FMO DATABASE

FMODB ID: R9148

Calculation Name: 5X7V-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5X7V

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y010

Base Structure: X-ray

Registration Date: 2023-06-21

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	OptHSide
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	-1909656.527408
FMO2-HF: Nuclear repulsion	1835680.77439
FMO2-HF: Total energy	-73975.753018
FMO2-MP2: Total energy	-74192.230471

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:29:PHE)

Summations of interaction energy for fragment #1(A:29: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.
-23.81	-16.334	10.249	-8.307	-9.417	-0.051

Interaction energy analysis for fragmet #1(A:29:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.014 / q_NPA : -0.011

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	31	GLN	0	-0.014	-0.008	2.249	-5.616	-2.952	1.962	-1.687	-2.939	0.007
4	A	32	ASP	-1	-0.852	-0.938	2.306	-19.010	-14.927	8.279	-6.474	-5.888	-0.058
5	A	33	PHE	0	-0.028	-0.010	3.713	0.659	1.388	0.008	-0.146	-0.590	0.000
6	A	34	GLU	-1	-0.897	-0.952	5.856	0.699	0.699	0.000	0.000	0.000	0.000
7	A	35	ASP	-1	-0.867	-0.914	6.912	-1.213	-1.213	0.000	0.000	0.000	0.000
8	A	36	ILE	0	-0.010	0.002	7.033	0.212	0.212	0.000	0.000	0.000	0.000
9	A	37	GLN	0	-0.051	-0.039	9.613	0.130	0.130	0.000	0.000	0.000	0.000
10	A	38	LYS	1	0.836	0.908	9.147	0.646	0.646	0.000	0.000	0.000	0.000
11	A	39	ASP	-1	-0.925	-0.962	12.786	-0.708	-0.708	0.000	0.000	0.000	0.000
12	A	40	ILE	0	-0.046	-0.018	11.566	0.060	0.060	0.000	0.000	0.000	0.000
13	A	41	GLU	-1	-0.804	-0.890	15.390	-0.092	-0.092	0.000	0.000	0.000	0.000
14	A	42	GLN	0	-0.028	-0.023	16.573	0.075	0.075	0.000	0.000	0.000	0.000
15	A	43	LEU	0	-0.067	-0.032	17.164	0.032	0.032	0.000	0.000	0.000	0.000
16	A	44	ASP	-1	-0.852	-0.924	18.944	-0.205	-0.205	0.000	0.000	0.000	0.000
17	A	45	ILE	0	-0.060	-0.032	20.689	0.028	0.028	0.000	0.000	0.000	0.000
18	A	46	LYS	1	0.871	0.925	21.164	0.303	0.303	0.000	0.000	0.000	0.000
19	A	47	CYS	0	0.009	0.023	23.957	0.012	0.012	0.000	0.000	0.000	0.000
20	A	48	ALA	0	0.032	0.006	25.558	0.016	0.016	0.000	0.000	0.000	0.000
21	A	49	HIS	0	-0.056	-0.020	27.455	0.011	0.011	0.000	0.000	0.000	0.000
22	A	50	GLU	-1	-0.895	-0.950	28.934	-0.147	-0.147	0.000	0.000	0.000	0.000
23	A	51	GLN	0	0.002	-0.012	27.521	0.010	0.010	0.000	0.000	0.000	0.000
24	A	52	MET	0	0.036	0.027	31.518	0.012	0.012	0.000	0.000	0.000	0.000
25	A	53	ASN	0	-0.053	-0.017	33.432	0.013	0.013	0.000	0.000	0.000	0.000
26	A	54	ILE	0	-0.003	-0.012	34.583	0.006	0.006	0.000	0.000	0.000	0.000
27	A	55	GLN	0	0.011	0.002	34.593	0.008	0.008	0.000	0.000	0.000	0.000
28	A	56	LYS	1	0.958	0.969	36.837	0.064	0.064	0.000	0.000	0.000	0.000
29	A	57	GLN	0	0.042	0.031	39.263	0.006	0.006	0.000	0.000	0.000	0.000
