FMO DATABASE

FMODB ID: JQK39

Calculation Name: 4ABM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4ABM

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H444

Base Structure: X-ray

Registration Date: 2023-09-23

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	79
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-481875.499482
FMO2-HF: Nuclear repulsion	449645.877669
FMO2-HF: Total energy	-32229.621813
FMO2-MP2: Total energy	-32324.124087

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:19:GLY)

Summations of interaction energy for fragment #1(A:19:GLY)

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.
-9.271	-9.423	12.076	-6.105	-5.82	-0.045

Interaction energy analysis for fragmet #1(A:19:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.038 / q_NPA : 0.015

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	21	MET	0	0.006	0.004	3.853	-0.168	1.688	-0.008	-1.027	-0.821	0.004
4	A	22	GLU	-1	-0.825	-0.905	1.929	-14.079	-16.865	12.080	-4.894	-4.401	-0.049
5	A	23	GLN	0	0.029	-0.003	3.401	2.353	3.002	0.005	-0.177	-0.476	0.000
6	A	24	GLU	-1	-0.923	-0.942	5.321	-0.438	-0.309	-0.001	-0.007	-0.122	0.000
7	A	25	ALA	0	0.021	0.006	7.695	0.609	0.609	0.000	0.000	0.000	0.000
8	A	26	ILE	0	0.003	0.001	4.947	0.503	0.503	0.000	0.000	0.000	0.000
9	A	27	GLN	0	-0.017	-0.008	8.839	0.342	0.342	0.000	0.000	0.000	0.000
10	A	28	ARG	1	0.760	0.860	11.376	1.281	1.281	0.000	0.000	0.000	0.000
11	A	29	LEU	0	-0.025	0.014	10.664	0.193	0.193	0.000	0.000	0.000	0.000
12	A	30	ARG	1	0.918	0.934	9.331	1.051	1.051	0.000	0.000	0.000	0.000
13	A	31	ASP	-1	-0.801	-0.878	14.831	-0.629	-0.629	0.000	0.000	0.000	0.000
14	A	32	THR	0	-0.076	-0.051	16.706	0.101	0.101	0.000	0.000	0.000	0.000
15	A	33	GLU	-1	-0.767	-0.876	14.783	-0.476	-0.476	0.000	0.000	0.000	0.000
16	A	34	GLU	-1	-0.840	-0.874	19.029	-0.272	-0.272	0.000	0.000	0.000	0.000
17	A	35	MET	0	-0.062	-0.023	21.090	0.064	0.064	0.000	0.000	0.000	0.000
18	A	36	LEU	0	-0.023	-0.025	20.662	0.039	0.039	0.000	0.000	0.000	0.000
19	A	37	SER	0	0.021	0.006	22.365	0.034	0.034	0.000	0.000	0.000	0.000
20	A	38	LYS	1	0.898	0.928	24.566	0.281	0.281	0.000	0.000	0.000	0.000
21	A	39	LYS	1	0.845	0.924	26.682	0.258	0.258	0.000	0.000	0.000	0.000
22	A	40	GLN	0	-0.008	-0.012	25.965	0.011	0.011	0.000	0.000	0.000	0.000
23	A	41	GLU	-1	-0.837	-0.920	27.184	-0.177	-0.177	0.000	0.000	0.000	0.000
24	A	42	PHE	0	-0.071	-0.035	30.909	0.017	0.017	0.000	0.000	0.000	0.000
25	A	43	LEU	0	-0.046	-0.035	31.101	0.014	0.014	0.000	0.000	0.000	0.000
26	A	44	GLU	-1	-0.861	-0.928	31.325	-0.118	-0.118	0.000	0.000	0.000	0.000
27	A	45	LYS	1	0.859	0.927	34.859	0.103	0.103	0.000	0.000	0.000	0.000
28	A	46	LYS	1	0.816	0.901	36.843	0.108	0.108	0.000	0.000	0.000	0.000
29	A	47	ILE	0	0.016	-0.007	35.872	0.009	0.009	0.000	0.000	0.000	0.000
30	A	48	GLU	-1	-0.797	-0.885	38.068	-0.082	-0.082	0.000	0.000	0.000	0.000
31	A	49	GLN	0	0.018	0.026	41.111	0.006	0.006	0.000	0.000	0.000	0.000
32	A	50	GLU	-1	-0.773	-0.865	42.413	-0.080	-0.080	0.000	0.000	0.000	0.000
33	A	51	LEU	0	0.009	0.010	41.610	0.005	0.005	0.000	0.000	0.000	0.000
34	A	52	THR	0	-0.038	-0.028	44.749	0.006	0.006	0.000	0.000	0.000	0.000
35	A	53	ALA	0	-0.057	-0.035	46.983	0.004	0.004	0.000	0.000	0.000	0.000
36	A	54	ALA	0	-0.018	-0.021	48.256	0.003	0.003	0.000	0.000	0.000	0.000
