FMO DATABASE

FMODB ID: YVQ22

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1981890.250123
FMO2-HF: Nuclear repulsion	1909457.087705
FMO2-HF: Total energy	-72433.162418
FMO2-MP2: Total energy	-72640.153194

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.
-34.449	-31.501	34.503	-13.07	-24.374	-0.097

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 : -0.063 / q_NPA : -0.030

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	-0.030	-0.026	2.228	-0.597	0.771	2.359	-1.092	-2.635	-0.002
4	A	4	SER	0	-0.037	-0.015	4.747	0.139	0.235	-0.001	-0.025	-0.069	0.000
5	A	5	ILE	0	0.066	0.020	8.347	0.153	0.153	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.018	0.019	11.201	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.046	0.020	14.824	0.041	0.041	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.006	0.034	17.499	0.009	0.009	0.000	0.000	0.000	0.000
9	A	9	PHE	0	-0.078	-0.055	16.093	0.022	0.022	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.037	0.020	14.975	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.902	-0.940	14.066	0.028	0.028	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.080	-0.031	11.744	0.034	0.034	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.916	0.984	6.916	-0.187	-0.187	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.002	-0.001	7.661	0.132	0.132	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.008	0.006	3.051	-1.266	-0.518	0.487	-0.351	-0.883	0.001
16	A	16	LEU	0	-0.038	-0.020	3.741	0.198	0.660	0.001	-0.101	-0.362	0.000
17	A	17	ALA	0	0.054	0.033	2.496	-4.724	-2.706	3.393	-2.510	-2.901	-0.024
18	A	18	LEU	0	0.013	0.010	3.502	0.941	0.942	0.035	0.110	-0.146	0.000
19	A	19	PHE	0	-0.001	0.003	5.995	-0.403	-0.403	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.860	-0.946	8.766	-0.485	-0.485	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.039	-0.031	11.913	0.126	0.126	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.019	-0.018	12.467	0.048	0.048	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.926	0.954	14.958	0.155	0.155	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.020	-0.013	15.548	-0.025	-0.025	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.070	0.045	17.139	0.024	0.024	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.935	0.972	18.095	0.040	0.040	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.917	-0.960	19.406	0.129	0.129	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.025	0.031	13.932	0.014	0.014	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.898	0.945	17.675	0.048	0.048	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.115	-0.068	19.564	0.007	0.007	0.000	0.000	0.000	0.000
31	A	31	LYS	1	1.019	1.011	19.077	-0.164	-0.164	0.000	0.000	0.000	0.000
32	A	32	MET	0	-0.006	0.020	16.739	0.017	0.017	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.004	-0.013	18.013	0.020	0.020	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.932	-0.967	19.872	0.169	0.169	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.025	-0.001	14.534	0.029	0.029	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.026	0.015	14.946	0.051	0.051	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.056	-0.031	15.486	0.018	0.018	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.051	-0.025	11.822	0.035	0.035	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.021	-0.018	6.814	0.118	0.118	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.012	0.012	10.925	-0.083	-0.083	0.000	0.000	0.000	0.000
41	A	41	PHE	0	0.024	-0.005	10.620	0.020	0.020	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.003	-0.007	11.423	0.014	0.014	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.788	-0.905	12.928	-0.335	-0.335	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.005	-0.003	11.773	0.001	0.001	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.892	0.957	14.020	0.214	0.214	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.032	-0.015	16.940	0.021	0.021	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.058	-0.028	12.261	0.015	0.015	0.000	0.000	0.000	0.000
48	A	48	CYS	0	-0.032	-0.003	14.623	-0.039	-0.039	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.020	-0.005	13.710	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.044	0.010	10.931	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.869	-0.896	11.690	-0.356	-0.356	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.047	0.033	14.931	0.025	0.025	0.000	0.000	0.000	0.000
53	A	53	MET	0	-0.012	0.000	9.978	0.072	0.072	0.000	0.000	0.000	0.000
54	A	54	TYR	0	0.018	-0.014	7.743	0.037	0.037	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.005	0.002	13.661	0.084	0.084	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.046	0.022	15.386	0.047	0.047	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.029	-0.007	10.470	0.056	0.056	0.000	0.000	0.000	0.000
