FMO DATABASE

FMODB ID: XMKZX

Calculation Name: 4GA2-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4GA2

Chain ID: A

ChEMBL ID:

UniProt ID: H2QII6

Base Structure: X-ray

Registration Date: 2017-11-22

Reference:

DOI:

Apendix: None

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1327989.129601
FMO2-HF: Nuclear repulsion	1269423.959221
FMO2-HF: Total energy	-58565.170381
FMO2-MP2: Total energy	-58737.045404

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:ACE)

Summations of interaction energy for fragment #1(A:1: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.
0.967	1.71	-0.011	-0.286	-0.447	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.042 / q_NPA : 0.012

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	3	ARG	1	0.870	0.963	3.847	0.658	1.401	-0.011	-0.286	-0.447
4	A	4	SER	0	0.015	0.009	6.237	0.004	0.004	0.000	0.000	0.000
5	A	5	LYS	1	1.003	0.980	9.845	0.391	0.391	0.000	0.000	0.000
6	A	6	ALA	0	0.053	0.031	13.003	0.054	0.054	0.000	0.000	0.000
7	A	7	ASP	-1	-0.833	-0.910	8.964	-0.345	-0.345	0.000	0.000	0.000
8	A	8	VAL	0	-0.046	-0.021	10.755	0.074	0.074	0.000	0.000	0.000
9	A	9	GLU	-1	-0.904	-0.957	12.934	-0.119	-0.119	0.000	0.000	0.000
10	A	10	ARG	1	0.903	0.953	11.659	0.121	0.121	0.000	0.000	0.000
11	A	11	TYR	0	-0.006	-0.002	14.202	0.028	0.028	0.000	0.000	0.000
12	A	12	ILE	0	0.038	0.030	16.149	0.016	0.016	0.000	0.000	0.000
13	A	13	ALA	0	-0.002	-0.002	18.654	0.009	0.009	0.000	0.000	0.000
14	A	14	SER	0	-0.067	-0.045	18.690	0.013	0.013	0.000	0.000	0.000
15	A	15	VAL	0	-0.004	-0.008	19.278	0.006	0.006	0.000	0.000	0.000
16	A	16	GLN	0	-0.009	-0.007	21.905	0.003	0.003	0.000	0.000	0.000
17	A	17	GLY	0	-0.010	-0.004	24.022	-0.001	-0.001	0.000	0.000	0.000
18	A	18	SER	0	-0.012	-0.004	24.378	0.004	0.004	0.000	0.000	0.000
19	A	19	THR	0	-0.111	-0.053	24.901	0.006	0.006	0.000	0.000	0.000
20	A	20	PRO	0	0.079	0.053	26.337	-0.001	-0.001	0.000	0.000	0.000
21	A	21	SER	0	0.000	0.005	28.347	-0.005	-0.005	0.000	0.000	0.000
22	A	22	PRO	0	0.075	0.013	28.444	0.001	0.001	0.000	0.000	0.000
23	A	23	ARG	1	1.010	1.004	27.937	-0.027	-0.027	0.000	0.000	0.000
24	A	24	GLN	0	0.008	0.003	26.748	0.001	0.001	0.000	0.000	0.000
25	A	25	LYS	1	0.960	0.993	23.881	0.018	0.018	0.000	0.000	0.000
26	A	26	SER	0	0.016	0.010	22.952	-0.001	-0.001	0.000	0.000	0.000
27	A	27	ILE	0	-0.037	-0.014	23.439	0.003	0.003	0.000	0.000	0.000
28	A	28	LYS	1	0.922	0.963	19.488	-0.058	-0.058	0.000	0.000	0.000
29	A	29	GLY	0	0.047	0.031	18.639	0.002	0.002	0.000	0.000	0.000
30	A	30	PHE	0	0.027	0.001	16.792	-0.004	-0.004	0.000	0.000	0.000
