FMO DATABASE

FMODB ID: 2J32R

Calculation Name: 1JQQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JQQ

Chain ID: A

ChEMBL ID:

UniProt ID: P80667

Base Structure: X-ray

Registration Date: 2023-09-19

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
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-516336.138742
FMO2-HF: Nuclear repulsion	484467.729055
FMO2-HF: Total energy	-31868.409687
FMO2-MP2: Total energy	-31962.176925

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:1:ILE)

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

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.
-9.525	-1.844	4.7	-5.122	-7.259	-0.027

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.014 / q_NPA : 0.002

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	3	GLU	-1	-0.815	-0.889	2.665	-5.681	-1.515	0.698	-2.422	-2.443	-0.001
4	A	4	PHE	0	-0.078	-0.055	5.189	0.298	0.455	-0.001	-0.007	-0.148	0.000
5	A	5	GLY	0	0.040	0.035	2.582	-0.065	0.469	0.785	-0.403	-0.916	0.001
6	A	6	SER	0	0.030	-0.005	2.512	-5.666	-3.086	3.199	-2.254	-3.525	-0.027
7	A	7	GLU	-1	-0.915	-0.935	3.725	0.827	1.071	0.019	-0.036	-0.227	0.000
8	A	8	PRO	0	-0.012	-0.017	7.018	-0.208	-0.208	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.004	0.003	8.359	0.097	0.097	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.875	-0.940	11.393	-0.046	-0.046	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.030	-0.009	14.996	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.011	0.007	17.160	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.920	0.967	12.422	-0.068	-0.068	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.032	-0.004	13.292	0.005	0.005	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.806	-0.877	16.976	-0.017	-0.017	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.010	-0.004	18.731	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.001	-0.007	21.280	0.021	0.021	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.839	0.902	23.619	0.065	0.065	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.021	0.024	26.647	0.010	0.010	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.019	0.000	27.763	0.002	0.002	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.033	-0.032	30.289	0.003	0.003	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.815	-0.892	29.875	-0.083	-0.083	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.026	-0.031	23.832	0.007	0.007	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.015	-0.010	27.650	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.032	-0.008	23.838	0.007	0.007	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.929	-0.948	25.795	-0.028	-0.028	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.021	-0.017	21.186	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	28	PRO	0	-0.018	-0.034	22.180	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.944	-0.948	18.804	-0.118	-0.118	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.040	-0.010	15.322	-0.023	-0.023	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.834	-0.925	17.871	-0.071	-0.071	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.030	0.021	18.513	-0.018	-0.018	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.022	-0.016	21.140	0.015	0.015	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.010	-0.018	23.619	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.867	0.952	26.555	0.097	0.097	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.909	0.945	29.269	0.051	0.051	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.019	-0.017	30.327	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.826	-0.908	25.560	-0.136	-0.136	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.013	-0.008	24.344	0.006	0.006	0.000	0.000	0.000	0.000
40	A	40	MET	0	-0.013	0.002	20.112	-0.008	-0.008	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.002	0.004	16.624	0.015	0.015	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.001	-0.016	16.139	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.057	-0.001	11.211	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.013	-0.021	11.192	0.047	0.047	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.827	0.898	13.334	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.808	0.901	12.175	-0.191	-0.191	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.734	-0.858	14.178	0.116	0.116	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.004	-0.006	12.018	0.028	0.028	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.035	-0.019	11.457	0.047	0.047	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.014	0.008	11.633	0.071	0.071	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.843	0.905	12.359	-0.149	-0.149	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.809	-0.880	15.771	0.155	0.155	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.029	-0.018	17.653	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.877	-0.936	19.857	0.032	0.032	0.000	0.000	0.000	0.000
55	A	55	TRP	0	0.048	0.017	19.788	-0.018	-0.018	0.000	0.000	0.000	0.000
56	A	56	TRP	0	0.009	-0.004	17.439	0.001	0.001	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.968	1.011	9.739	0.383	0.383	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.001	-0.019	15.410	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.840	0.896	10.617	0.667	0.667	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.042	0.003	16.546	0.013	0.013	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.847	0.918	19.664	0.116	0.116	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.036	-0.026	21.374	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.037	0.040	17.587	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.053	-0.021	16.199	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.010	-0.018	11.537	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.040	0.004	15.273	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.086	-0.064	13.511	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.017	-0.005	18.536	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.052	0.038	21.700	0.009	0.009	0.000	0.000	0.000	0.000
70	A	70	TYR	0	0.025	0.001	22.746	-0.010	-0.010	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.017	-0.007	24.129	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.013	-0.014	26.698	0.001	0.001	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.044	-0.019	21.992	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.837	-0.893	26.430	-0.051	-0.051	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.007	0.001	22.768	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.031	-0.015	24.828	0.009	0.009	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.961	0.981	25.604	0.022	0.022	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.937	0.952	23.459	0.039	0.039	0.000	0.000	0.000	0.000
79	A	79	ARG	1	1.005	1.019	28.902	0.069	0.069	0.000	0.000	0.000	0.000

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