FMO DATABASE

FMODB ID: KG9Q3

Calculation Name: 2QZJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QZJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q180B0

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	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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1067734.340403
FMO2-HF: Nuclear repulsion	1019152.41069
FMO2-HF: Total energy	-48581.929714
FMO2-MP2: Total energy	-48721.865407

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:4:GLN)

Summations of interaction energy for fragment #1(A:4:GLN)

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.
-32.373	-26.688	11.168	-7.599	-9.254	-0.047

Interaction energy analysis for fragmet #1(A:4:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : -0.026

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	6	LYS	1	0.873	0.936	2.520	-6.975	-3.690	1.098	-1.983	-2.400	-0.013
4	A	7	ILE	0	-0.015	-0.007	5.097	0.163	0.227	-0.001	-0.005	-0.059	0.000
5	A	8	LEU	0	-0.010	0.009	8.336	0.371	0.371	0.000	0.000	0.000	0.000
6	A	9	ILE	0	-0.012	-0.011	11.680	-0.120	-0.120	0.000	0.000	0.000	0.000
7	A	10	ILE	0	0.007	0.002	14.487	0.118	0.118	0.000	0.000	0.000	0.000
8	A	11	ASP	-1	-0.738	-0.877	18.048	-0.441	-0.441	0.000	0.000	0.000	0.000
9	A	12	GLY	0	0.060	0.039	20.348	0.027	0.027	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.865	-0.931	21.900	-0.344	-0.344	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.897	0.942	19.288	0.043	0.043	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.831	-0.890	18.550	-0.389	-0.389	0.000	0.000	0.000	0.000
13	A	16	ASN	0	-0.067	-0.049	18.735	-0.108	-0.108	0.000	0.000	0.000	0.000
14	A	17	CYS	0	-0.042	-0.015	15.759	-0.091	-0.091	0.000	0.000	0.000	0.000
15	A	18	GLN	0	0.015	0.005	13.693	-0.160	-0.160	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.805	0.891	13.836	0.410	0.410	0.000	0.000	0.000	0.000
17	A	20	LEU	0	0.009	0.004	12.701	-0.155	-0.155	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.836	0.905	8.021	0.115	0.115	0.000	0.000	0.000	0.000
19	A	22	GLY	0	0.042	0.025	9.251	-0.396	-0.396	0.000	0.000	0.000	0.000
20	A	23	PHE	0	-0.031	-0.010	10.072	-0.301	-0.301	0.000	0.000	0.000	0.000
21	A	24	LEU	0	-0.008	-0.017	7.884	-0.212	-0.212	0.000	0.000	0.000	0.000
22	A	25	GLU	-1	-0.848	-0.910	5.019	-2.085	-2.085	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.905	-0.934	5.719	-2.763	-2.763	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.758	0.881	7.540	1.735	1.735	0.000	0.000	0.000	0.000
25	A	28	GLY	0	0.013	0.013	3.722	0.206	0.706	0.001	-0.259	-0.242	-0.001
26	A	29	ILE	0	-0.068	-0.031	1.860	-18.017	-18.974	8.452	-3.800	-3.694	-0.049
27	A	30	SER	0	-0.001	0.008	2.572	-1.808	0.741	1.593	-1.461	-2.681	0.015
28	A	31	ILE	0	0.001	-0.001	4.045	-0.772	-0.528	0.025	-0.091	-0.178	0.001
29	A	32	ASP	-1	-0.785	-0.864	7.634	1.211	1.211	0.000	0.000	0.000	0.000
30	A	33	LEU	0	-0.021	-0.018	10.643	-0.268	-0.268	0.000	0.000	0.000	0.000
31	A	34	ALA	0	-0.003	-0.002	14.011	0.142	0.142	0.000	0.000	0.000	0.000
32	A	35	TYR	0	0.019	-0.011	16.632	-0.039	-0.039	0.000	0.000	0.000	0.000
33	A	36	ASN	0	-0.037	-0.023	20.731	0.010	0.010	0.000	0.000	0.000	0.000
34	A	37	CYS	0	0.010	-0.011	21.701	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.958	-0.964	22.591	0.054	0.054	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.800	-0.899	18.968	0.020	0.020	0.000	0.000	0.000	0.000
