FMO DATABASE

FMODB ID: G63Z1

Calculation Name: 3EVZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EVZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q8U2I7

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:

Apendix: None

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	198
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2337510.868104
FMO2-HF: Nuclear repulsion	2260121.313473
FMO2-HF: Total energy	-77389.554631
FMO2-MP2: Total energy	-77619.588612

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:34:PHE)

Summations of interaction energy for fragment #1(A:34:PHE)

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.
-16.87	-9.22	6.704	-4.558	-9.796	0.035

Interaction energy analysis for fragmet #1(A:34:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.053 / q_NPA : 0.002

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	36	ASN	0	0.054	0.021	2.366	-7.018	-3.107	4.834	-3.257	-5.488	0.027
4	A	37	ARG	1	0.844	0.914	2.199	-5.068	-2.661	1.828	-1.072	-3.163	0.008
5	A	38	GLN	0	0.042	0.041	4.023	-1.172	-0.561	0.006	-0.098	-0.518	0.000
6	A	39	ALA	0	0.060	0.046	6.212	-0.113	-0.113	0.000	0.000	0.000	0.000
7	A	40	ARG	1	0.971	0.989	3.049	-2.451	-1.849	0.037	-0.124	-0.516	0.000
8	A	41	ILE	0	-0.016	0.007	7.026	-0.134	-0.134	0.000	0.000	0.000	0.000
9	A	42	LEU	0	0.041	0.020	9.683	-0.063	-0.063	0.000	0.000	0.000	0.000
10	A	43	TYR	0	-0.016	-0.002	11.642	-0.050	-0.050	0.000	0.000	0.000	0.000
11	A	44	ASN	0	-0.001	-0.047	11.152	-0.090	-0.090	0.000	0.000	0.000	0.000
12	A	45	LYS	1	0.942	1.000	13.336	-0.196	-0.196	0.000	0.000	0.000	0.000
13	A	46	ALA	0	0.016	0.013	15.594	-0.026	-0.026	0.000	0.000	0.000	0.000
14	A	47	ILE	0	-0.012	-0.002	17.029	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	48	ALA	0	-0.019	-0.019	18.075	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	49	LYS	1	0.998	0.999	19.804	-0.135	-0.135	0.000	0.000	0.000	0.000
17	A	50	ALA	0	-0.038	-0.010	21.599	-0.011	-0.011	0.000	0.000	0.000	0.000
18	A	51	LEU	0	-0.017	-0.015	22.017	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	52	PHE	0	0.004	0.002	21.367	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	53	GLY	0	0.009	0.015	24.867	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	54	LEU	0	-0.049	-0.025	21.755	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	55	ASP	-1	-0.957	-0.968	19.034	0.131	0.131	0.000	0.000	0.000	0.000
23	A	56	ILE	0	0.003	-0.005	15.508	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	57	GLU	-1	-0.836	-0.917	14.326	0.102	0.102	0.000	0.000	0.000	0.000
25	A	58	TYR	0	-0.066	-0.050	10.364	0.004	0.004	0.000	0.000	0.000	0.000
26	A	59	HIS	0	0.127	0.080	10.408	-0.036	-0.036	0.000	0.000	0.000	0.000
27	A	60	PRO	0	0.027	0.006	6.134	-0.024	-0.024	0.000	0.000	0.000	0.000
28	A	61	LYS	1	0.834	0.887	4.387	0.165	0.284	-0.001	-0.007	-0.111	0.000
29	A	62	GLY	0	0.090	0.069	8.344	0.068	0.068	0.000	0.000	0.000	0.000
30	A	63	LEU	0	-0.024	-0.021	9.258	0.054	0.054	0.000	0.000	0.000	0.000
31	A	64	VAL	0	-0.025	-0.017	7.326	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	65	THR	0	0.012	0.005	10.389	0.023	0.023	0.000	0.000	0.000	0.000
