FMO DATABASE

FMODB ID: N1Q6Q

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1131719.690503
FMO2-HF: Nuclear repulsion	1082472.899479
FMO2-HF: Total energy	-49246.791024
FMO2-MP2: Total energy	-49393.358118

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.
-1.687	1.505	4.098	-2.588	-4.702	-0.009

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 : 0.007 / q_NPA : -0.003

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	0.045	0.024	2.656	-2.390	1.679	0.326	-1.703	-2.692	0.003
4	A	4	LYS	1	0.908	0.982	4.504	1.344	1.634	-0.001	-0.022	-0.267	0.000
5	A	5	VAL	0	0.019	0.004	5.974	0.223	0.223	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.821	0.906	6.667	1.662	1.662	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.052	0.023	11.775	0.100	0.100	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.070	0.034	13.804	-0.069	-0.069	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.980	0.995	11.590	0.106	0.106	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.792	-0.894	9.499	-0.669	-0.669	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.009	-0.004	10.370	-0.053	-0.053	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.010	0.006	12.832	0.028	0.028	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.876	-0.929	9.639	0.180	0.180	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.049	-0.028	7.636	0.029	0.029	0.000	0.000	0.000	0.000
15	A	15	MET	0	-0.003	0.005	9.798	0.017	0.017	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.884	0.949	12.152	-0.092	-0.092	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.004	0.002	12.581	0.019	0.019	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.830	0.903	8.530	0.325	0.325	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.022	0.000	15.510	-0.028	-0.028	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.014	-0.004	19.052	0.020	0.020	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.761	-0.858	21.427	-0.025	-0.025	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.920	-0.963	19.939	-0.032	-0.032	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.065	-0.051	23.988	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.800	0.889	26.407	0.045	0.045	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.892	-0.947	25.632	-0.085	-0.085	0.000	0.000	0.000	0.000
26	A	26	HIS	0	0.006	0.003	22.460	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.037	-0.014	22.356	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.017	-0.002	17.793	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.002	0.006	17.453	0.004	0.004	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.012	-0.013	11.936	-0.028	-0.028	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.004	-0.008	12.944	0.040	0.040	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.008	0.000	10.229	-0.176	-0.176	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.071	0.038	7.633	0.152	0.152	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.032	0.004	10.600	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.867	0.934	8.133	0.437	0.437	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.008	-0.004	8.993	-0.054	-0.054	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.044	-0.023	2.297	-2.414	-3.581	3.773	-0.863	-1.743	-0.012
38	A	38	ILE	0	0.038	0.009	6.205	0.356	0.356	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.050	-0.014	6.964	-0.270	-0.270	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.792	0.868	9.087	0.441	0.441	0.000	0.000	0.000	0.000
41	A	41	HIS	0	0.043	0.023	11.581	-0.082	-0.082	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.864	-0.922	14.417	-0.249	-0.249	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.002	-0.002	18.138	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.038	-0.021	21.100	0.010	0.010	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.021	-0.013	23.711	0.012	0.012	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.017	0.011	24.600	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	47	GLY	0	-0.027	-0.013	27.155	0.007	0.007	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.001	0.023	29.296	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.028	0.014	27.784	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.023	0.006	30.795	0.004	0.004	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.043	-0.005	31.589	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.039	-0.010	32.296	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.006	-0.002	30.520	0.000	0.000	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.008	0.014	26.998	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.921	0.962	28.406	0.121	0.121	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.050	0.015	26.725	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.964	0.977	26.296	0.099	0.099	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.953	-0.972	26.066	-0.138	-0.138	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.049	0.021	21.231	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.056	0.015	21.391	-0.022	-0.022	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.936	0.994	22.460	0.159	0.159	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.015	-0.008	19.245	0.000	0.000	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.058	0.036	17.688	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.002	-0.006	17.934	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.871	0.945	19.009	0.260	0.260	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.835	-0.893	14.263	-0.428	-0.428	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.064	-0.026	14.471	-0.038	-0.038	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.029	-0.016	13.957	-0.042	-0.042	0.000	0.000	0.000	0.000
69	A	69	HIS	0	-0.003	-0.005	13.935	0.055	0.055	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.004	0.002	14.807	0.028	0.028	0.000	0.000	0.000	0.000
71	A	71	ILE	0	0.009	0.007	15.169	-0.052	-0.052	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.020	-0.010	13.344	0.016	0.016	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.016	0.011	16.756	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.017	0.003	16.175	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	75	HIS	0	0.047	0.021	19.514	0.016	0.016	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.015	0.008	21.074	-0.011	-0.011	0.000	0.000	0.000	0.000
77	A	77	HIS	1	0.806	0.882	22.714	0.096	0.096	0.000	0.000	0.000	0.000
78	A	78	PRO	0	0.001	0.011	25.643	0.005	0.005	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.055	-0.030	27.131	0.006	0.006	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.012	0.014	26.892	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.882	-0.938	26.565	-0.052	-0.052	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.032	0.009	22.871	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	83	GLN	0	0.041	0.015	25.906	-0.017	-0.017	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.000	0.012	27.773	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.007	0.013	29.233	0.008	0.008	0.000	0.000	0.000	0.000
86	A	86	ASN	0	0.009	-0.030	31.630	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.049	0.042	32.371	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.720	-0.887	27.594	-0.117	-0.117	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.911	0.955	28.345	0.074	0.074	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.016	0.003	30.331	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.027	0.009	26.781	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.011	0.003	25.111	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.055	-0.023	27.003	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.044	-0.029	28.584	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.025	0.002	23.638	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.912	0.956	24.859	0.138	0.138	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.951	0.968	25.911	0.114	0.114	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.013	0.003	26.850	0.005	0.005	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.039	0.015	23.626	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.916	-0.958	24.317	-0.180	-0.180	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.117	-0.047	26.384	0.005	0.005	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.055	-0.046	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	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.025	0.001	18.333	-0.016	-0.016	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.910	-0.963	19.458	-0.275	-0.275	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.014	-0.012	19.068	-0.032	-0.032	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.012	0.008	14.582	0.013	0.013	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.773	-0.885	17.926	-0.241	-0.241	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.048	-0.031	19.383	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	110	VAL	0	-0.012	-0.006	17.298	0.014	0.014	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.028	0.002	20.279	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.007	-0.010	17.221	0.003	0.003	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.071	0.023	20.563	0.002	0.002	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.004	-0.003	20.777	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.031	-0.022	20.121	0.020	0.020	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.891	-0.949	20.553	-0.046	-0.046	0.000	0.000	0.000	0.000
117	A	117	TRP	0	-0.026	-0.025	17.718	-0.032	-0.032	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.028	0.028	20.716	0.005	0.005	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.025	-0.031	20.032	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	120	PHE	0	0.044	-0.010	22.057	0.020	0.020	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.852	0.933	19.722	0.267	0.267	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.892	-0.949	20.786	-0.192	-0.192	0.000	0.000	0.000	0.000
123	A	123	HIS	0	-0.074	-0.029	23.802	0.027	0.027	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.030	-0.013	26.611	0.008	0.008	0.000	0.000	0.000	0.000
125	A	125	LEU	0	0.005	0.006	26.991	0.007	0.007	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.020	0.016	21.807	0.015	0.015	0.000	0.000	0.000	0.000

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