FMO DATABASE

FMODB ID: MVNGZ

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	OptH
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	-679046.516083
FMO2-HF: Nuclear repulsion	642313.303262
FMO2-HF: Total energy	-36733.212822
FMO2-MP2: Total energy	-36840.828411

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.
-10.139	-4.959	0.752	-2.352	-3.58	-0.001

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 : 0.036 / q_NPA : 0.006

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	0.043	0.037	3.274	-4.359	-2.045	0.037	-0.960	-1.392	0.004
4	A	112	ASN	0	-0.049	-0.033	2.523	-4.297	-1.826	0.714	-1.303	-1.882	-0.005
5	A	113	SER	0	-0.052	-0.035	4.278	-0.665	-0.270	0.001	-0.089	-0.306	0.000
6	A	114	SER	0	0.007	-0.015	6.220	-0.110	-0.110	0.000	0.000	0.000	0.000
7	A	115	PRO	0	0.001	0.020	8.995	-0.254	-0.254	0.000	0.000	0.000	0.000
8	A	116	SER	0	0.046	0.022	10.975	0.006	0.006	0.000	0.000	0.000	0.000
9	A	117	ASP	-1	-0.759	-0.889	12.483	-0.209	-0.209	0.000	0.000	0.000	0.000
10	A	118	ARG	1	0.895	0.946	14.358	0.331	0.331	0.000	0.000	0.000	0.000
11	A	119	GLN	0	0.124	0.052	8.973	0.125	0.125	0.000	0.000	0.000	0.000
12	A	120	ILE	0	0.011	0.018	14.602	0.087	0.087	0.000	0.000	0.000	0.000
13	A	121	ASN	0	-0.031	-0.028	17.246	0.049	0.049	0.000	0.000	0.000	0.000
14	A	122	GLN	0	-0.031	-0.014	15.116	0.009	0.009	0.000	0.000	0.000	0.000
15	A	123	LEU	0	0.047	0.019	15.982	0.029	0.029	0.000	0.000	0.000	0.000
16	A	124	ALA	0	-0.017	-0.016	18.836	0.017	0.017	0.000	0.000	0.000	0.000
17	A	125	GLN	0	-0.103	-0.035	22.080	0.001	0.001	0.000	0.000	0.000	0.000
18	A	126	ARG	1	0.921	0.962	18.689	-0.113	-0.113	0.000	0.000	0.000	0.000
19	A	127	LEU	0	-0.048	-0.013	20.182	0.018	0.018	0.000	0.000	0.000	0.000
20	A	128	GLY	0	0.059	0.046	23.189	-0.026	-0.026	0.000	0.000	0.000	0.000
21	A	129	PRO	0	-0.028	-0.035	26.121	0.001	0.001	0.000	0.000	0.000	0.000
22	A	130	GLU	-1	-0.762	-0.885	23.182	0.165	0.165	0.000	0.000	0.000	0.000
23	A	131	TRP	0	0.026	-0.006	22.969	0.020	0.020	0.000	0.000	0.000	0.000
24	A	132	GLU	-1	-0.894	-0.941	23.773	0.107	0.107	0.000	0.000	0.000	0.000
25	A	133	PRO	0	0.004	0.003	25.419	0.009	0.009	0.000	0.000	0.000	0.000
26	A	134	MET	0	0.026	0.040	16.991	0.008	0.008	0.000	0.000	0.000	0.000
27	A	135	VAL	0	0.009	0.004	21.003	0.025	0.025	0.000	0.000	0.000	0.000
28	A	136	LEU	0	-0.044	-0.019	22.124	0.003	0.003	0.000	0.000	0.000	0.000
29	A	137	SER	0	-0.085	-0.050	20.718	0.017	0.017	0.000	0.000	0.000	0.000
30	A	138	LEU	0	-0.059	-0.032	16.398	0.025	0.025	0.000	0.000	0.000	0.000
31	A	139	GLY	0	0.009	0.010	19.506	0.011	0.011	0.000	0.000	0.000	0.000
32	A	140	LEU	0	-0.107	-0.045	22.188	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	141	SER	0	0.027	0.010	24.535	0.001	0.001	0.000	0.000	0.000	0.000
34	A	142	GLN	0	0.102	0.021	28.252	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	143	THR	0	0.008	0.007	30.921	-0.007	-0.007	0.000	0.000	0.000	0.000
36	A	144	ASP	-1	-0.830	-0.892	26.830	0.093	0.093	0.000	0.000	0.000	0.000
37	A	145	ILE	0	0.048	0.021	26.645	-0.014	-0.014	0.000	0.000	0.000	0.000
38	A	146	TYR	0	-0.029	-0.013	29.199	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	147	ARG	1	0.948	0.963	30.649	-0.053	-0.053	0.000	0.000	0.000	0.000
40	A	148	CYS	0	-0.030	0.024	27.058	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	149	LYS	1	0.876	0.932	29.616	-0.083	-0.083	0.000	0.000	0.000	0.000
42	A	150	ALA	0	-0.043	-0.021	32.532	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	151	ASN	0	-0.058	-0.053	29.613	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	152	HIS	0	-0.085	-0.045	28.061	-0.016	-0.016	0.000	0.000	0.000	0.000
