FMO DATABASE

FMODB ID: J3ZQ9

Calculation Name: 4QXZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4QXZ

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

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:

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	146
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1409714.288607
FMO2-HF: Nuclear repulsion	1349684.798852
FMO2-HF: Total energy	-60029.489755
FMO2-MP2: Total energy	-60204.205398

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:SER)

Summations of interaction energy for fragment #1(A:-1:SER)

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.
-14.194	-5.965	2.675	-5.189	-5.714	0.029

Interaction energy analysis for fragmet #1(A:-1:SER)

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 : 0.015

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	1	MET	0	-0.050	-0.002	2.331	-11.401	-4.294	1.280	-4.189	-4.197	0.028
4	A	2	LYS	1	0.984	0.988	4.286	-0.146	-0.042	-0.001	-0.034	-0.069	0.000
5	A	3	THR	0	0.019	0.015	6.232	-0.353	-0.353	0.000	0.000	0.000	0.000
6	A	4	PHE	0	0.003	0.000	2.010	-1.169	-0.151	1.396	-0.966	-1.448	0.001
7	A	5	LYS	1	1.004	1.009	7.288	-0.013	-0.013	0.000	0.000	0.000	0.000
8	A	6	ALA	0	-0.029	-0.008	10.011	-0.083	-0.083	0.000	0.000	0.000	0.000
9	A	7	VAL	0	-0.034	-0.034	12.116	0.067	0.067	0.000	0.000	0.000	0.000
10	A	8	ARG	1	0.837	0.907	14.290	0.092	0.092	0.000	0.000	0.000	0.000
11	A	9	PHE	0	0.063	0.031	15.255	-0.050	-0.050	0.000	0.000	0.000	0.000
12	A	10	GLN	0	-0.041	-0.030	17.785	0.017	0.017	0.000	0.000	0.000	0.000
13	A	11	ILE	0	0.029	0.018	19.648	-0.026	-0.026	0.000	0.000	0.000	0.000
14	A	12	VAL	0	-0.028	-0.006	21.253	0.023	0.023	0.000	0.000	0.000	0.000
15	A	13	ASN	0	0.043	0.018	23.994	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	14	GLU	-1	-0.863	-0.944	26.852	-0.098	-0.098	0.000	0.000	0.000	0.000
17	A	15	HIS	0	-0.023	0.009	28.978	0.000	0.000	0.000	0.000	0.000	0.000
18	A	16	GLY	0	0.060	0.022	26.055	0.009	0.009	0.000	0.000	0.000	0.000
19	A	17	ARG	1	0.871	0.928	26.920	0.066	0.066	0.000	0.000	0.000	0.000
20	A	18	ILE	0	0.054	0.030	22.255	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	19	ILE	0	-0.007	-0.001	24.826	0.013	0.013	0.000	0.000	0.000	0.000
22	A	20	GLU	-1	-0.783	-0.874	20.447	-0.087	-0.087	0.000	0.000	0.000	0.000
23	A	21	TYR	0	-0.050	-0.036	21.869	0.016	0.016	0.000	0.000	0.000	0.000
24	A	22	GLU	-1	-0.914	-0.957	21.316	-0.023	-0.023	0.000	0.000	0.000	0.000
25	A	23	LEU	0	-0.086	-0.040	16.499	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	24	GLU	-1	-0.943	-0.968	20.517	0.015	0.015	0.000	0.000	0.000	0.000
27	A	25	ASP	-1	-0.959	-0.992	17.839	0.015	0.015	0.000	0.000	0.000	0.000
28	A	26	GLY	0	0.040	0.003	15.348	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	27	VAL	0	-0.031	0.015	11.581	0.010	0.010	0.000	0.000	0.000	0.000
30	A	28	ILE	0	0.014	-0.002	8.666	-0.029	-0.029	0.000	0.000	0.000	0.000
