FMO DATABASE

FMODB ID: 72LMK

Calculation Name: 1OZ7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OZ7

Chain ID: A

ChEMBL ID:

UniProt ID: Q7T248

Base Structure: X-ray

Registration Date: 2023-09-20

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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1170006.088855
FMO2-HF: Nuclear repulsion	1114364.834704
FMO2-HF: Total energy	-55641.254151
FMO2-MP2: Total energy	-55797.44553

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
-7.004	-3.016	1.049	-1.879	-3.157	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.054 / q_NPA : -0.030

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	3	PRO	0	0.018	0.006	2.781	-5.198	-2.103	1.019	-1.658	-2.455	-0.009
4	A	4	PRO	0	0.052	0.013	4.164	0.216	0.324	-0.001	0.001	-0.107	0.000
5	A	5	GLY	0	0.020	0.014	6.137	0.189	0.189	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.015	-0.003	6.832	0.190	0.190	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.019	0.011	7.339	0.099	0.099	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.002	-0.018	4.143	-1.056	-0.908	0.000	-0.059	-0.089	0.000
9	A	9	ASN	0	-0.003	0.000	6.656	-0.390	-0.390	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.006	0.009	8.723	-0.099	-0.099	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.045	-0.027	4.810	-0.152	-0.152	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.024	0.019	6.298	-0.424	-0.424	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.077	-0.096	7.251	-0.263	-0.263	0.000	0.000	0.000	0.000
14	A	15	MET	0	0.019	0.018	10.726	0.031	0.031	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.025	0.005	13.146	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.050	0.014	13.240	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.844	0.937	18.218	-0.058	-0.058	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.940	-0.985	19.965	0.011	0.011	0.000	0.000	0.000	0.000
19	A	20	PRO	0	-0.058	-0.037	22.867	0.005	0.005	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.940	0.983	21.964	-0.042	-0.042	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.061	0.055	26.520	0.004	0.004	0.000	0.000	0.000	0.000
22	A	23	TRP	0	0.043	0.041	25.381	0.002	0.002	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.823	-0.946	25.023	0.047	0.047	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.937	-0.990	25.490	0.034	0.034	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.004	0.003	22.171	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.774	-0.865	20.672	0.086	0.086	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.895	0.936	20.558	-0.036	-0.036	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.001	-0.022	16.357	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	30	CYS	0	-0.021	0.028	14.400	-0.022	-0.022	0.000	0.000	0.000	0.000
30	A	31	ASN	0	-0.033	0.022	16.015	0.002	0.002	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.805	0.886	17.331	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	33	GLN	0	-0.070	-0.029	12.497	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.045	0.028	11.646	0.010	0.010	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.858	0.935	12.528	-0.033	-0.033	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.893	-0.960	13.019	0.023	0.023	0.000	0.000	0.000	0.000
36	A	37	GLY	0	-0.002	0.007	13.651	0.011	0.011	0.000	0.000	0.000	0.000
37	A	38	HIS	1	0.800	0.852	14.386	-0.094	-0.094	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.026	0.032	16.154	0.023	0.023	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.061	-0.014	15.765	0.004	0.004	0.000	0.000	0.000	0.000
40	A	41	SER	0	0.039	0.040	16.377	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.014	-0.010	16.711	0.033	0.033	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.896	-0.957	16.636	0.123	0.123	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.012	-0.009	17.171	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	45	LYS	1	1.008	1.016	19.606	-0.173	-0.173	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.917	0.946	15.949	-0.308	-0.308	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.735	-0.827	14.077	0.331	0.331	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.817	-0.919	16.343	0.175	0.175	0.000	0.000	0.000	0.000
48	A	49	ILE	0	-0.062	-0.035	18.029	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.045	-0.013	11.918	0.004	0.004	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.031	0.002	15.273	0.027	0.027	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.816	-0.915	16.843	0.182	0.182	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.029	0.058	16.309	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.047	0.024	13.520	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.053	-0.032	16.562	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.116	-0.114	19.744	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.972	-0.969	15.858	0.216	0.216	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.043	-0.012	15.302	-0.044	-0.044	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.007	0.008	18.497	-0.024	-0.024	0.000	0.000	0.000	0.000
59	A	60	GLY	0	-0.003	0.011	21.519	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.934	0.936	24.839	-0.076	-0.076	0.000	0.000	0.000	0.000
