FMO DATABASE

FMODB ID: 6N48Z

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	OptHSide
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	-2084849.142333
FMO2-HF: Nuclear repulsion	2010212.08139
FMO2-HF: Total energy	-74637.060944
FMO2-MP2: Total energy	-74857.867761

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.
-7.985	-1.148	6.582	-5.566	-7.853	-0.037

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 : -0.064 / q_NPA : -0.036

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	0.029	0.028	3.857	-0.332	1.621	-0.020	-0.967	-0.966	0.003
4	A	3	ALA	0	-0.008	-0.011	6.018	0.251	0.251	0.000	0.000	0.000	0.000
5	A	4	VAL	0	0.030	0.005	7.008	0.186	0.186	0.000	0.000	0.000	0.000
6	A	5	THR	0	-0.071	-0.039	8.798	0.187	0.187	0.000	0.000	0.000	0.000
7	A	6	GLN	0	-0.040	0.000	3.404	1.515	1.982	0.018	-0.105	-0.381	0.000
8	A	7	HIS	0	0.012	0.002	2.776	-2.480	-0.736	0.395	-0.674	-1.464	0.002
9	A	8	ALA	0	0.030	-0.001	2.348	-5.917	-3.719	3.852	-3.185	-2.866	-0.037
10	A	9	PRO	0	-0.008	0.000	2.287	-1.338	-0.146	2.307	-1.629	-1.870	-0.005
11	A	10	TYR	0	-0.036	-0.016	3.221	1.029	0.297	0.031	0.995	-0.294	0.000
12	A	11	PHE	0	0.009	0.008	5.307	-0.289	-0.274	-0.001	-0.001	-0.012	0.000
13	A	12	LYS	1	0.894	0.929	8.853	0.038	0.038	0.000	0.000	0.000	0.000
14	A	13	GLY	0	-0.001	0.010	12.216	-0.051	-0.051	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.010	0.007	15.689	0.020	0.020	0.000	0.000	0.000	0.000
16	A	15	ALA	0	0.024	0.011	18.740	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	16	VAL	0	-0.058	-0.021	20.664	0.004	0.004	0.000	0.000	0.000	0.000
18	A	17	VAL	0	0.020	-0.011	21.714	0.002	0.002	0.000	0.000	0.000	0.000
19	A	18	ASN	0	0.013	0.003	24.732	0.000	0.000	0.000	0.000	0.000	0.000
20	A	19	GLY	0	0.007	0.001	28.148	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.935	-0.951	27.734	0.025	0.025	0.000	0.000	0.000	0.000
22	A	21	PHE	0	-0.055	-0.032	24.514	0.000	0.000	0.000	0.000	0.000	0.000
23	A	22	LYS	1	1.000	0.995	20.759	-0.077	-0.077	0.000	0.000	0.000	0.000
24	A	23	ASP	-1	-0.862	-0.932	17.717	0.019	0.019	0.000	0.000	0.000	0.000
25	A	24	LEU	0	-0.024	-0.011	15.518	0.012	0.012	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.048	-0.057	10.948	-0.045	-0.045	0.000	0.000	0.000	0.000
27	A	26	LEU	0	0.022	0.006	5.716	0.010	0.010	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.821	-0.888	9.790	0.615	0.615	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.862	-0.913	11.491	0.168	0.168	0.000	0.000	0.000	0.000
30	A	29	PHE	0	-0.041	-0.038	12.156	-0.044	-0.044	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.907	0.974	9.387	-0.919	-0.919	0.000	0.000	0.000	0.000
32	A	31	GLY	0	-0.057	-0.031	13.072	-0.050	-0.050	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.884	0.954	15.041	-0.228	-0.228	0.000	0.000	0.000	0.000
34	A	33	TYR	0	-0.029	-0.030	14.254	0.033	0.033	0.000	0.000	0.000	0.000
35	A	34	LEU	0	-0.033	-0.014	10.809	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	35	VAL	0	0.001	0.002	13.536	-0.006	-0.006	0.000	0.000	0.000	0.000
