FMO DATABASE

FMODB ID: 6GNMZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-599546.380277
FMO2-HF: Nuclear repulsion	561236.510147
FMO2-HF: Total energy	-38309.87013
FMO2-MP2: Total energy	-38415.572327

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.
-10.764	-8.665	8.246	-5.028	-5.317	-0.035

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 : 0.036 / q_NPA : 0.019

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	-0.906	1.918	-15.054	-14.075	7.978	-4.721	-4.236	-0.035
4	A	4	ALA	0	0.029	0.009	4.259	0.312	0.395	0.000	-0.023	-0.061	0.000
5	A	5	ALA	0	-0.024	-0.001	5.542	0.494	0.494	0.000	0.000	0.000	0.000
6	A	6	TYR	0	0.020	0.003	3.793	0.772	1.026	0.000	-0.058	-0.196	0.000
7	A	7	CYS	0	-0.017	0.011	5.923	0.319	0.319	0.000	0.000	0.000	0.000
8	A	8	PHE	0	-0.002	-0.016	8.591	0.378	0.378	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.841	0.933	8.666	1.645	1.645	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.023	-0.014	10.337	0.284	0.284	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.020	0.018	11.729	-0.087	-0.087	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.007	0.013	12.764	0.182	0.182	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.828	-0.909	14.107	-0.456	-0.456	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.041	-0.016	11.386	0.111	0.111	0.000	0.000	0.000	0.000
15	A	15	CYS	0	-0.085	-0.039	9.542	-0.087	-0.087	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.015	-0.016	7.046	0.321	0.321	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.749	0.863	9.078	0.749	0.749	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.032	0.012	12.677	0.054	0.054	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.007	0.001	14.645	0.050	0.050	0.000	0.000	0.000	0.000
20	A	21	TYR	0	-0.065	-0.032	16.886	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.009	0.001	19.013	0.013	0.013	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.813	-0.911	21.415	-0.150	-0.150	0.000	0.000	0.000	0.000
23	A	24	PHE	0	0.033	-0.005	22.186	0.007	0.007	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.918	0.966	26.251	0.108	0.108	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.794	0.855	24.748	0.194	0.194	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.759	-0.839	24.337	-0.188	-0.188	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.023	-0.004	22.587	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.008	0.021	26.774	0.011	0.011	0.000	0.000	0.000	0.000
29	A	30	TRP	0	-0.042	-0.025	23.263	0.008	0.008	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.944	0.946	29.916	0.048	0.048	0.000	0.000	0.000	0.000
31	A	32	TRP	0	0.001	0.000	26.241	0.003	0.003	0.000	0.000	0.000	0.000
32	A	33	ILE	0	-0.007	0.012	25.190	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	HIS	0	-0.018	-0.003	29.409	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.842	-0.908	27.762	-0.117	-0.117	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.024	0.016	22.642	0.008	0.008	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.847	0.881	25.972	0.114	0.114	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.036	0.023	23.682	0.006	0.006	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.052	-0.037	16.557	0.007	0.007	0.000	0.000	0.000	0.000
39	A	40	ASN	0	0.018	-0.001	15.831	0.027	0.027	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.027	0.022	14.934	-0.039	-0.039	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.018	-0.017	10.853	-0.035	-0.035	0.000	0.000	0.000	0.000