33	A	66	THR	0	0.019	0.011	12.907	0.005	0.005	0.000	0.000	0.000	0.000
34	A	67	PRO	0	0.024	0.023	15.237	-0.021	-0.021	0.000	0.000	0.000	0.000
35	A	68	ILE	0	0.077	0.037	18.667	-0.014	-0.014	0.000	0.000	0.000	0.000
36	A	69	SER	0	0.006	-0.034	18.243	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	70	ARG	1	0.913	0.968	16.475	-0.176	-0.176	0.000	0.000	0.000	0.000
38	A	71	TYR	0	0.065	0.042	21.491	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	72	ILE	0	-0.022	-0.015	23.627	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	73	PHE	0	-0.040	-0.026	23.634	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	74	LEU	0	0.055	0.035	25.442	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	75	LYS	1	0.957	0.989	27.714	-0.074	-0.074	0.000	0.000	0.000	0.000
43	A	76	THR	0	-0.048	0.035	28.538	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	77	PHE	0	-0.035	-0.040	27.858	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	78	LEU	0	-0.022	0.009	29.659	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	79	ARG	1	0.741	0.837	33.130	-0.052	-0.052	0.000	0.000	0.000	0.000
47	A	80	GLY	0	-0.015	-0.002	35.968	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	81	GLY	0	-0.016	-0.002	36.788	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	82	GLU	-1	-0.790	-0.887	35.093	0.048	0.048	0.000	0.000	0.000	0.000
50	A	83	VAL	0	0.002	0.006	35.966	0.002	0.002	0.000	0.000	0.000	0.000
51	A	84	ALA	0	-0.015	-0.028	31.552	0.000	0.000	0.000	0.000	0.000	0.000
52	A	85	LEU	0	0.006	0.016	30.170	0.000	0.000	0.000	0.000	0.000	0.000
53	A	86	GLU	-1	-0.824	-0.954	22.898	0.089	0.089	0.000	0.000	0.000	0.000
54	A	87	ILE	0	-0.021	-0.022	25.652	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	88	GLY	0	-0.008	0.011	22.575	0.006	0.006	0.000	0.000	0.000	0.000
56	A	89	THR	0	-0.013	0.005	21.224	0.007	0.007	0.000	0.000	0.000	0.000
57	A	90	GLY	0	-0.030	-0.013	17.886	0.013	0.013	0.000	0.000	0.000	0.000
58	A	91	HIS	0	-0.034	-0.015	11.782	-0.022	-0.022	0.000	0.000	0.000	0.000
59	A	92	THR	0	-0.043	-0.016	15.167	0.007	0.007	0.000	0.000	0.000	0.000
60	A	93	ALA	0	0.092	0.046	17.253	0.000	0.000	0.000	0.000	0.000	0.000
61	A	94	MET	0	-0.021	-0.023	17.362	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	95	MET	0	-0.049	-0.025	20.844	0.002	0.002	0.000	0.000	0.000	0.000
63	A	96	ALA	0	0.076	0.049	23.621	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	97	LEU	0	0.036	0.022	21.784	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	98	MET	0	-0.092	-0.040	22.028	0.001	0.001	0.000	0.000	0.000	0.000
66	A	99	ALA	0	0.021	0.002	26.229	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	100	GLU	-1	-0.756	-0.846	28.908	0.057	0.057	0.000	0.000	0.000	0.000
68	A	101	LYS	1	0.863	0.950	27.030	-0.087	-0.087	0.000	0.000	0.000	0.000
69	A	102	PHE	0	-0.076	-0.052	26.652	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	103	PHE	0	-0.035	-0.021	28.585	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	104	ASN	0	0.024	0.023	33.242	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	105	CYS	0	-0.029	0.018	32.298	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	106	LYS	1	0.994	1.000	33.738	-0.037	-0.037	0.000	0.000	0.000	0.000
