FMO DATABASE

FMODB ID: 3QRGL

Calculation Name: 2QLC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QLC

Chain ID: A

ChEMBL ID:

UniProt ID: Q8KES1

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1132767.5555
FMO2-HF: Nuclear repulsion	1083519.543179
FMO2-HF: Total energy	-49248.012321
FMO2-MP2: Total energy	-49394.564157

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:MET)

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

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.
-1.428	3.618	2.475	-2.56	-4.961	-0.006

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.018 / q_NPA : -0.002

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	LEU	0	0.032	0.024	2.448	-2.751	1.412	0.731	-1.861	-3.033	0.002
4	A	4	LYS	1	0.907	0.978	4.321	1.879	2.211	-0.001	-0.037	-0.294	0.000
5	A	5	VAL	0	0.003	0.010	5.596	0.316	0.316	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.759	0.860	7.301	1.311	1.311	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.064	0.030	11.474	0.109	0.109	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.055	0.037	13.675	-0.064	-0.064	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.959	0.980	10.895	0.216	0.216	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.758	-0.882	9.413	-0.637	-0.637	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.006	0.007	10.413	-0.078	-0.078	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.030	0.015	12.999	0.033	0.033	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.869	-0.926	9.336	0.151	0.151	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.055	-0.040	8.013	0.040	0.040	0.000	0.000	0.000	0.000
15	A	15	MET	0	-0.006	-0.003	10.004	0.037	0.037	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.836	0.926	12.380	-0.034	-0.034	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.009	0.006	12.903	0.009	0.009	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.833	0.917	8.651	0.262	0.262	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.014	0.007	15.620	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.029	-0.017	19.175	0.019	0.019	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.739	-0.830	21.575	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.911	-0.951	19.609	-0.031	-0.031	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.056	-0.049	23.857	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.795	0.879	26.577	0.035	0.035	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.811	-0.896	25.928	-0.087	-0.087	0.000	0.000	0.000	0.000
26	A	26	HIS	0	-0.005	-0.024	22.631	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.036	-0.010	21.815	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.009	-0.017	17.637	0.004	0.004	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.002	-0.001	17.277	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.013	0.008	11.604	-0.015	-0.015	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.045	0.021	12.844	0.035	0.035	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.000	0.003	10.159	-0.159	-0.159	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.082	0.036	7.566	0.138	0.138	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.063	0.027	10.388	-0.031	-0.031	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.830	0.906	8.347	0.538	0.538	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.035	0.016	8.389	-0.114	-0.114	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.016	-0.008	2.459	-2.250	-1.699	1.745	-0.662	-1.634	-0.008
38	A	38	ILE	0	0.028	0.012	6.211	0.409	0.409	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.027	-0.012	6.615	-0.241	-0.241	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.767	0.853	8.962	0.395	0.395	0.000	0.000	0.000	0.000
41	A	41	HIS	0	0.046	0.027	10.857	-0.093	-0.093	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.805	-0.862	14.102	-0.185	-0.185	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.008	-0.013	17.842	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.021	0.002	20.895	0.014	0.014	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.040	-0.034	23.665	0.015	0.015	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.017	0.017	24.305	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	47	GLY	0	-0.008	-0.002	27.332	0.008	0.008	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.067	-0.033	29.296	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.003	0.012	28.022	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.025	0.000	30.831	0.005	0.005	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.017	-0.004	31.581	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.014	-0.002	32.311	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.017	0.005	30.517	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.009	0.027	26.824	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.840	0.918	27.835	0.110	0.110	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.065	0.020	26.499	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.856	0.906	26.128	0.089	0.089	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.770	-0.868	25.749	-0.118	-0.118	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.014	0.016	21.510	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.054	0.018	21.417	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.933	0.980	22.232	0.120	0.120	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.015	-0.006	19.469	0.002	0.002	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.060	0.018	17.580	-0.013	-0.013	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.011	-0.006	17.741	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.759	0.874	18.511	0.216	0.216	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.790	-0.868	14.427	-0.338	-0.338	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.101	-0.044	14.432	-0.038	-0.038	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.014	-0.005	13.924	-0.034	-0.034	0.000	0.000	0.000	0.000
69	A	69	HIS	0	0.006	0.005	13.811	0.047	0.047	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.017	-0.015	14.667	0.020	0.020	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.008	-0.004	15.093	-0.044	-0.044	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.012	-0.006	13.118	0.004	0.004	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.014	0.010	16.629	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.003	-0.011	16.221	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	75	HIS	0	0.027	0.003	19.657	0.020	0.020	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.008	-0.003	21.299	-0.016	-0.016	0.000	0.000	0.000	0.000
77	A	77	HIS	1	0.856	0.927	22.891	0.095	0.095	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.007	0.009	26.176	0.005	0.005	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.035	-0.020	27.338	0.005	0.005	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.011	0.018	26.344	0.006	0.006	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.880	-0.942	26.168	-0.067	-0.067	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.013	0.014	22.697	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	83	GLN	0	0.005	0.002	25.679	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	84	PRO	0	-0.032	0.001	27.630	0.002	0.002	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.010	-0.041	29.074	0.010	0.010	0.000	0.000	0.000	0.000
86	A	86	ASN	0	0.035	-0.015	31.748	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.034	0.032	32.291	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.710	-0.842	27.719	-0.113	-0.113	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.882	0.962	28.183	0.079	0.079	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.015	0.008	30.401	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.018	0.002	26.814	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.020	0.002	24.983	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.023	-0.017	26.940	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.084	-0.026	29.020	0.003	0.003	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.024	0.002	24.161	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.899	0.957	24.357	0.152	0.152	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.936	0.959	25.587	0.115	0.115	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.038	-0.012	26.639	0.005	0.005	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.054	0.020	23.312	0.000	0.000	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.902	-0.971	24.028	-0.189	-0.189	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.079	-0.033	25.888	0.005	0.005	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.057	-0.034	24.539	0.008	0.008	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.042	-0.009	23.320	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.023	0.010	18.090	-0.018	-0.018	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.809	-0.894	18.711	-0.309	-0.309	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.011	0.002	18.702	-0.034	-0.034	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.008	-0.004	13.864	0.011	0.011	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.767	-0.867	17.591	-0.268	-0.268	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.056	-0.020	19.060	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	110	VAL	0	0.009	0.009	17.160	0.013	0.013	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.036	-0.001	20.231	0.003	0.003	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.007	-0.008	17.129	0.002	0.002	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.060	0.018	20.522	0.005	0.005	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.004	-0.013	20.733	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.050	-0.029	19.791	0.027	0.027	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.871	-0.924	20.247	-0.057	-0.057	0.000	0.000	0.000	0.000
117	A	117	TRP	0	-0.047	-0.042	17.681	-0.032	-0.032	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.045	0.037	20.554	0.004	0.004	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.037	-0.043	20.010	-0.015	-0.015	0.000	0.000	0.000	0.000
120	A	120	PHE	0	0.062	-0.001	21.912	0.023	0.023	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.765	0.869	19.562	0.306	0.306	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.861	-0.939	20.195	-0.232	-0.232	0.000	0.000	0.000	0.000
123	A	123	HIS	0	-0.059	-0.026	23.002	0.030	0.030	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.003	0.004	25.785	0.013	0.013	0.000	0.000	0.000	0.000
125	A	125	LEU	0	-0.023	-0.020	27.294	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.074	-0.013	22.351	0.006	0.006	0.000	0.000	0.000	0.000

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