FMO DATABASE

FMODB ID: 7633K

Calculation Name: 1SMT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SMT

Chain ID: A

ChEMBL ID:

UniProt ID: P30340

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	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	98
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-664296.773279
FMO2-HF: Nuclear repulsion	625924.253232
FMO2-HF: Total energy	-38372.520047
FMO2-MP2: Total energy	-38485.650024

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:24:GLU)

Summations of interaction energy for fragment #1(A:24:GLU)

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.
6.734	8.51	-0.025	-0.811	-0.94	0

Interaction energy analysis for fragmet #1(A:24:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.908 / q_NPA : -0.966

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].
3	A	26	GLN	0	-0.013	-0.006	3.817	-5.882	-4.106	-0.025	-0.811	-0.940
4	A	27	ALA	0	-0.009	0.007	6.658	-1.151	-1.151	0.000	0.000	0.000
5	A	28	ILE	0	0.007	0.000	10.174	0.308	0.308	0.000	0.000	0.000
6	A	29	ALA	0	0.027	0.018	12.897	-0.240	-0.240	0.000	0.000	0.000
7	A	30	PRO	0	0.039	0.012	14.780	-0.553	-0.553	0.000	0.000	0.000
8	A	31	GLU	-1	-0.840	-0.935	17.648	15.312	15.312	0.000	0.000	0.000
9	A	32	VAL	0	-0.013	-0.010	16.689	-0.616	-0.616	0.000	0.000	0.000
10	A	33	ALA	0	-0.013	-0.009	17.258	-0.425	-0.425	0.000	0.000	0.000
11	A	34	GLN	0	-0.047	-0.030	19.087	-0.303	-0.303	0.000	0.000	0.000
12	A	35	SER	0	-0.001	-0.011	22.317	-0.641	-0.641	0.000	0.000	0.000
13	A	36	LEU	0	-0.032	-0.006	19.131	-0.446	-0.446	0.000	0.000	0.000
14	A	37	ALA	0	0.007	0.002	22.647	-0.400	-0.400	0.000	0.000	0.000
15	A	38	GLU	-1	-0.881	-0.936	24.430	10.147	10.147	0.000	0.000	0.000
16	A	39	PHE	0	-0.035	-0.012	25.469	-0.478	-0.478	0.000	0.000	0.000
17	A	40	PHE	0	0.018	-0.011	22.037	-0.357	-0.357	0.000	0.000	0.000
18	A	41	ALA	0	-0.002	0.010	27.607	-0.335	-0.335	0.000	0.000	0.000
19	A	42	VAL	0	-0.042	-0.016	30.311	-0.418	-0.418	0.000	0.000	0.000
20	A	43	LEU	0	-0.013	-0.013	28.406	-0.371	-0.371	0.000	0.000	0.000
21	A	44	ALA	0	-0.018	0.015	31.563	-0.149	-0.149	0.000	0.000	0.000
22	A	45	ASP	-1	-0.860	-0.946	33.329	7.566	7.566	0.000	0.000	0.000
23	A	46	PRO	0	0.047	0.001	36.960	0.008	0.008	0.000	0.000	0.000
24	A	47	ASN	0	-0.012	-0.006	38.987	-0.121	-0.121	0.000	0.000	0.000
25	A	48	ARG	1	0.888	0.956	35.809	-8.310	-8.310	0.000	0.000	0.000
26	A	49	LEU	0	0.044	0.027	33.078	-0.014	-0.014	0.000	0.000	0.000
