FMO DATABASE

FMODB ID: 2JM8R

Calculation Name: 5JCG-A-Xray372

Preferred Name: Thioredoxin-dependent peroxide reductase, mitochondrial

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 5JCG

Chain ID: A

ChEMBL ID: CHEMBL4295742

UniProt ID: P30048

Base Structure: X-ray

Registration Date: 2023-06-22

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	195
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2081854.409295
FMO2-HF: Nuclear repulsion	2007218.028024
FMO2-HF: Total energy	-74636.38127
FMO2-MP2: Total energy	-74857.10298

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:0:THR)

Summations of interaction energy for fragment #1(A:0: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.
-14.137	-4.965	6.483	-7.021	-8.632	-0.042

Interaction energy analysis for fragmet #1(A:0:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.035 / q_NPA : -0.008

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	2	PRO	0	0.034	0.034	3.857	-0.938	1.633	-0.021	-1.375	-1.174	0.006
4	A	3	ALA	0	-0.011	-0.015	6.023	0.524	0.524	0.000	0.000	0.000	0.000
5	A	4	VAL	0	0.029	0.005	7.021	0.063	0.063	0.000	0.000	0.000	0.000
6	A	5	THR	0	-0.095	-0.049	8.403	-0.179	-0.179	0.000	0.000	0.000	0.000
7	A	6	GLN	0	-0.030	0.001	3.015	-4.250	-2.754	0.104	-0.847	-0.753	-0.008
8	A	7	HIS	0	0.038	0.014	2.636	-1.675	0.348	0.618	-0.958	-1.683	0.005
9	A	8	ALA	0	0.035	-0.002	2.332	-7.471	-4.927	3.765	-3.361	-2.948	-0.039
10	A	9	PRO	0	-0.017	0.000	2.478	-0.260	0.872	1.991	-1.335	-1.787	-0.006
11	A	10	TYR	0	0.012	0.016	3.365	0.810	0.199	0.027	0.856	-0.272	0.000
12	A	11	PHE	0	0.003	0.000	5.336	-0.462	-0.445	-0.001	-0.001	-0.015	0.000
13	A	12	LYS	1	0.943	0.963	8.860	-0.232	-0.232	0.000	0.000	0.000	0.000
14	A	13	GLY	0	-0.003	0.008	12.229	-0.082	-0.082	0.000	0.000	0.000	0.000
15	A	14	THR	0	0.002	0.014	15.692	0.029	0.029	0.000	0.000	0.000	0.000
16	A	15	ALA	0	0.017	0.007	18.783	-0.036	-0.036	0.000	0.000	0.000	0.000
17	A	16	VAL	0	-0.064	-0.022	20.686	0.009	0.009	0.000	0.000	0.000	0.000
18	A	17	VAL	0	0.024	-0.010	21.761	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	18	ASN	0	0.015	0.004	24.717	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	19	GLY	0	-0.005	-0.004	28.107	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.933	-0.951	27.733	0.105	0.105	0.000	0.000	0.000	0.000
22	A	21	PHE	0	-0.065	-0.038	24.506	0.001	0.001	0.000	0.000	0.000	0.000
23	A	22	LYS	1	1.002	0.998	21.033	-0.216	-0.216	0.000	0.000	0.000	0.000
24	A	23	ASP	-1	-0.907	-0.959	17.665	0.214	0.214	0.000	0.000	0.000	0.000
25	A	24	LEU	0	-0.010	0.000	15.469	0.006	0.006	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.026	-0.012	11.018	0.015	0.015	0.000	0.000	0.000	0.000
27	A	26	LEU	0	0.020	-0.001	5.693	-0.039	-0.039	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.887	-0.949	9.789	1.567	1.567	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.906	-0.952	11.593	0.454	0.454	0.000	0.000	0.000	0.000
30	A	29	PHE	0	-0.057	-0.040	12.327	-0.105	-0.105	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.961	1.001	9.658	-1.782	-1.782	0.000	0.000	0.000	0.000
