FMO DATABASE

FMODB ID: 66JGZ

Calculation Name: 1LKT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1LKT

Chain ID: A

ChEMBL ID:

UniProt ID: P12528

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:

Apendix: None

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	104
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-724223.39177
FMO2-HF: Nuclear repulsion	685224.485402
FMO2-HF: Total energy	-38998.906368
FMO2-MP2: Total energy	-39114.873817

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:6:ALA)

Summations of interaction energy for fragment #1(A:6: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.
-2.145	0.477	-0.031	-1.258	-1.333	0.001

Interaction energy analysis for fragmet #1(A:6:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.022 / q_NPA : -0.024

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	8	VAL	0	-0.013	0.001	3.463	-2.275	0.227	-0.030	-1.254	-1.219	0.001
4	A	9	VAL	0	0.021	0.024	5.056	-0.340	-0.220	-0.001	-0.004	-0.114	0.000
5	A	10	VAL	0	-0.004	0.000	6.779	0.232	0.232	0.000	0.000	0.000	0.000
6	A	11	SER	0	0.000	-0.009	9.165	-0.039	-0.039	0.000	0.000	0.000	0.000
7	A	12	ASN	0	-0.025	-0.025	12.649	0.051	0.051	0.000	0.000	0.000	0.000
8	A	13	PRO	0	0.021	0.016	15.300	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	14	ARG	1	0.907	0.955	17.444	-0.017	-0.017	0.000	0.000	0.000	0.000
10	A	15	PRO	0	0.035	0.033	21.136	-0.015	-0.015	0.000	0.000	0.000	0.000
11	A	16	ILE	0	-0.050	-0.033	23.313	0.005	0.005	0.000	0.000	0.000	0.000
12	A	17	PHE	0	0.024	0.004	25.598	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	18	THR	0	-0.008	-0.019	28.093	0.000	0.000	0.000	0.000	0.000	0.000
14	A	19	GLU	-1	-0.943	-0.980	30.729	-0.029	-0.029	0.000	0.000	0.000	0.000
15	A	20	SER	0	0.012	0.008	32.556	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	21	ARG	1	0.918	0.957	34.343	0.036	0.036	0.000	0.000	0.000	0.000
17	A	22	SER	0	-0.034	-0.022	35.192	0.000	0.000	0.000	0.000	0.000	0.000
18	A	23	PHE	0	0.042	0.025	27.066	0.000	0.000	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.966	0.985	32.515	0.037	0.037	0.000	0.000	0.000	0.000
20	A	25	ALA	0	0.048	0.039	30.693	0.000	0.000	0.000	0.000	0.000	0.000
21	A	26	VAL	0	0.034	0.023	31.986	0.001	0.001	0.000	0.000	0.000	0.000
22	A	27	ALA	0	-0.052	-0.031	34.244	0.004	0.004	0.000	0.000	0.000	0.000
23	A	28	ASN	0	-0.026	-0.015	35.615	0.001	0.001	0.000	0.000	0.000	0.000
24	A	29	GLY	0	0.057	0.027	35.991	0.001	0.001	0.000	0.000	0.000	0.000
25	A	30	LYS	1	0.815	0.906	36.827	0.008	0.008	0.000	0.000	0.000	0.000
26	A	31	ILE	0	0.030	0.020	31.028	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	32	TYR	0	0.002	0.005	35.181	0.003	0.003	0.000	0.000	0.000	0.000
28	A	33	ILE	0	-0.001	-0.015	31.543	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	34	GLY	0	0.057	0.009	35.047	0.002	0.002	0.000	0.000	0.000	0.000
30	A	35	GLN	0	0.006	0.011	35.637	0.002	0.002	0.000	0.000	0.000	0.000
31	A	36	ILE	0	0.001	0.016	32.837	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	37	ASP	-1	-0.860	-0.948	36.303	0.004	0.004	0.000	0.000	0.000	0.000
33	A	38	THR	0	-0.023	-0.007	38.741	0.000	0.000	0.000	0.000	0.000	0.000
34	A	39	ASP	-1	-0.785	-0.900	39.600	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	40	PRO	0	-0.036	0.002	37.225	0.002	0.002	0.000	0.000	0.000	0.000
36	A	41	VAL	0	0.036	0.012	39.811	0.002	0.002	0.000	0.000	0.000	0.000
37	A	42	ASN	0	-0.002	0.006	42.240	0.001	0.001	0.000	0.000	0.000	0.000
38	A	43	PRO	0	0.050	0.009	43.435	0.001	0.001	0.000	0.000	0.000	0.000
39	A	44	ALA	0	-0.037	-0.011	43.721	0.002	0.002	0.000	0.000	0.000	0.000
40	A	45	ASN	0	-0.077	-0.044	41.374	0.002	0.002	0.000	0.000	0.000	0.000
41	A	46	GLN	0	-0.051	-0.009	38.970	0.002	0.002	0.000	0.000	0.000	0.000
42	A	47	ILE	0	-0.041	-0.007	33.124	0.002	0.002	0.000	0.000	0.000	0.000
43	A	48	PRO	0	-0.002	-0.006	35.130	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	49	VAL	0	-0.015	0.007	32.385	0.002	0.002	0.000	0.000	0.000	0.000
45	A	50	TYR	0	0.012	-0.015	30.002	0.000	0.000	0.000	0.000	0.000	0.000
46	A	51	ILE	0	0.002	0.005	28.377	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	52	GLU	-1	-0.786	-0.858	22.061	0.116	0.116	0.000	0.000	0.000	0.000
48	A	53	ASN	0	-0.078	-0.058	25.261	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	54	GLU	-1	-0.943	-0.965	21.434	0.109	0.109	0.000	0.000	0.000	0.000