37	A	40	ALA	0	-0.018	-0.005	17.978	0.034	0.034	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.015	-0.013	18.236	0.001	0.001	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.020	0.020	19.442	0.022	0.022	0.000	0.000	0.000	0.000
40	A	43	LYS	1	0.844	0.927	13.190	-0.171	-0.171	0.000	0.000	0.000	0.000
41	A	44	ILE	0	0.018	-0.002	14.741	0.050	0.050	0.000	0.000	0.000	0.000
42	A	45	PHE	0	-0.042	-0.030	16.296	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	46	SER	0	-0.053	-0.021	15.092	0.043	0.043	0.000	0.000	0.000	0.000
44	A	47	ASN	0	-0.078	-0.037	10.527	0.463	0.463	0.000	0.000	0.000	0.000
45	A	48	LYS	1	0.921	0.956	9.600	-0.049	-0.049	0.000	0.000	0.000	0.000
46	A	49	TYR	0	-0.013	-0.035	8.758	0.066	0.066	0.000	0.000	0.000	0.000
47	A	50	ASP	-1	-0.818	-0.908	6.556	-3.703	-3.703	0.000	0.000	0.000	0.000
48	A	51	LEU	0	-0.066	-0.045	9.644	0.165	0.165	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.002	0.000	10.993	-0.048	-0.048	0.000	0.000	0.000	0.000
50	A	53	PHE	0	0.004	-0.009	11.888	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	54	LEU	0	-0.023	-0.008	15.895	0.070	0.070	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.734	-0.820	19.456	-0.354	-0.354	0.000	0.000	0.000	0.000
53	A	56	ILE	0	-0.013	-0.024	22.602	0.019	0.019	0.000	0.000	0.000	0.000
54	A	57	ILE	0	-0.010	0.002	25.948	0.028	0.028	0.000	0.000	0.000	0.000
55	A	58	LEU	0	0.006	0.002	22.514	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	59	SER	0	-0.012	-0.018	26.467	0.009	0.009	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.789	-0.882	26.351	-0.083	-0.083	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.016	0.002	28.368	0.012	0.012	0.000	0.000	0.000	0.000
59	A	62	ASP	-1	-0.788	-0.860	27.758	-0.194	-0.194	0.000	0.000	0.000	0.000
60	A	63	GLY	0	0.040	0.007	24.215	0.003	0.003	0.000	0.000	0.000	0.000
61	A	64	TRP	0	0.003	-0.001	24.568	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	65	THR	0	-0.086	-0.080	27.073	0.003	0.003	0.000	0.000	0.000	0.000
63	A	66	LEU	0	-0.021	-0.012	21.265	0.011	0.011	0.000	0.000	0.000	0.000
64	A	67	CYS	0	-0.028	-0.008	21.965	-0.012	-0.012	0.000	0.000	0.000	0.000
65	A	68	LYS	1	0.901	0.962	22.962	0.206	0.206	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.927	0.967	24.443	0.071	0.071	0.000	0.000	0.000	0.000
67	A	70	ILE	0	0.012	0.004	18.186	0.026	0.026	0.000	0.000	0.000	0.000
68	A	71	ARG	1	0.798	0.880	18.127	0.468	0.468	0.000	0.000	0.000	0.000
69	A	72	ASN	0	-0.073	-0.023	22.418	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	73	VAL	0	-0.057	-0.021	18.392	0.036	0.036	0.000	0.000	0.000	0.000
71	A	74	THR	0	-0.029	-0.019	14.883	-0.021	-0.021	0.000	0.000	0.000	0.000
72	A	75	THR	0	0.025	0.012	17.631	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	76	CYS	0	-0.054	0.003	12.269	-0.038	-0.038	0.000	0.000	0.000	0.000
74	A	77	PRO	0	0.051	0.029	13.886	0.078	0.078	0.000	0.000	0.000	0.000
75	A	78	ILE	0	-0.002	-0.003	15.217	-0.061	-0.061	0.000	0.000	0.000	0.000
76	A	79	VAL	0	-0.027	-0.010	16.497	0.039	0.039	0.000	0.000	0.000	0.000
77	A	80	TYR	0	0.029	-0.007	18.309	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	81	MET	0	-0.052	-0.017	17.684	-0.089	-0.089	0.000	0.000	0.000	0.000
