FMO DATABASE

FMODB ID: Z64LN

Calculation Name: 2RBB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2RBB

Chain ID: A

ChEMBL ID:

UniProt ID: B2TEV0

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	OptAll
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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1099106.48066
FMO2-HF: Nuclear repulsion	1047932.619448
FMO2-HF: Total energy	-51173.861211
FMO2-MP2: Total energy	-51323.808988

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:32:ASN)

Summations of interaction energy for fragment #1(A:32:ASN)

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.
-16.34	-11.299	1.209	-2.816	-3.434	-0.021

Interaction energy analysis for fragmet #1(A:32:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.020 / q_NPA : -0.020

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

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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	34	ALA	0	-0.002	0.000	3.101	-0.850	1.265	0.012	-0.933	-1.194	0.002
4	A	35	ASP	-1	-0.863	-0.953	2.492	-18.516	-15.715	1.197	-1.853	-2.144	-0.023
5	A	36	LEU	0	-0.050	0.000	4.281	2.353	2.478	0.000	-0.030	-0.096	0.000
6	A	37	SER	0	0.056	0.035	6.980	0.846	0.846	0.000	0.000	0.000	0.000
7	A	38	TYR	0	0.012	-0.004	8.230	0.571	0.571	0.000	0.000	0.000	0.000
8	A	39	VAL	0	-0.033	-0.005	11.671	-0.046	-0.046	0.000	0.000	0.000	0.000
9	A	40	ASN	0	-0.004	-0.012	14.030	0.094	0.094	0.000	0.000	0.000	0.000
10	A	41	ILE	0	-0.013	-0.002	17.422	0.037	0.037	0.000	0.000	0.000	0.000
11	A	42	PHE	0	-0.014	-0.002	21.010	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	43	THR	0	-0.030	-0.018	24.118	0.014	0.014	0.000	0.000	0.000	0.000
13	A	44	ARG	1	0.897	0.939	26.734	0.380	0.380	0.000	0.000	0.000	0.000
14	A	45	ASP	-1	-0.830	-0.913	29.555	-0.396	-0.396	0.000	0.000	0.000	0.000
15	A	46	ILE	0	-0.034	-0.012	25.206	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	47	VAL	0	-0.022	-0.006	25.855	-0.036	-0.036	0.000	0.000	0.000	0.000
17	A	48	ALA	0	0.011	0.003	28.107	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	49	MET	0	-0.033	0.007	24.280	0.001	0.001	0.000	0.000	0.000	0.000
19	A	50	SER	0	0.000	-0.013	23.570	-0.047	-0.047	0.000	0.000	0.000	0.000
20	A	51	ALA	0	0.015	0.004	24.584	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	52	PHE	0	-0.012	-0.004	25.540	0.015	0.015	0.000	0.000	0.000	0.000
22	A	53	TYR	0	-0.025	-0.052	21.717	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	54	GLN	0	-0.004	0.002	23.085	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	55	GLN	0	-0.068	-0.028	24.465	0.030	0.030	0.000	0.000	0.000	0.000
25	A	56	VAL	0	-0.047	-0.014	25.522	0.032	0.032	0.000	0.000	0.000	0.000
26	A	57	PHE	0	-0.017	-0.021	21.346	0.021	0.021	0.000	0.000	0.000	0.000
27	A	58	GLY	0	0.005	0.020	22.237	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	59	PHE	0	-0.012	-0.003	17.825	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	60	GLN	0	-0.017	-0.014	19.625	0.078	0.078	0.000	0.000	0.000	0.000
30	A	61	GLU	-1	-0.797	-0.897	19.490	-0.718	-0.718	0.000	0.000	0.000	0.000
31	A	62	ILE	0	-0.008	0.001	14.968	0.020	0.020	0.000	0.000	0.000	0.000
32	A	63	GLU	-1	-0.933	-0.983	19.264	-0.547	-0.547	0.000	0.000	0.000	0.000
33	A	64	SER	0	-0.051	-0.027	18.200	0.027	0.027	0.000	0.000	0.000	0.000
34	A	65	ILE	0	-0.033	-0.016	15.971	-0.020	-0.020	0.000	0.000	0.000	0.000
35	A	66	ARG	1	0.851	0.934	19.839	0.556	0.556	0.000	0.000	0.000	0.000
36	A	67	SER	0	0.008	0.005	22.949	0.048	0.048	0.000	0.000	0.000	0.000