31	A	29	ILE	0	-0.032	-0.022	9.123	-0.055	-0.055	0.000	0.000	0.000	0.000
32	A	30	ASN	0	-0.024	-0.018	6.949	0.082	0.082	0.000	0.000	0.000	0.000
33	A	31	LYS	1	0.917	0.949	9.651	0.330	0.330	0.000	0.000	0.000	0.000
34	A	32	GLU	-1	-0.859	-0.937	10.833	-0.479	-0.479	0.000	0.000	0.000	0.000
35	A	33	GLU	-1	-0.986	-0.976	13.360	-0.130	-0.130	0.000	0.000	0.000	0.000
36	A	34	SER	0	-0.052	-0.019	16.066	0.039	0.039	0.000	0.000	0.000	0.000
37	A	35	GLY	0	0.014	0.027	16.409	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	36	THR	0	-0.050	-0.069	16.646	0.022	0.022	0.000	0.000	0.000	0.000
39	A	37	GLY	0	0.050	0.055	14.328	0.021	0.021	0.000	0.000	0.000	0.000
40	A	38	TRP	0	-0.020	-0.029	6.155	-0.101	-0.101	0.000	0.000	0.000	0.000
41	A	39	LEU	0	-0.031	-0.005	12.938	0.058	0.058	0.000	0.000	0.000	0.000
42	A	40	LEU	0	-0.024	0.005	13.418	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	41	GLU	-1	-0.925	-0.959	15.044	-0.052	-0.052	0.000	0.000	0.000	0.000
44	A	42	ILE	0	-0.002	0.003	16.477	0.000	0.000	0.000	0.000	0.000	0.000
45	A	43	VAL	0	0.001	0.004	18.807	0.007	0.007	0.000	0.000	0.000	0.000
46	A	44	ILE	0	0.029	0.021	21.942	0.003	0.003	0.000	0.000	0.000	0.000
47	A	45	SER	0	0.058	0.019	24.297	0.004	0.004	0.000	0.000	0.000	0.000
48	A	46	ASN	0	0.070	0.009	28.017	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	47	GLU	-1	-0.960	-0.971	30.623	-0.033	-0.033	0.000	0.000	0.000	0.000
50	A	48	HIS	1	0.896	0.948	27.540	0.052	0.052	0.000	0.000	0.000	0.000
51	A	49	TYR	0	0.056	0.001	29.399	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	50	GLU	-1	-0.888	-0.954	30.965	-0.052	-0.052	0.000	0.000	0.000	0.000
53	A	51	THR	0	-0.026	0.002	28.553	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	52	PHE	0	0.010	-0.011	23.406	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	53	LYS	1	0.870	0.955	28.270	0.062	0.062	0.000	0.000	0.000	0.000
56	A	54	GLU	-1	-0.889	-0.947	31.047	-0.075	-0.075	0.000	0.000	0.000	0.000
57	A	55	TYR	0	-0.044	-0.039	26.392	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	56	GLN	0	-0.050	-0.029	27.740	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	57	ASP	-1	-0.889	-0.942	28.902	-0.078	-0.078	0.000	0.000	0.000	0.000
60	A	58	ASN	0	-0.046	-0.019	31.756	0.004	0.004	0.000	0.000	0.000	0.000
61	A	59	GLU	-1	-0.980	-0.981	28.409	-0.129	-0.129	0.000	0.000	0.000	0.000
62	A	60	GLN	0	-0.072	-0.016	27.230	0.001	0.001	0.000	0.000	0.000	0.000
63	A	61	LEU	0	0.006	0.004	24.078	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	62	LEU	0	-0.062	-0.035	22.182	0.012	0.012	0.000	0.000	0.000	0.000
65	A	63	ASP	-1	-0.729	-0.821	20.096	-0.264	-0.264	0.000	0.000	0.000	0.000
66	A	64	ILE	0	-0.020	-0.013	16.191	0.023	0.023	0.000	0.000	0.000	0.000
67	A	65	ARG	1	0.766	0.882	15.725	0.198	0.198	0.000	0.000	0.000	0.000
68	A	66	VAL	0	0.029	0.015	11.619	0.040	0.040	0.000	0.000	0.000	0.000
69	A	67	VAL	0	-0.004	0.017	11.684	-0.094	-0.094	0.000	0.000	0.000	0.000
