FMO DATABASE

FMODB ID: Z6Z1N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2091852.550943
FMO2-HF: Nuclear repulsion	2017215.327175
FMO2-HF: Total energy	-74637.223769
FMO2-MP2: Total energy	-74858.183362

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.
-8.386	-1.4	6.402	-5.711	-7.676	-0.034

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 : -0.058 / 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	0.038	0.029	3.867	-0.250	1.645	-0.021	-0.947	-0.927	0.002
4	A	3	ALA	0	-0.012	-0.014	6.133	0.214	0.214	0.000	0.000	0.000	0.000
5	A	4	VAL	0	0.033	0.013	7.002	0.256	0.256	0.000	0.000	0.000	0.000
6	A	5	THR	0	-0.076	-0.035	8.815	0.168	0.168	0.000	0.000	0.000	0.000
7	A	6	GLN	0	-0.033	-0.007	3.522	0.997	1.542	0.020	-0.160	-0.404	0.001
8	A	7	HIS	0	-0.013	-0.011	2.610	-2.436	-0.679	0.689	-0.776	-1.670	0.003
9	A	8	ALA	0	0.040	0.009	2.341	-5.144	-3.354	3.515	-2.888	-2.417	-0.031
10	A	9	PRO	0	-0.006	0.002	2.226	-2.035	-0.617	2.195	-1.668	-1.945	-0.009
11	A	10	TYR	0	-0.037	-0.029	3.254	1.020	0.594	0.005	0.730	-0.309	0.000
12	A	11	PHE	0	0.013	0.005	5.251	-0.239	-0.232	-0.001	-0.002	-0.004	0.000
13	A	12	LYS	1	0.895	0.920	9.018	0.059	0.059	0.000	0.000	0.000	0.000
14	A	13	GLY	0	-0.009	0.009	12.294	-0.048	-0.048	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.007	-0.008	15.854	0.018	0.018	0.000	0.000	0.000	0.000
16	A	15	ALA	0	0.000	-0.006	18.725	-0.018	-0.018	0.000	0.000	0.000	0.000
17	A	16	VAL	0	-0.045	-0.016	20.672	0.005	0.005	0.000	0.000	0.000	0.000
18	A	17	VAL	0	0.035	0.001	21.638	0.002	0.002	0.000	0.000	0.000	0.000
19	A	18	ASN	0	0.014	0.006	24.631	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	19	GLY	0	0.004	0.012	27.766	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.949	-0.966	27.636	0.024	0.024	0.000	0.000	0.000	0.000
22	A	21	PHE	0	-0.042	-0.033	24.609	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	22	LYS	1	0.905	0.948	19.073	-0.094	-0.094	0.000	0.000	0.000	0.000
24	A	23	ASP	-1	-0.858	-0.907	17.562	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	24	LEU	0	-0.026	-0.011	15.615	0.020	0.020	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.027	-0.054	10.952	-0.047	-0.047	0.000	0.000	0.000	0.000
27	A	26	LEU	0	0.013	0.008	5.437	0.021	0.021	0.000	0.000	0.000	0.000
28	A	27	ASP	-1	-0.811	-0.865	9.687	0.563	0.563	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.826	-0.896	11.670	0.147	0.147	0.000	0.000	0.000	0.000
30	A	29	PHE	0	0.003	-0.003	11.825	-0.031	-0.031	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.879	0.954	9.336	-0.974	-0.974	0.000	0.000	0.000	0.000
32	A	31	GLY	0	-0.054	-0.037	12.800	-0.058	-0.058	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.857	0.932	14.631	-0.258	-0.258	0.000	0.000	0.000	0.000
34	A	33	TYR	0	-0.029	-0.047	14.071	0.042	0.042	0.000	0.000	0.000	0.000
35	A	34	LEU	0	-0.027	-0.005	10.745	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	35	VAL	0	0.005	0.006	13.681	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	36	LEU	0	0.009	0.010	10.275	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	37	PHE	0	-0.030	-0.030	14.038	-0.028	-0.028	0.000	0.000	0.000	0.000