37	A	55	LYS	1	0.953	0.973	47.399	0.057	0.057	0.000	0.000	0.000	0.000
38	A	56	LYS	1	0.984	1.012	50.156	0.064	0.064	0.000	0.000	0.000	0.000
39	A	57	HIS	0	-0.079	-0.028	52.914	0.001	0.001	0.000	0.000	0.000	0.000
40	A	58	GLY	0	0.058	0.021	54.013	0.002	0.002	0.000	0.000	0.000	0.000
41	A	59	THR	0	-0.011	-0.026	55.638	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	60	LYS	1	0.918	0.988	56.109	0.051	0.051	0.000	0.000	0.000	0.000
43	A	61	ASN	0	0.070	0.024	57.128	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	62	LYS	1	1.049	1.030	54.657	0.046	0.046	0.000	0.000	0.000	0.000
45	A	63	ARG	1	0.957	0.993	53.831	0.055	0.055	0.000	0.000	0.000	0.000
46	A	64	ALA	0	0.076	0.018	52.978	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	65	ALA	0	0.014	0.012	51.387	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	66	LEU	0	-0.022	-0.016	50.298	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	67	GLN	0	-0.019	-0.014	48.900	0.000	0.000	0.000	0.000	0.000	0.000
50	A	68	ALA	0	0.027	0.018	47.009	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	69	LEU	0	0.009	0.008	45.566	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	70	LYS	1	0.940	0.967	44.584	0.076	0.076	0.000	0.000	0.000	0.000
53	A	71	ARG	1	0.825	0.897	42.664	0.077	0.077	0.000	0.000	0.000	0.000
54	A	72	LYS	1	0.822	0.897	41.019	0.072	0.072	0.000	0.000	0.000	0.000
55	A	73	LYS	1	1.003	1.000	39.893	0.066	0.066	0.000	0.000	0.000	0.000
56	A	74	ARG	1	0.872	0.949	37.570	0.121	0.121	0.000	0.000	0.000	0.000
57	A	75	TYR	0	-0.005	-0.024	36.363	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	76	GLU	-1	-0.738	-0.853	35.127	-0.088	-0.088	0.000	0.000	0.000	0.000
59	A	77	LYS	1	0.922	0.974	34.676	0.117	0.117	0.000	0.000	0.000	0.000
60	A	78	GLN	0	0.005	-0.013	32.610	0.002	0.002	0.000	0.000	0.000	0.000
61	A	79	LEU	0	0.027	0.031	30.080	-0.011	-0.011	0.000	0.000	0.000	0.000
62	A	80	ALA	0	0.068	0.039	29.689	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	81	GLN	0	-0.052	-0.034	28.900	0.005	0.005	0.000	0.000	0.000	0.000
64	A	82	ILE	0	-0.033	0.004	25.933	-0.016	-0.016	0.000	0.000	0.000	0.000
65	A	83	ASP	-1	-0.782	-0.892	25.002	-0.177	-0.177	0.000	0.000	0.000	0.000
66	A	84	GLY	0	-0.014	-0.002	24.449	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	85	THR	0	-0.067	-0.043	21.670	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	86	LEU	0	0.001	0.000	20.016	-0.035	-0.035	0.000	0.000	0.000	0.000
69	A	87	SER	0	0.040	0.003	19.552	-0.023	-0.023	0.000	0.000	0.000	0.000
70	A	88	THR	0	-0.111	-0.055	18.812	0.005	0.005	0.000	0.000	0.000	0.000
71	A	89	ILE	0	-0.064	-0.034	15.658	-0.036	-0.036	0.000	0.000	0.000	0.000
72	A	90	GLU	-1	-0.846	-0.909	14.871	-0.301	-0.301	0.000	0.000	0.000	0.000
73	A	91	PHE	0	0.024	0.008	14.473	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	92	GLN	0	-0.061	-0.020	11.723	-0.066	-0.066	0.000	0.000	0.000	0.000
75	A	93	ARG	1	0.725	0.809	10.297	0.394	0.394	0.000	0.000	0.000	0.000
76	A	94	GLU	-1	-0.803	-0.904	9.651	-0.348	-0.348	0.000	0.000	0.000	0.000
77	A	95	ALA	0	-0.079	-0.026	10.322	0.112	0.112	0.000	0.000	0.000	0.000
78	A	96	LEU	0	-0.049	-0.011	6.375	0.065	0.065	0.000	0.000	0.000	0.000
79	A	97	GLU	-1	-0.909	-0.936	5.505	-0.358	-0.358	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:19:GLY)