74	A	107	VAL	0	-0.017	-0.007	28.467	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	108	THR	0	-0.013	-0.004	30.882	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	109	ALA	0	-0.012	0.009	25.561	0.002	0.002	0.000	0.000	0.000	0.000
77	A	110	THR	0	0.056	0.036	26.438	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	111	GLU	-1	-0.839	-0.931	19.726	0.069	0.069	0.000	0.000	0.000	0.000
79	A	112	VAL	0	0.016	0.006	21.500	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	113	ASP	-1	-0.836	-0.890	17.021	0.019	0.019	0.000	0.000	0.000	0.000
81	A	114	GLU	-1	-0.877	-0.954	19.805	0.023	0.023	0.000	0.000	0.000	0.000
82	A	115	GLU	-1	-0.901	-0.950	14.349	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	116	PHE	0	-0.119	-0.092	12.527	0.011	0.011	0.000	0.000	0.000	0.000
84	A	117	PHE	0	0.030	-0.001	17.069	0.008	0.008	0.000	0.000	0.000	0.000
85	A	118	GLU	-1	-0.765	-0.864	18.288	0.053	0.053	0.000	0.000	0.000	0.000
86	A	119	TYR	0	-0.020	-0.016	12.229	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	120	ALA	0	0.012	0.025	17.708	0.007	0.007	0.000	0.000	0.000	0.000
88	A	121	ARG	1	0.879	0.929	20.368	-0.048	-0.048	0.000	0.000	0.000	0.000
89	A	122	ARG	1	0.859	0.938	15.796	-0.061	-0.061	0.000	0.000	0.000	0.000
90	A	123	ASN	0	-0.038	-0.027	16.529	0.010	0.010	0.000	0.000	0.000	0.000
91	A	124	ILE	0	0.018	0.010	20.768	0.003	0.003	0.000	0.000	0.000	0.000
92	A	125	GLU	-1	-0.911	-0.954	24.364	0.057	0.057	0.000	0.000	0.000	0.000
93	A	126	ARG	1	0.802	0.890	18.059	-0.094	-0.094	0.000	0.000	0.000	0.000
94	A	127	ASN	0	-0.104	-0.069	21.627	0.006	0.006	0.000	0.000	0.000	0.000
95	A	128	ASN	0	-0.033	-0.005	25.555	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	129	SER	0	-0.065	-0.058	27.004	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	130	ASN	0	0.003	-0.006	29.082	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	131	VAL	0	-0.090	-0.035	26.694	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	132	ARG	1	0.986	0.990	29.499	-0.037	-0.037	0.000	0.000	0.000	0.000
100	A	133	LEU	0	0.026	0.000	23.355	0.001	0.001	0.000	0.000	0.000	0.000
101	A	134	VAL	0	-0.066	-0.027	27.638	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	135	LYS	1	0.924	0.962	23.203	-0.026	-0.026	0.000	0.000	0.000	0.000
103	A	136	SER	0	-0.013	0.000	26.042	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	137	ASN	0	-0.003	-0.015	26.263	0.001	0.001	0.000	0.000	0.000	0.000
105	A	138	GLY	0	0.010	-0.011	26.546	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	139	GLY	0	-0.002	0.021	27.615	0.001	0.001	0.000	0.000	0.000	0.000
107	A	140	ILE	0	-0.053	-0.025	28.309	0.003	0.003	0.000	0.000	0.000	0.000
108	A	141	ILE	0	0.010	-0.022	29.574	0.003	0.003	0.000	0.000	0.000	0.000
109	A	142	LYS	1	0.927	0.970	32.583	-0.026	-0.026	0.000	0.000	0.000	0.000
110	A	143	GLY	0	0.014	0.011	34.224	0.000	0.000	0.000	0.000	0.000	0.000
111	A	144	VAL	0	-0.114	-0.033	29.602	0.000	0.000	0.000	0.000	0.000	0.000
112	A	145	VAL	0	-0.030	-0.025	31.715	0.001	0.001	0.000	0.000	0.000	0.000
113	A	146	GLU	-1	-0.892	-0.955	34.498	0.023	0.023	0.000	0.000	0.000	0.000
114	A	147	GLY	0	-0.028	-0.006	37.783	0.001	0.001	0.000	0.000	0.000	0.000
