FMO DATABASE

FMODB ID: M9NRZ

Calculation Name: 1YW5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1YW5

Chain ID: A

ChEMBL ID:

UniProt ID: Q59KZ2

Base Structure: X-ray

Registration Date: 2023-09-27

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	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1821512.440852
FMO2-HF: Nuclear repulsion	1752250.713507
FMO2-HF: Total energy	-69261.727345
FMO2-MP2: Total energy	-69466.158089

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.
-0.144	1.334	0	-0.644	-0.834	0.002

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 : 0.038 / q_NPA : 0.010

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	SER	0	0.068	0.035	3.817	-1.324	0.079	0.001	-0.637	-0.767	0.002
4	A	4	THR	0	-0.013	-0.013	5.992	0.291	0.291	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.019	-0.012	8.819	0.111	0.111	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.072	0.021	9.892	0.023	0.023	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.041	0.015	12.444	0.035	0.035	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.031	0.001	12.957	0.002	0.002	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.004	0.019	16.659	-0.010	-0.010	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.026	-0.010	19.155	0.001	0.001	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.010	0.002	20.949	0.002	0.002	0.000	0.000	0.000	0.000
12	A	12	TRP	0	-0.015	0.014	20.371	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.030	-0.023	19.163	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	ILE	0	0.006	0.002	15.018	0.001	0.001	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.795	0.896	19.519	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.039	0.019	20.717	0.001	0.001	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.005	0.005	23.262	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.959	0.959	26.576	-0.025	-0.025	0.000	0.000	0.000	0.000
19	A	19	SER	0	0.021	0.006	29.077	0.001	0.001	0.000	0.000	0.000	0.000
20	A	20	HIS	0	-0.008	-0.001	27.508	0.000	0.000	0.000	0.000	0.000	0.000
21	A	21	ASN	0	-0.046	-0.022	22.585	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.983	1.002	22.343	-0.012	-0.012	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.885	-0.944	17.681	0.033	0.033	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.028	-0.010	21.011	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.002	-0.016	17.207	0.003	0.003	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.007	0.001	22.050	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	27	ASN	0	0.047	0.040	23.692	0.000	0.000	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.001	-0.041	24.312	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.042	-0.017	27.277	0.000	0.000	0.000	0.000	0.000	0.000
30	A	30	THR	0	0.001	-0.008	29.275	0.000	0.000	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.049	-0.027	29.652	0.001	0.001	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.932	-0.955	28.464	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.033	-0.029	26.738	0.002	0.002	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.008	-0.019	24.123	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	35	TRP	0	-0.016	-0.017	23.711	0.003	0.003	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.875	-0.921	22.131	0.006	0.006	0.000	0.000	0.000	0.000
37	A	37	PRO	0	-0.033	-0.020	18.014	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.034	0.045	19.666	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.039	0.018	20.554	0.003	0.003	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.005	-0.008	19.878	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.012	-0.025	15.476	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.948	-0.967	11.075	0.173	0.173	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.979	0.950	12.493	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.951	-0.952	7.280	0.218	0.218	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.005	0.005	7.785	0.114	0.114	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.034	0.022	9.061	-0.051	-0.051	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.034	-0.020	10.917	-0.039	-0.039	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.008	0.002	5.830	-0.037	-0.037	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.033	-0.044	7.972	-0.079	-0.079	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.013	-0.008	9.556	-0.016	-0.016	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.039	-0.015	9.740	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.961	0.973	4.423	-0.194	-0.119	-0.001	-0.007	-0.067	0.000
