FMO DATABASE

FMODB ID: YVGV2

Calculation Name: 2B0A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2B0A

Chain ID: A

ChEMBL ID:

UniProt ID: Q58193

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	186
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2064395.916682
FMO2-HF: Nuclear repulsion	1990689.285005
FMO2-HF: Total energy	-73706.631677
FMO2-MP2: Total energy	-73921.917776

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:GLU)

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

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.
-5.76	-1.267	0.879	-2.275	-3.096	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.914 / q_NPA : -0.962

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	LEU	0	-0.020	-0.005	3.687	-3.572	-2.049	-0.011	-0.721	-0.790	0.003
4	A	4	ASP	-1	-0.746	-0.846	6.867	21.865	21.865	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.007	-0.002	9.829	-1.187	-1.187	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.013	-0.023	13.119	-1.748	-1.748	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.002	0.014	15.437	0.565	0.565	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.045	-0.023	18.275	0.325	0.325	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.002	-0.007	19.145	-0.564	-0.564	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.013	-0.004	21.900	-0.198	-0.198	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.004	-0.033	25.108	0.078	0.078	0.000	0.000	0.000	0.000
12	A	12	PHE	0	-0.011	-0.003	26.379	-0.208	-0.208	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.037	0.016	27.921	0.391	0.391	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.903	0.962	30.233	-9.540	-9.540	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.001	-0.020	32.041	-0.167	-0.167	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.001	0.007	35.622	-0.133	-0.133	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.924	-0.954	31.255	9.756	9.756	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.066	-0.046	33.148	-0.094	-0.094	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.860	-0.917	32.067	9.107	9.107	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.063	-0.020	26.105	0.087	0.087	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.923	0.957	30.095	-8.741	-8.741	0.000	0.000	0.000	0.000
22	A	22	ILE	0	0.032	0.015	26.084	0.072	0.072	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.071	-0.035	30.556	-0.281	-0.281	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.848	-0.911	30.976	9.561	9.561	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.907	0.947	32.824	-8.700	-8.700	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.899	0.943	33.903	-8.601	-8.601	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.015	-0.018	35.798	-0.286	-0.286	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.901	-0.954	36.343	8.171	8.171	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.005	0.010	36.400	0.091	0.091	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.019	0.001	31.070	0.346	0.346	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.013	-0.012	29.958	-0.285	-0.285	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.005	0.008	29.786	0.340	0.340	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.034	-0.044	28.565	-0.065	-0.065	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.927	-0.938	30.149	8.992	8.992	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.008	-0.027	25.525	0.131	0.131	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.003	0.014	29.768	-0.079	-0.079	0.000	0.000	0.000	0.000
37	A	37	MET	0	0.028	0.008	24.524	0.237	0.237	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.041	0.033	30.106	-0.175	-0.175	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.067	-0.067	28.246	0.357	0.357	0.000	0.000	0.000	0.000
40	A	40	HIS	1	0.839	0.906	26.988	-10.198	-10.198	0.000	0.000	0.000	0.000
41	A	41	LEU	0	-0.016	0.013	25.760	0.182	0.182	0.000	0.000	0.000	0.000
42	A	42	CYS	0	-0.045	0.012	21.875	0.434	0.434	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.021	0.004	17.552	-0.093	-0.093	0.000	0.000	0.000	0.000
44	A	44	HIS	1	0.830	0.930	20.801	-12.082	-12.082	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.009	-0.012	21.127	0.293	0.293	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.786	-0.892	23.342	10.787	10.787	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.043	-0.035	24.064	0.567	0.567	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.011	-0.005	28.782	-0.252	-0.252	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.832	0.916	32.198	-9.324	-9.324	0.000	0.000	0.000	0.000
50	A	50	HIS	0	-0.007	-0.001	31.126	-0.377	-0.377	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.026	-0.002	33.266	-0.187	-0.187	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.017	0.000	35.786	-0.270	-0.270	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.073	-0.040	35.310	-0.235	-0.235	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.906	-0.950	35.179	8.740	8.740	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.017	-0.013	30.487	0.193	0.193	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.901	0.939	29.726	-9.937	-9.937	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.023	-0.014	25.445	0.298	0.298	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.005	0.009	24.453	0.046	0.046	0.000	0.000	0.000	0.000