115	A	148	THR	0	-0.043	-0.030	39.092	0.000	0.000	0.000	0.000	0.000	0.000
116	A	149	PHE	0	-0.039	-0.024	34.911	0.001	0.001	0.000	0.000	0.000	0.000
117	A	150	ASP	-1	-0.778	-0.864	37.434	0.036	0.036	0.000	0.000	0.000	0.000
118	A	151	VAL	0	-0.081	-0.046	31.912	0.001	0.001	0.000	0.000	0.000	0.000
119	A	152	ILE	0	0.048	0.047	30.907	0.001	0.001	0.000	0.000	0.000	0.000
120	A	153	PHE	0	-0.006	-0.016	25.899	0.001	0.001	0.000	0.000	0.000	0.000
121	A	154	SER	0	0.017	-0.006	24.506	0.000	0.000	0.000	0.000	0.000	0.000
122	A	155	ALA	0	-0.030	-0.014	19.829	0.002	0.002	0.000	0.000	0.000	0.000
123	A	156	PRO	0	0.013	0.021	20.464	0.005	0.005	0.000	0.000	0.000	0.000
124	A	157	PRO	0	0.039	0.005	18.609	0.010	0.010	0.000	0.000	0.000	0.000
125	A	158	TYR	0	-0.055	-0.034	15.728	0.022	0.022	0.000	0.000	0.000	0.000
126	A	159	TYR	0	0.033	0.030	14.302	0.002	0.002	0.000	0.000	0.000	0.000
127	A	175	GLY	0	0.076	0.047	24.560	0.001	0.001	0.000	0.000	0.000	0.000
128	A	176	GLY	0	-0.013	-0.013	25.541	0.003	0.003	0.000	0.000	0.000	0.000
129	A	177	LYS	1	0.924	0.957	27.042	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	178	TYR	0	-0.061	-0.057	26.151	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	179	GLY	0	0.026	0.027	23.567	0.006	0.006	0.000	0.000	0.000	0.000
132	A	180	GLU	-1	-0.854	-0.955	24.494	0.036	0.036	0.000	0.000	0.000	0.000
133	A	181	GLU	-1	-0.881	-0.938	27.223	0.026	0.026	0.000	0.000	0.000	0.000
134	A	182	PHE	0	0.004	-0.004	25.222	0.000	0.000	0.000	0.000	0.000	0.000
135	A	183	SER	0	0.034	0.012	26.130	0.001	0.001	0.000	0.000	0.000	0.000
136	A	184	VAL	0	0.010	-0.001	28.173	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	185	LYS	1	0.970	0.993	28.451	-0.032	-0.032	0.000	0.000	0.000	0.000
138	A	186	LEU	0	0.021	0.021	28.022	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	187	LEU	0	-0.039	-0.026	31.256	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	188	GLU	-1	-0.920	-0.960	33.662	0.022	0.022	0.000	0.000	0.000	0.000
141	A	189	GLU	-1	-0.850	-0.921	33.316	0.029	0.029	0.000	0.000	0.000	0.000
142	A	190	ALA	0	0.002	-0.011	33.745	0.000	0.000	0.000	0.000	0.000	0.000
143	A	191	PHE	0	0.052	0.038	35.725	0.000	0.000	0.000	0.000	0.000	0.000
144	A	192	ASP	-1	-0.871	-0.928	39.101	0.022	0.022	0.000	0.000	0.000	0.000
145	A	193	HIS	0	-0.079	-0.036	37.013	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	194	LEU	0	-0.053	-0.014	35.914	0.002	0.002	0.000	0.000	0.000	0.000
147	A	195	ASN	0	0.050	0.019	39.698	-0.004	-0.004	0.000	0.000	0.000	0.000
148	A	196	PRO	0	0.036	0.013	41.964	0.001	0.001	0.000	0.000	0.000	0.000
149	A	197	GLY	0	-0.056	-0.035	42.624	0.001	0.001	0.000	0.000	0.000	0.000
150	A	198	GLY	0	-0.002	0.012	39.059	0.002	0.002	0.000	0.000	0.000	0.000
151	A	199	LYS	1	0.873	0.926	34.540	-0.045	-0.045	0.000	0.000	0.000	0.000
152	A	200	VAL	0	0.073	0.043	30.709	0.001	0.001	0.000	0.000	0.000	0.000
153	A	201	ALA	0	-0.027	-0.006	29.297	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	202	LEU	0	0.019	-0.002	26.147	0.003	0.003	0.000	0.000	0.000	0.000
155	A	203	TYR	0	-0.037	-0.012	18.267	0.010	0.010	0.000	0.000	0.000	0.000
156	A	204	LEU	0	0.018	-0.011	22.040	0.005	0.005	0.000	0.000	0.000	0.000