27	A	50	ARG	1	0.960	0.988	37.054	-6.864	-6.864	0.000	0.000	0.000
28	A	51	LEU	0	-0.010	0.008	40.171	-0.097	-0.097	0.000	0.000	0.000
29	A	52	LEU	0	-0.001	-0.013	33.684	-0.038	-0.038	0.000	0.000	0.000
30	A	53	SER	0	-0.037	-0.015	37.262	-0.003	-0.003	0.000	0.000	0.000
31	A	54	LEU	0	-0.031	-0.012	38.260	-0.076	-0.076	0.000	0.000	0.000
32	A	55	LEU	0	-0.022	-0.022	38.298	-0.014	-0.014	0.000	0.000	0.000
33	A	56	ALA	0	-0.015	0.004	35.275	0.079	0.079	0.000	0.000	0.000
34	A	57	ARG	1	0.895	0.948	36.730	-7.236	-7.236	0.000	0.000	0.000
35	A	58	SER	0	-0.002	-0.008	39.541	-0.123	-0.123	0.000	0.000	0.000
36	A	59	GLU	-1	-0.829	-0.854	41.308	7.187	7.187	0.000	0.000	0.000
37	A	60	LEU	0	-0.022	-0.014	42.375	-0.169	-0.169	0.000	0.000	0.000
38	A	61	CYS	0	-0.033	-0.010	45.289	0.084	0.084	0.000	0.000	0.000
39	A	62	VAL	0	0.016	-0.012	47.401	0.030	0.030	0.000	0.000	0.000
40	A	63	GLY	0	0.080	0.039	48.780	-0.004	-0.004	0.000	0.000	0.000
41	A	64	ASP	-1	-0.832	-0.911	48.161	6.146	6.146	0.000	0.000	0.000
42	A	65	LEU	0	-0.012	-0.010	43.545	0.025	0.025	0.000	0.000	0.000
43	A	66	ALA	0	-0.027	-0.015	47.361	0.024	0.024	0.000	0.000	0.000
44	A	67	GLN	0	-0.014	-0.014	50.174	-0.084	-0.084	0.000	0.000	0.000
45	A	68	ALA	0	-0.014	0.007	47.230	-0.037	-0.037	0.000	0.000	0.000
46	A	69	ILE	0	-0.068	-0.032	44.094	0.060	0.060	0.000	0.000	0.000
47	A	70	GLY	0	0.007	0.022	48.196	-0.025	-0.025	0.000	0.000	0.000
48	A	71	VAL	0	-0.048	-0.020	48.553	-0.060	-0.060	0.000	0.000	0.000
49	A	72	SER	0	0.042	0.010	51.821	-0.004	-0.004	0.000	0.000	0.000
50	A	73	GLU	-1	-0.823	-0.932	51.203	5.903	5.903	0.000	0.000	0.000
51	A	74	SER	0	-0.057	-0.021	50.626	0.154	0.154	0.000	0.000	0.000
52	A	75	ALA	0	0.037	0.013	49.313	0.095	0.095	0.000	0.000	0.000
53	A	76	VAL	0	0.033	0.025	45.801	0.162	0.162	0.000	0.000	0.000
54	A	77	SER	0	-0.014	-0.023	45.757	0.162	0.162	0.000	0.000	0.000
55	A	78	HIS	0	0.016	0.021	46.066	0.211	0.211	0.000	0.000	0.000
56	A	79	GLN	0	0.008	0.001	42.533	0.230	0.230	0.000	0.000	0.000
57	A	80	LEU	0	0.030	0.015	41.397	0.202	0.202	0.000	0.000	0.000
58	A	81	ARG	1	0.859	0.929	41.262	-6.434	-6.434	0.000	0.000	0.000
59	A	82	SER	0	-0.025	-0.012	38.927	0.160	0.160	0.000	0.000	0.000
60	A	83	LEU	0	0.079	0.023	36.732	0.181	0.181	0.000	0.000	0.000
61	A	84	ARG	1	0.905	0.972	36.519	-7.162	-7.162	0.000	0.000	0.000
62	A	85	ASN	0	-0.046	-0.038	36.793	0.137	0.137	0.000	0.000	0.000
