FMO DATABASE

FMODB ID: VQ241

Calculation Name: 4XAH-A-Xray372

Preferred Name:

Target Type:

Ligand Name: s,s-(2-hydroxyethyl)thiocysteine

ligand 3-letter code: CME

PDB ID: 4XAH

Chain ID: A

ChEMBL ID:

UniProt ID: Q03705

Base Structure: X-ray

Registration Date: 2023-09-20

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	177
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1983798.965774
FMO2-HF: Nuclear repulsion	1911364.958036
FMO2-HF: Total energy	-72434.007738
FMO2-MP2: Total energy	-72641.038311

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:MET)

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

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.
-30.485	-24.749	29.299	-13.193	-21.838	-0.078

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.061 / q_NPA : -0.032

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	VAL	0	-0.008	-0.013	2.391	-0.623	0.559	2.398	-1.129	-2.451	-0.001
4	A	4	SER	0	-0.035	-0.015	4.659	0.228	0.320	-0.001	-0.017	-0.074	0.000
5	A	5	ILE	0	0.053	0.015	8.199	0.154	0.154	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.024	0.020	11.236	-0.002	-0.002	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.047	0.020	14.741	0.048	0.048	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.000	0.012	17.593	0.015	0.015	0.000	0.000	0.000	0.000
9	A	9	PHE	0	-0.088	-0.054	15.994	0.030	0.030	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.041	0.025	15.095	-0.024	-0.024	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.926	-0.956	14.469	-0.056	-0.056	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.068	-0.025	11.601	0.034	0.034	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.905	0.966	7.418	-0.061	-0.061	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.004	-0.002	7.309	0.130	0.130	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.002	0.018	2.305	-0.838	-0.360	1.040	-0.564	-0.954	0.000
16	A	16	LEU	0	-0.037	-0.019	3.628	0.410	0.892	0.003	-0.100	-0.384	0.000
17	A	17	ALA	0	0.050	0.027	2.426	-3.956	-1.925	3.303	-2.496	-2.838	-0.020
18	A	18	LEU	0	0.012	0.011	3.504	0.579	0.598	0.027	0.084	-0.130	0.000
19	A	19	PHE	0	0.005	0.005	5.721	-0.394	-0.394	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.822	-0.916	8.787	-0.409	-0.409	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.069	-0.057	11.929	0.136	0.136	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.028	-0.025	12.339	0.050	0.050	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.917	0.956	14.975	0.119	0.119	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.035	-0.032	15.415	-0.024	-0.024	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.072	0.046	16.900	0.023	0.023	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.892	0.933	17.858	0.019	0.019	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.887	-0.927	18.792	0.178	0.178	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.026	0.026	13.537	0.011	0.011	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.859	0.912	17.522	0.035	0.035	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.106	-0.059	19.646	0.002	0.002	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.887	0.928	19.227	-0.179	-0.179	0.000	0.000	0.000	0.000
32	A	32	MET	0	-0.003	0.022	17.033	0.014	0.014	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.003	-0.013	18.185	0.015	0.015	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.836	-0.898	19.875	0.187	0.187	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.032	0.004	15.070	0.028	0.028	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.017	0.032	14.903	0.050	0.050	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.051	-0.024	14.998	0.004	0.004	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.062	-0.028	11.620	0.031	0.031	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.055	-0.001	6.860	0.069	0.069	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.015	0.012	11.067	-0.054	-0.054	0.000	0.000	0.000	0.000
41	A	41	PHE	0	0.029	-0.003	10.276	0.005	0.005	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.006	-0.011	11.899	0.014	0.014	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.759	-0.887	12.931	-0.304	-0.304	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.011	0.001	11.777	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.814	0.897	14.021	0.195	0.195	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.038	-0.021	16.930	0.018	0.018	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.059	-0.027	12.256	0.008	0.008	0.000	0.000	0.000	0.000
48	A	48	CYS	0	0.005	0.008	14.626	-0.026	-0.026	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.004	-0.014	13.736	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.026	0.001	10.939	-0.024	-0.024	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.854	-0.888	11.696	-0.414	-0.414	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.039	0.028	14.940	0.026	0.026	0.000	0.000	0.000	0.000
