FMO DATABASE

FMODB ID: LZL29

Calculation Name: 2BPS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BPS

Chain ID: A

ChEMBL ID:

UniProt ID: P71071

Base Structure: X-ray

Registration Date: 2023-06-21

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	81
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-557044.341756
FMO2-HF: Nuclear repulsion	524609.420108
FMO2-HF: Total energy	-32434.921648
FMO2-MP2: Total energy	-32529.508655

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:HIS)

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

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.
-2.22	2.638	2.964	-2.536	-5.282	-0.012

Interaction energy analysis for fragmet #1(A:-1:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.020

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

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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	1	SER	0	0.027	0.013	3.830	-0.199	2.165	-0.022	-1.188	-1.153	0.000
4	A	2	TYR	0	-0.056	-0.013	6.082	-0.869	-0.869	0.000	0.000	0.000	0.000
5	A	3	ILE	0	-0.009	0.014	9.043	0.097	0.097	0.000	0.000	0.000	0.000
6	A	4	ASP	-1	-0.792	-0.871	12.496	0.075	0.075	0.000	0.000	0.000	0.000
7	A	5	ILE	0	-0.029	-0.013	14.864	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	6	THR	0	0.004	-0.003	17.719	0.027	0.027	0.000	0.000	0.000	0.000
9	A	7	ILE	0	-0.044	-0.018	17.369	-0.049	-0.049	0.000	0.000	0.000	0.000
10	A	8	ASP	-1	-0.794	-0.917	21.385	-0.184	-0.184	0.000	0.000	0.000	0.000
11	A	9	LEU	0	-0.004	-0.007	23.241	-0.031	-0.031	0.000	0.000	0.000	0.000
12	A	10	LYS	1	0.969	0.988	26.287	0.216	0.216	0.000	0.000	0.000	0.000
13	A	11	HIS	0	-0.078	-0.033	27.997	0.002	0.002	0.000	0.000	0.000	0.000
14	A	12	TYR	0	-0.011	-0.022	25.503	-0.013	-0.013	0.000	0.000	0.000	0.000
15	A	13	ASN	0	-0.010	0.024	28.290	0.011	0.011	0.000	0.000	0.000	0.000
16	A	14	GLY	0	0.035	0.022	29.944	0.017	0.017	0.000	0.000	0.000	0.000
17	A	15	SER	0	-0.059	-0.041	27.672	0.008	0.008	0.000	0.000	0.000	0.000
18	A	16	VAL	0	-0.017	-0.028	25.114	-0.018	-0.018	0.000	0.000	0.000	0.000
19	A	17	PHE	0	-0.028	0.002	18.641	0.021	0.021	0.000	0.000	0.000	0.000
20	A	18	ASP	-1	-0.807	-0.888	19.616	-0.138	-0.138	0.000	0.000	0.000	0.000
21	A	19	LEU	0	-0.055	-0.035	13.700	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	20	ARG	1	0.866	0.921	11.236	-0.299	-0.299	0.000	0.000	0.000	0.000
23	A	21	LEU	0	-0.048	-0.020	9.616	-0.025	-0.025	0.000	0.000	0.000	0.000
24	A	22	SER	0	-0.020	-0.011	4.197	0.594	0.747	-0.001	-0.058	-0.093	0.000
25	A	23	ASP	-1	-0.812	-0.930	7.122	-1.253	-1.253	0.000	0.000	0.000	0.000
26	A	24	TYR	0	-0.024	-0.024	2.585	-4.062	-1.952	2.989	-1.281	-3.817	-0.012
27	A	25	HIS	0	-0.011	-0.012	5.176	-1.308	-1.185	-0.001	-0.004	-0.118	0.000
28	A	26	PRO	0	0.026	0.009	7.316	0.270	0.270	0.000	0.000	0.000	0.000
29	A	27	VAL	0	0.052	0.012	10.283	0.192	0.192	0.000	0.000	0.000	0.000
30	A	28	LYS	1	0.956	0.983	13.466	1.364	1.364	0.000	0.000	0.000	0.000
31	A	29	LYS	1	0.896	0.950	10.109	1.320	1.320	0.000	0.000	0.000	0.000
32	A	30	VAL	0	0.008	0.009	12.967	0.124	0.124	0.000	0.000	0.000	0.000
33	A	31	ILE	0	-0.007	-0.016	15.447	0.113	0.113	0.000	0.000	0.000	0.000
34	A	32	ASP	-1	-0.896	-0.939	14.944	-0.857	-0.857	0.000	0.000	0.000	0.000
35	A	33	ILE	0	-0.017	-0.020	13.075	0.077	0.077	0.000	0.000	0.000	0.000