59	A	59	PHE	0	0.045	0.022	19.410	0.425	0.425	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.896	0.917	21.215	-14.174	-14.174	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.873	-0.926	20.249	14.981	14.981	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.072	0.035	21.727	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.070	-0.019	15.275	0.306	0.306	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.026	0.023	17.318	0.014	0.014	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.937	0.972	14.109	-17.018	-17.018	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.024	0.009	14.068	-1.550	-1.550	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.852	0.935	12.868	-18.292	-18.292	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.036	0.015	12.410	-1.402	-1.402	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.029	-0.035	13.063	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.070	-0.018	13.454	-0.626	-0.626	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.001	0.009	15.152	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.021	-0.011	18.364	0.355	0.355	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.065	-0.039	20.379	-0.238	-0.238	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.845	-0.899	23.546	11.415	11.415	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.921	-0.961	20.958	12.299	12.299	0.000	0.000	0.000	0.000
76	A	76	PHE	0	-0.072	-0.051	21.855	0.052	0.052	0.000	0.000	0.000	0.000
77	A	77	PRO	0	0.003	0.009	25.096	-0.183	-0.183	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.012	-0.008	28.411	-0.275	-0.275	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.037	0.003	23.856	-0.457	-0.457	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.960	0.971	25.037	-11.268	-11.268	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.011	0.017	23.166	0.400	0.400	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.002	0.005	17.999	-0.069	-0.069	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.006	0.005	19.436	-0.144	-0.144	0.000	0.000	0.000	0.000
84	A	84	CYS	0	-0.101	-0.048	16.675	0.869	0.869	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.786	-0.871	17.309	15.887	15.887	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.030	-0.014	15.512	-0.745	-0.745	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.030	0.012	16.344	0.665	0.665	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.028	-0.013	12.981	-0.321	-0.321	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.020	-0.002	17.032	-0.200	-0.200	0.000	0.000	0.000	0.000
90	A	90	TYR	0	0.012	-0.004	17.097	0.067	0.067	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.008	-0.031	19.106	-0.622	-0.622	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.006	0.016	20.809	-0.446	-0.446	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.025	-0.032	21.975	-0.231	-0.231	0.000	0.000	0.000	0.000
94	A	94	SER	0	0.041	-0.011	19.659	-0.191	-0.191	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.823	0.920	21.608	-11.286	-11.286	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.054	-0.035	23.174	-0.498	-0.498	0.000	0.000	0.000	0.000
97	A	97	TRP	0	0.058	0.028	21.896	-0.435	-0.435	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.011	0.002	24.575	0.060	0.060	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.818	0.885	26.766	-10.336	-10.336	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.840	-0.925	29.864	9.311	9.311	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.842	-0.913	31.049	9.580	9.580	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.057	-0.050	23.790	0.100	0.100	0.000	0.000	0.000	0.000
103	A	103	PHE	0	-0.001	-0.013	28.777	0.155	0.155	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.869	-0.943	30.975	8.718	8.718	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.839	0.942	28.075	-9.830	-9.830	0.000	0.000	0.000	0.000
106	A	106	ILE	0	0.005	0.000	28.731	0.374	0.374	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.040	-0.013	26.313	-0.117	-0.117	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.915	-0.952	28.758	8.601	8.601	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.008	-0.013	25.539	0.256	0.256	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.031	0.021	28.534	-0.134	-0.134	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.028	0.011	23.979	-0.156	-0.156	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.027	0.010	28.358	0.254	0.254	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.784	-0.879	29.449	8.924	8.924	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.870	-0.932	28.577	9.557	9.557	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.003	0.000	24.409	0.234	0.234	0.000	0.000	0.000	0.000
116	A	116	ILE	0	0.003	0.016	26.928	0.180	0.180	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.785	0.902	29.977	-9.386	-9.386	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.059	-0.034	25.514	0.227	0.227	0.000	0.000	0.000	0.000
