FMO DATABASE

FMODB ID: P7JGK

Calculation Name: 1SAU-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SAU

Chain ID: A

ChEMBL ID:

UniProt ID: O28055

Base Structure: X-ray

Registration Date: 2018-02-14

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	114
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1012861.694239
FMO2-HF: Nuclear repulsion	965839.943483
FMO2-HF: Total energy	-47021.750757
FMO2-MP2: Total energy	-47158.529538

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.
-3.64	-3.239	2.87	-1.935	-1.337	-0.015

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 : -0.030

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	3	GLU	-1	-0.865	-0.920	3.942	-1.536	-1.224	0.001	-0.253	-0.061	0.000
4	A	4	LEU	0	0.007	-0.001	6.790	0.326	0.326	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.890	-0.937	10.032	-0.421	-0.421	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.036	0.011	13.023	0.068	0.068	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.723	0.821	15.858	0.211	0.211	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.010	0.014	17.779	0.024	0.024	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.800	0.888	14.223	0.220	0.220	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.891	0.948	10.051	0.534	0.534	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.009	0.027	9.558	0.005	0.005	0.000	0.000	0.000	0.000
12	A	12	ARG	1	0.995	0.993	3.274	-2.397	-2.119	0.039	-0.149	-0.169	0.001
13	A	13	LEU	0	-0.031	-0.017	4.422	0.785	0.947	-0.001	-0.046	-0.114	0.000
14	A	14	ASP	-1	-0.792	-0.892	2.448	-1.223	-1.640	2.826	-1.483	-0.926	-0.016
15	A	15	GLU	-1	-0.934	-0.981	3.688	0.721	0.782	0.006	-0.003	-0.064	0.000
16	A	16	ASP	-1	-0.970	-0.965	5.392	0.152	0.157	-0.001	-0.001	-0.003	0.000
17	A	17	GLY	0	0.022	-0.002	6.682	-0.040	-0.040	0.000	0.000	0.000	0.000
18	A	18	PHE	0	-0.078	-0.042	7.562	-0.059	-0.059	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.013	0.022	6.790	-0.082	-0.082	0.000	0.000	0.000	0.000
20	A	20	GLN	0	-0.091	-0.091	4.978	0.399	0.399	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.797	-0.873	7.899	-0.334	-0.334	0.000	0.000	0.000	0.000
22	A	22	TRP	0	-0.005	-0.019	10.449	-0.050	-0.050	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.914	-0.964	12.867	-0.069	-0.069	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.840	-0.909	13.272	-0.203	-0.203	0.000	0.000	0.000	0.000
25	A	25	TRP	0	-0.070	-0.024	15.025	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.759	-0.876	16.185	-0.175	-0.175	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.939	-0.975	18.754	-0.115	-0.115	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.824	-0.910	20.112	-0.164	-0.164	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.035	-0.012	13.739	-0.032	-0.032	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.035	-0.010	15.706	-0.027	-0.027	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.808	-0.892	17.626	-0.172	-0.172	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.017	-0.013	15.061	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.007	-0.002	11.016	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	34	ALA	0	-0.056	-0.027	14.441	0.011	0.011	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.805	0.883	17.440	0.187	0.187	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.759	-0.864	10.991	-0.659	-0.659	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.041	-0.031	14.305	0.002	0.002	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.733	0.857	8.693	1.046	1.046	0.000	0.000	0.000	0.000
39	A	39	PHE	0	-0.026	0.006	6.850	0.041	0.041	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.032	0.006	12.583	0.067	0.067	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.018	0.018	16.332	-0.020	-0.020	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.050	-0.040	19.516	0.011	0.011	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.007	0.009	19.285	0.003	0.003	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.002	0.003	20.193	0.017	0.017	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.933	-0.957	22.233	-0.111	-0.111	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.024	-0.019	20.431	0.012	0.012	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.040	-0.002	24.820	0.004	0.004	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.900	-0.962	27.692	-0.046	-0.046	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.827	-0.892	29.426	-0.036	-0.036	0.000	0.000	0.000	0.000
50	A	50	HIS	0	0.015	0.025	23.758	0.005	0.005	0.000	0.000	0.000	0.000
51	A	51	TRP	0	0.055	0.027	21.930	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.857	0.937	25.919	0.039	0.039	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.033	-0.015	23.345	0.006	0.006	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.036	0.019	20.303	0.008	0.008	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.986	0.990	22.245	0.053	0.053	0.000	0.000	0.000	0.000
