FMO DATABASE

FMODB ID: Z6L7N

Calculation Name: 2CU5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CU5

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SHL7

Base Structure: X-ray

Registration Date: 2023-06-22

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	129
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1073868.2178
FMO2-HF: Nuclear repulsion	1024201.965916
FMO2-HF: Total energy	-49666.251884
FMO2-MP2: Total energy	-49814.028993

3D Structure Molmil

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:1:MET)

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

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.
-17.782	-8.698	9.027	-5.269	-12.84	-0.015

Interaction energy analysis for fragmet #1(A:1:MET)

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 : 0.000

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	3	GLY	0	-0.020	-0.012	3.871	-0.372	1.384	-0.009	-0.833	-0.913	0.004
4	A	4	VAL	0	-0.081	-0.042	2.399	0.715	1.768	1.464	-0.515	-2.003	0.001
5	A	5	VAL	0	0.034	0.028	2.544	-6.789	-4.656	1.123	-1.548	-1.707	-0.019
6	A	6	ARG	1	0.864	0.917	2.364	-13.407	-12.035	4.670	-1.593	-4.450	0.007
7	A	7	LEU	0	-0.020	0.003	4.083	0.378	0.481	0.003	-0.032	-0.074	0.000
8	A	8	GLU	-1	-0.863	-0.938	7.352	1.110	1.110	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.062	-0.046	9.742	-0.125	-0.125	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.012	0.011	13.116	0.076	0.076	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.059	-0.039	15.253	-0.055	-0.055	0.000	0.000	0.000	0.000
12	A	12	PRO	0	0.026	0.012	18.104	0.021	0.021	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.813	-0.898	20.833	0.167	0.167	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.807	-0.888	21.621	0.134	0.134	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.012	-0.006	21.414	-0.016	-0.016	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.015	-0.002	19.982	0.006	0.006	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.027	0.018	17.018	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.006	0.001	17.521	-0.063	-0.063	0.000	0.000	0.000	0.000
19	A	19	ILE	0	0.005	-0.002	12.380	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	20	THR	0	0.007	0.001	15.232	-0.100	-0.100	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.869	0.904	16.748	0.356	0.356	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.920	0.953	12.874	0.237	0.237	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.038	0.015	11.669	-0.147	-0.147	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.790	-0.882	13.223	-0.623	-0.623	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.031	-0.008	14.315	-0.045	-0.045	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.024	0.021	9.848	-0.072	-0.072	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.051	-0.019	11.618	-0.207	-0.207	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.028	-0.011	12.188	0.022	0.022	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.013	0.008	14.866	0.044	0.044	0.000	0.000	0.000	0.000
30	A	30	HIS	0	-0.016	-0.020	15.043	0.055	0.055	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.020	-0.017	17.189	0.107	0.107	0.000	0.000	0.000	0.000
32	A	32	GLY	0	0.021	0.022	18.342	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.009	0.007	16.165	0.007	0.007	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.006	0.001	11.474	-0.136	-0.136	0.000	0.000	0.000	0.000
35	A	35	TYR	0	0.007	0.013	8.201	0.146	0.146	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.004	-0.005	8.958	-0.304	-0.304	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.016	-0.002	5.663	0.208	0.208	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.058	0.029	7.277	-0.224	-0.224	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.008	0.025	5.520	0.009	0.009	0.000	0.000	0.000	0.000
40	A	40	HIS	0	-0.033	-0.044	8.012	0.018	0.018	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.020	0.007	11.605	-0.067	-0.067	0.000	0.000	0.000	0.000
42	A	42	THR	0	-0.023	-0.028	15.154	-0.035	-0.035	0.000	0.000	0.000	0.000
43	A	43	CYS	0	0.011	0.010	13.096	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.053	0.030	14.708	0.037	0.037	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.081	-0.022	10.287	-0.044	-0.044	0.000	0.000	0.000	0.000
46	A	46	THR	0	0.049	0.018	14.900	0.010	0.010	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.033	-0.021	18.003	-0.045	-0.045	0.000	0.000	0.000	0.000
48	A	48	GLN	0	0.024	0.016	20.437	0.018	0.018	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.845	-0.925	23.666	-0.130	-0.130	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.020	-0.021	25.792	0.009	0.009	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.074	-0.029	26.705	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.802	-0.867	29.855	-0.051	-0.051	0.000	0.000	0.000	0.000
53	A	53	PRO	0	-0.031	-0.031	28.888	0.002	0.002	0.000	0.000	0.000	0.000
54	A	54	THR	0	-0.023	-0.037	29.529	0.010	0.010	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.030	0.025	27.894	0.010	0.010	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.024	0.006	25.409	0.008	0.008	0.000	0.000	0.000	0.000
