FMO DATABASE

FMODB ID: 1NJQZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1988122.720745
FMO2-HF: Nuclear repulsion	1915688.376228
FMO2-HF: Total energy	-72434.344518
FMO2-MP2: Total energy	-72641.375402

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.
-35.702	-34.225	39.074	-15.369	-25.18	-0.072

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 : -0.019

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	-0.002	-0.020	2.301	-1.951	-0.380	2.713	-1.492	-2.792	-0.008
4	A	4	SER	0	-0.034	-0.002	4.706	0.265	0.335	-0.001	-0.018	-0.051	0.000
5	A	5	ILE	0	0.054	0.017	8.341	0.161	0.161	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.027	0.023	11.386	-0.027	-0.027	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.032	0.004	14.931	0.057	0.057	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.007	0.021	17.906	0.016	0.016	0.000	0.000	0.000	0.000
9	A	9	PHE	0	-0.082	-0.048	16.067	0.029	0.029	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.038	0.022	15.055	-0.023	-0.023	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.927	-0.961	14.042	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.081	-0.032	11.589	0.048	0.048	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.837	0.905	7.205	-0.267	-0.267	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.007	-0.019	7.340	0.151	0.151	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.003	0.023	2.208	-0.224	-0.485	2.327	-0.694	-1.372	0.002
16	A	16	LEU	0	-0.032	-0.020	3.455	0.679	1.135	0.004	-0.034	-0.426	0.000
17	A	17	ALA	0	0.037	0.018	2.410	-5.217	-2.617	1.614	-1.929	-2.285	-0.015
18	A	18	LEU	0	0.008	0.008	3.663	0.850	0.949	0.013	-0.010	-0.102	0.000
19	A	19	PHE	0	0.022	0.009	5.580	-0.428	-0.428	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.816	-0.908	8.946	-0.523	-0.523	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.055	-0.046	12.130	0.150	0.150	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.001	-0.001	12.365	0.069	0.069	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.870	0.932	15.012	0.215	0.215	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.010	-0.027	15.091	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.059	0.041	16.609	0.029	0.029	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.905	0.938	17.572	0.065	0.065	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.840	-0.890	18.211	0.151	0.151	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.019	0.026	13.161	0.016	0.016	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.862	0.907	17.127	0.100	0.100	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.105	-0.059	19.475	0.010	0.010	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.887	0.925	19.102	-0.159	-0.159	0.000	0.000	0.000	0.000
32	A	32	MET	0	-0.008	0.021	16.863	0.012	0.012	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.007	-0.005	18.198	0.006	0.006	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.797	-0.874	19.503	0.184	0.184	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.058	0.014	14.865	0.029	0.029	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.008	0.028	14.551	0.057	0.057	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.062	-0.036	14.903	0.005	0.005	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.057	-0.012	11.625	0.043	0.043	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.058	-0.003	6.664	0.020	0.020	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.021	-0.004	10.840	-0.032	-0.032	0.000	0.000	0.000	0.000
41	A	41	PHE	0	0.029	0.000	10.122	-0.055	-0.055	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.007	0.000	12.307	0.057	0.057	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.759	-0.865	13.267	-0.434	-0.434	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.021	0.003	12.254	0.003	0.003	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.794	0.868	14.570	0.301	0.301	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.038	-0.019	17.521	0.030	0.030	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.052	-0.028	12.774	0.013	0.013	0.000	0.000	0.000	0.000
48	A	48	CYS	0	0.023	0.022	14.612	-0.049	-0.049	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.008	-0.011	14.057	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.020	-0.001	11.298	-0.044	-0.044	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.852	-0.890	12.038	-0.504	-0.504	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.027	0.011	15.416	0.026	0.026	0.000	0.000	0.000	0.000
53	A	53	MET	0	-0.001	0.012	10.434	0.072	0.072	0.000	0.000	0.000	0.000
54	A	54	TYR	0	0.027	-0.014	7.942	0.062	0.062	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.001	0.002	13.949	0.098	0.098	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.045	0.031	15.858	0.062	0.062	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.023	-0.008	10.184	0.068	0.068	0.000	0.000	0.000	0.000
