FMO DATABASE

FMODB ID: XNNJQ

Calculation Name: 2OHW-A-Xray19

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OHW

Chain ID: A

ChEMBL ID:

UniProt ID: O32092

Base Structure: X-ray

Registration Date: 2018-06-04

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	Apo structure with with a 3 angstrom solvent shell.
Procedure	Auto-FMO protocol ver. 1.20180227

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	172
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1307912.817599
FMO2-HF: Nuclear repulsion	1253250.238757
FMO2-HF: Total energy	-54662.578842
FMO2-MP2: Total energy	-54822.64285

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:2:ACE)

Summations of interaction energy for fragment #1(A:2: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.
1.572	2.712	-0.011	-0.47	-0.658	0

Interaction energy analysis for fragmet #1(A:2:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : -0.011

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

Sort

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	4	ASP	-1	-0.798	-0.894	3.858	-0.343	0.587	-0.011	-0.405	-0.514
4	A	5	LYS	1	0.787	0.899	5.724	1.803	1.803	0.000	0.000	0.000
5	A	6	MET	0	-0.029	-0.014	4.052	0.159	0.291	0.000	-0.029	-0.103
6	A	7	ASP	-1	-0.823	-0.918	5.476	0.171	0.171	0.000	0.000	0.000
7	A	8	LEU	0	-0.019	-0.007	7.495	0.111	0.111	0.000	0.000	0.000
8	A	9	TYR	0	-0.054	-0.032	9.040	0.100	0.100	0.000	0.000	0.000
9	A	10	LEU	0	0.026	-0.003	7.355	0.041	0.041	0.000	0.000	0.000
10	A	11	GLN	0	0.011	0.024	11.004	-0.019	-0.019	0.000	0.000	0.000
11	A	12	GLN	0	-0.009	-0.020	13.160	0.003	0.003	0.000	0.000	0.000
12	A	13	GLY	0	0.020	0.015	14.641	-0.005	-0.005	0.000	0.000	0.000
13	A	14	MET	0	-0.052	-0.005	11.977	0.038	0.038	0.000	0.000	0.000
14	A	15	TYR	0	0.053	0.028	14.175	0.011	0.011	0.000	0.000	0.000
15	A	16	GLY	0	0.050	0.027	15.466	-0.020	-0.020	0.000	0.000	0.000
16	A	17	PRO	0	-0.030	-0.003	14.853	0.031	0.031	0.000	0.000	0.000
17	A	18	LEU	0	0.003	0.005	8.277	-0.024	-0.024	0.000	0.000	0.000
18	A	19	GLU	-1	-0.901	-0.952	8.710	-0.442	-0.442	0.000	0.000	0.000
19	A	20	THR	0	-0.036	-0.010	9.888	0.046	0.046	0.000	0.000	0.000
20	A	21	LYS	1	0.957	0.954	11.890	-0.034	-0.034	0.000	0.000	0.000
21	A	22	PRO	0	0.014	-0.010	11.086	0.028	0.028	0.000	0.000	0.000
22	A	23	ASP	-1	-0.759	-0.864	7.271	0.293	0.293	0.000	0.000	0.000
23	A	24	GLU	-1	-0.795	-0.885	8.916	0.227	0.227	0.000	0.000	0.000
24	A	25	ARG	1	0.879	0.949	11.447	-0.153	-0.153	0.000	0.000	0.000