45	A	153	PRO	0	0.014	0.001	32.629	0.006	0.006	0.000	0.000	0.000	0.000
46	A	154	HIS	0	0.007	0.006	35.441	0.006	0.006	0.000	0.000	0.000	0.000
47	A	155	ASN	0	0.023	0.005	29.843	0.001	0.001	0.000	0.000	0.000	0.000
48	A	156	VAL	0	0.103	0.047	29.296	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	157	GLN	0	0.037	0.017	24.568	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	158	SER	0	-0.008	-0.019	25.889	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	159	GLN	0	-0.026	0.003	26.445	0.012	0.012	0.000	0.000	0.000	0.000
52	A	160	VAL	0	0.015	0.016	22.909	0.009	0.009	0.000	0.000	0.000	0.000
53	A	161	VAL	0	0.006	-0.003	20.998	0.014	0.014	0.000	0.000	0.000	0.000
54	A	162	GLU	-1	-0.836	-0.887	21.710	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	163	ALA	0	0.044	0.008	23.149	0.007	0.007	0.000	0.000	0.000	0.000
56	A	164	PHE	0	0.044	0.002	18.024	0.020	0.020	0.000	0.000	0.000	0.000
57	A	165	ILE	0	-0.012	0.000	18.488	0.012	0.012	0.000	0.000	0.000	0.000
58	A	166	ARG	1	0.897	0.947	19.331	0.002	0.002	0.000	0.000	0.000	0.000
59	A	167	TRP	0	0.006	0.027	13.098	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	168	ARG	1	0.858	0.896	13.019	0.175	0.175	0.000	0.000	0.000	0.000
61	A	169	GLN	0	-0.073	-0.034	16.076	0.019	0.019	0.000	0.000	0.000	0.000
62	A	170	ARG	1	0.826	0.904	18.366	-0.124	-0.124	0.000	0.000	0.000	0.000
63	A	171	PHE	0	-0.009	0.002	16.430	0.007	0.007	0.000	0.000	0.000	0.000
64	A	172	GLY	0	0.046	0.032	14.524	0.061	0.061	0.000	0.000	0.000	0.000
65	A	173	LYS	1	0.956	0.973	10.941	-0.411	-0.411	0.000	0.000	0.000	0.000
66	A	174	GLN	0	-0.012	-0.011	10.480	0.133	0.133	0.000	0.000	0.000	0.000
67	A	175	ALA	0	0.001	0.026	12.412	0.051	0.051	0.000	0.000	0.000	0.000
68	A	176	THR	0	-0.004	-0.012	7.846	-0.105	-0.105	0.000	0.000	0.000	0.000
69	A	177	PHE	0	0.063	0.011	7.370	-0.154	-0.154	0.000	0.000	0.000	0.000
70	A	178	GLN	0	0.003	0.014	7.049	-0.238	-0.238	0.000	0.000	0.000	0.000
71	A	179	SER	0	-0.033	-0.025	8.791	-0.105	-0.105	0.000	0.000	0.000	0.000
72	A	180	LEU	0	0.005	0.009	11.943	-0.094	-0.094	0.000	0.000	0.000	0.000
73	A	181	HIS	0	0.038	0.018	10.989	-0.108	-0.108	0.000	0.000	0.000	0.000
74	A	182	ASN	0	-0.004	-0.009	11.960	-0.063	-0.063	0.000	0.000	0.000	0.000
75	A	183	GLY	0	0.037	0.022	14.919	-0.057	-0.057	0.000	0.000	0.000	0.000
76	A	184	LEU	0	-0.008	-0.015	15.173	-0.042	-0.042	0.000	0.000	0.000	0.000
77	A	185	ARG	1	0.896	0.951	13.949	-0.661	-0.661	0.000	0.000	0.000	0.000
78	A	186	ALA	0	-0.037	-0.012	18.855	-0.033	-0.033	0.000	0.000	0.000	0.000
79	A	187	VAL	0	-0.066	-0.026	21.083	-0.030	-0.030	0.000	0.000	0.000	0.000
80	A	188	GLU	-1	-0.947	-0.966	22.845	0.196	0.196	0.000	0.000	0.000	0.000
81	A	189	VAL	0	-0.014	0.005	20.419	-0.019	-0.019	0.000	0.000	0.000	0.000
82	A	190	ASP	-1	-0.815	-0.881	19.560	0.408	0.408	0.000	0.000	0.000	0.000
83	A	191	PRO	0	0.010	-0.011	14.826	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	192	SER	0	-0.035	-0.057	15.028	0.093	0.093	0.000	0.000	0.000	0.000
85	A	193	LEU	0	-0.061	-0.019	16.306	-0.012	-0.012	0.000	0.000	0.000	0.000
86	A	194	LEU	0	0.008	-0.021	11.485	-0.051	-0.051	0.000	0.000	0.000	0.000
87	A	195	LEU	0	0.005	0.010	11.258	0.003	0.003	0.000	0.000	0.000	0.000
88	A	196	HIS	0	0.017	0.001	13.348	-0.110	-0.110	0.000	0.000	0.000	0.000
89	A	197	MET	0	-0.113	-0.032	13.559	-0.083	-0.083	0.000	0.000	0.000	0.000
90	A	198	LEU	0	-0.115	-0.049	8.401	-0.118	-0.118	0.000	0.000	0.000	0.000
91	A	199	GLU	-1	-0.974	-0.968	10.947	0.395	0.395	0.000	0.000	0.000	0.000

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