37	A	68	PRO	0	-0.024	-0.033	25.280	0.012	0.012	0.000	0.000	0.000	0.000
38	A	69	ILE	0	0.025	0.022	24.838	0.022	0.022	0.000	0.000	0.000	0.000
39	A	70	PHE	0	0.006	0.017	17.204	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	71	ARG	1	0.862	0.937	22.197	0.618	0.618	0.000	0.000	0.000	0.000
41	A	72	GLY	0	0.066	0.030	18.083	-0.047	-0.047	0.000	0.000	0.000	0.000
42	A	73	LEU	0	-0.051	-0.009	17.495	0.073	0.073	0.000	0.000	0.000	0.000
43	A	74	ASP	-1	-0.802	-0.920	14.210	-1.509	-1.509	0.000	0.000	0.000	0.000
44	A	75	THR	0	-0.051	-0.046	12.868	0.098	0.098	0.000	0.000	0.000	0.000
45	A	76	GLY	0	-0.016	0.000	12.683	0.097	0.097	0.000	0.000	0.000	0.000
46	A	77	LYS	1	0.857	0.915	8.999	1.272	1.272	0.000	0.000	0.000	0.000
47	A	78	SER	0	0.000	-0.005	8.172	-0.061	-0.061	0.000	0.000	0.000	0.000
48	A	79	CYS	0	-0.025	0.027	9.789	0.456	0.456	0.000	0.000	0.000	0.000
49	A	80	ILE	0	0.003	0.001	12.928	-0.044	-0.044	0.000	0.000	0.000	0.000
50	A	81	GLY	0	0.044	0.013	16.070	0.055	0.055	0.000	0.000	0.000	0.000
51	A	82	PHE	0	-0.028	-0.011	18.314	0.028	0.028	0.000	0.000	0.000	0.000
52	A	83	ASN	0	0.015	-0.006	20.768	0.038	0.038	0.000	0.000	0.000	0.000
53	A	84	ALA	0	0.068	0.042	23.319	0.027	0.027	0.000	0.000	0.000	0.000
54	A	85	HIS	0	0.002	-0.025	26.606	0.004	0.004	0.000	0.000	0.000	0.000
55	A	86	GLU	-1	-0.879	-0.944	28.628	-0.418	-0.418	0.000	0.000	0.000	0.000
56	A	87	ALA	0	-0.031	-0.018	23.484	0.000	0.000	0.000	0.000	0.000	0.000
57	A	88	TYR	0	0.007	-0.001	24.724	-0.033	-0.033	0.000	0.000	0.000	0.000
58	A	89	GLU	-1	-0.850	-0.924	26.577	-0.363	-0.363	0.000	0.000	0.000	0.000
59	A	90	LEU	0	-0.046	-0.015	25.367	0.004	0.004	0.000	0.000	0.000	0.000
60	A	91	MET	0	-0.052	-0.019	20.661	-0.071	-0.071	0.000	0.000	0.000	0.000
61	A	92	GLN	0	-0.066	-0.036	24.115	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	93	LEU	0	0.000	-0.007	21.783	0.021	0.021	0.000	0.000	0.000	0.000
63	A	94	ALA	0	0.037	0.020	26.477	0.007	0.007	0.000	0.000	0.000	0.000
64	A	95	GLN	0	-0.050	-0.014	28.141	0.032	0.032	0.000	0.000	0.000	0.000
65	A	96	PHE	0	-0.042	-0.024	25.486	0.013	0.013	0.000	0.000	0.000	0.000
66	A	97	SER	0	-0.026	-0.021	28.759	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	98	GLU	-1	-0.965	-0.963	30.111	-0.260	-0.260	0.000	0.000	0.000	0.000
68	A	99	THR	0	-0.049	-0.025	27.249	0.018	0.018	0.000	0.000	0.000	0.000
69	A	100	SER	0	-0.022	-0.014	30.349	0.021	0.021	0.000	0.000	0.000	0.000
70	A	101	GLY	0	-0.020	-0.004	30.289	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	102	ILE	0	0.009	0.003	25.699	-0.020	-0.020	0.000	0.000	0.000	0.000
72	A	103	LYS	1	0.939	0.959	22.714	0.457	0.457	0.000	0.000	0.000	0.000
73	A	104	PHE	0	-0.013	-0.003	19.370	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	105	LEU	0	-0.007	0.001	19.429	0.058	0.058	0.000	0.000	0.000	0.000
75	A	106	LEU	0	0.038	0.032	16.723	-0.082	-0.082	0.000	0.000	0.000	0.000
76	A	107	ASN	0	-0.037	-0.031	17.072	0.171	0.171	0.000	0.000	0.000	0.000
77	A	108	PHE	0	0.034	0.025	17.223	-0.089	-0.089	0.000	0.000	0.000	0.000
78	A	109	ASP	-1	-0.838	-0.910	16.443	-0.500	-0.500	0.000	0.000	0.000	0.000
79	A	110	VAL	0	-0.013	-0.011	19.292	-0.028	-0.028	0.000	0.000	0.000	0.000
80	A	111	ASP	-1	-0.830	-0.912	21.904	-0.220	-0.220	0.000	0.000	0.000	0.000
81	A	112	THR	0	-0.056	-0.033	23.318	0.036	0.036	0.000	0.000	0.000	0.000
82	A	113	LYS	1	0.914	0.965	26.618	0.097	0.097	0.000	0.000	0.000	0.000
83	A	114	GLU	-1	-0.811	-0.932	28.582	-0.158	-0.158	0.000	0.000	0.000	0.000
