FMO DATABASE

FMODB ID: 59KQZ

Calculation Name: 1S29-A-Xray310

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1S29

Chain ID: A

ChEMBL ID:

UniProt ID: Q9NIH4

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	92
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-668346.778301
FMO2-HF: Nuclear repulsion	631542.820029
FMO2-HF: Total energy	-36803.958271
FMO2-MP2: Total energy	-36911.274897

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:GLY )

Summations of interaction energy for fragment #1(A:1: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.
-5.943	-2.339	0.693	-1.68	-2.616	-0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.047 / q_NPA : 0.011

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	HIS	0	0.017	0.013	3.282	-1.725	-0.168	0.126	-0.733	-0.950	-0.001
4	A	4	MET	0	-0.087	-0.047	3.062	1.021	1.610	0.065	-0.181	-0.473	0.000
5	A	5	PRO	0	0.038	0.030	2.817	-2.808	-1.713	0.502	-0.739	-0.859	-0.007
6	A	6	LEU	0	0.060	0.039	4.993	0.306	0.463	0.000	-0.008	-0.148	0.000
7	A	7	SER	0	0.016	-0.012	6.047	0.247	0.247	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.079	0.027	9.286	-0.017	-0.017	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.879	-0.947	12.679	-0.223	-0.223	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.022	-0.027	7.204	0.168	0.168	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.953	0.997	9.849	0.856	0.856	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.023	0.009	11.325	0.052	0.052	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.879	0.947	11.987	0.311	0.311	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.031	0.019	9.196	0.066	0.066	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.001	-0.001	12.620	0.032	0.032	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.964	0.974	15.765	0.238	0.238	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.000	0.006	13.337	0.061	0.061	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.019	0.008	14.562	0.038	0.038	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.821	-0.891	17.146	-0.173	-0.173	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.058	-0.026	18.987	0.029	0.029	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.027	0.007	15.742	0.025	0.025	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.047	0.028	19.434	0.014	0.014	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.020	0.009	23.386	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.727	-0.867	25.585	-0.069	-0.069	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.048	-0.016	28.035	0.008	0.008	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.064	-0.051	23.595	0.018	0.018	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.083	0.059	26.170	0.008	0.008	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.035	-0.030	27.005	0.009	0.009	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.868	0.923	28.194	0.028	0.028	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.876	-0.931	23.501	-0.026	-0.026	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.000	-0.007	27.100	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	PHE	0	-0.002	0.006	21.297	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.008	0.007	21.730	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.926	0.954	24.688	0.025	0.025	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.003	0.009	27.978	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.941	0.974	22.472	0.034	0.034	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.036	-0.011	25.621	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.009	-0.003	27.286	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.976	-0.977	26.187	-0.045	-0.045	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.021	-0.018	26.631	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.011	-0.004	30.714	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.945	-0.965	29.060	-0.101	-0.101	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.018	0.002	28.179	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	44	PHE	0	-0.067	-0.047	23.483	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.017	0.008	19.989	0.014	0.014	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.053	0.031	19.213	-0.022	-0.022	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.045	-0.004	14.398	0.003	0.003	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.922	-0.964	14.230	-0.110	-0.110	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.008	-0.006	15.203	0.043	0.043	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.026	0.002	14.851	0.023	0.023	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.031	-0.012	9.316	0.003	0.003	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.067	-0.037	11.984	0.071	0.071	0.000	0.000	0.000	0.000
53	A	53	PHE	0	0.003	0.008	14.692	0.038	0.038	0.000	0.000	0.000	0.000
54	A	54	LYS	1	1.009	0.993	13.361	-0.123	-0.123	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.838	0.915	12.245	0.069	0.069	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.030	0.033	10.516	-0.054	-0.054	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.044	0.014	9.040	-0.069	-0.069	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.124	-0.047	7.851	0.085	0.085	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.066	-0.027	6.263	0.084	0.084	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.018	-0.052	4.395	-0.666	-0.528	0.000	-0.010	-0.128	0.000
61	A	61	THR	0	-0.008	-0.004	4.723	0.657	0.693	0.000	-0.003	-0.032	0.000
62	A	62	ASP	-1	-0.807	-0.899	6.377	-0.898	-0.898	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.039	0.010	7.775	-0.096	-0.096	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.949	0.959	10.280	0.529	0.529	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.877	-0.898	4.792	-4.035	-4.003	0.000	-0.006	-0.026	0.000
66	A	66	VAL	0	-0.028	-0.018	9.152	0.119	0.119	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.029	0.025	11.400	0.084	0.084	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.880	-0.932	11.521	-0.517	-0.517	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.075	-0.040	11.251	0.055	0.055	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.007	-0.009	13.196	0.077	0.077	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.831	0.906	16.102	0.469	0.469	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.039	-0.026	17.050	0.032	0.032	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.049	-0.038	19.718	0.034	0.034	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.916	-0.951	21.364	-0.149	-0.149	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.900	0.941	23.720	0.159	0.159	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.026	-0.010	19.198	0.010	0.010	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.010	-0.002	23.113	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.009	-0.009	17.638	0.003	0.003	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.013	-0.028	21.721	0.009	0.009	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.906	-0.954	22.661	-0.182	-0.182	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.862	-0.908	22.186	-0.192	-0.192	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.039	-0.018	19.051	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.027	-0.009	17.475	-0.042	-0.042	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.047	-0.027	18.693	0.014	0.014	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.022	-0.002	18.624	-0.019	-0.019	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.966	1.008	21.106	0.144	0.144	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.797	0.865	24.111	0.076	0.076	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.913	0.962	25.949	0.125	0.125	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.912	-0.957	28.039	-0.095	-0.095	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.002	-0.007	30.077	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.046	-0.019	29.687	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	92	PRO	-1	-0.924	-0.949	31.522	-0.045	-0.045	0.000	0.000	0.000	0.000

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