58	A	58	TYR	0	-0.026	-0.030	14.376	0.063	0.063	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.858	0.921	16.903	0.305	0.305	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.012	-0.048	15.985	0.042	0.042	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.024	-0.010	13.741	0.045	0.045	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.013	0.008	18.107	0.036	0.036	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.843	-0.920	21.556	-0.122	-0.122	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.042	-0.037	19.038	0.025	0.025	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.887	0.964	20.772	0.100	0.100	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.020	-0.015	22.570	0.009	0.009	0.000	0.000	0.000	0.000
67	A	67	ASN	0	-0.031	-0.009	25.396	0.019	0.019	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.855	0.903	25.404	0.081	0.081	0.000	0.000	0.000	0.000
69	A	69	MET	0	-0.036	0.026	19.784	-0.015	-0.015	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.874	0.926	23.126	0.113	0.113	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.068	-0.064	20.663	0.009	0.009	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.913	0.932	20.478	-0.038	-0.038	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.026	0.033	15.999	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.105	0.051	13.745	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.007	0.011	11.327	-0.110	-0.110	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.037	-0.044	13.876	-0.041	-0.041	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.770	-0.836	17.489	-0.128	-0.128	0.000	0.000	0.000	0.000
78	A	78	CYS	0	0.007	0.019	14.235	-0.045	-0.045	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.017	0.011	15.531	-0.034	-0.034	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.063	-0.049	17.518	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	81	CME	0	-0.089	-0.025	18.347	0.013	0.013	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.050	0.027	15.498	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.014	0.026	19.141	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.040	0.035	22.146	0.020	0.020	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.092	-0.072	24.742	0.025	0.025	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.051	0.012	26.196	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	87	ASN	0	0.002	0.021	27.189	0.015	0.015	0.000	0.000	0.000	0.000
88	A	88	ILE	0	0.077	0.039	20.072	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.026	-0.024	23.227	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.779	-0.855	25.023	-0.153	-0.153	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.014	0.011	21.419	-0.014	-0.014	0.000	0.000	0.000	0.000
92	A	92	PHE	0	0.021	-0.010	16.900	-0.022	-0.022	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.046	-0.009	21.211	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.858	0.916	23.069	0.154	0.154	0.000	0.000	0.000	0.000
95	A	95	PHE	0	0.061	0.020	17.991	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.023	0.022	17.101	-0.044	-0.044	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.036	-0.004	14.532	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.798	0.863	17.558	0.302	0.302	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.800	-0.891	19.769	-0.079	-0.079	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.788	-0.860	21.891	-0.211	-0.211	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.003	0.008	16.541	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.002	0.006	16.651	0.006	0.006	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.017	-0.004	12.811	0.023	0.023	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.073	-0.034	9.486	0.105	0.105	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.048	0.038	8.141	-0.206	-0.206	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.049	-0.019	6.236	0.367	0.367	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.014	0.008	6.275	-0.322	-0.322	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.844	0.921	6.154	-0.269	-0.269	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.030	0.009	6.993	-0.198	-0.198	0.000	0.000	0.000	0.000
110	A	110	HIS	0	-0.036	-0.034	4.342	0.170	0.245	-0.001	-0.004	-0.070	0.000
111	A	111	THR	0	0.013	-0.015	9.408	-0.085	-0.085	0.000	0.000	0.000	0.000
112	A	112	ASN	0	0.003	0.010	12.115	-0.047	-0.047	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.032	-0.005	7.705	0.017	0.017	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.824	-0.904	10.821	0.422	0.422	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.861	-0.929	8.868	0.370	0.370	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.047	-0.013	3.103	-0.302	0.047	0.046	-0.084	-0.311	-0.001