84	A	115	ALA	0	-0.058	-0.021	26.248	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	116	VAL	0	-0.006	0.003	25.410	-0.021	-0.021	0.000	0.000	0.000	0.000
86	A	117	ASP	-1	-0.851	-0.915	27.818	-0.189	-0.189	0.000	0.000	0.000	0.000
87	A	118	LYS	1	0.889	0.947	30.309	0.199	0.199	0.000	0.000	0.000	0.000
88	A	119	LEU	0	0.013	0.018	25.168	0.002	0.002	0.000	0.000	0.000	0.000
89	A	120	VAL	0	0.010	0.007	29.347	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	121	PRO	0	-0.015	-0.010	30.818	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	122	VAL	0	0.018	0.014	29.896	0.002	0.002	0.000	0.000	0.000	0.000
92	A	123	ALA	0	0.034	0.011	28.344	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	124	ILE	0	-0.028	-0.020	30.001	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	125	ALA	0	-0.046	-0.016	33.354	0.003	0.003	0.000	0.000	0.000	0.000
95	A	126	ALA	0	-0.010	0.003	30.349	0.003	0.003	0.000	0.000	0.000	0.000
96	A	127	GLY	0	0.006	0.001	32.007	-0.014	-0.014	0.000	0.000	0.000	0.000
97	A	128	ALA	0	-0.044	-0.007	29.558	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	129	THR	0	-0.043	-0.022	31.269	0.029	0.029	0.000	0.000	0.000	0.000
99	A	130	LEU	0	0.019	0.003	31.616	-0.015	-0.015	0.000	0.000	0.000	0.000
100	A	131	ILE	0	-0.045	-0.018	30.822	0.013	0.013	0.000	0.000	0.000	0.000
101	A	132	LYS	1	0.860	0.935	30.506	0.197	0.197	0.000	0.000	0.000	0.000
102	A	133	ALA	0	0.055	0.027	31.090	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	134	PRO	0	0.006	0.006	30.560	0.000	0.000	0.000	0.000	0.000	0.000
104	A	135	TYR	0	-0.070	-0.036	26.970	0.028	0.028	0.000	0.000	0.000	0.000
105	A	136	GLU	-1	-0.790	-0.898	28.366	-0.100	-0.100	0.000	0.000	0.000	0.000
106	A	137	THR	0	-0.044	-0.005	24.595	0.018	0.018	0.000	0.000	0.000	0.000
107	A	138	TYR	0	0.055	0.012	25.164	0.006	0.006	0.000	0.000	0.000	0.000
108	A	139	TYR	0	-0.017	-0.002	22.138	0.011	0.011	0.000	0.000	0.000	0.000
109	A	140	HIS	1	0.836	0.903	23.863	0.048	0.048	0.000	0.000	0.000	0.000
110	A	141	TRP	0	0.035	0.018	17.075	-0.018	-0.018	0.000	0.000	0.000	0.000
111	A	142	TYR	0	-0.047	-0.049	24.317	0.013	0.013	0.000	0.000	0.000	0.000
112	A	143	GLN	0	0.018	-0.005	23.177	-0.026	-0.026	0.000	0.000	0.000	0.000
113	A	144	ALA	0	0.027	0.022	26.535	0.028	0.028	0.000	0.000	0.000	0.000
114	A	145	VAL	0	-0.026	-0.020	26.358	-0.033	-0.033	0.000	0.000	0.000	0.000
115	A	146	LEU	0	0.014	0.006	27.164	0.034	0.034	0.000	0.000	0.000	0.000
116	A	147	LEU	0	-0.028	-0.003	27.304	-0.020	-0.020	0.000	0.000	0.000	0.000
117	A	148	ASP	-1	-0.710	-0.828	24.969	-0.497	-0.497	0.000	0.000	0.000	0.000
118	A	149	PRO	0	0.018	-0.006	27.938	0.019	0.019	0.000	0.000	0.000	0.000
119	A	150	GLU	-1	-0.810	-0.895	27.990	-0.436	-0.436	0.000	0.000	0.000	0.000
120	A	151	ARG	1	0.867	0.938	28.930	0.307	0.307	0.000	0.000	0.000	0.000
121	A	152	ASN	0	0.003	-0.013	23.692	0.006	0.006	0.000	0.000	0.000	0.000
122	A	153	VAL	0	-0.019	-0.012	24.421	0.013	0.013	0.000	0.000	0.000	0.000
123	A	154	PHE	0	0.010	0.005	22.295	-0.056	-0.056	0.000	0.000	0.000	0.000
124	A	155	ARG	1	0.815	0.902	20.065	0.447	0.447	0.000	0.000	0.000	0.000
125	A	156	ILE	0	0.039	0.037	22.260	-0.050	-0.050	0.000	0.000	0.000	0.000
126	A	157	ASN	0	-0.001	-0.028	19.779	0.081	0.081	0.000	0.000	0.000	0.000
127	A	158	ASN	0	0.013	0.000	22.251	0.002	0.002	0.000	0.000	0.000	0.000
128	A	159	VAL	0	-0.011	0.000	18.489	0.028	0.028	0.000	0.000	0.000	0.000
129	A	160	LEU	0	-0.030	0.003	21.757	0.023	0.023	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:32:ASN)