53	A	53	MET	0	-0.010	0.006	9.935	0.069	0.069	0.000	0.000	0.000	0.000
54	A	54	TYR	0	0.023	-0.012	7.656	0.050	0.050	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.005	-0.001	13.673	0.081	0.081	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.050	0.023	15.449	0.048	0.048	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.033	-0.003	10.468	0.057	0.057	0.000	0.000	0.000	0.000
58	A	58	TYR	0	-0.018	-0.028	14.751	0.049	0.049	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.897	0.948	17.295	0.227	0.227	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.003	-0.043	16.174	0.035	0.035	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.017	-0.008	13.863	0.034	0.034	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.001	0.003	18.171	0.028	0.028	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.869	-0.937	21.638	-0.095	-0.095	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.054	-0.029	19.104	0.019	0.019	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.886	0.962	20.866	0.097	0.097	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.038	-0.033	22.627	0.008	0.008	0.000	0.000	0.000	0.000
67	A	67	ASN	0	-0.022	-0.017	25.199	0.015	0.015	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.894	0.952	26.018	0.061	0.061	0.000	0.000	0.000	0.000
69	A	69	MET	0	-0.033	0.007	20.031	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.896	0.943	23.394	0.080	0.080	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.057	-0.058	20.656	0.014	0.014	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.941	0.952	20.610	-0.064	-0.064	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.001	0.014	16.612	0.002	0.002	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.126	0.062	14.266	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.007	0.014	11.504	-0.077	-0.077	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.025	-0.041	14.035	-0.031	-0.031	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.750	-0.836	17.571	-0.090	-0.090	0.000	0.000	0.000	0.000
78	A	78	CYS	0	-0.024	0.002	14.258	-0.041	-0.041	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.013	0.005	15.364	-0.027	-0.027	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.072	-0.052	17.237	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	81	CME	0	-0.099	-0.035	18.615	0.003	0.003	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.029	0.034	15.081	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.005	0.019	18.698	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.027	0.009	21.892	0.010	0.010	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.112	-0.044	24.467	0.016	0.016	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.082	0.034	25.673	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.016	0.004	27.217	0.012	0.012	0.000	0.000	0.000	0.000
88	A	88	ILE	0	0.080	0.037	20.269	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.033	-0.027	23.212	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.782	-0.864	24.984	-0.101	-0.101	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.025	0.015	21.172	-0.010	-0.010	0.000	0.000	0.000	0.000
92	A	92	PHE	0	0.019	-0.004	16.920	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.041	0.000	20.923	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.869	0.906	22.821	0.104	0.104	0.000	0.000	0.000	0.000
95	A	95	PHE	0	0.037	0.007	17.659	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.024	0.026	16.925	-0.027	-0.027	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.043	-0.009	14.420	-0.015	-0.015	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.805	0.879	17.462	0.200	0.200	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.790	-0.888	19.809	-0.020	-0.020	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.814	-0.887	21.737	-0.132	-0.132	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.011	0.014	16.522	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.031	0.019	17.075	0.029	0.029	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.005	0.004	12.270	0.017	0.017	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.061	-0.031	9.311	0.091	0.091	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.040	0.031	7.703	-0.160	-0.160	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.054	-0.019	6.342	0.207	0.207	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.024	0.014	5.919	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.875	0.940	6.393	-0.344	-0.344	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.015	-0.003	7.180	-0.156	-0.156	0.000	0.000	0.000	0.000
110	A	110	HIS	0	-0.057	-0.047	4.835	0.121	0.121	0.000	0.000	0.000	0.000
111	A	111	THR	0	0.018	-0.012	9.609	-0.058	-0.058	0.000	0.000	0.000	0.000
112	A	112	ASN	0	0.011	0.001	12.879	-0.035	-0.035	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.061	-0.013	7.667	0.010	0.010	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.829	-0.910	10.729	0.206	0.206	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.932	-0.995	9.147	0.121	0.121	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.062	-0.012	2.921	-0.358	0.033	0.129	-0.103	-0.417	-0.001
