FMO DATABASE

FMODB ID: V24M1

Calculation Name: 2QLC-A-Xray316

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: 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:

Apendix: None

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. 1.20200129

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. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1131479.03267
FMO2-HF: Nuclear repulsion	1082232.739477
FMO2-HF: Total energy	-49246.293193
FMO2-MP2: Total energy	-49392.850031

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.
-1.801	1.333	4.103	-2.57	-4.666	-0.011

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 : 0.005 / q_NPA : -0.004

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	0.046	0.025	2.656	-2.358	1.633	0.335	-1.666	-2.660	0.002
4	A	4	LYS	1	0.907	0.982	4.504	1.401	1.687	0.000	-0.023	-0.262	0.000
5	A	5	VAL	0	0.021	0.005	5.974	0.249	0.249	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.816	0.904	6.668	1.713	1.713	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.057	0.025	11.775	0.105	0.105	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.075	0.037	13.804	-0.070	-0.070	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.979	0.995	11.569	0.115	0.115	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.799	-0.898	9.499	-0.689	-0.689	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.003	-0.001	10.370	-0.052	-0.052	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.009	0.006	12.832	0.035	0.035	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.875	-0.929	9.639	0.192	0.192	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.051	-0.029	7.636	0.030	0.030	0.000	0.000	0.000	0.000
15	A	15	MET	0	-0.003	0.005	9.798	0.022	0.022	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.885	0.950	12.152	-0.091	-0.091	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.006	0.001	12.581	0.022	0.022	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.829	0.903	8.530	0.313	0.313	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.022	0.000	15.510	-0.029	-0.029	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.015	-0.005	19.052	0.022	0.022	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.761	-0.859	21.427	-0.021	-0.021	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.918	-0.962	19.939	-0.028	-0.028	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.066	-0.052	23.988	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.797	0.887	26.407	0.043	0.043	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.892	-0.947	25.632	-0.086	-0.086	0.000	0.000	0.000	0.000
26	A	26	HIS	0	0.007	0.003	22.460	-0.011	-0.011	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.032	-0.011	22.356	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.012	-0.004	17.793	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.001	0.008	17.453	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.014	-0.014	11.936	-0.032	-0.032	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.007	-0.006	12.944	0.038	0.038	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.011	0.002	10.229	-0.188	-0.188	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.070	0.037	7.638	0.156	0.156	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.032	0.005	10.600	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.864	0.932	8.133	0.467	0.467	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.013	-0.001	8.993	-0.067	-0.067	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.048	-0.025	2.297	-2.537	-3.680	3.768	-0.881	-1.744	-0.013
38	A	38	ILE	0	0.038	0.009	6.205	0.367	0.367	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.053	-0.014	6.964	-0.277	-0.277	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.792	0.867	9.087	0.459	0.459	0.000	0.000	0.000	0.000
41	A	41	HIS	0	0.039	0.023	11.581	-0.081	-0.081	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.862	-0.923	14.417	-0.250	-0.250	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.002	-0.002	18.138	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.035	-0.020	21.100	0.010	0.010	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.024	-0.014	23.711	0.013	0.013	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.018	0.012	24.600	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	47	GLY	0	-0.031	-0.016	27.155	0.008	0.008	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.000	0.022	29.296	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.026	0.015	27.784	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.021	0.005	30.795	0.004	0.004	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.049	-0.001	31.589	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.041	-0.011	32.296	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.005	-0.002	30.520	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.009	0.015	26.998	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.922	0.961	28.406	0.124	0.124	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.050	0.016	26.725	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.964	0.977	26.296	0.102	0.102	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.955	-0.975	26.066	-0.141	-0.141	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.051	0.022	21.231	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.060	0.017	21.391	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.934	0.992	22.460	0.164	0.164	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.019	-0.009	19.246	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.059	0.037	17.688	-0.025	-0.025	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.004	-0.003	17.934	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.865	0.942	19.010	0.266	0.266	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.841	-0.896	14.263	-0.441	-0.441	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.064	-0.026	14.471	-0.040	-0.040	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.031	-0.018	13.957	-0.045	-0.045	0.000	0.000	0.000	0.000
69	A	69	HIS	0	-0.003	-0.006	13.935	0.057	0.057	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.007	0.005	14.807	0.029	0.029	0.000	0.000	0.000	0.000
71	A	71	ILE	0	0.008	0.004	15.169	-0.054	-0.054	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.020	-0.008	13.344	0.014	0.014	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.012	0.012	16.756	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.010	0.002	16.175	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	75	HIS	0	0.047	0.020	19.514	0.018	0.018	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.018	0.010	21.074	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	77	HIS	1	0.811	0.885	22.714	0.098	0.098	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.008	0.006	25.643	0.006	0.006	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.072	-0.036	27.131	0.008	0.008	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.019	0.017	26.892	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.883	-0.940	26.565	-0.053	-0.053	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.030	0.010	22.870	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	83	GLN	0	0.038	0.016	25.906	-0.017	-0.017	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.006	0.015	27.773	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.000	0.009	29.233	0.008	0.008	0.000	0.000	0.000	0.000
86	A	86	ASN	0	0.008	-0.030	31.630	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.045	0.040	32.371	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.719	-0.888	27.594	-0.119	-0.119	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.919	0.960	28.345	0.076	0.076	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.020	0.002	30.331	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.021	0.005	26.781	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.017	0.008	25.111	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.038	-0.013	27.003	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.054	-0.034	28.584	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.013	-0.006	23.638	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.851	0.924	24.859	0.143	0.143	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.954	0.970	25.911	0.119	0.119	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.024	-0.004	26.850	0.005	0.005	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.038	0.014	23.626	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.906	-0.952	24.317	-0.188	-0.188	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.123	-0.050	26.384	0.006	0.006	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.064	-0.050	24.613	0.006	0.006	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.038	-0.002	23.166	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.035	-0.004	18.333	-0.018	-0.018	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.905	-0.962	19.458	-0.286	-0.286	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.013	-0.013	19.068	-0.035	-0.035	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.006	0.007	14.582	0.009	0.009	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.754	-0.873	17.926	-0.250	-0.250	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.044	-0.030	19.383	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	110	VAL	0	-0.015	-0.008	17.299	0.014	0.014	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.028	0.002	20.279	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.007	-0.011	17.221	0.004	0.004	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.075	0.024	20.563	0.003	0.003	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.010	-0.006	20.777	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.035	-0.023	20.121	0.022	0.022	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.893	-0.950	20.553	-0.047	-0.047	0.000	0.000	0.000	0.000
117	A	117	TRP	0	-0.026	-0.026	17.718	-0.033	-0.033	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.026	0.027	20.716	0.005	0.005	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.034	-0.038	20.035	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	120	PHE	0	0.040	-0.011	22.057	0.021	0.021	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.891	0.956	19.726	0.273	0.273	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.910	-0.960	20.786	-0.198	-0.198	0.000	0.000	0.000	0.000
123	A	123	HIS	0	-0.091	-0.039	23.802	0.029	0.029	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.043	-0.021	26.603	0.008	0.008	0.000	0.000	0.000	0.000
125	A	125	LEU	0	-0.032	-0.017	26.972	0.009	0.009	0.000	0.000	0.000	0.000
126	A	126	LEU	-1	-0.846	-0.891	21.815	-0.160	-0.160	0.000	0.000	0.000	0.000

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