FMO DATABASE

FMODB ID: 529QZ

Calculation Name: 1CEI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1CEI

Chain ID: A

ChEMBL ID:

UniProt ID: Q03708

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-579546.102567
FMO2-HF: Nuclear repulsion	546332.75986
FMO2-HF: Total energy	-33213.342707
FMO2-MP2: Total energy	-33312.721128

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-9.835	-2.179	6.146	-4.122	-9.681	-0.024

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / 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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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	5	ASN	0	0.000	-0.012	3.890	-1.453	0.240	-0.019	-0.849	-0.826	0.003
4	A	6	SER	0	-0.024	-0.025	6.800	-0.073	-0.073	0.000	0.000	0.000	0.000
5	A	7	ILE	0	0.055	0.018	7.574	0.355	0.355	0.000	0.000	0.000	0.000
6	A	8	SER	0	-0.004	-0.013	9.416	0.139	0.139	0.000	0.000	0.000	0.000
7	A	9	ASP	-1	-0.863	-0.900	7.161	0.572	0.572	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.023	-0.012	2.312	-1.528	-0.626	2.040	-1.280	-1.662	-0.007
9	A	11	THR	0	-0.022	-0.027	8.770	-0.355	-0.355	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.753	-0.873	10.771	0.776	0.776	0.000	0.000	0.000	0.000
11	A	13	ALA	0	0.016	0.014	12.496	0.025	0.025	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.733	-0.832	7.459	2.032	2.032	0.000	0.000	0.000	0.000
13	A	15	PHE	0	0.013	0.005	7.553	0.764	0.764	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.051	0.022	8.536	-0.083	-0.083	0.000	0.000	0.000	0.000
15	A	17	GLN	0	-0.051	-0.022	8.130	0.034	0.034	0.000	0.000	0.000	0.000
16	A	18	LEU	0	-0.002	0.005	2.505	-0.500	-0.092	1.005	-0.199	-1.215	-0.002
17	A	19	LEU	0	0.033	0.017	5.936	-0.598	-0.598	0.000	0.000	0.000	0.000
18	A	20	LYS	1	0.766	0.865	8.955	-0.600	-0.600	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.864	-0.911	5.548	-0.211	-0.211	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.036	0.013	6.004	-0.255	-0.255	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.812	-0.882	8.178	0.230	0.230	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.754	0.860	9.132	0.384	0.384	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.817	-0.923	7.387	-0.741	-0.741	0.000	0.000	0.000	0.000
24	A	26	ASN	0	-0.050	-0.011	10.576	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	27	VAL	0	-0.074	-0.026	13.226	0.034	0.034	0.000	0.000	0.000	0.000
26	A	28	ALA	0	-0.007	0.012	12.454	0.020	0.020	0.000	0.000	0.000	0.000
27	A	29	ALA	0	-0.076	-0.046	14.588	0.027	0.027	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.078	-0.066	13.907	0.043	0.043	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.838	-0.918	12.366	-0.406	-0.406	0.000	0.000	0.000	0.000
30	A	32	ASP	-1	-0.902	-0.926	10.394	-0.657	-0.657	0.000	0.000	0.000	0.000
31	A	33	VAL	0	-0.044	-0.024	5.527	-0.219	-0.219	0.000	0.000	0.000	0.000
32	A	34	LEU	0	0.021	0.012	6.156	-0.408	-0.408	0.000	0.000	0.000	0.000
33	A	35	ASP	-1	-0.856	-0.926	7.630	-0.661	-0.661	0.000	0.000	0.000	0.000
34	A	36	VAL	0	-0.019	-0.009	3.765	-0.274	-0.086	0.001	-0.036	-0.154	0.000
35	A	37	LEU	0	-0.057	-0.029	2.560	-2.368	-1.169	1.028	-0.381	-1.846	-0.004
36	A	38	LEU	0	0.024	0.012	4.117	0.572	0.663	-0.001	-0.007	-0.082	0.000
37	A	39	GLU	-1	-0.923	-0.961	6.665	-0.790	-0.790	0.000	0.000	0.000	0.000
38	A	40	HIS	0	-0.056	-0.031	2.748	-4.345	-1.327	2.094	-1.358	-3.754	-0.014
39	A	41	PHE	0	0.029	0.010	4.603	0.451	0.525	-0.001	-0.009	-0.064	0.000
