FMO DATABASE

FMODB ID: 141RZ

Calculation Name: 4AJ5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4AJ5

Chain ID: A

ChEMBL ID:

UniProt ID: Q96BD8

Base Structure: X-ray

Registration Date: 2023-06-20

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

Total energy (hartree)

FMO2-HF: Electronic energy	-366319.507809
FMO2-HF: Nuclear repulsion	334216.347727
FMO2-HF: Total energy	-32103.160082
FMO2-MP2: Total energy	-32195.605049

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:SER)

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

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.
-5.842	-0.768	1.086	-2.594	-3.566	0.013

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.034 / q_NPA : 0.016

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	5	ASP	-1	-0.851	-0.924	3.808	-2.395	0.556	-0.021	-1.662	-1.268	0.008
4	A	6	LEU	0	-0.014	-0.007	6.686	0.641	0.641	0.000	0.000	0.000	0.000
5	A	7	GLU	-1	-0.891	-0.955	2.692	0.742	1.301	0.232	-0.209	-0.581	-0.002
6	A	8	GLN	0	-0.034	-0.024	2.646	-1.986	-0.482	0.876	-0.715	-1.666	0.007
7	A	9	LEU	0	-0.002	0.013	4.917	-0.755	-0.695	-0.001	-0.008	-0.051	0.000
8	A	10	CYS	0	0.000	-0.002	7.678	-0.190	-0.190	0.000	0.000	0.000	0.000
9	A	11	SER	0	-0.016	-0.010	5.998	-0.276	-0.276	0.000	0.000	0.000	0.000
10	A	12	HIS	0	0.010	0.009	8.453	-0.363	-0.363	0.000	0.000	0.000	0.000
11	A	13	VAL	0	0.004	-0.007	10.468	-0.180	-0.180	0.000	0.000	0.000	0.000
12	A	14	ASN	0	-0.004	-0.010	10.555	-0.220	-0.220	0.000	0.000	0.000	0.000
13	A	15	GLU	-1	-0.822	-0.888	12.046	0.446	0.446	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.923	0.967	13.761	-0.385	-0.385	0.000	0.000	0.000	0.000
15	A	17	ILE	0	-0.008	-0.012	16.165	-0.062	-0.062	0.000	0.000	0.000	0.000
16	A	18	GLY	0	0.002	-0.012	16.615	-0.045	-0.045	0.000	0.000	0.000	0.000
17	A	19	ASN	0	-0.034	-0.040	16.679	-0.065	-0.065	0.000	0.000	0.000	0.000
18	A	20	ILE	0	0.012	0.031	19.340	-0.038	-0.038	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.985	0.993	19.761	-0.334	-0.334	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.918	0.972	17.025	-0.435	-0.435	0.000	0.000	0.000	0.000
21	A	23	THR	0	0.008	-0.016	23.418	-0.026	-0.026	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.053	-0.011	25.324	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.013	-0.011	26.379	-0.017	-0.017	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.011	0.009	27.336	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.918	0.961	29.548	-0.132	-0.132	0.000	0.000	0.000	0.000
26	A	28	ASN	0	0.007	-0.007	31.055	-0.013	-0.013	0.000	0.000	0.000	0.000
27	A	29	CYS	0	0.018	0.003	31.319	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	30	GLY	0	0.048	0.046	33.903	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	31	GLN	0	-0.076	-0.044	35.675	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.769	-0.874	36.624	0.089	0.089	0.000	0.000	0.000	0.000
31	A	33	PRO	0	0.016	0.012	38.361	0.002	0.002	0.000	0.000	0.000	0.000
32	A	34	THR	0	-0.044	-0.052	39.440	0.000	0.000	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.007	-0.018	33.997	0.002	0.002	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.882	0.955	37.988	-0.088	-0.088	0.000	0.000	0.000	0.000
35	A	37	THR	0	-0.006	0.007	39.492	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	38	VAL	0	-0.013	0.002	38.680	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	39	LEU	0	0.009	0.009	34.817	0.002	0.002	0.000	0.000	0.000	0.000
38	A	40	ASN	0	-0.013	-0.027	38.744	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	41	LYS	1	0.955	0.980	42.005	-0.082	-0.082	0.000	0.000	0.000	0.000
40	A	42	ILE	0	0.011	0.018	37.392	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	43	GLY	0	0.000	-0.004	40.653	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	44	ASP	-1	-0.905	-0.963	41.319	0.072	0.072	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.999	-1.006	43.719	0.077	0.077	0.000	0.000	0.000	0.000
44	A	46	ILE	0	-0.018	-0.017	39.579	0.001	0.001	0.000	0.000	0.000	0.000
45	A	47	ILE	0	0.006	0.005	43.085	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	48	VAL	0	-0.002	-0.004	45.963	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	49	ILE	0	-0.035	-0.001	43.258	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	50	ASN	0	0.000	0.004	44.601	0.002	0.002	0.000	0.000	0.000	0.000
49	A	51	GLU	-1	-0.809	-0.905	46.372	0.057	0.057	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.039	-0.026	49.009	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.007	0.018	44.187	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	54	ASN	0	0.015	0.006	48.870	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.782	0.878	51.344	-0.058	-0.058	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.000	0.013	48.963	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.951	-0.971	49.259	0.061	0.061	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.008	-0.015	52.483	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	59	GLU	-1	-0.954	-0.981	55.798	0.045	0.045	0.000	0.000	0.000	0.000
58	A	60	ILE	0	-0.024	-0.008	52.084	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	61	GLN	0	0.009	-0.005	55.378	0.000	0.000	0.000	0.000	0.000	0.000
60	A	62	TYR	0	-0.039	-0.023	57.066	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	63	GLN	0	-0.021	-0.014	56.428	0.000	0.000	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.899	-0.926	56.938	0.045	0.045	0.000	0.000	0.000	0.000
63	A	65	GLN	0	-0.010	-0.006	59.043	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	66	THR	0	-0.013	-0.014	62.248	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	67	ASN	0	-0.011	-0.010	60.020	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	68	ASN	0	-0.061	-0.026	60.479	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	69	SER	0	0.035	0.003	64.205	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	70	LEU	0	-0.086	-0.037	64.983	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	71	LYS	1	0.802	0.878	63.717	-0.034	-0.034	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.870	-0.930	66.760	0.031	0.031	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.038	-0.020	69.992	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	74	CYS	0	-0.058	-0.028	68.562	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.792	-0.874	68.671	0.032	0.032	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.016	-0.016	71.796	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	LEU	0	-0.070	-0.035	74.350	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	78	GLU	-1	-0.900	-0.927	71.731	0.028	0.028	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.977	-0.972	74.840	0.025	0.025	0.000	0.000	0.000	0.000
78	A	80	ASP	-1	-0.997	-0.983	76.491	0.022	0.022	0.000	0.000	0.000	0.000
79	A	81	TYR	0	-0.185	-0.110	75.760	0.000	0.000	0.000	0.000	0.000	0.000

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