39	A	38	PHE	0	0.062	0.034	11.068	0.005	0.005	0.000	0.000	0.000	0.000
40	A	39	TYR	0	-0.029	-0.049	16.980	0.020	0.020	0.000	0.000	0.000	0.000
41	A	40	PRO	0	0.005	0.006	20.136	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	41	LEU	0	0.031	-0.004	22.012	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	42	ASP	-1	-0.741	-0.845	24.380	-0.051	-0.051	0.000	0.000	0.000	0.000
44	A	43	PHE	0	-0.050	-0.037	26.550	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	44	THR	0	-0.023	-0.001	27.077	0.002	0.002	0.000	0.000	0.000	0.000
46	A	45	PHE	0	0.023	-0.010	29.840	0.004	0.004	0.000	0.000	0.000	0.000
47	A	46	VAL	0	0.026	0.019	26.993	0.004	0.004	0.000	0.000	0.000	0.000
48	A	47	CYS	0	-0.026	0.043	25.146	0.002	0.002	0.000	0.000	0.000	0.000
49	A	48	PRO	0	0.059	0.047	26.299	0.004	0.004	0.000	0.000	0.000	0.000
50	A	49	THR	0	-0.066	-0.044	28.710	0.006	0.006	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.721	-0.820	23.798	-0.045	-0.045	0.000	0.000	0.000	0.000
52	A	51	ILE	0	0.007	0.007	23.322	0.008	0.008	0.000	0.000	0.000	0.000
53	A	52	VAL	0	-0.006	-0.011	25.461	0.007	0.007	0.000	0.000	0.000	0.000
54	A	53	ALA	0	-0.003	0.017	27.494	0.006	0.006	0.000	0.000	0.000	0.000
55	A	54	PHE	0	0.013	-0.015	21.100	0.007	0.007	0.000	0.000	0.000	0.000
56	A	55	SER	0	0.016	0.019	24.940	0.009	0.009	0.000	0.000	0.000	0.000
57	A	56	ASP	-1	-0.849	-0.895	26.749	0.019	0.019	0.000	0.000	0.000	0.000
58	A	57	LYS	1	0.799	0.886	26.848	-0.044	-0.044	0.000	0.000	0.000	0.000
59	A	58	ALA	0	0.007	0.013	24.668	0.007	0.007	0.000	0.000	0.000	0.000
60	A	59	ASN	0	-0.011	-0.011	24.883	0.004	0.004	0.000	0.000	0.000	0.000
61	A	60	GLU	-1	-0.770	-0.866	26.567	0.067	0.067	0.000	0.000	0.000	0.000
62	A	61	PHE	0	-0.043	-0.026	20.554	0.006	0.006	0.000	0.000	0.000	0.000
63	A	62	HIS	0	-0.009	-0.011	21.639	0.010	0.010	0.000	0.000	0.000	0.000
64	A	63	ASP	-1	-0.885	-0.942	23.749	0.086	0.086	0.000	0.000	0.000	0.000
65	A	64	VAL	0	-0.101	-0.044	21.847	0.003	0.003	0.000	0.000	0.000	0.000
66	A	65	ASN	0	-0.042	-0.024	18.953	0.009	0.009	0.000	0.000	0.000	0.000
67	A	66	CYS	0	-0.053	-0.016	18.102	0.028	0.028	0.000	0.000	0.000	0.000
68	A	67	GLU	-1	-0.852	-0.918	16.530	0.091	0.091	0.000	0.000	0.000	0.000
69	A	68	VAL	0	-0.024	-0.018	17.538	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	69	VAL	0	-0.019	-0.006	15.225	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	70	ALA	0	0.030	0.033	16.789	-0.017	-0.017	0.000	0.000	0.000	0.000
72	A	71	VAL	0	-0.028	-0.018	14.133	0.003	0.003	0.000	0.000	0.000	0.000
73	A	72	SER	0	0.007	-0.016	17.449	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	73	VAL	0	0.006	0.005	17.748	0.000	0.000	0.000	0.000	0.000	0.000
75	A	74	ASP	-1	-0.793	-0.857	19.648	-0.090	-0.090	0.000	0.000	0.000	0.000
76	A	75	SER	0	-0.002	0.013	21.500	0.000	0.000	0.000	0.000	0.000	0.000
