FMO DATABASE

FMODB ID: 85K9Y

Calculation Name: 1SMX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SMX

Chain ID: A

ChEMBL ID:

UniProt ID: P21513

Base Structure: X-ray

Registration Date: 2023-06-26

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	87
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-570512.324959
FMO2-HF: Nuclear repulsion	537470.48946
FMO2-HF: Total energy	-33041.835499
FMO2-MP2: Total energy	-33141.01675

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:39:ALA)

Summations of interaction energy for fragment #1(A:39:ALA)

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.
-1.852	0.688	0.012	-1.27	-1.282	0.002

Interaction energy analysis for fragmet #1(A:39:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : 0.010

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	41	ILE	0	0.003	0.003	3.160	-0.553	1.909	0.013	-1.259	-1.216	0.002
4	A	42	TYR	0	0.009	0.017	4.816	-0.183	-0.105	-0.001	-0.011	-0.066	0.000
5	A	43	LYS	1	0.845	0.911	7.654	0.406	0.406	0.000	0.000	0.000	0.000
6	A	44	GLY	0	0.043	0.033	11.032	0.013	0.013	0.000	0.000	0.000	0.000
7	A	45	LYS	1	0.820	0.899	13.387	0.312	0.312	0.000	0.000	0.000	0.000
8	A	46	ILE	0	-0.002	0.005	17.164	-0.027	-0.027	0.000	0.000	0.000	0.000
9	A	47	THR	0	-0.048	-0.037	19.526	0.032	0.032	0.000	0.000	0.000	0.000
10	A	48	ARG	1	0.873	0.924	22.198	0.223	0.223	0.000	0.000	0.000	0.000
11	A	49	ILE	0	-0.043	0.001	23.841	-0.022	-0.022	0.000	0.000	0.000	0.000
12	A	50	GLU	-1	-0.822	-0.908	25.826	-0.177	-0.177	0.000	0.000	0.000	0.000
13	A	51	PRO	0	-0.002	-0.016	28.198	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	52	SER	0	-0.023	-0.006	30.394	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	53	LEU	0	-0.022	-0.011	27.054	0.001	0.001	0.000	0.000	0.000	0.000
16	A	54	GLU	-1	-0.797	-0.847	26.926	-0.182	-0.182	0.000	0.000	0.000	0.000
17	A	55	ALA	0	0.014	0.013	22.993	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	56	ALA	0	0.008	0.002	21.142	0.025	0.025	0.000	0.000	0.000	0.000
19	A	57	PHE	0	-0.017	-0.002	20.092	-0.033	-0.033	0.000	0.000	0.000	0.000
20	A	58	VAL	0	0.005	-0.009	15.080	0.033	0.033	0.000	0.000	0.000	0.000
21	A	59	ASP	-1	-0.820	-0.902	15.053	-0.548	-0.548	0.000	0.000	0.000	0.000
22	A	60	TYR	0	-0.041	-0.046	9.468	0.005	0.005	0.000	0.000	0.000	0.000
23	A	61	GLY	0	0.004	0.009	10.107	-0.155	-0.155	0.000	0.000	0.000	0.000
24	A	62	ALA	0	-0.018	-0.005	11.488	-0.041	-0.041	0.000	0.000	0.000	0.000
25	A	63	GLU	-1	-0.932	-0.965	13.198	-0.321	-0.321	0.000	0.000	0.000	0.000
26	A	64	ARG	1	0.806	0.909	15.950	0.527	0.527	0.000	0.000	0.000	0.000
27	A	65	HIS	0	-0.004	0.003	15.790	-0.052	-0.052	0.000	0.000	0.000	0.000
28	A	66	GLY	0	0.051	0.024	15.238	0.006	0.006	0.000	0.000	0.000	0.000
29	A	67	PHE	0	-0.083	-0.048	16.215	0.075	0.075	0.000	0.000	0.000	0.000
30	A	68	LEU	0	0.028	0.015	15.952	-0.048	-0.048	0.000	0.000	0.000	0.000
31	A	69	PRO	0	0.007	-0.009	18.763	0.045	0.045	0.000	0.000	0.000	0.000
32	A	70	LEU	0	0.052	0.016	21.041	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	71	LYS	1	0.806	0.883	20.790	0.317	0.317	0.000	0.000	0.000	0.000
34	A	72	GLU	-1	-0.791	-0.847	17.448	-0.367	-0.367	0.000	0.000	0.000	0.000
35	A	73	ILE	0	-0.028	0.015	17.681	-0.036	-0.036	0.000	0.000	0.000	0.000
36	A	74	ALA	0	0.038	0.025	17.963	0.030	0.030	0.000	0.000	0.000	0.000
37	A	75	ARG	1	0.951	0.960	19.976	0.136	0.136	0.000	0.000	0.000	0.000
38	A	76	GLU	-1	-0.874	-0.937	18.775	-0.138	-0.138	0.000	0.000	0.000	0.000
39	A	77	TYR	0	-0.012	-0.005	14.656	0.005	0.005	0.000	0.000	0.000	0.000