58	A	58	TYR	0	-0.031	-0.060	14.938	0.051	0.051	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.909	0.951	17.782	0.180	0.180	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.008	-0.026	16.738	0.033	0.033	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.023	-0.012	14.115	0.029	0.029	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.007	0.008	18.504	0.022	0.022	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.907	-0.971	22.030	-0.067	-0.067	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.031	-0.024	19.516	0.015	0.015	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.875	0.959	21.015	0.048	0.048	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.040	-0.033	22.786	0.005	0.005	0.000	0.000	0.000	0.000
67	A	67	ASN	0	-0.040	-0.013	25.467	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.936	0.971	26.324	0.031	0.031	0.000	0.000	0.000	0.000
69	A	69	MET	0	-0.015	0.019	20.318	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.921	0.959	23.773	0.047	0.047	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.067	-0.049	21.140	0.011	0.011	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.948	0.955	21.335	-0.077	-0.077	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.008	0.005	16.934	0.010	0.010	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.125	0.062	14.656	-0.014	-0.014	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.017	0.027	11.922	-0.051	-0.051	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.012	-0.023	14.514	-0.045	-0.045	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.758	-0.863	17.678	-0.051	-0.051	0.000	0.000	0.000	0.000
78	A	78	CYS	0	0.004	0.014	12.839	-0.038	-0.038	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.010	-0.001	15.181	-0.034	-0.034	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.065	-0.048	17.122	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	81	CME	0	-0.093	-0.016	18.832	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.021	0.035	14.932	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.005	0.015	18.597	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.033	0.012	21.757	0.011	0.011	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.083	-0.012	24.401	0.016	0.016	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.055	0.018	25.572	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.019	-0.009	27.098	0.010	0.010	0.000	0.000	0.000	0.000
88	A	88	ILE	0	0.061	0.031	20.118	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.048	-0.034	23.055	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.790	-0.899	24.787	-0.092	-0.092	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.022	0.014	20.997	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	92	PHE	0	0.009	-0.003	16.807	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.037	-0.001	20.685	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.859	0.914	22.640	0.095	0.095	0.000	0.000	0.000	0.000
95	A	95	PHE	0	0.045	0.012	17.439	-0.012	-0.012	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.019	0.027	16.676	-0.027	-0.027	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.046	-0.015	14.372	-0.018	-0.018	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.807	0.875	17.200	0.203	0.203	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.841	-0.943	19.843	-0.042	-0.042	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.871	-0.930	21.983	-0.145	-0.145	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.013	0.011	16.545	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.035	0.019	17.080	0.025	0.025	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.014	0.002	12.244	0.010	0.010	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.063	-0.031	9.328	0.108	0.108	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.050	0.037	7.685	-0.198	-0.198	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.048	-0.016	6.143	0.234	0.234	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.019	0.011	5.715	0.053	0.053	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.906	0.954	6.852	-0.581	-0.581	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.014	-0.002	7.610	-0.045	-0.045	0.000	0.000	0.000	0.000
110	A	110	HIS	0	-0.044	-0.036	4.984	-0.100	-0.100	0.000	0.000	0.000	0.000
111	A	111	THR	0	0.011	-0.010	9.654	-0.052	-0.052	0.000	0.000	0.000	0.000
112	A	112	ASN	0	0.013	0.000	13.111	-0.035	-0.035	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.082	-0.030	8.139	0.011	0.011	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.838	-0.912	10.922	0.227	0.227	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.908	-0.990	9.154	0.263	0.263	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.082	-0.030	2.971	-0.429	-0.005	0.230	-0.112	-0.541	-0.001
