FMO DATABASE

FMODB ID: P8J8Y

Calculation Name: 4GS3-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4GS3

Chain ID: A

ChEMBL ID:

UniProt ID: Q8RBI8

Base Structure: X-ray

Registration Date: 2017-12-04

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20171117

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	93
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-656289.253266
FMO2-HF: Nuclear repulsion	620091.861529
FMO2-HF: Total energy	-36197.391737
FMO2-MP2: Total energy	-36305.350372

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:6:ACE)

Summations of interaction energy for fragment #1(A:6:ACE)

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.
2.585	3.227	-0.008	-0.248	-0.385	0.001

Interaction energy analysis for fragmet #1(A:6:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.015 / q_NPA : -0.019

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	8	ASN	0	-0.070	-0.026	3.835	1.558	2.200	-0.008	-0.248	-0.385	0.001
4	A	9	ASN	0	-0.025	-0.027	6.853	0.441	0.441	0.000	0.000	0.000	0.000
5	A	10	THR	0	-0.063	-0.044	5.274	-0.108	-0.108	0.000	0.000	0.000	0.000
6	A	11	VAL	0	0.017	0.024	7.842	0.161	0.161	0.000	0.000	0.000	0.000
7	A	12	THR	0	-0.018	-0.020	9.565	0.010	0.010	0.000	0.000	0.000	0.000
8	A	13	LEU	0	-0.016	0.003	11.942	0.025	0.025	0.000	0.000	0.000	0.000
9	A	14	VAL	0	0.000	-0.012	15.743	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	15	GLY	0	0.012	0.004	18.470	0.005	0.005	0.000	0.000	0.000	0.000
11	A	16	LYS	1	0.854	0.919	21.894	0.001	0.001	0.000	0.000	0.000	0.000
12	A	17	VAL	0	-0.015	0.010	24.192	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	18	PHE	0	0.012	-0.005	25.828	0.006	0.006	0.000	0.000	0.000	0.000
14	A	19	THR	0	0.018	0.006	27.753	0.002	0.002	0.000	0.000	0.000	0.000
15	A	20	PRO	0	0.031	0.005	28.120	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.024	0.003	24.676	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	22	GLU	-1	-0.963	-0.964	28.094	-0.058	-0.058	0.000	0.000	0.000	0.000
18	A	23	PHE	0	-0.022	-0.006	28.350	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	24	SER	0	-0.048	-0.029	26.490	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	25	HIS	0	-0.063	-0.068	25.669	0.001	0.001	0.000	0.000	0.000	0.000
21	A	26	GLU	-1	-0.920	-0.969	27.719	-0.097	-0.097	0.000	0.000	0.000	0.000
22	A	27	LEU	0	-0.007	0.008	22.982	0.000	0.000	0.000	0.000	0.000	0.000
23	A	28	TYR	0	-0.027	-0.027	26.486	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	29	GLY	0	0.035	0.023	28.851	0.001	0.001	0.000	0.000	0.000	0.000
25	A	30	GLU	-1	-0.866	-0.895	21.761	-0.187	-0.187	0.000	0.000	0.000	0.000
26	A	31	LYS	1	0.971	0.990	26.691	0.082	0.082	0.000	0.000	0.000	0.000
27	A	32	PHE	0	0.026	0.018	20.257	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	33	PHE	0	-0.001	0.003	24.108	0.014	0.014	0.000	0.000	0.000	0.000
29	A	34	ASN	0	0.002	0.011	23.583	-0.026	-0.026	0.000	0.000	0.000	0.000
30	A	35	PHE	0	0.033	0.011	21.065	0.009	0.009	0.000	0.000	0.000	0.000
31	A	36	ILE	0	0.003	0.012	23.672	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	37	LEU	0	0.003	0.007	19.229	0.006	0.006	0.000	0.000	0.000	0.000
33	A	38	GLU	-1	-0.876	-0.941	23.195	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	39	VAL	0	-0.014	-0.023	19.306	0.004	0.004	0.000	0.000	0.000	0.000
35	A	40	PRO	0	-0.013	0.003	22.596	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	41	ARG	1	0.839	0.882	22.956	0.013	0.013	0.000	0.000	0.000	0.000
37	A	42	LEU	0	0.039	0.014	23.882	0.000	0.000	0.000	0.000	0.000	0.000
38	A	43	SER	0	-0.034	-0.019	25.547	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	44	GLU	-1	-0.867	-0.928	27.561	0.020	0.020	0.000	0.000	0.000	0.000
40	A	45	THR	0	-0.104	-0.057	27.155	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	46	LYS	1	0.903	0.965	26.099	0.004	0.004	0.000	0.000	0.000	0.000
