FMO DATABASE

FMODB ID: 853GY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1235113.602968
FMO2-HF: Nuclear repulsion	1177340.701086
FMO2-HF: Total energy	-57772.901882
FMO2-MP2: Total energy	-57933.515587

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.
58.797	62.235	0.107	-1.416	-2.132	0.003

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 : -0.941 / q_NPA : -0.979

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	0.059	0.040	3.375	3.090	5.466	0.035	-1.082	-1.329	0.002
4	A	4	ASP	-1	-0.846	-0.925	5.597	33.739	33.869	-0.001	-0.004	-0.126	0.000
5	A	5	GLY	0	-0.071	-0.047	7.640	-2.432	-2.432	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.046	-0.022	7.467	-3.256	-3.256	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.029	-0.015	7.994	1.068	1.068	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.073	0.024	5.326	0.126	0.126	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.046	-0.015	7.251	-1.656	-1.656	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.936	0.963	6.947	-19.765	-19.765	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.051	0.012	6.807	2.772	2.772	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.002	0.014	8.494	0.653	0.653	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.044	-0.063	8.439	-1.641	-1.641	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.936	0.975	11.439	-21.315	-21.315	0.000	0.000	0.000	0.000
15	A	16	PRO	0	0.006	0.013	13.731	-0.768	-0.768	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.015	-0.002	15.118	0.578	0.578	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.986	0.982	19.527	-13.725	-13.725	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.933	-0.966	21.067	13.981	13.981	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.915	0.956	24.415	-10.168	-10.168	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.890	0.948	22.749	-13.122	-13.122	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.080	0.060	27.558	0.158	0.158	0.000	0.000	0.000	0.000
22	A	23	TRP	0	0.029	0.008	25.251	0.434	0.434	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.785	-0.917	25.750	10.616	10.616	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.905	-0.959	25.586	11.070	11.070	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.034	-0.003	22.953	0.576	0.576	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.758	-0.878	20.991	15.163	15.163	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.948	0.983	20.686	-11.144	-11.144	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.062	0.030	18.195	0.422	0.422	0.000	0.000	0.000	0.000
29	A	30	CYS	0	-0.098	0.001	14.807	0.246	0.246	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.057	-0.043	16.026	0.959	0.959	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.926	-0.969	17.184	14.297	14.297	0.000	0.000	0.000	0.000
32	A	33	GLN	0	-0.121	-0.052	12.890	1.409	1.409	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.935	-0.968	8.497	32.584	32.584	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.853	0.952	7.943	-23.318	-23.318	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.935	-0.958	10.655	16.822	16.822	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.051	-0.036	12.727	1.078	1.078	0.000	0.000	0.000	0.000
37	A	38	HIS	1	0.841	0.890	14.202	-16.994	-16.994	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.036	0.022	16.794	0.767	0.767	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.051	-0.018	16.536	0.182	0.182	0.000	0.000	0.000	0.000
40	A	41	SER	0	0.069	0.030	17.681	-0.567	-0.567	0.000	0.000	0.000	0.000
41	A	42	MET	0	-0.073	-0.038	17.934	0.587	0.587	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.890	-0.946	18.813	14.474	14.474	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.025	-0.018	18.512	-0.350	-0.350	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.993	0.991	21.389	-10.719	-10.719	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.021	0.002	19.182	0.002	0.002	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.732	-0.817	15.705	17.327	17.327	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.033	0.008	18.096	0.288	0.288	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.040	-0.034	20.928	-0.161	-0.161	0.000	0.000	0.000	0.000
49	A	50	PHE	0	0.007	0.004	11.782	-0.063	-0.063	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.037	0.003	16.459	0.341	0.341	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.795	-0.873	17.810	12.222	12.222	0.000	0.000	0.000	0.000
52	A	53	MET	0	-0.013	-0.004	18.355	-0.199	-0.199	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.000	0.011	14.102	0.110	0.110	0.000	0.000	0.000	0.000
54	A	55	MET	0	-0.034	0.005	17.121	0.347	0.347	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.825	-0.926	20.001	11.613	11.613	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.063	-0.027	16.683	-0.875	-0.875	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.076	-0.043	16.387	-0.239	-0.239	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.066	-0.042	19.775	-0.304	-0.304	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.967	-0.985	23.172	10.587	10.587	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.051	-0.024	24.370	-0.203	-0.203	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.896	0.966	26.148	-10.523	-10.523	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.046	0.024	27.310	0.200	0.200	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.110	-0.080	23.278	0.274	0.274	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.871	0.935	27.679	-9.551	-9.551	0.000	0.000	0.000	0.000
