FMO DATABASE

FMODB ID: 9G392

Calculation Name: 2DOK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2DOK

Chain ID: A

ChEMBL ID:

UniProt ID: Q86US8

Base Structure: X-ray

Registration Date: 2023-06-20

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1865378.443663
FMO2-HF: Nuclear repulsion	1794915.032785
FMO2-HF: Total energy	-70463.410878
FMO2-MP2: Total energy	-70669.058738

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:GLY)

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

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.
-0.718	0.489	0.034	-0.601	-0.639	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.010 / q_NPA : -0.004

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	PRO	0	-0.032	-0.032	3.489	-1.465	-0.253	0.035	-0.599	-0.648	0.001
4	A	4	GLU	-1	-0.913	-0.944	5.334	-0.010	-0.010	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.064	-0.027	6.852	0.033	0.033	0.000	0.000	0.000	0.000
6	A	6	MET	0	-0.015	0.003	10.030	0.050	0.050	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.833	-0.903	12.086	0.389	0.389	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.019	-0.016	14.806	-0.018	-0.018	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.841	-0.909	18.420	0.179	0.179	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.044	-0.027	20.244	-0.019	-0.019	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.835	0.897	23.125	-0.101	-0.101	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.056	-0.027	26.390	-0.007	-0.007	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.034	0.034	29.570	0.001	0.001	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.017	-0.001	30.810	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.018	-0.010	32.102	0.002	0.002	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.037	0.017	33.268	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.004	0.009	35.169	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.765	-0.861	37.631	0.012	0.012	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.019	-0.041	39.418	0.002	0.002	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.035	-0.026	41.474	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.001	-0.004	40.707	0.001	0.001	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.005	-0.007	41.494	0.002	0.002	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.030	-0.010	44.841	0.000	0.000	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.860	-0.931	44.419	0.013	0.013	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.032	-0.013	40.667	0.002	0.002	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.038	0.035	44.195	0.002	0.002	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.012	-0.002	46.081	0.001	0.001	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.006	-0.006	41.924	0.001	0.001	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.003	0.005	39.820	0.002	0.002	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.010	0.010	42.669	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.940	0.955	44.276	-0.031	-0.031	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.028	-0.009	37.713	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.001	0.029	40.938	0.002	0.002	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.884	-0.950	42.909	0.028	0.028	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.099	-0.062	40.272	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.776	0.852	41.710	-0.028	-0.028	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.863	0.934	36.494	-0.054	-0.054	