30	A	58	TYR	0	-0.027	-0.034	39.568	0.006	0.006	0.000	0.000	0.000	0.000
31	A	59	ASP	-1	-0.807	-0.882	40.256	-0.042	-0.042	0.000	0.000	0.000	0.000
32	A	60	GLU	-1	-0.944	-0.981	42.773	-0.042	-0.042	0.000	0.000	0.000	0.000
33	A	61	LYS	1	0.827	0.925	42.722	0.064	0.064	0.000	0.000	0.000	0.000
34	A	62	LYS	1	0.866	0.920	40.197	0.049	0.049	0.000	0.000	0.000	0.000
35	A	63	LYS	1	0.959	0.995	47.038	0.034	0.034	0.000	0.000	0.000	0.000
36	A	64	PRO	0	0.034	0.011	49.266	0.002	0.002	0.000	0.000	0.000	0.000
37	A	65	LEU	0	0.011	0.014	48.124	0.002	0.002	0.000	0.000	0.000	0.000
38	A	66	PHE	0	0.007	-0.009	45.017	0.002	0.002	0.000	0.000	0.000	0.000
39	A	67	GLU	-1	-0.837	-0.915	51.157	-0.019	-0.019	0.000	0.000	0.000	0.000
40	A	68	LYS	1	0.777	0.879	54.463	0.024	0.024	0.000	0.000	0.000	0.000
41	A	69	ARG	1	0.835	0.908	49.001	0.021	0.021	0.000	0.000	0.000	0.000
42	A	70	ASP	-1	-0.726	-0.857	53.860	-0.016	-0.016	0.000	0.000	0.000	0.000
43	A	71	GLU	-1	-0.817	-0.885	56.446	-0.020	-0.020	0.000	0.000	0.000	0.000
44	A	72	ILE	0	-0.070	-0.048	56.804	0.001	0.001	0.000	0.000	0.000	0.000
45	A	73	ILE	0	-0.008	0.012	54.076	0.001	0.001	0.000	0.000	0.000	0.000
46	A	74	GLN	0	-0.001	0.001	58.717	0.001	0.001	0.000	0.000	0.000	0.000
47	A	75	LYS	1	0.854	0.940	61.884	0.018	0.018	0.000	0.000	0.000	0.000
48	A	76	ILE	0	-0.022	0.000	58.937	0.000	0.000	0.000	0.000	0.000	0.000
49	A	77	PRO	0	-0.009	-0.020	61.806	0.001	0.001	0.000	0.000	0.000	0.000
50	A	78	GLY	0	0.063	0.042	62.189	0.000	0.000	0.000	0.000	0.000	0.000
51	A	79	PHE	0	0.016	0.016	53.883	0.001	0.001	0.000	0.000	0.000	0.000
52	A	80	TRP	0	0.096	0.035	51.102	0.000	0.000	0.000	0.000	0.000	0.000
53	A	81	ALA	0	0.013	0.027	55.817	0.001	0.001	0.000	0.000	0.000	0.000
54	A	82	ASN	0	-0.037	-0.038	57.233	0.002	0.002	0.000	0.000	0.000	0.000
55	A	83	THR	0	-0.023	-0.010	51.852	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	84	LEU	0	0.009	-0.009	50.990	0.000	0.000	0.000	0.000	0.000	0.000
57	A	85	ARG	1	0.941	0.978	51.666	0.001	0.001	0.000	0.000	0.000	0.000
58	A	86	LYS	1	0.823	0.900	52.854	0.008	0.008	0.000	0.000	0.000	0.000
59	A	87	HIS	0	-0.001	-0.010	44.202	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	88	PRO	0	0.031	0.008	46.688	0.002	0.002	0.000	0.000	0.000	0.000
61	A	89	ALA	0	-0.017	0.005	45.625	0.001	0.001	0.000	0.000	0.000	0.000
62	A	90	LEU	0	-0.040	-0.036	47.783	0.001	0.001	0.000	0.000	0.000	0.000
63	A	91	SER	0	-0.036	-0.001	51.005	0.000	0.000	0.000	0.000	0.000	0.000
64	A	92	ASP	-1	-0.915	-0.954	52.841	0.009	0.009	0.000	0.000	0.000	0.000
65	A	93	ILE	0	-0.033	0.002	53.495	0.001	0.001	0.000	0.000	0.000	0.000
66	A	94	VAL	0	-0.030	-0.014	55.988	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	95	PRO	0	0.011	-0.010	59.529	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	96	GLU	-1	-0.812	-0.919	62.206	0.007	0.007	0.000	0.000	0.000	0.000
