FMO DATABASE

FMODB ID: 72JJK

Calculation Name: 5HIZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HIZ

Chain ID: A

ChEMBL ID:

UniProt ID: P0C6Y4

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	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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-710953.714687
FMO2-HF: Nuclear repulsion	672790.230786
FMO2-HF: Total energy	-38163.483901
FMO2-MP2: Total energy	-38276.273978

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:7:GLY)

Summations of interaction energy for fragment #1(A:7:GLY)

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.
1.122	2.265	0.022	-0.416	-0.749	0

Interaction energy analysis for fragmet #1(A:7:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.037 / q_NPA : 0.006

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].
3	A	9	LEU	0	0.008	0.018	3.863	1.226	2.162	-0.006	-0.345	-0.585
4	A	10	LYS	1	0.976	0.993	5.637	-0.462	-0.462	0.000	0.000	0.000
5	A	11	GLN	0	0.016	-0.005	9.354	0.089	0.089	0.000	0.000	0.000
6	A	12	ARG	1	0.825	0.890	12.193	-0.205	-0.205	0.000	0.000	0.000
7	A	13	SER	0	0.007	0.014	15.688	-0.013	-0.013	0.000	0.000	0.000
8	A	14	ILE	0	0.005	0.013	18.255	0.014	0.014	0.000	0.000	0.000
9	A	15	LYS	1	0.866	0.912	20.462	-0.061	-0.061	0.000	0.000	0.000
10	A	16	ALA	0	-0.006	-0.002	21.658	0.013	0.013	0.000	0.000	0.000
11	A	17	GLU	-1	-0.789	-0.884	23.720	0.073	0.073	0.000	0.000	0.000
12	A	18	GLY	0	0.016	-0.012	25.690	0.005	0.005	0.000	0.000	0.000
13	A	19	ASP	-1	-0.978	-0.981	28.020	0.039	0.039	0.000	0.000	0.000
14	A	20	GLY	0	0.023	0.011	31.169	-0.002	-0.002	0.000	0.000	0.000
15	A	21	ILE	0	0.028	0.027	28.374	-0.001	-0.001	0.000	0.000	0.000
16	A	22	VAL	0	0.033	0.015	27.595	0.005	0.005	0.000	0.000	0.000
17	A	23	GLY	0	-0.056	-0.027	25.895	-0.009	-0.009	0.000	0.000	0.000
18	A	24	GLU	-1	-0.808	-0.871	22.662	0.050	0.050	0.000	0.000	0.000
19	A	25	GLY	0	0.011	-0.005	19.998	-0.006	-0.006	0.000	0.000	0.000
20	A	26	LYS	1	0.877	0.928	15.135	0.021	0.021	0.000	0.000	0.000
21	A	27	ALA	0	0.028	0.023	14.418	-0.002	-0.002	0.000	0.000	0.000
22	A	28	LEU	0	0.017	0.013	9.025	-0.013	-0.013	0.000	0.000	0.000
23	A	29	TYR	0	-0.040	-0.022	9.511	0.008	0.008	0.000	0.000	0.000
24	A	30	ASN	0	-0.014	-0.023	6.042	-0.021	-0.021	0.000	0.000	0.000
25	A	31	ASN	0	-0.016	-0.001	8.532	-0.113	-0.113	0.000	0.000	0.000
26	A	32	GLU	-1	-0.792	-0.875	7.762	2.158	2.158	0.000	0.000	0.000
