FMO DATABASE

FMODB ID: 2LJYR

Calculation Name: 5TX2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5TX2

Chain ID: A

ChEMBL ID:

UniProt ID: P27090

Base Structure: X-ray

Registration Date: 2023-09-26

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	88
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-599916.929944
FMO2-HF: Nuclear repulsion	561607.210681
FMO2-HF: Total energy	-38309.719263
FMO2-MP2: Total energy	-38415.400973

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:1:ALA)

Summations of interaction energy for fragment #1(A:1: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.
-7.977	-2.208	0.426	-2.863	-3.33	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.031 / 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	3	ASP	-1	-0.773	-0.911	2.699	-11.599	-6.792	0.376	-2.690	-2.494	-0.009
4	A	4	ALA	0	0.039	0.018	4.796	0.350	0.389	-0.001	-0.008	-0.029	0.000
5	A	5	ALA	0	-0.011	0.001	5.827	0.398	0.398	0.000	0.000	0.000	0.000
6	A	6	TYR	0	-0.032	-0.024	3.953	0.639	0.892	-0.001	-0.048	-0.203	0.000
7	A	7	CYS	0	-0.033	0.015	6.014	0.180	0.180	0.000	0.000	0.000	0.000
8	A	8	PHE	0	-0.018	-0.035	8.646	0.364	0.364	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.898	0.973	9.214	1.461	1.461	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.025	-0.015	10.606	0.256	0.256	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.027	0.025	11.707	-0.098	-0.098	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.025	0.011	12.842	0.156	0.156	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.811	-0.907	14.449	-0.413	-0.413	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.070	-0.030	10.975	0.106	0.106	0.000	0.000	0.000	0.000
15	A	15	CYS	0	-0.081	-0.029	9.682	-0.078	-0.078	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.004	-0.033	7.455	0.281	0.281	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.754	0.874	9.599	0.716	0.716	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.039	0.013	13.263	0.035	0.035	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.010	0.008	15.329	0.049	0.049	0.000	0.000	0.000	0.000
20	A	21	TYR	0	-0.026	-0.004	17.592	-0.012	-0.012	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.009	0.005	19.555	0.018	0.018	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.856	-0.935	22.087	-0.168	-0.168	0.000	0.000	0.000	0.000
23	A	24	PHE	0	0.041	-0.001	22.678	0.006	0.006	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.915	0.967	26.679	0.127	0.127	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.802	0.862	25.547	0.208	0.208	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.770	-0.844	24.889	-0.204	-0.204	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.017	-0.007	22.844	0.004	0.004	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.010	0.027	27.071	0.012	0.012	0.000	0.000	0.000	0.000
29	A	30	TRP	0	-0.055	-0.039	23.754	0.008	0.008	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.957	0.955	30.115	0.064	0.064	0.000	0.000	0.000	0.000
31	A	32	TRP	0	-0.023	-0.014	26.573	0.002	0.002	0.000	0.000	0.000	0.000
32	A	33	ILE	0	-0.002	0.014	25.488	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	HIS	0	-0.012	0.003	29.674	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.851	-0.910	28.111	-0.142	-0.142	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.021	0.014	22.916	0.007	0.007	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.863	0.892	26.226	0.135	0.135	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.052	0.018	24.053	0.008	0.008	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.084	-0.042	16.820	0.009	0.009	0.000	0.000	0.000	0.000