77	A	76	HIS	0	0.044	0.011	22.251	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	77	PHE	0	0.024	0.000	23.855	0.008	0.008	0.000	0.000	0.000	0.000
79	A	78	SER	0	-0.018	0.012	25.755	0.003	0.003	0.000	0.000	0.000	0.000
80	A	79	HIS	1	0.851	0.886	20.446	0.071	0.071	0.000	0.000	0.000	0.000
81	A	80	LEU	0	0.033	0.033	26.086	0.005	0.005	0.000	0.000	0.000	0.000
82	A	81	ALA	0	0.007	0.011	28.784	0.004	0.004	0.000	0.000	0.000	0.000
83	A	82	TRP	0	-0.015	-0.011	25.313	0.002	0.002	0.000	0.000	0.000	0.000
84	A	83	ILE	0	0.002	-0.003	26.419	0.002	0.002	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.067	-0.039	30.653	0.005	0.005	0.000	0.000	0.000	0.000
86	A	85	THR	0	-0.029	0.007	33.347	0.000	0.000	0.000	0.000	0.000	0.000
87	A	86	PRO	0	0.009	0.000	34.338	0.001	0.001	0.000	0.000	0.000	0.000
88	A	87	ARG	1	0.827	0.862	31.155	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.877	0.940	35.656	0.002	0.002	0.000	0.000	0.000	0.000
90	A	89	ASN	0	-0.035	-0.019	37.795	0.001	0.001	0.000	0.000	0.000	0.000
91	A	90	GLY	0	0.032	0.026	34.509	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	91	GLY	0	0.009	0.004	32.472	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.010	0.005	26.692	0.002	0.002	0.000	0.000	0.000	0.000
94	A	93	GLY	0	0.004	0.007	31.048	0.005	0.005	0.000	0.000	0.000	0.000
95	A	94	HIS	0	-0.002	-0.010	30.258	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	95	MET	0	-0.038	-0.014	26.206	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	96	ASN	0	-0.050	-0.025	26.841	0.003	0.003	0.000	0.000	0.000	0.000
98	A	97	ILE	0	0.023	0.008	21.737	0.008	0.008	0.000	0.000	0.000	0.000
99	A	98	ALA	0	0.004	0.016	18.952	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	99	LEU	0	0.013	0.002	20.379	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	100	LEU	0	0.025	0.010	13.681	0.005	0.005	0.000	0.000	0.000	0.000
102	A	101	SER	0	-0.078	-0.048	18.310	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	102	ASP	-1	-0.705	-0.832	14.615	-0.285	-0.285	0.000	0.000	0.000	0.000
104	A	103	LEU	0	0.030	0.013	16.750	-0.015	-0.015	0.000	0.000	0.000	0.000
105	A	104	THR	0	-0.001	-0.004	15.038	0.000	0.000	0.000	0.000	0.000	0.000
106	A	105	LYS	1	0.776	0.888	16.059	0.151	0.151	0.000	0.000	0.000	0.000
107	A	106	GLN	0	0.017	0.007	9.674	0.057	0.057	0.000	0.000	0.000	0.000
108	A	107	ILE	0	0.017	0.008	10.006	-0.107	-0.107	0.000	0.000	0.000	0.000
109	A	108	SER	0	-0.006	-0.053	10.147	-0.080	-0.080	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.723	0.837	11.409	0.391	0.391	0.000	0.000	0.000	0.000
111	A	110	ASP	-1	-0.839	-0.907	6.133	-1.000	-1.000	0.000	0.000	0.000	0.000
112	A	111	TYR	0	-0.066	-0.068	6.422	-0.349	-0.349	0.000	0.000	0.000	0.000
113	A	112	GLY	0	-0.026	-0.007	8.699	0.102	0.102	0.000	0.000	0.000	0.000
114	A	113	VAL	0	-0.027	-0.016	11.224	0.103	0.103	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.057	-0.014	14.069	0.063	0.063	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.016	0.012	16.018	-0.013	-0.013	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.733	-0.858	16.099	-0.336	-0.336	0.000	0.000	0.000	0.000
