FMO DATABASE

FMODB ID: MV9LZ

Calculation Name: 3TQN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3TQN

Chain ID: A

ChEMBL ID:

UniProt ID: Q83DG1

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:

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	107
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-826673.058987
FMO2-HF: Nuclear repulsion	782581.975239
FMO2-HF: Total energy	-44091.083748
FMO2-MP2: Total energy	-44219.647021

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:MET)

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

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.
-20.98	-14.627	6.314	-3.394	-9.276	-0.018

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.004

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	3	ARG	1	0.947	0.971	2.454	-17.550	-13.344	5.255	-3.568	-5.894	-0.015
4	A	4	TRP	0	-0.005	-0.017	2.422	-1.718	-0.436	1.059	0.297	-2.638	-0.003
5	A	5	ASP	-1	-0.879	-0.926	4.246	-3.923	-3.687	-0.001	-0.020	-0.216	0.000
6	A	6	ASP	-1	-0.803	-0.873	6.772	-0.110	-0.110	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.818	0.878	9.097	0.337	0.337	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.842	0.924	10.511	0.713	0.713	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.056	0.028	9.792	-0.262	-0.262	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.097	0.046	5.942	0.281	0.281	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.024	-0.007	8.650	0.002	0.002	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.026	-0.021	11.665	0.108	0.108	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.007	-0.005	7.450	0.113	0.113	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.016	0.011	8.202	0.140	0.140	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.806	0.876	9.801	0.698	0.698	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.818	-0.915	12.558	-0.556	-0.556	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.814	0.901	8.574	0.412	0.412	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.022	-0.007	11.976	0.123	0.123	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.001	-0.004	14.532	0.084	0.084	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.793	-0.871	13.344	-0.118	-0.118	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.036	0.023	14.664	0.061	0.061	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.035	-0.023	16.653	0.041	0.041	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.042	-0.019	19.825	0.034	0.034	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.891	-0.938	17.701	0.033	0.033	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.065	-0.024	20.521	0.030	0.030	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.052	-0.020	17.316	0.024	0.024	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.020	-0.011	14.494	-0.022	-0.022	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.026	0.014	20.769	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.869	-0.947	24.429	-0.139	-0.139	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.023	-0.010	26.439	0.016	0.016	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.864	-0.921	22.188	-0.080	-0.080	0.000	0.000	0.000	0.000
32	A	32	MET	0	-0.069	-0.038	19.706	-0.027	-0.027	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.022	0.022	16.617	0.008	0.008	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.028	0.003	13.763	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.006	0.002	15.948	-0.060	-0.060	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.091	0.036	14.253	-0.035	-0.035	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.972	0.994	13.122	0.225	0.225	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.946	0.992	12.904	0.183	0.183	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.070	0.039	8.821	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.034	-0.033	8.347	-0.234	-0.234	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.041	-0.042	8.625	-0.148	-0.148	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.891	-0.915	8.500	-0.259	-0.259	0.000	0.000	0.000	0.000
43	A	43	TYR	0	-0.046	-0.051	4.161	-0.108	0.097	-0.001	-0.018	-0.186	0.000
44	A	44	GLN	0	-0.042	-0.009	3.926	-1.476	-1.052	0.002	-0.085	-0.342	0.000
45	A	45	ILE	0	-0.001	0.011	5.431	-0.569	-0.569	0.000	0.000	0.000	0.000
46	A	46	ASN	0	0.037	0.009	7.383	0.598	0.598	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.105	0.036	10.497	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.019	0.020	13.480	0.058	0.058	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.010	-0.003	10.170	0.049	0.049	0.000	0.000	0.000	0.000
50	A	50	VAL	0	0.019	0.014	10.134	0.064	0.064	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.025	-0.032	12.784	0.142	0.142	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.914	0.982	15.367	0.799	0.799	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.001	-0.009	13.003	0.069	0.069	0.000	0.000	0.000	0.000
54	A	54	TYR	0	-0.002	-0.036	13.233	0.065	0.065	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.053	-0.032	17.501	0.053	0.053	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.001	0.018	17.950	0.040	0.040	0.000	0.000	0.000	0.000
57	A	57	LEU	0	0.025	0.005	16.289	0.045	0.045	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.040	-0.017	20.383	0.051	0.051	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.854	-0.920	23.261	-0.370	-0.370	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.851	-0.884	22.687	-0.306	-0.306	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.041	-0.009	24.769	0.042	0.042	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.021	0.022	20.679	0.029	0.029	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.007	-0.001	19.108	0.019	0.019	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.824	-0.908	23.168	-0.182	-0.182	0.000	0.000	0.000	0.000
65	A	65	LYS	1	1.005	0.998	24.001	0.302	0.302	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.835	0.897	25.167	0.185	0.185	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.913	0.948	27.034	0.131	0.131	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.058	0.028	28.152	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.002	0.004	26.444	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.020	0.027	22.596	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.043	-0.017	19.525	0.011	0.011	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.007	0.007	21.495	0.009	0.009	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.027	0.026	21.238	-0.029	-0.029	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.863	0.933	23.746	0.228	0.228	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.058	0.024	26.880	0.003	0.003	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.004	-0.004	29.645	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.004	-0.002	24.243	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.954	0.968	24.235	0.053	0.053	0.000	0.000	0.000	0.000
79	A	79	GLN	0	0.033	0.013	25.310	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.837	0.909	26.872	0.189	0.189	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.011	0.015	20.784	-0.013	-0.013	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.052	0.042	23.900	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.078	-0.058	25.501	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	GLN	0	-0.035	-0.036	23.530	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.894	-0.941	19.986	-0.228	-0.228	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.961	0.981	23.695	0.094	0.094	0.000	0.000	0.000	0.000
87	A	87	GLN	0	-0.007	-0.020	26.995	0.003	0.003	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.024	-0.009	20.071	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.049	0.020	23.775	0.000	0.000	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.026	-0.006	25.280	0.008	0.008	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.921	0.948	28.548	0.168	0.168	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.923	0.950	24.246	0.244	0.244	0.000	0.000	0.000	0.000
93	A	93	GLN	0	-0.008	0.004	20.978	-0.022	-0.022	0.000	0.000	0.000	0.000
94	A	94	TRP	0	0.025	0.022	25.454	0.010	0.010	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.033	0.016	28.573	0.014	0.014	0.000	0.000	0.000	0.000
96	A	96	GLN	0	0.023	-0.001	26.780	0.002	0.002	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.035	-0.032	26.076	0.004	0.004	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.934	0.960	29.011	0.072	0.072	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.036	-0.004	32.072	0.002	0.002	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.878	0.931	26.505	0.091	0.091	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.036	0.013	31.410	0.004	0.004	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.866	-0.896	34.441	-0.052	-0.052	0.000	0.000	0.000	0.000
103	A	103	ARG	1	0.876	0.939	30.252	0.100	0.100	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.020	0.004	32.600	0.004	0.004	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.045	0.023	36.868	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	106	ILE	0	0.003	-0.015	34.354	0.005	0.005	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-1.000	-0.977	38.134	-0.019	-0.019	0.000	0.000	0.000	0.000

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