FMO DATABASE

FMODB ID: NN1RQ

Calculation Name: 2IAZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2IAZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q97Q59

Base Structure: X-ray

Registration Date: 2023-09-21

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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-734702.013891
FMO2-HF: Nuclear repulsion	691336.544735
FMO2-HF: Total energy	-43365.469156
FMO2-MP2: Total energy	-43492.121039

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:0:GLY)

Summations of interaction energy for fragment #1(A:0: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.
-6.483	-4.969	5.831	-3.588	-3.756	-0.026

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.010 / q_NPA : -0.008

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

Sort

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	2	SER	0	0.034	0.014	3.473	-1.718	0.012	0.012	-0.840	-0.901	0.001
4	A	3	ASN	0	0.067	0.039	2.001	-5.771	-6.312	5.818	-2.647	-2.630	-0.027
5	A	4	ILE	0	0.043	0.040	4.030	0.942	1.267	0.001	-0.101	-0.225	0.000
6	A	5	TYR	0	-0.008	-0.019	6.270	0.623	0.623	0.000	0.000	0.000	0.000
7	A	6	ASP	-1	-0.911	-0.964	6.914	-0.673	-0.673	0.000	0.000	0.000	0.000
8	A	7	SER	0	-0.005	-0.010	7.895	0.224	0.224	0.000	0.000	0.000	0.000
9	A	8	ALA	0	0.016	0.013	10.129	0.196	0.196	0.000	0.000	0.000	0.000
10	A	9	ASN	0	-0.039	-0.005	11.884	0.165	0.165	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.919	-0.968	12.157	-0.512	-0.512	0.000	0.000	0.000	0.000
12	A	11	LEU	0	0.034	0.030	14.325	0.073	0.073	0.000	0.000	0.000	0.000
13	A	12	SER	0	0.015	0.017	16.012	0.078	0.078	0.000	0.000	0.000	0.000
14	A	13	ARG	1	0.850	0.901	16.081	0.294	0.294	0.000	0.000	0.000	0.000
15	A	14	GLY	0	0.020	0.013	18.695	0.031	0.031	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.008	-0.004	19.511	0.029	0.029	0.000	0.000	0.000	0.000
17	A	16	ARG	1	0.886	0.929	19.136	0.231	0.231	0.000	0.000	0.000	0.000
18	A	17	GLY	0	-0.041	-0.022	23.422	0.021	0.021	0.000	0.000	0.000	0.000
19	A	18	LEU	0	0.024	0.035	24.955	0.009	0.009	0.000	0.000	0.000	0.000
20	A	19	PRO	0	0.016	-0.007	26.656	0.009	0.009	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.766	-0.872	28.976	-0.128	-0.128	0.000	0.000	0.000	0.000
22	A	21	TYR	0	0.021	0.019	26.673	0.007	0.007	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.849	0.919	27.727	0.145	0.145	0.000	0.000	0.000	0.000
24	A	23	ALA	0	-0.020	-0.002	31.133	0.008	0.008	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.036	0.026	31.466	0.007	0.007	0.000	0.000	0.000	0.000
26	A	25	LYS	1	0.829	0.892	30.763	0.087	0.087	0.000	0.000	0.000	0.000
27	A	26	ALA	0	0.015	0.002	33.139	0.006	0.006	0.000	0.000	0.000	0.000
28	A	27	ALA	0	0.041	0.025	36.211	0.005	0.005	0.000	0.000	0.000	0.000
29	A	28	LYS	1	0.898	0.957	34.997	0.066	0.066	0.000	0.000	0.000	0.000
30	A	29	ASP	-1	-0.854	-0.911	35.470	-0.068	-0.068	0.000	0.000	0.000	0.000
31	A	30	ALA	0	-0.003	-0.003	38.329	0.004	0.004	0.000	0.000	0.000	0.000
32	A	31	ILE	0	-0.003	0.007	39.611	0.003	0.003	0.000	0.000	0.000	0.000
33	A	32	ALA	0	-0.079	-0.035	39.542	0.003	0.003	0.000	0.000	0.000	0.000
34	A	33	ALA	0	-0.033	-0.007	41.664	0.003	0.003	0.000	0.000	0.000	0.000
35	A	34	ASP	-1	-0.795	-0.899	44.250	-0.038	-0.038	0.000	0.000	0.000	0.000
36	A	35	ALA	0	-0.011	-0.017	46.668	0.000	0.000	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.936	-0.956	48.757	-0.037	-0.037	0.000	0.000	0.000	0.000
38	A	37	ALA	0	0.033	0.012	44.821	0.000	0.000	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.021	-0.027	43.766	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	39	LYS	1	0.781	0.900	44.502	0.031	0.031	0.000	0.000	0.000	0.000
41	A	40	ILE	0	0.047	0.025	46.004	0.000	0.000	0.000	0.000	0.000	0.000
42	A	41	PHE	0	0.013	0.001	37.032	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	42	THR	0	-0.034	-0.031	42.160	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	43	ASP	-1	-0.819	-0.892	43.464	-0.033	-0.033	0.000	0.000	0.000	0.000
45	A	44	TYR	0	-0.047	-0.027	40.562	0.001	0.001	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.009	-0.023	37.812	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	46	ALA	0	0.005	0.013	40.872	0.000	0.000	0.000	0.000	0.000	0.000
48	A	47	PHE	0	-0.031	-0.008	43.512	0.002	0.002	0.000	0.000	0.000	0.000
49	A	48	GLN	0	0.015	-0.003	36.666	0.001	0.001	0.000	0.000	0.000	0.000
50	A	49	GLU	-1	-0.909	-0.947	40.741	-0.033	-0.033	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.867	-0.944	42.202	-0.030	-0.030	0.000	0.000	0.000	0.000
52	A	51	ILE	0	-0.038	-0.012	38.355	0.001	0.001	0.000	0.000	0.000	0.000
