FMO DATABASE

FMODB ID: X638Z

Calculation Name: 2PTH-A-Xray13

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: 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	193
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-2089588.918496
FMO2-HF: Nuclear repulsion	2017000.931166
FMO2-HF: Total energy	-72587.98733
FMO2-MP2: Total energy	-72802.864384

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.
-36.311	-30.827	0.394	-1.774	-4.104	-0.002

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 : 1 / q_Mulliken : 0.862 / q_NPA : 0.919

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	0.959	0.975	2.899	48.552	50.812	0.104	-0.857	-1.508	-0.002
4	A	4	LEU	0	-0.029	-0.006	4.769	5.067	5.173	-0.001	-0.008	-0.096	0.000
5	A	5	ILE	0	0.025	0.019	8.366	-1.682	-1.682	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.024	-0.020	10.851	1.740	1.740	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.034	0.016	14.298	-0.315	-0.315	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.064	-0.042	17.593	0.665	0.665	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.019	0.000	20.446	0.223	0.223	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.024	0.010	23.914	-0.107	-0.107	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.034	0.019	26.831	-0.092	-0.092	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.058	0.025	27.989	0.347	0.347	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.003	-0.020	30.731	-0.145	-0.145	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.966	-0.970	32.724	-8.790	-8.790	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.032	0.004	29.843	0.018	0.018	0.000	0.000	0.000	0.000
16	A	16	ALA	0	-0.001	0.019	28.560	-0.290	-0.290	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.000	0.003	28.270	-0.293	-0.293	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.069	-0.044	29.672	0.059	0.059	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.941	0.964	27.519	9.445	9.445	0.000	0.000	0.000	0.000
20	A	20	HIS	0	-0.074	-0.062	25.709	-0.376	-0.376	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.011	0.019	24.245	-0.455	-0.455	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.035	0.020	22.404	-0.354	-0.354	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.008	-0.007	18.732	-0.463	-0.463	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.011	-0.014	18.517	-0.804	-0.804	0.000	0.000	0.000	0.000
25	A	25	TRP	0	0.021	0.018	20.470	-0.187	-0.187	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.003	-0.002	12.647	-0.119	-0.119	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.004	-0.008	14.945	-0.478	-0.478	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.894	-0.948	16.905	-13.805	-13.805	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.043	-0.010	18.534	0.209	0.209	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.031	-0.023	12.119	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.017	0.010	16.030	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.960	-0.975	17.658	-12.138	-12.138	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.869	0.916	17.715	14.955	14.955	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.005	0.007	13.151	0.141	0.141	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.851	0.936	17.478	12.719	12.719	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.014	0.020	16.785	0.315	0.315	0.000	0.000	0.000	0.000
37	A	37	PRO	0	-0.034	-0.029	18.577	-0.468	-0.468	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.024	0.029	17.314	-0.447	-0.447	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.953	0.972	20.466	13.708	13.708	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.893	-0.930	21.268	-12.200	-12.200	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.941	-0.961	18.917	-14.442	-14.442	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.049	0.006	22.327	-0.282	-0.282	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.890	0.957	20.219	13.948	13.948	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.000	