FMO DATABASE

FMODB ID: 14QYZ

Calculation Name: 1VQ3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VQ3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X0X1

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:

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	86
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-557306.347859
FMO2-HF: Nuclear repulsion	522324.662108
FMO2-HF: Total energy	-34981.68575
FMO2-MP2: Total energy	-35085.945277

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:-3:HIS)

Summations of interaction energy for fragment #1(A:-3:HIS)

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.
-1.925	0.44	0.053	-0.9	-1.518	-0.001

Interaction energy analysis for fragmet #1(A:-3:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / 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	-1	HIS	0	-0.035	-0.005	3.153	-3.142	-0.882	0.054	-0.884	-1.430	-0.001
4	A	0	HIS	0	0.019	0.012	4.536	0.921	1.026	-0.001	-0.016	-0.088	0.000
5	A	1	LEU	0	-0.013	0.005	8.324	-0.296	-0.296	0.000	0.000	0.000	0.000
6	A	2	PRO	0	-0.055	-0.026	10.019	0.139	0.139	0.000	0.000	0.000	0.000
7	A	3	LEU	0	0.048	0.037	13.829	-0.004	-0.004	0.000	0.000	0.000	0.000
8	A	4	PHE	0	-0.035	-0.016	15.898	-0.049	-0.049	0.000	0.000	0.000	0.000
9	A	5	LYS	1	0.814	0.888	19.582	-0.195	-0.195	0.000	0.000	0.000	0.000
10	A	6	PHE	0	0.012	-0.007	21.008	-0.034	-0.034	0.000	0.000	0.000	0.000
11	A	7	ALA	0	-0.008	-0.004	25.697	0.023	0.023	0.000	0.000	0.000	0.000
12	A	8	ILE	0	0.007	0.009	26.902	-0.018	-0.018	0.000	0.000	0.000	0.000
13	A	9	ASP	-1	-0.822	-0.880	30.441	0.054	0.054	0.000	0.000	0.000	0.000
14	A	10	VAL	0	0.000	-0.004	33.286	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	11	GLN	0	0.007	-0.003	35.995	0.004	0.004	0.000	0.000	0.000	0.000
16	A	12	TYR	0	0.030	0.015	39.772	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	13	ARG	1	0.838	0.916	38.673	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	14	SER	0	0.013	-0.001	43.841	0.002	0.002	0.000	0.000	0.000	0.000
19	A	15	ASN	0	-0.039	-0.012	46.428	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	16	VAL	0	-0.046	-0.017	44.877	0.001	0.001	0.000	0.000	0.000	0.000
21	A	17	ARG	1	0.819	0.896	47.963	-0.024	-0.024	0.000	0.000	0.000	0.000
22	A	18	ASP	-1	-0.722	-0.876	46.200	0.046	0.046	0.000	0.000	0.000	0.000
23	A	19	PRO	0	0.027	0.009	48.457	0.001	0.001	0.000	0.000	0.000	0.000
24	A	20	ARG	1	0.934	0.991	41.891	-0.069	-0.069	0.000	0.000	0.000	0.000
25	A	21	GLY	0	0.078	0.030	47.618	0.001	0.001	0.000	0.000	0.000	0.000
26	A	22	GLU	-1	-0.801	-0.892	48.256	0.027	0.027	0.000	0.000	0.000	0.000
27	A	23	THR	0	-0.054	-0.032	51.242	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	24	ILE	0	0.002	-0.005	46.331	0.000	0.000	0.000	0.000	0.000	0.000
29	A	25	GLU	-1	-0.815	-0.902	50.614	0.023	0.023	0.000	0.000	0.000	0.000
30	A	26	ARG	1	0.854	0.928	52.416	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	27	VAL	0	-0.016	-0.019	52.693	0.000	0.000	0.000	0.000	0.000	0.000
32	A	28	LEU	0	-0.020	-0.017	49.226	0.000	0.000	0.000	0.000	0.000	0.000
33	A	29	ARG	1	0.797	0.876	53.861	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	30	GLU	-1	-0.856	-0.928	56.956	0.027	0.027	0.000	0.000	0.000	0.000
35	A	31	GLU	-1	-0.856	-0.902	56.791	0.040	0.040	0.000	0.000	0.000	0.000
36	A	32	LYS	1	0.827	0.908	54.281	-0.044	-0.044	0.000	0.000	0.000	0.000
37	A	33	GLY	0	0.043	0.045	57.483	0.000	0.000	0.000	0.000	0.000	0.000
