FMO DATABASE

FMODB ID: 6N33Z

Calculation Name: 5H77-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5H77

Chain ID: A

ChEMBL ID:

UniProt ID:

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	84
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-517634.403384
FMO2-HF: Nuclear repulsion	484574.923418
FMO2-HF: Total energy	-33059.479965
FMO2-MP2: Total energy	-33158.7009

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:4:PRO)

Summations of interaction energy for fragment #1(A:4:PRO)

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.
0.088	2.383	2.406	-1.371	-3.33	0.003

Interaction energy analysis for fragmet #1(A:4:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.045 / q_NPA : 0.003

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	6	GLY	0	0.073	0.032	3.822	-0.344	1.201	-0.013	-0.609	-0.923	0.003
4	A	7	LEU	0	-0.023	-0.005	2.271	-0.189	0.344	2.419	-0.719	-2.234	0.000
5	A	8	THR	0	0.028	0.008	4.263	0.683	0.900	0.000	-0.043	-0.173	0.000
6	A	9	GLU	-1	-0.851	-0.938	6.969	-1.684	-1.684	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.034	0.004	7.010	0.281	0.281	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.006	-0.010	6.589	0.235	0.235	0.000	0.000	0.000	0.000
9	A	12	GLN	0	0.004	0.006	9.777	0.236	0.236	0.000	0.000	0.000	0.000
10	A	13	GLY	0	0.009	0.011	12.210	0.119	0.119	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.014	-0.010	12.764	0.076	0.076	0.000	0.000	0.000	0.000
12	A	15	THR	0	0.003	-0.011	13.347	0.084	0.084	0.000	0.000	0.000	0.000
13	A	16	VAL	0	-0.035	-0.018	15.815	0.062	0.062	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.904	-0.961	17.655	-0.278	-0.278	0.000	0.000	0.000	0.000
15	A	18	VAL	0	0.001	0.011	17.589	0.039	0.039	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.055	-0.023	20.080	0.034	0.034	0.000	0.000	0.000	0.000
17	A	20	ARG	1	0.901	0.947	21.887	0.324	0.324	0.000	0.000	0.000	0.000
18	A	21	GLN	0	-0.032	-0.025	22.030	0.033	0.033	0.000	0.000	0.000	0.000
19	A	22	GLN	0	-0.091	-0.030	24.029	0.023	0.023	0.000	0.000	0.000	0.000
20	A	23	PRO	0	-0.008	0.019	21.622	0.015	0.015	0.000	0.000	0.000	0.000
21	A	24	PRO	0	-0.001	-0.010	24.905	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	25	ASP	-1	-0.827	-0.925	23.043	-0.158	-0.158	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.017	-0.001	18.998	-0.013	-0.013	0.000	0.000	0.000	0.000
24	A	27	VAL	0	0.016	0.003	18.385	-0.032	-0.032	0.000	0.000	0.000	0.000
25	A	28	GLU	-1	-0.907	-0.939	19.374	-0.164	-0.164	0.000	0.000	0.000	0.000
26	A	29	PHE	0	0.016	0.005	18.596	-0.011	-0.011	0.000	0.000	0.000	0.000
27	A	30	ALA	0	-0.027	-0.013	15.470	-0.031	-0.031	0.000	0.000	0.000	0.000
28	A	31	VAL	0	0.016	0.007	16.563	-0.029	-0.029	0.000	0.000	0.000	0.000
29	A	32	GLU	-1	-0.901	-0.911	18.290	-0.191	-0.191	0.000	0.000	0.000	0.000
30	A	33	TYR	0	-0.021	-0.026	13.486	0.013	0.013	0.000	0.000	0.000	0.000
31	A	34	PHE	0	0.005	-0.021	11.160	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.034	-0.042	14.900	0.005	0.005	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.928	0.977	17.545	0.267	0.267	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.001	0.001	12.140	0.000	0.000	0.000	0.000	0.000	0.000
35	A	38	ARG	1	0.907	0.975	14.334	0.166	0.166	0.000	0.000	0.000	0.000
36	A	39	GLN	0	0.029	0.000	15.218	0.026	0.026	0.000	0.000	0.000	0.000
37	A	40	GLN	0	-0.006	0.004	16.427	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.955	0.973	8.589	0.633	0.633	0.000	0.000	0.000	0.000