25	A	26	HIS	0	0.059	0.026	8.437	0.010	0.010	0.000	0.000	0.000
26	A	27	LEU	0	0.044	0.065	8.389	0.108	0.108	0.000	0.000	0.000
27	A	28	PHE	0	-0.026	-0.026	9.882	-0.033	-0.033	0.000	0.000	0.000
28	A	29	LEU	0	0.013	0.010	13.256	-0.063	-0.063	0.000	0.000	0.000
29	A	30	GLY	0	0.050	0.018	14.378	-0.047	-0.047	0.000	0.000	0.000
30	A	31	SER	0	-0.061	-0.030	16.141	-0.043	-0.043	0.000	0.000	0.000
31	A	32	LEU	0	-0.022	-0.013	15.275	0.025	0.025	0.000	0.000	0.000
32	A	33	ARG	1	0.869	0.929	14.435	-0.103	-0.103	0.000	0.000	0.000
33	A	34	GLU	-1	-0.844	-0.915	16.320	0.058	0.058	0.000	0.000	0.000
34	A	35	ARG	1	0.814	0.899	19.454	-0.100	-0.100	0.000	0.000	0.000
35	A	36	VAL	0	-0.033	0.007	16.444	0.000	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.014	0.008	19.885	-0.015	-0.015	0.000	0.000	0.000
37	A	38	LEU	0	-0.003	-0.016	20.997	-0.011	-0.011	0.000	0.000	0.000
38	A	39	ALA	0	0.016	0.021	16.301	0.015	0.015	0.000	0.000	0.000
39	A	40	LEU	0	-0.024	0.015	18.396	-0.020	-0.020	0.000	0.000	0.000
40	A	41	THR	0	0.088	0.029	14.408	0.027	0.027	0.000	0.000	0.000
41	A	42	LYS	1	0.926	0.952	13.979	-0.372	-0.372	0.000	0.000	0.000
42	A	43	GLY	0	0.024	0.014	16.598	-0.026	-0.026	0.000	0.000	0.000
43	A	44	GLN	0	0.054	0.039	18.516	-0.003	-0.003	0.000	0.000	0.000
44	A	45	VAL	0	-0.010	-0.012	19.966	-0.017	-0.017	0.000	0.000	0.000
45	A	46	LEU	0	-0.046	-0.023	19.487	-0.012	-0.012	0.000	0.000	0.000
46	A	47	ARG	1	0.833	0.939	22.891	-0.097	-0.097	0.000	0.000	0.000
47	A	48	SER	0	0.023	-0.001	25.198	0.001	0.001	0.000	0.000	0.000
48	A	49	LYS	1	0.931	0.975	28.793	-0.065	-0.065	0.000	0.000	0.000
49	A	50	PRO	0	0.028	0.029	27.527	0.003	0.003	0.000	0.000	0.000
50	A	51	TYR	0	-0.052	-0.064	23.363	-0.004	-0.004	0.000	0.000	0.000
51	A	52	LYS	1	0.858	0.909	27.577	-0.057	-0.057	0.000	0.000	0.000
52	A	53	GLU	-1	-0.809	-0.917	26.385	0.069	0.069	0.000	0.000	0.000
53	A	54	ALA	0	0.036	0.015	25.117	0.001	0.001	0.000	0.000	0.000
54	A	55	GLU	-1	-0.799	-0.879	26.744	0.063	0.063	0.000	0.000	0.000
55	A	56	HIS	0	-0.074	-0.027	29.933	-0.006	-0.006	0.000	0.000	0.000
56	A	57	GLU	-1	-0.718	-0.855	25.550	0.065	0.065	0.000	0.000	0.000
57	A	58	LEU	0	0.003	-0.010	26.930	0.000	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.898	0.967	29.855	-0.050	-0.050	0.000	0.000	0.000
59	A	60	ASN	0	-0.098	-0.054	31.925	-0.007	-0.007	0.000	0.000	0.000
60	A	61	SER	0	-0.035	0.000	29.594	-0.002	-0.002	0.000	0.000	0.000
61	A	62	HIS	0	0.025	0.005	30.586	-0.005	-0.005	0.000	0.000	0.000
62	A	63	ASN	0	-0.038	-0.008	30.237	0.004	0.004	0.000	0.000	0.000