69	A	97	ASP	-1	-0.730	-0.837	57.070	0.006	0.006	0.000	0.000	0.000	0.000
70	A	98	ILE	0	-0.048	-0.041	59.771	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	99	ASP	-1	-0.897	-0.935	61.530	0.001	0.001	0.000	0.000	0.000	0.000
72	A	100	ILE	0	-0.028	-0.009	61.305	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	101	LEU	0	0.033	0.008	56.272	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	102	ASN	0	-0.049	-0.021	60.163	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	103	HIS	0	-0.110	-0.056	62.686	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	104	LEU	0	-0.021	0.002	55.294	0.000	0.000	0.000	0.000	0.000	0.000
77	A	105	VAL	0	-0.060	-0.036	59.786	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	106	LYS	1	0.726	0.825	54.698	0.015	0.015	0.000	0.000	0.000	0.000
79	A	107	LEU	0	0.034	0.032	50.304	0.001	0.001	0.000	0.000	0.000	0.000
80	A	108	ASP	-1	-0.809	-0.883	50.934	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	109	LEU	0	0.037	0.020	43.103	0.002	0.002	0.000	0.000	0.000	0.000
82	A	110	LYS	1	0.760	0.872	46.294	0.017	0.017	0.000	0.000	0.000	0.000
83	A	111	ASP	-1	-0.716	-0.889	40.447	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	112	ASN	0	-0.097	-0.040	38.110	0.000	0.000	0.000	0.000	0.000	0.000
85	A	113	MET	0	-0.069	-0.005	39.620	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	114	ASP	-1	-0.823	-0.870	36.332	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	115	ASN	0	-0.087	-0.051	31.250	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	116	ASN	0	0.027	-0.011	32.111	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	117	GLY	0	0.009	0.027	34.054	0.005	0.005	0.000	0.000	0.000	0.000
90	A	118	SER	0	-0.014	-0.046	36.223	0.005	0.005	0.000	0.000	0.000	0.000
91	A	119	TYR	0	0.011	-0.012	39.628	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	120	LYS	1	0.864	0.931	42.945	0.010	0.010	0.000	0.000	0.000	0.000
93	A	121	ILE	0	-0.022	0.007	45.600	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	122	THR	0	-0.045	-0.023	48.956	0.002	0.002	0.000	0.000	0.000	0.000
95	A	123	PHE	0	0.007	0.001	51.015	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	124	ILE	0	0.000	0.000	55.515	0.001	0.001	0.000	0.000	0.000	0.000
97	A	125	PHE	0	0.006	-0.012	57.949	0.000	0.000	0.000	0.000	0.000	0.000
98	A	126	GLY	0	0.024	0.004	61.879	0.000	0.000	0.000	0.000	0.000	0.000
99	A	127	GLU	-1	-0.746	-0.878	65.226	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	128	LYS	1	0.954	0.977	68.411	0.004	0.004	0.000	0.000	0.000	0.000
101	A	129	ALA	0	0.041	0.036	64.377	0.001	0.001	0.000	0.000	0.000	0.000
102	A	130	LYS	1	0.818	0.890	66.477	0.003	0.003	0.000	0.000	0.000	0.000
103	A	131	GLU	-1	-0.932	-0.937	68.595	0.002	0.002	0.000	0.000	0.000	0.000
104	A	132	PHE	0	0.064	0.012	65.530	0.001	0.001	0.000	0.000	0.000	0.000