32	A	31	GLY	0	-0.061	-0.031	13.344	-0.086	-0.086	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.913	0.969	15.272	-0.428	-0.428	0.000	0.000	0.000	0.000
34	A	33	TYR	0	0.023	0.001	14.458	0.051	0.051	0.000	0.000	0.000	0.000
35	A	34	LEU	0	-0.021	-0.007	10.981	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	35	VAL	0	-0.008	-0.005	13.571	-0.063	-0.063	0.000	0.000	0.000	0.000
37	A	36	LEU	0	0.010	0.011	10.198	0.027	0.027	0.000	0.000	0.000	0.000
38	A	37	PHE	0	-0.035	-0.038	13.924	-0.097	-0.097	0.000	0.000	0.000	0.000
39	A	38	PHE	0	0.055	0.026	11.099	0.036	0.036	0.000	0.000	0.000	0.000
40	A	39	TYR	0	-0.077	-0.090	16.952	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	40	PRO	0	-0.008	0.004	20.328	0.008	0.008	0.000	0.000	0.000	0.000
42	A	41	LEU	0	0.025	-0.005	21.822	0.000	0.000	0.000	0.000	0.000	0.000
43	A	42	ASP	-1	-0.737	-0.837	24.484	-0.078	-0.078	0.000	0.000	0.000	0.000
44	A	43	PHE	0	-0.035	-0.020	26.638	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	44	THR	0	-0.026	-0.008	27.351	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	45	PHE	0	0.008	-0.011	29.752	0.008	0.008	0.000	0.000	0.000	0.000
47	A	46	VAL	0	0.043	0.022	26.820	0.007	0.007	0.000	0.000	0.000	0.000
48	A	47	CYS	0	-0.039	0.036	25.152	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	48	PRO	0	0.077	0.053	26.323	0.004	0.004	0.000	0.000	0.000	0.000
50	A	49	THR	0	-0.079	-0.049	28.712	0.008	0.008	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.702	-0.828	23.672	-0.189	-0.189	0.000	0.000	0.000	0.000
52	A	51	ILE	0	0.006	0.009	23.456	0.009	0.009	0.000	0.000	0.000	0.000
53	A	52	VAL	0	-0.026	-0.020	25.534	0.015	0.015	0.000	0.000	0.000	0.000
54	A	53	ALA	0	-0.002	0.019	27.268	0.009	0.009	0.000	0.000	0.000	0.000
55	A	54	PHE	0	0.006	-0.017	21.035	0.008	0.008	0.000	0.000	0.000	0.000
56	A	55	SER	0	0.007	0.002	25.176	0.019	0.019	0.000	0.000	0.000	0.000
57	A	56	ASP	-1	-0.855	-0.921	26.951	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	57	LYS	1	0.901	0.964	27.117	0.028	0.028	0.000	0.000	0.000	0.000
59	A	58	ALA	0	0.006	0.006	24.965	0.004	0.004	0.000	0.000	0.000	0.000
60	A	59	ASN	0	0.045	0.017	25.310	0.007	0.007	0.000	0.000	0.000	0.000
61	A	60	GLU	-1	-0.893	-0.939	27.445	0.013	0.013	0.000	0.000	0.000	0.000
62	A	61	PHE	0	-0.042	-0.034	20.637	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	62	HIS	0	-0.005	-0.008	22.349	0.014	0.014	0.000	0.000	0.000	0.000
64	A	63	ASP	-1	-0.922	-0.953	24.243	0.102	0.102	0.000	0.000	0.000	0.000
65	A	64	VAL	0	-0.122	-0.047	22.127	0.004	0.004	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.022	-0.011	19.116	0.007	0.007	0.000	0.000	0.000	0.000
67	A	66	CYS	0	-0.034	-0.006	18.202	0.026	0.026	0.000	0.000	0.000	0.000
68	A	67	GLU	-1	-0.875	-0.931	16.871	0.176	0.176	0.000	0.000	0.000	0.000
69	A	68	VAL	0	-0.010	-0.009	17.348	-0.021	-0.021	0.000	0.000	0.000	0.000
70	A	69	VAL	0	0.000	0.000	15.287	0.019	0.019	0.000	0.000	0.000	0.000
71	A	70	ALA	0	-0.001	0.018	16.668	-0.043	-0.043	0.000	0.000	0.000	0.000
72	A	71	VAL	0	-0.018	-0.009	14.124	0.032	0.032	0.000	0.000	0.000	0.000
