FMO DATABASE

FMODB ID: 53L4Z

Calculation Name: 2EJB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EJB

Chain ID: A

ChEMBL ID:

UniProt ID: O66811

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:

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	176
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1860028.474401
FMO2-HF: Nuclear repulsion	1791442.532531
FMO2-HF: Total energy	-68585.94187
FMO2-MP2: Total energy	-68785.761491

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.
-15.476	-13.538	17.719	-9.656	-10.003	-0.009

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 : 0.029 / q_NPA : 0.046

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	LYS	1	0.953	0.983	3.039	-1.914	0.809	0.131	-1.454	-1.401	0.000
4	A	4	ILE	0	0.037	0.025	5.282	0.123	0.193	-0.001	-0.004	-0.065	0.000
5	A	5	ALA	0	0.006	0.016	8.098	0.141	0.141	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.001	0.008	11.309	-0.001	-0.001	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.033	-0.016	13.660	0.019	0.019	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.025	0.019	16.905	-0.001	-0.001	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.053	-0.095	19.822	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.003	-0.021	23.407	0.003	0.003	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.028	-0.018	26.379	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.030	-0.009	26.985	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.034	0.005	26.355	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.024	-0.020	23.246	0.001	0.001	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.032	0.018	21.801	0.004	0.004	0.000	0.000	0.000	0.000
16	A	16	TYR	0	0.014	0.001	20.874	0.005	0.005	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.041	0.022	18.096	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.062	-0.022	16.813	0.011	0.011	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.954	0.977	16.520	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.028	0.013	13.241	0.009	0.009	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.015	-0.010	11.670	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.028	-0.028	11.639	0.036	0.036	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.078	0.043	11.702	0.029	0.029	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.023	-0.010	8.289	-0.020	-0.020	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.782	-0.870	7.027	0.435	0.435	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.984	-0.985	7.660	0.193	0.193	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.082	-0.030	7.590	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.927	-0.945	3.729	-0.415	-0.034	0.014	-0.133	-0.263	0.000
29	A	29	PHE	0	-0.045	-0.034	2.304	-6.986	-4.272	2.848	-2.572	-2.990	-0.032
30	A	30	SER	0	-0.058	-0.060	2.248	-3.381	-8.567	14.546	-4.959	-4.401	0.024
31	A	31	VAL	0	-0.005	-0.002	4.047	-1.774	-1.533	0.030	-0.141	-0.130	0.002
32	A	32	ASP	-1	-0.755	-0.814	7.657	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.012	-0.010	10.351	-0.051	-0.051	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.002	0.007	13.545	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.001	-0.006	17.087	0.001	0.001	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.007	0.018	19.976	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	37	ARG	1	1.009	0.974	23.502	0.013	0.013	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.041	-0.028	26.503	0.000	0.000	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.031	