FMO DATABASE

FMODB ID: 49NKN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-578687.180348
FMO2-HF: Nuclear repulsion	545474.023136
FMO2-HF: Total energy	-33213.157213
FMO2-MP2: Total energy	-33312.529353

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.
-8.945	-1.053	4.533	-3.603	-8.819	-0.025

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 : -0.013 / 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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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	-0.009	3.820	-1.464	0.186	-0.023	-0.721	-0.906	0.004
4	A	6	SER	0	-0.021	-0.025	6.262	-0.008	-0.008	0.000	0.000	0.000	0.000
5	A	7	ILE	0	0.071	0.030	7.838	0.258	0.258	0.000	0.000	0.000	0.000
6	A	8	SER	0	0.002	-0.003	9.524	0.121	0.121	0.000	0.000	0.000	0.000
7	A	9	ASP	-1	-0.842	-0.900	7.397	0.347	0.347	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.033	-0.017	2.502	-1.391	-0.215	1.067	-0.910	-1.333	-0.007
9	A	11	THR	0	-0.032	-0.025	8.750	-0.290	-0.290	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.781	-0.884	10.742	0.615	0.615	0.000	0.000	0.000	0.000
11	A	13	ALA	0	0.031	0.011	12.204	0.049	0.049	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.761	-0.853	7.743	1.868	1.868	0.000	0.000	0.000	0.000
13	A	15	PHE	0	0.011	-0.002	7.759	0.540	0.540	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.046	0.022	8.750	-0.055	-0.055	0.000	0.000	0.000	0.000
15	A	17	GLN	0	-0.048	-0.022	8.669	0.009	0.009	0.000	0.000	0.000	0.000
16	A	18	LEU	0	0.010	0.013	2.664	-0.484	0.112	0.411	-0.141	-0.865	-0.001
17	A	19	LEU	0	0.022	0.008	6.068	-0.459	-0.459	0.000	0.000	0.000	0.000
18	A	20	LYS	1	0.759	0.863	9.180	-0.548	-0.548	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.875	-0.912	5.545	0.222	0.222	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.031	0.007	6.264	-0.232	-0.232	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.812	-0.878	8.418	0.212	0.212	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.761	0.866	9.376	0.093	0.093	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.847	-0.940	7.631	-0.467	-0.467	0.000	0.000	0.000	0.000
24	A	26	ASN	0	-0.023	0.003	10.807	-0.033	-0.033	0.000	0.000	0.000	0.000
25	A	27	VAL	0	-0.066	-0.021	13.444	0.015	0.015	0.000	0.000	0.000	0.000
26	A	28	ALA	0	-0.026	0.006	12.635	0.018	0.018	0.000	0.000	0.000	0.000
27	A	29	ALA	0	-0.070	-0.037	14.700	0.009	0.009	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.086	-0.070	13.970	0.026	0.026	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.816	-0.908	12.870	-0.310	-0.310	0.000	0.000	0.000	0.000
30	A	32	ASP	-1	-0.925	-0.937	10.597	-0.551	-0.551	0.000	0.000	0.000	0.000
31	A	33	VAL	0	-0.036	-0.024	5.874	-0.192	-0.192	0.000	0.000	0.000	0.000
32	A	34	LEU	0	0.047	0.016	6.422	-0.331	-0.331	0.000	0.000	0.000	0.000
33	A	35	ASP	-1	-0.824	-0.911	7.855	-0.567	-0.567	0.000	0.000	0.000	0.000
34	A	36	VAL	0	-0.035	-0.012	3.273	-0.468	-0.155	0.020	-0.074	-0.259	0.000
35	A	37	LEU	0	-0.071	-0.039	2.587	-1.635	-0.609	0.374	-0.255	-1.144	-0.003
36	A	38	LEU	0	0.034	0.006	4.418	0.367	0.441	-0.001	-0.007	-0.066	0.000
37	A	39	GLU	-1	-0.931	-0.956	6.536	-0.725	-0.725	0.000	0.000	0.000	0.000
38	A	40	HIS	0	-0.075	-0.043	2.736	-4.362	-1.457	2.687	-1.487	-4.105	-0.018
39	A	41	PHE	0	0.006	0.000	4.857	0.345	0.410	-0.001	-0.004	-0.059	0.000
40	A	42	VAL	0	0.049	0.038	6.663	0.133	0.133	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.837	0.927	4.265	1.259	1.346	-0.001	-0.004	-0.082	0.000
