FMO DATABASE

FMODB ID: N95ZQ

Calculation Name: 1SB2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SB2

Chain ID: A

ChEMBL ID:

UniProt ID: P81397

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:

Apendix: None

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	129
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1237200.854076
FMO2-HF: Nuclear repulsion	1179426.813935
FMO2-HF: Total energy	-57774.040141
FMO2-MP2: Total energy	-57934.676521

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:ASP)

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

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.
55.803	59.21	0.133	-1.402	-2.137	0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.959 / q_NPA : -0.990

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	3	PRO	0	0.056	0.039	3.474	3.128	5.295	0.018	-0.955	-1.230	0.002
4	A	4	ASP	-1	-0.838	-0.917	5.731	32.540	32.654	-0.001	-0.003	-0.109	0.000
5	A	5	GLY	0	-0.067	-0.051	7.742	-2.425	-2.425	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.046	-0.018	7.554	-3.261	-3.261	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.024	-0.007	8.038	1.128	1.128	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.064	0.023	5.345	0.376	0.376	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.047	-0.023	7.252	-1.696	-1.696	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.937	0.966	6.927	-20.167	-20.167	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.039	0.003	6.765	2.666	2.666	0.000	0.000	0.000	0.000
12	A	12	TYR	0	-0.021	0.003	8.445	1.034	1.034	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.038	-0.070	8.418	-1.666	-1.666	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.903	0.962	11.165	-22.106	-22.106	0.000	0.000	0.000	0.000
15	A	16	PRO	0	-0.014	0.012	13.734	-0.751	-0.751	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.015	-0.005	15.253	0.560	0.560	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.916	0.950	19.607	-14.011	-14.011	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.865	-0.936	21.050	13.830	13.830	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.923	0.957	24.503	-10.053	-10.053	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.833	0.925	22.336	-13.630	-13.630	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.052	0.034	27.558	0.127	0.127	0.000	0.000	0.000	0.000
22	A	23	TRP	0	0.019	0.000	25.361	0.447	0.447	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.750	-0.898	25.901	10.743	10.743	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.869	-0.916	25.719	11.061	11.061	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.034	-0.005	23.055	0.565	0.565	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.724	-0.852	20.919	15.143	15.143	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.896	0.968	20.826	-11.194	-11.194	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.080	0.037	18.341	0.501	0.501	0.000	0.000	0.000	0.000
29	A	30	CYS	0	-0.102	-0.006	14.859	0.287	0.287	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.048	-0.037	16.148	0.898	0.898	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.943	-0.983	17.288	14.153	14.153	0.000	0.000	0.000	0.000
32	A	33	GLN	0	-0.109	-0.044	13.046	1.369	1.369	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.935	-0.965	9.427	30.401	30.401	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.783	0.896	7.951	-22.793	-22.793	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.811	-0.884	10.737	18.010	18.010	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.028	-0.009	12.844	1.078	1.078	0.000	0.000	0.000	0.000
37	A	38	HIS	1	0.788	0.847	14.359	-17.043	-17.043	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.015	0.012	16.973	0.753	0.753	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.054	-0.021	16.511	0.175	0.175	0.000	0.000	0.000	0.000
40	A	41	SER	0	0.023	-0.004	17.649	-0.620	-0.620	0.000	0.000	0.000	0.000
41	A	42	MET	0	-0.056	-0.029	17.902	0.595	0.595	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.747	-0.859	17.290	15.621	15.621	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.028	-0.015	18.135	-0.546	-0.546	0.000	0.000	0.000	0.000
44	A	45	ARG	1	1.007	0.995	21.361	-10.740	-10.740	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.019	0.004	19.235	-0.015	-0.015	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.732	-0.811	15.362	17.572	17.572	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.038	0.011	18.074	0.284	0.284	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.041	-0.032	20.910	-0.172	-0.172	0.000	0.000	0.000	0.000
49	A	50	PHE	0	0.001	-0.001	11.758	-0.073	-0.073	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.043	0.006	16.378	0.339	0.339	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.778	-0.867	17.803	12.152	12.152	0.000	0.000	0.000	0.000
52	A	53	MET	0	-0.025	-0.008	18.524	-0.226	-0.226	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.000	0.006	14.078	0.095	0.095	0.000	0.000	0.000	0.000
54	A	55	MET	0	-0.029	0.002	17.132	0.332	0.332	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.829	-0.926	20.010	11.628	11.628	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.065	-0.029	16.552	-0.734	-0.734	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.052	-0.024	16.670	-0.285	-0.285	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.008	-0.019	19.819	-0.274	-0.274	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.846	-0.916	23.208	10.521	10.521	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.071	-0.033	24.396	-0.188	-0.188	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.791	0.908	26.170	-11.029	-11.029	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.033	0.020	27.323	0.212	0.212	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.081	-0.070	23.264	0.275	0.275	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.817	0.872	27.686	-9.518	-9.518	0.000	0.000	0.000	0.000