73	A	72	SER	0	0.023	0.015	17.419	-0.030	-0.030	0.000	0.000	0.000	0.000
74	A	73	VAL	0	0.021	0.004	17.420	0.014	0.014	0.000	0.000	0.000	0.000
75	A	74	ASP	-1	-0.847	-0.896	19.569	-0.110	-0.110	0.000	0.000	0.000	0.000
76	A	75	SER	0	0.010	0.022	21.555	0.014	0.014	0.000	0.000	0.000	0.000
77	A	76	HIS	0	0.069	0.019	22.404	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	77	PHE	0	0.006	-0.008	24.201	0.004	0.004	0.000	0.000	0.000	0.000
79	A	78	SER	0	-0.001	0.004	26.129	0.004	0.004	0.000	0.000	0.000	0.000
80	A	79	HIS	1	0.826	0.891	20.645	0.057	0.057	0.000	0.000	0.000	0.000
81	A	80	LEU	0	0.026	0.027	26.282	0.000	0.000	0.000	0.000	0.000	0.000
82	A	81	ALA	0	0.000	0.006	29.091	0.001	0.001	0.000	0.000	0.000	0.000
83	A	82	TRP	0	0.005	-0.004	25.440	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	83	ILE	0	-0.012	-0.011	26.684	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.045	-0.021	30.781	0.004	0.004	0.000	0.000	0.000	0.000
86	A	85	THR	0	-0.019	0.001	33.602	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	86	PRO	0	0.014	-0.003	34.564	0.000	0.000	0.000	0.000	0.000	0.000
88	A	87	ARG	1	0.871	0.927	32.074	0.014	0.014	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.884	0.941	35.787	0.019	0.019	0.000	0.000	0.000	0.000
90	A	89	ASN	0	-0.035	-0.018	38.085	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.050	0.039	34.756	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	91	GLY	0	-0.012	-0.006	32.564	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	92	LEU	0	-0.010	0.002	26.893	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	93	GLY	0	0.001	0.001	31.062	0.003	0.003	0.000	0.000	0.000	0.000
95	A	94	HIS	0	0.015	-0.002	31.244	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	95	MET	0	-0.037	-0.015	26.481	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	96	ASN	0	-0.034	-0.017	27.006	0.015	0.015	0.000	0.000	0.000	0.000
98	A	97	ILE	0	0.003	0.000	21.653	0.009	0.009	0.000	0.000	0.000	0.000
99	A	98	ALA	0	0.001	0.016	19.231	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	99	LEU	0	0.003	-0.007	20.457	-0.022	-0.022	0.000	0.000	0.000	0.000
101	A	100	LEU	0	0.041	0.009	13.944	0.020	0.020	0.000	0.000	0.000	0.000
102	A	101	SER	0	-0.104	-0.077	18.473	-0.035	-0.035	0.000	0.000	0.000	0.000
103	A	102	ASP	-1	-0.730	-0.874	14.350	-0.247	-0.247	0.000	0.000	0.000	0.000
104	A	103	LEU	0	-0.003	-0.005	16.618	-0.034	-0.034	0.000	0.000	0.000	0.000
105	A	104	THR	0	-0.021	-0.020	14.812	-0.026	-0.026	0.000	0.000	0.000	0.000
106	A	105	LYS	1	0.901	0.979	15.664	0.199	0.199	0.000	0.000	0.000	0.000
107	A	106	GLN	0	-0.030	-0.012	9.941	0.011	0.011	0.000	0.000	0.000	0.000
108	A	107	ILE	0	0.030	0.023	9.779	-0.143	-0.143	0.000	0.000	0.000	0.000
109	A	108	SER	0	-0.013	-0.040	9.806	-0.165	-0.165	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.787	0.880	11.130	0.392	0.392	0.000	0.000	0.000	0.000
111	A	110	ASP	-1	-0.867	-0.930	5.945	-0.963	-0.963	0.000	0.000	0.000	0.000
112	A	111	TYR	0	-0.071	-0.063	6.457	-0.661	-0.661	0.000	0.000	0.000	0.000
113	A	112	GLY	0	-0.031	-0.009	8.622	0.022	0.022	0.000	0.000	0.000	0.000
