FMO DATABASE

FMODB ID: NNGGQ

Calculation Name: 2PTH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PTH

Chain ID: A

ChEMBL ID:

UniProt ID: P0A7D1

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	OptH
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	193
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2089520.773116
FMO2-HF: Nuclear repulsion	2016932.686956
FMO2-HF: Total energy	-72588.086161
FMO2-MP2: Total energy	-72802.954777

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:THR)

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

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.
-8.398	-2.229	0.406	-2.288	-4.287	0.007

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.023

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	LYS	1	0.947	0.964	2.902	2.023	4.954	0.108	-1.333	-1.706	0.005
4	A	4	LEU	0	-0.041	-0.014	4.770	0.230	0.329	-0.001	-0.008	-0.091	0.000
5	A	5	ILE	0	0.026	0.019	8.367	-0.032	-0.032	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.025	-0.021	10.851	-0.021	-0.021	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.032	0.015	14.299	0.049	0.049	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.063	-0.042	17.585	-0.021	-0.021	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.017	-0.002	20.439	0.024	0.024	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.025	0.011	23.914	-0.026	-0.026	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.035	0.020	26.831	0.007	0.007	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.058	0.025	27.990	0.003	0.003	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.004	-0.020	30.731	0.004	0.004	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.967	-0.970	32.724	-0.025	-0.025	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.032	0.004	29.844	0.002	0.002	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.001	0.020	28.560	0.005	0.005	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.001	0.002	28.259	0.007	0.007	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.069	-0.044	29.664	0.006	0.006	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.939	0.962	27.513	-0.036	-0.036	0.000	0.000	0.000	0.000
20	A	20	HIS	0	-0.074	-0.063	25.703	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.013	0.021	24.237	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.032	0.018	22.398	0.004	0.004	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.008	-0.007	18.724	0.019	0.019	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.008	-0.012	18.507	0.013	0.013	0.000	0.000	0.000	0.000
25	A	25	TRP	0	0.018	0.016	20.470	0.013	0.013	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.005	-0.003	12.635	0.005	0.005	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.001	-0.005	14.946	0.026	0.026	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.893	-0.948	16.904	0.008	0.008	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.047	-0.012	18.534	0.002	0.002	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.029	-0.021	12.120	0.013	0.013	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.020	0.012	16.029	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.962	-0.976	17.676	0.067	0.067	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.868	0.915	17.725	-0.226	-0.226	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.001	0.009	13.167	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.848	0.934	17.491	-0.080	-0.080	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.016	0.021	16.804	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	37	PRO	0	-0.035	-0.030	18.598	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.025	0.029	17.317	-0.024	-0.024	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.951	0.972	20.467	0.175	0.175	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.895	-0.931	21.268	-0.132	-0.132	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.941	-0.961	18.917	-0.254	-0.254	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.047	0.004	