79	A	82	THR	0	0.008	-0.010	21.333	0.038	0.038	0.000	0.000	0.000	0.000
80	A	83	TYR	0	0.012	0.001	25.024	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.011	0.020	28.200	0.015	0.015	0.000	0.000	0.000	0.000
82	A	85	ASN	0	-0.007	-0.004	28.872	-0.049	-0.049	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.803	-0.909	31.155	-0.225	-0.225	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.897	-0.948	32.427	-0.249	-0.249	0.000	0.000	0.000	0.000
85	A	88	GLN	0	0.006	-0.012	32.712	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.004	-0.001	29.145	0.007	0.007	0.000	0.000	0.000	0.000
87	A	90	ILE	0	0.019	0.008	27.504	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	91	LEU	0	0.016	0.007	28.430	-0.013	-0.013	0.000	0.000	0.000	0.000
89	A	92	ASN	0	0.044	0.025	30.117	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	93	ALA	0	-0.018	0.018	25.238	0.000	0.000	0.000	0.000	0.000	0.000
91	A	94	LEU	0	0.014	0.006	24.155	-0.013	-0.013	0.000	0.000	0.000	0.000
92	A	95	ASN	0	-0.043	-0.039	26.309	0.008	0.008	0.000	0.000	0.000	0.000
93	A	96	SER	0	-0.104	-0.062	25.897	0.027	0.027	0.000	0.000	0.000	0.000
94	A	97	GLY	0	-0.001	0.004	24.288	0.009	0.009	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.016	0.021	21.365	-0.032	-0.032	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.848	-0.924	18.958	-0.584	-0.584	0.000	0.000	0.000	0.000
97	A	100	ASP	-1	-0.804	-0.897	19.581	-0.636	-0.636	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.039	-0.038	21.454	0.018	0.018	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.051	-0.019	18.276	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	103	ILE	0	0.027	0.016	22.480	0.013	0.013	0.000	0.000	0.000	0.000
101	A	104	LYS	1	0.718	0.847	21.657	0.368	0.368	0.000	0.000	0.000	0.000
102	A	105	PRO	0	-0.008	-0.011	23.738	0.033	0.033	0.000	0.000	0.000	0.000
103	A	106	LEU	0	0.035	0.008	18.218	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	107	ASN	0	0.013	0.007	20.395	-0.081	-0.081	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.062	0.024	15.387	-0.030	-0.030	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.794	-0.913	15.547	-1.386	-1.386	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.032	-0.014	17.319	-0.044	-0.044	0.000	0.000	0.000	0.000
108	A	111	LEU	0	0.005	0.016	13.835	-0.025	-0.025	0.000	0.000	0.000	0.000
109	A	112	TYR	0	0.092	0.028	9.564	0.102	0.102	0.000	0.000	0.000	0.000
110	A	113	ALA	0	-0.058	-0.033	14.018	-0.108	-0.108	0.000	0.000	0.000	0.000
111	A	114	LYS	1	0.832	0.895	16.361	0.654	0.654	0.000	0.000	0.000	0.000
112	A	115	VAL	0	0.021	0.021	9.898	0.008	0.008	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.877	0.954	11.955	1.391	1.391	0.000	0.000	0.000	0.000
114	A	117	ALA	0	-0.059	-0.026	13.053	0.070	0.070	0.000	0.000	0.000	0.000
115	A	118	ILE	0	0.011	0.004	13.290	0.088	0.088	0.000	0.000	0.000	0.000
116	A	119	LEU	0	0.036	0.020	7.919	0.089	0.089	0.000	0.000	0.000	0.000
117	A	120	ARG	1	0.971	0.991	11.302	0.928	0.928	0.000	0.000	0.000	0.000
118	A	121	ARG	1	0.929	0.958	13.292	0.659	0.659	0.000	0.000	0.000	0.000
119	A	122	MET	0	-0.007	0.009	11.536	0.151	0.151	0.000	0.000	0.000	0.000
120	A	123	ASN	0	-0.033	-0.006	8.703	0.074	0.074	0.000	0.000	0.000	0.000
121	A	124	SER	0	-0.091	-0.045	12.013	0.205	0.205	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:GLN)