FMO DATABASE

FMODB ID: 66ZJZ

Calculation Name: 1S29-A-Xray372

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: 2023-03-13

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	92
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-668815.130414
FMO2-HF: Nuclear repulsion	632010.092473
FMO2-HF: Total energy	-36805.037941
FMO2-MP2: Total energy	-36912.336986

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.
-5.353	-1.641	0.796	-1.76	-2.748	-0.009

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 : 0.012

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	0.020	0.014	3.102	-1.810	-0.118	0.257	-0.846	-1.103	-0.002
4	A	4	MET	0	-0.081	-0.049	3.079	1.093	1.672	0.054	-0.176	-0.457	0.000
5	A	5	PRO	0	0.035	0.024	2.826	-2.629	-1.541	0.488	-0.719	-0.857	-0.007
6	A	6	LEU	0	0.039	0.039	4.992	0.309	0.468	-0.001	-0.007	-0.151	0.000
7	A	7	SER	0	0.014	-0.013	6.048	0.231	0.231	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.078	0.027	9.286	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.793	-0.888	12.679	-0.213	-0.213	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.003	-0.014	7.105	0.157	0.157	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.957	1.001	9.803	0.848	0.848	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.028	0.011	11.326	0.055	0.055	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.768	0.872	11.918	0.329	0.329	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.025	0.012	9.047	0.065	0.065	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.007	-0.002	12.645	0.033	0.033	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.961	0.969	15.767	0.235	0.235	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.025	0.027	13.380	0.061	0.061	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.025	0.010	14.487	0.037	0.037	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.761	-0.833	17.125	-0.160	-0.160	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.032	-0.014	19.046	0.027	0.027	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.027	0.011	15.828	0.024	0.024	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.046	0.027	19.376	0.015	0.015	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.033	-0.002	23.366	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.757	-0.873	25.609	-0.064	-0.064	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.040	-0.017	28.037	0.007	0.007	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.040	-0.038	23.234	0.017	0.017	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.082	0.054	25.849	0.008	0.008	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.017	-0.024	26.986	0.008	0.008	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.874	0.939	28.184	0.025	0.025	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.855	-0.913	23.463	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.010	-0.016	27.112	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.014	0.020	21.285	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.008	0.000	21.660	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.852	0.913	24.674	0.019	0.019	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.006	0.013	27.953	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.824	0.899	22.841	0.032	0.032	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.056	-0.019	25.620	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.007	-0.003	27.274	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.847	-0.901	26.256	-0.034	-0.034	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.027	-0.023	26.653	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.017	-0.002	30.707	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.852	-0.916	28.918	-0.102	-0.102	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.028	-0.002	28.167	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	PHE	0	-0.041	-0.034	23.418	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.002	-0.001	20.100	0.014	0.014	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.055	0.033	19.197	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.041	-0.005	14.387	0.004	0.004	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.912	-0.961	14.227	-0.095	-0.095	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.010	-0.007	15.198	0.041	0.041	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.021	0.003	14.823	0.022	0.022	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.036	-0.014	9.221	0.001	0.001	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.064	-0.033	11.974	0.067	0.067	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.006	0.001	14.683	0.034	0.034	0.000	0.000	0.000	0.000
54	A	54	LYS	1	1.010	0.991	13.377	-0.138	-0.138	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.841	0.913	12.257	0.070	0.070	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.025	0.024	10.562	-0.056	-0.056	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.037	0.019	9.060	-0.087	-0.087	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.074	-0.032	7.862	0.116	0.116	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.107	-0.051	6.273	0.090	0.090	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.012	-0.044	4.386	-0.609	-0.476	-0.001	-0.008	-0.124	0.000
61	A	61	THR	0	0.011	0.004	4.801	0.552	0.552	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.811	-0.903	6.525	-0.764	-0.764	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.040	0.014	7.777	-0.104	-0.104	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.945	0.963	10.211	0.502	0.502	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.870	-0.903	4.744	-3.708	-3.647	-0.001	-0.004	-0.056	0.000
66	A	66	VAL	0	-0.024	-0.019	9.145	0.102	0.102	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.030	0.028	11.388	0.074	0.074	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.890	-0.920	11.484	-0.504	-0.504	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.065	-0.037	11.219	0.050	0.050	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.009	-0.003	13.199	0.070	0.070	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.840	0.897	16.048	0.458	0.458	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.032	-0.020	17.012	0.029	0.029	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.054	-0.047	19.719	0.032	0.032	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.916	-0.948	21.366	-0.144	-0.144	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.821	0.886	23.410	0.162	0.162	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.035	-0.015	19.264	0.010	0.010	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.001	0.001	23.096	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.012	-0.009	17.569	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.013	-0.033	21.712	0.007	0.007	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.915	-0.956	22.656	-0.170	-0.170	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.847	-0.904	22.452	-0.176	-0.176	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.040	-0.015	19.049	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.029	-0.008	17.473	-0.039	-0.039	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.050	-0.028	18.689	0.015	0.015	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.021	-0.004	18.536	-0.019	-0.019	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.881	0.962	21.095	0.129	0.129	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.792	0.859	24.096	0.071	0.071	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.917	0.973	25.933	0.116	0.116	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.907	-0.958	28.022	-0.091	-0.091	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.031	0.009	30.060	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.018	-0.004	29.375	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.013	0.007	31.527	0.003	0.003	0.000	0.000	0.000	0.000

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