42	A	47	ASP	-1	-0.819	-0.865	22.379	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	48	TYR	0	-0.019	-0.016	24.205	0.001	0.001	0.000	0.000	0.000	0.000
44	A	49	LEU	0	-0.029	-0.022	18.678	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	50	PRO	0	-0.007	0.015	20.565	0.003	0.003	0.000	0.000	0.000	0.000
46	A	51	ILE	0	0.024	0.020	18.018	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	52	THR	0	-0.019	-0.016	19.155	0.011	0.011	0.000	0.000	0.000	0.000
48	A	53	ILE	0	-0.008	0.004	18.821	-0.027	-0.027	0.000	0.000	0.000	0.000
49	A	54	SER	0	0.002	-0.026	19.955	0.022	0.022	0.000	0.000	0.000	0.000
50	A	55	ASN	0	0.028	-0.007	21.808	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	56	ARG	1	0.925	0.954	20.730	0.152	0.152	0.000	0.000	0.000	0.000
52	A	57	LEU	0	-0.027	-0.018	16.308	0.004	0.004	0.000	0.000	0.000	0.000
53	A	58	PHE	0	0.011	0.008	20.179	0.006	0.006	0.000	0.000	0.000	0.000
54	A	59	GLU	-1	-0.936	-0.953	22.674	-0.068	-0.068	0.000	0.000	0.000	0.000
55	A	60	GLY	0	-0.036	-0.013	24.298	0.002	0.002	0.000	0.000	0.000	0.000
56	A	61	MET	0	-0.068	-0.015	20.973	0.004	0.004	0.000	0.000	0.000	0.000
57	A	62	ASN	0	0.007	0.000	26.114	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	63	LEU	0	0.014	-0.006	22.710	0.001	0.001	0.000	0.000	0.000	0.000
59	A	64	GLU	-1	-0.917	-0.953	26.752	-0.034	-0.034	0.000	0.000	0.000	0.000
60	A	65	VAL	0	-0.003	-0.002	28.751	0.001	0.001	0.000	0.000	0.000	0.000
61	A	66	GLY	0	-0.029	-0.008	28.964	0.003	0.003	0.000	0.000	0.000	0.000
62	A	67	THR	0	-0.031	-0.017	24.814	0.006	0.006	0.000	0.000	0.000	0.000
63	A	68	ARG	1	0.884	0.944	22.754	-0.029	-0.029	0.000	0.000	0.000	0.000
64	A	69	VAL	0	0.021	0.002	19.823	0.000	0.000	0.000	0.000	0.000	0.000
65	A	70	LYS	1	0.963	0.986	12.400	-0.105	-0.105	0.000	0.000	0.000	0.000
66	A	71	ILE	0	0.015	0.003	14.514	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.734	-0.832	7.895	-0.706	-0.706	0.000	0.000	0.000	0.000
68	A	73	GLY	0	0.049	0.016	10.847	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	74	GLN	0	0.026	0.051	10.288	0.038	0.038	0.000	0.000	0.000	0.000
70	A	75	LEU	0	-0.003	-0.007	11.695	0.084	0.084	0.000	0.000	0.000	0.000
71	A	76	ARG	1	0.890	0.941	14.307	0.375	0.375	0.000	0.000	0.000	0.000
72	A	77	SER	0	0.007	0.005	16.853	0.030	0.030	0.000	0.000	0.000	0.000
73	A	78	TYR	0	0.013	-0.001	20.190	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	79	ASN	0	0.003	-0.001	22.792	0.021	0.021	0.000	0.000	0.000	0.000
75	A	80	ARG	1	0.999	1.009	26.543	0.094	0.094	0.000	0.000	0.000	0.000
76	A	81	NME	0	0.037	0.024	28.142	0.007	0.007	0.000	0.000	0.000	0.000
77	A	88	ACE	0	0.052	0.012	32.388	0.000	0.000	0.000	0.000	0.000	0.000
78	A	89	LYS	1	0.890	0.938	29.204	0.082	0.082	0.000	0.000	0.000	0.000
79	A	90	LEU	0	0.011	0.018	23.473	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	91	ILE	0	-0.079	-0.034	23.655	0.012	0.012	0.000	0.000	0.000	0.000
81	A	92	LEU	0	0.038	0.010	19.407	-0.016	-0.016	0.000	0.000	0.000	0.000
82	A	93	THR	0	-0.025	-0.042	18.701	0.021	0.021	0.000	0.000	0.000	0.000
83	A	94	VAL	0	0.021	0.019	14.167	-0.038	-0.038	0.000	0.000	0.000	0.000
84	A	95	PHE	0	-0.021	-0.016	14.899	0.031	0.031	0.000	0.000	0.000	0.000
85	A	96	ALA	0	-0.002	-0.008	14.025	-0.062	-0.062	0.000	0.000	0.000	0.000
86	A	97	ARG	1	0.758	0.850	7.932	0.966	0.966	0.000	0.000	0.000	0.000
87	A	98	ASP	-1	-0.902	-0.958	12.377	-0.087	-0.087	0.000	0.000	0.000	0.000
88	A	99	ILE	0	-0.014	-0.013	14.026	0.005	0.005	0.000	0.000	0.000	0.000
89	A	100	SER	0	-0.001	0.013	16.706	0.015	0.015	0.000	0.000	0.000	0.000
90	A	101	VAL	0	0.017	0.003	18.857	0.004	0.004	0.000	0.000	0.000	0.000
91	A	102	VAL	0	-0.069	-0.031	20.061	0.009	0.009	0.000	0.000	0.000	0.000
92	A	103	PRO	0	0.005	0.006	23.118	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	104	GLU	-2	-1.752	-1.861	25.405	0.035	0.035	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ACE)