FMO DATABASE

FMODB ID: 4N44N

Calculation Name: 2Q00-A-Xray311

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2Q00

Chain ID: A

ChEMBL ID:

UniProt ID: P95883

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	124
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1100338.89823
FMO2-HF: Nuclear repulsion	1051660.625197
FMO2-HF: Total energy	-48678.273033
FMO2-MP2: Total energy	-48824.021101

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:1:ACE )

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

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.
3.282	5.839	2.392	-2.765	-2.181	-0.018

Interaction energy analysis for fragmet #1(A:1:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.081 / q_NPA : 0.033

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	3	ILE	0	-0.020	-0.001	3.839	0.246	1.491	-0.003	-0.648	-0.594	0.000
4	A	4	SER	0	0.000	0.003	5.017	0.355	0.454	0.000	-0.005	-0.093	0.000
5	A	5	THR	0	-0.015	-0.023	5.781	-0.083	-0.083	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.015	-0.047	8.184	-0.074	-0.074	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.002	-0.005	10.593	-0.043	-0.043	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.796	-0.897	6.236	0.620	0.620	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.025	0.025	10.608	-0.059	-0.059	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.025	-0.008	12.901	-0.034	-0.034	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.016	0.002	13.651	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.869	-0.928	13.405	0.016	0.016	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.912	-0.971	15.629	0.016	0.016	0.000	0.000	0.000	0.000
14	A	14	ALA	0	-0.059	-0.041	18.279	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.819	-0.884	16.886	0.061	0.061	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.973	-0.979	19.331	-0.028	-0.028	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.017	-0.026	21.703	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.017	0.002	23.046	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.047	-0.016	22.919	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.874	0.942	24.795	0.007	0.007	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.002	0.004	28.018	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.897	-0.946	27.345	0.023	0.023	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.027	-0.020	27.237	0.004	0.004	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.069	0.051	27.609	0.006	0.006	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.022	-0.003	25.582	0.009	0.009	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.009	-0.002	23.146	0.007	0.007	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.046	-0.020	22.722	0.011	0.011	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.797	-0.903	23.607	0.084	0.084	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.867	0.946	19.694	-0.035	-0.035	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.001	-0.049	18.772	0.015	0.015	0.000	0.000	0.000	0.000
31	A	31	TYR	0	-0.023	-0.004	19.231	0.021	0.021	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.881	0.940	19.098	-0.049	-0.049	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.024	0.013	15.168	0.018	0.018	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.009	0.002	15.335	0.039	0.039	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.876	-0.961	17.407	0.134	0.134	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.867	-0.932	13.779	0.190	0.190	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.027	0.027	12.903	0.046	0.046	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.034	-0.010	13.976	0.026	0.026	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.832	0.917	15.825	-0.142	-0.142	0.000	0.000	0.000	0.000
40	A	40	LEU	0	0.049	0.028	8.349	-0.037	-0.037	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.043	0.028	12.896	0.013	0.013	0.000	0.000	0.000	0.000
42	A	42	VAL	0	-0.083	-0.042	14.453	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.068	-0.044	13.191	-0.035	-0.035	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.866	-0.931	10.432	0.554	0.554	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.106	-0.049	13.491	-0.067	-0.067	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.021	-0.002	16.560	-0.054	-0.054	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.052	0.034	18.362	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.954	0.951	21.399	-0.117	-0.117	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.899	-0.947	23.548	0.122	0.122	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.009	-0.007	22.183	-0.012	-0.012	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.006	0.003	19.986	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.007	-0.003	23.186	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	53	ASN	0	-0.095	-0.044	26.621	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.025	0.043	22.700	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.910	0.954	26.100	-0.077	-0.077	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.022	-0.023	27.694	0.000	0.000	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.954	0.957	25.640	-0.047	-0.047	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.007	0.029	22.778	0.000	0.000	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.907	0.965	22.091	-0.071	-0.071	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.004	0.012	19.260	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.952	0.980	24.527	-0.070	-0.070	0.000	0.000	0.000	0.000
62	A	62	SER	0	0.157	0.056	26.330	0.009	0.009	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.851	-0.933	26.828	0.079	0.079	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.085	-0.043	24.742	0.003	0.003	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.099	0.075	20.750	0.007	0.007	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.016	0.021	23.506	0.010	0.010	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.841	0.935	25.868	-0.086	-0.086	0.000	0.000	0.000	0.000
68	A	68	ALA	0	0.056	0.015	21.134	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.002	-0.009	21.592	0.007	0.007	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.897	0.944	22.632	-0.097	-0.097	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.011	-0.014	23.910	0.001	0.001	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.048	0.037	18.007	0.002	0.002	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.857	0.930	21.015	-0.107	-0.107	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.033	-0.025	23.325	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.042	0.009	15.981	0.005	0.005	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.077	0.029	17.626	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	77	THR	0	0.029	-0.006	20.137	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.811	-0.908	20.449	0.152	0.152	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.061	0.046	17.829	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	80	PRO	0	-0.051	-0.022	20.572	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.061	-0.063	23.934	-0.013	-0.013	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.056	0.047	18.152	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	83	TRP	0	0.034	0.001	20.324	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.858	0.936	22.569	-0.111	-0.111	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.012	-0.015	23.325	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.033	0.028	21.325	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	87	TRP	0	-0.034	-0.026	23.235	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	88	THR	0	0.004	-0.002	26.422	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.014	-0.009	22.965	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	90	HIS	0	-0.033	-0.016	25.712	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.033	-0.027	27.222	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.860	-0.941	30.932	0.051	0.051	0.000	0.000	0.000	0.000
93	A	93	GLY	0	-0.008	-0.001	29.190	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	94	PHE	0	-0.095	-0.045	27.788	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	HIS	0	-0.063	-0.038	29.790	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.940	-0.974	32.921	0.041	0.041	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.093	-0.015	33.225	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.010	-0.002	34.194	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.018	0.017	29.134	0.002	0.002	0.000	0.000	0.000	0.000
100	A	100	ASN	0	0.008	0.007	32.629	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.818	-0.917	28.752	0.035	0.035	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.883	0.920	28.796	-0.025	-0.025	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.903	-0.968	29.045	0.046	0.046	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.058	0.029	25.163	0.007	0.007	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.895	0.951	24.461	-0.026	-0.026	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.953	0.971	23.887	-0.048	-0.048	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.027	0.026	24.597	0.008	0.008	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.921	0.976	19.859	-0.069	-0.069	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.954	-0.971	19.182	0.131	0.131	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.844	-0.898	19.239	0.135	0.135	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.047	-0.030	16.710	0.024	0.024	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.957	0.999	12.408	-0.121	-0.121	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.874	0.925	14.034	-0.122	-0.122	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.008	-0.006	14.715	0.036	0.036	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.004	-0.017	10.581	0.051	0.051	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.011	-0.005	9.675	0.096	0.096	0.000	0.000	0.000	0.000
117	A	117	PHE	0	-0.021	-0.002	9.865	0.097	0.097	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.010	-0.008	10.592	0.057	0.057	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.023	0.023	4.757	0.030	0.068	0.000	-0.006	-0.031	0.000
120	A	120	ASN	0	-0.020	-0.016	6.021	0.586	0.586	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.132	-0.073	8.268	-0.052	-0.052	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.003	0.012	5.233	-0.111	-0.111	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.948	-0.967	2.423	1.610	2.785	2.395	-2.106	-1.463	-0.018
124	A	124	NME	0	-0.051	-0.018	5.854	-0.309	-0.309	0.000	0.000	0.000	0.000

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