FMO DATABASE

FMODB ID: ZYJZN

Calculation Name: 1A32-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A32

Chain ID: A

ChEMBL ID:

UniProt ID: P05766

Base Structure: X-ray

Registration Date: 2023-06-20

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	85
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-542853.100766
FMO2-HF: Nuclear repulsion	507837.989334
FMO2-HF: Total energy	-35015.111432
FMO2-MP2: Total energy	-35119.498982

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-3.727	1.019	3.784	-1.874	-6.654	-0.01

Interaction energy analysis for fragmet #1(A:2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.011 / q_NPA : -0.017

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	4	GLN	0	0.048	0.004	2.744	-2.419	-0.257	0.536	-1.127	-1.570	-0.004
4	A	5	GLU	-1	-0.814	-0.894	5.312	0.129	0.307	-0.001	-0.008	-0.169	0.000
5	A	6	ARG	1	0.911	0.950	2.366	-0.811	-0.156	1.174	-0.302	-1.526	-0.001
6	A	7	LYS	1	0.932	0.963	2.244	-0.935	0.713	1.611	-0.887	-2.371	-0.003
7	A	8	ARG	1	0.884	0.916	3.151	0.850	0.388	0.129	0.608	-0.275	0.000
8	A	9	GLU	-1	-0.786	-0.857	6.319	-0.041	-0.041	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.029	-0.020	2.510	-0.643	-0.078	0.335	-0.158	-0.743	-0.002
10	A	11	ILE	0	-0.026	-0.018	6.311	0.049	0.049	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.962	-0.987	8.615	-0.139	-0.139	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.018	-0.007	8.788	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.036	-0.024	8.516	0.027	0.027	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.875	0.982	11.658	0.186	0.186	0.000	0.000	0.000	0.000
15	A	16	VAL	0	-0.004	-0.013	14.037	0.018	0.018	0.000	0.000	0.000	0.000
16	A	17	HIS	0	-0.003	-0.014	17.403	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.922	-0.957	20.119	-0.108	-0.108	0.000	0.000	0.000	0.000
18	A	19	ASN	0	-0.039	-0.019	19.821	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.853	-0.924	21.452	-0.057	-0.057	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.069	-0.041	22.453	0.005	0.005	0.000	0.000	0.000	0.000
21	A	22	GLY	0	0.065	0.049	24.638	0.004	0.004	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.031	-0.009	25.536	0.005	0.005	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.002	-0.024	28.720	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.733	-0.856	32.209	-0.024	-0.024	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.058	0.037	28.174	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	27	GLN	0	-0.045	-0.021	27.751	0.001	0.001	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.044	-0.029	31.786	0.000	0.000	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.033	0.027	33.796	0.001	0.001	0.000	0.000	0.000	0.000
29	A	30	ILE	0	0.039	0.027	29.216	0.000	0.000	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.030	-0.021	33.582	0.000	0.000	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.025	-0.026	36.050	0.002	0.002	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.868	-0.913	35.737	-0.040	-0.040	0.000	0.000	0.000	0.000
33	A	34	GLN	0	0.026	0.008	32.852	0.002	0.002	0.000	0.000	0.000	0.000
34	A	35	ILE	0	-0.095	-0.058	37.932	0.001	0.001	0.000	0.000	0.000	0.000
35	A	36	ASN	0	0.009	0.001	41.046	0.003	0.003	0.000	0.000	0.000	0.000
36	A	37	ASN	0	0.020	0.019	38.625	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.018	-0.014	40.789	0.001	0.001	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.055	-0.046	42.911	0.002	0.002	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.912	-0.944	43.497	-0.033	-0.033	0.000	0.000	0.000	0.000
40	A	41	HIS	0	0.023	0.016	44.270	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.034	-0.037	46.174	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.914	0.980	48.696	0.027	0.027	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.002	-0.002	49.093	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	HIS	0	0.018	0.035	47.781	0.001	0.001	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.948	0.953	50.971	0.023	0.023	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.941	0.961	50.774	0.029	0.029	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.809	-0.869	46.646	-0.030	-0.030	0.000	0.000	0.000	0.000
48	A	49	HIS	0	0.072	0.033	48.663	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	HIS	0	0.010	-0.002	43.462	0.002	0.002	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.012	-0.028	43.184	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.825	0.911	44.122	0.024	0.024	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.993	0.988	43.556	0.026	0.026	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.024	0.011	40.466	0.000	0.000	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.063	0.038	40.509	0.000	0.000	0.000	0.000	0.000	0.000
55	A	56	LEU	0	0.017	0.005	42.607	0.001	0.001	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.930	0.966	38.672	0.027	0.027	0.000	0.000	0.000	0.000
57	A	58	MET	0	0.016	0.021	37.160	0.000	0.000	0.000	0.000	0.000	0.000
58	A	59	VAL	0	0.030	0.019	39.178	0.001	0.001	0.000	0.000	0.000	0.000
59	A	60	GLY	0	-0.012	-0.011	41.846	0.001	0.001	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.918	0.953	31.230	0.039	0.039	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.988	0.983	37.401	0.027	0.027	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.959	0.987	38.860	0.018	0.018	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.960	0.988	35.974	0.021	0.021	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.029	0.014	32.854	0.002	0.002	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.020	0.014	36.817	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.031	-0.009	39.677	0.001	0.001	0.000	0.000	0.000	0.000
67	A	68	TYR	0	-0.008	-0.009	32.115	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.012	-0.005	35.533	0.002	0.002	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.907	0.958	37.843	0.008	0.008	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.054	-0.030	40.547	0.000	0.000	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.925	0.982	32.392	0.006	0.006	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.815	-0.915	37.522	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.051	0.010	39.415	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.017	0.021	40.670	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.884	0.902	31.648	0.015	0.015	0.000	0.000	0.000	0.000
76	A	77	TYR	0	-0.056	-0.018	38.699	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.970	0.965	40.526	0.008	0.008	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.815	-0.878	39.824	-0.019	-0.019	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.040	-0.023	36.471	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.045	-0.030	39.567	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.948	-0.963	42.711	-0.017	-0.017	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.864	0.920	38.597	0.022	0.022	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.060	-0.024	37.615	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.009	0.026	41.732	0.000	0.000	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.094	-0.044	41.082	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)