0.011	23.169	0.001	0.001	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.932	0.977	22.467	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.010	-0.010	25.633	0.002	0.002	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.036	0.033	27.072	0.001	0.001	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.011	-0.005	22.463	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.867	0.940	26.546	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.980	-0.996	29.172	0.005	0.005	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.805	-0.882	28.642	0.012	0.012	0.000	0.000	0.000	0.000
47	A	54	VAL	0	0.007	-0.001	20.276	0.004	0.004	0.000	0.000	0.000	0.000
48	A	55	LEU	0	0.009	-0.002	19.160	0.009	0.009	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.922	0.958	15.348	-0.089	-0.089	0.000	0.000	0.000	0.000
50	A	57	GLY	0	0.016	0.016	15.196	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	58	LEU	0	-0.049	-0.043	11.201	-0.028	-0.028	0.000	0.000	0.000	0.000
52	A	59	LYS	1	0.932	0.949	7.207	-0.297	-0.297	0.000	0.000	0.000	0.000
53	A	60	ASN	0	-0.025	-0.016	3.514	-2.032	-1.037	0.151	-0.393	-0.753	-0.003
54	A	61	VAL	0	0.035	0.027	6.303	0.352	0.352	0.000	0.000	0.000	0.000
55	A	62	ARG	1	0.834	0.905	9.291	-0.027	-0.027	0.000	0.000	0.000	0.000
56	A	63	ILE	0	0.000	-0.010	11.122	-0.024	-0.024	0.000	0.000	0.000	0.000
57	A	64	HIS	0	-0.044	-0.017	12.003	-0.042	-0.042	0.000	0.000	0.000	0.000
58	A	65	GLU	-1	-0.858	-0.929	16.943	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	66	GLU	-1	-0.873	-0.941	20.712	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	67	ASN	0	-0.002	-0.016	22.131	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.807	-0.874	19.893	-0.062	-0.062	0.000	0.000	0.000	0.000
62	A	69	PHE	0	-0.038	-0.027	20.851	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	70	THR	0	-0.083	-0.059	21.039	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.015	-0.010	16.158	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	72	PRO	0	-0.031	-0.032	13.528	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	73	LEU	0	0.027	0.014	11.678	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	74	ALA	0	0.000	0.016	15.262	0.006	0.006	0.000	0.000	0.000	0.000
68	A	75	SER	0	-0.029	-0.020	17.402	0.013	0.013	0.000	0.000	0.000	0.000
69	A	76	GLY	0	0.040	0.014	16.852	-0.019	-0.019	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.002	-0.005	16.950	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	78	ARG	1	0.903	0.948	13.464	0.193	0.193	0.000	0.000	0.000	0.000
72	A	79	LEU	0	0.045	-0.001	12.569	-0.055	-0.055	0.000	0.000	0.000	0.000
73	A	80	VAL	0	0.007	0.008	13.142	-0.027	-0.027	0.000	0.000	0.000	0.000
74	A	81	HIS	0	-0.045	-0.009	9.889	0.031	0.031	0.000	0.000	0.000	0.000
75	A	82	TYR	0	-0.149	-0.083	8.664	-0.201	-0.201	0.000	0.000	0.000	0.000
76	A	83	ARG	1	0.892	0.971	6.975	0.193	0.193	0.000	0.000	0.000	0.000
77	A	84	GLY	0	0.007	-0.013	10.002	0.098	0.098	0.000	0.000	0.000	0.000
78	A	85	VAL	0	-0.039	-0.016	11.658	-0.044	-0.044	0.000	0.000	0.000	0.000
79	A	86	TYR	0	0.007	-0.005	11.738	0.014	0.014	0.000	0.000	0.000	0.000
80	A	87	VAL	0	-0.010	-0.008	15.755	0.005	0.005	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.014	0.026	17.833	0.003	0.003	0.000	0.000	0.000	0.000
82	A	89	PRO	0	0.055	0.019	19.424	0.006	0.006	0.000	0.000	0.000	0.000
83	A	90	CYS	0	0.025	0.051	22.536	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	91	SER	0	-0.001	0.005	24.010	0.001	0.001	0.000	0.000	0.000	0.000