40	A	42	VAL	0	0.039	0.032	6.687	0.145	0.145	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.830	0.921	4.544	1.335	1.418	-0.001	-0.003	-0.078	0.000
42	A	44	ILE	0	-0.062	-0.027	5.079	0.108	0.108	0.000	0.000	0.000	0.000
43	A	45	THR	0	-0.023	-0.025	8.861	0.080	0.080	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.916	-0.922	11.362	0.144	0.144	0.000	0.000	0.000	0.000
45	A	47	HIS	0	0.031	0.018	13.790	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	48	PRO	0	-0.033	-0.020	15.620	-0.032	-0.032	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.839	-0.916	17.560	0.044	0.044	0.000	0.000	0.000	0.000
48	A	50	GLY	0	-0.033	-0.021	13.556	-0.024	-0.024	0.000	0.000	0.000	0.000
49	A	51	THR	0	0.002	-0.020	11.462	0.032	0.032	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.868	-0.930	13.478	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	53	LEU	0	-0.025	-0.008	13.427	0.028	0.028	0.000	0.000	0.000	0.000
52	A	54	ILE	0	-0.016	-0.017	10.362	0.047	0.047	0.000	0.000	0.000	0.000
53	A	55	TYR	0	-0.054	-0.044	12.610	-0.018	-0.018	0.000	0.000	0.000	0.000
54	A	56	TYR	0	-0.089	-0.041	17.507	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	57	PRO	0	0.023	0.034	19.418	0.004	0.004	0.000	0.000	0.000	0.000
56	A	58	SER	0	0.036	0.012	20.738	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.882	-0.951	23.656	0.070	0.070	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.156	-0.076	26.327	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	61	ARG	1	0.684	0.823	17.523	-0.173	-0.173	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.845	-0.897	21.437	0.216	0.216	0.000	0.000	0.000	0.000
61	A	63	ASP	-1	-0.876	-0.926	19.311	0.158	0.158	0.000	0.000	0.000	0.000
62	A	64	SER	0	0.007	-0.020	17.840	0.016	0.016	0.000	0.000	0.000	0.000
63	A	65	PRO	0	0.023	-0.008	12.792	0.019	0.019	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.945	-0.975	14.470	0.432	0.432	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.014	0.017	16.826	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	68	ILE	0	0.020	0.008	13.010	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.029	-0.014	12.662	0.011	0.011	0.000	0.000	0.000	0.000
68	A	70	LYS	1	0.816	0.884	14.948	-0.236	-0.236	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.812	-0.895	17.839	0.162	0.162	0.000	0.000	0.000	0.000
70	A	72	ILE	0	-0.005	-0.002	11.975	-0.017	-0.017	0.000	0.000	0.000	0.000
71	A	73	LYS	1	0.787	0.870	16.152	-0.466	-0.466	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.859	-0.910	17.506	0.198	0.198	0.000	0.000	0.000	0.000
73	A	75	TRP	0	0.011	0.018	17.069	-0.030	-0.030	0.000	0.000	0.000	0.000
74	A	76	ARG	1	0.775	0.840	14.017	-0.313	-0.313	0.000	0.000	0.000	0.000
75	A	77	ALA	0	-0.019	-0.006	18.598	-0.020	-0.020	0.000	0.000	0.000	0.000
76	A	78	ALA	0	-0.014	-0.009	21.367	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	79	ASN	0	-0.023	-0.001	20.597	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	80	GLY	0	-0.037	-0.002	22.577	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.829	0.909	17.442	-0.118	-0.118	0.000	0.000	0.000	0.000
80	A	82	PRO	0	-0.002	0.012	15.346	0.017	0.017	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.080	0.029	14.659	0.000	0.000	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.014	0.009	10.304	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	85	LYS	1	0.804	0.903	9.894	-1.483	-1.483	0.000	0.000	0.000	0.000
84	A	86	GLN	0	0.017	0.003	14.190	0.026	0.026	0.000	0.000	0.000	0.000
85	A	87	GLY	0	-0.012	-0.004	16.341	0.022	0.022	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)