FMO DATABASE

FMODB ID: QY85Y

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	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	-1914146.951942
FMO2-HF: Nuclear repulsion	1840170.504697
FMO2-HF: Total energy	-73976.447246
FMO2-MP2: Total energy	-74192.929067

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.
-21.228	-18.555	12.133	-7.293	-7.513	-0.056

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 : -0.015 / q_NPA : -0.022

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	-0.022	-0.016	3.048	-3.248	-0.738	0.070	-1.115	-1.465	0.003
4	A	32	ASP	-1	-0.825	-0.914	1.909	-18.675	-19.400	12.060	-5.933	-5.403	-0.060
5	A	33	PHE	0	-0.031	-0.017	4.023	0.728	1.616	0.003	-0.245	-0.645	0.001
6	A	34	GLU	-1	-0.865	-0.929	5.993	0.335	0.335	0.000	0.000	0.000	0.000
7	A	35	ASP	-1	-0.854	-0.903	7.403	-1.156	-1.156	0.000	0.000	0.000	0.000
8	A	36	ILE	0	-0.014	-0.008	7.164	0.228	0.228	0.000	0.000	0.000	0.000
9	A	37	GLN	0	-0.052	-0.037	9.932	0.147	0.147	0.000	0.000	0.000	0.000
10	A	38	LYS	1	0.801	0.884	9.544	0.708	0.708	0.000	0.000	0.000	0.000
11	A	39	ASP	-1	-0.869	-0.942	13.089	-0.622	-0.622	0.000	0.000	0.000	0.000
12	A	40	ILE	0	-0.048	-0.015	11.578	0.058	0.058	0.000	0.000	0.000	0.000
13	A	41	GLU	-1	-0.814	-0.893	15.404	-0.149	-0.149	0.000	0.000	0.000	0.000
14	A	42	GLN	0	-0.067	-0.038	16.851	0.103	0.103	0.000	0.000	0.000	0.000
15	A	43	LEU	0	-0.057	-0.015	17.146	0.033	0.033	0.000	0.000	0.000	0.000
16	A	44	ASP	-1	-0.857	-0.926	18.765	-0.216	-0.216	0.000	0.000	0.000	0.000
17	A	45	ILE	0	-0.031	-0.019	21.081	0.030	0.030	0.000	0.000	0.000	0.000
18	A	46	LYS	1	0.814	0.904	21.638	0.313	0.313	0.000	0.000	0.000	0.000
19	A	47	CYS	0	0.012	0.003	24.177	0.018	0.018	0.000	0.000	0.000	0.000
20	A	48	ALA	0	0.039	0.016	25.538	0.017	0.017	0.000	0.000	0.000	0.000
21	A	49	HIS	0	-0.036	-0.010	27.389	0.011	0.011	0.000	0.000	0.000	0.000
22	A	50	GLU	-1	-0.914	-0.957	28.708	-0.151	-0.151	0.000	0.000	0.000	0.000
23	A	51	GLN	0	0.009	-0.005	27.301	0.009	0.009	0.000	0.000	0.000	0.000
24	A	52	MET	0	0.013	0.012	31.381	0.012	0.012	0.000	0.000	0.000	0.000
25	A	53	ASN	0	-0.052	-0.018	33.362	0.014	0.014	0.000	0.000	0.000	0.000
26	A	54	ILE	0	-0.020	-0.019	34.560	0.008	0.008	0.000	0.000	0.000	0.000
27	A	55	GLN	0	0.046	0.019	34.818	0.009	0.009	0.000	0.000	0.000	0.000
28	A	56	LYS	1	1.017	1.004	36.943	0.072	0.072	0.000	0.000	0.000	0.000
29	A	57	GLN	0	0.006	0.018	39.155	0.007	0.007	0.000	0.000	0.000	0.000
30	A	58	TYR	0	-0.025	-0.034	39.602	0.004	0.004	0.000	0.000	0.000	0.000
31	A	59	ASP	-1	-0.782	-0.872	40.434	-0.049	-0.049	0.000	0.000	0.000	0.000
32	A	60	GLU	-1	-0.862	-0.921	42.948	-0.043	-0.043	0.000	0.000	0.000	0.000
33	A	61	LYS	1	0.825	0.920	42.563	0.068	0.068	0.000	0.000	0.000	0.000
