FMO DATABASE

FMODB ID: K31M3

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	OptH
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	-476565.249488
FMO2-HF: Nuclear repulsion	445147.469594
FMO2-HF: Total energy	-31417.779895
FMO2-MP2: Total energy	-31510.410256

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.
-18.372	-9.456	15.468	-9.806	-14.577	-0.079

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 : 0.033 / q_NPA : 0.022

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	0.055	0.023	2.146	-4.568	-0.366	3.629	-2.675	-5.156	-0.007
4	A	5	GLN	0	-0.034	-0.026	5.354	0.393	0.433	-0.001	-0.002	-0.037	0.000
5	A	6	ALA	0	-0.017	-0.008	9.064	-0.072	-0.072	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.028	-0.014	11.535	0.074	0.074	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.045	-0.030	14.977	-0.005	-0.005	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.038	0.032	17.448	0.040	0.040	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.032	-0.020	21.131	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.919	-0.966	23.813	-0.191	-0.191	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.034	0.015	27.051	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.851	0.950	29.591	0.173	0.173	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.986	0.969	30.273	0.176	0.176	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.007	0.009	34.741	0.001	0.001	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.049	-0.006	33.916	0.007	0.007	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.018	-0.008	36.553	0.000	0.000	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.727	-0.856	33.529	-0.118	-0.118	0.000	0.000	0.000	0.000
18	A	19	PRO	0	-0.007	-0.001	36.466	0.003	0.003	0.000	0.000	0.000	0.000
19	A	20	GLN	0	0.024	0.006	32.223	0.006	0.006	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.072	0.035	35.174	0.003	0.003	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.822	0.898	35.808	0.101	0.101	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.018	-0.004	38.575	0.004	0.004	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.013	0.005	34.500	0.004	0.004	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.782	-0.893	37.733	-0.087	-0.087	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.039	-0.029	39.480	0.003	0.003	0.000	0.000	0.000	0.000
26	A	27	VAL	0	0.058	0.035	39.924	0.003	0.003	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.003	-0.011	35.820	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.845	0.966	40.326	0.071	0.071	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.922	-0.940	43.625	-0.048	-0.048	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.106	-0.053	40.380	0.003	0.003	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.038	-0.009	43.555	0.001	0.001	0.000	0.000	0.000	0.000
32	A	33	HIS	0	-0.051	-0.024	39.229	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	34	PRO	0	-0.003	-0.051	40.152	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.021	0.016	36.766	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.978	-0.999	38.480	-0.090	-0.090	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.906	-0.950	34.915	-0.121	-0.121	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.059	-0.014	33.106	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.837	0.902	29.128	0.155	0.155	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.004	-0.009	30.113	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.016	0.010	26.955	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.819	0.918	24.007	0.179	0.179	0.000	0.000	0.000	0.000
42	A	43	VAL	0	0.064	0.037	19.168	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.051	-0.028	17.846	0.027	0.027	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.819	-0.897	14.703	-0.394	-0.394	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.040	-0.027	11.978	0.053	0.053	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.010	-0.007	8.376	-0.129	-0.129	0.000	0.000	0.000	0.000
47	A	48	PHE	0	-0.061	-0.030	7.419	0.188	0.188	0.000	0.000	0.000	0.000
48	A	49	PRO	0	-0.021	-0.006	3.954	-0.615	-0.428	-0.001	-0.097	-0.089	0.000
49	A	50	ALA	0	-0.046	-0.029	2.413	0.883	2.075	0.143	-0.521	-0.814	0.002
50	A	51	GLU	-1	-0.871	-0.933	2.070	-7.665	-8.708	8.122	-3.326	-3.753	-0.044
51	A	52	ASN	0	0.001	0.003	2.971	-2.209	-0.710	0.357	-0.673	-1.183	-0.006
52	A	53	LEU	0	0.047	0.010	4.049	0.222	0.279	-0.001	0.010	-0.066	0.000
53	A	54	LEU	0	0.009	0.004	6.224	0.337	0.337	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.777	-0.897	6.403	-1.542	-1.542	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.033	-0.021	5.480	0.252	0.252	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.866	-0.946	7.392	-0.462	-0.462	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.952	-0.968	10.727	-0.740	-0.740	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.903	0.951	7.461	1.346	1.346	0.000	0.000	0.000	0.000
59	A	60	ALA	0	-0.003	-0.003	11.186	0.158	0.158	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.928	0.953	12.779	0.706	0.706	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.034	0.001	14.989	0.089	0.089	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.019	-0.013	11.674	0.104	0.104	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.029	0.018	16.724	0.058	0.058	0.000	0.000	0.000	0.000
64	A	65	ALA	0	-0.049	-0.044	19.018	0.048	0.048	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.075	-0.024	18.974	0.036	0.036	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.033	-0.021	18.582	0.034	0.034	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.007	0.019	22.509	0.021	0.021	0.000	0.000	0.000	0.000
68	A	69	ASN	0	0.026	0.003	25.019	0.007	0.007	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.024	0.009	27.932	0.003	0.003	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.038	-0.025	29.515	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.036	-0.007	31.149	0.007	0.007	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.831	-0.935	27.313	-0.172	-0.172	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.018	-0.009	25.884	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.010	0.008	18.415	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	76	ALA	0	0.002	-0.007	20.391	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.041	-0.014	12.620	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.895	-0.940	16.708	-0.330	-0.330	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.024	-0.016	13.822	0.005	0.005	0.000	0.000	0.000	0.000
79	A	80	LEU	0	0.006	0.009	8.322	-0.025	-0.025	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.931	0.976	8.062	0.397	0.397	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.875	-0.938	2.259	-5.518	-2.983	3.222	-2.507	-3.250	-0.024
82	A	83	LEU	0	-0.107	-0.055	4.426	0.272	0.398	-0.001	-0.011	-0.113	0.000
83	A	84	PRO	0	0.019	0.004	4.601	0.138	0.259	-0.001	-0.004	-0.116	0.000

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