FMO DATABASE

FMODB ID: 72N1K

Calculation Name: 3LAZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3LAZ

Chain ID: A

ChEMBL ID:

UniProt ID: P39829

Base Structure: X-ray

Registration Date: 2023-06-22

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	96
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-631941.085424
FMO2-HF: Nuclear repulsion	595250.096781
FMO2-HF: Total energy	-36690.988643
FMO2-MP2: Total energy	-36799.279181

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
-1.597	1.018	-0.023	-1.224	-1.368	0.001

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / 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

Sort

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	2	ALA	0	-0.001	0.011	3.342	-2.619	-0.168	-0.022	-1.208	-1.221	0.001
4	A	3	ASN	0	0.001	0.001	4.591	0.124	0.288	-0.001	-0.016	-0.147	0.000
5	A	4	ILE	0	0.029	0.016	5.514	-0.199	-0.199	0.000	0.000	0.000	0.000
6	A	5	LYS	1	0.903	0.950	7.303	0.950	0.950	0.000	0.000	0.000	0.000
7	A	6	ILE	0	0.052	0.036	10.433	-0.017	-0.017	0.000	0.000	0.000	0.000
8	A	7	ARG	1	0.875	0.928	13.251	0.311	0.311	0.000	0.000	0.000	0.000
9	A	8	GLN	0	0.034	0.023	16.064	0.008	0.008	0.000	0.000	0.000	0.000
10	A	9	GLU	-1	-0.910	-0.957	19.524	-0.103	-0.103	0.000	0.000	0.000	0.000
11	A	10	THR	0	-0.046	-0.029	22.193	0.000	0.000	0.000	0.000	0.000	0.000
12	A	11	PRO	0	0.020	0.018	24.068	0.006	0.006	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.022	-0.022	26.941	0.000	0.000	0.000	0.000	0.000	0.000
14	A	13	ALA	0	0.029	0.027	30.440	0.004	0.004	0.000	0.000	0.000	0.000
15	A	14	PHE	0	-0.034	-0.020	28.452	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	15	TYR	0	-0.026	-0.012	33.016	0.002	0.002	0.000	0.000	0.000	0.000
17	A	16	ILE	0	-0.025	-0.012	34.245	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	17	LYS	1	0.888	0.947	35.829	0.018	0.018	0.000	0.000	0.000	0.000
19	A	18	VAL	0	-0.044	-0.010	36.763	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	19	HIS	0	0.061	0.058	38.581	0.000	0.000	0.000	0.000	0.000	0.000
21	A	20	ASP	-1	-0.907	-0.957	36.523	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	21	THR	0	-0.059	-0.079	38.935	0.001	0.001	0.000	0.000	0.000	0.000
23	A	22	ASP	-1	-0.730	-0.846	40.906	-0.017	-0.017	0.000	0.000	0.000	0.000
24	A	23	ASN	0	0.001	-0.007	41.340	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	24	VAL	0	-0.007	-0.002	42.474	0.000	0.000	0.000	0.000	0.000	0.000
26	A	25	ALA	0	-0.003	0.000	38.281	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	26	ILE	0	-0.071	-0.018	39.760	0.001	0.001	0.000	0.000	0.000	0.000
28	A	27	ILE	0	0.041	0.026	38.004	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	28	VAL	0	-0.009	-0.016	35.641	0.001	0.001	0.000	0.000	0.000	0.000
30	A	29	ASN	0	0.018	-0.029	34.870	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	30	ASP	-1	-0.878	-0.924	36.951	-0.044	-0.044	0.000	0.000	0.000	0.000
32	A	31	ASN	0	-0.062	-0.021	39.364	0.003	0.003	0.000	0.000	0.000	0.000
33	A	32	GLY	0	0.027	0.012	40.612	0.002	0.002	0.000	0.000	0.000	0.000
34	A	33	LEU	0	-0.065	-0.010	35.123	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	34	LYS	1	0.976	0.990	34.900	0.037	0.037	0.000	0.000	0.000	0.000
36	A	35	ALA	0	0.072	0.038	38.623	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	36	GLY	0	-0.014	-0.011	37.343	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	37	THR	0	-0.095	-0.054	33.441	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	38	ARG	1	0.872	0.921	30.881	0.023	0.023	0.000	0.000	0.000	0.000
40	A	39	PHE	0	0.018	0.008	30.714	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	40	PRO	0	-0.025	-0.018	26.755	0.004	0.004	0.000	0.000	0.000	0.000
42	A	41	ASP	-1	-0.744	-0.879	28.854	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	42	GLY	0	-0.063	-0.030	31.468	0.005	0.005	0.000	0.000	0.000	0.000
44	A	43	LEU	0	-0.089	-0.017	33.308	0.002	0.002	0.000	0.000	0.000	0.000
