FMO DATABASE

FMODB ID: XV2J1

Calculation Name: 3F7E-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3F7E

Chain ID: A

ChEMBL ID:

UniProt ID: A0QXP8

Base Structure: X-ray

Registration Date: 2018-03-01

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. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1120870.775313
FMO2-HF: Nuclear repulsion	1070590.676687
FMO2-HF: Total energy	-50280.098626
FMO2-MP2: Total energy	-50429.585197

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.
1.219	2.075	-0.007	-0.364	-0.484	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 : 0.010 / q_NPA : -0.007

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	ALA	0	0.031	0.023	3.844	1.029	1.744	-0.010	-0.307	-0.397
4	A	4	VAL	0	0.037	0.021	6.800	-0.017	-0.017	0.000	0.000	0.000
5	A	5	PRO	0	-0.028	-0.020	9.816	0.057	0.057	0.000	0.000	0.000
6	A	6	GLU	-1	-0.891	-0.905	12.967	-0.173	-0.173	0.000	0.000	0.000
7	A	7	GLY	0	0.044	-0.014	14.788	0.015	0.015	0.000	0.000	0.000
8	A	8	TYR	0	-0.052	-0.049	14.921	0.029	0.029	0.000	0.000	0.000
9	A	9	GLU	-1	-0.807	-0.892	11.669	-0.075	-0.075	0.000	0.000	0.000
10	A	10	SER	0	0.060	0.022	14.227	0.023	0.023	0.000	0.000	0.000
11	A	11	LEU	0	-0.078	-0.040	17.127	0.019	0.019	0.000	0.000	0.000
12	A	12	LEU	0	-0.045	-0.022	11.707	0.007	0.007	0.000	0.000	0.000
13	A	13	GLU	-1	-0.881	-0.939	15.728	0.010	0.010	0.000	0.000	0.000
14	A	14	ARG	1	0.878	0.945	17.713	0.077	0.077	0.000	0.000	0.000
15	A	15	PRO	0	-0.001	0.028	20.307	-0.004	-0.004	0.000	0.000	0.000
16	A	16	LEU	0	-0.009	0.000	20.906	-0.002	-0.002	0.000	0.000	0.000
17	A	17	TYR	0	-0.011	-0.002	21.372	0.004	0.004	0.000	0.000	0.000
18	A	18	GLY	0	0.024	0.012	18.934	-0.013	-0.013	0.000	0.000	0.000
19	A	19	HIS	0	-0.043	-0.030	19.905	0.017	0.017	0.000	0.000	0.000
20	A	20	LEU	0	-0.009	-0.007	15.949	-0.017	-0.017	0.000	0.000	0.000
21	A	21	ALA	0	0.000	-0.014	18.498	0.014	0.014	0.000	0.000	0.000
22	A	22	THR	0	-0.021	-0.014	18.225	-0.001	-0.001	0.000	0.000	0.000
23	A	23	VAL	0	0.045	0.013	19.973	-0.005	-0.005	0.000	0.000	0.000
24	A	24	ARG	1	0.904	0.966	22.339	0.039	0.039	0.000	0.000	0.000
25	A	25	PRO	0	0.013	-0.011	25.309	-0.005	-0.005	0.000	0.000	0.000
26	A	26	ASP	-1	-0.873	-0.918	26.596	-0.036	-0.036	0.000	0.000	0.000
27	A	27	GLY	0	0.004	0.007	25.472	-0.003	-0.003	0.000	0.000	0.000
28	A	28	THR	0	-0.046	-0.024	26.276	-0.008	-0.008	0.000	0.000	0.000
29	A	29	PRO	0	0.019	0.005	23.664	0.003	0.003	0.000	0.000	0.000
30	A	30	GLN	0	-0.083	-0.038	23.671	0.010	0.010	0.000	0.000	0.000
31	A	31	VAL	0	0.045	0.018	21.934	-0.006	-0.006	0.000	0.000	0.000
32	A	32	ASN	0	-0.021	-0.026	22.923	0.009	0.009	0.000	0.000	0.000
33	A	33	ALA	0	0.066	0.054	22.753	-0.004	-0.004	0.000	0.000	0.000
34	A	34	MET	0	-0.063	-0.033	20.553	0.010	0.010	0.000	0.000	0.000
35	A	35	TRP	0	0.044	0.043	21.810	-0.005	-0.005	0.000	0.000	0.000
36	A	36	PHE	0	-0.016	-0.011	15.749	0.003	0.003	0.000	0.000	0.000
37	A	37	ALA	0	0.018	0.009	16.723	-0.003	-0.003	0.000	0.000	0.000
38	A	38	TRP	0	-0.041	-0.037	7.433	0.010	0.010	0.000	0.000	0.000
39	A	39	ASP	-1	-0.807	-0.892	10.642	0.350	0.350	0.000	0.000	0.000