31	A	31	TYR	0	-0.022	-0.010	14.896	0.002	0.002	0.000	0.000	0.000
32	A	32	PHE	0	0.020	0.002	13.755	-0.001	-0.001	0.000	0.000	0.000
33	A	33	ALA	0	0.003	0.016	14.154	-0.027	-0.027	0.000	0.000	0.000
34	A	34	LYS	1	0.943	0.969	11.483	-0.184	-0.184	0.000	0.000	0.000
35	A	35	LEU	0	0.003	0.012	9.063	-0.009	-0.009	0.000	0.000	0.000
36	A	36	TYR	0	0.054	0.004	9.503	-0.082	-0.082	0.000	0.000	0.000
37	A	37	TYR	0	-0.017	0.004	10.284	-0.067	-0.067	0.000	0.000	0.000
38	A	38	GLU	-1	-0.900	-0.942	5.667	0.387	0.387	0.000	0.000	0.000
39	A	39	ALA	0	-0.052	-0.028	6.435	-0.366	-0.366	0.000	0.000	0.000
40	A	40	LYS	1	0.878	0.954	7.459	0.828	0.828	0.000	0.000	0.000
41	A	41	GLU	-1	-0.857	-0.925	11.195	-0.260	-0.260	0.000	0.000	0.000
42	A	42	TYR	0	0.070	0.011	12.245	0.026	0.026	0.000	0.000	0.000
43	A	43	ASP	-1	-0.886	-0.935	16.007	-0.075	-0.075	0.000	0.000	0.000
44	A	44	LEU	0	0.023	0.004	16.493	0.022	0.022	0.000	0.000	0.000
45	A	45	ALA	0	-0.025	-0.013	14.518	0.023	0.023	0.000	0.000	0.000
46	A	46	LYS	1	0.933	0.965	16.537	0.106	0.106	0.000	0.000	0.000
47	A	47	LYS	1	0.994	1.013	19.991	0.080	0.080	0.000	0.000	0.000
48	A	48	TYR	0	-0.014	-0.023	18.159	0.016	0.016	0.000	0.000	0.000
49	A	49	ILE	0	0.017	0.016	18.646	0.015	0.015	0.000	0.000	0.000
50	A	50	CYS	0	-0.013	-0.004	20.560	0.009	0.009	0.000	0.000	0.000
51	A	51	THR	0	-0.054	-0.024	22.461	0.006	0.006	0.000	0.000	0.000
52	A	52	TYR	0	-0.080	-0.069	21.872	0.006	0.006	0.000	0.000	0.000
53	A	53	ILE	0	0.005	-0.010	23.481	0.005	0.005	0.000	0.000	0.000
54	A	54	ASN	0	-0.053	-0.026	25.998	-0.002	-0.002	0.000	0.000	0.000
55	A	55	VAL	0	-0.025	-0.006	26.565	0.001	0.001	0.000	0.000	0.000
56	A	56	GLN	0	-0.037	-0.021	25.684	0.000	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.901	-0.937	27.280	0.016	0.016	0.000	0.000	0.000
58	A	58	ARG	1	0.929	0.949	29.590	-0.027	-0.027	0.000	0.000	0.000
59	A	59	ASP	-1	-0.818	-0.878	23.419	0.067	0.067	0.000	0.000	0.000
60	A	60	PRO	0	0.031	0.015	25.418	-0.003	-0.003	0.000	0.000	0.000
61	A	61	LYS	1	0.970	0.972	19.839	-0.118	-0.118	0.000	0.000	0.000
62	A	62	ALA	0	0.001	0.017	20.737	0.000	0.000	0.000	0.000	0.000
63	A	63	HIS	0	0.061	0.016	21.725	-0.009	-0.009	0.000	0.000	0.000
64	A	64	ARG	1	0.829	0.905	20.600	-0.067	-0.067	0.000	0.000	0.000
65	A	65	PHE	0	-0.027	-0.013	13.490	-0.001	-0.001	0.000	0.000	0.000
66	A	66	LEU	0	0.029	0.007	18.660	-0.012	-0.012	0.000	0.000	0.000
67	A	67	GLY	0	0.050	0.008	20.891	-0.010	-0.010	0.000	0.000	0.000
68	A	68	LEU	0	-0.009	0.015	14.941	-0.004	-0.004	0.000	0.000	0.000
69	A	69	LEU	0	-0.062	-0.043	15.150	-0.015	-0.015	0.000	0.000	0.000