34	A	62	LYS	1	0.851	0.916	39.694	0.057	0.057	0.000	0.000	0.000	0.000
35	A	63	LYS	1	0.856	0.923	46.689	0.045	0.045	0.000	0.000	0.000	0.000
36	A	64	PRO	0	0.017	0.002	48.958	0.002	0.002	0.000	0.000	0.000	0.000
37	A	65	LEU	0	-0.005	0.005	48.070	0.002	0.002	0.000	0.000	0.000	0.000
38	A	66	PHE	0	0.018	0.009	44.602	0.002	0.002	0.000	0.000	0.000	0.000
39	A	67	GLU	-1	-0.792	-0.883	50.828	-0.024	-0.024	0.000	0.000	0.000	0.000
40	A	68	LYS	1	0.809	0.892	54.175	0.027	0.027	0.000	0.000	0.000	0.000
41	A	69	ARG	1	0.830	0.893	48.720	0.026	0.026	0.000	0.000	0.000	0.000
42	A	70	ASP	-1	-0.729	-0.847	53.607	-0.021	-0.021	0.000	0.000	0.000	0.000
43	A	71	GLU	-1	-0.803	-0.873	56.042	-0.022	-0.022	0.000	0.000	0.000	0.000
44	A	72	ILE	0	-0.046	-0.034	56.649	0.001	0.001	0.000	0.000	0.000	0.000
45	A	73	ILE	0	0.010	0.016	53.918	0.001	0.001	0.000	0.000	0.000	0.000
46	A	74	GLN	0	-0.033	-0.014	58.534	0.001	0.001	0.000	0.000	0.000	0.000
47	A	75	LYS	1	0.788	0.898	61.613	0.021	0.021	0.000	0.000	0.000	0.000
48	A	76	ILE	0	-0.014	0.004	58.503	0.000	0.000	0.000	0.000	0.000	0.000
49	A	77	PRO	0	-0.001	-0.013	61.683	0.000	0.000	0.000	0.000	0.000	0.000
50	A	78	GLY	0	0.055	0.030	61.991	0.000	0.000	0.000	0.000	0.000	0.000
51	A	79	PHE	0	0.009	0.015	53.664	0.001	0.001	0.000	0.000	0.000	0.000
52	A	80	TRP	0	0.088	0.036	51.008	0.000	0.000	0.000	0.000	0.000	0.000
53	A	81	ALA	0	0.028	0.025	55.319	0.001	0.001	0.000	0.000	0.000	0.000
54	A	82	ASN	0	-0.030	-0.035	56.646	0.002	0.002	0.000	0.000	0.000	0.000
55	A	83	THR	0	-0.014	-0.012	51.491	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	84	LEU	0	-0.005	-0.005	50.624	0.000	0.000	0.000	0.000	0.000	0.000
57	A	85	ARG	1	0.912	0.962	51.615	0.005	0.005	0.000	0.000	0.000	0.000
58	A	86	LYS	1	0.807	0.885	52.679	0.012	0.012	0.000	0.000	0.000	0.000
59	A	87	HIS	0	0.012	-0.007	43.818	0.000	0.000	0.000	0.000	0.000	0.000
60	A	88	PRO	0	-0.005	-0.011	46.743	0.001	0.001	0.000	0.000	0.000	0.000
61	A	89	ALA	0	-0.018	0.009	45.191	0.002	0.002	0.000	0.000	0.000	0.000
62	A	90	LEU	0	-0.027	-0.029	47.299	0.001	0.001	0.000	0.000	0.000	0.000
63	A	91	SER	0	-0.031	-0.015	50.730	0.000	0.000	0.000	0.000	0.000	0.000
64	A	92	ASP	-1	-0.908	-0.939	52.657	0.004	0.004	0.000	0.000	0.000	0.000
65	A	93	ILE	0	-0.007	0.017	53.241	0.001	0.001	0.000	0.000	0.000	0.000
66	A	94	VAL	0	0.004	-0.002	55.486	0.000	0.000	0.000	0.000	0.000	0.000
67	A	95	PRO	0	-0.018	-0.024	59.172	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	96	GLU	-1	-0.821	-0.925	61.867	0.002	0.002	0.000	0.000	0.000	0.000
69	A	97	ASP	-1	-0.708	-0.834	56.944	0.001	0.001	0.000	0.000	0.000	0.000
