FMO DATABASE

FMODB ID: 53Y7Z

Calculation Name: 2HIQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2HIQ

Chain ID: A

ChEMBL ID:

UniProt ID: P0ACX3

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	96
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-667831.488499
FMO2-HF: Nuclear repulsion	630669.08546
FMO2-HF: Total energy	-37162.403039
FMO2-MP2: Total energy	-37273.098075

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:9:ALA)

Summations of interaction energy for fragment #1(A:9:ALA)

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.
-7.551	0.804	2.54	-4.558	-6.331	-0.022

Interaction energy analysis for fragmet #1(A:9:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / q_NPA : 0.017

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	11	LEU	0	-0.006	0.005	3.794	-0.431	1.844	-0.020	-1.202	-1.052	0.005
4	A	12	LEU	0	-0.038	-0.019	6.135	0.087	0.087	0.000	0.000	0.000	0.000
5	A	13	GLN	0	-0.012	0.001	9.373	0.102	0.102	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.012	-0.009	12.428	0.001	0.001	0.000	0.000	0.000	0.000
7	A	15	HIS	0	-0.004	-0.002	15.656	0.036	0.036	0.000	0.000	0.000	0.000
8	A	16	PHE	0	0.019	0.003	18.882	-0.014	-0.014	0.000	0.000	0.000	0.000
9	A	17	ALA	0	0.064	0.042	22.640	0.009	0.009	0.000	0.000	0.000	0.000
10	A	18	PHE	0	-0.018	-0.031	24.820	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	19	ASN	0	-0.017	-0.018	26.970	0.000	0.000	0.000	0.000	0.000	0.000
12	A	20	GLY	0	0.014	0.047	28.389	0.009	0.009	0.000	0.000	0.000	0.000
13	A	21	PRO	0	-0.029	-0.039	28.213	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	22	PHE	0	0.028	-0.002	25.998	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	23	GLY	0	0.034	0.013	26.416	0.009	0.009	0.000	0.000	0.000	0.000
16	A	24	ASP	-1	-0.923	-0.973	26.653	-0.037	-0.037	0.000	0.000	0.000	0.000
17	A	25	ALA	0	0.011	0.013	28.492	0.003	0.003	0.000	0.000	0.000	0.000
18	A	26	MET	0	-0.055	-0.008	23.228	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	27	ALA	0	-0.019	-0.010	24.011	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	28	GLU	-1	-0.989	-0.987	25.047	-0.024	-0.024	0.000	0.000	0.000	0.000
21	A	29	GLN	0	-0.033	-0.014	27.652	0.003	0.003	0.000	0.000	0.000	0.000
22	A	30	LEU	0	-0.019	-0.027	22.374	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	31	LYS	1	0.901	0.957	22.392	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	32	PRO	0	0.014	-0.006	22.330	0.004	0.004	0.000	0.000	0.000	0.000
25	A	33	LEU	0	-0.014	0.004	19.700	0.000	0.000	0.000	0.000	0.000	0.000
26	A	34	ALA	0	0.009	0.009	18.079	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	35	GLU	-1	-0.847	-0.922	17.554	0.021	0.021	0.000	0.000	0.000	0.000
28	A	36	SER	0	-0.091	-0.053	18.693	0.010	0.010	0.000	0.000	0.000	0.000
29	A	37	ILE	0	-0.003	-0.009	13.096	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	38	ASN	0	-0.006	-0.006	13.949	0.005	0.005	0.000	0.000	0.000	0.000
31	A	39	GLN	0	-0.054	-0.016	14.747	0.047	0.047	0.000	0.000	0.000	0.000
32	A	40	GLU	-1	-0.819	-0.888	12.714	-0.148	-0.148	0.000	0.000	0.000	0.000
33	A	41	PRO	0	0.021	0.009	12.187	0.047	0.047	0.000	0.000	0.000	0.000
34	A	42	GLY	0	0.035	0.002	8.319	-0.084	-0.084	0.000	0.000	0.000	0.000
35	A	43	PHE	0	-0.039	-0.004	6.854	-0.025	-0.025	0.000	0.000	0.000	0.000
36	A	44	LEU	0	-0.028	-0.004	3.548	0.024	0.212	0.007	-0.039	-0.156	0.000
37	A	45	TRP	0	0.023	0.010	7.155	-0.072	-0.072	0.000	0.000	0.000	0.000
38	A	46	LYS	1	0.848	0.926	8.876	0.079	0.079	0.000	0.000	0.000	0.000
39	A	47	VAL	0	-0.017	0.011	11.440	0.057	0.057	0.000	0.000	0.000	0.000
40	A	48	TRP	0	0.064	0.000	13.803	-0.063	-0.063	0.000	0.000	0.000	0.000
41	A	49	THR	0	-0.014	-0.011	16.187	0.016	0.016	0.000	0.000	0.000	0.000
42	A	50	GLU	-1	-0.804	-0.913	18.794	-0.102	-0.102	0.000	0.000	0.000	0.000
43	A	51	SER	0	-0.022	-0.016	22.496	0.009	0.009	0.000	0.000	0.000	0.000
44	A	52	GLU	-1	-0.867	-0.928	25.459	-0.082	-0.082	0.000	0.000	0.000	0.000