-0.012	17.401	-0.394	-0.394	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.017	-0.016	19.883	-0.243	-0.243	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.121	0.052	20.666	-0.055	-0.055	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.005	0.007	20.366	0.185	0.185	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.039	-0.032	16.152	-0.734	-0.734	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.027	-0.004	15.389	0.743	0.743	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.778	0.868	11.328	20.244	20.244	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.007	0.008	10.645	1.392	1.392	0.000	0.000	0.000	0.000
52	A	52	THR	0	0.006	0.011	9.537	-1.050	-1.050	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.003	-0.006	7.638	1.812	1.812	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.051	0.025	6.900	-2.744	-2.744	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.036	-0.016	7.511	-1.111	-1.111	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.935	-0.964	2.854	-46.192	-45.375	0.043	-0.272	-0.588	-0.002
57	A	57	ASP	-1	-0.844	-0.898	5.795	-22.224	-22.224	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.003	0.004	5.654	-3.850	-3.850	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.917	0.958	7.887	25.629	25.629	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.013	0.008	10.400	-1.328	-1.328	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.006	-0.015	13.179	0.835	0.835	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.031	0.033	15.677	-0.437	-0.437	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.041	-0.027	18.354	0.513	0.513	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.017	-0.017	20.995	0.136	0.136	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.053	-0.031	23.335	0.343	0.343	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.045	0.022	25.744	0.386	0.386	0.000	0.000	0.000	0.000
67	A	67	MET	0	0.059	0.039	23.516	-0.581	-0.581	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.029	-0.024	24.550	-0.756	-0.756	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.024	0.002	25.652	0.020	0.020	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.006	-0.017	20.503	-0.252	-0.252	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.019	-0.020	19.633	-0.761	-0.761	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.899	0.962	19.452	11.243	11.243	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.046	0.029	19.193	-0.192	-0.192	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.003	0.004	13.935	-0.666	-0.666	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.019	0.012	15.011	-1.119	-1.119	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.003	0.005	16.633	-0.375	-0.375	0.000	0.000	0.000	0.000
77	A	77	MET	0	-0.022	0.000	12.815	0.145	0.145	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.011	0.001	11.745	-0.844	-0.844	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.011	-0.007	12.674	-0.715	-0.715	0.000	0.000	0.000	0.000
80	A	80	PHE	0	-0.046	-0.024	15.194	0.557	0.557	0.000	0.000	0.000	0.000
81	A	81	PHE	0	-0.040	-0.036	10.432	0.411	0.411	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.906	0.967	10.467	19.527	19.527	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.036	-0.002	6.778	-1.991	-1.991	0.000	0.000	0.000	0.000
84	A	84	ASN	0	0.039	0.012	7.161	6.549	6.549	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.020	-0.012	8.238	-2.596	-2.596	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.902	-0.947	6.279	-43.431	-43.431	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.888	-0.937	3.293	-61.668	-60.996	0.007	-0.158	-0.521	-0.001
88	A	88	ILE	0	-0.018	-0.008	5.351	2.335	2.364	-0.001	-0.009	-0.019	0.000
89	A	89	LEU	0	0.007	0.004	8.109	-0.188	-0.188	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.026	-0.018	9.797	1.627	1.627	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.010	0.011	13.616	0.264	0.264	0.000	0.000	0.000	0.000