70	A	68	ILE	0	0.044	0.015	5.820	0.055	0.055	0.000	0.000	0.000	0.000
71	A	69	THR	0	-0.044	-0.013	6.935	0.221	0.221	0.000	0.000	0.000	0.000
72	A	70	ARG	1	0.905	0.917	9.496	-0.402	-0.402	0.000	0.000	0.000	0.000
73	A	71	PRO	0	0.040	0.026	12.262	-0.033	-0.033	0.000	0.000	0.000	0.000
74	A	72	ALA	0	0.000	-0.010	14.693	-0.022	-0.022	0.000	0.000	0.000	0.000
75	A	73	ASN	0	-0.043	-0.015	8.445	0.105	0.105	0.000	0.000	0.000	0.000
76	A	74	ASP	-1	-0.859	-0.925	11.288	-0.030	-0.030	0.000	0.000	0.000	0.000
77	A	75	PRO	0	-0.084	-0.043	10.947	-0.100	-0.100	0.000	0.000	0.000	0.000
78	A	76	ALA	0	0.004	0.015	9.327	-0.023	-0.023	0.000	0.000	0.000	0.000
79	A	77	LEU	0	-0.033	-0.028	11.396	0.092	0.092	0.000	0.000	0.000	0.000
80	A	78	PHE	0	0.007	-0.011	10.014	-0.081	-0.081	0.000	0.000	0.000	0.000
81	A	79	GLU	-1	-0.902	-0.941	15.639	-0.205	-0.205	0.000	0.000	0.000	0.000
82	A	80	SER	0	-0.053	-0.042	18.120	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	81	THR	0	0.103	0.067	20.118	0.016	0.016	0.000	0.000	0.000	0.000
84	A	82	VAL	0	0.006	-0.004	21.874	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	83	LYS	1	0.978	0.999	21.125	0.168	0.168	0.000	0.000	0.000	0.000
86	A	84	SER	0	-0.085	-0.055	23.563	0.016	0.016	0.000	0.000	0.000	0.000
87	A	85	ILE	0	0.057	0.032	24.477	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	86	LYS	1	0.920	0.965	26.028	0.059	0.059	0.000	0.000	0.000	0.000
89	A	87	ASN	0	0.017	0.008	27.801	0.002	0.002	0.000	0.000	0.000	0.000
90	A	88	PHE	0	-0.017	-0.011	25.893	0.004	0.004	0.000	0.000	0.000	0.000
91	A	89	LYS	1	0.931	0.963	31.216	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	90	THR	0	0.035	0.012	30.954	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	91	THR	0	-0.006	0.010	26.527	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	92	MET	0	-0.030	0.007	25.983	0.002	0.002	0.000	0.000	0.000	0.000
95	A	93	SER	0	-0.031	0.001	22.257	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	94	ILE	0	0.019	0.005	21.970	0.002	0.002	0.000	0.000	0.000	0.000
97	A	95	VAL	0	0.005	0.012	18.911	-0.012	-0.012	0.000	0.000	0.000	0.000
98	A	96	PHE	0	0.002	-0.019	17.868	0.010	0.010	0.000	0.000	0.000	0.000
99	A	97	GLU	-1	-0.925	-0.969	17.780	-0.254	-0.254	0.000	0.000	0.000	0.000
100	A	98	CYS	0	-0.050	-0.027	14.615	0.019	0.019	0.000	0.000	0.000	0.000
101	A	99	HIS	0	0.075	0.043	15.141	-0.075	-0.075	0.000	0.000	0.000	0.000
102	A	100	ILE	0	-0.061	-0.019	9.041	0.005	0.005	0.000	0.000	0.000	0.000
103	A	101	TYR	0	-0.067	-0.088	13.104	0.041	0.041	0.000	0.000	0.000	0.000
104	A	102	THR	0	0.010	-0.001	12.928	-0.056	-0.056	0.000	0.000	0.000	0.000
105	A	103	LEU	0	-0.030	-0.005	14.439	0.033	0.033	0.000	0.000	0.000	0.000
106	A	104	ARG	1	0.803	0.881	17.361	0.159	0.159	0.000	0.000	0.000	0.000
107	A	105	GLN	0	0.049	0.003	18.027	0.029	0.029	0.000	0.000	0.000	0.000
108	A	106	GLN	0	0.011	0.002	21.338	0.001	0.001	0.000	0.000	0.000	0.000