70	A	98	ILE	0	-0.040	-0.029	59.332	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	99	ASP	-1	-0.896	-0.929	61.238	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	100	ILE	0	-0.033	-0.006	60.857	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	101	LEU	0	0.016	-0.003	56.182	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	102	ASN	0	-0.045	-0.028	59.826	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	103	HIS	0	-0.090	-0.049	62.595	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	104	LEU	0	-0.023	0.002	55.146	0.000	0.000	0.000	0.000	0.000	0.000
77	A	105	VAL	0	-0.025	-0.019	59.225	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	106	LYS	1	0.732	0.824	54.370	0.020	0.020	0.000	0.000	0.000	0.000
79	A	107	LEU	0	0.015	0.015	50.691	0.001	0.001	0.000	0.000	0.000	0.000
80	A	108	ASP	-1	-0.812	-0.886	51.117	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	109	LEU	0	0.032	0.023	43.175	0.002	0.002	0.000	0.000	0.000	0.000
82	A	110	LYS	1	0.751	0.858	46.111	0.024	0.024	0.000	0.000	0.000	0.000
83	A	111	ASP	-1	-0.716	-0.861	40.096	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	112	ASN	0	-0.108	-0.064	37.917	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	113	MET	0	-0.067	-0.010	39.295	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	114	ASP	-1	-0.804	-0.850	36.694	-0.029	-0.029	0.000	0.000	0.000	0.000
87	A	115	ASN	0	-0.095	-0.067	31.191	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	116	ASN	0	0.017	-0.010	32.506	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	117	GLY	0	0.017	0.018	34.076	0.004	0.004	0.000	0.000	0.000	0.000
90	A	118	SER	0	-0.031	-0.047	36.082	0.005	0.005	0.000	0.000	0.000	0.000
91	A	119	TYR	0	-0.011	-0.004	39.454	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	120	LYS	1	0.845	0.905	42.667	0.019	0.019	0.000	0.000	0.000	0.000
93	A	121	ILE	0	-0.015	0.003	45.418	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	122	THR	0	-0.030	-0.011	48.772	0.002	0.002	0.000	0.000	0.000	0.000
95	A	123	PHE	0	0.022	0.007	50.598	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	124	ILE	0	-0.004	0.000	55.288	0.001	0.001	0.000	0.000	0.000	0.000
97	A	125	PHE	0	0.018	-0.003	57.555	0.000	0.000	0.000	0.000	0.000	0.000
98	A	126	GLY	0	0.014	0.003	61.792	0.000	0.000	0.000	0.000	0.000	0.000
99	A	127	GLU	-1	-0.776	-0.889	65.278	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	128	LYS	1	0.966	0.980	68.213	0.007	0.007	0.000	0.000	0.000	0.000
101	A	129	ALA	0	0.056	0.038	64.090	0.001	0.001	0.000	0.000	0.000	0.000
102	A	130	LYS	1	0.819	0.887	66.179	0.007	0.007	0.000	0.000	0.000	0.000
103	A	131	GLU	-1	-0.919	-0.938	68.375	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	132	PHE	0	0.040	0.007	65.259	0.001	0.001	0.000	0.000	0.000	0.000
105	A	133	MET	0	-0.026	-0.001	60.112	0.001	0.001	0.000	0.000	0.000	0.000
