FMO DATABASE

FMODB ID: 4JKMN

Calculation Name: 2QTP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QTP

Chain ID: A

ChEMBL ID:

UniProt ID: Q5LV76

Base Structure: X-ray

Registration Date: 2023-09-23

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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1263753.779429
FMO2-HF: Nuclear repulsion	1208280.146241
FMO2-HF: Total energy	-55473.633188
FMO2-MP2: Total energy	-55634.660829

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-219.721	-224.658	34.908	-16.612	-13.362	-0.179

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.808 / q_NPA : 0.870

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

Sort

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	5	ARG	1	0.709	0.823	3.878	29.470	30.816	-0.016	-0.594	-0.736	0.000
4	A	6	LYS	1	0.861	0.899	5.840	23.056	23.056	0.000	0.000	0.000	0.000
5	A	7	ILE	0	-0.004	-0.001	8.583	-0.834	-0.834	0.000	0.000	0.000	0.000
6	A	8	ALA	0	-0.044	-0.008	11.157	0.653	0.653	0.000	0.000	0.000	0.000
7	A	9	VAL	0	-0.004	-0.011	14.804	-0.232	-0.232	0.000	0.000	0.000	0.000
8	A	10	PHE	0	-0.028	-0.007	16.902	0.187	0.187	0.000	0.000	0.000	0.000
9	A	11	ILE	0	0.018	-0.001	21.068	-0.052	-0.052	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.950	-0.963	24.169	-10.115	-10.115	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.849	-0.914	27.491	-8.783	-8.783	0.000	0.000	0.000	0.000
12	A	14	THR	0	0.008	0.008	30.841	0.058	0.058	0.000	0.000	0.000	0.000
13	A	15	ARG	1	0.867	0.906	33.823	8.374	8.374	0.000	0.000	0.000	0.000
14	A	16	ILE	0	-0.016	0.005	37.138	0.226	0.226	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.885	-0.947	35.387	-8.289	-8.289	0.000	0.000	0.000	0.000
16	A	18	DAL	0	-0.027	-0.014	39.203	0.172	0.172	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.025	-0.003	41.995	0.161	0.161	0.000	0.000	0.000	0.000
18	A	20	ARG	1	0.923	0.958	40.345	7.195	7.195	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.932	-0.973	41.535	-6.787	-6.787	0.000	0.000	0.000	0.000
20	A	22	ILE	0	-0.099	-0.041	36.492	0.129	0.129	0.000	0.000	0.000	0.000
21	A	23	SER	0	-0.031	0.002	38.546	-0.161	-0.161	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.012	-0.015	35.842	0.184	0.184	0.000	0.000	0.000	0.000
23	A	25	PRO	0	0.017	-0.007	33.746	0.017	0.017	0.000	0.000	0.000	0.000
24	A	26	THR	0	0.042	0.043	32.422	-0.095	-0.095	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.793	0.877	28.128	9.328	9.328	0.000	0.000	0.000	0.000
26	A	28	LYS	1	0.855	0.934	25.302	9.895	9.895	0.000	0.000	0.000	0.000
27	A	29	ALA	0	0.003	-0.003	21.404	-0.052	-0.052	0.000	0.000	0.000	0.000
28	A	30	VAL	0	0.006	-0.001	17.671	-0.097	-0.097	0.000	0.000	0.000	0.000
29	A	31	ALA	0	-0.012	0.007	14.542	-0.081	-0.081	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.004	-0.014	12.631	-0.238	-0.238	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.010	0.008	7.458	-0.100	-0.100	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.026	-0.009	7.645	0.448	0.448	0.000	0.000	0.000	0.000