63	A	64	VAL	0	0.022	0.016	26.072	0.004	0.004	0.000	0.000	0.000
64	A	65	THR	0	-0.061	-0.034	24.442	-0.004	-0.004	0.000	0.000	0.000
65	A	66	LEU	0	-0.011	-0.002	23.366	0.006	0.006	0.000	0.000	0.000
66	A	67	LEU	0	-0.035	-0.010	18.916	-0.004	-0.004	0.000	0.000	0.000
67	A	68	ILE	0	0.004	-0.008	20.610	0.005	0.005	0.000	0.000	0.000
68	A	69	ASN	0	0.029	0.006	14.196	-0.024	-0.024	0.000	0.000	0.000
69	A	70	GLY	0	0.037	0.010	18.212	-0.020	-0.020	0.000	0.000	0.000
70	A	71	GLU	-1	-0.762	-0.783	15.091	0.409	0.409	0.000	0.000	0.000
71	A	72	LEU	0	-0.115	-0.039	18.421	-0.017	-0.017	0.000	0.000	0.000
72	A	73	GLN	0	0.105	0.066	20.749	-0.019	-0.019	0.000	0.000	0.000
73	A	74	TYR	0	0.094	0.056	24.379	-0.004	-0.004	0.000	0.000	0.000
74	A	75	GLN	0	0.026	-0.025	27.168	-0.002	-0.002	0.000	0.000	0.000
75	A	76	SER	0	-0.051	-0.013	23.466	-0.002	-0.002	0.000	0.000	0.000
76	A	77	TYR	0	0.069	0.047	23.144	0.000	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.028	0.003	25.595	-0.008	-0.008	0.000	0.000	0.000
78	A	79	SER	0	0.054	0.012	29.033	-0.008	-0.008	0.000	0.000	0.000
79	A	80	TYR	0	0.006	-0.031	25.163	-0.008	-0.008	0.000	0.000	0.000
80	A	81	ILE	0	0.011	0.026	27.493	-0.003	-0.003	0.000	0.000	0.000
81	A	82	GLN	0	-0.065	-0.045	29.701	-0.010	-0.010	0.000	0.000	0.000
82	A	83	MET	0	-0.081	-0.019	27.824	-0.006	-0.006	0.000	0.000	0.000
83	A	84	ALA	0	0.037	0.015	28.827	-0.005	-0.005	0.000	0.000	0.000
84	A	85	SER	0	0.038	0.018	30.912	-0.005	-0.005	0.000	0.000	0.000
85	A	86	ARG	1	0.857	0.951	34.084	-0.069	-0.069	0.000	0.000	0.000
86	A	87	TYR	0	-0.058	-0.064	32.891	-0.007	-0.007	0.000	0.000	0.000
87	A	88	GLY	0	0.006	0.021	34.862	-0.001	-0.001	0.000	0.000	0.000
88	A	89	VAL	0	-0.035	-0.002	28.320	0.001	0.001	0.000	0.000	0.000
89	A	90	PRO	0	0.024	0.031	28.756	0.002	0.002	0.000	0.000	0.000
90	A	91	PHE	0	0.032	-0.009	26.302	0.005	0.005	0.000	0.000	0.000
91	A	92	LYS	1	0.931	0.963	23.401	-0.137	-0.137	0.000	0.000	0.000
92	A	93	ILE	0	0.004	0.000	22.379	0.009	0.009	0.000	0.000	0.000
93	A	94	VAL	0	-0.034	-0.017	16.986	-0.010	-0.010	0.000	0.000	0.000
94	A	95	SER	0	0.003	-0.015	18.862	0.022	0.022	0.000	0.000	0.000
95	A	96	ASP	-1	-0.902	-0.933	17.773	0.284	0.284	0.000	0.000	0.000
96	A	97	LEU	0	-0.050	-0.017	13.041	0.017	0.017	0.000	0.000	0.000
97	A	98	GLN	0	0.044	0.032	11.247	-0.031	-0.031	0.000	0.000	0.000
98	A	99	PHE	0	-0.026	-0.005	4.263	-0.052	0.026	0.000	-0.036	-0.041
99	A	100	HIS	0	0.043	0.035	8.320	-0.149	-0.149	0.000	0.000	0.000