85	A	92	THR	0	0.097	0.033	27.483	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	93	ASN	0	-0.027	-0.015	29.841	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	94	THR	0	0.038	0.019	23.472	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	95	LEU	0	0.000	0.007	26.548	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	96	SER	0	-0.017	-0.011	27.491	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	97	CYS	0	-0.062	-0.030	27.754	0.000	0.000	0.000	0.000	0.000	0.000
91	A	98	ILE	0	0.042	0.020	22.389	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	99	ALA	0	-0.037	-0.008	26.458	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.087	-0.054	29.022	0.002	0.002	0.000	0.000	0.000	0.000
94	A	101	GLY	0	0.003	0.021	28.104	0.000	0.000	0.000	0.000	0.000	0.000
95	A	102	ILE	0	-0.046	-0.007	29.191	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	103	ASN	0	0.008	-0.016	25.368	0.001	0.001	0.000	0.000	0.000	0.000
97	A	104	LYS	1	0.933	0.964	27.907	0.013	0.013	0.000	0.000	0.000	0.000
98	A	105	ASN	0	-0.012	-0.005	24.027	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	106	LEU	0	0.046	0.025	17.856	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	107	ILE	0	0.021	-0.008	19.612	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	108	HIS	0	0.015	0.016	20.937	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	109	ARG	1	0.895	0.941	21.176	0.055	0.055	0.000	0.000	0.000	0.000
103	A	110	VAL	0	-0.011	-0.018	16.037	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	111	GLY	0	0.020	0.019	18.836	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	112	GLU	-1	-0.831	-0.903	20.878	-0.039	-0.039	0.000	0.000	0.000	0.000
106	A	113	VAL	0	-0.058	-0.037	18.206	0.003	0.003	0.000	0.000	0.000	0.000
107	A	114	ALA	0	0.043	0.013	17.514	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	115	LEU	0	0.013	0.016	18.710	0.006	0.006	0.000	0.000	0.000	0.000
109	A	116	LYS	1	0.795	0.895	22.088	0.066	0.066	0.000	0.000	0.000	0.000
110	A	117	GLU	-1	-0.859	-0.924	18.509	-0.063	-0.063	0.000	0.000	0.000	0.000
111	A	118	ARG	1	0.875	0.948	19.241	0.015	0.015	0.000	0.000	0.000	0.000
112	A	119	VAL	0	-0.009	0.014	14.053	0.006	0.006	0.000	0.000	0.000	0.000
113	A	120	PRO	0	0.018	0.004	14.463	0.007	0.007	0.000	0.000	0.000	0.000
114	A	121	LEU	0	0.027	0.021	15.868	-0.022	-0.022	0.000	0.000	0.000	0.000
115	A	122	VAL	0	-0.017	-0.009	16.694	0.014	0.014	0.000	0.000	0.000	0.000
116	A	123	LEU	0	0.008	-0.016	18.882	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	124	LEU	0	0.021	0.021	21.202	0.004	0.004	0.000	0.000	0.000	0.000
118	A	125	VAL	0	0.002	0.000	22.976	0.000	0.000	0.000	0.000	0.000	0.000
119	A	126	ARG	1	0.967	0.983	26.679	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	127	GLU	-1	-0.913	-0.950	28.914	0.002	0.002	0.000	0.000	0.000	0.000
121	A	128	ALA	0	-0.109	-0.040	32.562	0.001	0.001	0.000	0.000	0.000	0.000
122	A	129	PRO	0	0.053	0.009	35.925	0.000	0.000	0.000	0.000	0.000	0.000
123	A	130	TYR	0	0.004	0.005	31.295	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	131	ASN	0	0.042	0.028	36.947	0.000	0.000	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.850	-0.962	37.571	0.002	0.002	0.000	0.000	0.000	0.000
126	A	133	ILE	0	0.054	0.031	35.132	0.000	0.000	0.000	0.000	0.000	0.000
127	A	134	HIS	0	-0.036	-0.021	33.382	0.000	0.000	0.000	0.000	0.000	0.000
128	A	135	LEU	0	0.023	0.005	32.693	0.000	0.000	0.000	0.000	0.000	0.000
129	A	136	GLU	-1	-0.898	-0.949	33.646	0.000	0.000	0.000	0.000	0.000	0.000
