FMO DATABASE

FMODB ID: 762KK

Calculation Name: 2QR3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QR3

Chain ID: A

ChEMBL ID:

UniProt ID: Q64UD2

Base Structure: X-ray

Registration Date: 2023-09-21

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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1078514.766486
FMO2-HF: Nuclear repulsion	1030629.011742
FMO2-HF: Total energy	-47885.754744
FMO2-MP2: Total energy	-48028.970518

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:0:SER)

Summations of interaction energy for fragment #1(A:0:SER)

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.
-8.547	-6.554	-0.015	-0.969	-1.008	0.002

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.009

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	2	GLY	0	0.027	0.026	3.855	1.217	3.126	-0.012	-0.951	-0.946	0.002
4	A	3	THR	0	-0.017	-0.021	5.259	0.746	0.804	-0.001	-0.002	-0.055	0.000
5	A	4	ILE	0	0.005	0.027	8.975	-0.126	-0.126	0.000	0.000	0.000	0.000
6	A	5	ILE	0	-0.011	-0.006	11.860	0.205	0.205	0.000	0.000	0.000	0.000
7	A	6	ILE	0	-0.015	-0.014	15.386	0.006	0.006	0.000	0.000	0.000	0.000
8	A	7	VAL	0	0.004	0.004	18.417	0.058	0.058	0.000	0.000	0.000	0.000
9	A	8	ASP	-1	-0.737	-0.885	21.703	-0.393	-0.393	0.000	0.000	0.000	0.000
10	A	9	ASP	-1	-0.755	-0.852	24.878	-0.299	-0.299	0.000	0.000	0.000	0.000
11	A	10	ASN	0	-0.032	-0.002	27.664	0.030	0.030	0.000	0.000	0.000	0.000
12	A	11	LYS	1	0.917	0.929	26.482	0.269	0.269	0.000	0.000	0.000	0.000
13	A	12	GLY	0	0.027	0.027	25.871	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	13	VAL	0	0.005	0.011	23.428	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	14	LEU	0	-0.014	0.000	21.402	-0.035	-0.035	0.000	0.000	0.000	0.000
16	A	15	THR	0	-0.039	-0.029	21.121	-0.026	-0.026	0.000	0.000	0.000	0.000
17	A	16	ALA	0	-0.007	-0.005	21.720	-0.010	-0.010	0.000	0.000	0.000	0.000
18	A	17	VAL	0	0.041	0.012	17.620	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	18	GLN	0	0.023	0.021	16.549	-0.063	-0.063	0.000	0.000	0.000	0.000
20	A	19	LEU	0	-0.056	-0.030	16.575	-0.033	-0.033	0.000	0.000	0.000	0.000
21	A	20	LEU	0	-0.034	-0.013	17.582	0.009	0.009	0.000	0.000	0.000	0.000
22	A	21	LEU	0	0.024	0.007	13.171	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.854	0.913	12.023	0.297	0.297	0.000	0.000	0.000	0.000
24	A	23	ASN	0	-0.051	-0.029	11.596	0.030	0.030	0.000	0.000	0.000	0.000
25	A	24	HIS	0	-0.020	0.016	8.945	0.079	0.079	0.000	0.000	0.000	0.000
26	A	25	PHE	0	0.018	0.007	7.174	-0.315	-0.315	0.000	0.000	0.000	0.000
27	A	26	SER	0	-0.026	-0.019	4.544	0.933	1.012	-0.001	-0.001	-0.077	0.000
28	A	27	LYS	1	0.757	0.855	7.214	1.181	1.181	0.000	0.000	0.000	0.000
29	A	28	VAL	0	0.031	0.026	10.597	-0.209	-0.209	0.000	0.000	0.000	0.000
30	A	29	ILE	0	0.000	0.008	13.454	0.177	0.177	0.000	0.000	0.000	0.000
31	A	30	THR	0	-0.014	0.008	16.187	-0.033	-0.033	0.000	0.000	0.000	0.000
32	A	31	LEU	0	-0.063	-0.026	19.481	0.056	0.056	0.000	0.000	0.000	0.000
33	A	32	SER	0	0.017	-0.034	22.403	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	33	SER	0	0.007	0.006	24.949	0.026	0.026	0.000	0.000	0.000	0.000
35	A	34	PRO	0	0.103	0.047	24.836	-0.028	-0.028	0.000	0.000	0.000	0.000
36	A	35	VAL	0	0.015	0.017	25.185	-0.017	-0.017	0.000	0.000	0.000	0.000
