FMO DATABASE

FMODB ID: 14R9Z

Calculation Name: 1B9L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1B9L

Chain ID: A

ChEMBL ID:

UniProt ID: P0AC19

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	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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1004028.581374
FMO2-HF: Nuclear repulsion	955944.327776
FMO2-HF: Total energy	-48084.253599
FMO2-MP2: Total energy	-48227.672145

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-0.611	2.358	0.096	-1.424	-1.64	0.006

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.039 / q_NPA : 0.021

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	4	PRO	0	-0.001	-0.019	3.018	-0.908	1.949	0.097	-1.413	-1.541	0.006
4	A	5	ALA	0	0.030	0.020	4.820	0.173	0.285	-0.001	-0.011	-0.099	0.000
5	A	6	ALA	0	-0.020	0.003	7.886	0.077	0.077	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.023	-0.024	9.498	-0.035	-0.035	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.027	-0.006	12.664	0.070	0.070	0.000	0.000	0.000	0.000
8	A	9	ARG	1	0.935	0.957	14.086	0.116	0.116	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.007	0.009	18.874	0.025	0.025	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.947	0.956	19.150	-0.026	-0.026	0.000	0.000	0.000	0.000
11	A	12	ASN	0	-0.019	-0.023	24.101	0.003	0.003	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.021	0.032	27.700	0.009	0.009	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.935	0.963	29.289	0.007	0.007	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.033	0.022	32.129	0.004	0.004	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.851	0.892	35.371	0.013	0.013	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.006	-0.013	37.432	0.001	0.001	0.000	0.000	0.000	0.000
17	A	18	PHE	0	-0.015	0.003	40.117	0.001	0.001	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.034	0.014	37.319	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	20	GLY	0	0.038	0.034	41.495	0.001	0.001	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.024	-0.033	44.114	0.001	0.001	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.946	0.985	47.074	0.040	0.040	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.845	-0.937	49.330	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.927	-0.955	49.012	-0.024	-0.024	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.857	-0.933	44.288	-0.040	-0.040	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.017	0.003	45.871	0.000	0.000	0.000	0.000	0.000	0.000
26	A	27	ASN	0	-0.025	-0.014	47.983	0.002	0.002	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.048	-0.019	47.578	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.782	0.903	40.034	0.021	0.021	0.000	0.000	0.000	0.000
29	A	30	GLN	0	0.009	-0.003	40.855	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.796	-0.862	37.786	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.009	0.001	33.998	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	33	VAL	0	-0.049	-0.024	29.416	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.025	0.016	27.265	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	35	ASN	0	0.002	0.008	23.913	0.016	0.016	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.026	0.016	21.337	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.018	-0.009	16.722	0.015	0.015	0.000	0.000	0.000	0.000
37	A	38	ILE	0	0.028	0.018	16.151	-0.019	-0.019	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.002	-0.001	12.474	-0.043	-0.043	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.049	0.017	11.746	0.032	0.032	0.000	0.000	0.000	0.000
40	A	41	PRO	0	0.018	0.024	9.027	-0.028	-0.028	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.004	-0.004	5.119	0.122	0.122	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.895	-0.953	7.233	-0.049	-0.049	0.000	0.000	0.000	0.000
43	A	44	LYS	1	1.002	0.995	8.204	0.260	0.260	0.000	0.000	0.000	0.000
44	A	45	ALA	0	-0.050	-0.018	9.773	0.032	0.032	0.000	0.000	0.000	0.000
45	A	46	ARG	1	0.903	0.955	8.125	-0.390	-0.390	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.010	0.015	11.897	0.021	0.021	0.000	0.000	0.000	0.000
47	A	48	SER	0	0.016	-0.007	14.532	-0.039	-0.039	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-1.034	-0.991	16.544	0.218	0.218	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.947	-0.980	17.489	0.109	0.109	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.012	-0.002	16.368	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.009	-0.011	20.267	0.010	0.010	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.947	-0.963	21.414	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	54	ALA	0	-0.002	-0.009	18.649	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.026	0.005	16.348	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	56	ASN	0	0.071	0.023	19.090	0.022	0.022	0.000	0.000	0.000	0.000
56	A	57	TYR	0	0.067	0.022	19.395	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.950	0.976	21.842	-0.050	-0.050	0.000	0.000	0.000	0.000
