FMO DATABASE

FMODB ID: LNRJ9

Calculation Name: 3ZQC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ZQC

Chain ID: A

ChEMBL ID:

UniProt ID: A2D9X4

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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-952639.517572
FMO2-HF: Nuclear repulsion	904621.283809
FMO2-HF: Total energy	-48018.233763
FMO2-MP2: Total energy	-48160.813782

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:52:MET)

Summations of interaction energy for fragment #1(A:52: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.
-13.644	-17.48	29.501	-13.273	-12.389	-0.056

Interaction energy analysis for fragmet #1(A:52:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.057 / q_NPA : 0.050

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	54	GLY	0	0.010	-0.001	2.574	-4.014	0.838	1.764	-2.924	-3.692	-0.003
4	A	55	PRO	0	0.014	-0.009	4.432	-1.315	-1.194	-0.001	-0.035	-0.085	0.000
5	A	56	PHE	0	0.024	0.012	4.435	-1.362	-1.251	-0.001	-0.011	-0.098	0.000
6	A	57	THR	0	-0.031	-0.012	5.221	0.528	0.528	0.000	0.000	0.000	0.000
7	A	58	GLU	-1	-0.756	-0.863	7.650	-0.878	-0.878	0.000	0.000	0.000	0.000
8	A	59	ALA	0	0.026	0.017	8.736	0.097	0.097	0.000	0.000	0.000	0.000
9	A	60	GLU	-1	-0.770	-0.866	3.907	-6.411	-6.074	0.004	-0.110	-0.230	-0.001
10	A	61	ASP	-1	-0.757	-0.858	8.431	-1.442	-1.442	0.000	0.000	0.000	0.000
11	A	62	ASP	-1	-0.802	-0.897	11.489	-0.597	-0.597	0.000	0.000	0.000	0.000
12	A	63	LEU	0	-0.044	-0.015	9.778	0.111	0.111	0.000	0.000	0.000	0.000
13	A	64	ILE	0	-0.062	-0.026	9.368	0.095	0.095	0.000	0.000	0.000	0.000
14	A	65	ARG	1	0.799	0.842	12.843	0.959	0.959	0.000	0.000	0.000	0.000
15	A	66	GLU	-1	-0.900	-0.927	15.478	-0.322	-0.322	0.000	0.000	0.000	0.000
16	A	67	TYR	0	-0.008	-0.026	14.314	0.072	0.072	0.000	0.000	0.000	0.000
17	A	68	VAL	0	-0.035	-0.027	15.965	0.061	0.061	0.000	0.000	0.000	0.000
18	A	69	LYS	1	0.895	0.975	18.378	0.360	0.360	0.000	0.000	0.000	0.000
19	A	70	GLU	-1	-0.956	-0.989	19.428	-0.214	-0.214	0.000	0.000	0.000	0.000
20	A	71	ASN	0	-0.110	-0.059	19.132	0.033	0.033	0.000	0.000	0.000	0.000
21	A	72	GLY	0	0.052	0.034	20.094	0.032	0.032	0.000	0.000	0.000	0.000
22	A	73	PRO	0	-0.033	-0.011	18.134	-0.042	-0.042	0.000	0.000	0.000	0.000
23	A	74	GLN	0	0.044	0.013	19.121	-0.031	-0.031	0.000	0.000	0.000	0.000
24	A	75	ASN	0	0.028	0.030	18.240	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	76	TRP	0	0.048	-0.006	13.189	-0.029	-0.029	0.000	0.000	0.000	0.000
26	A	77	PRO	0	0.006	-0.009	12.802	-0.085	-0.085	0.000	0.000	0.000	0.000
27	A	78	ARG	1	0.971	0.993	12.703	0.198	0.198	0.000	0.000	0.000	0.000
28	A	79	ILE	0	0.012	0.031	10.460	0.045	0.045	0.000	0.000	0.000	0.000
29	A	80	THR	0	-0.006	-0.014	8.744	-0.134	-0.134	0.000	0.000	0.000	0.000
30	A	81	SER	0	-0.085	-0.044	10.558	0.155	0.155	0.000	0.000	0.000	0.000
31	A	82	PHE	0	0.020	0.013	11.245	0.069	0.069	0.000	0.000	0.000	0.000
32	A	83	LEU	0	-0.007	0.003	6.022	-0.105	-0.105	0.000	0.000	0.000	0.000
33	A	84	PRO	0	0.072	0.036	6.959	-0.270	-0.270	0.000	0.000	0.000	0.000
34	A	85	ASN	0	-0.038	-0.018	2.588	-3.116	-1.523	0.929	-1.028	-1.494	0.002