65	A	66	SER	0	0.000	0.002	22.606	0.276	0.276	0.000	0.000	0.000	0.000
66	A	67	TRP	0	-0.038	-0.018	24.086	-0.112	-0.112	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.012	-0.020	22.300	0.619	0.619	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.044	0.029	21.999	-0.415	-0.415	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.078	-0.036	22.969	-0.096	-0.096	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.834	0.912	26.498	-9.828	-9.828	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.084	-0.037	29.505	0.036	0.036	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.832	-0.932	32.811	9.115	9.115	0.000	0.000	0.000	0.000
73	A	74	ASN	0	0.030	0.020	35.515	0.182	0.182	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.952	1.002	37.765	-7.760	-7.760	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.009	0.016	37.215	0.193	0.193	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.036	-0.013	35.351	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.908	0.986	27.654	-10.247	-10.247	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.003	0.014	32.648	0.168	0.168	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.044	-0.030	33.770	0.088	0.088	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.029	-0.021	34.824	-0.171	-0.171	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.928	-0.967	36.122	8.609	8.609	0.000	0.000	0.000	0.000
82	A	83	TRP	0	-0.028	0.005	38.666	-0.263	-0.263	0.000	0.000	0.000	0.000
83	A	84	SER	0	-0.006	-0.017	40.672	0.098	0.098	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.883	-0.934	42.191	7.032	7.032	0.000	0.000	0.000	0.000
85	A	86	GLY	0	-0.009	-0.004	39.183	0.012	0.012	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.082	-0.034	39.392	0.140	0.140	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.014	-0.020	38.921	0.067	0.067	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.011	0.010	38.472	-0.216	-0.216	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.029	-0.022	40.530	0.038	0.038	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.013	-0.016	43.024	-0.136	-0.136	0.000	0.000	0.000	0.000
91	A	92	GLH	0	-0.042	-0.061	41.262	0.111	0.111	0.000	0.000	0.000	0.000
92	A	93	ASN	0	-0.024	-0.011	45.894	-0.045	-0.045	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.013	0.009	42.807	-0.101	-0.101	0.000	0.000	0.000	0.000
94	A	95	TYR	0	0.010	0.009	47.500	-0.057	-0.057	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.893	-0.930	42.565	7.266	7.266	0.000	0.000	0.000	0.000
96	A	97	PRO	0	0.023	0.007	44.624	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.005	-0.011	41.391	0.116	0.116	0.000	0.000	0.000	0.000
98	A	99	MET	0	-0.079	-0.045	39.760	-0.090	-0.090	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.813	-0.907	34.158	9.027	9.027	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.909	0.958	34.419	-8.187	-8.187	0.000	0.000	0.000	0.000
101	A	102	CYS	0	-0.013	0.008	29.403	0.449	0.449	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.019	-0.014	27.687	-0.286	-0.286	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.001	0.013	26.554	0.401	0.401	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.047	-0.015	20.680	-0.320	-0.320	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.847	-0.913	26.765	9.698	9.698	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.065	-0.038	25.573	-0.465	-0.465	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.041	-0.046	28.502	-0.349	-0.349	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.038	-0.012	31.246	-0.141	-0.141	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.032	0.002	28.804	-0.172	-0.172	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.021	-0.013	23.738	0.116	0.116	0.000	0.000	0.000	0.000
111	A	112	PRO	0	0.042	0.041	24.997	-0.406	-0.406	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.896	0.943	27.311	-9.201	-9.201	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.023	-0.008	23.766	0.068	0.068	0.000	0.000	0.000	0.000
114	A	115	HIS	0	-0.024	-0.003	29.159	-0.416	-0.416	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.038	-0.019	30.972	0.152	0.152	0.000	0.000	0.000	0.000
116	A	117	ALA	0	-0.035	-0.015	32.162	-0.179	-0.179	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.828	-0.923	34.042	8.641	8.641	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.841	-0.919	31.500	9.625	9.625	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.857	-0.904	32.326	9.259	9.259	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.824	0.916	29.961	-9.991	-9.991	0.000	0.000	0.000	0.000
121	A	123	ASN	0	-0.052	-0.035	27.419	-0.244	-0.244	0.000	0.000	0.000	0.000
122	A	124	VAL	0	-0.016	-0.002	23.416	0.207	0.207	0.000	0.000	0.000	0.000
123	A	125	PHE	0	-0.008	-0.005	19.520	-0.309	-0.309	0.000	0.000	0.000	0.000
124	A	126	MET	0	0.030	0.020	15.702	0.493	0.493	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.869	0.917	12.778	-17.027	-17.027	0.000	0.000	0.000	0.000
126	A	129	PHE	0	0.013	-0.006	6.316	-1.205	-1.205	0.000	0.000	0.000	0.000
127	A	130	GLN	0	-0.042	-0.018	9.695	0.967	0.967	0.000	0.000	0.000	0.000
128	A	131	LEU	0	0.025	0.004	3.095	-1.259	-0.470	0.074	-0.324	-0.540	0.001
129	A	132	PRO	0	0.003	0.004	4.482	-2.862	-2.719	-0.001	-0.006	-0.137	0.000

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