105	A	133	MET	0	-0.043	-0.005	60.273	0.001	0.001	0.000	0.000	0.000	0.000
106	A	134	GLU	-1	-0.906	-0.922	64.089	0.001	0.001	0.000	0.000	0.000	0.000
107	A	135	PRO	0	0.018	0.003	60.421	0.001	0.001	0.000	0.000	0.000	0.000
108	A	136	LEU	0	0.005	-0.008	61.936	0.000	0.000	0.000	0.000	0.000	0.000
109	A	137	THR	0	0.019	0.009	57.090	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	138	LEU	0	-0.031	-0.008	55.688	0.001	0.001	0.000	0.000	0.000	0.000
111	A	139	VAL	0	0.003	-0.007	52.055	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	140	LYS	1	0.920	0.969	46.629	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	141	HIS	0	-0.114	-0.068	44.537	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	142	VAL	0	0.008	0.011	41.190	0.002	0.002	0.000	0.000	0.000	0.000
115	A	143	THR	0	-0.002	-0.007	38.990	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	144	PHE	0	0.050	0.015	35.167	0.003	0.003	0.000	0.000	0.000	0.000
117	A	145	ASP	-1	-0.867	-0.894	33.849	0.035	0.035	0.000	0.000	0.000	0.000
118	A	146	ASN	0	-0.025	-0.028	29.573	0.004	0.004	0.000	0.000	0.000	0.000
119	A	147	ASN	0	-0.074	-0.041	28.420	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	148	GLN	0	-0.002	0.009	32.729	0.003	0.003	0.000	0.000	0.000	0.000
121	A	149	GLU	-1	-0.922	-0.966	35.847	0.011	0.011	0.000	0.000	0.000	0.000
122	A	150	LYS	1	0.847	0.902	37.190	-0.033	-0.033	0.000	0.000	0.000	0.000
123	A	151	VAL	0	0.018	0.015	41.643	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	152	VAL	0	-0.025	0.003	43.176	0.001	0.001	0.000	0.000	0.000	0.000
125	A	153	GLU	-1	-0.834	-0.916	45.989	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	154	CYS	0	0.035	-0.003	49.471	0.000	0.000	0.000	0.000	0.000	0.000
127	A	155	THR	0	-0.047	0.013	52.043	0.000	0.000	0.000	0.000	0.000	0.000
128	A	156	ARG	1	0.897	0.962	54.956	-0.010	-0.010	0.000	0.000	0.000	0.000
129	A	157	ILE	0	0.000	-0.004	56.664	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	158	LYS	1	0.843	0.906	59.905	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	159	TRP	0	0.027	0.001	59.023	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	160	LYS	1	0.867	0.939	64.807	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	161	GLU	-1	-0.870	-0.950	68.140	0.009	0.009	0.000	0.000	0.000	0.000
134	A	162	GLY	0	-0.034	-0.015	69.543	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	163	LYS	1	0.810	0.900	67.452	-0.004	-0.004	0.000	0.000	0.000	0.000
136	A	164	ASN	0	0.012	0.005	61.225	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	165	PRO	0	0.058	0.039	60.257	0.001	0.001	0.000	0.000	0.000	0.000
138	A	166	ILE	0	-0.041	-0.026	56.945	0.001	0.001	0.000	0.000	0.000	0.000
139	A	167	ALA	0	-0.065	-0.024	59.705	0.001	0.001	0.000	0.000	0.000	0.000
140	A	168	ALA	0	0.002	0.014	60.771	0.000	0.000	0.000	0.000	0.000	0.000