27	A	33	GLY	0	-0.032	-0.003	11.215	-0.138	-0.138	0.000	0.000	0.000
28	A	34	GLY	0	0.046	0.005	11.798	0.108	0.108	0.000	0.000	0.000
29	A	35	ARG	1	0.964	0.979	14.623	-0.451	-0.451	0.000	0.000	0.000
30	A	36	THR	0	0.018	0.014	13.246	0.163	0.163	0.000	0.000	0.000
31	A	37	PHE	0	0.011	-0.003	11.813	-0.096	-0.096	0.000	0.000	0.000
32	A	38	MET	0	-0.006	0.011	10.700	0.133	0.133	0.000	0.000	0.000
33	A	39	TYR	0	-0.021	-0.028	4.494	0.126	0.181	-0.001	-0.002	-0.052
34	A	40	ALA	0	0.005	-0.012	10.166	-0.056	-0.056	0.000	0.000	0.000
35	A	41	PHE	0	0.006	-0.004	12.372	-0.004	-0.004	0.000	0.000	0.000
36	A	42	ILE	0	0.054	0.035	12.915	-0.017	-0.017	0.000	0.000	0.000
37	A	43	SER	0	-0.005	0.002	16.841	-0.001	-0.001	0.000	0.000	0.000
38	A	44	ASP	-1	-0.802	-0.901	20.603	-0.043	-0.043	0.000	0.000	0.000
39	A	45	LYS	1	0.888	0.949	23.765	-0.019	-0.019	0.000	0.000	0.000
40	A	46	PRO	0	-0.015	0.009	24.279	0.004	0.004	0.000	0.000	0.000
41	A	47	ASP	-1	-0.869	-0.954	25.718	0.020	0.020	0.000	0.000	0.000
42	A	48	LEU	0	-0.053	-0.010	22.454	0.005	0.005	0.000	0.000	0.000
43	A	49	ARG	1	0.844	0.891	23.998	-0.076	-0.076	0.000	0.000	0.000
44	A	50	VAL	0	-0.015	-0.013	22.430	0.012	0.012	0.000	0.000	0.000
45	A	51	VAL	0	-0.014	-0.010	18.554	-0.010	-0.010	0.000	0.000	0.000
46	A	52	LYS	1	0.890	0.941	21.420	-0.085	-0.085	0.000	0.000	0.000
47	A	53	TRP	0	-0.038	-0.031	14.203	0.000	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.859	-0.919	20.542	0.143	0.143	0.000	0.000	0.000
49	A	55	PHE	0	-0.055	-0.044	16.224	0.019	0.019	0.000	0.000	0.000
50	A	56	ASP	-1	-0.880	-0.941	18.084	0.320	0.320	0.000	0.000	0.000
51	A	57	GLY	0	0.019	0.022	21.598	-0.025	-0.025	0.000	0.000	0.000
52	A	58	GLY	0	-0.057	-0.036	21.817	0.019	0.019	0.000	0.000	0.000
53	A	59	CYM	-1	-0.860	-0.889	22.146	0.150	0.150	0.000	0.000	0.000
54	A	60	ASN	0	-0.099	-0.082	20.502	0.016	0.016	0.000	0.000	0.000
55	A	61	THR	0	0.068	0.024	21.904	-0.004	-0.004	0.000	0.000	0.000
56	A	62	ILE	0	-0.028	0.000	16.821	0.017	0.017	0.000	0.000	0.000
57	A	63	GLU	-1	-0.799	-0.877	20.181	0.090	0.090	0.000	0.000	0.000
58	A	64	LEU	0	-0.080	-0.039	17.497	0.017	0.017	0.000	0.000	0.000
59	A	65	GLU	-1	-0.839	-0.913	17.121	0.101	0.101	0.000	0.000	0.000
60	A	66	PRO	0	0.024	-0.003	19.916	-0.004	-0.004	0.000	0.000	0.000
61	A	67	PRO	0	-0.028	0.006	19.586	-0.001	-0.001	0.000	0.000	0.000
62	A	68	ARG	1	0.878	0.933	17.680	0.038	0.038	0.000	0.000	0.000
63	A	69	LYS	1	0.946	0.955	19.118	0.011	0.011	0.000	0.000	0.000