39	A	42	ALA	0	0.043	0.027	15.463	0.025	0.025	0.000	0.000	0.000	0.000
40	A	43	PHE	0	0.006	-0.010	18.153	0.021	0.021	0.000	0.000	0.000	0.000
41	A	44	TYR	0	-0.021	-0.009	15.816	0.010	0.010	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.955	-0.988	15.410	-0.117	-0.117	0.000	0.000	0.000	0.000
43	A	46	ILE	0	-0.014	-0.011	18.597	0.022	0.022	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.051	-0.036	21.643	0.016	0.016	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.035	0.005	19.163	0.020	0.020	0.000	0.000	0.000	0.000
46	A	49	LEU	0	-0.016	0.001	21.662	0.016	0.016	0.000	0.000	0.000	0.000
47	A	50	PRO	0	-0.018	-0.007	23.925	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	51	ASN	0	0.033	0.005	26.849	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	52	LEU	0	0.001	0.027	26.464	0.004	0.004	0.000	0.000	0.000	0.000
50	A	53	ASN	0	0.013	0.005	29.825	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	54	GLU	-1	-0.911	-0.970	30.991	-0.067	-0.067	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.881	-0.941	31.468	-0.052	-0.052	0.000	0.000	0.000	0.000
53	A	56	GLN	0	-0.048	-0.033	31.855	0.002	0.002	0.000	0.000	0.000	0.000
54	A	57	ARG	1	0.854	0.930	25.819	0.071	0.071	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.022	-0.017	28.001	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	59	ALA	0	0.036	0.030	29.647	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	60	PHE	0	0.042	0.010	25.778	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	61	ILE	0	-0.004	0.000	24.524	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	62	GLN	0	0.013	-0.003	26.442	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	63	SER	0	-0.034	-0.026	27.766	0.002	0.002	0.000	0.000	0.000	0.000
61	A	64	LEU	0	-0.044	-0.015	21.407	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.860	0.944	24.880	0.094	0.094	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.940	-0.949	27.012	-0.082	-0.082	0.000	0.000	0.000	0.000
64	A	67	ASP	-1	-0.898	-0.988	26.362	-0.089	-0.089	0.000	0.000	0.000	0.000
65	A	68	PRO	0	-0.029	0.003	21.212	0.001	0.001	0.000	0.000	0.000	0.000
66	A	69	SER	0	-0.033	-0.001	21.766	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	70	GLN	0	-0.022	-0.026	23.724	0.012	0.012	0.000	0.000	0.000	0.000
68	A	71	SER	0	0.042	0.023	19.515	0.001	0.001	0.000	0.000	0.000	0.000
69	A	72	ALA	0	0.015	0.003	19.595	0.002	0.002	0.000	0.000	0.000	0.000
70	A	73	ASN	0	0.015	0.005	20.970	0.016	0.016	0.000	0.000	0.000	0.000
71	A	74	LEU	0	0.043	0.026	23.552	0.005	0.005	0.000	0.000	0.000	0.000
72	A	75	LEU	0	-0.008	0.013	17.685	0.003	0.003	0.000	0.000	0.000	0.000
73	A	76	ALA	0	-0.013	-0.013	21.937	0.009	0.009	0.000	0.000	0.000	0.000
74	A	77	GLU	-1	-0.899	-0.950	23.954	0.001	0.001	0.000	0.000	0.000	0.000
75	A	78	ALA	0	-0.002	-0.002	24.198	0.002	0.002	0.000	0.000	0.000	0.000
76	A	79	LYS	1	0.916	0.953	19.261	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.911	0.965	24.641	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	81	LEU	0	0.000	0.000	27.915	0.002	0.002	0.000	0.000	0.000	0.000
79	A	82	ASN	0	0.074	0.030	24.613	0.006	0.006	0.000	0.000	0.000	0.000
80	A	83	ASP	-1	-0.989	-0.997	24.460	0.017	0.017	0.000	0.000	0.000	0.000
81	A	84	ALA	0	-0.045	-0.030	28.008	0.007	0.007	0.000	0.000	0.000	0.000
82	A	85	GLN	0	-0.061	-0.003	31.249	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	86	ALA	0	-0.017	-0.019	31.997	0.000	0.000	0.000	0.000	0.000	0.000
84	A	87	PRO	0	-0.049	-0.012	31.811	0.006	0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)