63	A	86	LEU	0	-0.036	0.001	33.303	0.152	0.152	0.000	0.000	0.000
64	A	87	ARG	1	0.939	0.971	30.039	-9.276	-9.276	0.000	0.000	0.000
65	A	88	LEU	0	0.057	0.038	31.193	0.195	0.195	0.000	0.000	0.000
66	A	89	VAL	0	-0.050	-0.018	33.707	-0.042	-0.042	0.000	0.000	0.000
67	A	90	SER	0	-0.010	-0.004	36.598	0.090	0.090	0.000	0.000	0.000
68	A	91	TYR	0	-0.008	-0.005	38.440	-0.126	-0.126	0.000	0.000	0.000
69	A	92	ARG	1	0.796	0.866	41.594	-6.917	-6.917	0.000	0.000	0.000
70	A	93	LYS	1	0.948	0.970	43.888	-6.552	-6.552	0.000	0.000	0.000
71	A	94	GLN	0	0.071	0.037	47.217	0.178	0.178	0.000	0.000	0.000
72	A	95	GLY	0	0.020	0.020	49.618	-0.096	-0.096	0.000	0.000	0.000
73	A	96	ARG	1	0.929	0.949	53.229	-5.332	-5.332	0.000	0.000	0.000
74	A	97	HIS	0	0.027	0.030	50.733	-0.013	-0.013	0.000	0.000	0.000
75	A	98	VAL	0	-0.035	-0.021	46.135	0.076	0.076	0.000	0.000	0.000
76	A	99	TYR	0	0.037	0.016	44.714	-0.091	-0.091	0.000	0.000	0.000
77	A	100	TYR	0	0.003	-0.022	41.285	0.121	0.121	0.000	0.000	0.000
78	A	101	GLN	0	0.050	0.018	37.831	-0.011	-0.011	0.000	0.000	0.000
79	A	102	LEU	0	0.034	0.019	33.445	0.019	0.019	0.000	0.000	0.000
80	A	103	GLN	0	-0.058	-0.028	31.460	-0.114	-0.114	0.000	0.000	0.000
81	A	104	ASP	-1	-0.823	-0.922	28.314	10.537	10.537	0.000	0.000	0.000
82	A	105	HIS	0	0.050	0.010	27.597	-0.298	-0.298	0.000	0.000	0.000
83	A	106	HIS	0	0.010	0.015	23.919	0.123	0.123	0.000	0.000	0.000
84	A	107	ILE	0	-0.010	0.000	26.825	0.059	0.059	0.000	0.000	0.000
85	A	108	VAL	0	0.007	0.002	29.347	-0.113	-0.113	0.000	0.000	0.000
86	A	109	ALA	0	-0.010	-0.009	26.018	-0.081	-0.081	0.000	0.000	0.000
87	A	110	LEU	0	-0.002	0.005	25.276	0.083	0.083	0.000	0.000	0.000
88	A	111	TYR	0	-0.013	-0.008	26.601	-0.121	-0.121	0.000	0.000	0.000
89	A	112	GLN	0	-0.012	-0.020	29.749	-0.174	-0.174	0.000	0.000	0.000
90	A	113	ASN	0	0.013	0.004	24.906	0.153	0.153	0.000	0.000	0.000
91	A	114	ALA	0	-0.029	0.000	27.301	0.086	0.086	0.000	0.000	0.000
92	A	115	LEU	0	-0.040	-0.024	28.156	-0.143	-0.143	0.000	0.000	0.000
93	A	116	ASP	-1	-0.867	-0.940	28.593	9.520	9.520	0.000	0.000	0.000
94	A	117	HIS	0	-0.008	-0.004	25.093	0.107	0.107	0.000	0.000	0.000
95	A	118	LEU	0	-0.056	-0.043	28.170	-0.141	-0.141	0.000	0.000	0.000
96	A	119	GLN	0	-0.089	-0.041	31.213	-0.137	-0.137	0.000	0.000	0.000
97	A	120	GLU	-1	-0.964	-0.963	28.338	9.957	9.957	0.000	0.000	0.000
98	A	121	CYS	0	-0.106	-0.033	28.288	0.123	0.123	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:GLU)