42	A	43	PHE	0	0.014	0.006	12.713	0.086	0.086	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.052	0.018	4.456	0.136	0.223	-0.002	-0.008	-0.077	0.000
44	A	45	ALA	0	0.034	0.010	11.343	0.121	0.121	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.064	0.035	12.461	-0.139	-0.139	0.000	0.000	0.000	0.000
46	A	47	ALA	0	-0.009	-0.002	14.274	0.066	0.066	0.000	0.000	0.000	0.000
47	A	48	CYS	0	0.006	0.006	7.128	-0.169	-0.169	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.003	-0.005	13.159	0.011	0.011	0.000	0.000	0.000	0.000
49	A	50	TYR	0	0.052	0.029	16.295	0.022	0.022	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.891	0.938	16.643	-0.059	-0.059	0.000	0.000	0.000	0.000
51	A	72	ALA	0	0.039	0.031	22.372	-0.010	-0.010	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.002	-0.004	24.684	0.000	0.000	0.000	0.000	0.000	0.000
53	A	74	LYS	1	0.963	0.969	21.817	-0.030	-0.030	0.000	0.000	0.000	0.000
54	A	75	SER	0	0.050	0.030	19.187	0.025	0.025	0.000	0.000	0.000	0.000
55	A	76	PRO	0	-0.054	-0.006	13.944	0.004	0.004	0.000	0.000	0.000	0.000
56	A	77	SER	0	0.059	0.020	15.233	-0.036	-0.036	0.000	0.000	0.000	0.000
57	A	79	VAL	0	-0.020	-0.004	10.462	0.003	0.003	0.000	0.000	0.000	0.000
58	A	80	SER	0	0.114	0.029	8.701	-0.070	-0.070	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.127	-0.083	4.186	-0.087	0.045	-0.001	-0.012	-0.119	0.000
60	A	82	ASP	-1	-0.804	-0.857	4.589	0.870	1.029	-0.001	-0.008	-0.150	0.000
61	A	83	LEU	0	-0.011	-0.013	7.622	-0.232	-0.232	0.000	0.000	0.000	0.000
62	A	84	GLU	-1	-0.827	-0.918	9.828	0.077	0.077	0.000	0.000	0.000	0.000
63	A	85	PRO	0	-0.052	-0.028	12.525	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	86	LEU	0	-0.029	-0.007	16.062	-0.033	-0.033	0.000	0.000	0.000	0.000
65	A	87	THR	0	-0.035	-0.039	18.370	0.016	0.016	0.000	0.000	0.000	0.000
66	A	88	ILE	0	-0.064	-0.022	21.260	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	89	LEU	0	0.008	0.006	24.502	0.013	0.013	0.000	0.000	0.000	0.000
68	A	90	TYR	0	0.007	-0.005	28.299	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	91	TYR	0	0.019	0.004	30.820	0.002	0.002	0.000	0.000	0.000	0.000
70	A	92	ILE	0	0.005	0.012	34.317	0.000	0.000	0.000	0.000	0.000	0.000
71	A	93	GLY	0	0.035	0.020	36.885	0.003	0.003	0.000	0.000	0.000	0.000
72	A	94	ASN	0	0.009	-0.010	38.905	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	95	THR	0	-0.026	-0.010	37.151	0.000	0.000	0.000	0.000	0.000	0.000
74	A	96	PRO	0	0.036	0.030	33.661	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	97	LYS	1	0.863	0.925	30.666	0.026	0.026	0.000	0.000	0.000	0.000
76	A	98	ILE	0	0.023	0.017	25.988	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	99	GLU	-1	-0.883	-0.933	24.605	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	100	GLN	0	0.020	0.023	18.785	-0.023	-0.023	0.000	0.000	0.000	0.000
79	A	101	LEU	0	0.037	0.018	21.043	0.016	0.016	0.000	0.000	0.000	0.000
80	A	102	SER	0	0.011	0.002	17.651	-0.016	-0.016	0.000	0.000	0.000	0.000
81	A	103	ASN	0	-0.026	-0.031	14.535	0.011	0.011	0.000	0.000	0.000	0.000
82	A	104	MET	0	0.024	0.042	15.601	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	105	ILE	0	-0.016	0.017	11.683	-0.035	-0.035	0.000	0.000	0.000	0.000
84	A	106	VAL	0	0.004	0.003	8.969	0.054	0.054	0.000	0.000	0.000	0.000
85	A	107	LYS	1	0.873	0.935	5.432	-0.209	-0.209	0.000	0.000	0.000	0.000
86	A	108	SER	0	-0.022	-0.048	2.923	-1.069	-0.730	0.273	-0.189	-0.423	0.000
87	A	110	LYS	1	0.908	0.955	4.539	-0.152	-0.086	-0.001	-0.009	-0.055	0.000
88	A	112	SER	0	-0.004	0.003	10.652	0.110	0.110	0.000	0.000	0.000	0.000

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