53	A	53	PHE	0	0.012	0.014	10.607	0.004	0.004	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.907	0.946	13.557	-0.044	-0.044	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.045	-0.007	12.635	-0.017	-0.017	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.054	-0.018	13.295	0.031	0.031	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.020	-0.018	15.297	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	58	TYR	0	-0.020	-0.011	17.525	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.961	0.992	17.115	-0.090	-0.090	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.021	0.010	15.373	0.006	0.006	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.030	0.008	8.875	0.019	0.019	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.014	0.007	12.337	-0.039	-0.039	0.000	0.000	0.000	0.000
63	A	63	ASN	0	0.035	0.009	8.990	0.027	0.027	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.896	-0.952	6.604	0.539	0.539	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.906	-0.937	8.798	0.468	0.468	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.080	-0.049	12.024	-0.067	-0.067	0.000	0.000	0.000	0.000
67	A	67	GLN	0	-0.077	-0.055	13.218	-0.053	-0.053	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.010	-0.006	13.443	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.846	0.908	14.817	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.009	0.002	16.793	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.009	0.003	19.934	0.001	0.001	0.000	0.000	0.000	0.000
72	A	72	HIS	0	0.011	-0.048	22.750	0.001	0.001	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.019	0.025	26.232	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.062	-0.028	29.812	0.001	0.001	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.021	0.027	32.331	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.808	0.898	35.567	-0.025	-0.025	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.030	-0.012	38.083	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.032	-0.018	41.570	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	GLN	0	0.016	0.026	42.295	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.057	-0.012	38.136	0.001	0.001	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.961	0.948	34.402	-0.039	-0.039	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.910	0.962	36.538	-0.031	-0.031	0.000	0.000	0.000	0.000
83	A	83	PRO	0	0.097	0.059	39.264	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	LYS	1	1.020	1.006	40.156	-0.024	-0.024	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.084	-0.067	37.057	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	TRP	0	0.023	-0.004	34.702	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.981	1.014	37.277	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.072	-0.037	40.083	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	89	PRO	0	0.010	0.005	42.420	0.001	0.001	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.901	-0.946	43.305	0.015	0.015	0.000	0.000	0.000	0.000
91	A	91	GLY	0	-0.049	-0.015	44.648	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.077	-0.034	39.789	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	SER	0	0.015	-0.009	44.167	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.880	0.962	39.698	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	95	THR	0	0.050	0.009	44.552	0.001	0.001	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.899	0.924	40.165	-0.021	-0.021	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.864	-0.918	41.723	0.015	0.015	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.853	-0.920	43.109	0.012	0.012	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.073	-0.056	38.872	0.000	0.000	0.000	0.000	0.000	0.000
100	A	100	ILE	0	0.018	0.009	38.368	0.000	0.000	0.000	0.000	0.000	0.000
101	A	101	GLN	0	-0.003	-0.009	38.849	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	102	ILE	0	-0.016	0.001	37.963	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.002	0.002	32.666	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.960	0.975	35.135	-0.012	-0.012	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.968	0.992	36.457	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	106	HIS	0	0.038	0.015	33.431	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.003	-0.011	29.942	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.952	-0.972	32.191	0.006	0.006	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.922	0.966	34.071	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.054	-0.018	27.804	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.038	-0.025	28.057	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	112	SER	0	0.011	0.022	30.175	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	113	GLY	0	-0.009	0.001	29.695	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.919	-0.952	30.685	0.000	0.000	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.023	-0.008	31.243	0.000	0.000	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.975	0.994	23.379	0.012	0.012	0.000	0.000	0.000	0.000