100	A	101	THR	0	0.009	-0.003	7.836	0.291	0.291	0.000	0.000	0.000
101	A	102	PRO	0	0.073	0.045	8.308	-0.134	-0.134	0.000	0.000	0.000
102	A	103	LEU	0	-0.020	-0.011	11.241	-0.133	-0.133	0.000	0.000	0.000
103	A	104	GLY	0	-0.009	-0.023	14.067	0.018	0.018	0.000	0.000	0.000
104	A	105	ILE	0	-0.031	-0.016	17.421	-0.015	-0.015	0.000	0.000	0.000
105	A	106	VAL	0	0.010	0.009	15.963	0.007	0.007	0.000	0.000	0.000
106	A	107	ILE	0	-0.016	0.003	19.196	-0.008	-0.008	0.000	0.000	0.000
107	A	108	ALA	0	0.022	0.008	20.340	-0.001	-0.001	0.000	0.000	0.000
108	A	109	ALA	0	0.023	0.008	22.247	-0.006	-0.006	0.000	0.000	0.000
109	A	110	ASP	-1	-0.838	-0.869	24.046	0.080	0.080	0.000	0.000	0.000
110	A	111	ILE	0	-0.017	-0.010	26.182	-0.003	-0.003	0.000	0.000	0.000
111	A	112	ALA	0	-0.049	-0.026	23.673	0.007	0.007	0.000	0.000	0.000
112	A	113	VAL	0	0.003	-0.008	23.520	-0.007	-0.007	0.000	0.000	0.000
113	A	114	ASN	0	-0.067	-0.031	22.098	-0.004	-0.004	0.000	0.000	0.000
114	A	115	ARG	1	0.889	0.930	22.316	-0.074	-0.074	0.000	0.000	0.000
115	A	116	GLU	-1	-0.949	-0.982	20.919	0.017	0.017	0.000	0.000	0.000
116	A	117	LEU	0	-0.033	-0.018	20.113	0.004	0.004	0.000	0.000	0.000
117	A	118	ILE	0	-0.039	-0.014	15.965	0.004	0.004	0.000	0.000	0.000
118	A	119	TYR	0	0.014	0.022	17.737	0.018	0.018	0.000	0.000	0.000
119	A	120	ILE	0	0.004	-0.001	19.785	-0.017	-0.017	0.000	0.000	0.000
120	A	121	GLN	0	0.023	0.012	20.893	0.010	0.010	0.000	0.000	0.000
121	A	122	ASP	-1	-0.759	-0.863	21.285	0.086	0.086	0.000	0.000	0.000
122	A	123	ASP	-1	-0.858	-0.942	21.075	0.066	0.066	0.000	0.000	0.000
123	A	124	ILE	0	-0.002	-0.007	19.710	0.005	0.005	0.000	0.000	0.000
124	A	125	TYR	0	-0.039	0.003	14.128	0.033	0.033	0.000	0.000	0.000
125	A	126	ASN	0	0.036	0.016	16.105	0.019	0.019	0.000	0.000	0.000
126	A	127	ARG	1	0.861	0.933	16.051	-0.066	-0.066	0.000	0.000	0.000
127	A	128	SER	0	-0.071	-0.048	15.307	0.017	0.017	0.000	0.000	0.000
128	A	129	VAL	0	-0.029	-0.003	11.286	0.049	0.049	0.000	0.000	0.000
129	A	130	LEU	0	-0.015	-0.014	8.066	0.086	0.086	0.000	0.000	0.000
130	A	131	NME	0	-0.039	0.003	9.359	0.025	0.025	0.000	0.000	0.000
131	A	133	HOH	0	-0.031	-0.038	19.029	-0.008	-0.008	0.000	0.000	0.000
132	A	134	HOH	0	0.000	-0.003	18.007	0.002	0.002	0.000	0.000	0.000
133	A	135	HOH	0	-0.017	-0.016	20.231	-0.007	-0.007	0.000	0.000	0.000
134	A	136	HOH	0	-0.015	-0.013	22.893	-0.001	-0.001	0.000	0.000	0.000
135	A	137	HOH	0	0.024	0.037	24.536	-0.001	-0.001	0.000	0.000	0.000
136	A	138	HOH	0	-0.027	-0.026	16.589	0.000	0.000	0.000	0.000	0.000