106	A	134	GLU	-1	-0.836	-0.892	63.537	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	135	PRO	0	0.015	0.006	60.314	0.001	0.001	0.000	0.000	0.000	0.000
108	A	136	LEU	0	-0.018	-0.016	61.697	0.000	0.000	0.000	0.000	0.000	0.000
109	A	137	THR	0	0.018	0.007	57.225	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	138	LEU	0	-0.026	-0.003	55.575	0.001	0.001	0.000	0.000	0.000	0.000
111	A	139	VAL	0	0.016	-0.006	51.806	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	140	LYS	1	0.915	0.969	46.471	0.000	0.000	0.000	0.000	0.000	0.000
113	A	141	HIS	0	-0.118	-0.070	44.446	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	142	VAL	0	0.017	0.019	40.985	0.002	0.002	0.000	0.000	0.000	0.000
115	A	143	THR	0	0.030	0.011	39.411	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	144	PHE	0	0.022	0.007	34.957	0.003	0.003	0.000	0.000	0.000	0.000
117	A	145	ASP	-1	-0.797	-0.859	34.359	0.014	0.014	0.000	0.000	0.000	0.000
118	A	146	ASN	0	-0.067	-0.048	29.783	0.001	0.001	0.000	0.000	0.000	0.000
119	A	147	ASN	0	-0.063	-0.048	28.166	0.000	0.000	0.000	0.000	0.000	0.000
120	A	148	GLN	0	-0.031	-0.008	32.440	0.000	0.000	0.000	0.000	0.000	0.000
121	A	149	GLU	-1	-0.889	-0.953	35.850	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	150	LYS	1	0.810	0.883	37.706	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	151	VAL	0	0.026	0.021	41.540	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	152	VAL	0	-0.025	0.000	43.510	0.001	0.001	0.000	0.000	0.000	0.000
125	A	153	GLU	-1	-0.823	-0.899	46.294	-0.013	-0.013	0.000	0.000	0.000	0.000
126	A	154	CYS	0	0.044	0.019	49.247	0.000	0.000	0.000	0.000	0.000	0.000
127	A	155	THR	0	-0.059	0.000	51.830	0.000	0.000	0.000	0.000	0.000	0.000
128	A	156	ARG	1	0.876	0.938	55.102	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	157	ILE	0	-0.011	-0.003	56.530	0.000	0.000	0.000	0.000	0.000	0.000
130	A	158	LYS	1	0.862	0.923	59.559	0.003	0.003	0.000	0.000	0.000	0.000
131	A	159	TRP	0	0.017	-0.004	58.730	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	160	LYS	1	0.804	0.913	64.465	0.002	0.002	0.000	0.000	0.000	0.000
133	A	161	GLU	-1	-0.878	-0.959	67.937	0.004	0.004	0.000	0.000	0.000	0.000
134	A	162	GLY	0	-0.036	-0.013	69.671	0.000	0.000	0.000	0.000	0.000	0.000
135	A	163	LYS	1	0.814	0.906	67.246	0.000	0.000	0.000	0.000	0.000	0.000
136	A	164	ASN	0	0.034	0.011	61.152	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	165	PRO	0	0.014	0.022	59.948	0.001	0.001	0.000	0.000	0.000	0.000
138	A	166	ILE	0	0.019	-0.009	56.615	0.001	0.001	0.000	0.000	0.000	0.000
139	A	167	ALA	0	-0.096	-0.030	59.457	0.001	0.001	0.000	0.000	0.000	0.000
140	A	168	ALA	0	-0.010	0.009	60.358	0.000	0.000	0.000	0.000	0.000	0.000
141	A	181	PRO	0	0.005	-0.007	53.576	0.000	0.000	0.000	0.000	0.000	0.000