109	A	107	TYR	0	-0.005	-0.005	21.980	0.009	0.009	0.000	0.000	0.000	0.000
110	A	108	ALA	0	0.016	-0.004	24.088	0.006	0.006	0.000	0.000	0.000	0.000
111	A	109	GLU	-1	-0.843	-0.938	26.537	-0.082	-0.082	0.000	0.000	0.000	0.000
112	A	110	SER	0	0.032	0.015	26.868	0.001	0.001	0.000	0.000	0.000	0.000
113	A	111	LEU	0	-0.045	-0.012	26.415	0.003	0.003	0.000	0.000	0.000	0.000
114	A	112	LEU	0	-0.055	-0.042	28.803	0.006	0.006	0.000	0.000	0.000	0.000
115	A	113	GLU	-1	-0.949	-0.975	31.818	-0.085	-0.085	0.000	0.000	0.000	0.000
116	A	114	GLN	0	0.079	0.048	30.035	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	115	LEU	0	-0.051	-0.037	31.211	0.005	0.005	0.000	0.000	0.000	0.000
118	A	116	ILE	0	-0.015	-0.014	34.521	0.005	0.005	0.000	0.000	0.000	0.000
119	A	117	ASP	-1	-0.899	-0.927	36.407	-0.067	-0.067	0.000	0.000	0.000	0.000
120	A	118	ASP	-1	-0.955	-0.969	35.113	-0.076	-0.076	0.000	0.000	0.000	0.000
121	A	119	GLY	0	-0.047	-0.030	38.390	0.003	0.003	0.000	0.000	0.000	0.000
122	A	120	LEU	0	-0.066	-0.028	35.614	0.004	0.004	0.000	0.000	0.000	0.000
123	A	121	SER	0	0.017	-0.007	39.438	0.001	0.001	0.000	0.000	0.000	0.000
124	A	122	GLY	0	0.020	0.002	40.658	0.001	0.001	0.000	0.000	0.000	0.000
125	A	123	GLU	-1	-0.805	-0.900	38.983	-0.022	-0.022	0.000	0.000	0.000	0.000
126	A	124	GLU	-1	-0.894	-0.943	37.886	-0.033	-0.033	0.000	0.000	0.000	0.000
127	A	125	LEU	0	-0.008	0.017	34.710	-0.004	-0.004	0.000	0.000	0.000	0.000
128	A	126	LYS	1	0.870	0.898	34.285	0.017	0.017	0.000	0.000	0.000	0.000
129	A	127	LYS	1	0.921	0.978	33.073	0.036	0.036	0.000	0.000	0.000	0.000
130	A	128	SER	0	-0.037	-0.045	32.109	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	129	PHE	0	0.059	0.041	28.722	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	130	ASN	0	0.031	0.005	28.449	-0.007	-0.007	0.000	0.000	0.000	0.000
133	A	131	ARG	1	0.756	0.887	27.205	0.065	0.065	0.000	0.000	0.000	0.000
134	A	132	MET	0	-0.015	-0.005	26.020	-0.007	-0.007	0.000	0.000	0.000	0.000
135	A	133	MET	0	0.016	0.018	24.041	-0.015	-0.015	0.000	0.000	0.000	0.000
136	A	134	GLN	0	-0.060	-0.020	21.627	-0.008	-0.008	0.000	0.000	0.000	0.000
137	A	135	SER	0	-0.051	-0.028	20.918	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	136	LYS	1	0.930	0.969	16.957	0.127	0.127	0.000	0.000	0.000	0.000
139	A	137	PRO	0	0.015	0.036	21.510	-0.017	-0.017	0.000	0.000	0.000	0.000
140	A	138	LYS	1	0.965	0.997	19.697	0.267	0.267	0.000	0.000	0.000	0.000
141	A	139	LEU	0	-0.028	0.000	23.908	0.016	0.016	0.000	0.000	0.000	0.000
142	A	140	LYS	1	0.919	0.938	26.819	0.080	0.080	0.000	0.000	0.000	0.000
143	A	141	ASP	-1	-0.808	-0.863	27.642	-0.144	-0.144	0.000	0.000	0.000	0.000
144	A	142	GLU	-1	-0.907	-0.962	23.069	-0.217	-0.217	0.000	0.000	0.000	0.000
145	A	143	LYS	1	0.872	0.948	26.604	0.131	0.131	0.000	0.000	0.000	0.000
146	A	144	LEU	0	0.008	0.010	29.293	0.006	0.006	0.000	0.000	0.000	0.000

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