114	A	113	VAL	0	-0.001	0.003	11.121	0.091	0.091	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.049	-0.015	13.812	0.116	0.116	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.010	0.009	15.709	-0.044	-0.044	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.809	-0.912	15.919	-0.452	-0.452	0.000	0.000	0.000	0.000
118	A	117	GLY	0	-0.049	-0.007	19.327	0.037	0.037	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.006	-0.010	22.523	0.019	0.019	0.000	0.000	0.000	0.000
120	A	119	GLY	0	-0.020	0.001	20.254	0.026	0.026	0.000	0.000	0.000	0.000
121	A	120	LEU	0	-0.004	-0.016	19.981	0.028	0.028	0.000	0.000	0.000	0.000
122	A	121	ALA	0	0.041	0.014	16.416	-0.036	-0.036	0.000	0.000	0.000	0.000
123	A	122	LEU	0	0.017	0.004	17.477	0.051	0.051	0.000	0.000	0.000	0.000
124	A	123	ARG	1	0.813	0.894	17.984	0.213	0.213	0.000	0.000	0.000	0.000
125	A	124	GLY	0	0.000	0.005	15.392	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.022	-0.015	15.527	0.060	0.060	0.000	0.000	0.000	0.000
127	A	126	PHE	0	-0.001	0.001	9.877	-0.098	-0.098	0.000	0.000	0.000	0.000
128	A	127	ILE	0	-0.002	-0.002	12.628	0.100	0.100	0.000	0.000	0.000	0.000
129	A	128	ILE	0	-0.021	-0.009	8.146	-0.078	-0.078	0.000	0.000	0.000	0.000
130	A	129	ASP	-1	-0.775	-0.889	11.085	0.654	0.654	0.000	0.000	0.000	0.000
131	A	130	PRO	0	0.028	0.010	11.541	0.130	0.130	0.000	0.000	0.000	0.000
132	A	131	ASN	0	-0.061	-0.048	10.519	0.436	0.436	0.000	0.000	0.000	0.000
133	A	132	GLY	0	0.009	0.017	7.545	0.458	0.458	0.000	0.000	0.000	0.000
134	A	133	VAL	0	-0.020	0.002	6.210	0.162	0.162	0.000	0.000	0.000	0.000
135	A	134	ILE	0	-0.009	0.007	6.185	-0.060	-0.060	0.000	0.000	0.000	0.000
136	A	135	LYS	1	0.910	0.950	8.884	-0.234	-0.234	0.000	0.000	0.000	0.000
137	A	136	HIS	0	-0.005	-0.014	12.371	-0.028	-0.028	0.000	0.000	0.000	0.000
138	A	137	LEU	0	0.006	0.017	10.574	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	138	SER	0	-0.029	-0.006	13.651	0.033	0.033	0.000	0.000	0.000	0.000
140	A	139	VAL	0	0.035	0.009	15.708	-0.009	-0.009	0.000	0.000	0.000	0.000
141	A	140	ASN	0	-0.036	0.007	18.424	0.003	0.003	0.000	0.000	0.000	0.000
142	A	141	ASP	-1	-0.825	-0.910	21.400	-0.321	-0.321	0.000	0.000	0.000	0.000
143	A	142	LEU	0	-0.002	-0.033	22.312	0.022	0.022	0.000	0.000	0.000	0.000
144	A	143	PRO	0	-0.029	-0.010	25.184	0.020	0.020	0.000	0.000	0.000	0.000
145	A	144	VAL	0	-0.006	0.008	26.893	0.019	0.019	0.000	0.000	0.000	0.000
146	A	145	GLY	0	0.012	0.004	25.714	-0.017	-0.017	0.000	0.000	0.000	0.000
147	A	146	ARG	1	0.764	0.844	18.660	0.253	0.253	0.000	0.000	0.000	0.000
148	A	147	SER	0	0.015	0.009	24.584	0.024	0.024	0.000	0.000	0.000	0.000
149	A	148	VAL	0	0.046	0.020	23.996	-0.011	-0.011	0.000	0.000	0.000	0.000
150	A	149	GLU	-1	-0.910	-0.953	24.755	-0.038	-0.038	0.000	0.000	0.000	0.000
151	A	150	GLU	-1	-0.840	-0.941	22.851	-0.150	-0.150	0.000	0.000	0.000	0.000
152	A	151	THR	0	-0.017	-0.011	19.110	-0.014	-0.014	0.000	0.000	0.000	0.000
153	A	152	LEU	0	0.029	0.017	20.995	0.011	0.011	0.000	0.000	0.000	0.000
154	A	153	ARG	1	0.804	0.901	23.326	0.138	0.138	0.000	0.000	0.000	0.000