53	A	52	GLN	0	-0.038	-0.006	37.255	0.002	0.002	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.932	0.953	41.606	0.027	0.027	0.000	0.000	0.000	0.000
55	A	54	LEU	0	-0.028	0.003	43.344	0.002	0.002	0.000	0.000	0.000	0.000
56	A	55	ALA	0	-0.004	0.003	43.467	0.000	0.000	0.000	0.000	0.000	0.000
57	A	56	GLN	0	-0.084	-0.050	44.782	0.002	0.002	0.000	0.000	0.000	0.000
58	A	57	THR	0	-0.009	-0.004	45.088	0.000	0.000	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.018	0.008	48.001	0.002	0.002	0.000	0.000	0.000	0.000
60	A	59	GLN	0	-0.073	-0.033	50.664	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	60	MET	0	0.029	0.020	51.527	0.001	0.001	0.000	0.000	0.000	0.000
62	A	61	PRO	0	-0.008	-0.012	50.833	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	62	ASP	-1	-0.768	-0.853	49.889	-0.028	-0.028	0.000	0.000	0.000	0.000
64	A	63	ALA	0	0.037	-0.002	51.418	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	64	SER	0	-0.020	-0.012	53.078	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	65	PHE	0	0.031	-0.003	43.850	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	66	GLN	0	-0.026	-0.013	49.119	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	67	ALA	0	0.007	0.007	50.297	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.848	0.917	49.533	0.029	0.029	0.000	0.000	0.000	0.000
70	A	69	MET	0	-0.023	0.001	42.238	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.862	-0.930	47.462	-0.037	-0.037	0.000	0.000	0.000	0.000
72	A	71	GLY	0	-0.018	-0.010	49.769	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	72	PHE	0	0.019	-0.011	45.862	0.000	0.000	0.000	0.000	0.000	0.000
74	A	73	GLY	0	0.033	0.036	45.997	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	74	LYS	1	0.865	0.917	47.035	0.035	0.035	0.000	0.000	0.000	0.000
76	A	75	GLN	0	-0.004	-0.001	48.690	0.001	0.001	0.000	0.000	0.000	0.000
77	A	76	ILE	0	-0.027	0.000	42.716	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	77	GLN	0	-0.044	-0.040	45.067	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	78	GLY	0	-0.014	0.008	47.853	0.000	0.000	0.000	0.000	0.000	0.000
80	A	79	ASN	0	0.019	0.007	46.749	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	80	SER	0	0.027	0.014	46.369	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	81	LEU	0	0.011	0.012	43.552	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.013	-0.002	42.066	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	83	SER	0	-0.006	-0.017	41.640	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.815	-0.871	39.299	-0.078	-0.078	0.000	0.000	0.000	0.000
86	A	85	PHE	0	0.005	-0.005	34.649	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	86	PHE	0	0.014	-0.011	36.667	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	87	THR	0	-0.027	-0.010	36.953	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.812	0.883	34.893	0.074	0.074	0.000	0.000	0.000	0.000
90	A	89	GLN	0	0.022	0.002	32.186	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	90	GLN	0	-0.050	-0.018	31.949	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	91	GLN	0	-0.002	-0.016	32.095	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.031	0.021	26.625	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	93	ALA	0	-0.022	-0.013	27.611	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	94	ILE	0	0.014	0.015	27.647	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	95	TYR	0	-0.041	-0.037	25.106	-0.012	-0.012	0.000	0.000	0.000	0.000
97	A	96	LEU	0	-0.049	-0.028	23.102	-0.018	-0.018	0.000	0.000	0.000	0.000
98	A	97	SER	0	0.028	0.021	22.449	-0.016	-0.016	0.000	0.000	0.000	0.000
99	A	98	ASP	-1	-0.877	-0.951	23.203	-0.186	-0.186	0.000	0.000	0.000	0.000
100	A	99	ILE	0	-0.026	-0.016	18.028	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	100	GLU	-1	-0.955	-0.976	18.321	-0.234	-0.234	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.866	0.928	18.493	0.157	0.157	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.006	0.007	15.603	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	103	VAL	0	-0.067	-0.035	13.062	-0.039	-0.039	0.000	0.000	0.000	0.000
105	A	104	PHE	0	-0.035	-0.029	13.598	-0.061	-0.061	0.000	0.000	0.000	0.000
106	A	105	GLU	-1	-0.858	-0.902	16.021	-0.186	-0.186	0.000	0.000	0.000	0.000
107	A	106	PRO	0	-0.010	-0.016	11.888	0.022	0.022	0.000	0.000	0.000	0.000
108	A	107	VAL	0	-0.041	-0.021	14.615	0.031	0.031	0.000	0.000	0.000	0.000
109	A	108	SER	0	0.000	-0.015	16.431	0.036	0.036	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.952	-0.962	16.157	-0.193	-0.193	0.000	0.000	0.000	0.000
111	A	110	LEU	0	-0.111	-0.047	14.904	0.025	0.025	0.000	0.000	0.000	0.000
112	A	111	LEU	0	-0.087	-0.027	19.221	0.025	0.025	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)