40	A	78	PHE	0	-0.049	-0.028	21.631	0.000	0.000	0.000	0.000	0.000	0.000
41	A	79	PRO	0	-0.028	0.002	25.327	0.010	0.010	0.000	0.000	0.000	0.000
42	A	80	ALA	0	0.022	0.003	27.883	0.011	0.011	0.000	0.000	0.000	0.000
43	A	81	ASN	0	-0.028	-0.011	29.659	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	82	TYR	0	-0.038	-0.037	29.015	0.009	0.009	0.000	0.000	0.000	0.000
45	A	83	SER	0	-0.019	-0.026	32.367	0.004	0.004	0.000	0.000	0.000	0.000
46	A	84	ALA	0	0.000	0.004	32.505	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	85	HIS	0	-0.012	0.007	33.732	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	86	GLY	0	0.022	0.017	34.518	0.002	0.002	0.000	0.000	0.000	0.000
49	A	87	ARG	1	0.773	0.829	28.372	0.148	0.148	0.000	0.000	0.000	0.000
50	A	88	PRO	0	0.011	0.027	28.809	0.006	0.006	0.000	0.000	0.000	0.000
51	A	89	ASN	0	0.066	0.028	30.487	-0.019	-0.019	0.000	0.000	0.000	0.000
52	A	90	ILE	0	0.033	0.026	22.977	0.003	0.003	0.000	0.000	0.000	0.000
53	A	91	LYS	1	0.828	0.900	26.556	0.167	0.167	0.000	0.000	0.000	0.000
54	A	92	ASP	-1	-0.890	-0.929	28.931	-0.115	-0.115	0.000	0.000	0.000	0.000
55	A	93	VAL	0	-0.077	-0.038	23.607	0.008	0.008	0.000	0.000	0.000	0.000
56	A	94	LEU	0	0.000	0.005	20.544	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	95	ARG	1	0.963	0.967	23.906	0.138	0.138	0.000	0.000	0.000	0.000
58	A	96	GLU	-1	-0.747	-0.883	23.457	-0.205	-0.205	0.000	0.000	0.000	0.000
59	A	97	GLY	0	-0.019	-0.003	22.243	0.018	0.018	0.000	0.000	0.000	0.000
60	A	98	GLN	0	0.005	0.006	20.442	0.005	0.005	0.000	0.000	0.000	0.000
61	A	99	GLU	-1	-0.817	-0.904	15.954	-0.251	-0.251	0.000	0.000	0.000	0.000
62	A	100	VAL	0	-0.009	-0.003	14.722	0.037	0.037	0.000	0.000	0.000	0.000
63	A	101	ILE	0	-0.005	0.002	9.849	-0.063	-0.063	0.000	0.000	0.000	0.000
64	A	102	VAL	0	-0.016	-0.023	10.289	0.059	0.059	0.000	0.000	0.000	0.000
65	A	103	GLN	0	0.085	0.070	8.084	-0.190	-0.190	0.000	0.000	0.000	0.000
66	A	104	ILE	0	0.010	-0.003	7.977	0.342	0.342	0.000	0.000	0.000	0.000
67	A	105	ASP	-1	-0.829	-0.893	9.897	-0.628	-0.628	0.000	0.000	0.000	0.000
68	A	106	LYS	1	0.724	0.837	12.722	0.656	0.656	0.000	0.000	0.000	0.000
69	A	107	GLU	-1	-0.841	-0.931	8.293	-1.933	-1.933	0.000	0.000	0.000	0.000
70	A	108	GLU	-1	-0.820	-0.914	12.110	-0.555	-0.555	0.000	0.000	0.000	0.000
71	A	109	ARG	1	0.903	0.948	13.999	0.634	0.634	0.000	0.000	0.000	0.000
72	A	110	GLY	0	0.015	0.013	17.651	0.038	0.038	0.000	0.000	0.000	0.000
73	A	111	ASN	0	0.020	0.008	20.275	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	112	LYS	1	0.925	0.975	19.568	0.391	0.391	0.000	0.000	0.000	0.000
75	A	113	GLY	0	0.088	0.043	17.106	-0.025	-0.025	0.000	0.000	0.000	0.000
76	A	114	ALA	0	-0.024	0.000	12.620	0.039	0.039	0.000	0.000	0.000	0.000
77	A	115	ALA	0	-0.029	-0.006	14.640	0.074	0.074	0.000	0.000	0.000	0.000
78	A	116	LEU	0	0.013	0.005	11.744	-0.142	-0.142	0.000	0.000	0.000	0.000
79	A	117	THR	0	-0.015	-0.042	12.905	0.119	0.119	0.000	0.000	0.000	0.000
80	A	118	THR	0	-0.021	-0.029	12.622	-0.079	-0.079	0.000	0.000	0.000	0.000
81	A	119	PHE	0	-0.037	-0.007	13.813	0.043	0.043	0.000	0.000	0.000	0.000
82	A	120	ILE	0	-0.026	-0.002	8.465	-0.062	-0.062	0.000	0.000	0.000	0.000
83	A	121	SER	0	-0.014	-0.032	8.355	0.142	0.142	0.000	0.000	0.000	0.000
84	A	122	LEU	0	-0.019	0.000	8.831	0.105	0.105	0.000	0.000	0.000	0.000
85	A	123	ALA	0	0.009	0.008	10.756	-0.023	-0.023	0.000	0.000	0.000	0.000
86	A	124	GLY	0	0.008	0.006	12.714	0.041	0.041	0.000	0.000	0.000	0.000
87	A	125	SER	0	-0.062	-0.031	14.548	-0.036	-0.036	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:39:ALA)