37	A	36	LEU	0	0.008	0.008	10.414	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	37	PHE	0	-0.027	-0.032	14.015	-0.033	-0.033	0.000	0.000	0.000	0.000
39	A	38	PHE	0	0.055	0.028	10.845	0.008	0.008	0.000	0.000	0.000	0.000
40	A	39	TYR	0	-0.050	-0.068	16.805	0.015	0.015	0.000	0.000	0.000	0.000
41	A	40	PRO	0	-0.006	0.005	20.244	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	41	LEU	0	0.033	-0.002	21.787	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	42	ASP	-1	-0.749	-0.840	24.433	-0.048	-0.048	0.000	0.000	0.000	0.000
44	A	43	PHE	0	-0.036	-0.022	26.554	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	44	THR	0	-0.029	-0.009	27.260	0.001	0.001	0.000	0.000	0.000	0.000
46	A	45	PHE	0	0.011	-0.010	29.622	0.005	0.005	0.000	0.000	0.000	0.000
47	A	46	VAL	0	0.037	0.022	26.624	0.004	0.004	0.000	0.000	0.000	0.000
48	A	47	CYS	0	-0.025	0.038	25.046	0.002	0.002	0.000	0.000	0.000	0.000
49	A	48	PRO	0	0.071	0.050	26.261	0.003	0.003	0.000	0.000	0.000	0.000
50	A	49	THR	0	-0.072	-0.047	28.642	0.006	0.006	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.711	-0.826	23.694	-0.047	-0.047	0.000	0.000	0.000	0.000
52	A	51	ILE	0	0.006	0.009	23.477	0.007	0.007	0.000	0.000	0.000	0.000
53	A	52	VAL	0	-0.009	-0.011	25.668	0.007	0.007	0.000	0.000	0.000	0.000
54	A	53	ALA	0	-0.015	0.012	27.434	0.005	0.005	0.000	0.000	0.000	0.000
55	A	54	PHE	0	0.010	-0.014	21.227	0.007	0.007	0.000	0.000	0.000	0.000
56	A	55	SER	0	0.010	0.006	25.241	0.008	0.008	0.000	0.000	0.000	0.000
57	A	56	ASP	-1	-0.831	-0.879	26.997	0.017	0.017	0.000	0.000	0.000	0.000
58	A	57	LYS	1	0.811	0.904	26.885	-0.037	-0.037	0.000	0.000	0.000	0.000
59	A	58	ALA	0	0.000	0.006	24.942	0.006	0.006	0.000	0.000	0.000	0.000
60	A	59	ASN	0	0.026	0.007	25.253	0.004	0.004	0.000	0.000	0.000	0.000
61	A	60	GLU	-1	-0.764	-0.865	27.160	0.059	0.059	0.000	0.000	0.000	0.000
62	A	61	PHE	0	-0.045	-0.033	20.863	0.005	0.005	0.000	0.000	0.000	0.000
63	A	62	HIS	0	-0.034	-0.022	22.163	0.008	0.008	0.000	0.000	0.000	0.000
64	A	63	ASP	-1	-0.909	-0.954	24.127	0.081	0.081	0.000	0.000	0.000	0.000
65	A	64	VAL	0	-0.114	-0.045	22.068	0.004	0.004	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.043	-0.025	18.944	0.008	0.008	0.000	0.000	0.000	0.000
67	A	66	CYS	0	-0.022	-0.004	18.284	0.024	0.024	0.000	0.000	0.000	0.000
68	A	67	GLU	-1	-0.850	-0.911	16.782	0.092	0.092	0.000	0.000	0.000	0.000
69	A	68	VAL	0	-0.020	-0.016	17.306	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	69	VAL	0	-0.005	-0.005	15.473	0.000	0.000	0.000	0.000	0.000	0.000
71	A	70	ALA	0	0.000	0.023	16.772	-0.017	-0.017	0.000	0.000	0.000	0.000
72	A	71	VAL	0	-0.005	-0.006	13.970	0.005	0.005	0.000	0.000	0.000	0.000
73	A	72	SER	0	0.006	-0.008	17.268	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	73	VAL	0	0.021	0.009	17.496	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	74	ASP	-1	-0.830	-0.888	19.564	-0.084	-0.084	0.000	0.000	0.000	0.000
76	A	75	SER	0	-0.006	0.019	21.517	0.002	0.002	0.000	0.000	0.000	0.000
