FMO DATABASE

FMODB ID: VQN61

Calculation Name: 1OUZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OUZ

Chain ID: A

ChEMBL ID:

UniProt ID: P0A6X7

Base Structure: X-ray

Registration Date: 2023-09-23

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	95
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-580289.913583
FMO2-HF: Nuclear repulsion	542823.413013
FMO2-HF: Total energy	-37466.500569
FMO2-MP2: Total energy	-37577.639873

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:2:ALA)

Summations of interaction energy for fragment #1(A:2: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.
-1.755	-0.262	-0.009	-0.785	-0.7	0.004

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.017 / q_NPA : 0.003

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	4	THR	0	-0.020	-0.036	3.872	0.418	1.999	-0.008	-0.773	-0.801	0.004
4	A	5	LYS	1	0.883	0.899	6.357	1.158	1.158	0.000	0.000	0.000	0.000
5	A	6	ALA	0	-0.008	0.028	8.785	0.295	0.295	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.723	-0.851	5.087	-4.555	-4.643	-0.001	-0.012	0.101	0.000
7	A	8	MET	0	-0.066	-0.022	9.192	0.298	0.298	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.009	-0.021	11.335	0.233	0.233	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.784	-0.875	12.136	-0.583	-0.583	0.000	0.000	0.000	0.000
10	A	11	TYR	0	0.043	-0.004	10.599	0.142	0.142	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.026	0.002	14.434	0.102	0.102	0.000	0.000	0.000	0.000
12	A	13	PHE	0	-0.010	-0.006	17.043	0.070	0.070	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.911	-0.963	15.292	-0.514	-0.514	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.803	0.905	13.663	0.595	0.595	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.044	-0.022	19.576	0.037	0.037	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.028	0.039	21.557	0.024	0.024	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.030	-0.005	20.577	0.017	0.017	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.003	-0.044	21.511	-0.032	-0.032	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.846	0.888	16.305	0.561	0.561	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.867	0.943	19.361	0.227	0.227	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.744	-0.840	21.033	-0.316	-0.316	0.000	0.000	0.000	0.000
22	A	23	ALA	0	0.006	0.013	17.497	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.977	0.986	16.181	0.472	0.472	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.985	-0.993	17.258	-0.321	-0.321	0.000	0.000	0.000	0.000
25	A	26	LEU	0	0.037	0.011	19.470	0.008	0.008	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.023	-0.005	12.741	0.002	0.002	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.819	-0.891	15.200	-0.558	-0.558	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.043	0.012	16.698	0.033	0.033	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.019	0.005	13.102	0.042	0.042	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.031	-0.031	10.202	0.019	0.019	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.825	-0.898	15.908	-0.211	-0.211	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.796	-0.860	19.281	-0.161	-0.161	0.000	0.000	0.000	0.000
33	A	34	ILE	0	-0.050	-0.020	15.905	0.033	0.033	0.000	0.000	0.000	0.000
34	A	35	ARG	1	0.740	0.845	15.232	0.379	0.379	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.890	0.915	19.519	0.208	0.208	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.036	0.035	22.396	0.019	0.019	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.079	-0.051	18.447	0.021	0.021	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.949	-0.980	22.659	-0.115	-0.115	0.000	0.000	0.000	0.000
39	A	40	ASN	0	-0.062	-0.037	24.560	0.018	0.018	0.000	0.000	0.000	0.000
40	A	41	GLY	0	-0.055	-0.021	26.179	0.009	0.009	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.933	-0.969	25.814	-0.088	-0.088	0.000	0.000	0.000	0.000
42	A	43	GLN	0	-0.045	-0.030	24.009	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.077	0.044	19.366	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.825	0.895	21.389	0.076	0.076	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.040	0.034	16.442	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.044	0.010	19.715	0.016	0.016	0.000	0.000	0.000	0.000
47	A	48	GLY	0	-0.014	-0.010	20.479	-0.016	-0.016	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.016	-0.006	11.611	0.009	0.009	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.028	-0.004	17.144	0.038	0.038	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.017	0.000	18.410	-0.034	-0.034	0.000	0.000	0.000	0.000
51	A	52	PHE	0	0.032	0.009	13.595	0.020	0.020	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.809	-0.878	19.303	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	54	LEU	0	0.032	0.042	21.710	0.012	0.012	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.890	0.934	23.556	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.750	-0.830	25.385	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.856	0.926	23.898	-0.046	-0.046	0.000	0.000	0.000	0.000
57	A	58	ASN	0	0.070	0.028	28.436	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	59	GLN	0	0.014	0.009	30.467	0.003	0.003	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.933	0.980	24.821	-0.080	-0.080	0.000	0.000	0.000	0.000
60	A	61	PRO	0	0.053	0.019	31.568	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	62	GLY	0	-0.030	-0.026	29.280	0.006	0.006	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.885	0.933	28.829	-0.091	-0.091	0.000	0.000	0.000	0.000
63	A	64	ASN	0	0.007	0.011	28.011	0.019	0.019	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.024	-0.028	23.903	0.002	0.002	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.915	0.963	22.789	-0.157	-0.157	0.000	0.000	0.000	0.000
66	A	67	THR	0	0.007	0.005	28.135	0.000	0.000	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.017	0.016	31.022	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.880	-0.935	32.550	0.058	0.058	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.816	-0.895	32.465	0.075	0.075	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.002	-0.003	30.265	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	72	PRO	0	-0.034	-0.008	31.494	0.005	0.005	0.000	0.000	0.000	0.000
72	A	73	ILE	0	-0.023	-0.014	26.133	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.041	0.008	29.258	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.019	0.010	28.707	0.003	0.003	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.876	0.938	23.817	-0.034	-0.034	0.000	0.000	0.000	0.000
76	A	77	ARG	1	0.917	0.933	24.540	0.040	0.040	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.067	-0.035	20.774	0.002	0.002	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.076	0.046	17.479	0.000	0.000	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.103	-0.060	18.051	0.025	0.025	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.055	0.009	13.931	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.832	0.916	17.095	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	83	PRO	0	0.046	0.041	15.471	-0.024	-0.024	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.058	0.013	17.417	0.010	0.010	0.000	0.000	0.000	0.000
84	A	85	GLN	0	0.038	0.007	19.291	0.013	0.013	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.974	0.993	19.887	0.055	0.055	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.013	0.020	12.819	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	88	LYS	1	0.884	0.931	16.132	-0.061	-0.061	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.030	-0.009	17.519	0.026	0.026	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.857	0.939	13.983	0.071	0.071	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.039	-0.023	12.189	0.020	0.020	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.902	-0.936	14.426	0.202	0.202	0.000	0.000	0.000	0.000
92	A	93	ASN	0	0.001	0.007	16.831	0.021	0.021	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.029	-0.001	11.498	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.030	0.010	12.247	-0.030	-0.030	0.000	0.000	0.000	0.000
95	A	96	PRO	0	-0.043	-0.009	8.647	0.117	0.117	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)