117	A	117	LEU	0	0.056	0.025	25.167	0.001	0.001	0.000	0.000	0.000	0.000
118	A	118	SER	0	0.013	-0.004	24.561	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.955	-0.977	26.643	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	120	LEU	0	0.024	0.010	29.925	0.001	0.001	0.000	0.000	0.000	0.000
121	A	121	ALA	0	-0.015	-0.016	28.529	0.002	0.002	0.000	0.000	0.000	0.000
122	A	122	ASN	0	0.008	0.005	30.464	0.003	0.003	0.000	0.000	0.000	0.000
123	A	123	THR	0	-0.049	-0.045	31.654	0.001	0.001	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.886	-0.930	34.275	0.010	0.010	0.000	0.000	0.000	0.000
125	A	125	SER	0	-0.004	0.013	30.404	0.002	0.002	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.797	-0.893	33.272	0.017	0.017	0.000	0.000	0.000	0.000
127	A	127	CYM	-1	-0.861	-0.819	29.588	0.032	0.032	0.000	0.000	0.000	0.000
128	A	128	SER	0	-0.041	-0.034	30.107	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	129	SER	0	0.033	-0.058	26.171	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	130	HIS	1	0.843	0.922	27.578	-0.017	-0.017	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.928	-0.946	29.435	0.017	0.017	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.886	0.933	21.032	-0.029	-0.029	0.000	0.000	0.000	0.000
133	A	133	GLY	0	0.003	0.007	24.254	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	134	GLY	0	0.049	0.017	24.973	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	135	ASP	-1	-0.845	-0.889	19.848	0.029	0.029	0.000	0.000	0.000	0.000
136	A	136	LEU	0	-0.012	-0.014	21.811	0.003	0.003	0.000	0.000	0.000	0.000
137	A	137	GLY	0	-0.023	-0.002	18.540	0.007	0.007	0.000	0.000	0.000	0.000
138	A	138	PHE	0	-0.009	-0.028	11.716	-0.010	-0.010	0.000	0.000	0.000	0.000
139	A	139	PHE	0	0.024	0.021	16.918	0.004	0.004	0.000	0.000	0.000	0.000
140	A	140	SER	0	0.056	0.032	17.904	0.004	0.004	0.000	0.000	0.000	0.000
141	A	141	LYS	1	0.903	0.948	18.955	-0.139	-0.139	0.000	0.000	0.000	0.000
142	A	142	GLY	0	-0.011	-0.019	21.917	0.007	0.007	0.000	0.000	0.000	0.000
143	A	143	GLN	0	-0.030	-0.006	22.174	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	144	MET	0	-0.017	0.001	23.045	-0.008	-0.008	0.000	0.000	0.000	0.000
145	A	145	GLN	0	0.000	-0.030	26.239	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	146	PRO	0	0.083	0.028	27.972	0.000	0.000	0.000	0.000	0.000	0.000
147	A	147	PRO	0	0.039	0.016	28.085	0.002	0.002	0.000	0.000	0.000	0.000
148	A	148	PHE	0	0.011	0.011	23.587	-0.002	-0.002	0.000	0.000	0.000	0.000
149	A	149	GLU	-1	-0.856	-0.910	22.965	0.086	0.086	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.892	-0.953	23.353	0.056	0.056	0.000	0.000	0.000	0.000
151	A	151	ALA	0	-0.003	-0.002	24.300	0.000	0.000	0.000	0.000	0.000	0.000
152	A	152	ALA	0	0.031	0.007	20.831	-0.002	-0.002	0.000	0.000	0.000	0.000
153	A	153	PHE	0	-0.062	-0.048	17.234	0.000	0.000	0.000	0.000	0.000	0.000
154	A	154	ASN	0	-0.077	-0.033	19.419	0.006	0.006	0.000	0.000	0.000	0.000
155	A	155	LEU	0	-0.042	0.010	19.997	-0.005	-0.005	0.000	0.000	0.000	0.000
156	A	156	HIS	0	0.050	0.059	16.214	0.002	0.002	0.000	0.000	0.000	0.000
157	A	157	VAL	0	-0.026	-0.028	12.579	0.005	0.005	0.000	0.000	0.000	0.000
158	A	158	GLY	0	-0.013	-0.010	15.790	-0.002	-0.002	0.000	0.000	0.000	0.000
159	A	159	GLU	-1	-0.816	-0.878	18.542	0.024	0.024	0.000	0.000	0.000	0.000
160	A	160	VAL	0	-0.018	-0.019	21.302	0.001	0.001	0.000	0.000	0.000	0.000
161	A	161	SER	0	-0.005	0.000	24.460	0.001	0.001	0.000	0.000	0.000	0.000
162	A	162	ASN	0	0.021	0.007	26.467	-0.004	-0.004	0.000	0.000	0.000	0.000
163	A	163	ILE	0	0.016	-0.005	29.759	0.001	0.001	0.000	0.000	0.000	0.000
164	A	164	ILE	0	-0.007	0.013	28.008	0.001	0.001	0.000	0.000	0.000	0.000
165	A	165	GLU	-1	-0.822	-0.895	31.443	0.023	0.023	0.000	0.000	0.000	0.000
166	A	166	THR	0	-0.035	-0.044	30.533	0.003	0.003	0.000	0.000	0.000	0.000
167	A	167	ASN	0	0.000	-0.003	33.839	-0.003	-0.003	0.000	0.000	0.000	0.000
168	A	168	SER	0	-0.033	-0.018	33.004	0.000	0.000	0.000	0.000	0.000	0.000
169	A	169	GLY	0	0.014	0.021	35.221	-0.002	-0.002	0.000	0.000	0.000	0.000
170	A	170	VAL	0	0.001	0.016	34.230	0.001	0.001	0.000	0.000	0.000	0.000
171	A	171	HIS	0	0.012	-0.002	29.327	0.000	0.000	0.000	0.000	0.000	0.000
172	A	172	ILE	0	0.012	0.035	27.471	0.000	0.000	0.000	0.000	0.000	0.000
173	A	173	LEU	0	-0.003	-0.013	23.448	0.000	0.000	0.000	0.000	0.000	0.000
174	A	174	GLN	0	0.057	0.033	20.296	0.001	0.001	0.000	0.000	0.000	0.000
175	A	175	ARG	1	0.789	0.880	13.003	-0.024	-0.024	0.000	0.000	0.000	0.000
176	A	176	THR	0	-0.014	-0.018	16.555	-0.006	-0.006	0.000	0.000	0.000	0.000
177	A	177	GLY	0	0.031	0.064	12.078	-0.030	-0.030	0.000	0.000	0.000	0.000

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