FMO DATABASE

FMODB ID: R5ZL8

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

Total energy (hartree)

FMO2-HF: Electronic energy	-543728.113348
FMO2-HF: Nuclear repulsion	508712.619338
FMO2-HF: Total energy	-35015.49401
FMO2-MP2: Total energy	-35119.861765

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.
-3.595	1.229	3.821	-2.015	-6.631	-0.012

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	0.052	0.009	2.704	-2.439	-0.458	0.725	-1.138	-1.568	-0.006
4	A	5	GLU	-1	-0.815	-0.887	5.207	-0.398	-0.232	-0.001	-0.008	-0.157	0.000
5	A	6	ARG	1	0.896	0.942	2.408	-0.373	0.344	1.035	-0.273	-1.479	-0.001
6	A	7	LYS	1	0.942	0.972	2.241	-0.561	1.027	1.574	-0.842	-2.321	-0.003
7	A	8	ARG	1	0.886	0.925	3.245	0.857	0.598	0.101	0.426	-0.268	0.000
8	A	9	GLU	-1	-0.781	-0.867	6.148	-0.289	-0.289	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.027	-0.016	2.487	-0.677	-0.046	0.387	-0.180	-0.838	-0.002
10	A	11	ILE	0	-0.031	-0.025	6.260	0.088	0.088	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.893	-0.939	8.680	-0.196	-0.196	0.000	0.000	0.000	0.000
12	A	13	GLN	0	-0.027	-0.001	8.742	0.010	0.010	0.000	0.000	0.000	0.000
13	A	14	PHE	0	-0.017	-0.014	8.220	0.034	0.034	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.805	0.906	11.863	0.263	0.263	0.000	0.000	0.000	0.000
15	A	16	VAL	0	-0.014	-0.003	14.232	0.020	0.020	0.000	0.000	0.000	0.000
16	A	17	HIS	0	0.005	-0.010	17.536	0.000	0.000	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.880	-0.922	19.963	-0.142	-0.142	0.000	0.000	0.000	0.000
18	A	19	ASN	0	-0.072	-0.059	19.257	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.813	-0.895	21.079	-0.094	-0.094	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.114	-0.057	22.379	0.006	0.006	0.000	0.000	0.000	0.000
21	A	22	GLY	0	0.055	0.031	24.564	0.005	0.005	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.029	-0.018	25.424	0.007	0.007	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.006	-0.020	28.639	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.743	-0.848	31.793	-0.047	-0.047	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.066	0.043	28.041	0.001	0.001	0.000	0.000	0.000	0.000
26	A	27	GLN	0	0.020	0.013	27.866	0.003	0.003	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.036	-0.020	31.751	0.002	0.002	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.038	0.035	33.743	0.002	0.002	0.000	0.000	0.000	0.000
29	A	30	ILE	0	0.031	0.019	29.312	0.001	0.001	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.034	-0.025	33.696	0.002	0.002	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.034	-0.034	36.065	0.003	0.003	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.830	-0.893	36.181	-0.050	-0.050	0.000	0.000	0.000	0.000
33	A	34	GLN	0	0.004	-0.008	32.928	0.002	0.002	0.000	0.000	0.000	0.000
34	A	35	ILE	0	-0.075	-0.052	37.828	0.002	0.002	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.004	0.003	40.969	0.004	0.004	0.000	0.000	0.000	0.000
36	A	37	ASN	0	0.033	0.008	38.786	0.000	0.000	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.029	-0.016	40.592	0.002	0.002	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.038	-0.040	42.972	0.003	0.003	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.909	-0.929	43.423	-0.042	-0.042	0.000	0.000	0.000	0.000
40	A	41	HIS	0	0.006	-0.008	44.280	0.001	0.001	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.043	-0.034	46.196	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.901	0.970	48.285	0.036	0.036	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.018	0.020	49.220	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	HIS	0	0.026	0.025	47.646	0.003	0.003	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.940	0.955	50.880	0.029	0.029	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.928	0.957	50.843	0.035	0.035	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.793	-0.861	46.524	-0.039	-0.039	0.000	0.000	0.000	0.000
48	A	49	HIS	0	0.085	0.042	48.449	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	HIS	0	0.046	0.024	43.137	0.002	0.002	0.000	0.000	0.000	0.000
50	A	51	SER	0	0.022	-0.021	42.954	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.829	0.905	43.641	0.031	0.031	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.912	0.951	43.646	0.033	0.033	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.013	0.015	40.317	0.000	0.000	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.045	0.022	40.481	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	56	LEU	0	0.022	0.007	42.293	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.933	0.972	38.714	0.039	0.039	0.000	0.000	0.000	0.000
57	A	58	MET	0	0.017	0.023	36.986	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	59	VAL	0	0.032	0.018	38.813	0.000	0.000	0.000	0.000	0.000	0.000
59	A	60	GLY	0	-0.006	-0.006	41.334	0.001	0.001	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.848	0.922	30.810	0.061	0.061	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.974	0.981	37.357	0.040	0.040	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.960	0.977	38.566	0.030	0.030	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.952	0.985	35.839	0.038	0.038	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.020	0.012	32.646	0.001	0.001	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.032	0.019	36.577	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.031	-0.013	39.557	0.002	0.002	0.000	0.000	0.000	0.000
67	A	68	TYR	0	0.004	-0.008	31.836	0.002	0.002	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.018	0.005	35.362	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.878	0.931	37.706	0.023	0.023	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.046	-0.013	40.473	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.933	0.985	32.195	0.030	0.030	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.806	-0.913	37.045	-0.027	-0.027	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.036	0.010	38.991	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.009	0.015	40.732	0.000	0.000	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.890	0.908	31.311	0.039	0.039	0.000	0.000	0.000	0.000
76	A	77	TYR	0	-0.034	-0.007	38.556	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.958	0.974	40.308	0.021	0.021	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.778	-0.869	39.367	-0.035	-0.035	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.034	-0.018	36.214	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.041	-0.031	39.346	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.943	-0.962	42.670	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.822	0.895	39.526	0.036	0.036	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.050	-0.015	37.419	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.003	0.014	41.655	0.000	0.000	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.108	-0.050	40.908	0.002	0.002	0.000	0.000	0.000	0.000

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