130	A	137	ASN	0	-0.010	-0.005	30.594	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	138	MET	0	-0.032	-0.010	28.781	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	139	LEU	0	0.029	0.023	29.126	0.000	0.000	0.000	0.000	0.000	0.000
133	A	140	LYS	1	0.950	0.986	30.181	0.009	0.009	0.000	0.000	0.000	0.000
134	A	141	ILE	0	0.006	0.001	24.469	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	142	THR	0	-0.026	-0.027	26.122	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	143	ARG	1	0.906	0.955	26.979	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	144	MET	0	-0.077	-0.028	26.158	0.001	0.001	0.000	0.000	0.000	0.000
138	A	145	GLY	0	-0.008	0.007	23.777	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	146	GLY	0	-0.023	0.002	21.761	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	147	VAL	0	-0.004	-0.011	20.540	0.007	0.007	0.000	0.000	0.000	0.000
141	A	148	VAL	0	-0.001	-0.011	22.249	-0.005	-0.005	0.000	0.000	0.000	0.000
142	A	149	VAL	0	-0.025	-0.013	20.957	0.004	0.004	0.000	0.000	0.000	0.000
143	A	150	PRO	0	0.016	0.029	24.131	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	151	ALA	0	0.005	-0.007	25.507	0.001	0.001	0.000	0.000	0.000	0.000
145	A	152	SER	0	-0.058	-0.041	26.434	0.000	0.000	0.000	0.000	0.000	0.000
146	A	153	PRO	0	-0.013	-0.005	26.832	0.001	0.001	0.000	0.000	0.000	0.000
147	A	154	ALA	0	0.013	0.018	27.801	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	155	PHE	0	0.029	-0.011	29.464	0.001	0.001	0.000	0.000	0.000	0.000
149	A	156	TYR	0	-0.030	-0.016	28.279	0.000	0.000	0.000	0.000	0.000	0.000
150	A	157	HIS	0	0.004	-0.011	24.667	0.000	0.000	0.000	0.000	0.000	0.000
151	A	158	LYS	1	0.914	0.973	29.256	-0.023	-0.023	0.000	0.000	0.000	0.000
152	A	159	PRO	0	-0.005	0.017	28.722	0.000	0.000	0.000	0.000	0.000	0.000
153	A	160	GLN	0	0.020	0.002	30.035	0.000	0.000	0.000	0.000	0.000	0.000
154	A	161	SER	0	-0.012	0.003	28.257	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	162	ILE	0	0.011	-0.020	27.536	0.000	0.000	0.000	0.000	0.000	0.000
156	A	163	ASP	-1	-0.915	-0.965	23.538	0.034	0.034	0.000	0.000	0.000	0.000
157	A	164	ASP	-1	-0.732	-0.861	24.054	0.028	0.028	0.000	0.000	0.000	0.000
158	A	165	MET	0	-0.071	-0.040	25.114	0.000	0.000	0.000	0.000	0.000	0.000
159	A	166	ILE	0	-0.027	-0.017	21.125	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	167	ASN	0	0.076	0.027	20.120	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	168	PHE	0	-0.005	0.023	20.273	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	169	VAL	0	-0.024	-0.017	21.524	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	170	VAL	0	-0.011	-0.011	16.079	-0.004	-0.004	0.000	0.000	0.000	0.000
164	A	171	GLY	0	0.056	0.028	16.890	-0.007	-0.007	0.000	0.000	0.000	0.000
165	A	172	LYS	1	0.951	0.975	17.882	-0.026	-0.026	0.000	0.000	0.000	0.000
166	A	173	LEU	0	-0.022	-0.014	16.715	-0.002	-0.002	0.000	0.000	0.000	0.000
167	A	174	LEU	0	0.022	0.028	11.454	-0.016	-0.016	0.000	0.000	0.000	0.000
168	A	175	ASP	-1	-0.837	-0.897	14.431	0.036	0.036	0.000	0.000	0.000	0.000
169	A	176	VAL	0	-0.087	-0.040	16.899	0.010	0.010	0.000	0.000	0.000	0.000
170	A	177	LEU	0	-0.030	-0.016	12.194	0.006	0.006	0.000	0.000	0.000	0.000
171	A	178	ARG	1	0.861	0.926	12.355	-0.048	-0.048	0.000	0.000	0.000	0.000
172	A	179	ILE	0	-0.059	-0.017	8.839	0.031	0.031	0.000	0.000	0.000	0.000
173	A	180	GLU	-1	-0.932	-0.957	10.073	0.218	0.218	0.000	0.000	0.000	0.000
174	A	181	HIS	0	-0.009	-0.033	11.537	-0.024	-0.024	0.000	0.000	0.000	0.000
175	A	182	ASN	0	0.020	-0.001	14.007	0.014	0.014	0.000	0.000	0.000	0.000
176	A	183	LEU	0	-0.047	-0.001	15.102	-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:1:MET)