FMO DATABASE

FMODB ID: 7M29K

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

Total energy (hartree)

FMO2-HF: Electronic energy	-599482.200531
FMO2-HF: Nuclear repulsion	561172.861983
FMO2-HF: Total energy	-38309.338548
FMO2-MP2: Total energy	-38415.011543

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.
-5.573	-0.523	0.149	-2.432	-2.768	-0.001

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 : 0.046 / q_NPA : 0.021

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	-0.771	-0.910	3.154	-8.955	-4.924	0.082	-2.180	-1.933	-0.001
4	A	4	ALA	0	0.036	0.016	4.690	0.367	0.414	-0.001	-0.009	-0.037	0.000
5	A	5	ALA	0	-0.025	0.000	5.780	0.442	0.442	0.000	0.000	0.000	0.000
6	A	6	TYR	0	-0.047	-0.030	3.916	0.638	0.879	-0.001	-0.042	-0.198	0.000
7	A	7	CYS	0	-0.031	0.014	5.921	0.193	0.193	0.000	0.000	0.000	0.000
8	A	8	PHE	0	-0.008	-0.031	8.551	0.356	0.356	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.919	0.978	9.305	1.300	1.300	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.027	-0.015	10.724	0.247	0.247	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.025	0.024	11.648	-0.094	-0.094	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.025	0.013	12.893	0.143	0.143	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.823	-0.920	14.449	-0.391	-0.391	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.071	-0.033	11.025	0.107	0.107	0.000	0.000	0.000	0.000
15	A	15	CYS	0	-0.080	-0.025	9.546	-0.097	-0.097	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.002	-0.030	7.471	0.273	0.273	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.774	0.895	9.514	0.719	0.719	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.027	0.009	13.132	0.029	0.029	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.018	0.010	15.212	0.050	0.050	0.000	0.000	0.000	0.000
20	A	21	TYR	0	-0.023	-0.003	17.487	-0.015	-0.015	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.005	0.006	19.513	0.019	0.019	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.875	-0.939	21.988	-0.178	-0.178	0.000	0.000	0.000	0.000
23	A	24	PHE	0	0.034	0.001	22.681	0.006	0.006	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.927	0.968	26.595	0.134	0.134	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.815	0.898	25.577	0.216	0.216	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.789	-0.883	24.782	-0.213	-0.213	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.013	-0.008	22.989	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.005	0.026	26.977	0.012	0.012	0.000	0.000	0.000	0.000
29	A	30	TRP	0	-0.044	-0.032	24.092	0.009	0.009	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.953	0.954	30.037	0.073	0.073	0.000	0.000	0.000	0.000
31	A	32	TRP	0	-0.031	-0.020	26.551	0.004	0.004	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.010	0.019	25.477	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	HIS	0	-0.030	-0.003	29.623	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.907	-0.955	28.149	-0.154	-0.154	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.036	0.023	22.908	0.006	0.006	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.908	0.925	26.174	0.143	0.143	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.051	0.018	23.975	0.008	0.008	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.076	-0.034	16.872	0.010	0.010	0.000	0.000	0.000	0.000
39	A	40	ASN	0	0.016	0.003	16.044	0.033	0.033	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.047	0.031	15.437	-0.035	-0.035	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.039	-0.032	10.976	-0.032	-0.032	0.000	0.000	0.000	0.000
