042	0.042	0.000	0.000	0.000	0.000
51	A	83	GLY	0	0.028	0.020	8.587	0.080	0.080	0.000	0.000	0.000	0.000
52	A	85	TRP	0	0.006	0.005	6.319	0.574	0.574	0.000	0.000	0.000	0.000
53	A	86	SER	0	-0.037	-0.004	7.616	-0.018	-0.018	0.000	0.000	0.000	0.000
54	A	87	HIS	0	-0.040	-0.039	5.711	-0.131	-0.131	0.000	0.000	0.000	0.000
55	A	88	ILE	0	0.019	0.014	7.765	0.034	0.034	0.000	0.000	0.000	0.000
56	A	89	GLY	0	-0.030	-0.020	9.875	-0.067	-0.067	0.000	0.000	0.000	0.000
57	A	90	ASP	-1	-0.853	-0.917	10.896	-0.348	-0.348	0.000	0.000	0.000	0.000
58	A	91	PRO	0	-0.069	-0.051	13.376	0.036	0.036	0.000	0.000	0.000	0.000
59	A	92	GLN	0	-0.056	-0.032	14.496	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	93	GLU	-1	-0.797	-0.862	11.009	0.380	0.380	0.000	0.000	0.000	0.000
61	A	94	CYS	0	-0.031	-0.024	8.819	-0.067	-0.067	0.000	0.000	0.000	0.000
62	A	95	HIS	0	-0.040	-0.035	8.950	0.036	0.036	0.000	0.000	0.000	0.000
63	A	96	TYR	0	0.004	0.003	9.718	0.004	0.004	0.000	0.000	0.000	0.000
64	A	97	GLU	-1	-0.851	-0.911	8.476	0.310	0.310	0.000	0.000	0.000	0.000
65	A	98	GLU	-1	-0.894	-0.939	8.476	-0.236	-0.236	0.000	0.000	0.000	0.000
66	A	99	CYS	0	-0.072	-0.007	10.290	0.025	0.025	0.000	0.000	0.000	0.000
67	A	100	VAL	0	-0.009	-0.017	11.598	0.027	0.027	0.000	0.000	0.000	0.000
68	A	101	VAL	0	-0.025	-0.009	14.979	-0.025	-0.025	0.000	0.000	0.000	0.000
69	A	102	THR	0	0.024	0.006	17.505	0.023	0.023	0.000	0.000	0.000	0.000
70	A	103	THR	0	0.002	-0.005	20.500	-0.019	-0.019	0.000	0.000	0.000	0.000
71	A	104	THR	0	0.010	0.009	19.330	0.021	0.021	0.000	0.000	0.000	0.000
72	A	105	PRO	0	-0.007	0.000	22.136	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	106	PRO	0	0.066	0.024	19.296	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	107	SER	0	0.019	0.004	21.612	0.013	0.013	0.000	0.000	0.000	0.000
75	A	108	ILE	0	-0.031	-0.019	23.398	0.011	0.011	0.000	0.000	0.000	0.000
76	A	109	GLN	0	-0.033	0.004	25.856	0.015	0.015	0.000	0.000	0.000	0.000
77	A	110	ASN	0	0.018	0.010	25.915	0.012	0.012	0.000	0.000	0.000	0.000
78	A	111	GLY	0	0.046	0.031	25.397	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	112	THR	0	-0.048	-0.025	25.897	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	113	TYR	0	-0.042	-0.035	20.515	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	114	ARG	1	0.743	0.856	18.538	0.240	0.240	0.000	0.000	0.000	0.000
82	A	115	PHE	0	0.028	0.011	12.688	-0.027	-0.027	0.000	0.000	0.000	0.000
83	A	118	CYS	0	-0.036	0.012	5.287	0.150	0.150	0.000	0.000	0.000	0.000
84	A	119	SER	0	0.017	-0.012	5.029	-0.588	-0.588	0.000	0.000	0.000	0.000
85	A	120	THR	0	-0.011	-0.005	3.644	0.158	0.750	0.014	-0.227	-0.380	-0.001
86	A	121	ASP	-1	-0.782	-0.899	2.395	-0.508	2.415	2.841	-2.893	-2.872	-0.027
87	A	122	LEU	0	-0.022	-0.017	3.247	0.685	0.483	0.026	0.350	-0.174	-0.001
88	A	124	ASN	0	-0.006	-0.019	6.936	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	125	VAL	0	0.001	0.004	8.881	0.058	0.058	0.000	0.000	0.000	0.000
90	A	126	ASN	0	-0.046	-0.029	11.036	0.073	0.073	0.000	0.000	0.000	0.000
91	A	127	PHE	0	0.020	0.009	12.684	-0.029	-0.029	0.000	0.000	0.000	0.000
92	A	128	THR	0	0.015	0.012	15.154	0.049	0.049	0.000	0.000	0.000	0.000
93	A	129	GLU	-1	-0.820	-0.889	17.397	-0.185	-0.185	0.000	0.000	0.000	0.000
94	A	130	ASN	0	0.000	0.002	19.656	0.028	0.028	0.000	0.000	0.000	0.000
95	A	131	PHE	0	-0.017	-0.007	21.559	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)