118	A	117	GLY	0	-0.035	-0.014	19.647	0.017	0.017	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.094	-0.054	22.408	0.020	0.020	0.000	0.000	0.000	0.000
120	A	119	GLY	0	-0.007	0.015	20.751	0.011	0.011	0.000	0.000	0.000	0.000
121	A	120	LEU	0	-0.014	-0.006	20.333	0.005	0.005	0.000	0.000	0.000	0.000
122	A	121	ALA	0	0.025	0.012	16.765	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	122	LEU	0	0.044	0.010	17.543	0.031	0.031	0.000	0.000	0.000	0.000
124	A	123	ARG	1	0.792	0.862	18.174	0.063	0.063	0.000	0.000	0.000	0.000
125	A	124	GLY	0	0.013	0.003	15.420	0.017	0.017	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.046	-0.030	15.470	0.005	0.005	0.000	0.000	0.000	0.000
127	A	126	PHE	0	-0.002	0.002	9.710	-0.018	-0.018	0.000	0.000	0.000	0.000
128	A	127	ILE	0	0.008	0.008	12.844	0.010	0.010	0.000	0.000	0.000	0.000
129	A	128	ILE	0	-0.010	-0.006	8.342	0.037	0.037	0.000	0.000	0.000	0.000
130	A	129	ASP	-1	-0.727	-0.845	10.545	0.636	0.636	0.000	0.000	0.000	0.000
131	A	130	PRO	0	0.044	0.031	11.146	0.058	0.058	0.000	0.000	0.000	0.000
132	A	131	ASN	0	-0.001	-0.016	10.758	0.076	0.076	0.000	0.000	0.000	0.000
133	A	132	GLY	0	0.025	0.022	7.057	0.297	0.297	0.000	0.000	0.000	0.000
134	A	133	VAL	0	-0.038	-0.015	6.013	0.021	0.021	0.000	0.000	0.000	0.000
135	A	134	ILE	0	-0.007	0.006	6.076	-0.237	-0.237	0.000	0.000	0.000	0.000
136	A	135	LYS	1	0.803	0.875	8.706	-0.370	-0.370	0.000	0.000	0.000	0.000
137	A	136	HIS	0	-0.007	-0.018	12.229	-0.033	-0.033	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.008	0.010	10.268	-0.012	-0.012	0.000	0.000	0.000	0.000
139	A	138	SER	0	-0.019	-0.002	13.552	0.015	0.015	0.000	0.000	0.000	0.000
140	A	139	VAL	0	0.023	-0.006	15.647	-0.027	-0.027	0.000	0.000	0.000	0.000
141	A	140	ASN	0	-0.063	-0.019	18.379	0.013	0.013	0.000	0.000	0.000	0.000
142	A	141	ASP	-1	-0.824	-0.913	21.225	-0.111	-0.111	0.000	0.000	0.000	0.000
143	A	142	LEU	0	0.003	-0.016	22.142	0.011	0.011	0.000	0.000	0.000	0.000
144	A	143	PRO	0	-0.022	-0.002	25.118	0.007	0.007	0.000	0.000	0.000	0.000
145	A	144	VAL	0	-0.003	0.003	26.739	0.008	0.008	0.000	0.000	0.000	0.000
146	A	145	GLY	0	0.020	0.024	25.568	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	146	ARG	1	0.767	0.843	18.693	0.074	0.074	0.000	0.000	0.000	0.000
148	A	147	SER	0	0.008	0.009	24.505	0.004	0.004	0.000	0.000	0.000	0.000
149	A	148	VAL	0	0.052	0.024	23.794	0.004	0.004	0.000	0.000	0.000	0.000
150	A	149	GLU	-1	-0.793	-0.899	24.299	0.054	0.054	0.000	0.000	0.000	0.000
151	A	150	GLU	-1	-0.841	-0.912	22.393	0.067	0.067	0.000	0.000	0.000	0.000
152	A	151	THR	0	-0.022	-0.018	18.923	0.008	0.008	0.000	0.000	0.000	0.000
153	A	152	LEU	0	-0.010	-0.001	20.717	0.017	0.017	0.000	0.000	0.000	0.000
154	A	153	ARG	1	0.766	0.868	23.123	-0.061	-0.061	0.000	0.000	0.000	0.000
155	A	154	LEU	0	-0.017	-0.010	18.736	0.013	0.013	0.000	0.000	0.000	0.000
156	A	155	VAL	0	-0.015	-0.008	17.764	0.022	0.022	0.000	0.000	0.000	0.000