70	A	70	TYR	0	0.023	-0.001	18.437	-0.011	-0.011	0.000	0.000	0.000
71	A	71	GLU	-1	-0.773	-0.859	20.725	-0.004	-0.004	0.000	0.000	0.000
72	A	72	LEU	0	-0.072	-0.038	15.014	-0.005	-0.005	0.000	0.000	0.000
73	A	73	GLU	-1	-0.946	-0.964	19.103	-0.109	-0.109	0.000	0.000	0.000
74	A	74	GLU	-1	-0.940	-0.960	21.503	-0.051	-0.051	0.000	0.000	0.000
75	A	75	ASN	0	-0.016	-0.001	24.158	0.009	0.009	0.000	0.000	0.000
76	A	76	THR	0	0.061	0.008	26.172	0.005	0.005	0.000	0.000	0.000
77	A	77	ASP	-1	-0.812	-0.892	28.216	-0.017	-0.017	0.000	0.000	0.000
78	A	78	LYS	1	0.854	0.928	26.411	0.029	0.029	0.000	0.000	0.000
79	A	79	ALA	0	0.030	0.015	24.408	0.005	0.005	0.000	0.000	0.000
80	A	80	VAL	0	0.008	0.005	25.684	0.008	0.008	0.000	0.000	0.000
81	A	81	GLU	-1	-0.899	-0.940	28.881	-0.012	-0.012	0.000	0.000	0.000
82	A	82	CYS	0	-0.051	-0.014	24.792	0.003	0.003	0.000	0.000	0.000
83	A	83	TYR	0	-0.054	-0.064	21.572	0.010	0.010	0.000	0.000	0.000
84	A	84	ARG	1	0.981	0.996	26.885	0.001	0.001	0.000	0.000	0.000
85	A	85	ARG	1	0.953	0.992	28.825	-0.011	-0.011	0.000	0.000	0.000
86	A	86	SER	0	-0.021	-0.030	25.125	0.005	0.005	0.000	0.000	0.000
87	A	87	VAL	0	-0.027	-0.017	27.672	0.005	0.005	0.000	0.000	0.000
88	A	88	GLU	-1	-0.925	-0.977	30.096	0.013	0.013	0.000	0.000	0.000
89	A	89	LEU	0	-0.091	-0.032	28.744	0.001	0.001	0.000	0.000	0.000
90	A	90	ASN	0	-0.013	0.011	26.752	0.001	0.001	0.000	0.000	0.000
91	A	91	PRO	0	0.047	0.018	29.637	0.002	0.002	0.000	0.000	0.000
92	A	92	THR	0	-0.065	-0.041	29.463	0.001	0.001	0.000	0.000	0.000
93	A	93	GLN	0	-0.041	-0.007	24.711	0.009	0.009	0.000	0.000	0.000
94	A	94	LYS	1	1.015	0.988	28.248	-0.046	-0.046	0.000	0.000	0.000
95	A	95	ASP	-1	-0.775	-0.875	23.969	0.056	0.056	0.000	0.000	0.000
96	A	96	LEU	0	-0.004	-0.006	23.738	-0.004	-0.004	0.000	0.000	0.000
97	A	97	VAL	0	-0.038	-0.008	27.282	-0.006	-0.006	0.000	0.000	0.000
98	A	98	LEU	0	0.009	0.014	28.482	-0.004	-0.004	0.000	0.000	0.000
99	A	99	LYS	1	0.866	0.938	22.212	-0.017	-0.017	0.000	0.000	0.000
100	A	100	ILE	0	-0.020	-0.019	27.241	-0.006	-0.006	0.000	0.000	0.000
101	A	101	ALA	0	0.019	0.006	29.572	-0.004	-0.004	0.000	0.000	0.000
102	A	102	GLU	-1	-0.909	-0.967	27.061	0.014	0.014	0.000	0.000	0.000
103	A	103	LEU	0	-0.083	-0.040	24.684	-0.004	-0.004	0.000	0.000	0.000
104	A	104	LEU	0	-0.019	-0.016	28.717	-0.004	-0.004	0.000	0.000	0.000
105	A	105	CYS	0	-0.028	-0.002	32.289	-0.001	-0.001	0.000	0.000	0.000
106	A	106	LYS	1	0.891	0.953	25.597	0.026	0.026	0.000	0.000	0.000
107	A	107	ASN	0	-0.078	-0.039	30.351	-0.001	-0.001	0.000	0.000	0.000
108	A	108	ASP	-1	-0.792	-0.887	31.863	-0.021	-0.021	0.000	0.000	0.000