77	A	76	HIS	0	0.057	0.010	22.440	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	77	PHE	0	0.016	-0.004	24.117	0.007	0.007	0.000	0.000	0.000	0.000
79	A	78	SER	0	0.004	0.008	26.015	0.004	0.004	0.000	0.000	0.000	0.000
80	A	79	HIS	1	0.818	0.880	20.450	0.063	0.063	0.000	0.000	0.000	0.000
81	A	80	LEU	0	0.021	0.027	26.160	0.004	0.004	0.000	0.000	0.000	0.000
82	A	81	ALA	0	0.003	0.008	28.997	0.003	0.003	0.000	0.000	0.000	0.000
83	A	82	TRP	0	0.002	-0.005	25.360	0.001	0.001	0.000	0.000	0.000	0.000
84	A	83	ILE	0	-0.008	-0.010	26.718	0.002	0.002	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.043	-0.020	30.793	0.005	0.005	0.000	0.000	0.000	0.000
86	A	85	THR	0	-0.032	0.004	33.526	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	86	PRO	0	0.014	0.000	34.553	0.001	0.001	0.000	0.000	0.000	0.000
88	A	87	ARG	1	0.828	0.864	31.554	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.895	0.946	35.823	0.001	0.001	0.000	0.000	0.000	0.000
90	A	89	ASN	0	-0.034	-0.017	38.037	0.000	0.000	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.043	0.033	34.622	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	91	GLY	0	-0.009	-0.005	32.439	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.002	0.005	26.831	0.001	0.001	0.000	0.000	0.000	0.000
94	A	93	GLY	0	0.011	0.012	31.115	0.004	0.004	0.000	0.000	0.000	0.000
95	A	94	HIS	0	-0.003	-0.012	30.903	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	95	MET	0	-0.041	-0.015	26.532	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	96	ASN	0	-0.037	-0.024	27.010	0.003	0.003	0.000	0.000	0.000	0.000
98	A	97	ILE	0	0.007	0.004	21.797	0.007	0.007	0.000	0.000	0.000	0.000
99	A	98	ALA	0	0.000	0.017	19.267	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	99	LEU	0	0.004	-0.006	20.534	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	100	LEU	0	0.035	0.009	13.805	0.005	0.005	0.000	0.000	0.000	0.000
102	A	101	SER	0	-0.099	-0.075	18.431	-0.015	-0.015	0.000	0.000	0.000	0.000
103	A	102	ASP	-1	-0.722	-0.859	14.381	-0.260	-0.260	0.000	0.000	0.000	0.000
104	A	103	LEU	0	0.005	-0.003	16.597	-0.017	-0.017	0.000	0.000	0.000	0.000
105	A	104	THR	0	-0.015	-0.022	14.954	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	105	LYS	1	0.875	0.957	15.712	0.149	0.149	0.000	0.000	0.000	0.000
107	A	106	GLN	0	-0.024	-0.012	9.647	0.055	0.055	0.000	0.000	0.000	0.000
108	A	107	ILE	0	0.034	0.023	9.788	-0.105	-0.105	0.000	0.000	0.000	0.000
109	A	108	SER	0	-0.013	-0.048	9.812	-0.091	-0.091	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.749	0.850	11.174	0.370	0.370	0.000	0.000	0.000	0.000
111	A	110	ASP	-1	-0.853	-0.918	6.045	-0.939	-0.939	0.000	0.000	0.000	0.000
112	A	111	TYR	0	-0.070	-0.071	6.439	-0.389	-0.389	0.000	0.000	0.000	0.000
113	A	112	GLY	0	-0.032	-0.008	8.602	0.106	0.106	0.000	0.000	0.000	0.000
114	A	113	VAL	0	-0.008	-0.001	11.195	0.094	0.094	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.046	-0.011	13.887	0.061	0.061	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.010	0.009	15.790	-0.015	-0.015	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.781	-0.890	15.918	-0.334	-0.334	0.000	0.000	0.000	0.000