61	A	62	MET	0	0.015	0.010	26.680	-0.006	-0.006	0.000	0.000	0.000	0.000
62	A	63	TYR	0	0.039	0.004	28.353	0.005	0.005	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.953	0.990	27.729	-0.061	-0.061	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.003	0.018	21.092	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	66	TRP	0	-0.001	0.010	23.249	0.006	0.006	0.000	0.000	0.000	0.000
66	A	67	THR	0	0.055	-0.011	20.231	0.011	0.011	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.011	-0.006	20.460	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.080	-0.023	21.888	-0.005	-0.005	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.016	-0.014	24.801	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.805	-0.864	27.453	0.040	0.040	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.876	0.917	27.386	-0.051	-0.051	0.000	0.000	0.000	0.000
72	A	73	SER	0	0.048	0.021	31.760	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.826	0.915	33.388	-0.033	-0.033	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.740	-0.864	36.849	0.032	0.032	0.000	0.000	0.000	0.000
75	A	76	GLN	0	0.014	0.009	39.357	0.000	0.000	0.000	0.000	0.000	0.000
76	A	77	HIS	0	-0.107	-0.069	38.518	0.000	0.000	0.000	0.000	0.000	0.000
77	A	78	CYS	0	-0.127	-0.062	36.753	0.001	0.001	0.000	0.000	0.000	0.000
78	A	79	SER	0	0.006	0.016	39.426	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.066	0.027	41.613	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.917	0.948	43.211	-0.026	-0.026	0.000	0.000	0.000	0.000
81	A	82	TRP	0	0.033	0.028	46.139	0.002	0.002	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.062	-0.019	48.580	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.880	-0.966	49.739	0.021	0.021	0.000	0.000	0.000	0.000
84	A	85	GLY	0	-0.020	-0.001	50.783	0.000	0.000	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.027	-0.016	48.457	0.001	0.001	0.000	0.000	0.000	0.000
86	A	87	PHE	0	-0.028	-0.004	44.236	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	PHE	0	0.015	0.013	47.106	0.000	0.000	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.952	0.969	49.554	-0.019	-0.019	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.030	0.024	46.511	0.000	0.000	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.086	-0.060	49.571	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.850	-0.916	44.413	0.031	0.031	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.019	-0.009	47.016	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.006	-0.004	43.152	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	ILE	0	-0.049	-0.033	40.361	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.937	0.996	37.063	-0.037	-0.037	0.000	0.000	0.000	0.000
96	A	97	TYR	0	0.014	0.002	38.114	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.022	-0.019	34.547	0.001	0.001	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.881	-0.950	32.388	0.040	0.040	0.000	0.000	0.000	0.000
99	A	100	CYS	0	0.045	0.036	28.530	0.005	0.005	0.000	0.000	0.000	0.000
100	A	101	PHE	0	0.036	0.017	26.997	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.048	-0.014	25.304	0.003	0.003	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.015	0.003	20.908	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.856	-0.936	25.483	0.069	0.069	0.000	0.000	0.000	0.000
104	A	105	LYN	0	-0.004	-0.004	27.468	0.003	0.003	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.002	0.000	28.455	0.003	0.003	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.062	-0.078	28.835	0.001	0.001	0.000	0.000	0.000	0.000
107	A	108	VAL	0	-0.017	-0.006	24.689	0.008	0.008	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.021	-0.022	23.155	0.011	0.011	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.946	0.972	23.395	-0.136	-0.136	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.012	0.057	24.803	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	TRP	0	-0.040	-0.046	22.861	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	113	VAL	0	-0.046	-0.020	27.894	-0.006	-0.006	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.033	0.017	30.385	0.002	0.002	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.041	-0.042	29.655	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	116	PRO	0	-0.022	-0.010	32.379	0.000	0.000	0.000	0.000	0.000	0.000
116	A	118	GLU	-1	-0.854	-0.934	30.518	0.038	0.038	0.000	0.000	0.000	0.000
117	A	119	ASN	0	-0.079	-0.037	31.672	0.000	0.000	0.000	0.000	0.000	0.000
118	A	120	THR	0	0.027	0.001	29.129	0.002	0.002	0.000	0.000	0.000	0.000
119	A	121	PHE	0	-0.026	-0.024	26.835	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	122	PRO	0	-0.032	-0.014	22.669	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.029	0.006	18.560	0.002	0.002	0.000	0.000	0.000	0.000
122	A	124	MET	0	0.038	0.050	13.237	0.012	0.012	0.000	0.000	0.000	0.000
123	A	126	LYS	1	0.900	0.922	11.448	-0.207	-0.207	0.000	0.000	0.000	0.000
124	A	127	TYR	0	0.030	0.030	7.553	-0.014	-0.014	0.000	0.000	0.000	0.000
125	A	128	PRO	0	0.010	0.026	8.056	0.077	0.077	0.000	0.000	0.000	0.000
126	A	129	VAL	0	0.114	0.038	3.156	-0.462	0.175	0.031	-0.163	-0.506	0.000
127	A	130	PRO	0	-0.079	-0.029	6.318	0.141	0.141	0.000	0.000	0.000	0.000
128	A	131	ARG	1	0.949	0.983	8.726	0.155	0.155	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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