42	A	43	PHE	0	0.003	-0.001	13.120	0.084	0.084	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.041	0.041	4.697	0.282	0.352	-0.002	-0.003	-0.065	0.000
44	A	45	ALA	0	0.025	0.003	11.601	0.119	0.119	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.061	0.025	12.827	-0.119	-0.119	0.000	0.000	0.000	0.000
46	A	47	ALA	0	-0.002	0.012	14.299	0.058	0.058	0.000	0.000	0.000	0.000
47	A	48	CYS	0	-0.025	-0.011	6.948	-0.162	-0.162	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.008	-0.005	12.650	0.006	0.006	0.000	0.000	0.000	0.000
49	A	50	TYR	0	0.055	0.030	15.837	0.008	0.008	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.925	0.953	15.945	-0.105	-0.105	0.000	0.000	0.000	0.000
51	A	72	ALA	0	0.046	0.033	21.800	-0.013	-0.013	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.020	-0.016	24.322	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	74	LYS	1	0.958	0.970	21.388	-0.039	-0.039	0.000	0.000	0.000	0.000
54	A	75	SER	0	0.038	0.027	19.119	0.025	0.025	0.000	0.000	0.000	0.000
55	A	76	PRO	0	-0.063	-0.029	13.826	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	77	SER	0	0.044	0.013	14.780	-0.030	-0.030	0.000	0.000	0.000	0.000
57	A	79	VAL	0	-0.013	-0.006	10.394	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	80	SER	0	0.061	0.007	9.104	-0.052	-0.052	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.075	-0.053	3.820	-0.247	0.067	0.004	-0.090	-0.229	0.000
60	A	82	ASP	-1	-0.884	-0.922	5.213	0.208	0.208	0.000	0.000	0.000	0.000
61	A	83	LEU	0	-0.042	-0.027	7.886	-0.189	-0.189	0.000	0.000	0.000	0.000
62	A	84	GLU	-1	-0.884	-0.949	9.909	-0.251	-0.251	0.000	0.000	0.000	0.000
63	A	85	PRO	0	-0.042	-0.027	12.706	0.007	0.007	0.000	0.000	0.000	0.000
64	A	86	LEU	0	-0.011	0.004	16.083	-0.042	-0.042	0.000	0.000	0.000	0.000
65	A	87	THR	0	-0.031	-0.019	18.702	0.019	0.019	0.000	0.000	0.000	0.000
66	A	88	ILE	0	-0.043	-0.012	21.746	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	89	LEU	0	0.006	0.003	24.861	0.013	0.013	0.000	0.000	0.000	0.000
68	A	90	TYR	0	0.003	-0.006	28.540	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	91	TYR	0	0.037	0.019	31.187	0.006	0.006	0.000	0.000	0.000	0.000
70	A	92	ILE	0	-0.012	0.007	34.523	0.000	0.000	0.000	0.000	0.000	0.000
71	A	93	GLY	0	0.020	0.002	36.817	0.003	0.003	0.000	0.000	0.000	0.000
72	A	94	ASN	0	0.009	-0.009	39.429	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	95	THR	0	-0.029	-0.011	36.336	0.001	0.001	0.000	0.000	0.000	0.000
74	A	96	PRO	0	0.008	0.015	33.730	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	97	LYS	1	0.909	0.950	30.910	0.058	0.058	0.000	0.000	0.000	0.000
76	A	98	ILE	0	0.034	0.010	26.046	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	99	GLU	-1	-0.932	-0.962	24.433	-0.068	-0.068	0.000	0.000	0.000	0.000
78	A	100	GLN	0	0.016	0.015	18.738	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	101	LEU	0	0.041	0.013	20.875	0.016	0.016	0.000	0.000	0.000	0.000
80	A	102	SER	0	-0.019	-0.008	17.892	-0.033	-0.033	0.000	0.000	0.000	0.000
81	A	103	ASN	0	0.007	-0.011	14.829	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	104	MET	0	0.019	0.030	15.901	0.007	0.007	0.000	0.000	0.000	0.000
83	A	105	ILE	0	-0.026	-0.005	11.763	-0.025	-0.025	0.000	0.000	0.000	0.000
84	A	106	VAL	0	0.008	0.001	9.061	0.020	0.020	0.000	0.000	0.000	0.000
85	A	107	LYS	1	0.957	0.984	5.792	0.601	0.601	0.000	0.000	0.000	0.000
86	A	108	SER	0	0.026	-0.006	3.199	-0.966	-0.667	0.068	-0.102	-0.265	0.000
87	A	110	LYS	1	0.990	0.996	4.692	-0.196	-0.148	-0.001	-0.006	-0.041	0.000
88	A	112	SER	0	0.003	0.013	10.300	0.107	0.107	0.000	0.000	0.000	0.000

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