50	A	55	ASP	-1	-0.882	-0.917	22.733	0.119	0.119	0.000	0.000	0.000	0.000
51	A	56	GLY	0	0.001	0.009	23.861	0.011	0.011	0.000	0.000	0.000	0.000
52	A	57	SER	0	-0.070	-0.054	24.561	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	58	HIS	0	-0.030	-0.041	25.438	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	59	VAL	0	-0.024	-0.002	29.924	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	60	GLN	0	-0.008	-0.002	32.810	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	61	ILE	0	-0.049	-0.014	32.967	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	62	THR	0	0.007	-0.001	36.204	0.000	0.000	0.000	0.000	0.000	0.000
58	A	63	GLN	0	-0.009	0.021	36.423	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	64	PRO	0	-0.008	-0.018	37.827	0.000	0.000	0.000	0.000	0.000	0.000
60	A	65	LEU	0	-0.006	0.001	31.242	0.002	0.002	0.000	0.000	0.000	0.000
61	A	66	ILE	0	0.014	-0.002	34.814	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	67	ILE	0	0.016	0.033	30.945	0.002	0.002	0.000	0.000	0.000	0.000
63	A	68	ASN	0	0.059	0.014	29.745	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	69	ALA	0	0.058	0.004	32.885	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	70	ALA	0	-0.044	-0.017	28.150	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	71	GLY	0	0.042	0.023	28.465	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	72	LYS	1	0.931	0.966	22.812	0.040	0.040	0.000	0.000	0.000	0.000
68	A	73	ILE	0	0.046	0.032	27.969	0.001	0.001	0.000	0.000	0.000	0.000
69	A	74	VAL	0	-0.071	-0.029	28.945	0.002	0.002	0.000	0.000	0.000	0.000
70	A	75	TYR	0	0.062	0.017	31.495	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	76	ASN	0	0.011	-0.003	33.083	0.000	0.000	0.000	0.000	0.000	0.000
72	A	77	GLY	0	-0.005	-0.003	34.470	0.001	0.001	0.000	0.000	0.000	0.000
73	A	78	GLN	0	0.000	0.014	29.687	0.001	0.001	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.009	-0.015	25.026	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	80	VAL	0	0.000	0.014	26.877	0.007	0.007	0.000	0.000	0.000	0.000
76	A	81	LYS	1	0.841	0.911	19.941	-0.109	-0.109	0.000	0.000	0.000	0.000
77	A	82	ILE	0	-0.008	-0.011	25.158	0.004	0.004	0.000	0.000	0.000	0.000
78	A	83	VAL	0	-0.006	0.001	24.221	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	84	THR	0	0.025	0.007	27.249	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	85	VAL	0	0.001	0.003	28.210	0.005	0.005	0.000	0.000	0.000	0.000
81	A	86	GLN	0	0.009	0.010	29.202	0.005	0.005	0.000	0.000	0.000	0.000
82	A	87	GLY	0	0.025	0.011	29.638	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	88	HIS	0	-0.017	-0.023	28.323	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	89	SER	0	-0.023	0.008	32.276	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	90	MET	0	-0.009	-0.024	28.611	0.001	0.001	0.000	0.000	0.000	0.000
86	A	91	ALA	0	0.019	0.032	33.948	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	92	ILE	0	-0.027	-0.013	30.986	0.003	0.003	0.000	0.000	0.000	0.000
88	A	93	TYR	0	0.043	0.017	35.556	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	94	ASP	-1	-0.732	-0.872	37.686	-0.017	-0.017	0.000	0.000	0.000	0.000
90	A	95	ALA	0	-0.062	-0.031	39.049	0.003	0.003	0.000	0.000	0.000	0.000
91	A	96	ASN	0	-0.109	-0.060	41.200	0.003	0.003	0.000	0.000	0.000	0.000
92	A	97	GLY	0	-0.020	0.002	42.757	0.001	0.001	0.000	0.000	0.000	0.000
93	A	98	SER	0	0.001	0.009	42.006	0.001	0.001	0.000	0.000	0.000	0.000
94	A	99	GLN	0	-0.061	-0.043	38.852	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	100	VAL	0	-0.039	-0.018	34.575	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	101	ASP	-1	-0.872	-0.950	31.960	-0.034	-0.034	0.000	0.000	0.000	0.000
97	A	102	TYR	0	-0.055	-0.044	35.265	0.004	0.004	0.000	0.000	0.000	0.000
98	A	103	ILE	0	-0.009	0.015	30.115	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	104	ALA	0	0.021	0.012	33.449	0.004	0.004	0.000	0.000	0.000	0.000
100	A	105	ASN	0	0.033	-0.005	31.423	0.006	0.006	0.000	0.000	0.000	0.000
101	A	106	VAL	0	0.037	0.017	26.968	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	107	LEU	0	-0.010	-0.012	26.404	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.776	0.903	27.224	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	109	TYR	0	-0.016	0.014	25.307	-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:6:ALA)