157	A	205	PRO	0	-0.073	-0.037	18.970	0.005	0.005	0.000	0.000	0.000	0.000
158	A	206	ASP	-1	-0.815	-0.917	20.818	0.064	0.064	0.000	0.000	0.000	0.000
159	A	207	LYS	1	0.887	0.948	18.093	-0.095	-0.095	0.000	0.000	0.000	0.000
160	A	208	GLU	-1	-0.842	-0.912	23.739	0.029	0.029	0.000	0.000	0.000	0.000
161	A	209	LYS	1	0.985	0.974	27.324	-0.018	-0.018	0.000	0.000	0.000	0.000
162	A	210	LEU	0	0.007	0.006	23.049	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	211	LEU	0	-0.021	-0.011	25.454	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	212	ASN	0	0.003	-0.003	28.487	0.000	0.000	0.000	0.000	0.000	0.000
165	A	213	VAL	0	0.013	0.020	30.354	-0.002	-0.002	0.000	0.000	0.000	0.000
166	A	214	ILE	0	-0.006	0.002	26.813	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	215	LYS	1	0.901	0.956	31.225	-0.041	-0.041	0.000	0.000	0.000	0.000
168	A	216	GLU	-1	-0.895	-0.948	33.679	0.025	0.025	0.000	0.000	0.000	0.000
169	A	217	ARG	1	0.861	0.936	33.774	-0.025	-0.025	0.000	0.000	0.000	0.000
170	A	218	GLY	0	0.055	0.025	34.950	-0.001	-0.001	0.000	0.000	0.000	0.000
171	A	219	ILE	0	0.016	0.003	36.103	-0.001	-0.001	0.000	0.000	0.000	0.000
172	A	220	LYS	1	0.889	0.938	39.088	-0.020	-0.020	0.000	0.000	0.000	0.000
173	A	221	LEU	0	-0.002	0.014	36.302	-0.001	-0.001	0.000	0.000	0.000	0.000
174	A	222	GLY	0	0.013	0.024	40.264	0.000	0.000	0.000	0.000	0.000	0.000
175	A	223	TYR	0	-0.096	-0.053	36.566	0.001	0.001	0.000	0.000	0.000	0.000
176	A	224	SER	0	0.035	0.027	39.718	0.000	0.000	0.000	0.000	0.000	0.000
177	A	225	VAL	0	-0.016	-0.026	33.799	0.002	0.002	0.000	0.000	0.000	0.000
178	A	226	LYS	1	0.925	0.984	34.545	-0.045	-0.045	0.000	0.000	0.000	0.000
179	A	227	ASP	-1	-0.803	-0.899	29.565	0.056	0.056	0.000	0.000	0.000	0.000
180	A	228	ILE	0	0.017	0.027	29.141	-0.002	-0.002	0.000	0.000	0.000	0.000
181	A	229	LYS	1	0.972	0.997	25.566	-0.053	-0.053	0.000	0.000	0.000	0.000
182	A	230	PHE	0	0.016	-0.007	22.370	-0.001	-0.001	0.000	0.000	0.000	0.000
183	A	231	LYS	1	0.852	0.978	18.160	-0.108	-0.108	0.000	0.000	0.000	0.000
184	A	232	VAL	0	0.002	0.030	20.408	0.000	0.000	0.000	0.000	0.000	0.000
185	A	233	GLY	0	0.092	0.022	17.047	0.006	0.006	0.000	0.000	0.000	0.000
186	A	234	THR	0	0.131	0.099	11.769	-0.006	-0.006	0.000	0.000	0.000	0.000
187	A	235	ARG	1	0.768	0.820	15.202	-0.133	-0.133	0.000	0.000	0.000	0.000
188	A	236	TRP	0	0.003	-0.012	18.107	0.007	0.007	0.000	0.000	0.000	0.000
189	A	237	ARG	1	0.884	0.951	16.279	-0.148	-0.148	0.000	0.000	0.000	0.000
190	A	238	HIS	0	0.016	-0.010	22.091	-0.005	-0.005	0.000	0.000	0.000	0.000
191	A	239	SER	0	-0.064	-0.061	24.791	0.005	0.005	0.000	0.000	0.000	0.000
192	A	240	LEU	0	-0.010	0.008	27.282	-0.004	-0.004	0.000	0.000	0.000	0.000
193	A	241	ILE	0	0.004	-0.010	29.803	0.002	0.002	0.000	0.000	0.000	0.000
194	A	242	PHE	0	0.035	0.012	30.931	-0.002	-0.002	0.000	0.000	0.000	0.000
195	A	243	PHE	0	-0.035	-0.044	35.217	0.002	0.002	0.000	0.000	0.000	0.000
196	A	244	LYS	1	0.886	0.950	38.562	-0.028	-0.028	0.000	0.000	0.000	0.000
197	A	245	GLY	0	-0.018	-0.003	40.864	-0.001	-0.001	0.000	0.000	0.000	0.000
198	A	246	ILE	0	0.069	0.036	43.687	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:34:PHE)