142	A	182	LYS	1	0.762	0.879	54.971	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	183	TRP	0	0.025	0.026	49.518	0.001	0.001	0.000	0.000	0.000	0.000
144	A	184	SER	0	-0.016	-0.038	54.896	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	185	ILE	0	0.034	0.005	51.863	0.000	0.000	0.000	0.000	0.000	0.000
146	A	186	PHE	0	-0.057	-0.043	52.782	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	187	GLU	-1	-0.818	-0.900	52.432	0.009	0.009	0.000	0.000	0.000	0.000
148	A	188	TRP	0	-0.007	-0.003	45.834	0.000	0.000	0.000	0.000	0.000	0.000
149	A	189	PHE	0	-0.030	-0.022	49.806	0.000	0.000	0.000	0.000	0.000	0.000
150	A	190	THR	0	-0.030	-0.051	49.642	0.000	0.000	0.000	0.000	0.000	0.000
151	A	191	THR	0	-0.007	-0.024	47.419	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	192	ASP	-1	-0.902	-0.917	46.634	0.014	0.014	0.000	0.000	0.000	0.000
153	A	193	GLU	-1	-0.841	-0.910	40.744	0.019	0.019	0.000	0.000	0.000	0.000
154	A	194	LEU	0	-0.035	-0.017	44.057	0.001	0.001	0.000	0.000	0.000	0.000
155	A	195	GLN	0	-0.059	-0.045	40.662	0.001	0.001	0.000	0.000	0.000	0.000
156	A	196	ASP	-1	-0.925	-0.954	42.894	0.025	0.025	0.000	0.000	0.000	0.000
157	A	197	LYS	1	0.849	0.920	44.651	-0.013	-0.013	0.000	0.000	0.000	0.000
158	A	198	PRO	0	-0.002	-0.002	44.816	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	199	ASP	-1	-0.696	-0.836	42.255	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	200	VAL	0	-0.025	-0.031	44.275	-0.002	-0.002	0.000	0.000	0.000	0.000
161	A	201	GLY	0	0.004	0.006	44.477	-0.002	-0.002	0.000	0.000	0.000	0.000
162	A	202	GLU	-1	-0.763	-0.871	37.358	-0.018	-0.018	0.000	0.000	0.000	0.000
163	A	203	LEU	0	-0.026	0.005	41.509	-0.003	-0.003	0.000	0.000	0.000	0.000
164	A	204	ILE	0	-0.020	-0.022	43.587	-0.002	-0.002	0.000	0.000	0.000	0.000
165	A	205	ARG	1	0.762	0.853	36.393	0.022	0.022	0.000	0.000	0.000	0.000
166	A	206	ARG	1	0.833	0.905	35.399	0.009	0.009	0.000	0.000	0.000	0.000
167	A	207	GLU	-1	-0.881	-0.917	39.973	-0.012	-0.012	0.000	0.000	0.000	0.000
168	A	208	ILE	0	-0.027	-0.011	42.610	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	209	TRP	0	-0.004	0.013	44.381	0.000	0.000	0.000	0.000	0.000	0.000
170	A	210	HIS	0	-0.007	-0.014	42.610	-0.001	-0.001	0.000	0.000	0.000	0.000
171	A	211	ASN	0	-0.021	-0.022	44.818	0.000	0.000	0.000	0.000	0.000	0.000
172	A	212	PRO	0	0.059	0.049	47.582	0.001	0.001	0.000	0.000	0.000	0.000
173	A	213	LEU	0	0.007	0.001	50.193	0.002	0.002	0.000	0.000	0.000	0.000
174	A	214	SER	0	0.008	0.004	47.253	0.001	0.001	0.000	0.000	0.000	0.000
175	A	215	TYR	0	0.047	0.050	44.603	0.000	0.000	0.000	0.000	0.000	0.000
176	A	216	TYR	0	-0.023	0.008	50.794	0.001	0.001	0.000	0.000	0.000	0.000
177	A	217	LEU	0	-0.078	-0.040	52.384	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:29:PHE)