117	A	117	ASP	-1	-0.779	-0.873	5.727	1.657	1.657	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.889	0.918	2.205	-5.353	-4.067	1.615	-0.510	-2.391	0.002
119	A	119	GLU	-1	-0.765	-0.876	3.816	6.561	7.403	0.122	-0.195	-0.769	-0.003
120	A	120	GLN	0	-0.043	0.001	6.699	-0.272	-0.272	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.002	-0.012	2.261	-1.171	-0.879	2.004	-0.433	-1.862	-0.003
122	A	122	ARG	1	0.847	0.880	1.994	-8.774	-7.349	4.804	-2.354	-3.876	0.002
123	A	123	THR	0	-0.012	-0.001	4.974	-1.403	-1.379	0.002	-0.025	-0.001	0.000
124	A	124	ILE	0	-0.004	0.006	8.247	-0.404	-0.404	0.000	0.000	0.000	0.000
125	A	125	MET	0	-0.015	-0.013	2.739	-1.535	-1.291	1.587	-0.376	-1.454	0.003
126	A	126	THR	0	-0.025	-0.022	7.304	-0.505	-0.505	0.000	0.000	0.000	0.000
127	A	127	SER	0	-0.033	-0.008	9.587	-0.222	-0.222	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.044	-0.015	11.258	-0.157	-0.157	0.000	0.000	0.000	0.000
129	A	129	VAL	0	-0.043	-0.028	9.546	-0.129	-0.129	0.000	0.000	0.000	0.000
130	A	130	LYS	1	0.854	0.929	11.836	-0.252	-0.252	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.060	0.021	12.184	-0.049	-0.049	0.000	0.000	0.000	0.000
132	A	132	GLN	0	-0.033	-0.012	9.907	0.125	0.125	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.800	-0.859	1.785	-12.235	-15.796	12.266	-4.899	-3.805	-0.057
134	A	134	ILE	0	-0.015	-0.001	6.124	0.231	0.231	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.868	-0.926	3.928	-2.921	-2.659	-0.001	-0.027	-0.234	0.000
136	A	136	PHE	0	-0.004	-0.006	3.941	0.670	0.937	0.002	-0.048	-0.221	0.000
137	A	137	ASN	0	-0.002	-0.023	5.348	0.044	0.024	-0.001	-0.001	0.023	0.000
138	A	138	ASP	-1	-0.749	-0.893	8.743	-0.747	-0.747	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.846	-0.898	12.184	-0.538	-0.538	0.000	0.000	0.000	0.000
140	A	140	ASN	0	-0.006	-0.021	8.115	0.334	0.334	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.037	-0.011	9.421	0.101	0.101	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.051	-0.028	12.367	0.123	0.123	0.000	0.000	0.000	0.000
143	A	143	ARG	1	0.789	0.883	12.420	0.753	0.753	0.000	0.000	0.000	0.000
144	A	144	PHE	0	-0.037	-0.022	11.788	0.064	0.064	0.000	0.000	0.000	0.000
145	A	145	TYR	0	-0.030	0.007	16.176	0.043	0.043	0.000	0.000	0.000	0.000
146	A	146	ASP	-1	-0.818	-0.915	17.799	-0.194	-0.194	0.000	0.000	0.000	0.000
147	A	147	GLU	-1	-0.785	-0.888	21.446	-0.215	-0.215	0.000	0.000	0.000	0.000
148	A	148	ALA	0	-0.023	-0.005	23.668	0.015	0.015	0.000	0.000	0.000	0.000
149	A	149	LEU	0	0.011	-0.009	21.240	0.015	0.015	0.000	0.000	0.000	0.000
150	A	150	ILE	0	0.033	0.016	18.902	0.014	0.014	0.000	0.000	0.000	0.000
151	A	151	ARG	1	0.759	0.865	23.223	0.193	0.193	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.885	0.957	26.778	0.162	0.162	0.000	0.000	0.000	0.000
153	A	153	ILE	0	-0.040	-0.019	23.069	0.013	0.013	0.000	0.000	0.000	0.000
154	A	154	TYR	0	-0.034	-0.050	19.641	0.000	0.000	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.858	0.943	25.817	0.136	0.136	0.000	0.000	0.000	0.000
156	A	156	LEU	0	0.009	0.012	24.857	0.001	0.001	0.000	0.000	0.000	0.000
157	A	157	SER	0	-0.012	-0.032	29.315	0.008	0.008	0.000	0.000	0.000	0.000
158	A	158	ASP	-1	-0.905	-0.958	31.976	-0.139	-0.139	0.000	0.000	0.000	0.000
159	A	159	ASP	-1	-0.874	-0.916	33.904	-0.118	-0.118	0.000	0.000	0.000	0.000
160	A	160	PHE	0	-0.029	-0.010	26.431	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	161	LYS	1	0.881	0.934	31.027	0.136	0.136	0.000	0.000	0.000	0.000
162	A	162	PRO	0	-0.016	0.008	26.147	0.003	0.003	0.000	0.000	0.000	0.000
163	A	163	GLN	0	0.009	-0.010	28.060	0.001	0.001	0.000	0.000	0.000	0.000
164	A	164	ASP	-1	-0.817	-0.896	23.808	-0.299	-0.299	0.000	0.000	0.000	0.000
165	A	165	VAL	0	0.043	0.025	18.050	0.009	0.009	0.000	0.000	0.000	0.000
166	A	166	ASN	0	-0.007	-0.014	20.002	-0.040	-0.040	0.000	0.000	0.000	0.000
167	A	167	GLY	0	-0.002	0.002	21.595	0.006	0.006	0.000	0.000	0.000	0.000
168	A	168	LEU	0	-0.008	-0.012	21.176	0.013	0.013	0.000	0.000	0.000	0.000
169	A	169	SER	0	-0.005	-0.044	18.381	-0.009	-0.009	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.976	0.996	20.304	0.231	0.231	0.000	0.000	0.000	0.000
171	A	171	ALA	0	-0.021	-0.012	22.852	0.014	0.014	0.000	0.000	0.000	0.000
172	A	172	LEU	0	-0.011	-0.005	19.455	0.016	0.016	0.000	0.000	0.000	0.000
173	A	173	VAL	0	0.008	0.003	18.754	0.009	0.009	0.000	0.000	0.000	0.000
174	A	174	ASP	-1	-0.996	-0.991	21.314	-0.178	-0.178	0.000	0.000	0.000	0.000
175	A	175	ALA	0	-0.009	0.004	24.094	0.014	0.014	0.000	0.000	0.000	0.000
176	A	176	ILE	0	-0.098	-0.034	18.603	0.014	0.014	0.000	0.000	0.000	0.000
177	A	177	GLN	0	-0.011	-0.005	22.140	0.011	0.011	0.000	0.000	0.000	0.000

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