57	A	57	GLN	0	-0.027	-0.023	26.984	0.008	0.008	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.809	-0.877	29.483	0.008	0.008	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.025	-0.006	25.460	0.009	0.009	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.021	-0.009	23.330	0.011	0.011	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.006	0.009	27.029	0.015	0.015	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.877	0.908	30.203	0.003	0.003	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.013	-0.008	23.613	0.009	0.009	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.048	-0.025	27.610	0.017	0.017	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.946	-0.971	29.399	0.046	0.046	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.054	-0.028	28.962	0.004	0.004	0.000	0.000	0.000	0.000
67	A	67	ALA	0	-0.044	-0.016	26.496	0.011	0.011	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.028	0.028	28.129	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.763	0.829	26.203	-0.134	-0.134	0.000	0.000	0.000	0.000
70	A	70	HIS	0	0.003	0.006	29.549	0.017	0.017	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.934	0.953	31.061	-0.167	-0.167	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.021	0.010	33.269	0.011	0.011	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.004	0.000	34.598	0.005	0.005	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.810	-0.876	29.280	0.199	0.199	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.911	0.943	30.217	-0.183	-0.183	0.000	0.000	0.000	0.000
76	A	76	HIS	1	0.791	0.907	22.467	-0.352	-0.352	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.041	0.008	27.442	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.845	-0.921	23.834	0.368	0.368	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.004	0.016	25.566	0.003	0.003	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.021	-0.004	20.356	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.016	-0.041	22.767	0.024	0.024	0.000	0.000	0.000	0.000
82	A	82	HIS	0	0.019	0.019	23.774	0.002	0.002	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.016	0.021	20.137	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	84	HIS	0	-0.028	-0.013	19.295	0.042	0.042	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.020	-0.001	20.718	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.848	0.922	21.909	-0.127	-0.127	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.059	-0.016	15.945	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.025	-0.019	18.398	-0.027	-0.027	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.033	-0.025	20.113	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.080	-0.033	18.047	-0.032	-0.032	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.018	0.024	17.230	-0.037	-0.037	0.000	0.000	0.000	0.000
92	A	92	VAL	0	0.023	-0.005	12.103	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.039	-0.026	11.233	-0.067	-0.067	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.004	0.013	12.381	0.025	0.025	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.002	-0.004	13.143	-0.099	-0.099	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.004	0.006	15.433	0.063	0.063	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.031	0.011	16.882	-0.059	-0.059	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.008	0.001	16.912	0.006	0.006	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.806	-0.884	18.951	-0.365	-0.365	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.874	0.927	21.638	0.412	0.412	0.000	0.000	0.000	0.000
101	A	101	GLY	0	-0.006	-0.002	17.733	0.020	0.020	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.897	0.960	18.237	0.464	0.464	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.030	0.004	15.708	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.758	0.867	19.587	0.414	0.414	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.025	0.022	19.836	0.004	0.004	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.025	0.006	23.806	0.007	0.007	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.898	0.936	26.729	0.147	0.147	0.000	0.000	0.000	0.000
108	A	108	TRP	0	0.030	0.015	28.608	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.059	0.038	23.283	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	110	GLN	0	-0.009	0.007	21.180	-0.031	-0.031	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.022	0.008	14.858	0.020	0.020	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.006	-0.013	17.633	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	113	LEU	0	0.016	0.007	11.973	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	114	ALA	0	-0.015	-0.003	15.373	0.015	0.015	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.689	-0.792	16.798	0.321	0.321	0.000	0.000	0.000	0.000
116	A	116	PHE	0	0.003	-0.019	18.233	-0.027	-0.027	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.783	-0.858	18.655	0.402	0.402	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.010	0.047	18.913	0.057	0.057	0.000	0.000	0.000	0.000
119	A	119	PRO	0	-0.022	-0.008	20.119	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.836	0.886	15.393	-0.427	-0.427	0.000	0.000	0.000	0.000
121	A	121	VAL	0	0.000	-0.002	11.781	-0.087	-0.087	0.000	0.000	0.000	0.000
122	A	122	ARG	1	0.750	0.856	11.267	-0.275	-0.275	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.770	-0.876	4.850	2.981	3.127	-0.001	-0.004	-0.141	0.000
124	A	124	VAL	0	-0.018	-0.023	7.121	0.008	0.008	0.000	0.000	0.000	0.000
125	A	125	TRP	0	-0.063	-0.044	2.776	-4.079	-1.642	1.778	-0.737	-3.477	-0.008
126	A	126	VAL	0	-0.003	-0.009	4.723	0.688	0.772	-0.001	-0.007	-0.075	0.000
127	A	127	ARG	1	0.921	0.958	6.075	0.830	0.830	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.053	0.033	7.944	0.414	0.414	0.000	0.000	0.000	0.000
129	A	129	LEU	0	-0.013	-0.003	11.378	-0.013	-0.013	0.000	0.000	0.000	0.000

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