117	A	117	ASP	-1	-0.795	-0.884	5.843	2.827	2.827	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.907	0.923	2.273	-5.901	-4.678	3.165	-1.079	-3.310	0.005
119	A	119	GLU	-1	-0.779	-0.866	3.548	7.503	7.594	0.711	0.664	-1.465	-0.010
120	A	120	GLN	0	-0.035	-0.008	6.197	-0.775	-0.761	-0.001	-0.003	-0.009	0.000
121	A	121	LEU	0	-0.011	-0.011	2.471	-1.865	-0.979	1.140	-0.402	-1.624	-0.001
122	A	122	ARG	1	0.827	0.860	1.987	-11.252	-15.093	13.879	-4.848	-5.189	0.018
123	A	123	THR	0	-0.010	0.003	5.240	-1.298	-1.271	0.000	-0.015	-0.012	0.000
124	A	124	ILE	0	-0.015	0.008	8.295	-0.450	-0.450	0.000	0.000	0.000	0.000
125	A	125	MET	0	-0.020	-0.020	2.524	-1.520	-1.794	2.608	-0.513	-1.821	0.002
126	A	126	THR	0	-0.016	-0.023	7.260	-0.487	-0.487	0.000	0.000	0.000	0.000
127	A	127	SER	0	-0.041	-0.017	9.476	-0.199	-0.199	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.050	-0.017	11.188	-0.144	-0.144	0.000	0.000	0.000	0.000
129	A	129	VAL	0	-0.024	-0.014	9.229	-0.111	-0.111	0.000	0.000	0.000	0.000
130	A	130	LYS	1	0.832	0.915	11.364	-0.197	-0.197	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.015	-0.005	11.998	-0.037	-0.037	0.000	0.000	0.000	0.000
132	A	132	GLN	0	-0.019	-0.001	10.038	0.105	0.105	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.789	-0.865	1.817	-14.098	-16.130	10.858	-4.860	-3.966	-0.064
134	A	134	ILE	0	-0.030	-0.015	5.922	0.271	0.271	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.861	-0.919	3.973	-3.288	-3.051	-0.001	-0.022	-0.214	0.000
136	A	136	PHE	0	-0.009	-0.011	3.955	0.828	1.015	0.000	-0.026	-0.161	0.000
137	A	137	ASN	0	0.003	-0.016	5.608	0.084	0.084	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.748	-0.892	9.011	-0.938	-0.938	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.848	-0.886	12.507	-0.656	-0.656	0.000	0.000	0.000	0.000
140	A	140	ASN	0	0.005	-0.010	8.313	0.377	0.377	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.038	-0.010	10.111	0.102	0.102	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.068	-0.051	12.817	0.144	0.144	0.000	0.000	0.000	0.000
143	A	143	ARG	1	0.796	0.885	12.368	0.914	0.914	0.000	0.000	0.000	0.000
144	A	144	PHE	0	-0.053	-0.034	11.996	0.066	0.066	0.000	0.000	0.000	0.000
145	A	145	TYR	0	-0.009	0.015	16.612	0.031	0.031	0.000	0.000	0.000	0.000
146	A	146	ASP	-1	-0.825	-0.918	18.329	-0.254	-0.254	0.000	0.000	0.000	0.000
147	A	147	GLU	-1	-0.778	-0.892	22.001	-0.278	-0.278	0.000	0.000	0.000	0.000
148	A	148	ALA	0	-0.017	0.005	24.256	0.020	0.020	0.000	0.000	0.000	0.000
149	A	149	LEU	0	0.015	-0.002	21.848	0.022	0.022	0.000	0.000	0.000	0.000
150	A	150	ILE	0	0.023	0.006	19.605	0.016	0.016	0.000	0.000	0.000	0.000
151	A	151	ARG	1	0.712	0.839	23.863	0.242	0.242	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.866	0.936	27.474	0.209	0.209	0.000	0.000	0.000	0.000
153	A	153	ILE	0	-0.037	-0.013	23.629	0.016	0.016	0.000	0.000	0.000	0.000
154	A	154	TYR	0	-0.021	-0.050	20.141	-0.005	-0.005	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.829	0.939	26.158	0.187	0.187	0.000	0.000	0.000	0.000
156	A	156	LEU	0	0.006	0.018	25.397	0.007	0.007	0.000	0.000	0.000	0.000
157	A	157	SER	0	0.011	-0.018	29.792	0.007	0.007	0.000	0.000	0.000	0.000
158	A	158	ASP	-1	-0.838	-0.927	32.505	-0.191	-0.191	0.000	0.000	0.000	0.000
159	A	159	ASP	-1	-0.906	-0.923	33.995	-0.150	-0.150	0.000	0.000	0.000	0.000
160	A	160	PHE	0	-0.030	-0.007	26.872	0.001	0.001	0.000	0.000	0.000	0.000
161	A	161	LYS	1	0.881	0.931	31.393	0.172	0.172	0.000	0.000	0.000	0.000
162	A	162	PRO	0	-0.008	0.017	26.394	0.005	0.005	0.000	0.000	0.000	0.000
163	A	163	GLN	0	0.000	-0.018	28.567	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	164	ASP	-1	-0.797	-0.885	23.366	-0.375	-0.375	0.000	0.000	0.000	0.000
165	A	165	VAL	0	0.040	0.028	18.320	0.009	0.009	0.000	0.000	0.000	0.000
166	A	166	ASN	0	-0.023	-0.025	20.209	-0.049	-0.049	0.000	0.000	0.000	0.000
167	A	167	GLY	0	-0.019	-0.014	21.825	0.008	0.008	0.000	0.000	0.000	0.000
168	A	168	LEU	0	-0.018	-0.016	21.528	0.017	0.017	0.000	0.000	0.000	0.000
169	A	169	SER	0	-0.009	-0.038	18.708	-0.012	-0.012	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.991	1.000	20.662	0.275	0.275	0.000	0.000	0.000	0.000
171	A	171	ALA	0	0.002	0.002	23.205	0.015	0.015	0.000	0.000	0.000	0.000
172	A	172	LEU	0	-0.028	-0.013	19.746	0.020	0.020	0.000	0.000	0.000	0.000
173	A	173	VAL	0	0.014	0.001	18.915	0.008	0.008	0.000	0.000	0.000	0.000
174	A	174	ASP	-1	-1.017	-0.999	21.474	-0.224	-0.224	0.000	0.000	0.000	0.000
175	A	175	ALA	0	0.011	0.002	24.673	0.014	0.014	0.000	0.000	0.000	0.000
176	A	176	ILE	0	-0.097	-0.029	18.829	0.016	0.016	0.000	0.000	0.000	0.000
177	A	177	GLN	0	-0.028	-0.003	22.578	0.021	0.021	0.000	0.000	0.000	0.000

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