37	A	36	SER	0	0.001	-0.008	22.681	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	37	LEU	0	0.035	0.017	19.501	-0.030	-0.030	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.046	-0.028	20.273	-0.033	-0.033	0.000	0.000	0.000	0.000
40	A	39	THR	0	-0.051	-0.021	20.481	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	40	VAL	0	0.026	0.004	16.499	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	41	LEU	0	-0.020	-0.008	15.813	-0.081	-0.081	0.000	0.000	0.000	0.000
43	A	42	ARG	1	0.850	0.938	15.995	0.299	0.299	0.000	0.000	0.000	0.000
44	A	43	GLU	-1	-0.886	-0.955	16.220	-0.355	-0.355	0.000	0.000	0.000	0.000
45	A	44	GLU	-1	-0.822	-0.892	12.742	-0.666	-0.666	0.000	0.000	0.000	0.000
46	A	45	ASN	0	-0.089	-0.028	9.577	-0.139	-0.139	0.000	0.000	0.000	0.000
47	A	46	PRO	0	-0.026	-0.006	9.086	-0.365	-0.365	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.767	-0.896	4.580	-8.525	-8.578	-0.001	-0.015	0.070	0.000
49	A	48	VAL	0	-0.015	-0.003	9.343	0.189	0.189	0.000	0.000	0.000	0.000
50	A	49	VAL	0	-0.030	-0.014	12.658	0.038	0.038	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.020	0.004	15.973	0.034	0.034	0.000	0.000	0.000	0.000
52	A	51	LEU	0	-0.017	-0.026	18.373	0.039	0.039	0.000	0.000	0.000	0.000
53	A	52	ASP	-1	-0.832	-0.921	21.768	-0.345	-0.345	0.000	0.000	0.000	0.000
54	A	53	MET	0	0.000	0.017	25.167	0.000	0.000	0.000	0.000	0.000	0.000
55	A	54	ASN	0	-0.013	-0.017	27.735	0.008	0.008	0.000	0.000	0.000	0.000
56	A	55	PHE	0	-0.025	-0.005	25.576	0.013	0.013	0.000	0.000	0.000	0.000
57	A	56	THR	0	-0.063	-0.042	28.313	0.011	0.011	0.000	0.000	0.000	0.000
58	A	57	SER	0	0.056	0.055	31.151	0.022	0.022	0.000	0.000	0.000	0.000
59	A	58	GLY	0	-0.007	-0.016	33.886	0.005	0.005	0.000	0.000	0.000	0.000
60	A	59	ILE	0	-0.040	-0.023	37.490	0.004	0.004	0.000	0.000	0.000	0.000
61	A	60	ASN	0	-0.065	-0.036	34.931	0.015	0.015	0.000	0.000	0.000	0.000
62	A	61	ASN	0	-0.061	-0.041	36.607	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	62	GLY	0	0.026	0.013	36.280	0.012	0.012	0.000	0.000	0.000	0.000
64	A	63	ASN	0	-0.070	-0.030	32.487	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	64	GLU	-1	-0.784	-0.893	30.852	-0.248	-0.248	0.000	0.000	0.000	0.000
66	A	65	GLY	0	0.037	0.021	27.050	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	66	LEU	0	-0.034	-0.016	26.639	-0.025	-0.025	0.000	0.000	0.000	0.000
68	A	67	PHE	0	0.006	0.008	28.049	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	68	TRP	0	0.019	-0.019	24.825	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	69	LEU	0	0.000	0.009	22.269	-0.035	-0.035	0.000	0.000	0.000	0.000
71	A	70	HIS	0	-0.007	0.004	23.637	-0.034	-0.034	0.000	0.000	0.000	0.000
72	A	71	GLU	-1	-0.776	-0.853	25.511	-0.305	-0.305	0.000	0.000	0.000	0.000
73	A	72	ILE	0	-0.032	-0.010	19.088	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	73	LYS	1	0.853	0.920	18.087	0.687	0.687	0.000	0.000	0.000	0.000
75	A	74	ARG	1	0.771	0.851	22.022	0.299	0.299	0.000	0.000	0.000	0.000
76	A	75	GLN	0	-0.084	-0.033	20.917	0.051	0.051	0.000	0.000	0.000	0.000
77	A	76	TYR	0	-0.008	-0.016	16.888	0.008	0.008	0.000	0.000	0.000	0.000
78	A	77	ARG	1	0.973	0.985	18.462	0.339	0.339	0.000	0.000	0.000	0.000
79	A	78	ASP	-1	-0.907	-0.958	15.200	-0.595	-0.595	0.000	0.000	0.000	0.000
80	A	79	LEU	0	-0.017	0.013	13.080	-0.123	-0.123	0.000	0.000	0.000	0.000
81	A	80	PRO	0	0.014	0.016	12.003	0.199	0.199	0.000	0.000	0.000	0.000
82	A	81	VAL	0	-0.004	0.001	15.286	-0.055	-0.055	0.000	0.000	0.000	0.000