92	A	92	HIS	0	-0.051	-0.051	15.645	-0.037	-0.037	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.754	-0.844	19.157	-13.224	-13.224	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.842	-0.932	21.060	-14.282	-14.282	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.020	-0.003	23.089	0.369	0.369	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.943	-0.967	24.591	-11.405	-11.405	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.083	-0.036	20.601	-0.173	-0.173	0.000	0.000	0.000	0.000
98	A	98	PRO	0	0.022	0.012	25.083	0.134	0.134	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.033	0.007	25.635	-0.493	-0.493	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.016	0.019	25.152	0.332	0.332	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.016	-0.007	21.861	-0.284	-0.284	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.041	0.010	17.723	-0.009	-0.009	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.886	0.951	16.633	15.025	15.025	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.070	0.039	11.096	-0.361	-0.361	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.867	0.927	12.856	18.909	18.909	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.040	0.032	8.503	-0.989	-0.989	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.012	0.020	11.599	1.364	1.364	0.000	0.000	0.000	0.000
108	A	108	GLY	0	-0.027	-0.019	14.023	0.748	0.748	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.029	0.004	17.781	-0.193	-0.193	0.000	0.000	0.000	0.000
110	A	110	HIS	0	0.054	0.022	19.373	-0.615	-0.615	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.005	0.003	21.492	0.068	0.068	0.000	0.000	0.000	0.000
112	A	112	GLY	0	-0.008	-0.005	24.110	0.369	0.369	0.000	0.000	0.000	0.000
113	A	113	HIS	0	0.027	0.014	22.411	0.279	0.279	0.000	0.000	0.000	0.000
114	A	114	ASN	0	0.015	-0.035	23.522	-0.513	-0.513	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.056	0.048	22.521	0.011	0.011	0.000	0.000	0.000	0.000
116	A	116	LEU	0	-0.015	-0.010	17.253	-0.549	-0.549	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.921	0.961	19.825	11.019	11.019	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.798	-0.884	22.079	-13.450	-13.450	0.000	0.000	0.000	0.000
119	A	119	ILE	0	0.030	0.013	15.774	-0.086	-0.086	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.022	0.000	17.570	-0.441	-0.441	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.062	-0.021	18.675	0.037	0.037	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.874	0.918	20.100	13.104	13.104	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.030	0.010	13.540	-0.218	-0.218	0.000	0.000	0.000	0.000
124	A	124	GLY	0	-0.004	0.000	17.057	-0.596	-0.596	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.062	-0.038	19.637	-0.055	-0.055	0.000	0.000	0.000	0.000
126	A	126	ASN	0	0.057	0.037	13.388	-0.298	-0.298	0.000	0.000	0.000	0.000
127	A	127	PRO	0	0.015	-0.006	15.547	-0.636	-0.636	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.053	-0.022	11.274	-0.076	-0.076	0.000	0.000	0.000	0.000
129	A	129	PHE	0	0.054	0.044	9.487	-1.963	-1.963	0.000	0.000	0.000	0.000
130	A	130	HIS	0	0.032	-0.003	5.270	6.311	6.311	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.796	0.908	9.875	21.188	21.188	0.000	0.000	0.000	0.000
132	A	132	LEU	0	0.004	0.013	12.921	-0.560	-0.560	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.829	0.899	14.317	16.230	16.230	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.052	0.014	17.711	0.133	0.133	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.004	0.006	20.272	0.399	0.399	0.000	0.000	0.000	0.000
136	A	136	ILE	0	-0.033	-0.010	23.626	0.230	0.230	0.000	0.000	0.000	0.000
137	A	137	GLY	0	0.008	0.009	26.757	0.494	0.494	0.000	0.000	0.000	0.000
138	A	138	HIS	0	0.048	0.011	29.244	0.080	0.080	0.000	0.000	0.000	0.000
139	A	139	PRO	0	-0.033	-0.012	31.479	0.239	0.239	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.024	0.020	34.725	0.307	0.307	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.821	-0.904	36.258	-8.078	-8.078	0.000	0.000	0.000	0.000