42	A	44	ILE	0	-0.053	-0.029	5.146	0.114	0.114	0.000	0.000	0.000	0.000
43	A	45	THR	0	-0.047	-0.030	8.714	0.082	0.082	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.908	-0.919	11.122	0.049	0.049	0.000	0.000	0.000	0.000
45	A	47	HIS	0	0.003	0.008	13.517	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	48	PRO	0	-0.039	-0.029	15.552	-0.028	-0.028	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.838	-0.918	17.418	0.019	0.019	0.000	0.000	0.000	0.000
48	A	50	GLY	0	-0.023	-0.003	13.524	-0.021	-0.021	0.000	0.000	0.000	0.000
49	A	51	THR	0	0.025	-0.019	11.219	0.026	0.026	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.875	-0.933	13.604	-0.030	-0.030	0.000	0.000	0.000	0.000
51	A	53	LEU	0	-0.050	-0.011	13.501	0.028	0.028	0.000	0.000	0.000	0.000
52	A	54	ILE	0	-0.052	-0.039	10.340	0.036	0.036	0.000	0.000	0.000	0.000
53	A	55	TYR	0	-0.033	-0.036	13.061	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	56	TYR	0	-0.095	-0.041	17.598	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	57	PRO	0	0.012	0.031	19.426	0.003	0.003	0.000	0.000	0.000	0.000
56	A	58	SER	0	0.026	-0.003	20.674	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.846	-0.928	23.673	0.057	0.057	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.172	-0.082	26.628	0.003	0.003	0.000	0.000	0.000	0.000
59	A	61	ARG	1	0.734	0.868	17.798	-0.146	-0.146	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.843	-0.893	21.756	0.193	0.193	0.000	0.000	0.000	0.000
61	A	63	ASP	-1	-0.883	-0.938	19.336	0.140	0.140	0.000	0.000	0.000	0.000
62	A	64	SER	0	-0.006	-0.032	18.323	0.017	0.017	0.000	0.000	0.000	0.000
63	A	65	PRO	0	0.035	-0.009	13.231	0.015	0.015	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.958	-0.987	14.912	0.364	0.364	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.023	0.022	17.119	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	68	ILE	0	0.016	0.010	13.037	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.042	-0.020	12.947	0.004	0.004	0.000	0.000	0.000	0.000
68	A	70	LYS	1	0.814	0.886	15.259	-0.196	-0.196	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.799	-0.898	17.653	0.119	0.119	0.000	0.000	0.000	0.000
70	A	72	ILE	0	-0.014	-0.001	11.947	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	73	LYS	1	0.803	0.875	16.144	-0.380	-0.380	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.851	-0.907	17.620	0.156	0.156	0.000	0.000	0.000	0.000
73	A	75	TRP	0	0.033	0.027	17.450	-0.022	-0.022	0.000	0.000	0.000	0.000
74	A	76	ARG	1	0.789	0.853	14.200	-0.186	-0.186	0.000	0.000	0.000	0.000
75	A	77	ALA	0	-0.016	0.003	18.774	-0.018	-0.018	0.000	0.000	0.000	0.000
76	A	78	ALA	0	-0.016	-0.006	21.632	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	79	ASN	0	-0.084	-0.044	21.068	-0.030	-0.030	0.000	0.000	0.000	0.000
78	A	80	GLY	0	-0.038	-0.007	22.710	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.896	0.956	17.434	-0.061	-0.061	0.000	0.000	0.000	0.000
80	A	82	PRO	0	-0.001	0.003	15.538	0.014	0.014	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.051	0.025	15.284	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.012	0.001	10.370	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	85	LYS	1	0.870	0.953	10.378	-1.173	-1.173	0.000	0.000	0.000	0.000
84	A	86	GLN	0	-0.006	-0.008	14.125	0.032	0.032	0.000	0.000	0.000	0.000
85	A	87	GLY	0	-0.009	-0.007	16.261	0.024	0.024	0.000	0.000	0.000	0.000

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