157	A	156	LYS	1	0.904	0.947	19.683	-0.063	-0.063	0.000	0.000	0.000	0.000
158	A	157	ALA	0	0.005	0.006	21.285	0.005	0.005	0.000	0.000	0.000	0.000
159	A	158	PHE	0	-0.021	-0.026	16.458	0.014	0.014	0.000	0.000	0.000	0.000
160	A	159	GLN	0	0.042	0.012	18.939	0.001	0.001	0.000	0.000	0.000	0.000
161	A	160	TYR	0	-0.021	-0.007	20.816	-0.002	-0.002	0.000	0.000	0.000	0.000
162	A	161	VAL	0	-0.018	-0.020	19.505	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	162	GLU	-1	-0.848	-0.880	15.856	0.353	0.353	0.000	0.000	0.000	0.000
164	A	163	THR	0	-0.051	-0.026	20.540	-0.006	-0.006	0.000	0.000	0.000	0.000
165	A	164	HIS	1	0.850	0.921	24.009	-0.148	-0.148	0.000	0.000	0.000	0.000
166	A	165	GLY	0	0.009	0.029	23.764	-0.010	-0.010	0.000	0.000	0.000	0.000
167	A	166	GLU	-1	-0.860	-0.910	24.793	0.098	0.098	0.000	0.000	0.000	0.000
168	A	167	VAL	0	-0.007	-0.014	22.406	0.012	0.012	0.000	0.000	0.000	0.000
169	A	168	CYS	0	0.030	0.015	23.527	-0.010	-0.010	0.000	0.000	0.000	0.000
170	A	169	PRO	0	-0.035	-0.007	24.743	0.003	0.003	0.000	0.000	0.000	0.000
171	A	170	ALA	0	0.037	0.015	26.208	0.002	0.002	0.000	0.000	0.000	0.000
172	A	171	ASN	0	-0.031	-0.032	27.180	-0.002	-0.002	0.000	0.000	0.000	0.000
173	A	172	TRP	0	-0.010	0.023	24.994	0.001	0.001	0.000	0.000	0.000	0.000
174	A	173	THR	0	0.042	0.016	27.290	0.000	0.000	0.000	0.000	0.000	0.000
175	A	174	PRO	0	0.056	0.018	27.622	0.003	0.003	0.000	0.000	0.000	0.000
176	A	175	ASP	-1	-0.896	-0.942	29.838	0.066	0.066	0.000	0.000	0.000	0.000
177	A	176	SER	0	-0.080	-0.018	30.486	-0.004	-0.004	0.000	0.000	0.000	0.000
178	A	177	PRO	0	0.004	-0.023	31.348	0.006	0.006	0.000	0.000	0.000	0.000
179	A	178	THR	0	-0.042	-0.025	27.315	0.002	0.002	0.000	0.000	0.000	0.000
180	A	179	ILE	0	-0.012	-0.006	28.163	-0.007	-0.007	0.000	0.000	0.000	0.000
181	A	180	LYS	1	0.871	0.915	27.917	-0.078	-0.078	0.000	0.000	0.000	0.000
182	A	181	PRO	0	0.029	0.027	24.664	-0.010	-0.010	0.000	0.000	0.000	0.000
183	A	182	SER	0	0.019	-0.004	26.910	0.001	0.001	0.000	0.000	0.000	0.000
184	A	183	PRO	0	0.042	0.025	29.335	-0.005	-0.005	0.000	0.000	0.000	0.000
185	A	184	ALA	0	0.009	0.018	32.149	-0.005	-0.005	0.000	0.000	0.000	0.000
186	A	185	ALA	0	0.051	0.013	32.185	-0.003	-0.003	0.000	0.000	0.000	0.000
187	A	186	SER	0	-0.003	-0.006	30.844	-0.003	-0.003	0.000	0.000	0.000	0.000
188	A	187	LYS	1	0.879	0.922	32.640	-0.068	-0.068	0.000	0.000	0.000	0.000
189	A	188	GLU	-1	-0.789	-0.853	35.205	0.074	0.074	0.000	0.000	0.000	0.000
190	A	189	TYR	0	0.002	-0.002	32.200	-0.003	-0.003	0.000	0.000	0.000	0.000
191	A	190	PHE	0	0.012	-0.009	31.475	-0.003	-0.003	0.000	0.000	0.000	0.000
192	A	191	GLN	0	0.022	0.007	36.534	-0.004	-0.004	0.000	0.000	0.000	0.000
193	A	192	LYS	1	0.821	0.912	34.251	-0.075	-0.075	0.000	0.000	0.000	0.000
194	A	193	VAL	0	-0.032	-0.009	35.148	-0.001	-0.001	0.000	0.000	0.000	0.000
195	A	194	ASN	0	-0.063	-0.011	37.143	-0.005	-0.005	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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