142	A	142	LYS	1	0.995	0.961	32.659	9.276	9.276	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.030	0.004	35.492	-0.131	-0.131	0.000	0.000	0.000	0.000
144	A	144	LYS	1	0.877	0.921	37.261	7.918	7.918	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.004	0.012	30.969	-0.089	-0.089	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.016	0.012	33.056	-0.201	-0.201	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.034	0.010	34.112	-0.114	-0.114	0.000	0.000	0.000	0.000
148	A	148	PHE	0	-0.004	0.008	30.056	0.061	0.061	0.000	0.000	0.000	0.000
149	A	149	VAL	0	0.038	0.002	28.808	-0.105	-0.105	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.033	-0.008	30.084	-0.292	-0.292	0.000	0.000	0.000	0.000
151	A	151	GLY	0	0.049	0.035	32.567	0.274	0.274	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.928	0.965	32.027	8.609	8.609	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.005	0.005	29.450	0.290	0.290	0.000	0.000	0.000	0.000
154	A	154	PRO	0	0.009	0.005	32.730	0.124	0.124	0.000	0.000	0.000	0.000
155	A	155	VAL	0	0.039	0.004	33.527	-0.249	-0.249	0.000	0.000	0.000	0.000
156	A	156	SER	0	-0.015	-0.014	33.047	-0.255	-0.255	0.000	0.000	0.000	0.000
157	A	157	GLU	-1	-0.812	-0.915	30.735	-9.823	-9.823	0.000	0.000	0.000	0.000
158	A	158	GLN	0	-0.054	-0.021	27.130	-0.053	-0.053	0.000	0.000	0.000	0.000
159	A	159	LYS	1	0.940	0.969	28.093	9.095	9.095	0.000	0.000	0.000	0.000
160	A	160	LEU	0	0.037	0.023	27.733	-0.312	-0.312	0.000	0.000	0.000	0.000
161	A	161	ILE	0	-0.004	-0.008	23.674	-0.477	-0.477	0.000	0.000	0.000	0.000
162	A	162	ASP	-1	-0.861	-0.936	23.310	-12.166	-12.166	0.000	0.000	0.000	0.000
163	A	163	GLU	-1	-0.908	-0.954	23.167	-11.529	-11.529	0.000	0.000	0.000	0.000
164	A	164	ALA	0	-0.028	-0.010	21.042	-0.524	-0.524	0.000	0.000	0.000	0.000
165	A	165	ILE	0	-0.009	0.001	18.891	-1.006	-1.006	0.000	0.000	0.000	0.000
166	A	166	ASP	-1	-0.840	-0.919	18.126	-14.858	-14.858	0.000	0.000	0.000	0.000
167	A	167	GLU	-1	-0.817	-0.905	17.876	-16.112	-16.112	0.000	0.000	0.000	0.000
168	A	168	ALA	0	0.002	-0.008	15.163	-1.078	-1.078	0.000	0.000	0.000	0.000
169	A	169	ALA	0	-0.016	-0.001	13.649	-1.754	-1.754	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.932	0.970	13.194	13.135	13.135	0.000	0.000	0.000	0.000
171	A	171	CYS	0	-0.023	-0.005	12.811	-0.783	-0.783	0.000	0.000	0.000	0.000
172	A	172	THR	0	-0.028	-0.028	8.624	-2.259	-2.259	0.000	0.000	0.000	0.000
173	A	173	GLU	-1	-0.962	-0.972	8.373	-23.057	-23.057	0.000	0.000	0.000	0.000
174	A	174	MET	0	-0.006	0.000	8.935	-0.910	-0.910	0.000	0.000	0.000	0.000
175	A	175	TRP	0	-0.045	-0.017	3.798	-0.425	-0.166	0.000	-0.054	-0.205	0.000
176	A	176	PHE	0	-0.060	-0.036	3.021	-4.859	-3.588	0.243	-0.416	-1.098	0.003
177	A	177	THR	0	0.003	0.010	5.608	-1.871	-1.801	-0.001	0.000	-0.069	0.000
178	A	178	ASP	-1	-0.932	-0.962	8.526	-21.286	-21.286	0.000	0.000	0.000	0.000
179	A	179	GLY	0	-0.007	0.007	6.645	0.505	0.505	0.000	0.000	0.000	0.000
180	A	180	LEU	0	0.001	-0.012	6.336	2.685	2.685	0.000	0.000	0.000	0.000
181	A	181	THR	0	0.005	-0.002	7.915	2.041	2.041	0.000	0.000	0.000	0.000
182	A	182	LYS	1	0.994	0.993	11.283	21.524	21.524	0.000	0.000	0.000	0.000
183	A	183	ALA	0	0.048	0.032	9.623	1.623	1.623	0.000	0.000	0.000	0.000
184	A	184	THR	0	-0.027	-0.030	10.906	1.300	1.300	0.000	0.000	0.000	0.000
185	A	185	ASN	0	-0.032	-0.018	13.153	1.325	1.325	0.000	0.000	0.000	0.000
186	A	186	ARG	1	0.861	0.936	15.300	17.512	17.512	0.000	0.000	0.000	0.000
187	A	187	LEU	0	0.043	0.014	14.225	0.876	0.876	0.000	0.000	0.000	0.000
188	A	188	HIS	0	-0.083	-0.057	15.906	0.380	0.380	0.000	0.000	0.000	0.000
189	A	189	ALA	0	0.046	0.035	18.699	0.630	0.630	0.000	0.000	0.000	0.000
190	A	190	PHE	0	0.019	0.021	20.225	0.768	0.768	0.000	0.000	0.000	0.000
191	A	191	LYS	1	0.801	0.898	22.030	11.575	11.575	0.000	0.000	0.000	0.000
192	A	192	ALA	0	-0.055	-0.023	23.849	0.379	0.379	0.000	0.000	0.000	0.000
193	A	193	GLN	-1	-0.963	-0.961	25.256	-11.147	-11.147	0.000	0.000	0.000	0.000

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