117	A	117	ASP	-1	-0.781	-0.885	5.481	1.118	1.118	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.931	0.936	2.061	-4.920	-7.137	9.231	-2.162	-4.852	0.002
119	A	119	GLU	-1	-0.801	-0.903	3.030	5.516	4.630	-0.009	1.485	-0.590	-0.002
120	A	120	GLN	0	-0.047	0.021	6.135	-0.099	-0.099	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.019	-0.017	2.159	-0.639	-1.137	3.766	-0.694	-2.573	-0.005
122	A	122	ARG	1	0.902	0.945	2.453	-8.434	-5.834	1.116	-1.284	-2.430	0.006
123	A	123	THR	0	-0.012	-0.007	5.306	-1.106	-1.088	0.000	-0.017	-0.002	0.000
124	A	124	ILE	0	-0.006	0.000	8.202	-0.304	-0.304	0.000	0.000	0.000	0.000
125	A	125	MET	0	-0.016	-0.016	2.781	-1.270	-0.543	0.854	-0.292	-1.288	0.001
126	A	126	THR	0	-0.025	-0.028	7.311	-0.435	-0.435	0.000	0.000	0.000	0.000
127	A	127	SER	0	-0.045	-0.010	9.625	-0.186	-0.186	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.069	-0.029	11.217	-0.123	-0.123	0.000	0.000	0.000	0.000
129	A	129	VAL	0	-0.037	-0.021	9.774	-0.107	-0.107	0.000	0.000	0.000	0.000
130	A	130	LYS	1	0.898	0.957	11.945	-0.161	-0.161	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.060	0.019	12.197	-0.034	-0.034	0.000	0.000	0.000	0.000
132	A	132	GLN	0	-0.036	-0.014	9.889	0.124	0.124	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.815	-0.894	1.784	-15.535	-17.936	13.041	-5.953	-4.687	-0.073
134	A	134	ILE	0	-0.014	0.000	6.072	0.298	0.298	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.900	-0.956	3.906	-3.001	-2.757	-0.001	-0.025	-0.218	0.000
136	A	136	PHE	0	-0.012	-0.013	3.952	0.699	0.963	0.002	-0.046	-0.220	0.000
137	A	137	ASN	0	0.024	0.008	5.349	0.047	0.027	-0.001	-0.001	0.023	0.000
138	A	138	ASP	-1	-0.742	-0.887	8.743	-0.725	-0.725	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.906	-0.941	11.960	-0.575	-0.575	0.000	0.000	0.000	0.000
140	A	140	ASN	0	-0.067	-0.049	8.151	0.350	0.350	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.041	-0.015	9.416	0.102	0.102	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.043	-0.027	12.367	0.126	0.126	0.000	0.000	0.000	0.000
143	A	143	ARG	1	0.899	0.953	13.214	0.708	0.708	0.000	0.000	0.000	0.000
144	A	144	PHE	0	-0.031	-0.019	12.056	0.059	0.059	0.000	0.000	0.000	0.000
145	A	145	TYR	0	-0.038	0.008	16.178	0.045	0.045	0.000	0.000	0.000	0.000
146	A	146	ASP	-1	-0.821	-0.925	17.798	-0.197	-0.197	0.000	0.000	0.000	0.000
147	A	147	GLU	-1	-0.804	-0.902	21.445	-0.205	-0.205	0.000	0.000	0.000	0.000
148	A	148	ALA	0	-0.013	0.004	23.666	0.017	0.017	0.000	0.000	0.000	0.000
149	A	149	LEU	0	0.028	0.005	21.448	0.017	0.017	0.000	0.000	0.000	0.000
150	A	150	ILE	0	0.035	0.021	18.989	0.016	0.016	0.000	0.000	0.000	0.000
151	A	151	ARG	1	0.767	0.871	23.219	0.187	0.187	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.857	0.936	26.773	0.162	0.162	0.000	0.000	0.000	0.000
153	A	153	ILE	0	-0.033	-0.013	22.925	0.014	0.014	0.000	0.000	0.000	0.000
154	A	154	TYR	0	-0.029	-0.042	19.641	0.000	0.000	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.860	0.947	25.810	0.120	0.120	0.000	0.000	0.000	0.000
156	A	156	LEU	0	0.000	0.006	24.867	0.002	0.002	0.000	0.000	0.000	0.000
157	A	157	SER	0	0.022	0.007	29.309	0.006	0.006	0.000	0.000	0.000	0.000
158	A	158	ASP	-1	-0.893	-0.960	31.971	-0.126	-0.126	0.000	0.000	0.000	0.000
159	A	159	ASP	-1	-0.945	-0.967	33.900	-0.106	-0.106	0.000	0.000	0.000	0.000
160	A	160	PHE	0	-0.067	-0.027	26.443	-0.002	-0.002	0.000	0.000	0.000	0.000
161	A	161	LYS	1	0.956	0.972	31.043	0.126	0.126	0.000	0.000	0.000	0.000
162	A	162	PRO	0	-0.021	0.001	26.185	0.003	0.003	0.000	0.000	0.000	0.000
163	A	163	GLN	0	0.011	-0.006	28.065	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	164	ASP	-1	-0.860	-0.923	23.626	-0.268	-0.268	0.000	0.000	0.000	0.000
165	A	165	VAL	0	0.037	0.016	17.998	0.010	0.010	0.000	0.000	0.000	0.000
166	A	166	ASN	0	0.049	0.024	19.911	-0.037	-0.037	0.000	0.000	0.000	0.000
167	A	167	GLY	0	-0.009	0.001	21.592	0.008	0.008	0.000	0.000	0.000	0.000
168	A	168	LEU	0	-0.014	-0.012	21.193	0.014	0.014	0.000	0.000	0.000	0.000
169	A	169	SER	0	0.007	-0.044	18.435	-0.005	-0.005	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.978	0.993	20.298	0.210	0.210	0.000	0.000	0.000	0.000
171	A	171	ALA	0	-0.017	-0.011	22.845	0.015	0.015	0.000	0.000	0.000	0.000
172	A	172	LEU	0	-0.016	-0.006	19.461	0.014	0.014	0.000	0.000	0.000	0.000
173	A	173	VAL	0	-0.001	0.005	18.819	0.010	0.010	0.000	0.000	0.000	0.000
174	A	174	ASP	-1	-0.981	-0.992	21.305	-0.151	-0.151	0.000	0.000	0.000	0.000
175	A	175	ALA	0	-0.013	0.007	24.050	0.014	0.014	0.000	0.000	0.000	0.000
176	A	176	ILE	0	-0.089	-0.030	18.547	0.014	0.014	0.000	0.000	0.000	0.000
177	A	177	GLN	0	-0.035	-0.023	22.157	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)