45	A	53	LYS	1	0.884	0.944	28.148	0.123	0.123	0.000	0.000	0.000	0.000
46	A	54	ASN	0	-0.062	-0.047	26.872	0.008	0.008	0.000	0.000	0.000	0.000
47	A	55	HIS	0	0.011	0.034	28.566	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	56	GLU	-1	-0.889	-0.946	23.607	-0.206	-0.206	0.000	0.000	0.000	0.000
49	A	57	ALA	0	-0.004	-0.010	21.772	0.013	0.013	0.000	0.000	0.000	0.000
50	A	58	GLY	0	0.022	0.008	18.181	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	59	GLY	0	-0.046	-0.016	14.814	0.044	0.044	0.000	0.000	0.000	0.000
52	A	60	ILE	0	-0.024	-0.001	9.461	-0.073	-0.073	0.000	0.000	0.000	0.000
53	A	61	TYR	0	0.012	-0.024	8.871	0.139	0.139	0.000	0.000	0.000	0.000
54	A	62	LEU	0	0.010	0.037	2.558	-0.863	-0.559	0.904	-0.311	-0.896	0.001
55	A	63	PHE	0	0.016	-0.014	4.058	0.342	0.511	-0.001	-0.030	-0.138	0.000
56	A	64	THR	0	0.004	-0.004	2.728	-2.798	-0.906	0.653	-1.180	-1.365	-0.013
57	A	65	ASP	-1	-0.839	-0.893	2.696	-1.375	0.401	0.702	-1.215	-1.262	-0.014
58	A	66	GLU	-1	-0.842	-0.936	4.441	-1.287	-1.236	-0.001	-0.007	-0.043	0.000
59	A	67	LYS	1	0.948	0.979	6.927	0.415	0.415	0.000	0.000	0.000	0.000
60	A	68	SER	0	-0.071	-0.075	7.598	0.097	0.097	0.000	0.000	0.000	0.000
61	A	69	ALA	0	-0.005	0.006	7.158	0.087	0.087	0.000	0.000	0.000	0.000
62	A	70	LEU	0	0.006	-0.003	9.168	0.127	0.127	0.000	0.000	0.000	0.000
63	A	71	ALA	0	0.006	0.013	12.124	0.087	0.087	0.000	0.000	0.000	0.000
64	A	72	TYR	0	-0.003	-0.002	11.933	0.077	0.077	0.000	0.000	0.000	0.000
65	A	73	LEU	0	0.019	0.008	13.296	0.046	0.046	0.000	0.000	0.000	0.000
66	A	74	GLU	-1	-0.935	-0.945	14.841	-0.222	-0.222	0.000	0.000	0.000	0.000
67	A	75	LYS	1	0.822	0.894	16.401	0.213	0.213	0.000	0.000	0.000	0.000
68	A	76	HIS	0	0.012	0.006	16.501	0.047	0.047	0.000	0.000	0.000	0.000
69	A	77	THR	0	0.033	0.004	18.285	0.015	0.015	0.000	0.000	0.000	0.000
70	A	78	ALA	0	-0.023	-0.008	20.380	0.021	0.021	0.000	0.000	0.000	0.000
71	A	79	ARG	1	0.854	0.926	17.280	0.170	0.170	0.000	0.000	0.000	0.000
72	A	80	LEU	0	0.028	0.006	19.770	0.016	0.016	0.000	0.000	0.000	0.000
73	A	81	LYS	1	0.944	1.001	23.350	0.189	0.189	0.000	0.000	0.000	0.000
74	A	82	ASN	0	-0.107	-0.045	25.867	0.015	0.015	0.000	0.000	0.000	0.000
75	A	83	LEU	0	-0.062	-0.030	24.109	0.010	0.010	0.000	0.000	0.000	0.000
76	A	84	GLY	0	-0.001	0.003	27.725	0.002	0.002	0.000	0.000	0.000	0.000
77	A	85	VAL	0	-0.029	-0.002	23.313	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	86	GLU	-1	-0.958	-0.991	26.272	-0.138	-0.138	0.000	0.000	0.000	0.000
79	A	87	GLU	-1	-0.936	-0.971	24.929	-0.219	-0.219	0.000	0.000	0.000	0.000
80	A	88	VAL	0	-0.034	-0.021	18.615	0.002	0.002	0.000	0.000	0.000	0.000
81	A	89	VAL	0	-0.015	0.010	19.235	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	90	ALA	0	0.011	-0.009	14.938	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	91	LYS	1	0.860	0.937	13.873	0.652	0.652	0.000	0.000	0.000	0.000
84	A	92	VAL	0	0.038	0.021	8.806	-0.018	-0.018	0.000	0.000	0.000	0.000
85	A	93	PHE	0	-0.037	-0.023	8.525	0.317	0.317	0.000	0.000	0.000	0.000
86	A	94	ASP	-1	-0.834	-0.898	4.766	-4.563	-4.457	-0.001	-0.032	-0.072	0.000
87	A	95	VAL	0	-0.023	-0.018	2.631	0.487	1.656	0.297	-0.427	-1.039	0.000
88	A	96	ASN	0	-0.003	-0.001	3.842	-0.165	0.082	0.001	-0.108	-0.139	-0.001
89	A	97	GLU	-1	-0.800	-0.890	4.622	1.452	1.630	-0.001	-0.007	-0.169	0.000
90	A	98	PRO	0	0.003	-0.003	6.271	0.009	0.009	0.000	0.000	0.000	0.000
91	A	99	LEU	0	0.011	-0.002	9.825	0.010	0.010	0.000	0.000	0.000	0.000
92	A	100	SER	0	0.012	-0.013	7.132	-0.053	-0.053	0.000	0.000	0.000	0.000
93	A	101	GLN	0	-0.113	-0.063	8.255	-0.105	-0.105	0.000	0.000	0.000	0.000
94	A	102	ILE	0	-0.049	-0.011	10.671	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	103	ASN	0	-0.111	-0.050	12.624	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	104	GLN	0	-0.010	0.005	7.736	-0.080	-0.080	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ALA)