FMO DATABASE

FMODB ID: JLJ49

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1236962.559256
FMO2-HF: Nuclear repulsion	1179188.157805
FMO2-HF: Total energy	-57774.401451
FMO2-MP2: Total energy	-57935.040237

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.
50.514	53.921	0.539	-1.397	-2.549	0.006

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 : -0.945 / 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	0.066	0.040	3.876	2.261	4.543	-0.004	-0.983	-1.295	0.003
4	A	4	ASP	-1	-0.854	-0.926	5.246	31.383	31.490	-0.001	-0.003	-0.103	0.000
5	A	5	GLY	0	-0.046	-0.025	7.866	-3.073	-3.073	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.097	-0.039	7.460	-3.656	-3.656	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.013	0.001	7.894	1.241	1.241	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.040	0.009	5.558	1.052	1.052	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.024	-0.012	7.427	-1.618	-1.618	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.945	0.961	6.699	-19.493	-19.493	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.008	-0.012	7.139	1.439	1.439	0.000	0.000	0.000	0.000
12	A	12	TYR	0	-0.024	-0.014	8.054	0.431	0.431	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.039	-0.065	8.035	-1.878	-1.878	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.901	0.946	10.379	-23.639	-23.639	0.000	0.000	0.000	0.000
15	A	16	PRO	0	-0.008	0.009	13.569	-0.912	-0.912	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.018	0.009	15.230	0.692	0.692	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.865	0.916	19.657	-14.021	-14.021	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.845	-0.923	21.065	13.987	13.987	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.931	0.966	24.528	-10.042	-10.042	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.804	0.906	22.031	-13.846	-13.846	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.021	0.020	27.286	0.121	0.121	0.000	0.000	0.000	0.000
22	A	23	TRP	0	0.023	0.001	24.666	0.450	0.450	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.754	-0.897	25.366	10.917	10.917	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.876	-0.914	25.759	11.122	11.122	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.007	0.000	22.663	0.548	0.548	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.735	-0.853	20.533	15.279	15.279	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.853	0.944	20.323	-11.597	-11.597	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.071	0.035	18.406	0.597	0.597	0.000	0.000	0.000	0.000
29	A	30	CYS	0	-0.086	0.008	14.771	0.247	0.247	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.058	-0.041	15.833	0.868	0.868	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.899	-0.960	16.928	14.166	14.166	0.000	0.000	0.000	0.000
32	A	33	GLN	0	-0.082	-0.032	13.116	1.482	1.482	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.890	-0.949	9.103	31.057	31.057	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.790	0.887	7.536	-23.118	-23.118	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.832	-0.890	10.609	18.861	18.861	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.022	0.000	12.527	1.032	1.032	0.000	0.000	0.000	0.000
37	A	38	HIS	1	0.806	0.861	14.068	-17.232	-17.232	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.033	0.010	16.656	0.854	0.854	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.049	-0.020	16.292	0.114	0.114	0.000	0.000	0.000	0.000
40	A	41	SER	0	0.001	-0.018	17.281	-0.703	-0.703	0.000	0.000	0.000	0.000
41	A	42	MET	0	-0.027	-0.013	17.353	0.683	0.683	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.718	-0.806	16.639	15.897	15.897	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.012	-0.009	17.488	-0.702	-0.702	0.000	0.000	0.000	0.000
44	A	45	ARG	1	1.007	0.994	20.764	-10.817	-10.817	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.010	0.007	19.112	-0.108	-0.108	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.751	-0.831	14.621	18.174	18.174	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.031	0.008	17.580	0.276	0.276	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.024	-0.019	20.491	-0.179	-0.179	0.000	0.000	0.000	0.000
49	A	50	PHE	0	-0.012	0.002	11.362	-0.166	-0.166	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.046	0.006	16.052	0.412	0.412	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.768	-0.859	17.550	12.239	12.239	0.000	0.000	0.000	0.000
52	A	53	MET	0	-0.033	-0.017	18.464	-0.211	-0.211	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.003	0.002	13.883	0.059	0.059	0.000	0.000	0.000	0.000
54	A	55	MET	0	-0.033	0.000	16.978	0.382	0.382	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.817	-0.912	19.954	11.613	11.613	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.041	-0.022	16.755	-0.710	-0.710	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.038	-0.011	16.977	-0.346	-0.346	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.001	-0.018	19.823	-0.382	-0.382	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.861	-0.918	23.073	11.147	11.147	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.081	-0.035	24.422	-0.221	-0.221	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.812	0.884	26.176	-11.592	-11.592	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.004	0.016	27.404	0.290	0.290	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.047	-0.049	23.108	0.147	0.147	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.812	0.872	27.618	-9.612	-9.612	0.000	0.000	0.000	0.000
