FMO DATABASE

FMODB ID: 726LK

Calculation Name: 2O71-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2O71

Chain ID: A

ChEMBL ID:

UniProt ID: P78560

Base Structure: X-ray

Registration Date: 2023-06-22

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

Total energy (hartree)

FMO2-HF: Electronic energy	-679056.81657
FMO2-HF: Nuclear repulsion	642323.107719
FMO2-HF: Total energy	-36733.708852
FMO2-MP2: Total energy	-36841.257832

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:109:HIS)

Summations of interaction energy for fragment #1(A:109: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.
-9.883	-4.84	0.23	-2.097	-3.176	0

Interaction energy analysis for fragmet #1(A:109:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.042 / q_NPA : 0.007

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	111	LEU	0	0.038	0.022	3.248	-4.440	-2.087	0.032	-0.985	-1.399	0.004
4	A	112	ASN	0	-0.041	-0.031	3.077	-3.703	-1.416	0.197	-1.016	-1.469	-0.004
5	A	113	SER	0	-0.050	-0.021	4.292	-0.732	-0.329	0.001	-0.096	-0.308	0.000
6	A	114	SER	0	0.015	-0.013	6.214	-0.113	-0.113	0.000	0.000	0.000	0.000
7	A	115	PRO	0	-0.028	0.008	8.985	-0.240	-0.240	0.000	0.000	0.000	0.000
8	A	116	SER	0	0.046	0.000	11.060	-0.035	-0.035	0.000	0.000	0.000	0.000
9	A	117	ASP	-1	-0.744	-0.877	12.481	-0.190	-0.190	0.000	0.000	0.000	0.000
10	A	118	ARG	1	0.885	0.960	14.576	0.281	0.281	0.000	0.000	0.000	0.000
11	A	119	GLN	0	0.105	0.060	9.075	-0.030	-0.030	0.000	0.000	0.000	0.000
12	A	120	ILE	0	0.005	0.014	14.683	0.087	0.087	0.000	0.000	0.000	0.000
13	A	121	ASN	0	-0.035	-0.038	17.243	0.044	0.044	0.000	0.000	0.000	0.000
14	A	122	GLN	0	-0.044	-0.015	14.985	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	123	LEU	0	0.031	0.005	16.083	0.029	0.029	0.000	0.000	0.000	0.000
16	A	124	ALA	0	-0.019	-0.018	18.836	0.017	0.017	0.000	0.000	0.000	0.000
17	A	125	GLN	0	-0.064	-0.028	22.084	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	126	ARG	1	0.917	0.961	18.668	-0.135	-0.135	0.000	0.000	0.000	0.000
19	A	127	LEU	0	-0.060	-0.005	20.270	0.016	0.016	0.000	0.000	0.000	0.000
20	A	128	GLY	0	0.075	0.048	23.169	-0.026	-0.026	0.000	0.000	0.000	0.000
21	A	129	PRO	0	-0.029	-0.037	26.102	0.001	0.001	0.000	0.000	0.000	0.000
22	A	130	GLU	-1	-0.758	-0.881	23.166	0.173	0.173	0.000	0.000	0.000	0.000
23	A	131	TRP	0	0.023	-0.010	22.951	0.019	0.019	0.000	0.000	0.000	0.000
24	A	132	GLU	-1	-0.833	-0.900	23.755	0.103	0.103	0.000	0.000	0.000	0.000
25	A	133	PRO	0	0.029	0.007	25.512	0.008	0.008	0.000	0.000	0.000	0.000
26	A	134	MET	0	0.028	0.046	16.864	0.007	0.007	0.000	0.000	0.000	0.000
27	A	135	VAL	0	0.013	-0.001	20.775	0.023	0.023	0.000	0.000	0.000	0.000
28	A	136	LEU	0	-0.056	-0.013	22.107	0.002	0.002	0.000	0.000	0.000	0.000
29	A	137	SER	0	-0.078	-0.046	20.764	0.016	0.016	0.000	0.000	0.000	0.000
30	A	138	LEU	0	-0.059	-0.032	16.167	0.024	0.024	0.000	0.000	0.000	0.000
31	A	139	GLY	0	0.013	0.011	19.492	0.010	0.010	0.000	0.000	0.000	0.000
32	A	140	LEU	0	-0.111	-0.047	22.175	-0.026	-0.026	0.000	0.000	0.000	0.000
33	A	141	SER	0	0.004	-0.024	24.520	0.001	0.001	0.000	0.000	0.000	0.000
34	A	142	GLN	0	0.110	0.023	28.237	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	143	THR	0	0.013	0.004	30.905	-0.007	-0.007	0.000	0.000	0.000	0.000
36	A	144	ASP	-1	-0.814	-0.859	27.101	0.089	0.089	0.000	0.000	0.000	0.000
37	A	145	ILE	0	0.070	0.039	26.505	-0.013	-0.013	0.000	0.000	0.000	0.000
38	A	146	TYR	0	-0.023	-0.008	29.181	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	147	ARG	1	0.942	0.966	30.242	-0.057	-0.057	0.000	0.000	0.000	0.000
40	A	148	CYS	0	-0.047	-0.004	27.240	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	149	LYS	1	0.828	0.890	29.602	-0.086	-0.086	0.000	0.000	0.000	0.000
