FMO DATABASE

FMODB ID: 3Q8YL

Calculation Name: 2HJM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2HJM

Chain ID: A

ChEMBL ID:

UniProt ID: Q8U1N0

Base Structure: X-ray

Registration Date: 2023-06-19

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	91
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-665962.049653
FMO2-HF: Nuclear repulsion	628950.49561
FMO2-HF: Total energy	-37011.554043
FMO2-MP2: Total energy	-37119.766081

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:-5:HIS)

Summations of interaction energy for fragment #1(A:-5:HIS)

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.
-12.576	-7.225	6.58	-4.54	-7.391	0.018

Interaction energy analysis for fragmet #1(A:-5:HIS)

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 : 0.003

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	-3	HIS	0	0.004	0.014	2.147	-12.295	-7.482	6.567	-4.453	-6.927	0.017
4	A	-2	HIS	0	-0.040	-0.026	4.014	-3.947	-3.572	0.014	-0.079	-0.310	0.001
5	A	-1	HIS	0	0.014	-0.009	3.869	0.030	0.193	-0.001	-0.008	-0.154	0.000
6	A	0	HIS	0	0.024	0.008	8.598	-0.124	-0.124	0.000	0.000	0.000	0.000
7	A	1	MET	0	0.016	0.000	12.317	0.101	0.101	0.000	0.000	0.000	0.000
8	A	2	ASP	-1	-0.811	-0.901	10.803	0.289	0.289	0.000	0.000	0.000	0.000
9	A	3	LEU	0	0.023	0.021	9.121	0.056	0.056	0.000	0.000	0.000	0.000
10	A	4	VAL	0	-0.027	-0.027	11.773	0.059	0.059	0.000	0.000	0.000	0.000
11	A	5	GLU	-1	-0.854	-0.923	15.438	0.145	0.145	0.000	0.000	0.000	0.000
12	A	6	LYS	1	0.863	0.938	11.482	-0.402	-0.402	0.000	0.000	0.000	0.000
13	A	7	VAL	0	0.014	0.011	14.730	0.021	0.021	0.000	0.000	0.000	0.000
14	A	8	LYS	1	0.759	0.869	16.621	-0.169	-0.169	0.000	0.000	0.000	0.000
15	A	9	GLU	-1	-0.871	-0.925	15.502	0.452	0.452	0.000	0.000	0.000	0.000
16	A	10	LEU	0	0.017	0.010	14.825	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	11	CYS	0	-0.071	-0.046	18.123	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	12	LEU	0	-0.017	-0.011	21.376	-0.029	-0.029	0.000	0.000	0.000	0.000
19	A	13	GLU	-1	-0.905	-0.933	17.298	0.474	0.474	0.000	0.000	0.000	0.000
20	A	14	LEU	0	-0.068	-0.035	19.627	0.020	0.020	0.000	0.000	0.000	0.000
21	A	15	GLU	-1	-0.919	-0.946	23.483	0.185	0.185	0.000	0.000	0.000	0.000
22	A	16	GLU	-1	-0.863	-0.899	24.153	0.256	0.256	0.000	0.000	0.000	0.000
23	A	17	GLU	-1	-0.765	-0.894	25.635	0.145	0.145	0.000	0.000	0.000	0.000
24	A	18	ASN	0	-0.007	-0.003	27.285	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	19	LEU	0	0.001	-0.001	23.069	-0.014	-0.014	0.000	0.000	0.000	0.000
26	A	20	ALA	0	0.065	0.033	22.855	0.004	0.004	0.000	0.000	0.000	0.000
27	A	21	LYS	1	0.874	0.915	23.884	-0.141	-0.141	0.000	0.000	0.000	0.000
28	A	22	ALA	0	-0.074	-0.017	26.057	-0.022	-0.022	0.000	0.000	0.000	0.000
29	A	23	ILE	0	0.039	0.024	19.665	-0.018	-0.018	0.000	0.000	0.000	0.000
30	A	24	GLU	-1	-0.852	-0.908	23.036	0.097	0.097	0.000	0.000	0.000	0.000
31	A	25	ARG	1	0.814	0.888	24.445	-0.156	-0.156	0.000	0.000	0.000	0.000
32	A	26	PHE	0	0.027	0.015	21.972	-0.018	-0.018	0.000	0.000	0.000	0.000
33	A	27	ILE	0	0.043	0.021	19.788	-0.017	-0.017	0.000	0.000	0.000	0.000
34	A	28	THR	0	-0.037	-0.009	23.015	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	29	LEU	0	-0.077	-0.039	26.141	-0.017	-0.017	0.000	0.000	0.000	0.000
36	A	30	THR	0	-0.021	-0.019	23.701	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	31	HIS	0	0.000	-0.009	23.135	-0.028	-0.028	0.000	0.000	0.000	0.000
38	A	32	GLY	0	-0.031	-0.017	25.141	-0.018	-0.018	0.000	0.000	0.000	0.000
39	A	33	ILE	0	0.011	0.010	23.840	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	34	GLU	-1	-0.857	-0.924	19.263	-0.159	-0.159	0.000	0.000	0.000	0.000
41	A	35	LYS	1	0.918	0.959	23.411	0.072	0.072	0.000	0.000	0.000	0.000