35	A	86	ARG	1	0.770	0.856	1.663	0.063	-11.167	26.807	-9.029	-6.548	-0.054
36	A	87	SER	0	0.032	0.018	4.080	1.077	1.358	0.000	-0.099	-0.182	0.000
37	A	88	PRO	0	0.073	0.052	6.669	-0.080	-0.080	0.000	0.000	0.000	0.000
38	A	89	LYS	1	0.918	0.965	9.850	0.910	0.910	0.000	0.000	0.000	0.000
39	A	90	GLN	0	-0.001	-0.019	4.516	-0.540	-0.441	-0.001	-0.037	-0.060	0.000
40	A	91	CYS	0	0.016	0.036	7.992	-0.118	-0.118	0.000	0.000	0.000	0.000
41	A	92	ARG	1	0.960	0.981	9.974	0.787	0.787	0.000	0.000	0.000	0.000
42	A	93	GLU	-1	-0.994	-1.013	11.896	-1.025	-1.025	0.000	0.000	0.000	0.000
43	A	94	ARG	1	0.823	0.887	9.817	1.614	1.614	0.000	0.000	0.000	0.000
44	A	95	TRP	0	0.052	0.019	12.220	0.072	0.072	0.000	0.000	0.000	0.000
45	A	96	PHE	0	-0.030	-0.025	15.275	0.059	0.059	0.000	0.000	0.000	0.000
46	A	97	ASN	0	-0.101	-0.058	15.392	0.094	0.094	0.000	0.000	0.000	0.000
47	A	98	HIS	0	-0.043	-0.039	13.014	-0.072	-0.072	0.000	0.000	0.000	0.000
48	A	99	LEU	0	-0.013	0.017	13.053	0.012	0.012	0.000	0.000	0.000	0.000
49	A	100	ASP	-1	-0.870	-0.919	16.435	-0.432	-0.432	0.000	0.000	0.000	0.000
50	A	101	PRO	0	0.009	-0.005	19.767	0.007	0.007	0.000	0.000	0.000	0.000
51	A	102	ALA	0	-0.031	-0.011	23.026	0.021	0.021	0.000	0.000	0.000	0.000
52	A	103	VAL	0	-0.061	-0.002	19.014	0.025	0.025	0.000	0.000	0.000	0.000
53	A	104	VAL	0	-0.003	0.005	22.327	0.010	0.010	0.000	0.000	0.000	0.000
54	A	105	LYS	1	0.961	0.966	22.543	0.328	0.328	0.000	0.000	0.000	0.000
55	A	106	HIS	0	-0.032	-0.006	23.725	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	107	ALA	0	0.057	0.019	26.150	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	108	TRP	0	-0.004	-0.014	23.468	0.000	0.000	0.000	0.000	0.000	0.000
58	A	109	THR	0	0.024	0.003	28.830	0.015	0.015	0.000	0.000	0.000	0.000
59	A	110	PRO	0	0.041	0.009	32.460	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	111	GLU	-1	-0.823	-0.915	34.640	-0.172	-0.172	0.000	0.000	0.000	0.000
61	A	112	GLU	-1	-0.766	-0.832	29.387	-0.277	-0.277	0.000	0.000	0.000	0.000
62	A	113	ASP	-1	-0.775	-0.856	30.455	-0.224	-0.224	0.000	0.000	0.000	0.000
63	A	114	GLU	-1	-0.783	-0.888	32.539	-0.141	-0.141	0.000	0.000	0.000	0.000
64	A	115	THR	0	-0.064	-0.026	33.359	0.006	0.006	0.000	0.000	0.000	0.000
65	A	116	ILE	0	-0.026	-0.025	28.403	0.000	0.000	0.000	0.000	0.000	0.000
66	A	117	PHE	0	-0.011	-0.008	32.090	0.003	0.003	0.000	0.000	0.000	0.000
67	A	118	ARG	1	0.879	0.925	34.557	0.145	0.145	0.000	0.000	0.000	0.000
68	A	119	ASN	0	-0.067	-0.042	33.891	0.008	0.008	0.000	0.000	0.000	0.000
69	A	120	TYR	0	-0.012	0.009	29.519	0.005	0.005	0.000	0.000	0.000	0.000
70	A	121	LEU	0	-0.016	0.006	33.990	0.006	0.006	0.000	0.000	0.000	0.000
71	A	122	LYS	1	0.927	0.985	37.571	0.139	0.139	0.000	0.000	0.000	0.000
72	A	123	LEU	0	-0.083	-0.050	33.917	0.003	0.003	0.000	0.000	0.000	0.000
73	A	124	GLY	0	0.101	0.054	33.350	0.002	0.002	0.000	0.000	0.000	0.000
74	A	125	SER	0	0.028	0.016	27.982	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	126	LYS	1	0.860	0.920	28.089	0.185	0.185	0.000	0.000	0.000	0.000
76	A	127	TRP	0	0.127	0.036	25.088	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	128	SER	0	0.015	0.026	25.276	0.000	0.000	0.000	0.000	0.000	0.000