38	A	34	LEU	0	0.003	0.010	52.610	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	35	PRO	0	0.012	0.008	55.226	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	36	VAL	0	-0.001	-0.007	50.788	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	37	LYS	1	0.849	0.902	52.278	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	38	LYS	1	0.929	0.971	49.927	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	39	LEU	0	0.002	0.023	46.682	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	40	ARG	1	0.815	0.892	42.101	-0.017	-0.017	0.000	0.000	0.000	0.000
45	A	41	LEU	0	-0.030	-0.012	42.398	0.003	0.003	0.000	0.000	0.000	0.000
46	A	42	GLY	0	0.029	0.007	39.617	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	43	LYS	1	0.731	0.857	34.189	-0.062	-0.062	0.000	0.000	0.000	0.000
48	A	44	SER	0	0.027	0.014	32.931	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	45	ILE	0	-0.033	-0.017	28.009	0.011	0.011	0.000	0.000	0.000	0.000
50	A	46	HIS	0	0.020	0.008	27.929	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	47	LEU	0	-0.022	-0.011	23.369	0.019	0.019	0.000	0.000	0.000	0.000
52	A	48	GLU	-1	-0.805	-0.888	19.706	0.233	0.233	0.000	0.000	0.000	0.000
53	A	49	VAL	0	-0.012	-0.004	17.386	0.028	0.028	0.000	0.000	0.000	0.000
54	A	50	GLU	-1	-0.892	-0.943	11.228	0.804	0.804	0.000	0.000	0.000	0.000
55	A	51	ALA	0	-0.041	-0.031	13.085	-0.019	-0.019	0.000	0.000	0.000	0.000
56	A	52	GLU	-1	-0.789	-0.903	9.199	-0.646	-0.646	0.000	0.000	0.000	0.000
57	A	53	ASN	0	-0.028	-0.011	12.759	0.012	0.012	0.000	0.000	0.000	0.000
58	A	54	LYS	1	0.885	0.937	16.469	0.145	0.145	0.000	0.000	0.000	0.000
59	A	55	GLU	-1	-0.859	-0.943	19.795	-0.195	-0.195	0.000	0.000	0.000	0.000
60	A	56	LYS	1	0.881	0.930	11.957	0.370	0.370	0.000	0.000	0.000	0.000
61	A	57	ALA	0	0.005	-0.001	17.964	0.038	0.038	0.000	0.000	0.000	0.000
62	A	58	TYR	0	0.032	0.015	19.146	0.030	0.030	0.000	0.000	0.000	0.000
63	A	59	GLU	-1	-0.840	-0.911	21.253	-0.114	-0.114	0.000	0.000	0.000	0.000
64	A	60	ILE	0	-0.014	0.004	16.744	0.017	0.017	0.000	0.000	0.000	0.000
65	A	61	VAL	0	-0.008	0.002	21.258	0.026	0.026	0.000	0.000	0.000	0.000
66	A	62	LYS	1	0.871	0.922	23.962	0.109	0.109	0.000	0.000	0.000	0.000
67	A	63	LYS	1	0.818	0.900	23.350	0.023	0.023	0.000	0.000	0.000	0.000
68	A	64	ALA	0	0.023	0.005	23.800	0.012	0.012	0.000	0.000	0.000	0.000
69	A	65	CYS	0	-0.078	-0.048	25.644	0.010	0.010	0.000	0.000	0.000	0.000
70	A	66	GLU	-1	-0.926	-0.952	28.449	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	67	GLU	-1	-0.902	-0.939	25.625	0.032	0.032	0.000	0.000	0.000	0.000
72	A	68	LEU	0	-0.064	-0.028	27.906	0.014	0.014	0.000	0.000	0.000	0.000
73	A	69	LEU	0	-0.025	-0.006	26.811	0.000	0.000	0.000	0.000	0.000	0.000
74	A	70	VAL	0	0.001	0.004	31.002	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	71	ASN	0	0.048	0.024	33.907	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	72	PRO	0	0.060	0.026	35.321	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	73	VAL	0	-0.024	-0.007	37.362	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	74	VAL	0	-0.025	-0.025	40.685	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	75	GLU	-1	-0.786	-0.871	37.115	0.057	0.057	0.000	0.000	0.000	0.000
80	A	76	GLU	-1	-0.844	-0.903	37.796	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	77	TYR	0	-0.005	-0.027	30.018	0.008	0.008	0.000	0.000	0.000	0.000
82	A	78	GLU	-1	-0.920	-0.940	33.779	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	79	VAL	0	-0.014	-0.021	27.121	0.013	0.013	0.000	0.000	0.000	0.000
84	A	80	ARG	1	0.826	0.909	29.764	-0.054	-0.054	0.000	0.000	0.000	0.000
85	A	81	GLU	-1	-0.772	-0.877	24.859	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	82	LEU	0	-0.060	-0.021	25.679	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:HIS)