33	A	35	ILE	0	0.025	0.006	3.340	-2.652	-2.097	0.011	-0.155	-0.412	0.000
34	A	36	GLU	-1	-0.839	-0.890	1.733	-154.087	-161.415	34.912	-15.754	-11.831	-0.178
35	A	37	ASN	0	-0.001	-0.020	3.892	-0.551	-0.126	0.002	-0.107	-0.321	-0.001
36	A	38	PRO	0	0.045	0.033	5.387	-2.618	-2.618	0.000	0.000	0.000	0.000
37	A	39	PHE	0	-0.014	-0.024	6.450	2.063	2.063	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.011	0.006	8.177	3.144	3.144	0.000	0.000	0.000	0.000
39	A	41	GLY	0	-0.044	-0.025	9.861	-1.239	-1.239	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.854	0.941	7.269	34.372	34.372	0.000	0.000	0.000	0.000
41	A	43	TYR	0	0.009	0.016	13.495	0.157	0.157	0.000	0.000	0.000	0.000
42	A	44	VAL	0	-0.045	-0.027	13.168	0.228	0.228	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.893	-0.947	16.215	-14.600	-14.600	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.888	-0.913	16.645	-18.026	-18.026	0.000	0.000	0.000	0.000
45	A	47	LEU	0	-0.032	-0.032	13.854	-1.598	-1.598	0.000	0.000	0.000	0.000
46	A	48	THR	0	0.020	-0.020	13.163	-0.445	-0.445	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.905	-0.947	6.862	-38.024	-38.024	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.032	-0.015	7.824	-1.459	-1.459	0.000	0.000	0.000	0.000
49	A	51	MET	0	-0.039	-0.009	9.872	0.845	0.845	0.000	0.000	0.000	0.000
50	A	52	ASP	-1	-0.900	-0.949	10.231	-19.339	-19.339	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.028	-0.035	4.729	-1.120	-1.055	-0.001	-0.002	-0.062	0.000
52	A	54	GLY	0	0.017	-0.003	7.397	0.508	0.508	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.041	-0.017	10.002	1.188	1.188	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.954	-0.965	7.226	-22.559	-22.559	0.000	0.000	0.000	0.000
55	A	57	LEU	0	-0.020	-0.018	5.781	0.688	0.688	0.000	0.000	0.000	0.000
56	A	58	GLY	0	0.021	0.011	9.181	0.936	0.936	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.011	-0.001	12.703	0.928	0.928	0.000	0.000	0.000	0.000
58	A	60	LEU	0	0.000	0.006	8.431	0.619	0.619	0.000	0.000	0.000	0.000
59	A	61	LEU	0	-0.022	-0.032	10.612	0.603	0.603	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.033	0.011	13.399	0.726	0.726	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.843	-0.910	15.470	-12.013	-12.013	0.000	0.000	0.000	0.000
62	A	64	ARG	1	0.861	0.925	13.602	15.802	15.802	0.000	0.000	0.000	0.000
63	A	65	CYS	0	-0.048	-0.011	16.734	0.463	0.463	0.000	0.000	0.000	0.000
64	A	66	VAL	0	0.023	0.015	19.313	0.460	0.460	0.000	0.000	0.000	0.000
65	A	67	GLN	0	-0.059	-0.042	17.554	0.080	0.080	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.057	-0.024	20.295	0.322	0.322	0.000	0.000	0.000	0.000
67	A	69	LEU	0	0.000	0.002	22.144	0.342	0.342	0.000	0.000	0.000	0.000
68	A	70	GLY	0	-0.013	0.011	24.467	0.432	0.432	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.073	-0.022	25.286	0.391	0.391	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.838	0.896	25.173	8.458	8.458	0.000	0.000	0.000	0.000