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.006	-0.003	33.185	0.004	0.004	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.008	-0.004	35.414	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.014	0.003	36.514	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.006	-0.016	36.159	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.028	0.006	37.852	0.000	0.000	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.035	0.006	37.161	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.014	-0.007	39.749	0.000	0.000	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.035	0.017	39.947	0.000	0.000	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.004	0.005	40.136	0.000	0.000	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.016	-0.008	43.208	0.001	0.001	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.029	0.009	46.089	0.000	0.000	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.817	-0.865	43.189	0.002	0.002	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.038	-0.016	45.817	0.000	0.000	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.732	-0.834	48.953	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.015	0.015	50.899	0.000	0.000	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.045	-0.031	48.071	0.000	0.000	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.007	0.005	52.372	0.000	0.000	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.815	0.906	54.743	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	63	ALA	0	0.030	0.000	59.659	0.000	0.000	0.000	0.000	0.000	0.000
57	A	64	GLY	0	0.023	0.015	61.593	0.000	0.000	0.000	0.000	0.000	0.000
58	A	65	GLY	0	0.022	0.002	59.824	0.000	0.000	0.000	0.000	0.000	0.000
59	A	66	TYR	0	0.063	0.020	49.356	0.000	0.000	0.000	0.000	0.000	0.000
60	A	67	ALA	0	0.044	0.028	55.254	0.000	0.000	0.000	0.000	0.000	0.000
61	A	68	ARG	1	0.948	0.972	56.336	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.016	-0.005	53.480	0.001	0.001	0.000	0.000	0.000	0.000
63	A	70	VAL	0	0.040	0.021	50.074	0.001	0.001	0.000	0.000	0.000	0.000
64	A	71	GLN	0	0.049	0.042	52.426	0.000	0.000	0.000	0.000	0.000	0.000
65	A	72	GLU	-1	-0.910	-0.950	54.967	0.012	0.012	0.000	0.000	0.000	0.000
66	A	73	LYS	1	0.848	0.907	49.023	-0.013	-0.013	0.000	0.000	0.000	0.000
67	A	74	ALA	0	0.006	0.013	50.360	0.001	0.001	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.847	0.923	51.427	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	76	LYS	1	0.898	0.947	52.873	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.022	-0.019	47.937	0.001	0.001	0.000	0.000	0.000	0.000
71	A	78	ILE	0	-0.011	0.002	49.331	0.001	0.001	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.902	-0.963	51.219	0.011	0.011	0.000	0.000	0.000	0.000
73	A	80	PHE	0	-0.014	-0.009	45.734	0.001	0.001	0.000	0.000	0.000	0.000
74	A	81	LEU	0	0.008	0.001	44.989	0.001	0.001	0.000	0.000	0.000	0.000
75	A	82	GLU	-1	-0.811	-0.898	48.896	0.009	0.009	0.000	0.000	0.000	0.000
76	A	83	GLN	0	0.045	0.025	51.843	0.001	0.001	0.000	0.000	0.000	0.000
77	A	84	ARG	1	0.772	0.891	47.550	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	85	PHE	0	0.020	-0.004	44.427	0.001	0.001	0.000	0.000	0.000	0.000
79	A	86	GLU	-1	-0.961	-0.973	49.540	0.011	0.011	0.000	0.000	0.000	0.000
80	A	87	SER	0	-0.087	-0.051	51.170	0.000	0.000	0.000	0.000	0.000	0.000
81	A	88	ARG	1	0.810	0.902	48.424	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	89	ASP	-1	-0.729	-0.840	45.449	0.026	0.026	0.000	0.000	0.000	0.000
83	A	90	SER	0	0.025	0.007	43.806	0.000	0.000	0.000	0.000	0.000	0.000
84	A	91	CYS	0	-0.063	-0.001	40.340	0.001	0.001	0.000	0.000	0.000	0.000