39	A	40	ASN	0	0.018	0.007	16.090	0.029	0.029	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.044	0.025	15.515	-0.032	-0.032	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.039	-0.031	11.132	-0.029	-0.029	0.000	0.000	0.000	0.000
42	A	43	PHE	0	0.016	0.007	13.223	0.084	0.084	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.043	0.034	4.749	0.244	0.314	-0.002	-0.003	-0.065	0.000
44	A	45	ALA	0	0.030	0.008	11.673	0.117	0.117	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.057	0.025	12.920	-0.123	-0.123	0.000	0.000	0.000	0.000
46	A	47	ALA	0	-0.012	0.008	14.398	0.063	0.063	0.000	0.000	0.000	0.000
47	A	48	CYS	0	-0.004	0.001	7.023	-0.186	-0.186	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.017	0.002	12.649	0.004	0.004	0.000	0.000	0.000	0.000
49	A	50	TYR	0	0.053	0.028	15.849	0.011	0.011	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.897	0.942	16.397	-0.109	-0.109	0.000	0.000	0.000	0.000
51	A	72	ALA	0	0.041	0.030	21.815	-0.012	-0.012	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.012	-0.015	24.355	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	74	LYS	1	0.968	0.978	21.538	-0.046	-0.046	0.000	0.000	0.000	0.000
54	A	75	SER	0	0.039	0.027	19.196	0.029	0.029	0.000	0.000	0.000	0.000
55	A	76	PRO	0	-0.055	-0.025	13.885	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	77	SER	0	0.050	0.014	14.864	-0.035	-0.035	0.000	0.000	0.000	0.000
57	A	79	VAL	0	-0.009	-0.005	10.535	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	80	SER	0	0.090	0.024	9.164	-0.056	-0.056	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.143	-0.102	4.018	0.017	0.179	-0.001	-0.016	-0.145	0.000
60	A	82	ASP	-1	-0.814	-0.858	4.843	0.315	0.445	-0.001	-0.003	-0.126	0.000
61	A	83	LEU	0	-0.017	-0.014	7.857	-0.199	-0.199	0.000	0.000	0.000	0.000
62	A	84	GLU	-1	-0.827	-0.915	9.968	-0.201	-0.201	0.000	0.000	0.000	0.000
63	A	85	PRO	0	-0.037	-0.024	12.726	0.001	0.001	0.000	0.000	0.000	0.000
64	A	86	LEU	0	-0.016	0.000	16.104	-0.042	-0.042	0.000	0.000	0.000	0.000
65	A	87	THR	0	-0.024	-0.024	18.731	0.019	0.019	0.000	0.000	0.000	0.000
66	A	88	ILE	0	-0.051	-0.016	21.761	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	89	LEU	0	0.003	0.001	24.889	0.013	0.013	0.000	0.000	0.000	0.000
68	A	90	TYR	0	0.010	-0.006	28.457	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	91	TYR	0	0.044	0.020	31.218	0.003	0.003	0.000	0.000	0.000	0.000
70	A	92	ILE	0	-0.004	0.013	34.336	0.000	0.000	0.000	0.000	0.000	0.000
71	A	93	GLY	0	0.012	0.000	36.843	0.003	0.003	0.000	0.000	0.000	0.000
72	A	94	ASN	0	0.012	-0.005	39.459	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	95	THR	0	-0.036	-0.013	36.739	0.001	0.001	0.000	0.000	0.000	0.000
74	A	96	PRO	0	0.002	0.011	33.718	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	97	LYS	1	0.910	0.951	30.933	0.048	0.048	0.000	0.000	0.000	0.000
76	A	98	ILE	0	0.024	0.005	26.043	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	99	GLU	-1	-0.894	-0.943	24.655	-0.047	-0.047	0.000	0.000	0.000	0.000
78	A	100	GLN	0	0.017	0.030	18.637	-0.022	-0.022	0.000	0.000	0.000	0.000
79	A	101	LEU	0	0.032	0.014	21.104	0.016	0.016	0.000	0.000	0.000	0.000
80	A	102	SER	0	-0.013	-0.006	17.909	-0.019	-0.019	0.000	0.000	0.000	0.000
81	A	103	ASN	0	-0.028	-0.033	14.864	0.001	0.001	0.000	0.000	0.000	0.000
82	A	104	MET	0	0.021	0.032	15.942	0.005	0.005	0.000	0.000	0.000	0.000
83	A	105	ILE	0	-0.017	0.007	11.763	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	106	VAL	0	-0.002	-0.004	9.110	0.032	0.032	0.000	0.000	0.000	0.000
85	A	107	LYS	1	0.892	0.937	5.690	0.300	0.300	0.000	0.000	0.000	0.000
86	A	108	SER	0	-0.007	-0.041	3.197	-0.873	-0.610	0.057	-0.089	-0.231	0.000
87	A	110	LYS	1	0.937	0.974	4.773	-0.217	-0.172	-0.001	-0.006	-0.037	0.000
88	A	112	SER	0	0.020	0.026	10.380	0.102	0.102	0.000	0.000	0.000	0.000

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