42	A	36	THR	0	-0.068	-0.048	26.645	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	37	ARG	1	0.876	0.941	25.180	0.027	0.027	0.000	0.000	0.000	0.000
44	A	38	GLY	0	0.042	0.036	22.765	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	39	GLU	-1	-0.828	-0.906	15.173	-0.391	-0.391	0.000	0.000	0.000	0.000
46	A	40	ALA	0	0.038	0.023	17.116	0.029	0.029	0.000	0.000	0.000	0.000
47	A	41	PHE	0	0.038	0.016	18.183	0.053	0.053	0.000	0.000	0.000	0.000
48	A	42	ALA	0	0.005	0.011	19.926	0.041	0.041	0.000	0.000	0.000	0.000
49	A	43	LYS	1	0.872	0.918	12.666	0.395	0.395	0.000	0.000	0.000	0.000
50	A	44	ALA	0	0.049	0.032	16.581	0.070	0.070	0.000	0.000	0.000	0.000
51	A	45	SER	0	-0.066	-0.040	17.940	0.053	0.053	0.000	0.000	0.000	0.000
52	A	46	ILE	0	-0.029	-0.017	16.981	0.034	0.034	0.000	0.000	0.000	0.000
53	A	47	TYR	0	0.049	0.017	10.356	0.058	0.058	0.000	0.000	0.000	0.000
54	A	48	GLY	0	0.056	0.029	16.164	0.071	0.071	0.000	0.000	0.000	0.000
55	A	49	PHE	0	-0.034	-0.022	19.072	0.025	0.025	0.000	0.000	0.000	0.000
56	A	50	LEU	0	0.007	-0.005	15.530	0.008	0.008	0.000	0.000	0.000	0.000
57	A	51	GLU	-1	-0.732	-0.850	15.098	0.707	0.707	0.000	0.000	0.000	0.000
58	A	52	GLY	0	-0.007	0.018	17.291	0.015	0.015	0.000	0.000	0.000	0.000
59	A	53	ILE	0	-0.006	-0.003	19.449	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	54	LEU	0	0.030	0.018	13.812	-0.019	-0.019	0.000	0.000	0.000	0.000
61	A	55	THR	0	-0.014	-0.021	17.822	0.024	0.024	0.000	0.000	0.000	0.000
62	A	56	THR	0	-0.071	-0.053	19.239	-0.028	-0.028	0.000	0.000	0.000	0.000
63	A	57	LEU	0	-0.015	0.008	19.526	-0.035	-0.035	0.000	0.000	0.000	0.000
64	A	58	LYS	1	0.839	0.902	15.571	-0.848	-0.848	0.000	0.000	0.000	0.000
65	A	59	MET	0	-0.084	-0.031	19.937	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	60	LYS	1	0.849	0.923	23.112	-0.372	-0.372	0.000	0.000	0.000	0.000
67	A	61	TYR	0	-0.046	-0.039	21.399	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	62	SER	0	0.006	-0.004	20.247	0.028	0.028	0.000	0.000	0.000	0.000
69	A	63	ASN	0	0.016	0.012	16.330	0.092	0.092	0.000	0.000	0.000	0.000
70	A	64	GLU	-1	-0.778	-0.878	11.129	1.366	1.366	0.000	0.000	0.000	0.000
71	A	65	LYS	1	0.791	0.872	12.196	-0.452	-0.452	0.000	0.000	0.000	0.000
72	A	66	ILE	0	-0.017	-0.014	12.690	0.085	0.085	0.000	0.000	0.000	0.000
73	A	67	GLU	-1	-0.752	-0.856	12.102	1.020	1.020	0.000	0.000	0.000	0.000
74	A	68	THR	0	-0.037	-0.030	7.159	0.245	0.245	0.000	0.000	0.000	0.000
75	A	69	LEU	0	0.021	0.019	8.459	0.313	0.313	0.000	0.000	0.000	0.000
76	A	70	LEU	0	-0.034	-0.010	10.470	-0.032	-0.032	0.000	0.000	0.000	0.000
77	A	71	ASN	0	-0.049	-0.043	7.904	-0.072	-0.072	0.000	0.000	0.000	0.000
78	A	72	GLU	-1	-0.805	-0.868	5.758	2.820	2.820	0.000	0.000	0.000	0.000
79	A	73	VAL	0	-0.025	-0.018	7.909	-0.324	-0.324	0.000	0.000	0.000	0.000
80	A	74	LYS	1	0.796	0.907	11.232	-0.967	-0.967	0.000	0.000	0.000	0.000
81	A	75	THR	0	0.014	-0.007	6.396	-0.118	-0.118	0.000	0.000	0.000	0.000
82	A	76	ALA	0	-0.012	-0.005	8.428	-0.406	-0.406	0.000	0.000	0.000	0.000
83	A	77	ARG	1	0.638	0.777	9.491	-0.767	-0.767	0.000	0.000	0.000	0.000
84	A	78	GLU	-1	-0.790	-0.899	11.967	0.655	0.655	0.000	0.000	0.000	0.000
85	A	79	GLU	-1	-0.961	-0.977	8.823	-0.863	-0.863	0.000	0.000	0.000	0.000
86	A	80	THR	0	-0.110	-0.069	11.460	-0.149	-0.149	0.000	0.000	0.000	0.000
87	A	81	GLU	-1	-0.879	-0.908	13.935	0.215	0.215	0.000	0.000	0.000	0.000
88	A	82	ALA	0	0.004	0.025	14.278	0.005	0.005	0.000	0.000	0.000	0.000
89	A	83	LEU	0	-0.026	-0.032	16.236	-0.040	-0.040	0.000	0.000	0.000	0.000
90	A	84	LEU	0	0.007	0.014	15.090	0.022	0.022	0.000	0.000	0.000	0.000
91	A	85	ARG	1	0.915	0.961	18.937	0.143	0.143	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-5:HIS)