65	A	66	SER	0	-0.006	-0.008	22.530	0.286	0.286	0.000	0.000	0.000	0.000
66	A	67	TRP	0	-0.027	-0.009	23.973	-0.076	-0.076	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.002	-0.011	21.852	0.566	0.566	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.029	0.027	21.291	-0.375	-0.375	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.072	-0.042	22.181	-0.148	-0.148	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.809	0.888	25.823	-9.907	-9.907	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.055	-0.007	28.946	0.052	0.052	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.699	-0.844	31.999	9.603	9.603	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.010	-0.003	35.235	0.136	0.136	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.963	0.992	37.327	-7.890	-7.890	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.039	0.023	36.788	0.207	0.207	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.023	-0.003	34.471	-0.111	-0.111	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.812	0.893	27.654	-10.107	-10.107	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.024	-0.007	32.118	0.141	0.141	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.031	-0.029	33.639	0.196	0.196	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.060	-0.029	34.600	-0.205	-0.205	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.913	-0.955	35.975	8.649	8.649	0.000	0.000	0.000	0.000
82	A	83	TRP	0	-0.036	-0.006	38.231	-0.261	-0.261	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.011	-0.007	40.334	0.087	0.087	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.880	-0.917	42.093	7.076	7.076	0.000	0.000	0.000	0.000
85	A	86	GLY	0	-0.010	0.001	38.632	0.028	0.028	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.096	-0.060	38.881	0.136	0.136	0.000	0.000	0.000	0.000
87	A	88	SER	0	0.005	-0.007	38.699	0.111	0.111	0.000	0.000	0.000	0.000
88	A	89	ILE	0	-0.005	0.012	38.065	-0.242	-0.242	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.038	-0.035	40.072	0.087	0.087	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.025	-0.020	42.281	-0.120	-0.120	0.000	0.000	0.000	0.000
91	A	92	GLH	0	-0.027	-0.039	41.158	0.154	0.154	0.000	0.000	0.000	0.000
92	A	93	ASN	0	-0.019	-0.012	45.493	-0.116	-0.116	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.008	0.012	42.300	-0.116	-0.116	0.000	0.000	0.000	0.000
94	A	95	TYR	0	0.000	0.008	47.040	-0.081	-0.081	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.874	-0.919	42.044	7.323	7.323	0.000	0.000	0.000	0.000
96	A	97	PRO	0	0.016	0.005	44.631	0.004	0.004	0.000	0.000	0.000	0.000
97	A	98	TYR	0	-0.006	-0.016	41.293	0.091	0.091	0.000	0.000	0.000	0.000
98	A	99	MET	0	-0.053	-0.032	39.484	-0.076	-0.076	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.868	-0.928	34.162	8.999	8.999	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.935	0.966	33.959	-8.182	-8.182	0.000	0.000	0.000	0.000
101	A	102	CYS	0	0.022	0.042	29.050	0.397	0.397	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.013	-0.009	27.382	-0.328	-0.328	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.012	0.006	26.259	0.432	0.432	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.040	-0.014	20.351	-0.300	-0.300	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.827	-0.903	26.470	9.857	9.857	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.042	-0.028	25.336	-0.540	-0.540	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.002	-0.021	28.548	-0.247	-0.247	0.000	0.000	0.000	0.000
108	A	109	SER	0	-0.008	-0.026	31.324	-0.187	-0.187	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.024	0.001	27.868	-0.174	-0.174	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.015	-0.016	23.806	-0.151	-0.151	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.009	0.032	24.376	-0.459	-0.459	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.859	0.923	26.908	-9.711	-9.711	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.008	-0.012	23.077	0.113	0.113	0.000	0.000	0.000	0.000
114	A	115	HIS	0	-0.010	-0.002	28.906	-0.485	-0.485	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.030	-0.007	30.753	0.197	0.197	0.000	0.000	0.000	0.000
116	A	117	ALA	0	-0.029	-0.018	31.687	-0.226	-0.226	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.847	-0.926	33.548	8.704	8.704	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.860	-0.943	31.094	9.696	9.696	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.847	-0.885	31.874	9.356	9.356	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.823	0.894	29.934	-9.914	-9.914	0.000	0.000	0.000	0.000
121	A	123	ASN	0	-0.051	-0.029	27.393	-0.226	-0.226	0.000	0.000	0.000	0.000
122	A	124	VAL	0	-0.023	-0.003	23.608	0.216	0.216	0.000	0.000	0.000	0.000
123	A	125	PHE	0	-0.007	-0.012	19.028	-0.312	-0.312	0.000	0.000	0.000	0.000
124	A	126	MET	0	0.032	0.018	15.767	0.574	0.574	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.781	0.851	12.531	-17.172	-17.172	0.000	0.000	0.000	0.000
126	A	129	PHE	0	0.033	0.011	5.904	-1.042	-1.042	0.000	0.000	0.000	0.000
127	A	130	GLN	0	-0.060	-0.024	9.000	-0.549	-0.549	0.000	0.000	0.000	0.000
128	A	131	LEU	0	0.031	0.015	2.479	-1.298	-0.453	0.544	-0.398	-0.991	0.003
129	A	132	PRO	0	-0.012	-0.001	4.089	-3.272	-3.099	0.000	-0.013	-0.160	0.000

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