85	A	92	LEU	0	-0.030	-0.011	40.938	0.001	0.001	0.000	0.000	0.000	0.000
86	A	93	ARG	1	0.878	0.917	36.922	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.019	0.021	41.505	0.000	0.000	0.000	0.000	0.000	0.000
88	A	95	LEU	0	-0.050	-0.014	34.901	0.000	0.000	0.000	0.000	0.000	0.000
89	A	96	THR	0	-0.028	-0.024	39.501	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	97	SER	0	-0.020	-0.049	37.638	0.000	0.000	0.000	0.000	0.000	0.000
91	A	98	ARG	1	0.861	0.921	36.386	0.001	0.001	0.000	0.000	0.000	0.000
92	A	99	GLY	0	0.037	0.026	35.859	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.067	-0.021	36.571	0.000	0.000	0.000	0.000	0.000	0.000
94	A	101	GLU	-1	-0.718	-0.819	36.445	0.018	0.018	0.000	0.000	0.000	0.000
95	A	102	LEU	0	-0.040	-0.020	40.544	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	103	GLU	-1	-0.819	-0.905	44.123	0.015	0.015	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.040	-0.031	46.178	0.001	0.001	0.000	0.000	0.000	0.000
98	A	105	ILE	0	0.049	0.024	46.768	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	106	ALA	0	0.035	0.035	49.561	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	107	PHE	0	-0.056	-0.042	52.611	0.000	0.000	0.000	0.000	0.000	0.000
101	A	108	ARG	1	0.682	0.802	49.060	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	109	SER	0	-0.011	-0.014	48.560	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	110	GLU	-1	-0.868	-0.932	47.902	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	111	ASP	-1	-0.797	-0.865	41.217	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	112	ILE	0	0.006	0.008	42.157	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	113	THR	0	0.072	0.028	40.755	0.000	0.000	0.000	0.000	0.000	0.000
107	A	114	GLY	0	-0.059	-0.016	40.646	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	115	GLN	0	-0.036	-0.029	35.205	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	116	LEU	0	0.005	0.008	30.478	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	117	GLY	0	-0.008	-0.002	35.077	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	118	ASN	0	-0.067	-0.033	35.976	0.003	0.003	0.000	0.000	0.000	0.000
112	A	119	ASN	0	0.048	-0.001	37.833	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	120	ASP	-1	-0.804	-0.886	34.923	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	121	ASP	-1	-0.844	-0.927	32.751	-0.017	-0.017	0.000	0.000	0.000	0.000
115	A	122	LEU	0	0.025	0.025	33.920	0.001	0.001	0.000	0.000	0.000	0.000
116	A	123	ILE	0	0.024	0.017	34.542	0.002	0.002	0.000	0.000	0.000	0.000
117	A	124	LEU	0	-0.014	-0.011	28.893	0.003	0.003	0.000	0.000	0.000	0.000
118	A	125	SER	0	-0.010	-0.019	30.753	0.001	0.001	0.000	0.000	0.000	0.000
119	A	126	CYS	0	-0.063	-0.023	32.285	0.002	0.002	0.000	0.000	0.000	0.000
120	A	127	CYS	0	-0.030	-0.010	29.445	0.004	0.004	0.000	0.000	0.000	0.000
121	A	128	LEU	0	0.029	-0.016	25.896	0.004	0.004	0.000	0.000	0.000	0.000
122	A	129	HIS	0	-0.023	0.007	28.402	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	130	TYR	0	-0.039	-0.063	29.385	0.000	0.000	0.000	0.000	0.000	0.000
124	A	131	CYS	0	-0.068	-0.015	24.020	0.005	0.005	0.000	0.000	0.000	0.000
125	A	132	LYS	1	0.885	0.961	24.307	-0.010	-0.010	0.000	0.000	0.000	0.000
126	A	133	ASP	-1	-0.751	-0.829	19.993	0.028	0.028	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.745	0.844	21.126	-0.034	-0.034	0.000	0.000	0.000	0.000
128	A	135	ALA	0	0.035	0.005	18.678	0.004	0.004	0.000	0.000	0.000	0.000
129	A	136	LYS	1	0.951	0.964	17.114	-0.022	-0.022	0.000	0.000	0.000	0.000
130	A	137	ASP	-1	-0.771	-0.866	16.882	0.042	0.042	0.000	0.000	0.000	0.000