40	A	40	GLY	0	0.050	0.036	10.435	0.032	0.032	0.000	0.000	0.000
41	A	41	GLU	-1	-1.018	-1.000	6.541	0.981	0.981	0.000	0.000	0.000
42	A	42	VAL	0	-0.078	-0.053	6.429	-0.037	-0.037	0.000	0.000	0.000
43	A	43	LEU	0	-0.010	-0.002	8.952	-0.062	-0.062	0.000	0.000	0.000
44	A	44	ARG	1	0.861	0.930	12.094	-0.247	-0.247	0.000	0.000	0.000
45	A	45	PHE	0	0.033	0.006	14.097	-0.024	-0.024	0.000	0.000	0.000
46	A	46	THR	0	0.044	0.042	18.405	0.012	0.012	0.000	0.000	0.000
47	A	47	HIS	0	-0.026	-0.018	19.390	-0.013	-0.013	0.000	0.000	0.000
48	A	48	THR	0	0.016	0.010	23.465	0.005	0.005	0.000	0.000	0.000
49	A	49	THR	0	0.003	-0.007	25.077	-0.006	-0.006	0.000	0.000	0.000
50	A	50	LYS	1	0.932	0.969	26.745	-0.031	-0.031	0.000	0.000	0.000
51	A	51	ARG	1	0.914	0.957	27.170	-0.008	-0.008	0.000	0.000	0.000
52	A	52	GLN	0	0.019	-0.009	26.861	0.006	0.006	0.000	0.000	0.000
53	A	53	LYS	1	0.904	0.959	22.792	0.008	0.008	0.000	0.000	0.000
54	A	54	TYR	0	0.105	0.069	22.323	-0.002	-0.002	0.000	0.000	0.000
55	A	55	ARG	1	0.886	0.928	22.713	-0.004	-0.004	0.000	0.000	0.000
56	A	56	ASN	0	0.010	0.007	22.260	0.005	0.005	0.000	0.000	0.000
57	A	57	ILE	0	0.030	0.020	18.017	-0.003	-0.003	0.000	0.000	0.000
58	A	58	LYS	1	0.848	0.931	18.990	-0.053	-0.053	0.000	0.000	0.000
59	A	59	ALA	0	-0.024	-0.001	21.396	0.006	0.006	0.000	0.000	0.000
60	A	60	ASN	0	0.010	0.002	18.011	-0.007	-0.007	0.000	0.000	0.000
61	A	61	PRO	0	0.050	0.035	14.245	-0.008	-0.008	0.000	0.000	0.000
62	A	62	ALA	0	-0.003	0.010	13.773	-0.002	-0.002	0.000	0.000	0.000
63	A	63	VAL	0	-0.027	-0.017	13.107	0.016	0.016	0.000	0.000	0.000
64	A	64	ALA	0	-0.020	-0.013	13.767	-0.053	-0.053	0.000	0.000	0.000
65	A	65	MET	0	-0.018	0.012	14.484	0.051	0.051	0.000	0.000	0.000
66	A	66	SER	0	0.007	0.024	15.844	-0.029	-0.029	0.000	0.000	0.000
67	A	67	VAL	0	0.018	0.007	16.868	0.025	0.025	0.000	0.000	0.000
68	A	68	ILE	0	-0.017	-0.004	19.563	-0.019	-0.019	0.000	0.000	0.000
69	A	69	ASP	-1	-0.815	-0.912	22.413	-0.069	-0.069	0.000	0.000	0.000
70	A	70	PRO	0	-0.065	-0.028	24.154	-0.001	-0.001	0.000	0.000	0.000
71	A	71	ASP	-1	-0.873	-0.934	27.402	-0.046	-0.046	0.000	0.000	0.000
72	A	72	ASN	0	-0.032	-0.018	27.069	0.000	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.035	0.013	26.130	-0.009	-0.009	0.000	0.000	0.000
74	A	74	TYR	0	-0.012	-0.025	25.527	-0.010	-0.010	0.000	0.000	0.000
75	A	75	ARG	1	0.840	0.947	19.711	0.119	0.119	0.000	0.000	0.000
76	A	76	TYR	0	0.018	0.004	19.228	0.017	0.017	0.000	0.000	0.000
77	A	77	LEU	0	-0.027	-0.022	12.718	-0.027	-0.027	0.000	0.000	0.000
78	A	78	GLU	-1	-0.963	-0.970	15.645	-0.212	-0.212	0.000	0.000	0.000
79	A	79	VAL	0	0.008	-0.001	9.817	-0.075	-0.075	0.000	0.000	0.000
80	A	80	ARG	1	0.959	0.970	11.134	0.517	0.517	0.000	0.000	0.000
81	A	81	GLY	0	0.087	0.037	8.971	-0.145	-0.145	0.000	0.000	0.000
82	A	82	LEU	0	-0.030	-0.004	8.878	0.020	0.020	0.000	0.000	0.000
83	A	83	VAL	0	-0.053	-0.035	10.242	0.065	0.065	0.000	0.000	0.000
84	A	84	GLU	-1	-0.843	-0.903	8.101	0.838	0.838	0.000	0.000	0.000
85	A	85	ASP	-1	-0.843	-0.921	11.878	0.266	0.266	0.000	0.000	0.000