83	A	82	VAL	0	0.000	0.007	16.121	0.060	0.060	0.000	0.000	0.000	0.000
84	A	83	LEU	0	0.016	0.010	18.914	0.011	0.011	0.000	0.000	0.000	0.000
85	A	84	PHE	0	0.010	-0.012	22.357	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	85	THR	0	0.032	0.001	23.837	0.026	0.026	0.000	0.000	0.000	0.000
87	A	86	ALA	0	0.047	0.044	27.345	0.001	0.001	0.000	0.000	0.000	0.000
88	A	87	TYR	0	0.024	-0.013	29.393	0.001	0.001	0.000	0.000	0.000	0.000
89	A	88	ALA	0	-0.054	-0.023	32.310	0.006	0.006	0.000	0.000	0.000	0.000
90	A	89	ASP	-1	-0.797	-0.890	31.106	-0.251	-0.251	0.000	0.000	0.000	0.000
91	A	90	ILE	0	-0.025	-0.017	29.425	-0.014	-0.014	0.000	0.000	0.000	0.000
92	A	91	ASP	-1	-0.896	-0.951	30.578	-0.237	-0.237	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.010	0.006	31.255	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	93	ALA	0	0.027	0.014	26.452	-0.018	-0.018	0.000	0.000	0.000	0.000
95	A	94	VAL	0	-0.030	-0.013	26.913	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	95	ARG	1	0.770	0.861	28.539	0.250	0.250	0.000	0.000	0.000	0.000
97	A	96	GLY	0	0.094	0.025	26.370	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	97	ILE	0	-0.033	0.003	22.501	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	98	LYS	1	0.872	0.938	25.117	0.236	0.236	0.000	0.000	0.000	0.000
100	A	99	GLU	-1	-0.851	-0.901	27.311	-0.271	-0.271	0.000	0.000	0.000	0.000
101	A	100	GLY	0	0.001	0.007	23.407	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	101	ALA	0	-0.059	-0.026	21.185	-0.052	-0.052	0.000	0.000	0.000	0.000
103	A	102	SER	0	-0.044	-0.032	16.506	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	103	ASP	-1	-0.814	-0.916	17.917	-0.576	-0.576	0.000	0.000	0.000	0.000
105	A	104	PHE	0	-0.072	-0.044	19.895	0.008	0.008	0.000	0.000	0.000	0.000
106	A	105	VAL	0	-0.008	0.006	19.349	0.009	0.009	0.000	0.000	0.000	0.000
107	A	106	VAL	0	-0.035	-0.018	22.535	0.010	0.010	0.000	0.000	0.000	0.000
108	A	107	LYS	1	0.782	0.887	25.350	0.384	0.384	0.000	0.000	0.000	0.000
109	A	108	PRO	0	-0.003	-0.027	27.359	0.017	0.017	0.000	0.000	0.000	0.000
110	A	109	TRP	0	0.014	0.007	22.044	0.004	0.004	0.000	0.000	0.000	0.000
111	A	110	ASP	-1	-0.839	-0.915	22.173	-0.312	-0.312	0.000	0.000	0.000	0.000
112	A	111	ASN	0	-0.032	-0.033	20.205	-0.062	-0.062	0.000	0.000	0.000	0.000
113	A	112	GLN	0	0.001	-0.006	15.468	-0.057	-0.057	0.000	0.000	0.000	0.000
114	A	113	LYS	1	1.021	1.002	17.367	0.316	0.316	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.052	-0.003	17.489	-0.057	-0.057	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.018	0.011	11.552	-0.094	-0.094	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.861	-0.921	13.346	-0.618	-0.618	0.000	0.000	0.000	0.000
118	A	117	THR	0	-0.053	-0.039	13.971	-0.066	-0.066	0.000	0.000	0.000	0.000
119	A	118	LEU	0	-0.033	-0.013	13.117	-0.066	-0.066	0.000	0.000	0.000	0.000
120	A	119	LEU	0	0.018	0.008	8.176	-0.260	-0.260	0.000	0.000	0.000	0.000
121	A	120	ASN	0	0.010	0.002	9.474	-0.307	-0.307	0.000	0.000	0.000	0.000
122	A	121	ALA	0	-0.034	-0.005	11.535	-0.030	-0.030	0.000	0.000	0.000	0.000
123	A	122	ALA	0	-0.012	-0.008	8.188	0.105	0.105	0.000	0.000	0.000	0.000
124	A	123	SER	0	-0.051	-0.018	7.145	-0.957	-0.957	0.000	0.000	0.000	0.000
125	A	124	GLN	0	-0.079	-0.041	8.114	0.611	0.611	0.000	0.000	0.000	0.000
126	A	125	ALA	0	-0.015	-0.004	9.851	-0.149	-0.149	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)