65	A	66	SER	0	-0.008	-0.003	22.594	0.286	0.286	0.000	0.000	0.000	0.000
66	A	67	TRP	0	-0.031	-0.013	24.174	-0.119	-0.119	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.010	-0.018	22.279	0.611	0.611	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.051	0.033	22.090	-0.409	-0.409	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.083	-0.041	23.036	-0.099	-0.099	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.805	0.880	26.583	-9.760	-9.760	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.071	-0.023	29.701	0.036	0.036	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.749	-0.875	32.385	9.446	9.446	0.000	0.000	0.000	0.000
73	A	74	ASN	0	0.017	0.006	35.706	0.153	0.153	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.954	0.993	37.943	-7.768	-7.768	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.016	0.016	37.392	0.194	0.194	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.050	0.012	35.362	-0.113	-0.113	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.830	0.924	27.812	-10.141	-10.141	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.008	0.005	32.837	0.141	0.141	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.042	-0.031	33.973	0.186	0.186	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.044	-0.029	35.030	-0.166	-0.166	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.913	-0.959	36.392	8.635	8.635	0.000	0.000	0.000	0.000
82	A	83	TRP	0	-0.037	0.003	38.872	-0.253	-0.253	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.030	-0.001	40.878	0.087	0.087	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.911	-0.935	42.399	7.053	7.053	0.000	0.000	0.000	0.000
85	A	86	GLY	0	-0.003	0.002	39.380	0.010	0.010	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.084	-0.049	39.581	0.133	0.133	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.015	-0.012	39.085	0.101	0.101	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.007	-0.007	38.803	-0.227	-0.227	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.036	-0.025	40.707	0.087	0.087	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.017	-0.016	43.197	-0.131	-0.131	0.000	0.000	0.000	0.000
91	A	92	GLH	0	-0.040	-0.043	41.580	0.129	0.129	0.000	0.000	0.000	0.000
92	A	93	ASN	0	-0.023	-0.014	46.080	-0.097	-0.097	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.007	0.011	42.948	-0.116	-0.116	0.000	0.000	0.000	0.000
94	A	95	TYR	0	0.006	0.006	47.697	-0.055	-0.055	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.884	-0.921	42.811	7.254	7.254	0.000	0.000	0.000	0.000
96	A	97	PRO	0	0.019	0.005	44.904	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.000	-0.014	41.552	0.102	0.102	0.000	0.000	0.000	0.000
98	A	99	MET	0	-0.063	-0.036	39.882	-0.088	-0.088	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.833	-0.907	34.559	8.920	8.920	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.917	0.961	34.487	-8.144	-8.144	0.000	0.000	0.000	0.000
101	A	102	CYS	0	0.005	0.026	29.483	0.406	0.406	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.024	-0.010	27.745	-0.290	-0.290	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.004	0.011	26.533	0.398	0.398	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.051	-0.017	20.541	-0.320	-0.320	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.832	-0.905	26.752	9.721	9.721	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.055	-0.035	25.471	-0.519	-0.519	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.039	-0.033	28.501	-0.309	-0.309	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.055	0.005	31.255	-0.138	-0.138	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.050	-0.015	28.803	-0.173	-0.173	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.009	-0.001	23.768	0.094	0.094	0.000	0.000	0.000	0.000
111	A	112	PRO	0	0.025	0.030	24.985	-0.461	-0.461	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.858	0.929	27.296	-9.508	-9.508	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.014	-0.014	23.541	0.107	0.107	0.000	0.000	0.000	0.000
114	A	115	HIS	0	-0.005	0.007	29.138	-0.440	-0.440	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.018	-0.004	30.951	0.194	0.194	0.000	0.000	0.000	0.000
116	A	117	ALA	0	-0.052	-0.029	32.125	-0.188	-0.188	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.831	-0.924	34.020	8.604	8.604	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.856	-0.933	31.624	9.571	9.571	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.842	-0.872	32.274	9.238	9.238	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.786	0.876	30.076	-9.900	-9.900	0.000	0.000	0.000	0.000
121	A	123	ASN	0	-0.056	-0.040	27.412	-0.248	-0.248	0.000	0.000	0.000	0.000
122	A	124	VAL	0	-0.003	0.010	23.490	0.207	0.207	0.000	0.000	0.000	0.000
123	A	125	PHE	0	-0.009	-0.007	19.316	-0.324	-0.324	0.000	0.000	0.000	0.000
124	A	126	MET	0	0.035	0.027	15.916	0.530	0.530	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.816	0.888	12.748	-16.897	-16.897	0.000	0.000	0.000	0.000
126	A	129	PHE	0	0.023	-0.001	6.448	-0.970	-0.970	0.000	0.000	0.000	0.000
127	A	130	GLN	0	-0.040	-0.015	9.916	0.548	0.548	0.000	0.000	0.000	0.000
128	A	131	LEU	0	0.024	0.004	3.160	-1.551	-0.562	0.117	-0.439	-0.667	0.003
129	A	132	PRO	0	-0.007	-0.001	4.670	-2.842	-2.705	-0.001	-0.005	-0.131	0.000

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