137	A	139	HOH	0	0.011	0.002	22.395	0.006	0.006	0.000	0.000	0.000
138	A	140	HOH	0	-0.027	-0.038	23.595	-0.003	-0.003	0.000	0.000	0.000
139	A	142	HOH	0	-0.049	-0.041	16.133	0.002	0.002	0.000	0.000	0.000
140	A	143	HOH	0	-0.020	-0.015	37.808	-0.001	-0.001	0.000	0.000	0.000
141	A	144	HOH	0	0.029	0.017	26.500	0.004	0.004	0.000	0.000	0.000
142	A	145	HOH	0	-0.045	-0.043	32.000	-0.001	-0.001	0.000	0.000	0.000
143	A	147	HOH	0	0.002	0.007	13.766	0.009	0.009	0.000	0.000	0.000
144	A	148	HOH	0	-0.037	-0.026	17.469	-0.007	-0.007	0.000	0.000	0.000
145	A	150	HOH	0	-0.058	-0.042	22.138	-0.003	-0.003	0.000	0.000	0.000
146	A	152	HOH	0	-0.018	-0.026	33.757	-0.002	-0.002	0.000	0.000	0.000
147	A	153	HOH	0	-0.021	-0.011	28.681	0.002	0.002	0.000	0.000	0.000
148	A	154	HOH	0	0.029	0.017	6.564	-0.079	-0.079	0.000	0.000	0.000
149	A	155	HOH	0	-0.022	-0.034	9.565	-0.058	-0.058	0.000	0.000	0.000
150	A	157	HOH	0	0.007	0.001	24.931	0.003	0.003	0.000	0.000	0.000
151	A	158	HOH	0	-0.026	-0.012	28.146	0.000	0.000	0.000	0.000	0.000
152	A	159	HOH	0	0.069	0.053	25.419	0.003	0.003	0.000	0.000	0.000
153	A	161	HOH	0	-0.053	-0.034	13.878	-0.013	-0.013	0.000	0.000	0.000
154	A	162	HOH	0	-0.023	-0.012	18.942	-0.011	-0.011	0.000	0.000	0.000
155	A	163	HOH	0	-0.004	0.006	31.624	-0.002	-0.002	0.000	0.000	0.000
156	A	164	HOH	0	-0.050	-0.025	19.725	-0.009	-0.009	0.000	0.000	0.000
157	A	165	HOH	0	-0.040	-0.032	14.837	-0.010	-0.010	0.000	0.000	0.000
158	A	166	HOH	0	0.010	0.017	13.292	0.014	0.014	0.000	0.000	0.000
159	A	167	HOH	0	-0.045	-0.023	39.438	-0.001	-0.001	0.000	0.000	0.000
160	A	169	HOH	0	-0.009	-0.029	30.533	-0.002	-0.002	0.000	0.000	0.000
161	A	170	HOH	0	-0.018	-0.004	23.908	-0.003	-0.003	0.000	0.000	0.000
162	A	171	HOH	0	0.029	0.021	29.125	0.002	0.002	0.000	0.000	0.000
163	A	172	HOH	0	-0.025	-0.015	27.777	0.000	0.000	0.000	0.000	0.000
164	A	173	HOH	0	-0.036	-0.030	11.308	-0.011	-0.011	0.000	0.000	0.000
165	A	175	HOH	0	0.034	0.028	12.381	-0.034	-0.034	0.000	0.000	0.000
166	A	176	HOH	0	-0.098	-0.093	13.912	-0.009	-0.009	0.000	0.000	0.000
167	A	177	HOH	0	-0.002	0.000	21.941	0.004	0.004	0.000	0.000	0.000
168	A	181	HOH	0	-0.049	-0.040	28.932	-0.002	-0.002	0.000	0.000	0.000
169	A	183	HOH	0	-0.034	-0.020	21.784	-0.003	-0.003	0.000	0.000	0.000
170	A	188	HOH	0	-0.074	-0.091	15.874	-0.018	-0.018	0.000	0.000	0.000
171	A	190	HOH	0	-0.038	-0.061	28.856	-0.001	-0.001	0.000	0.000	0.000
172	A	191	HOH	0	-0.015	-0.015	11.476	-0.025	-0.025	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ACE)