FMO DATABASE

FMODB ID: 3JGQL

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

Total energy (hartree)

FMO2-HF: Electronic energy	-953771.470755
FMO2-HF: Nuclear repulsion	905754.54426
FMO2-HF: Total energy	-48016.926495
FMO2-MP2: Total energy	-48159.658703

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.
-9.854	-13.731	27.122	-10.371	-12.874	-0.057

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 : 0.010 / 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

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	-0.002	-0.006	2.514	-4.160	-1.807	2.473	-1.924	-2.901	-0.016
4	A	55	PRO	0	-0.003	-0.002	4.328	-1.027	-0.892	-0.001	-0.034	-0.100	0.000
5	A	56	PHE	0	0.035	0.001	4.935	-0.891	-0.762	-0.001	-0.006	-0.122	0.000
6	A	57	THR	0	-0.052	-0.006	5.361	0.608	0.608	0.000	0.000	0.000	0.000
7	A	58	GLU	-1	-0.806	-0.918	7.631	-0.676	-0.676	0.000	0.000	0.000	0.000
8	A	59	ALA	0	0.060	0.031	8.717	0.015	0.015	0.000	0.000	0.000	0.000
9	A	60	GLU	-1	-0.804	-0.912	3.466	-5.860	-4.710	0.023	-0.689	-0.485	-0.005
10	A	61	ASP	-1	-0.786	-0.896	7.983	-1.172	-1.172	0.000	0.000	0.000	0.000
11	A	62	ASP	-1	-0.848	-0.936	10.832	-0.413	-0.413	0.000	0.000	0.000	0.000
12	A	63	LEU	0	-0.026	-0.010	9.082	0.037	0.037	0.000	0.000	0.000	0.000
13	A	64	ILE	0	-0.050	-0.025	9.960	0.036	0.036	0.000	0.000	0.000	0.000
14	A	65	ARG	1	0.864	0.922	12.773	0.657	0.657	0.000	0.000	0.000	0.000
15	A	66	GLU	-1	-0.918	-0.937	15.272	-0.259	-0.259	0.000	0.000	0.000	0.000
16	A	67	TYR	0	-0.012	-0.033	14.190	0.047	0.047	0.000	0.000	0.000	0.000
17	A	68	VAL	0	-0.032	-0.023	15.885	0.050	0.050	0.000	0.000	0.000	0.000
18	A	69	LYS	1	0.893	0.966	18.280	0.305	0.305	0.000	0.000	0.000	0.000
19	A	70	GLU	-1	-0.980	-0.998	19.112	-0.205	-0.205	0.000	0.000	0.000	0.000
20	A	71	ASN	0	-0.051	-0.028	18.988	0.011	0.011	0.000	0.000	0.000	0.000
21	A	72	GLY	0	0.032	0.027	20.011	0.028	0.028	0.000	0.000	0.000	0.000
22	A	73	PRO	0	-0.049	-0.021	17.990	-0.044	-0.044	0.000	0.000	0.000	0.000
23	A	74	GLN	0	0.023	-0.008	18.963	-0.015	-0.015	0.000	0.000	0.000	0.000
24	A	75	ASN	0	0.073	0.058	18.232	-0.026	-0.026	0.000	0.000	0.000	0.000
25	A	76	TRP	0	0.021	-0.014	13.390	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	77	PRO	0	0.000	-0.011	12.816	-0.102	-0.102	0.000	0.000	0.000	0.000
27	A	78	ARG	1	0.963	0.980	12.749	0.194	0.194	0.000	0.000	0.000	0.000
28	A	79	ILE	0	0.020	0.034	10.472	0.051	0.051	0.000	0.000	0.000	0.000
29	A	80	THR	0	-0.005	-0.007	9.351	-0.160	-0.160	0.000	0.000	0.000	0.000
30	A	81	SER	0	-0.081	-0.040	10.702	0.070	0.070	0.000	0.000	0.000	0.000
31	A	82	PHE	0	0.025	0.019	11.233	0.082	0.082	0.000	0.000	0.000	0.000
32	A	83	LEU	0	-0.021	0.002	6.053	-0.146	-0.146	0.000	0.000	0.000	0.000
33	A	84	PRO	0	0.072	0.036	6.922	-0.404	-0.404	0.000	0.000	0.000	0.000
34	A	85	ASN	0	-0.054	-0.025	2.049	-0.809	0.137	1.823	-1.124	-1.645	0.006
35	A	86	ARG	1	0.797	0.877	1.855	1.296	-7.674	22.806	-6.476	-7.360	-0.042
36	A	87	SER	0	0.009	0.001	4.168	1.246	1.496	0.000	-0.070	-0.180	0.000
37	A	88	PRO	0	0.082	0.042	6.577	-0.097	-0.097	0.000	0.000	0.000	0.000