42	A	150	ALA	0	-0.035	-0.018	32.520	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	151	ASN	0	-0.045	-0.029	29.339	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	152	HIS	0	-0.075	-0.037	28.184	-0.016	-0.016	0.000	0.000	0.000	0.000
45	A	153	PRO	0	0.021	0.010	32.620	0.006	0.006	0.000	0.000	0.000	0.000
46	A	154	HIS	0	-0.002	0.004	35.415	0.006	0.006	0.000	0.000	0.000	0.000
47	A	155	ASN	0	0.011	0.002	29.795	0.002	0.002	0.000	0.000	0.000	0.000
48	A	156	VAL	0	0.102	0.045	29.375	0.000	0.000	0.000	0.000	0.000	0.000
49	A	157	GLN	0	0.043	0.023	24.563	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	158	SER	0	0.022	-0.005	25.884	0.001	0.001	0.000	0.000	0.000	0.000
51	A	159	GLN	0	-0.040	-0.006	26.437	0.011	0.011	0.000	0.000	0.000	0.000
52	A	160	VAL	0	0.004	0.011	22.856	0.008	0.008	0.000	0.000	0.000	0.000
53	A	161	VAL	0	0.008	-0.003	21.021	0.014	0.014	0.000	0.000	0.000	0.000
54	A	162	GLU	-1	-0.793	-0.870	21.699	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	163	ALA	0	0.029	0.008	23.134	0.006	0.006	0.000	0.000	0.000	0.000
56	A	164	PHE	0	0.056	0.006	18.118	0.021	0.021	0.000	0.000	0.000	0.000
57	A	165	ILE	0	-0.010	0.001	18.472	0.012	0.012	0.000	0.000	0.000	0.000
58	A	166	ARG	1	0.824	0.898	19.313	0.003	0.003	0.000	0.000	0.000	0.000
59	A	167	TRP	0	-0.009	0.011	13.107	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	168	ARG	1	0.836	0.880	12.910	0.162	0.162	0.000	0.000	0.000	0.000
61	A	169	GLN	0	-0.066	-0.031	16.053	0.011	0.011	0.000	0.000	0.000	0.000
62	A	170	ARG	1	0.807	0.890	18.343	-0.119	-0.119	0.000	0.000	0.000	0.000
63	A	171	PHE	0	-0.008	0.003	16.477	0.008	0.008	0.000	0.000	0.000	0.000
64	A	172	GLY	0	0.048	0.031	14.498	0.059	0.059	0.000	0.000	0.000	0.000
65	A	173	LYS	1	0.951	0.974	10.914	-0.391	-0.391	0.000	0.000	0.000	0.000
66	A	174	GLN	0	0.002	-0.007	10.464	0.159	0.159	0.000	0.000	0.000	0.000
67	A	175	ALA	0	-0.013	0.024	12.399	0.051	0.051	0.000	0.000	0.000	0.000
68	A	176	THR	0	0.001	-0.007	7.838	-0.096	-0.096	0.000	0.000	0.000	0.000
69	A	177	PHE	0	0.077	0.017	7.381	-0.172	-0.172	0.000	0.000	0.000	0.000
70	A	178	GLN	0	0.023	0.031	6.986	-0.209	-0.209	0.000	0.000	0.000	0.000
71	A	179	SER	0	-0.024	-0.020	8.777	-0.106	-0.106	0.000	0.000	0.000	0.000
72	A	180	LEU	0	0.006	0.013	11.927	-0.088	-0.088	0.000	0.000	0.000	0.000
73	A	181	HIS	0	0.031	0.013	11.025	-0.110	-0.110	0.000	0.000	0.000	0.000
74	A	182	ASN	0	-0.019	-0.021	11.918	-0.081	-0.081	0.000	0.000	0.000	0.000
75	A	183	GLY	0	0.037	0.023	14.908	-0.056	-0.056	0.000	0.000	0.000	0.000
76	A	184	LEU	0	-0.002	-0.017	15.364	-0.041	-0.041	0.000	0.000	0.000	0.000
77	A	185	ARG	1	0.887	0.946	14.030	-0.647	-0.647	0.000	0.000	0.000	0.000
78	A	186	ALA	0	-0.034	-0.009	18.844	-0.033	-0.033	0.000	0.000	0.000	0.000
79	A	187	VAL	0	-0.077	-0.030	21.071	-0.030	-0.030	0.000	0.000	0.000	0.000
80	A	188	GLU	-1	-0.947	-0.964	22.826	0.200	0.200	0.000	0.000	0.000	0.000
81	A	189	VAL	0	-0.014	0.002	20.501	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	190	ASP	-1	-0.801	-0.888	19.419	0.426	0.426	0.000	0.000	0.000	0.000
83	A	191	PRO	0	-0.003	-0.010	14.754	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	192	SER	0	-0.045	-0.046	15.014	0.099	0.099	0.000	0.000	0.000	0.000
85	A	193	LEU	0	-0.047	-0.017	16.290	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	194	LEU	0	-0.007	-0.023	11.618	-0.044	-0.044	0.000	0.000	0.000	0.000
87	A	195	LEU	0	0.008	0.009	11.133	0.008	0.008	0.000	0.000	0.000	0.000
88	A	196	HIS	0	0.026	0.008	13.439	-0.123	-0.123	0.000	0.000	0.000	0.000
89	A	197	MET	0	-0.112	-0.031	13.863	-0.098	-0.098	0.000	0.000	0.000	0.000
90	A	198	LEU	0	-0.106	-0.049	8.609	-0.123	-0.123	0.000	0.000	0.000	0.000
91	A	199	GLU	-1	-0.961	-0.962	11.067	0.415	0.415	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:109:HIS)