22.329	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.890	0.957	20.222	0.290	0.290	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.002	-0.010	17.402	-0.027	-0.027	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.018	-0.016	19.885	0.000	0.000	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.120	0.052	20.668	0.007	0.007	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.008	0.006	20.366	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.037	-0.030	16.153	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.024	-0.006	15.389	0.018	0.018	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.777	0.868	11.326	0.509	0.509	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.003	0.005	10.665	0.032	0.032	0.000	0.000	0.000	0.000
52	A	52	THR	0	0.005	0.011	9.553	-0.062	-0.062	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.001	-0.008	7.650	0.062	0.062	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.050	0.025	6.906	0.075	0.075	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.040	-0.018	7.506	-0.046	-0.046	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.923	-0.957	2.854	-5.058	-4.328	0.046	-0.228	-0.548	-0.002
57	A	57	ASP	-1	-0.847	-0.900	5.805	-0.164	-0.164	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.006	0.009	5.677	-0.179	-0.179	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.913	0.956	7.886	0.619	0.619	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.012	0.007	10.401	0.037	0.037	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.006	-0.015	13.179	-0.044	-0.044	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.028	0.032	15.677	0.022	0.022	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.040	-0.027	18.355	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.018	-0.017	20.996	0.015	0.015	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.052	-0.030	23.338	0.002	0.002	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.043	0.020	25.745	0.005	0.005	0.000	0.000	0.000	0.000
67	A	67	MET	0	0.058	0.039	23.510	-0.023	-0.023	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.031	-0.024	24.494	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.024	0.002	25.655	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.006	-0.017	20.505	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.017	-0.019	19.629	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.897	0.961	19.455	0.128	0.128	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.044	0.028	19.196	-0.021	-0.021	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.001	0.005	13.939	-0.034	-0.034	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.020	0.013	15.014	-0.075	-0.075	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.005	0.004	16.636	-0.038	-0.038	0.000	0.000	0.000	0.000
77	A	77	MET	0	-0.023	-0.001	12.818	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.015	0.004	11.749	-0.062	-0.062	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.013	-0.007	12.677	-0.072	-0.072	0.000	0.000	0.000	0.000
80	A	80	PHE	0	-0.050	-0.026	15.197	0.015	0.015	0.000	0.000	0.000	0.000
81	A	81	PHE	0	-0.041	-0.036	10.434	0.028	0.028	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.903	0.966	10.470	0.552	0.552	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.031	0.001	6.782	-0.130	-0.130	0.000	0.000	0.000	0.000
84	A	84	ASN	0	0.038	0.011	7.145	0.575	0.575	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.009	-0.019	8.209	-0.241	-0.241	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.910	-0.954	6.258	-1.656	-1.656	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.846	-0.910	3.267	-4.972	-4.326	0.010	-0.142	-0.514	0.000
88	A	88	ILE	0	-0.031	-0.014	5.283	0.702	0.718	-0.001	-0.008	-0.006	0.000
89	A	89	LEU	0	0.010	0.005	8.104	0.067	0.067	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.028	-0.020	9.793	0.045	0.045	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.008	0.010	13.613	0.052	0.052	0.000	0.000	0.000	0.000