38	A	89	LYS	1	0.936	0.974	9.457	0.766	0.766	0.000	0.000	0.000	0.000
39	A	90	GLN	0	0.020	0.010	4.117	-0.924	-0.794	-0.001	-0.048	-0.081	0.000
40	A	91	CYS	0	0.037	0.053	8.123	-0.191	-0.191	0.000	0.000	0.000	0.000
41	A	92	ARG	1	0.973	0.998	9.791	0.778	0.778	0.000	0.000	0.000	0.000
42	A	93	GLU	-1	-1.018	-1.021	11.777	-1.033	-1.033	0.000	0.000	0.000	0.000
43	A	94	ARG	1	0.861	0.939	9.791	1.354	1.354	0.000	0.000	0.000	0.000
44	A	95	TRP	0	0.093	0.033	12.083	0.097	0.097	0.000	0.000	0.000	0.000
45	A	96	PHE	0	-0.019	-0.018	14.995	0.061	0.061	0.000	0.000	0.000	0.000
46	A	97	ASN	0	-0.112	-0.058	15.474	0.071	0.071	0.000	0.000	0.000	0.000
47	A	98	HIS	0	-0.049	-0.041	13.616	-0.030	-0.030	0.000	0.000	0.000	0.000
48	A	99	LEU	0	-0.031	0.004	11.938	0.016	0.016	0.000	0.000	0.000	0.000
49	A	100	ASP	-1	-0.880	-0.939	16.031	-0.372	-0.372	0.000	0.000	0.000	0.000
50	A	101	PRO	0	-0.013	-0.011	19.362	0.010	0.010	0.000	0.000	0.000	0.000
51	A	102	ALA	0	-0.025	-0.010	22.573	0.020	0.020	0.000	0.000	0.000	0.000
52	A	103	VAL	0	-0.065	0.005	18.867	0.019	0.019	0.000	0.000	0.000	0.000
53	A	104	VAL	0	-0.004	0.004	22.165	0.015	0.015	0.000	0.000	0.000	0.000
54	A	105	LYS	1	0.975	0.966	22.723	0.246	0.246	0.000	0.000	0.000	0.000
55	A	106	HIS	0	-0.042	-0.014	23.825	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	107	ALA	0	0.070	0.023	26.564	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	108	TRP	0	-0.022	-0.029	23.831	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	109	THR	0	0.016	0.041	29.230	0.012	0.012	0.000	0.000	0.000	0.000
59	A	110	PRO	0	0.075	0.024	32.711	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	111	GLU	-1	-0.803	-0.914	34.978	-0.151	-0.151	0.000	0.000	0.000	0.000
61	A	112	GLU	-1	-0.820	-0.898	29.623	-0.242	-0.242	0.000	0.000	0.000	0.000
62	A	113	ASP	-1	-0.806	-0.918	30.760	-0.202	-0.202	0.000	0.000	0.000	0.000
63	A	114	GLU	-1	-0.862	-0.940	32.646	-0.129	-0.129	0.000	0.000	0.000	0.000
64	A	115	THR	0	-0.061	-0.032	33.239	0.005	0.005	0.000	0.000	0.000	0.000
65	A	116	ILE	0	-0.015	-0.019	28.166	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	117	PHE	0	-0.002	0.001	31.993	0.001	0.001	0.000	0.000	0.000	0.000
67	A	118	ARG	1	0.935	0.962	34.419	0.130	0.130	0.000	0.000	0.000	0.000
68	A	119	ASN	0	-0.070	-0.040	33.641	0.003	0.003	0.000	0.000	0.000	0.000
69	A	120	TYR	0	-0.006	0.014	29.744	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	121	LEU	0	-0.003	0.010	33.824	0.005	0.005	0.000	0.000	0.000	0.000
71	A	122	LYS	1	0.915	0.979	37.389	0.127	0.127	0.000	0.000	0.000	0.000
72	A	123	LEU	0	-0.090	-0.055	33.545	0.003	0.003	0.000	0.000	0.000	0.000
73	A	124	GLY	0	0.093	0.050	33.145	0.002	0.002	0.000	0.000	0.000	0.000
74	A	125	SER	0	0.042	0.018	27.702	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	126	LYS	1	0.877	0.931	27.905	0.164	0.164	0.000	0.000	0.000	0.000
76	A	127	TRP	0	0.128	0.038	25.065	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	128	SER	0	0.007	0.016	25.484	0.001	0.001	0.000	0.000	0.000	0.000
78	A	129	VAL	0	-0.015	-0.012	26.399	0.001	0.001	0.000	0.000	0.000	0.000
