FMO DATABASE

FMODB ID: 53L8Z

Calculation Name: 2CUW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CUW

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SI58

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	83
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-475960.50348
FMO2-HF: Nuclear repulsion	444541.907216
FMO2-HF: Total energy	-31418.596264
FMO2-MP2: Total energy	-31511.156858

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:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-19.197	-10.322	11.179	-8.13	-11.926	-0.067

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.021 / q_NPA : 0.010

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	TYR	0	0.012	-0.038	2.510	-4.049	0.297	2.530	-2.342	-4.535	-0.008
4	A	5	GLN	0	-0.046	-0.051	5.605	0.446	0.446	0.000	0.000	0.000	0.000
5	A	6	ALA	0	-0.006	-0.005	9.361	-0.082	-0.082	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.044	-0.036	11.978	0.071	0.071	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.037	-0.018	15.306	-0.002	-0.002	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.033	0.025	17.740	0.044	0.044	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.025	-0.025	21.380	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.767	-0.848	24.058	-0.153	-0.153	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.047	0.025	27.467	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.825	0.913	30.511	0.154	0.154	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.855	0.912	29.891	0.176	0.176	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.035	0.016	35.229	0.001	0.001	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.067	-0.022	34.748	0.007	0.007	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.015	-0.007	37.338	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.732	-0.868	33.940	-0.112	-0.112	0.000	0.000	0.000	0.000
18	A	19	PRO	0	-0.023	-0.016	36.950	0.003	0.003	0.000	0.000	0.000	0.000
19	A	20	GLN	0	-0.006	-0.001	32.328	0.008	0.008	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.038	0.021	35.599	0.002	0.002	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.806	0.873	36.285	0.102	0.102	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.022	0.002	39.232	0.004	0.004	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.005	-0.001	35.067	0.004	0.004	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.789	-0.896	38.129	-0.089	-0.089	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.027	-0.005	39.951	0.002	0.002	0.000	0.000	0.000	0.000
26	A	27	VAL	0	0.058	0.021	40.532	0.002	0.002	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.014	-0.007	36.271	0.002	0.002	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.838	0.927	40.931	0.076	0.076	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.925	-0.957	44.283	-0.049	-0.049	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.086	-0.044	40.875	0.003	0.003	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.029	-0.007	44.252	0.001	0.001	0.000	0.000	0.000	0.000
32	A	33	HIS	0	-0.057	-0.028	39.901	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	34	PRO	0	-0.011	-0.027	40.956	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.017	0.023	37.159	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.964	-0.979	38.967	-0.091	-0.091	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.851	-0.902	35.158	-0.119	-0.119	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.048	-0.026	33.214	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.774	0.845	29.497	0.153	0.153	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.031	-0.018	30.367	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	41	GLY	0	-0.003	0.006	27.249	0.003	0.003	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.796	0.887	24.341	0.180	0.180	0.000	0.000	0.000	0.000
42	A	43	VAL	0	0.028	0.006	19.946	-0.016	-0.016	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.039	-0.015	18.240	0.026	0.026	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.788	-0.861	15.017	-0.411	-0.411	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.015	0.002	12.353	0.049	0.049	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.008	-0.008	8.913	-0.124	-0.124	0.000	0.000	0.000	0.000
47	A	48	PHE	0	-0.051	-0.024	8.115	0.152	0.152	0.000	0.000	0.000	0.000
48	A	49	PRO	0	0.001	0.004	4.486	-0.507	-0.442	-0.001	-0.039	-0.025	0.000
49	A	50	ALA	0	-0.067	-0.043	2.945	0.851	1.557	0.012	-0.256	-0.462	0.000
50	A	51	GLU	-1	-0.864	-0.932	1.965	-8.918	-9.443	6.522	-3.170	-2.827	-0.037
51	A	52	ASN	0	-0.012	-0.012	3.167	-1.240	0.006	0.234	-0.444	-1.036	-0.003
52	A	53	LEU	0	0.057	0.025	3.905	0.388	0.432	-0.001	0.016	-0.060	0.000
53	A	54	LEU	0	0.020	0.016	6.569	0.367	0.367	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.709	-0.842	6.636	-1.686	-1.686	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.014	-0.014	6.033	0.220	0.220	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.847	-0.923	8.003	-0.448	-0.448	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.951	-0.973	11.265	-0.647	-0.647	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.786	0.888	6.662	1.687	1.687	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.005	0.003	11.601	0.145	0.145	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.877	0.917	13.380	0.738	0.738	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.035	-0.006	15.301	0.080	0.080	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.022	-0.016	11.974	0.096	0.096	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.030	0.011	17.019	0.050	0.050	0.000	0.000	0.000	0.000
64	A	65	ALA	0	-0.052	-0.039	19.337	0.045	0.045	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.048	-0.011	18.965	0.033	0.033	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.019	-0.007	19.409	0.030	0.030	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.007	0.008	23.154	0.017	0.017	0.000	0.000	0.000	0.000
68	A	69	ASN	0	0.027	0.001	25.444	0.004	0.004	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.061	0.023	27.882	0.001	0.001	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.022	0.004	29.786	0.000	0.000	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.002	-0.002	31.591	0.003	0.003	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.817	-0.887	27.615	-0.164	-0.164	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.001	-0.006	25.999	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.005	0.002	18.398	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	76	ALA	0	0.021	0.011	20.712	0.000	0.000	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.046	-0.018	12.757	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.896	-0.943	16.664	-0.335	-0.335	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.016	-0.010	14.048	0.005	0.005	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.007	0.002	8.522	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.886	0.957	8.480	0.533	0.533	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.800	-0.878	2.536	-7.476	-4.660	1.885	-1.882	-2.819	-0.019
82	A	83	LEU	0	-0.063	-0.032	4.402	0.265	0.376	-0.001	-0.009	-0.101	0.000
83	A	84	PRO	0	0.027	0.026	4.600	0.342	0.408	-0.001	-0.004	-0.061	0.000

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