118	A	117	GLY	0	-0.053	-0.010	19.501	0.015	0.015	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.024	-0.017	22.648	0.012	0.012	0.000	0.000	0.000	0.000
120	A	119	GLY	0	-0.006	0.014	20.378	0.011	0.011	0.000	0.000	0.000	0.000
121	A	120	LEU	0	-0.021	-0.018	20.008	0.010	0.010	0.000	0.000	0.000	0.000
122	A	121	ALA	0	0.030	0.010	16.357	-0.016	-0.016	0.000	0.000	0.000	0.000
123	A	122	LEU	0	0.025	0.006	17.470	0.030	0.030	0.000	0.000	0.000	0.000
124	A	123	ARG	1	0.789	0.864	17.900	0.064	0.064	0.000	0.000	0.000	0.000
125	A	124	GLY	0	0.005	0.003	15.260	0.013	0.013	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.032	-0.018	15.615	0.006	0.006	0.000	0.000	0.000	0.000
127	A	126	PHE	0	0.008	0.002	9.969	-0.024	-0.024	0.000	0.000	0.000	0.000
128	A	127	ILE	0	-0.006	-0.001	12.740	0.015	0.015	0.000	0.000	0.000	0.000
129	A	128	ILE	0	-0.020	-0.009	8.259	0.028	0.028	0.000	0.000	0.000	0.000
130	A	129	ASP	-1	-0.746	-0.857	10.926	0.565	0.565	0.000	0.000	0.000	0.000
131	A	130	PRO	0	0.046	0.026	11.316	0.055	0.055	0.000	0.000	0.000	0.000
132	A	131	ASN	0	-0.007	-0.019	10.913	0.111	0.111	0.000	0.000	0.000	0.000
133	A	132	GLY	0	0.006	0.003	7.258	0.249	0.249	0.000	0.000	0.000	0.000
134	A	133	VAL	0	-0.030	-0.005	5.981	0.072	0.072	0.000	0.000	0.000	0.000
135	A	134	ILE	0	-0.010	0.009	6.177	-0.197	-0.197	0.000	0.000	0.000	0.000
136	A	135	LYS	1	0.810	0.877	8.883	-0.341	-0.341	0.000	0.000	0.000	0.000
137	A	136	HIS	0	-0.015	-0.019	12.364	-0.031	-0.031	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.002	0.017	10.300	-0.016	-0.016	0.000	0.000	0.000	0.000
139	A	138	SER	0	-0.013	0.000	13.653	0.017	0.017	0.000	0.000	0.000	0.000
140	A	139	VAL	0	0.021	0.004	15.589	-0.023	-0.023	0.000	0.000	0.000	0.000
141	A	140	ASN	0	-0.054	-0.010	18.298	0.015	0.015	0.000	0.000	0.000	0.000
142	A	141	ASP	-1	-0.821	-0.910	21.319	-0.112	-0.112	0.000	0.000	0.000	0.000
143	A	142	LEU	0	-0.008	-0.030	22.098	0.010	0.010	0.000	0.000	0.000	0.000
144	A	143	PRO	0	-0.016	0.000	25.122	0.007	0.007	0.000	0.000	0.000	0.000
145	A	144	VAL	0	-0.006	0.007	26.788	0.007	0.007	0.000	0.000	0.000	0.000
146	A	145	GLY	0	0.018	0.013	25.572	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	146	ARG	1	0.769	0.853	18.580	0.075	0.075	0.000	0.000	0.000	0.000
148	A	147	SER	0	0.013	0.011	24.735	0.005	0.005	0.000	0.000	0.000	0.000
149	A	148	VAL	0	0.045	0.016	24.093	0.002	0.002	0.000	0.000	0.000	0.000
150	A	149	GLU	-1	-0.833	-0.922	24.795	0.047	0.047	0.000	0.000	0.000	0.000
151	A	150	GLU	-1	-0.826	-0.916	22.911	0.055	0.055	0.000	0.000	0.000	0.000
152	A	151	THR	0	-0.013	-0.004	19.182	0.005	0.005	0.000	0.000	0.000	0.000
153	A	152	LEU	0	0.001	0.001	20.991	0.015	0.015	0.000	0.000	0.000	0.000
154	A	153	ARG	1	0.787	0.883	23.306	-0.053	-0.053	0.000	0.000	0.000	0.000
155	A	154	LEU	0	-0.016	-0.010	19.060	0.012	0.012	0.000	0.000	0.000	0.000