71	A	73	PRO	0	0.055	0.003	22.560	0.087	0.087	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.816	-0.899	24.850	-9.224	-9.224	0.000	0.000	0.000	0.000
73	A	75	GLN	0	-0.043	-0.028	28.167	0.165	0.165	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.026	0.011	25.167	0.071	0.071	0.000	0.000	0.000	0.000
75	A	77	GLU	-1	-0.842	-0.872	27.228	-8.484	-8.484	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.030	-0.011	26.806	0.135	0.135	0.000	0.000	0.000	0.000
77	A	79	TYR	0	-0.025	-0.020	21.726	-0.275	-0.275	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.029	0.011	21.126	0.373	0.373	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.822	0.927	16.060	14.536	14.536	0.000	0.000	0.000	0.000
80	A	82	SER	0	0.036	0.015	16.430	0.686	0.686	0.000	0.000	0.000	0.000
81	A	83	ALA	0	-0.015	0.008	12.966	-0.844	-0.844	0.000	0.000	0.000	0.000
82	A	84	MET	0	-0.022	0.008	13.593	0.785	0.785	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.031	-0.024	11.847	-1.875	-1.875	0.000	0.000	0.000	0.000
84	A	86	GLY	0	0.018	0.012	11.688	1.384	1.384	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.862	-0.962	13.226	-17.119	-17.119	0.000	0.000	0.000	0.000
86	A	88	ASN	0	-0.089	-0.039	12.275	1.785	1.785	0.000	0.000	0.000	0.000
87	A	89	GLY	0	-0.004	-0.002	12.950	-1.191	-1.191	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.850	-0.925	13.663	-15.973	-15.973	0.000	0.000	0.000	0.000
89	A	91	LEU	0	0.038	0.003	15.126	-0.736	-0.736	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.851	-0.952	16.933	-15.256	-15.256	0.000	0.000	0.000	0.000
91	A	93	HIS	0	0.080	0.053	11.580	-1.200	-1.200	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.015	0.012	12.722	-0.686	-0.686	0.000	0.000	0.000	0.000
93	A	95	ALA	0	-0.032	-0.029	14.259	0.412	0.412	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.005	0.010	13.505	0.462	0.462	0.000	0.000	0.000	0.000
95	A	97	ILE	0	0.002	0.005	7.718	0.301	0.301	0.000	0.000	0.000	0.000
96	A	98	LEU	0	-0.050	-0.035	11.967	0.483	0.483	0.000	0.000	0.000	0.000
97	A	99	HIS	0	-0.005	0.013	15.069	1.119	1.119	0.000	0.000	0.000	0.000
98	A	100	PRO	0	0.001	0.027	13.376	1.006	1.006	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.943	0.964	16.601	11.965	11.965	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.011	0.004	15.868	0.057	0.057	0.000	0.000	0.000	0.000
101	A	116	LEU	0	0.010	0.006	23.717	0.077	0.077	0.000	0.000	0.000	0.000
102	A	117	VAL	0	-0.053	-0.031	20.843	0.162	0.162	0.000	0.000	0.000	0.000
103	A	118	PRO	0	-0.001	0.031	23.118	-0.260	-0.260	0.000	0.000	0.000	0.000
104	A	119	SER	0	0.005	-0.021	19.080	-0.581	-0.581	0.000	0.000	0.000	0.000
105	A	120	SER	0	-0.047	-0.022	19.832	0.467	0.467	0.000	0.000	0.000	0.000
106	A	121	LYS	1	0.921	0.965	17.747	13.929	13.929	0.000	0.000	0.000	0.000
107	A	122	LYS	1	0.878	0.939	17.490	14.176	14.176	0.000	0.000	0.000	0.000
108	A	123	MET	0	0.070	0.059	15.788	-0.862	-0.862	0.000	0.000	0.000	0.000