131	A	138	PHE	0	-0.018	-0.011	13.452	0.021	0.021	0.000	0.000	0.000	0.000
132	A	139	MET	0	-0.047	-0.020	11.524	-0.022	-0.022	0.000	0.000	0.000	0.000
133	A	140	PRO	0	0.001	0.027	8.769	0.000	0.000	0.000	0.000	0.000	0.000
134	A	141	ALA	0	-0.048	-0.047	11.878	-0.039	-0.039	0.000	0.000	0.000	0.000
135	A	142	SER	0	-0.102	-0.064	12.534	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	143	LYS	1	0.828	0.873	8.888	-0.507	-0.507	0.000	0.000	0.000	0.000
137	A	144	GLU	-1	-0.877	-0.922	4.776	0.616	0.611	-0.001	-0.002	0.009	0.000
138	A	145	GLU	-1	-0.774	-0.836	7.121	0.637	0.637	0.000	0.000	0.000	0.000
139	A	146	PRO	0	-0.003	-0.001	8.464	-0.042	-0.042	0.000	0.000	0.000	0.000
140	A	147	ILE	0	0.029	0.023	8.073	-0.067	-0.067	0.000	0.000	0.000	0.000
141	A	148	ARG	1	0.819	0.894	11.291	-0.337	-0.337	0.000	0.000	0.000	0.000
142	A	149	LEU	0	0.018	0.022	14.782	-0.013	-0.013	0.000	0.000	0.000	0.000
143	A	150	LEU	0	-0.047	-0.017	17.885	0.009	0.009	0.000	0.000	0.000	0.000
144	A	151	ARG	1	0.745	0.823	20.694	-0.049	-0.049	0.000	0.000	0.000	0.000
145	A	152	GLU	-1	-0.810	-0.903	23.849	0.074	0.074	0.000	0.000	0.000	0.000
146	A	153	VAL	0	-0.023	-0.004	26.995	-0.004	-0.004	0.000	0.000	0.000	0.000
147	A	154	VAL	0	-0.028	-0.018	27.653	0.004	0.004	0.000	0.000	0.000	0.000
148	A	155	LEU	0	0.009	0.010	29.828	-0.003	-0.003	0.000	0.000	0.000	0.000
149	A	156	LEU	0	-0.036	-0.030	31.824	0.003	0.003	0.000	0.000	0.000	0.000
150	A	157	THR	0	0.004	-0.034	33.019	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	158	ASP	-1	-0.821	-0.916	34.738	0.027	0.027	0.000	0.000	0.000	0.000
152	A	159	ASP	-1	-0.786	-0.868	36.358	0.003	0.003	0.000	0.000	0.000	0.000
153	A	160	ARG	1	0.826	0.895	33.264	-0.018	-0.018	0.000	0.000	0.000	0.000
154	A	161	ASN	0	-0.029	-0.044	32.128	-0.004	-0.004	0.000	0.000	0.000	0.000
155	A	162	LEU	0	0.026	0.012	31.874	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	163	ARG	1	0.974	0.995	27.362	-0.029	-0.029	0.000	0.000	0.000	0.000
157	A	164	VAL	0	-0.007	-0.003	27.382	0.002	0.002	0.000	0.000	0.000	0.000
158	A	165	LYS	1	0.868	0.936	26.957	0.007	0.007	0.000	0.000	0.000	0.000
159	A	166	ALA	0	0.023	0.011	27.247	-0.004	-0.004	0.000	0.000	0.000	0.000
160	A	167	LEU	0	-0.007	-0.008	23.594	0.001	0.001	0.000	0.000	0.000	0.000
161	A	168	THR	0	-0.047	-0.043	22.386	-0.002	-0.002	0.000	0.000	0.000	0.000
162	A	169	ARG	1	0.859	0.944	22.534	0.009	0.009	0.000	0.000	0.000	0.000
163	A	170	ASN	0	0.001	0.005	18.702	0.013	0.013	0.000	0.000	0.000	0.000
164	A	171	VAL	0	0.027	0.018	21.901	0.008	0.008	0.000	0.000	0.000	0.000
165	A	172	PRO	0	0.007	0.005	23.811	0.000	0.000	0.000	0.000	0.000	0.000
166	A	173	VAL	0	-0.016	-0.007	25.835	-0.006	-0.006	0.000	0.000	0.000	0.000
167	A	174	ARG	1	0.785	0.884	28.763	-0.047	-0.047	0.000	0.000	0.000	0.000
168	A	175	ASP	-1	-0.725	-0.832	31.525	0.038	0.038	0.000	0.000	0.000	0.000
169	A	176	ILE	0	0.050	0.020	35.156	0.004	0.004	0.000	0.000	0.000	0.000
170	A	177	PRO	0	0.024	0.011	37.693	0.002	0.002	0.000	0.000	0.000	0.000
171	A	178	ALA	0	0.010	0.016	33.903	0.003	0.003	0.000	0.000	0.000	0.000
172	A	179	PHE	0	0.007	0.005	31.200	0.005	0.005	0.000	0.000	0.000	0.000
173	A	180	LEU	0	0.009	0.000	34.678	0.003	0.003	0.000	0.000	0.000	0.000
174	A	181	THR	0	-0.042	-0.031	36.689	0.001	0.001	0.000	0.000	0.000	0.000
175	A	182	TRP	0	-0.028	-0.012	28.951	0.000	0.000	0.000	0.000	0.000	0.000
176	A	183	ALA	0	0.003	0.013	34.170	0.003	0.003	0.000	0.000	0.000	0.000
177	A	184	GLN	0	-0.095	-0.031	35.528	-0.003	-0.003	0.000	0.000	0.000	0.000

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