36	A	34	ALA	0	-0.018	-0.002	17.406	0.077	0.077	0.000	0.000	0.000	0.000
37	A	35	TRP	0	-0.029	-0.024	20.437	0.048	0.048	0.000	0.000	0.000	0.000
38	A	36	GLN	0	-0.103	-0.030	17.268	-0.044	-0.044	0.000	0.000	0.000	0.000
39	A	37	ALA	0	-0.010	-0.005	20.109	0.039	0.039	0.000	0.000	0.000	0.000
40	A	38	GLN	0	0.039	0.026	22.034	0.041	0.041	0.000	0.000	0.000	0.000
41	A	39	SER	0	-0.016	-0.004	25.341	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	40	VAL	0	-0.018	-0.019	24.924	0.019	0.019	0.000	0.000	0.000	0.000
43	A	41	SER	0	-0.001	0.009	28.141	-0.013	-0.013	0.000	0.000	0.000	0.000
44	A	42	MET	0	-0.114	-0.022	28.126	0.012	0.012	0.000	0.000	0.000	0.000
45	A	43	PRO	0	-0.007	-0.006	26.109	0.012	0.012	0.000	0.000	0.000	0.000
46	A	44	PRO	0	0.067	0.007	22.409	0.015	0.015	0.000	0.000	0.000	0.000
47	A	45	ARG	1	0.944	0.967	25.020	0.338	0.338	0.000	0.000	0.000	0.000
48	A	46	GLU	-1	-0.894	-0.951	23.839	-0.493	-0.493	0.000	0.000	0.000	0.000
49	A	47	GLY	0	-0.009	-0.006	22.519	0.022	0.022	0.000	0.000	0.000	0.000
50	A	48	HIS	0	-0.034	-0.021	18.399	-0.052	-0.052	0.000	0.000	0.000	0.000
51	A	49	TRP	0	0.044	0.037	19.313	-0.079	-0.079	0.000	0.000	0.000	0.000
52	A	50	ILE	0	0.036	0.019	18.144	0.039	0.039	0.000	0.000	0.000	0.000
53	A	51	ARG	1	0.917	0.966	20.808	0.256	0.256	0.000	0.000	0.000	0.000
54	A	52	VAL	0	0.007	0.002	18.916	0.012	0.012	0.000	0.000	0.000	0.000
55	A	53	VAL	0	0.020	0.006	21.875	0.029	0.029	0.000	0.000	0.000	0.000
56	A	54	ASN	0	-0.017	-0.012	21.848	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	55	LYS	1	0.844	0.911	18.820	0.319	0.319	0.000	0.000	0.000	0.000
58	A	56	ASP	-1	-0.922	-0.942	24.347	-0.247	-0.247	0.000	0.000	0.000	0.000
59	A	57	LYS	1	0.955	0.993	19.661	0.478	0.478	0.000	0.000	0.000	0.000
60	A	58	VAL	0	-0.021	-0.012	21.877	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	59	PHE	0	-0.018	-0.019	16.566	-0.014	-0.014	0.000	0.000	0.000	0.000
62	A	60	SER	0	0.050	0.015	16.850	0.025	0.025	0.000	0.000	0.000	0.000
63	A	61	GLY	0	0.046	0.021	15.888	-0.091	-0.091	0.000	0.000	0.000	0.000
64	A	62	GLU	-1	-0.919	-0.983	13.319	-1.451	-1.451	0.000	0.000	0.000	0.000
65	A	63	CYS	0	-0.067	-0.016	11.833	-0.178	-0.178	0.000	0.000	0.000	0.000
66	A	64	LYS	1	0.928	0.994	4.240	5.199	5.307	-0.001	-0.005	-0.101	0.000
67	A	65	LEU	0	0.052	0.015	9.208	0.291	0.291	0.000	0.000	0.000	0.000
68	A	66	SER	0	0.066	0.031	7.559	0.003	0.003	0.000	0.000	0.000	0.000
69	A	67	ASP	-1	-0.945	-0.968	8.719	-2.047	-2.047	0.000	0.000	0.000	0.000
70	A	68	CYS	0	-0.109	-0.049	10.963	0.190	0.190	0.000	0.000	0.000	0.000
71	A	69	GLY	0	-0.027	-0.016	13.131	0.136	0.136	0.000	0.000	0.000	0.000
72	A	70	ILE	0	-0.049	-0.019	13.827	0.126	0.126	0.000	0.000	0.000	0.000
73	A	71	THR	0	-0.056	-0.044	13.772	0.016	0.016	0.000	0.000	0.000	0.000
74	A	72	ASN	0	0.059	0.000	15.057	0.008	0.008	0.000	0.000	0.000	0.000
75	A	73	GLY	0	-0.028	0.009	17.327	0.007	0.007	0.000	0.000	0.000	0.000
76	A	74	ASP	-1	-0.810	-0.892	18.168	-0.330	-0.330	0.000	0.000	0.000	0.000
77	A	75	ARG	1	0.888	0.941	20.320	0.187	0.187	0.000	0.000	0.000	0.000
78	A	76	LEU	0	-0.026	-0.025	16.036	-0.022	-0.022	0.000	0.000	0.000	0.000
79	A	77	GLU	-1	-0.896	-0.953	20.784	-0.257	-0.257	0.000	0.000	0.000	0.000
80	A	78	ILE	0	-0.001	0.000	20.205	-0.035	-0.035	0.000	0.000	0.000	0.000
81	A	79	LEU	0	-0.005	0.001	22.937	0.027	0.027	0.000	0.000	0.000	0.000

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