109	A	124	GLY	0	-0.026	-0.027	16.611	0.951	0.951	0.000	0.000	0.000	0.000
110	A	125	SER	0	0.016	0.006	16.242	-0.918	-0.918	0.000	0.000	0.000	0.000
111	A	126	PRO	0	-0.030	-0.035	14.339	0.243	0.243	0.000	0.000	0.000	0.000
112	A	127	GLY	0	-0.027	0.005	16.465	0.941	0.941	0.000	0.000	0.000	0.000
113	A	128	GLN	0	0.043	0.036	18.633	0.655	0.655	0.000	0.000	0.000	0.000
114	A	129	VAL	0	-0.008	-0.010	18.847	-0.690	-0.690	0.000	0.000	0.000	0.000
115	A	130	LEU	0	-0.054	-0.016	15.909	0.102	0.102	0.000	0.000	0.000	0.000
116	A	131	ASP	-1	-0.887	-0.949	19.891	-11.389	-11.389	0.000	0.000	0.000	0.000
117	A	132	VAL	0	-0.051	-0.033	18.801	-0.462	-0.462	0.000	0.000	0.000	0.000
118	A	133	PRO	0	0.026	0.026	21.166	0.458	0.458	0.000	0.000	0.000	0.000
119	A	134	LEU	0	0.014	0.004	23.165	-0.325	-0.325	0.000	0.000	0.000	0.000
120	A	135	GLY	0	-0.030	-0.022	25.640	0.370	0.370	0.000	0.000	0.000	0.000
121	A	136	HIS	0	0.005	0.006	27.350	0.045	0.045	0.000	0.000	0.000	0.000
122	A	146	PHE	0	-0.082	-0.058	27.996	0.073	0.073	0.000	0.000	0.000	0.000
123	A	147	ASP	-1	-0.776	-0.858	29.421	-9.621	-9.621	0.000	0.000	0.000	0.000
124	A	148	GLY	0	0.031	-0.015	25.753	-0.274	-0.274	0.000	0.000	0.000	0.000
125	A	149	ILE	0	0.008	0.009	21.936	0.249	0.249	0.000	0.000	0.000	0.000
126	A	150	GLU	-1	-0.897	-0.934	22.776	-11.645	-11.645	0.000	0.000	0.000	0.000
127	A	151	VAL	0	-0.011	-0.001	17.499	-0.111	-0.111	0.000	0.000	0.000	0.000
128	A	152	ARG	1	0.892	0.937	18.099	13.432	13.432	0.000	0.000	0.000	0.000
129	A	153	LEU	0	0.054	0.018	13.190	0.006	0.006	0.000	0.000	0.000	0.000
130	A	154	ASN	0	-0.049	-0.033	16.840	-0.451	-0.451	0.000	0.000	0.000	0.000
131	A	155	ASP	-1	-0.798	-0.869	12.852	-20.954	-20.954	0.000	0.000	0.000	0.000
132	A	156	ALA	0	-0.018	0.021	11.512	-1.956	-1.956	0.000	0.000	0.000	0.000
133	A	157	PRO	0	0.049	0.029	11.218	1.288	1.288	0.000	0.000	0.000	0.000
134	A	158	ARG	1	0.926	0.928	7.705	32.795	32.795	0.000	0.000	0.000	0.000
135	A	159	ALA	0	0.027	0.010	11.240	-0.824	-0.824	0.000	0.000	0.000	0.000
136	A	160	ASN	0	0.009	-0.003	5.877	5.095	5.095	0.000	0.000	0.000	0.000
137	A	161	GLU	-1	-0.751	-0.831	6.347	-37.934	-37.934	0.000	0.000	0.000	0.000
138	A	162	ILE	0	0.039	0.017	7.297	3.057	3.057	0.000	0.000	0.000	0.000
139	A	163	MET	0	-0.042	-0.006	8.254	-1.869	-1.869	0.000	0.000	0.000	0.000
140	A	164	VAL	0	0.013	0.002	9.531	1.532	1.532	0.000	0.000	0.000	0.000
141	A	165	ALA	0	0.016	0.002	11.798	-0.094	-0.094	0.000	0.000	0.000	0.000
142	A	166	VAL	0	-0.005	-0.004	14.052	0.276	0.276	0.000	0.000	0.000	0.000
143	A	167	ALA	0	0.029	0.010	16.564	-0.044	-0.044	0.000	0.000	0.000	0.000
144	A	168	VAL	0	-0.015	-0.016	20.143	0.071	0.071	0.000	0.000	0.000	0.000
145	A	169	THR	0	0.027	0.017	22.937	-0.098	-0.098	0.000	0.000	0.000	0.000
146	A	170	ASP	-1	-0.854	-0.928	26.552	-9.112	-9.112	0.000	0.000	0.000	0.000
147	A	171	SER	0	-0.037	-0.050	29.085	0.292	0.292	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)