86	A	86	ILE	0	-0.107	-0.065	14.771	-0.038	-0.038	0.000	0.000	0.000
87	A	87	VAL	0	0.032	0.028	17.370	0.000	0.000	0.000	0.000	0.000
88	A	88	PRO	0	-0.031	-0.018	20.081	-0.014	-0.014	0.000	0.000	0.000
89	A	89	ASP	-1	-0.799	-0.917	23.254	0.085	0.085	0.000	0.000	0.000
90	A	90	PRO	0	0.030	0.019	25.066	-0.008	-0.008	0.000	0.000	0.000
91	A	91	THR	0	-0.045	-0.034	28.325	-0.006	-0.006	0.000	0.000	0.000
92	A	92	GLY	0	0.006	-0.001	27.461	-0.005	-0.005	0.000	0.000	0.000
93	A	93	ALA	0	0.043	0.029	26.073	-0.003	-0.003	0.000	0.000	0.000
94	A	94	PHE	0	-0.016	-0.020	18.439	0.001	0.001	0.000	0.000	0.000
95	A	95	TYR	0	-0.024	-0.030	23.387	-0.006	-0.006	0.000	0.000	0.000
96	A	96	LEU	0	0.006	-0.001	25.219	-0.005	-0.005	0.000	0.000	0.000
97	A	97	LYS	1	0.954	0.985	22.181	-0.094	-0.094	0.000	0.000	0.000
98	A	98	LEU	0	-0.047	-0.013	19.496	-0.004	-0.004	0.000	0.000	0.000
99	A	99	ASN	0	0.048	0.000	23.284	-0.010	-0.010	0.000	0.000	0.000
100	A	100	ASP	-1	-0.942	-0.962	26.107	0.033	0.033	0.000	0.000	0.000
101	A	101	ARG	1	0.831	0.914	19.124	-0.006	-0.006	0.000	0.000	0.000
102	A	102	TYR	0	-0.096	-0.079	20.990	-0.006	-0.006	0.000	0.000	0.000
103	A	103	ASP	-1	-0.925	-0.940	26.158	0.007	0.007	0.000	0.000	0.000
104	A	104	GLY	0	-0.030	-0.013	29.076	-0.004	-0.004	0.000	0.000	0.000
105	A	105	PRO	0	0.002	-0.021	30.551	0.003	0.003	0.000	0.000	0.000
106	A	106	LEU	0	-0.113	-0.035	29.147	0.001	0.001	0.000	0.000	0.000
107	A	107	THR	0	0.032	-0.016	30.880	0.003	0.003	0.000	0.000	0.000
108	A	108	GLU	-1	-0.896	-0.920	32.924	0.025	0.025	0.000	0.000	0.000
109	A	109	PRO	0	-0.062	-0.028	31.450	0.000	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.021	0.019	29.329	-0.003	-0.003	0.000	0.000	0.000
111	A	111	ALA	0	0.045	0.004	32.662	0.002	0.002	0.000	0.000	0.000
112	A	112	ASP	-1	-0.868	-0.910	30.563	0.029	0.029	0.000	0.000	0.000
113	A	113	LYS	1	0.994	0.987	29.924	-0.039	-0.039	0.000	0.000	0.000
114	A	114	ALA	0	0.012	0.011	29.550	0.005	0.005	0.000	0.000	0.000
115	A	115	ASP	-1	-0.887	-0.939	29.211	0.040	0.040	0.000	0.000	0.000
116	A	116	ARG	1	0.770	0.863	25.532	-0.034	-0.034	0.000	0.000	0.000
117	A	117	VAL	0	-0.017	-0.008	21.580	0.006	0.006	0.000	0.000	0.000
118	A	118	ILE	0	0.007	0.001	17.127	-0.012	-0.012	0.000	0.000	0.000
119	A	119	ILE	0	-0.041	-0.018	15.588	0.012	0.012	0.000	0.000	0.000
120	A	120	VAL	0	0.054	0.020	11.019	-0.022	-0.022	0.000	0.000	0.000
121	A	121	VAL	0	-0.015	-0.009	10.064	0.008	0.008	0.000	0.000	0.000
122	A	122	ARG	1	0.919	0.939	3.608	-1.747	-1.590	0.004	-0.049	-0.112
123	A	123	PRO	0	-0.017	-0.007	5.582	-0.111	-0.111	0.000	0.000	0.000
124	A	124	THR	0	-0.032	-0.032	4.742	-0.292	-0.308	-0.001	-0.008	0.025
125	A	125	ALA	0	-0.040	-0.024	6.882	-0.241	-0.241	0.000	0.000	0.000
126	A	126	PHE	0	0.040	0.021	6.646	0.212	0.212	0.000	0.000	0.000
127	A	127	SER	0	-0.024	-0.007	11.302	-0.018	-0.018	0.000	0.000	0.000
128	A	128	LYS	1	0.954	0.989	15.007	0.306	0.306	0.000	0.000	0.000
129	A	129	GLN	0	-0.008	-0.006	17.733	0.040	0.040	0.000	0.000	0.000
130	A	130	NME	0	0.021	0.022	20.027	-0.016	-0.016	0.000	0.000	0.000

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