FMO DATABASE

FMODB ID: 43M8N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-476831.743449
FMO2-HF: Nuclear repulsion	445413.35582
FMO2-HF: Total energy	-31418.387629
FMO2-MP2: Total energy	-31510.995526

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.
-20.255	-10.49	12.829	-9.393	-13.201	-0.077

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 : 0.007 / q_NPA : 0.007

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	4	TYR	0	0.007	-0.025	2.433	-4.359	0.531	2.306	-2.482	-4.714	-0.008
4	A	5	GLN	0	-0.018	-0.034	5.585	0.481	0.481	0.000	0.000	0.000	0.000
5	A	6	ALA	0	-0.018	-0.008	9.296	-0.096	-0.096	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.036	-0.035	11.730	0.084	0.084	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.038	-0.023	15.178	-0.010	-0.010	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.023	0.022	17.634	0.047	0.047	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.030	-0.020	21.316	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.755	-0.867	23.994	-0.160	-0.160	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.050	0.026	27.227	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.859	0.945	29.992	0.161	0.161	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.893	0.934	29.935	0.179	0.179	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.012	0.010	34.884	0.001	0.001	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.064	-0.018	34.221	0.008	0.008	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.013	-0.002	36.726	0.000	0.000	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.718	-0.862	33.767	-0.111	-0.111	0.000	0.000	0.000	0.000
18	A	19	PRO	0	-0.009	-0.002	36.658	0.003	0.003	0.000	0.000	0.000	0.000
19	A	20	GLN	0	0.006	0.003	32.124	0.008	0.008	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.069	0.039	35.371	0.003	0.003	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.792	0.872	36.012	0.100	0.100	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.015	-0.006	38.885	0.004	0.004	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.015	0.000	34.677	0.004	0.004	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.806	-0.887	37.951	-0.086	-0.086	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.021	-0.019	39.685	0.003	0.003	0.000	0.000	0.000	0.000
26	A	27	VAL	0	0.046	0.020	40.210	0.003	0.003	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.007	-0.005	35.954	0.002	0.002	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.863	0.945	40.539	0.074	0.074	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.938	-0.947	43.833	-0.045	-0.045	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.101	-0.051	40.713	0.004	0.004	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.038	-0.012	43.770	0.001	0.001	0.000	0.000	0.000	0.000
32	A	33	HIS	0	-0.058	-0.028	39.443	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.000	-0.023	40.351	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.008	0.016	36.837	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.966	-0.992	38.639	-0.092	-0.092	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.881	-0.933	34.873	-0.121	-0.121	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.039	-0.021	33.211	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.756	0.863	29.088	0.157	0.157	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.033	-0.028	30.317	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.006	0.001	27.155	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.779	0.884	24.276	0.169	0.169	0.000	0.000	0.000	0.000
42	A	43	VAL	0	0.049	0.024	19.418	-0.020	-0.020	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.047	-0.025	18.277	0.030	0.030	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.799	-0.856	14.962	-0.393	-0.393	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.023	-0.021	11.841	0.063	0.063	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.020	-0.012	8.504	-0.138	-0.138	0.000	0.000	0.000	0.000
47	A	48	PHE	0	-0.051	-0.022	7.492	0.179	0.179	0.000	0.000	0.000	0.000
48	A	49	PRO	0	-0.009	0.001	4.043	-0.672	-0.501	-0.001	-0.089	-0.081	0.000
49	A	50	ALA	0	-0.032	-0.024	2.436	0.719	1.781	0.132	-0.447	-0.747	0.001
50	A	51	GLU	-1	-0.873	-0.941	1.971	-8.032	-8.647	7.494	-3.681	-3.199	-0.045
51	A	52	ASN	0	-0.007	-0.010	3.228	-1.688	-0.460	0.189	-0.472	-0.945	-0.003
52	A	53	LEU	0	0.059	0.021	4.128	0.340	0.383	-0.001	0.003	-0.044	0.000
53	A	54	LEU	0	0.018	0.007	6.449	0.398	0.398	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.748	-0.857	6.705	-1.463	-1.463	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.008	-0.009	5.901	0.303	0.303	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.832	-0.914	7.864	-0.460	-0.460	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.947	-0.963	11.119	-0.708	-0.708	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.823	0.901	7.132	1.330	1.330	0.000	0.000	0.000	0.000
59	A	60	ALA	0	-0.012	-0.010	11.345	0.167	0.167	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.883	0.920	12.896	0.786	0.786	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.035	-0.002	14.975	0.090	0.090	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.015	-0.011	11.554	0.110	0.110	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.026	0.014	16.646	0.055	0.055	0.000	0.000	0.000	0.000
64	A	65	ALA	0	-0.056	-0.042	18.974	0.047	0.047	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.075	-0.023	19.071	0.035	0.035	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.020	-0.015	18.720	0.033	0.033	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.008	0.018	22.451	0.020	0.020	0.000	0.000	0.000	0.000
68	A	69	ASN	0	0.025	0.014	24.928	0.005	0.005	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.055	0.020	27.859	0.001	0.001	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.034	-0.021	29.527	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.030	0.000	31.105	0.005	0.005	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.818	-0.918	27.310	-0.158	-0.158	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.005	-0.003	25.923	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.016	0.007	18.349	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	76	ALA	0	0.009	-0.001	20.524	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.046	-0.018	12.614	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.897	-0.944	16.843	-0.340	-0.340	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.016	-0.011	13.991	0.000	0.000	0.000	0.000	0.000	0.000
79	A	80	LEU	0	0.009	0.009	8.255	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.876	0.957	8.204	0.399	0.399	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.815	-0.895	2.380	-8.182	-5.434	2.712	-2.208	-3.251	-0.022
82	A	83	LEU	0	-0.082	-0.044	4.586	0.264	0.389	-0.001	-0.011	-0.113	0.000
83	A	84	PRO	0	0.031	0.018	4.515	0.262	0.375	-0.001	-0.006	-0.107	0.000

Top

Graph

Manual

About

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