92	A	92	HIS	0	-0.049	-0.051	15.639	-0.040	-0.040	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.758	-0.846	19.153	0.032	0.032	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.840	-0.931	21.060	0.037	0.037	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.021	-0.003	23.088	0.009	0.009	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.942	-0.966	24.580	0.052	0.052	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.085	-0.037	20.602	0.017	0.017	0.000	0.000	0.000	0.000
98	A	98	PRO	0	0.019	0.011	25.083	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.037	0.009	25.631	0.013	0.013	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.014	0.018	25.146	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.029	-0.016	21.859	0.021	0.021	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.047	0.014	17.718	-0.020	-0.020	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.877	0.946	16.632	-0.221	-0.221	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.080	0.044	11.090	-0.040	-0.040	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.859	0.923	12.853	-0.058	-0.058	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.050	0.038	8.506	-0.029	-0.029	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.012	0.021	11.595	0.034	0.034	0.000	0.000	0.000	0.000
108	A	108	GLY	0	-0.031	-0.022	14.008	0.050	0.050	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.029	0.004	17.768	-0.032	-0.032	0.000	0.000	0.000	0.000
110	A	110	HIS	0	0.055	0.022	19.346	0.005	0.005	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.004	0.002	21.460	0.010	0.010	0.000	0.000	0.000	0.000
112	A	112	GLY	0	-0.009	-0.006	24.086	0.010	0.010	0.000	0.000	0.000	0.000
113	A	113	HIS	0	0.025	0.014	22.375	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	114	ASN	0	0.014	-0.035	23.481	-0.020	-0.020	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.056	0.048	22.470	-0.012	-0.012	0.000	0.000	0.000	0.000
116	A	116	LEU	0	-0.013	-0.009	17.212	-0.032	-0.032	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.919	0.960	19.778	0.059	0.059	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.799	-0.885	22.030	-0.190	-0.190	0.000	0.000	0.000	0.000
119	A	119	ILE	0	0.031	0.014	15.719	-0.019	-0.019	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.020	0.001	17.530	-0.033	-0.033	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.064	-0.022	18.627	-0.016	-0.016	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.873	0.917	20.038	0.178	0.178	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.025	0.013	13.482	-0.024	-0.024	0.000	0.000	0.000	0.000
124	A	124	GLY	0	-0.004	0.000	17.004	-0.030	-0.030	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.065	-0.040	19.592	0.014	0.014	0.000	0.000	0.000	0.000
126	A	126	ASN	0	0.059	0.038	13.350	0.036	0.036	0.000	0.000	0.000	0.000
127	A	127	PRO	0	0.011	-0.009	15.504	-0.036	-0.036	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.054	-0.023	11.254	0.096	0.096	0.000	0.000	0.000	0.000
129	A	129	PHE	0	0.060	0.049	9.447	-0.134	-0.134	0.000	0.000	0.000	0.000
130	A	130	HIS	0	0.041	0.002	5.228	0.671	0.671	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.792	0.906	9.848	0.124	0.124	0.000	0.000	0.000	0.000
132	A	132	LEU	0	0.003	0.013	12.915	0.079	0.079	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.829	0.898	14.313	-0.156	-0.156	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.051	0.013	17.704	0.036	0.036	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.002	0.004	20.267	-0.025	-0.025	0.000	0.000	0.000	0.000
136	A	136	ILE	0	-0.030	-0.009	23.623	0.000	0.000	0.000	0.000	0.000	0.000
137	A	137	GLY	0	0.004	0.006	26.752	-0.005	-0.005	0.000	0.000	0.000	0.000
138	A	138	HIS	0	0.049	0.012	29.242	-0.008	-0.008	0.000	0.000	0.000	0.000
139	A	139	PRO	0	-0.032	-0.012	31.478	0.002	0.002	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.023	0.020	34.723	0.000	0.000	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.821	-0.905	36.239	0.014	0.014	0.000	0.000	0.000	0.000