64	A	70	PHE	0	-0.028	-0.024	16.267	-0.005	-0.005	0.000	0.000	0.000
65	A	71	LEU	0	0.058	0.043	20.717	0.004	0.004	0.000	0.000	0.000
66	A	72	VAL	0	-0.004	-0.017	18.384	-0.016	-0.016	0.000	0.000	0.000
67	A	73	ASP	-1	-0.892	-0.958	21.495	-0.087	-0.087	0.000	0.000	0.000
68	A	74	SER	0	-0.015	0.023	23.379	-0.009	-0.009	0.000	0.000	0.000
69	A	75	PRO	0	0.026	0.002	25.167	0.005	0.005	0.000	0.000	0.000
70	A	76	ASN	0	-0.079	-0.060	27.662	0.003	0.003	0.000	0.000	0.000
71	A	77	GLY	0	0.003	0.024	29.990	0.005	0.005	0.000	0.000	0.000
72	A	78	ALA	0	0.046	0.026	25.921	-0.002	-0.002	0.000	0.000	0.000
73	A	79	GLN	0	0.008	0.028	24.525	0.007	0.007	0.000	0.000	0.000
74	A	80	ILE	0	-0.031	-0.025	23.778	-0.008	-0.008	0.000	0.000	0.000
75	A	81	LYS	1	0.826	0.907	19.441	0.058	0.058	0.000	0.000	0.000
76	A	82	TYR	0	0.001	-0.009	20.458	-0.002	-0.002	0.000	0.000	0.000
77	A	83	LEU	0	0.007	-0.002	12.975	0.003	0.003	0.000	0.000	0.000
78	A	84	TYR	0	-0.012	-0.009	16.340	0.003	0.003	0.000	0.000	0.000
79	A	85	PHE	0	0.018	0.026	10.919	0.014	0.014	0.000	0.000	0.000
80	A	86	VAL	0	0.046	0.024	13.062	-0.018	-0.018	0.000	0.000	0.000
81	A	87	ARG	1	0.925	0.957	15.400	-0.107	-0.107	0.000	0.000	0.000
82	A	88	ASN	0	-0.041	-0.016	16.420	0.014	0.014	0.000	0.000	0.000
83	A	89	LEU	0	0.024	0.042	9.458	0.030	0.030	0.000	0.000	0.000
84	A	90	ASN	0	0.067	0.011	9.722	0.009	0.009	0.000	0.000	0.000
85	A	91	THR	0	0.046	0.008	10.861	0.035	0.035	0.000	0.000	0.000
86	A	92	LEU	0	0.008	0.019	6.777	-0.007	-0.007	0.000	0.000	0.000
87	A	93	ARG	1	0.913	0.952	5.748	-1.267	-1.267	0.000	0.000	0.000
88	A	94	ARG	1	0.822	0.900	7.198	-0.194	-0.194	0.000	0.000	0.000
89	A	95	GLY	0	0.040	0.018	8.866	-0.055	-0.055	0.000	0.000	0.000
90	A	96	ALA	0	-0.017	-0.017	3.199	-0.238	-0.064	0.030	-0.067	-0.137
91	A	97	VAL	0	-0.046	-0.010	5.244	-0.358	-0.380	-0.001	-0.002	0.025
92	A	98	LEU	0	0.003	0.000	7.511	-0.141	-0.141	0.000	0.000	0.000
93	A	99	GLY	0	0.019	0.014	7.141	-0.020	-0.020	0.000	0.000	0.000
94	A	100	TYR	0	0.032	0.006	5.794	0.019	0.019	0.000	0.000	0.000
95	A	101	ILE	0	-0.035	-0.030	7.674	0.099	0.099	0.000	0.000	0.000
96	A	102	GLY	0	-0.015	0.010	11.081	0.005	0.005	0.000	0.000	0.000
97	A	103	ALA	0	-0.003	0.000	9.395	0.013	0.013	0.000	0.000	0.000
98	A	104	THR	0	-0.110	-0.049	11.490	-0.013	-0.013	0.000	0.000	0.000
99	A	105	VAL	0	-0.009	0.005	13.689	0.068	0.068	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)