119	A	119	ASN	0	0.001	-0.011	24.522	-0.252	-0.252	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.009	0.005	21.029	0.569	0.569	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.838	0.899	21.290	-14.751	-14.751	0.000	0.000	0.000	0.000
122	A	122	CYS	0	-0.070	-0.029	19.708	-0.195	-0.195	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.031	0.029	20.329	0.441	0.441	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.021	0.005	18.444	0.020	0.020	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.008	0.003	19.370	0.086	0.086	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.738	-0.822	18.267	14.122	14.122	0.000	0.000	0.000	0.000
127	A	127	ALA	0	0.016	0.013	20.069	-0.394	-0.394	0.000	0.000	0.000	0.000
128	A	128	CYS	0	-0.031	0.001	23.888	0.131	0.131	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.009	-0.004	26.532	-0.144	-0.144	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.008	0.005	24.616	0.194	0.194	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.010	0.007	27.207	-0.167	-0.167	0.000	0.000	0.000	0.000
132	A	132	GLY	0	0.045	0.023	31.049	0.022	0.022	0.000	0.000	0.000	0.000
133	A	133	PHE	0	-0.017	-0.003	33.390	0.272	0.272	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.838	-0.931	34.911	8.225	8.225	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.874	-0.929	31.058	9.006	9.006	0.000	0.000	0.000	0.000
136	A	136	HIS	1	0.780	0.869	28.534	-10.127	-10.127	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.933	0.966	31.418	-8.057	-8.057	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.855	0.911	33.192	-8.811	-8.811	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.022	0.031	26.651	0.051	0.051	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.009	-0.001	28.238	0.061	0.061	0.000	0.000	0.000	0.000
141	A	141	SER	0	-0.070	-0.057	30.798	-0.026	-0.026	0.000	0.000	0.000	0.000
142	A	142	ASN	0	-0.055	-0.034	31.599	-0.234	-0.234	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.027	-0.011	27.613	-0.092	-0.092	0.000	0.000	0.000	0.000
144	A	144	ILE	0	-0.012	0.014	24.633	0.479	0.479	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.027	-0.016	23.300	-0.259	-0.259	0.000	0.000	0.000	0.000
146	A	146	ILE	0	0.035	0.012	23.648	0.224	0.224	0.000	0.000	0.000	0.000
147	A	147	ILE	0	0.008	-0.004	18.316	0.013	0.013	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.760	-0.857	21.569	11.418	11.418	0.000	0.000	0.000	0.000
149	A	149	ASN	0	0.013	0.007	22.089	0.028	0.028	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.001	0.021	15.687	0.575	0.575	0.000	0.000	0.000	0.000
151	A	151	ASN	0	-0.050	-0.032	13.058	-0.543	-0.543	0.000	0.000	0.000	0.000
152	A	152	GLU	-1	-0.809	-0.933	15.574	17.316	17.316	0.000	0.000	0.000	0.000
153	A	153	ASN	0	-0.034	-0.028	10.627	0.687	0.687	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.032	0.012	11.639	1.037	1.037	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.993	1.011	13.792	-15.503	-15.503	0.000	0.000	0.000	0.000
156	A	156	ASN	0	-0.079	-0.040	9.695	-1.254	-1.254	0.000	0.000	0.000	0.000
157	A	157	LEU	0	0.010	0.012	7.761	1.528	1.528	0.000	0.000	0.000	0.000
158	A	158	VAL	0	0.010	0.011	10.884	-0.294	-0.294	0.000	0.000	0.000	0.000
159	A	159	GLY	0	0.000	0.004	13.879	0.179	0.179	0.000	0.000	0.000	0.000
160	A	160	LYS	1	0.816	0.916	8.885	-22.517	-22.517	0.000	0.000	0.000	0.000
161	A	161	SER	0	0.004	-0.004	10.977	-1.004	-1.004	0.000	0.000	0.000	0.000
162	A	162	PHE	0	0.027	0.025	7.570	1.407	1.407	0.000	0.000	0.000	0.000
163	A	163	TYR	0	0.008	0.018	8.131	-3.190	-3.190	0.000	0.000	0.000	0.000
164	A	164	PHE	0	0.044	0.005	9.133	1.967	1.967	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.024	-0.019	8.920	-0.882	-0.882	0.000	0.000	0.000	0.000
166	A	166	GLY	0	0.049	0.019	12.241	0.409	0.409	0.000	0.000	0.000	0.000
167	A	167	LEU	0	-0.045	-0.032	12.318	-0.772	-0.772	0.000	0.000	0.000	0.000
168	A	168	PRO	0	0.006	0.005	16.356	-0.067	-0.067	0.000	0.000	0.000	0.000
169	A	169	LEU	0	0.021	0.016	19.972	0.191	0.191	0.000	0.000	0.000	0.000
170	A	170	LYS	1	0.857	0.926	21.497	-14.506	-14.506	0.000	0.000	0.000	0.000
171	A	171	ILE	0	0.024	0.018	23.430	-0.440	-0.440	0.000	0.000	0.000	0.000
172	A	172	PHE	0	-0.029	-0.029	24.314	0.321	0.321	0.000	0.000	0.000	0.000
173	A	173	ASP	-1	-0.846	-0.921	28.970	8.898	8.898	0.000	0.000	0.000	0.000
174	A	174	ILE	0	0.027	0.041	28.174	-0.334	-0.334	0.000	0.000	0.000	0.000
175	A	175	ASP	-1	-0.779	-0.880	30.852	10.228	10.228	0.000	0.000	0.000	0.000
176	A	176	ALA	0	0.036	0.009	26.987	0.157	0.157	0.000	0.000	0.000	0.000
177	A	177	SER	0	-0.031	-0.020	23.729	-0.116	-0.116	0.000	0.000	0.000	0.000
178	A	178	PRO	0	0.034	0.027	21.700	0.354	0.354	0.000	0.000	0.000	0.000
179	A	179	ILE	0	-0.019	-0.020	17.304	0.269	0.269	0.000	0.000	0.000	0.000
180	A	180	ARG	1	0.865	0.936	11.999	-21.643	-21.643	0.000	0.000	0.000	0.000
181	A	181	CYS	0	-0.024	-0.008	13.616	-0.057	-0.057	0.000	0.000	0.000	0.000
182	A	182	ILE	0	-0.002	0.001	7.117	0.431	0.431	0.000	0.000	0.000	0.000
183	A	183	ALA	0	0.016	0.013	7.581	-1.511	-1.511	0.000	0.000	0.000	0.000
184	A	184	ILE	0	-0.012	-0.013	3.931	2.199	2.609	0.002	-0.163	-0.248	0.001
185	A	185	LEU	0	-0.041	-0.028	2.212	-7.190	-6.136	0.798	-0.639	-1.214	0.002
186	A	186	GLU	-1	-0.925	-0.960	3.072	28.022	29.528	0.090	-0.752	-0.844	-0.007

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