142	A	142	LYS	1	0.996	0.962	32.634	0.001	0.001	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.029	0.004	35.465	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	144	LYS	1	0.877	0.922	37.260	-0.018	-0.018	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.003	0.011	30.937	0.001	0.001	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.017	0.013	33.054	0.001	0.001	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.034	0.010	34.109	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	148	PHE	0	-0.005	0.007	30.054	0.000	0.000	0.000	0.000	0.000	0.000
149	A	149	VAL	0	0.038	0.002	28.805	0.004	0.004	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.031	-0.007	30.079	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	151	GLY	0	0.049	0.035	32.562	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.928	0.965	32.020	-0.023	-0.023	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.005	0.005	29.441	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	154	PRO	0	0.008	0.005	32.722	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	155	VAL	0	0.040	0.005	33.519	0.005	0.005	0.000	0.000	0.000	0.000
156	A	156	SER	0	-0.016	-0.015	33.038	0.005	0.005	0.000	0.000	0.000	0.000
157	A	157	GLU	-1	-0.814	-0.916	30.728	0.066	0.066	0.000	0.000	0.000	0.000
158	A	158	GLN	0	-0.050	-0.020	27.120	-0.002	-0.002	0.000	0.000	0.000	0.000
159	A	159	LYS	1	0.940	0.969	28.083	-0.067	-0.067	0.000	0.000	0.000	0.000
160	A	160	LEU	0	0.032	0.020	27.725	0.012	0.012	0.000	0.000	0.000	0.000
161	A	161	ILE	0	-0.002	-0.007	23.666	0.017	0.017	0.000	0.000	0.000	0.000
162	A	162	ASP	-1	-0.857	-0.933	23.300	0.113	0.113	0.000	0.000	0.000	0.000
163	A	163	GLU	-1	-0.911	-0.955	23.156	0.170	0.170	0.000	0.000	0.000	0.000
164	A	164	ALA	0	-0.034	-0.014	21.035	0.028	0.028	0.000	0.000	0.000	0.000
165	A	165	ILE	0	-0.004	0.004	18.879	0.041	0.041	0.000	0.000	0.000	0.000
166	A	166	ASP	-1	-0.840	-0.918	18.116	0.273	0.273	0.000	0.000	0.000	0.000
167	A	167	GLU	-1	-0.826	-0.911	17.870	0.428	0.428	0.000	0.000	0.000	0.000
168	A	168	ALA	0	0.002	-0.009	15.153	0.076	0.076	0.000	0.000	0.000	0.000
169	A	169	ALA	0	-0.012	0.002	13.639	0.114	0.114	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.930	0.969	13.195	-0.193	-0.193	0.000	0.000	0.000	0.000
171	A	171	CYS	0	-0.031	-0.011	12.805	0.091	0.091	0.000	0.000	0.000	0.000
172	A	172	THR	0	-0.020	-0.023	8.613	0.183	0.183	0.000	0.000	0.000	0.000
173	A	173	GLU	-1	-0.958	-0.970	8.373	1.001	1.001	0.000	0.000	0.000	0.000
174	A	174	MET	0	-0.015	-0.005	8.934	0.140	0.140	0.000	0.000	0.000	0.000
175	A	175	TRP	0	-0.036	-0.015	3.725	-0.513	-0.262	0.000	-0.046	-0.205	0.000
176	A	176	PHE	0	-0.042	-0.025	3.014	-0.541	0.888	0.245	-0.523	-1.151	0.004
177	A	177	THR	0	0.000	0.009	5.607	-0.433	-0.366	-0.001	0.000	-0.066	0.000
178	A	178	ASP	-1	-0.942	-0.968	8.508	0.779	0.779	0.000	0.000	0.000	0.000
179	A	179	GLY	0	0.004	0.013	6.647	-0.100	-0.100	0.000	0.000	0.000	0.000
180	A	180	LEU	0	0.010	-0.006	6.341	-0.385	-0.385	0.000	0.000	0.000	0.000
181	A	181	THR	0	0.002	-0.004	7.919	-0.291	-0.291	0.000	0.000	0.000	0.000
182	A	182	LYS	1	0.989	0.989	11.286	-0.949	-0.949	0.000	0.000	0.000	0.000
183	A	183	ALA	0	0.053	0.035	9.621	-0.165	-0.165	0.000	0.000	0.000	0.000
184	A	184	THR	0	-0.023	-0.028	10.909	-0.191	-0.191	0.000	0.000	0.000	0.000
185	A	185	ASN	0	-0.034	-0.019	13.155	-0.127	-0.127	0.000	0.000	0.000	0.000
186	A	186	ARG	1	0.854	0.933	15.299	-0.551	-0.551	0.000	0.000	0.000	0.000
187	A	187	LEU	0	0.049	0.018	14.220	-0.066	-0.066	0.000	0.000	0.000	0.000
188	A	188	HIS	0	-0.074	-0.050	15.909	-0.060	-0.060	0.000	0.000	0.000	0.000
189	A	189	ALA	0	0.035	0.029	18.698	-0.038	-0.038	0.000	0.000	0.000	0.000
190	A	190	PHE	0	0.015	0.017	20.220	-0.034	-0.034	0.000	0.000	0.000	0.000
191	A	191	LYS	1	0.806	0.902	22.026	-0.189	-0.189	0.000	0.000	0.000	0.000
192	A	192	ALA	0	-0.018	0.001	23.848	-0.017	-0.017	0.000	0.000	0.000	0.000
193	A	193	GLN	0	-0.031	-0.001	25.253	0.006	0.006	0.000	0.000	0.000	0.000

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