156	A	155	VAL	0	-0.009	0.001	17.995	0.020	0.020	0.000	0.000	0.000	0.000
157	A	156	LYS	1	0.918	0.959	19.939	-0.057	-0.057	0.000	0.000	0.000	0.000
158	A	157	ALA	0	0.010	0.012	21.617	0.006	0.006	0.000	0.000	0.000	0.000
159	A	158	PHE	0	-0.012	-0.029	16.636	0.013	0.013	0.000	0.000	0.000	0.000
160	A	159	GLN	0	0.027	0.008	19.175	0.006	0.006	0.000	0.000	0.000	0.000
161	A	160	TYR	0	-0.037	-0.013	21.009	0.002	0.002	0.000	0.000	0.000	0.000
162	A	161	VAL	0	-0.021	-0.026	19.582	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	162	GLU	-1	-0.856	-0.899	15.912	0.339	0.339	0.000	0.000	0.000	0.000
164	A	163	THR	0	-0.058	-0.022	20.696	-0.003	-0.003	0.000	0.000	0.000	0.000
165	A	164	HIS	1	0.851	0.927	24.153	-0.134	-0.134	0.000	0.000	0.000	0.000
166	A	165	GLY	0	0.015	0.025	23.902	-0.008	-0.008	0.000	0.000	0.000	0.000
167	A	166	GLU	-1	-0.883	-0.922	24.947	0.092	0.092	0.000	0.000	0.000	0.000
168	A	167	VAL	0	-0.002	-0.016	22.495	0.010	0.010	0.000	0.000	0.000	0.000
169	A	168	CYS	0	0.024	0.007	23.596	-0.009	-0.009	0.000	0.000	0.000	0.000
170	A	169	PRO	0	-0.028	-0.009	24.967	0.001	0.001	0.000	0.000	0.000	0.000
171	A	170	ALA	0	0.029	0.017	26.338	0.003	0.003	0.000	0.000	0.000	0.000
172	A	171	ASN	0	-0.035	-0.034	27.349	-0.002	-0.002	0.000	0.000	0.000	0.000
173	A	172	TRP	0	-0.002	0.024	25.387	0.000	0.000	0.000	0.000	0.000	0.000
174	A	173	THR	0	0.055	0.026	27.625	-0.001	-0.001	0.000	0.000	0.000	0.000
175	A	174	PRO	0	0.022	0.002	28.375	0.003	0.003	0.000	0.000	0.000	0.000
176	A	175	ASP	-1	-0.890	-0.941	30.378	0.060	0.060	0.000	0.000	0.000	0.000
177	A	176	SER	0	-0.096	-0.029	30.780	-0.002	-0.002	0.000	0.000	0.000	0.000
178	A	177	PRO	0	0.004	-0.020	32.044	0.004	0.004	0.000	0.000	0.000	0.000
179	A	178	THR	0	-0.034	-0.030	27.722	0.002	0.002	0.000	0.000	0.000	0.000
180	A	179	ILE	0	-0.031	-0.012	28.242	-0.006	-0.006	0.000	0.000	0.000	0.000
181	A	180	LYS	1	0.930	0.961	28.013	-0.073	-0.073	0.000	0.000	0.000	0.000
182	A	181	PRO	0	0.001	0.021	24.824	-0.009	-0.009	0.000	0.000	0.000	0.000
183	A	182	SER	0	0.012	-0.010	27.098	0.003	0.003	0.000	0.000	0.000	0.000
184	A	183	PRO	0	0.040	0.012	29.805	-0.006	-0.006	0.000	0.000	0.000	0.000
185	A	184	ALA	0	-0.001	0.000	32.554	-0.004	-0.004	0.000	0.000	0.000	0.000
186	A	185	ALA	0	0.045	0.009	32.296	-0.003	-0.003	0.000	0.000	0.000	0.000
187	A	186	SER	0	-0.013	0.002	31.175	-0.002	-0.002	0.000	0.000	0.000	0.000
188	A	187	LYS	1	0.933	0.959	32.995	-0.063	-0.063	0.000	0.000	0.000	0.000
189	A	188	GLU	-1	-0.783	-0.853	35.663	0.068	0.068	0.000	0.000	0.000	0.000
190	A	189	TYR	0	0.010	0.005	32.290	-0.002	-0.002	0.000	0.000	0.000	0.000
191	A	190	PHE	0	0.019	-0.008	31.361	-0.003	-0.003	0.000	0.000	0.000	0.000
192	A	191	GLN	0	-0.007	-0.010	36.570	-0.005	-0.005	0.000	0.000	0.000	0.000
193	A	192	LYS	1	0.813	0.910	35.002	-0.068	-0.068	0.000	0.000	0.000	0.000
194	A	193	VAL	0	-0.016	-0.007	35.357	-0.002	-0.002	0.000	0.000	0.000	0.000
195	A	194	ASN	0	-0.049	-0.001	37.412	-0.005	-0.005	0.000	0.000	0.000	0.000

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