141	A	181	PRO	0	0.015	-0.006	53.749	0.000	0.000	0.000	0.000	0.000	0.000
142	A	182	LYS	1	0.783	0.891	54.902	-0.010	-0.010	0.000	0.000	0.000	0.000
143	A	183	TRP	0	0.035	0.032	49.762	0.001	0.001	0.000	0.000	0.000	0.000
144	A	184	SER	0	-0.006	-0.040	54.865	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	185	ILE	0	0.043	0.017	52.016	0.001	0.001	0.000	0.000	0.000	0.000
146	A	186	PHE	0	-0.061	-0.040	53.013	0.000	0.000	0.000	0.000	0.000	0.000
147	A	187	GLU	-1	-0.827	-0.914	52.765	0.017	0.017	0.000	0.000	0.000	0.000
148	A	188	TRP	0	-0.019	-0.004	45.885	0.000	0.000	0.000	0.000	0.000	0.000
149	A	189	PHE	0	-0.050	-0.022	49.884	0.000	0.000	0.000	0.000	0.000	0.000
150	A	190	THR	0	-0.020	-0.033	49.326	0.000	0.000	0.000	0.000	0.000	0.000
151	A	191	THR	0	-0.006	-0.020	47.840	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	192	ASP	-1	-0.924	-0.930	46.905	0.024	0.024	0.000	0.000	0.000	0.000
153	A	193	GLU	-1	-0.842	-0.923	41.183	0.032	0.032	0.000	0.000	0.000	0.000
154	A	194	LEU	0	-0.061	-0.036	44.169	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	195	GLN	0	-0.043	-0.033	40.644	0.001	0.001	0.000	0.000	0.000	0.000
156	A	196	ASP	-1	-0.918	-0.952	42.930	0.034	0.034	0.000	0.000	0.000	0.000
157	A	197	LYS	1	0.850	0.913	44.857	-0.022	-0.022	0.000	0.000	0.000	0.000
158	A	198	PRO	0	-0.004	-0.003	45.074	0.000	0.000	0.000	0.000	0.000	0.000
159	A	199	ASP	-1	-0.716	-0.858	42.199	0.008	0.008	0.000	0.000	0.000	0.000
160	A	200	VAL	0	-0.020	-0.020	44.443	-0.002	-0.002	0.000	0.000	0.000	0.000
161	A	201	GLY	0	0.001	-0.005	44.949	-0.003	-0.003	0.000	0.000	0.000	0.000
162	A	202	GLU	-1	-0.731	-0.848	37.775	-0.005	-0.005	0.000	0.000	0.000	0.000
163	A	203	LEU	0	-0.028	0.000	41.674	-0.003	-0.003	0.000	0.000	0.000	0.000
164	A	204	ILE	0	-0.014	-0.009	43.622	-0.003	-0.003	0.000	0.000	0.000	0.000
165	A	205	ARG	1	0.788	0.888	36.335	0.010	0.010	0.000	0.000	0.000	0.000
166	A	206	ARG	1	0.836	0.911	35.308	-0.002	-0.002	0.000	0.000	0.000	0.000
167	A	207	GLU	-1	-0.881	-0.934	40.241	-0.005	-0.005	0.000	0.000	0.000	0.000
168	A	208	ILE	0	-0.058	-0.021	42.684	-0.002	-0.002	0.000	0.000	0.000	0.000
169	A	209	TRP	0	-0.007	0.006	44.422	0.000	0.000	0.000	0.000	0.000	0.000
170	A	210	HIS	0	-0.014	-0.011	42.880	-0.001	-0.001	0.000	0.000	0.000	0.000
171	A	211	ASN	0	-0.024	-0.029	45.022	0.000	0.000	0.000	0.000	0.000	0.000
172	A	212	PRO	0	0.069	0.048	47.577	0.001	0.001	0.000	0.000	0.000	0.000
173	A	213	LEU	0	0.012	0.007	50.292	0.002	0.002	0.000	0.000	0.000	0.000
174	A	214	SER	0	0.020	0.002	47.221	0.001	0.001	0.000	0.000	0.000	0.000
175	A	215	TYR	0	0.033	0.070	44.712	0.001	0.001	0.000	0.000	0.000	0.000
176	A	216	TYR	0	-0.002	0.008	51.283	0.001	0.001	0.000	0.000	0.000	0.000
177	A	217	LEU	0	-0.089	-0.067	52.332	0.002	0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:29:PHE)