79	A	130	ILE	0	0.064	0.027	28.887	0.001	0.001	0.000	0.000	0.000	0.000
80	A	131	ALA	0	-0.014	0.004	25.286	0.004	0.004	0.000	0.000	0.000	0.000
81	A	132	LYS	1	0.922	0.964	27.276	0.209	0.209	0.000	0.000	0.000	0.000
82	A	133	LEU	0	-0.092	-0.047	29.873	0.014	0.014	0.000	0.000	0.000	0.000
83	A	134	ILE	0	0.009	0.016	29.009	0.010	0.010	0.000	0.000	0.000	0.000
84	A	135	PRO	0	0.009	0.008	28.646	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	136	GLY	0	0.087	0.029	25.888	0.002	0.002	0.000	0.000	0.000	0.000
86	A	137	ARG	1	0.708	0.869	24.302	0.259	0.259	0.000	0.000	0.000	0.000
87	A	138	THR	0	0.053	0.025	19.436	0.007	0.007	0.000	0.000	0.000	0.000
88	A	139	ASP	-1	-0.853	-0.960	21.010	-0.401	-0.401	0.000	0.000	0.000	0.000
89	A	140	ASN	0	0.028	0.004	16.729	0.055	0.055	0.000	0.000	0.000	0.000
90	A	141	ALA	0	-0.002	0.007	20.128	0.009	0.009	0.000	0.000	0.000	0.000
91	A	142	ILE	0	0.040	0.015	21.460	0.020	0.020	0.000	0.000	0.000	0.000
92	A	143	LYS	1	0.876	0.959	19.201	0.455	0.455	0.000	0.000	0.000	0.000
93	A	144	ASN	0	0.000	-0.004	17.974	0.033	0.033	0.000	0.000	0.000	0.000
94	A	145	ARG	1	0.842	0.953	22.349	0.253	0.253	0.000	0.000	0.000	0.000
95	A	146	TRP	0	0.062	0.015	25.605	0.017	0.017	0.000	0.000	0.000	0.000
96	A	147	ASN	0	-0.002	-0.002	23.255	0.036	0.036	0.000	0.000	0.000	0.000
97	A	148	SER	0	-0.080	-0.047	23.416	0.017	0.017	0.000	0.000	0.000	0.000
98	A	149	SER	0	-0.007	-0.002	25.557	0.017	0.017	0.000	0.000	0.000	0.000
99	A	150	ILE	0	-0.006	-0.007	28.608	0.011	0.011	0.000	0.000	0.000	0.000
100	A	151	SER	0	-0.019	0.012	29.547	0.016	0.016	0.000	0.000	0.000	0.000
101	A	152	LYS	1	0.896	0.949	26.649	0.199	0.199	0.000	0.000	0.000	0.000
102	A	153	ARG	1	0.842	0.927	30.807	0.172	0.172	0.000	0.000	0.000	0.000
103	A	154	ILE	0	0.052	0.056	35.098	0.001	0.001	0.000	0.000	0.000	0.000
104	A	155	SER	0	0.040	-0.007	37.490	0.005	0.005	0.000	0.000	0.000	0.000
105	A	156	THR	0	0.017	0.043	41.177	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	157	ASN	0	0.039	0.025	44.886	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	158	SER	0	0.007	-0.005	47.515	0.001	0.001	0.000	0.000	0.000	0.000
108	A	159	ASN	0	-0.013	-0.016	50.367	0.003	0.003	0.000	0.000	0.000	0.000
109	A	160	HIS	0	-0.004	-0.003	48.849	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	161	LYS	1	0.881	0.952	44.780	0.086	0.086	0.000	0.000	0.000	0.000
111	A	162	GLU	-1	-0.910	-0.983	39.385	-0.105	-0.105	0.000	0.000	0.000	0.000
112	A	163	ILE	0	-0.033	-0.013	41.560	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	164	LEU	0	-0.027	-0.013	34.649	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	165	LEU	0	-0.019	-0.003	37.722	0.003	0.003	0.000	0.000	0.000	0.000
115	A	166	PRO	0	-0.008	0.012	36.710	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	167	ASP	-1	-0.909	-0.987	31.403	-0.169	-0.169	0.000	0.000	0.000	0.000
117	A	168	ARG	1	0.961	0.965	33.597	0.119	0.119	0.000	0.000	0.000	0.000
118	A	169	SER	0	-0.005	0.025	29.282	0.003	0.003	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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