78	A	129	VAL	0	-0.014	-0.015	26.459	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	130	ILE	0	0.060	0.020	29.001	0.001	0.001	0.000	0.000	0.000	0.000
80	A	131	ALA	0	-0.011	0.008	25.254	0.003	0.003	0.000	0.000	0.000	0.000
81	A	132	LYS	1	0.921	0.964	27.286	0.227	0.227	0.000	0.000	0.000	0.000
82	A	133	LEU	0	-0.077	-0.041	29.843	0.014	0.014	0.000	0.000	0.000	0.000
83	A	134	ILE	0	-0.004	0.013	29.061	0.011	0.011	0.000	0.000	0.000	0.000
84	A	135	PRO	0	0.028	0.005	28.594	-0.021	-0.021	0.000	0.000	0.000	0.000
85	A	136	GLY	0	0.072	0.033	25.988	0.001	0.001	0.000	0.000	0.000	0.000
86	A	137	ARG	1	0.711	0.855	24.265	0.297	0.297	0.000	0.000	0.000	0.000
87	A	138	THR	0	0.044	0.017	19.112	0.017	0.017	0.000	0.000	0.000	0.000
88	A	139	ASP	-1	-0.802	-0.938	20.934	-0.420	-0.420	0.000	0.000	0.000	0.000
89	A	140	ASN	0	-0.007	-0.007	16.361	0.087	0.087	0.000	0.000	0.000	0.000
90	A	141	ALA	0	0.015	0.022	20.225	0.015	0.015	0.000	0.000	0.000	0.000
91	A	142	ILE	0	0.034	0.011	21.524	0.023	0.023	0.000	0.000	0.000	0.000
92	A	143	LYS	1	0.816	0.926	20.104	0.442	0.442	0.000	0.000	0.000	0.000
93	A	144	ASN	0	-0.005	-0.009	18.113	0.045	0.045	0.000	0.000	0.000	0.000
94	A	145	ARG	1	0.798	0.890	22.331	0.271	0.271	0.000	0.000	0.000	0.000
95	A	146	TRP	0	0.053	0.019	25.460	0.019	0.019	0.000	0.000	0.000	0.000
96	A	147	ASN	0	0.034	0.019	23.060	0.038	0.038	0.000	0.000	0.000	0.000
97	A	148	SER	0	-0.063	-0.041	23.207	0.021	0.021	0.000	0.000	0.000	0.000
98	A	149	SER	0	0.004	0.004	25.347	0.018	0.018	0.000	0.000	0.000	0.000
99	A	150	ILE	0	-0.006	-0.003	28.361	0.013	0.013	0.000	0.000	0.000	0.000
100	A	151	SER	0	-0.028	0.011	29.364	0.014	0.014	0.000	0.000	0.000	0.000
101	A	152	LYS	1	0.845	0.903	26.263	0.198	0.198	0.000	0.000	0.000	0.000
102	A	153	ARG	1	0.817	0.899	30.636	0.188	0.188	0.000	0.000	0.000	0.000
103	A	154	ILE	0	0.023	0.042	34.891	0.001	0.001	0.000	0.000	0.000	0.000
104	A	155	SER	0	0.024	-0.004	37.265	0.006	0.006	0.000	0.000	0.000	0.000
105	A	156	THR	0	0.043	0.053	40.961	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	157	ASN	0	0.027	0.012	44.673	0.000	0.000	0.000	0.000	0.000	0.000
107	A	158	SER	0	0.004	0.005	47.316	0.002	0.002	0.000	0.000	0.000	0.000
108	A	159	ASN	0	-0.015	-0.022	50.290	0.003	0.003	0.000	0.000	0.000	0.000
109	A	160	HIS	0	-0.013	-0.003	48.769	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	161	LYS	1	0.810	0.909	44.144	0.096	0.096	0.000	0.000	0.000	0.000
111	A	162	GLU	-1	-0.812	-0.927	40.661	-0.104	-0.104	0.000	0.000	0.000	0.000
112	A	163	ILE	0	-0.046	-0.025	41.467	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	164	LEU	0	-0.030	-0.010	34.352	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	165	LEU	0	0.014	0.005	37.669	0.002	0.002	0.000	0.000	0.000	0.000
115	A	166	PRO	0	0.013	0.020	36.424	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	167	ASP	-1	-0.825	-0.934	30.563	-0.197	-0.197	0.000	0.000	0.000	0.000
117	A	168	ARG	1	0.905	0.937	33.360	0.130	0.130	0.000	0.000	0.000	0.000
118	A	169	SER	0	0.014	0.034	28.978	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:52:MET)