56	A	56	TYR	0	0.003	0.019	24.663	0.009	0.009	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.026	-0.026	19.087	0.009	0.009	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.861	0.935	15.664	0.091	0.091	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.900	-0.951	21.032	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	60	TYR	0	-0.103	-0.054	22.961	0.010	0.010	0.000	0.000	0.000	0.000
61	A	61	PHE	0	0.017	0.011	15.596	0.008	0.008	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.009	0.002	19.351	0.010	0.010	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.847	0.933	21.941	0.002	0.002	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.039	-0.040	24.153	0.002	0.002	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.001	0.016	20.660	0.008	0.008	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.035	-0.008	18.794	0.019	0.019	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.050	0.022	17.909	-0.019	-0.019	0.000	0.000	0.000	0.000
68	A	68	PRO	0	-0.011	0.002	19.855	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.023	0.012	22.631	0.000	0.000	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.115	0.032	23.607	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.934	0.967	25.681	-0.041	-0.041	0.000	0.000	0.000	0.000
72	A	72	MET	0	-0.076	-0.047	27.102	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.078	0.050	22.482	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.014	0.012	27.194	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.848	0.918	30.214	-0.016	-0.016	0.000	0.000	0.000	0.000
76	A	76	HIS	0	0.036	0.021	28.719	0.002	0.002	0.000	0.000	0.000	0.000
77	A	85	CYS	0	-0.023	0.018	29.475	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.910	0.951	31.349	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.893	0.945	34.534	0.002	0.002	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.869	-0.924	32.350	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.067	-0.024	30.195	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.879	0.886	33.612	0.021	0.021	0.000	0.000	0.000	0.000
83	A	83	PRO	0	0.020	0.021	35.851	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.849	-0.883	37.888	-0.013	-0.013	0.000	0.000	0.000	0.000
85	A	86	ASN	0	0.029	0.002	32.580	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.050	0.009	26.413	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	88	GLN	0	0.023	0.013	28.580	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.082	-0.082	29.700	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.029	-0.004	24.956	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	TYR	0	0.022	0.016	23.106	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.898	0.969	25.708	0.029	0.029	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.066	-0.024	25.796	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	94	PHE	0	0.024	0.010	20.592	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	95	PRO	0	0.042	0.037	21.370	0.014	0.014	0.000	0.000	0.000	0.000
95	A	96	GLN	0	-0.093	-0.074	15.584	0.022	0.022	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.012	-0.001	19.686	0.017	0.017	0.000	0.000	0.000	0.000
97	A	98	PRO	0	-0.044	-0.033	19.799	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.039	0.011	17.088	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.917	0.950	11.299	0.038	0.038	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.725	-0.843	14.741	-0.124	-0.124	0.000	0.000	0.000	0.000
101	A	102	ALA	0	-0.008	0.003	16.902	-0.016	-0.016	0.000	0.000	0.000	0.000
102	A	103	CYS	0	-0.055	-0.037	15.819	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.863	0.940	11.273	0.209	0.209	0.000	0.000	0.000	0.000
104	A	105	ILE	0	0.009	0.009	13.719	-0.033	-0.033	0.000	0.000	0.000	0.000
105	A	106	ALA	0	-0.012	0.001	16.136	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.035	0.007	13.355	0.010	0.010	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.035	-0.014	13.717	0.016	0.016	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.033	0.029	10.071	-0.020	-0.020	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.823	0.886	7.064	-0.701	-0.701	0.000	0.000	0.000	0.000
110	A	111	PRO	0	0.046	0.044	11.951	-0.037	-0.037	0.000	0.000	0.000	0.000
111	A	112	THR	0	0.011	-0.012	14.803	-0.009	-0.009	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.028	0.009	16.664	-0.015	-0.015	0.000	0.000	0.000	0.000
113	A	114	CYS	0	-0.101	-0.022	18.933	-0.020	-0.020	0.000	0.000	0.000	0.000
114	A	115	VAL	-1	-0.874	-0.943	20.565	0.052	0.052	0.000	0.000	0.000	0.000

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