155	A	154	LEU	0	-0.009	-0.010	18.803	0.012	0.012	0.000	0.000	0.000	0.000
156	A	155	VAL	0	0.003	0.009	18.111	0.012	0.012	0.000	0.000	0.000	0.000
157	A	156	LYS	1	0.975	0.986	20.018	0.010	0.010	0.000	0.000	0.000	0.000
158	A	157	ALA	0	0.015	0.009	21.676	0.016	0.016	0.000	0.000	0.000	0.000
159	A	158	PHE	0	-0.015	-0.027	16.518	0.009	0.009	0.000	0.000	0.000	0.000
160	A	159	GLN	0	-0.017	-0.016	19.182	0.019	0.019	0.000	0.000	0.000	0.000
161	A	160	TYR	0	-0.030	-0.006	21.013	0.021	0.021	0.000	0.000	0.000	0.000
162	A	161	VAL	0	-0.022	-0.028	19.566	0.008	0.008	0.000	0.000	0.000	0.000
163	A	162	GLU	-1	-0.952	-0.973	16.312	0.319	0.319	0.000	0.000	0.000	0.000
164	A	163	THR	0	-0.057	-0.018	20.708	0.017	0.017	0.000	0.000	0.000	0.000
165	A	164	HIS	1	0.850	0.927	24.163	-0.083	-0.083	0.000	0.000	0.000	0.000
166	A	165	GLY	0	0.019	0.026	23.921	-0.007	-0.007	0.000	0.000	0.000	0.000
167	A	166	GLU	-1	-0.945	-0.966	24.965	0.005	0.005	0.000	0.000	0.000	0.000
168	A	167	VAL	0	-0.002	-0.013	22.454	0.002	0.002	0.000	0.000	0.000	0.000
169	A	168	CYS	0	0.018	0.004	23.660	0.007	0.007	0.000	0.000	0.000	0.000
170	A	169	PRO	0	-0.023	-0.005	24.983	-0.019	-0.019	0.000	0.000	0.000	0.000
171	A	170	ALA	0	0.034	0.019	26.351	-0.006	-0.006	0.000	0.000	0.000	0.000
172	A	171	ASN	0	-0.034	-0.034	27.356	0.003	0.003	0.000	0.000	0.000	0.000
173	A	172	TRP	0	-0.013	0.023	25.314	0.006	0.006	0.000	0.000	0.000	0.000
174	A	173	THR	0	0.072	0.034	27.630	-0.008	-0.008	0.000	0.000	0.000	0.000
175	A	174	PRO	0	-0.002	-0.023	28.325	0.004	0.004	0.000	0.000	0.000	0.000
176	A	175	ASP	-1	-0.882	-0.932	30.381	0.011	0.011	0.000	0.000	0.000	0.000
177	A	176	SER	0	-0.102	-0.021	30.735	-0.005	-0.005	0.000	0.000	0.000	0.000
178	A	177	PRO	0	0.003	-0.021	32.055	0.006	0.006	0.000	0.000	0.000	0.000
179	A	178	THR	0	-0.019	-0.012	27.821	-0.007	-0.007	0.000	0.000	0.000	0.000
180	A	179	ILE	0	-0.042	-0.018	27.739	0.002	0.002	0.000	0.000	0.000	0.000
181	A	180	LYS	1	0.962	0.993	27.988	-0.014	-0.014	0.000	0.000	0.000	0.000
182	A	181	PRO	0	0.024	0.030	24.732	-0.011	-0.011	0.000	0.000	0.000	0.000
183	A	182	SER	0	0.010	-0.012	26.627	-0.001	-0.001	0.000	0.000	0.000	0.000
184	A	183	PRO	0	0.045	0.017	29.329	-0.002	-0.002	0.000	0.000	0.000	0.000
185	A	184	ALA	0	-0.008	-0.004	31.941	-0.002	-0.002	0.000	0.000	0.000	0.000
186	A	185	ALA	0	0.044	0.008	31.901	-0.001	-0.001	0.000	0.000	0.000	0.000
187	A	186	SER	0	-0.012	-0.001	30.719	-0.001	-0.001	0.000	0.000	0.000	0.000
188	A	187	LYS	1	0.938	0.962	32.652	0.044	0.044	0.000	0.000	0.000	0.000
189	A	188	GLU	-1	-0.864	-0.923	35.679	0.004	0.004	0.000	0.000	0.000	0.000
190	A	189	TYR	0	-0.029	-0.012	32.481	-0.001	-0.001	0.000	0.000	0.000	0.000
191	A	190	PHE	0	0.022	-0.008	30.978	-0.002	-0.002	0.000	0.000	0.000	0.000
192	A	191	GLN	0	-0.003	0.003	36.401	-0.004	-0.004	0.000	0.000	0.000	0.000
193	A	192	LYS	1	0.902	0.968	35.045	0.013	0.013	0.000	0.000	0.000	0.000
194	A	193	VAL	0	-0.019	-0.009	35.356	0.002	0.002	0.000	0.000	0.000	0.000
195	A	194	ASN	0	-0.046	-0.008	37.315	-0.008	-0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:THR)