FMO DATABASE

FMODB ID: 6NV6Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-515924.339179
FMO2-HF: Nuclear repulsion	484055.644788
FMO2-HF: Total energy	-31868.69439
FMO2-MP2: Total energy	-31962.441227

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.
-8.259	0.247	3.276	-5.22	-6.561	-0.032

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 : -0.005 / q_NPA : 0.009

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	-0.807	-0.886	2.770	-6.045	-1.547	0.938	-2.699	-2.737	-0.010
4	A	4	PHE	0	-0.058	-0.038	4.797	0.278	0.438	-0.001	-0.006	-0.153	0.000
5	A	5	GLY	0	0.033	0.038	3.167	0.021	0.607	0.113	-0.158	-0.540	0.000
6	A	6	SER	0	0.003	-0.027	2.489	-3.830	-0.789	2.221	-2.308	-2.954	-0.022
7	A	7	GLU	-1	-0.900	-0.925	3.960	0.459	0.680	0.005	-0.049	-0.177	0.000
8	A	8	PRO	0	-0.018	-0.022	7.285	-0.223	-0.223	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.010	0.000	8.104	0.072	0.072	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.837	-0.922	11.886	-0.104	-0.104	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.037	-0.001	15.625	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.045	-0.008	17.626	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.944	0.965	12.869	0.040	0.040	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.022	0.005	13.510	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.792	-0.874	17.058	-0.081	-0.081	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.001	-0.004	18.441	-0.033	-0.033	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.006	-0.006	21.132	0.022	0.022	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.832	0.876	23.506	0.087	0.087	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.022	0.028	26.251	0.007	0.007	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.011	0.001	27.424	0.004	0.004	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.057	-0.036	29.883	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.810	-0.897	29.588	-0.099	-0.099	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.029	-0.019	23.657	0.007	0.007	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.001	-0.011	27.272	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.039	-0.013	23.154	0.007	0.007	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.916	-0.941	25.266	-0.049	-0.049	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.004	-0.011	20.471	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	28	PRO	0	-0.011	-0.031	21.344	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.951	-0.949	18.372	-0.128	-0.128	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.055	-0.026	15.142	-0.025	-0.025	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.838	-0.915	17.376	-0.112	-0.112	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.044	-0.013	18.126	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.004	0.002	20.923	0.015	0.015	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.040	-0.029	22.674	-0.015	-0.015	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.883	0.939	26.135	0.110	0.110	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.908	0.945	28.997	0.067	0.067	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.014	-0.008	30.141	0.002	0.002	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.835	-0.906	25.233	-0.153	-0.153	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.031	-0.019	24.244	0.007	0.007	0.000	0.000	0.000	0.000
40	A	40	MET	0	-0.009	0.003	19.376	-0.012	-0.012	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.009	0.020	16.447	0.020	0.020	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.012	-0.018	15.886	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.049	-0.013	10.831	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.007	-0.010	11.411	0.030	0.030	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.810	0.887	13.411	0.078	0.078	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.805	0.897	12.473	-0.068	-0.068	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.690	-0.826	14.041	0.019	0.019	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.002	0.004	11.985	0.015	0.015	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.031	-0.010	11.703	0.035	0.035	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.015	-0.002	12.058	0.054	0.054	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.825	0.887	12.705	-0.070	-0.070	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.833	-0.901	16.407	0.048	0.048	0.000	0.000	0.000	0.000
53	A	53	SER	0	0.000	0.000	18.263	0.000	0.000	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.885	-0.944	20.466	-0.022	-0.022	0.000	0.000	0.000	0.000
55	A	55	TRP	0	0.048	0.024	19.747	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	56	TRP	0	-0.001	-0.010	17.250	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.968	1.010	9.272	0.553	0.553	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.004	-0.017	14.929	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.809	0.864	10.345	0.673	0.673	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.044	0.015	16.130	0.014	0.014	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.859	0.916	19.413	0.129	0.129	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.031	-0.012	20.995	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.006	0.015	17.134	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.027	-0.012	15.726	-0.021	-0.021	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.003	-0.016	10.785	-0.014	-0.014	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.045	0.025	14.551	0.009	0.009	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.093	-0.070	13.278	-0.025	-0.025	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.016	0.000	17.893	0.003	0.003	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.066	0.041	21.347	0.004	0.004	0.000	0.000	0.000	0.000
70	A	70	TYR	0	-0.005	-0.010	22.891	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	71	ASN	0	0.009	0.001	24.209	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.004	-0.010	26.411	0.004	0.004	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.042	-0.016	22.198	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.830	-0.874	26.446	-0.078	-0.078	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.001	-0.005	22.973	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.021	-0.004	24.765	0.012	0.012	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.946	0.974	25.450	0.052	0.052	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.941	0.964	23.144	0.074	0.074	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.968	0.988	28.598	0.085	0.085	0.000	0.000	0.000	0.000

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