45	A	44	GLU	-1	-0.866	-0.929	34.381	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.032	-0.009	36.646	0.002	0.002	0.000	0.000	0.000	0.000
47	A	46	ILE	0	0.022	0.011	39.240	0.000	0.000	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.877	-0.945	42.298	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	48	HIS	0	-0.082	-0.050	42.116	0.000	0.000	0.000	0.000	0.000	0.000
50	A	49	ILE	0	0.006	0.018	41.131	0.001	0.001	0.000	0.000	0.000	0.000
51	A	50	PRO	0	0.029	0.012	42.050	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	51	GLN	0	0.056	0.027	39.176	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	52	GLY	0	-0.028	-0.025	41.586	0.001	0.001	0.000	0.000	0.000	0.000
54	A	53	HIS	0	0.002	0.018	43.374	0.002	0.002	0.000	0.000	0.000	0.000
55	A	54	LYS	1	0.946	0.967	42.854	0.017	0.017	0.000	0.000	0.000	0.000
56	A	55	VAL	0	0.024	0.026	38.862	0.000	0.000	0.000	0.000	0.000	0.000
57	A	56	ALA	0	0.026	0.019	42.198	0.000	0.000	0.000	0.000	0.000	0.000
58	A	57	LEU	0	-0.015	-0.010	37.461	0.000	0.000	0.000	0.000	0.000	0.000
59	A	58	LEU	0	-0.032	-0.033	39.556	0.001	0.001	0.000	0.000	0.000	0.000
60	A	59	ASP	-1	-0.850	-0.914	42.268	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	60	ILE	0	-0.033	-0.012	45.352	0.001	0.001	0.000	0.000	0.000	0.000
62	A	61	PRO	0	0.018	0.015	48.271	0.000	0.000	0.000	0.000	0.000	0.000
63	A	62	ALA	0	0.033	0.005	51.599	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	63	ASN	0	-0.032	-0.036	54.835	0.000	0.000	0.000	0.000	0.000	0.000
65	A	64	GLY	0	-0.039	0.010	51.872	0.000	0.000	0.000	0.000	0.000	0.000
66	A	65	GLU	-1	-0.895	-0.961	50.570	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	66	ILE	0	-0.040	-0.004	47.924	0.000	0.000	0.000	0.000	0.000	0.000
68	A	67	ILE	0	0.000	0.010	45.507	0.000	0.000	0.000	0.000	0.000	0.000
69	A	68	ARG	1	0.958	0.968	42.469	0.022	0.022	0.000	0.000	0.000	0.000
70	A	69	TYR	0	-0.073	-0.053	43.227	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	70	GLY	0	-0.022	-0.009	44.570	0.000	0.000	0.000	0.000	0.000	0.000
72	A	71	GLU	-1	-0.950	-0.956	45.576	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	72	VAL	0	-0.004	-0.008	48.856	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.054	-0.039	48.342	0.000	0.000	0.000	0.000	0.000	0.000
75	A	74	GLY	0	0.018	-0.004	51.834	0.000	0.000	0.000	0.000	0.000	0.000
76	A	75	TYR	0	-0.018	-0.001	53.004	0.000	0.000	0.000	0.000	0.000	0.000
77	A	76	ALA	0	0.001	0.014	51.726	0.000	0.000	0.000	0.000	0.000	0.000
78	A	77	VAL	0	0.006	0.017	53.706	0.001	0.001	0.000	0.000	0.000	0.000
79	A	78	ARG	1	0.903	0.942	50.882	0.011	0.011	0.000	0.000	0.000	0.000
80	A	79	ALA	0	-0.012	-0.016	51.299	0.000	0.000	0.000	0.000	0.000	0.000
81	A	80	ILE	0	-0.041	-0.026	46.878	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	81	PRO	0	0.017	0.020	45.731	0.001	0.001	0.000	0.000	0.000	0.000
83	A	82	ARG	1	0.936	0.957	35.475	0.009	0.009	0.000	0.000	0.000	0.000
84	A	83	GLY	0	-0.022	-0.016	40.463	0.000	0.000	0.000	0.000	0.000	0.000
85	A	84	SER	0	-0.051	-0.022	41.200	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	85	TRP	0	0.001	-0.038	44.299	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	86	ILE	0	-0.047	-0.024	45.799	0.001	0.001	0.000	0.000	0.000	0.000
88	A	87	ASP	-1	-0.843	-0.902	48.126	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	88	GLU	-1	-0.929	-0.985	51.074	-0.015	-0.015	0.000	0.000	0.000	0.000
90	A	89	SER	0	-0.078	-0.050	53.833	0.001	0.001	0.000	0.000	0.000	0.000
91	A	90	MET	0	-0.049	-0.012	52.900	0.001	0.001	0.000	0.000	0.000	0.000
92	A	91	VAL	0	-0.027	-0.012	51.836	0.000	0.000	0.000	0.000	0.000	0.000
93	A	92	VAL	0	-0.012	0.008	55.043	0.000	0.000	0.000	0.000	0.000	0.000
94	A	93	LEU	0	0.028	-0.002	55.858	0.000	0.000	0.000	0.000	0.000	0.000
95	A	94	PRO	0	0.001	0.005	55.478	0.001	0.001	0.000	0.000	0.000	0.000
96	A	95	GLU	-1	-1.001	-0.987	58.422	-0.009	-0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)