109	A	109	VAL	0	-0.055	-0.016	35.628	0.002	0.002	0.000	0.000	0.000
110	A	110	THR	0	-0.019	-0.025	38.256	0.001	0.001	0.000	0.000	0.000
111	A	111	ASP	-1	-0.806	-0.889	37.846	-0.010	-0.010	0.000	0.000	0.000
112	A	112	GLY	0	0.024	0.017	40.406	0.001	0.001	0.000	0.000	0.000
113	A	113	ARG	1	0.772	0.862	33.700	0.014	0.014	0.000	0.000	0.000
114	A	114	ALA	0	0.057	0.021	35.940	0.003	0.003	0.000	0.000	0.000
115	A	115	LYS	1	1.042	1.020	36.946	0.000	0.000	0.000	0.000	0.000
116	A	116	TYR	0	-0.030	-0.009	37.219	0.002	0.002	0.000	0.000	0.000
117	A	117	TRP	0	-0.011	-0.023	33.276	0.004	0.004	0.000	0.000	0.000
118	A	118	VAL	0	0.058	0.037	35.634	0.003	0.003	0.000	0.000	0.000
119	A	119	GLU	-1	-0.942	-0.959	36.909	0.009	0.009	0.000	0.000	0.000
120	A	120	ARG	1	0.888	0.947	34.648	-0.018	-0.018	0.000	0.000	0.000
121	A	121	ALA	0	0.020	-0.011	33.630	0.003	0.003	0.000	0.000	0.000
122	A	122	ALA	0	0.017	0.010	35.200	0.003	0.003	0.000	0.000	0.000
123	A	123	LYS	1	0.926	0.959	38.078	-0.013	-0.013	0.000	0.000	0.000
124	A	124	LEU	0	-0.070	-0.034	33.469	0.002	0.002	0.000	0.000	0.000
125	A	125	PHE	0	-0.072	-0.022	29.874	0.004	0.004	0.000	0.000	0.000
126	A	126	PRO	0	0.045	0.018	35.325	-0.002	-0.002	0.000	0.000	0.000
127	A	127	GLY	0	0.001	0.004	37.890	0.002	0.002	0.000	0.000	0.000
128	A	128	SER	0	-0.010	0.003	32.737	0.000	0.000	0.000	0.000	0.000
129	A	129	PRO	0	0.078	0.025	32.934	-0.002	-0.002	0.000	0.000	0.000
130	A	130	ALA	0	-0.008	0.007	30.548	-0.003	-0.003	0.000	0.000	0.000
131	A	131	VAL	0	-0.014	-0.020	32.381	-0.003	-0.003	0.000	0.000	0.000
132	A	132	TYR	0	0.014	-0.001	35.117	-0.002	-0.002	0.000	0.000	0.000
133	A	133	LYS	1	0.949	0.986	30.801	-0.001	-0.001	0.000	0.000	0.000
134	A	134	LEU	0	-0.045	-0.026	31.989	-0.003	-0.003	0.000	0.000	0.000
135	A	135	LYS	1	0.925	0.957	35.954	-0.006	-0.006	0.000	0.000	0.000
136	A	136	GLU	-1	-0.896	-0.953	38.874	0.004	0.004	0.000	0.000	0.000
137	A	137	GLN	0	0.062	0.037	33.780	0.000	0.000	0.000	0.000	0.000
138	A	138	LEU	0	-0.064	-0.041	38.756	-0.001	-0.001	0.000	0.000	0.000
139	A	139	LEU	0	-0.039	-0.020	41.011	0.000	0.000	0.000	0.000	0.000
140	A	140	ASP	-1	-0.908	-0.941	41.316	-0.004	-0.004	0.000	0.000	0.000
141	A	141	CYS	0	-0.129	-0.059	41.292	-0.001	-0.001	0.000	0.000	0.000
142	A	142	GLU	-1	-0.977	-0.983	43.932	-0.001	-0.001	0.000	0.000	0.000
143	A	143	GLY	0	-0.041	-0.017	46.815	-0.001	-0.001	0.000	0.000	0.000
144	A	144	GLU	-1	-1.001	-1.001	49.863	-0.005	-0.005	0.000	0.000	0.000
145	A	145	ASP	-2	-1.945	-1.965	53.248	-0.006	-0.006	0.000	0.000	0.000

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