58	A	59	THR	0	0.006	0.006	24.934	0.001	0.001	0.000	0.000	0.000	0.000
59	A	60	VAL	0	0.043	0.033	22.020	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	61	THR	0	0.016	-0.004	25.009	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.876	0.951	27.158	0.019	0.019	0.000	0.000	0.000	0.000
62	A	63	ASN	0	0.018	-0.001	28.487	0.007	0.007	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.046	0.028	25.874	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.010	0.001	30.248	0.000	0.000	0.000	0.000	0.000	0.000
65	A	66	GLN	0	-0.030	-0.014	32.901	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	HIS	0	-0.014	-0.014	33.177	0.004	0.004	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.030	0.022	32.631	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.891	-0.952	35.575	-0.018	-0.018	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.098	-0.052	38.042	0.004	0.004	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.013	-0.006	37.742	0.000	0.000	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.829	0.913	40.807	0.030	0.030	0.000	0.000	0.000	0.000
72	A	73	PHE	0	-0.010	0.004	36.407	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.008	0.004	40.701	0.001	0.001	0.000	0.000	0.000	0.000
74	A	75	LEU	0	0.013	-0.003	38.763	0.002	0.002	0.000	0.000	0.000	0.000
75	A	76	LEU	0	0.049	0.023	33.701	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.835	-0.920	33.945	-0.078	-0.078	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.912	0.956	33.638	0.069	0.069	0.000	0.000	0.000	0.000
78	A	79	LEU	0	0.035	0.033	33.497	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	80	THR	0	0.009	-0.024	28.934	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	GLN	0	-0.063	-0.035	28.634	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.805	-0.896	29.644	-0.073	-0.073	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.025	-0.018	27.179	0.001	0.001	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.030	-0.016	23.438	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.821	-0.895	25.132	-0.125	-0.125	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.002	0.000	26.141	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	ALA	0	-0.082	-0.036	22.566	0.004	0.004	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.761	0.855	21.301	0.139	0.139	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.952	-0.956	22.336	-0.074	-0.074	0.000	0.000	0.000	0.000
89	A	90	HIS	0	-0.001	-0.009	18.704	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	91	HIS	0	0.064	0.026	20.431	-0.025	-0.025	0.000	0.000	0.000	0.000
91	A	92	TRP	0	-0.051	-0.028	14.982	-0.027	-0.027	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.038	-0.019	15.185	-0.044	-0.044	0.000	0.000	0.000	0.000
93	A	94	THR	0	-0.043	-0.024	12.690	-0.029	-0.029	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.069	-0.069	15.343	-0.029	-0.029	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.006	0.004	16.980	0.018	0.018	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.856	-0.916	19.665	-0.230	-0.230	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.031	-0.020	21.735	0.014	0.014	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.830	-0.880	24.919	-0.101	-0.101	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.051	-0.033	26.912	0.010	0.010	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.821	-0.883	30.175	-0.060	-0.060	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.827	0.905	32.617	0.048	0.048	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.030	-0.045	34.116	0.000	0.000	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.015	0.003	37.561	0.000	0.000	0.000	0.000	0.000	0.000
104	A	105	ALA	0	0.017	0.022	39.354	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.038	-0.015	39.205	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.935	0.965	42.264	0.028	0.028	0.000	0.000	0.000	0.000
107	A	108	TYR	0	-0.035	-0.050	43.740	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.035	0.033	38.553	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.908	-0.942	35.693	-0.030	-0.030	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.090	-0.072	33.225	0.003	0.003	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.019	0.004	35.030	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	113	SER	0	-0.019	-0.031	29.517	0.004	0.004	0.000	0.000	0.000	0.000
113	A	114	MET	0	-0.022	0.004	30.802	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	115	THR	0	0.046	0.011	24.543	0.006	0.006	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.035	-0.006	26.380	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.004	-0.011	21.454	0.002	0.002	0.000	0.000	0.000	0.000
117	A	118	TRP	0	0.017	0.013	19.752	0.005	0.005	0.000	0.000	0.000	0.000
118	A	119	GLN	0	0.003	-0.015	15.885	-0.024	-0.024	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.998	1.019	18.031	0.348	0.348	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)