FMO DATABASE

FMODB ID: YY2J2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1861395.038543
FMO2-HF: Nuclear repulsion	1792807.823928
FMO2-HF: Total energy	-68587.214615
FMO2-MP2: Total energy	-68786.927101

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.
-15.55	-11.2	13.496	-8.13	-9.716	-0.011

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 : 0.017 / q_NPA : 0.037

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	0.975	0.991	3.595	-0.911	1.335	-0.008	-1.148	-1.090	0.005
4	A	4	ILE	0	0.024	0.019	6.171	0.076	0.076	0.000	0.000	0.000	0.000
5	A	5	ALA	0	0.003	0.014	8.631	0.077	0.077	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.004	0.010	12.096	0.003	0.003	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.036	-0.012	14.178	-0.009	-0.009	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.037	0.023	17.159	0.002	0.002	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.041	-0.052	20.270	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.021	-0.007	23.910	0.002	0.002	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.025	-0.018	26.521	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.035	-0.028	27.090	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.032	-0.002	26.252	0.002	0.002	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.038	-0.024	23.269	0.005	0.005	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.029	0.017	21.729	0.006	0.006	0.000	0.000	0.000	0.000
16	A	16	TYR	0	0.016	-0.001	20.810	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.040	0.023	17.978	0.008	0.008	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.055	-0.022	16.694	0.015	0.015	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.839	0.892	16.454	-0.044	-0.044	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.022	0.012	13.299	0.012	0.012	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.019	-0.011	11.447	0.019	0.019	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.023	-0.020	11.576	0.045	0.045	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.080	0.043	11.828	0.031	0.031	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.019	-0.011	8.259	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.798	-0.893	7.059	0.481	0.481	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.932	-0.962	7.448	0.238	0.238	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.088	-0.036	7.792	-0.032	-0.032	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.886	-0.927	3.536	-0.012	0.385	0.027	-0.130	-0.295	0.000
29	A	29	PHE	0	-0.040	-0.020	2.482	-6.235	-3.040	2.303	-2.482	-3.017	-0.028
30	A	30	SER	0	-0.046	-0.047	2.351	-4.840	-7.968	10.668	-3.707	-3.832	0.016
31	A	31	VAL	0	-0.006	-0.003	4.496	-1.657	-1.441	0.030	-0.143	-0.104	0.002
32	A	32	ASP	-1	-0.765	-0.790	8.179	-0.221	-0.221	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.009	-0.012	10.899	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.014	0.008	14.027	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.013	0.006	17.246	0.008	0.008	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.003	0.009	20.245	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.926	0.930	23.939	0.009	0.009	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.025	-0.025	26.487	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.041	0.022	23.425	0.001	0.001	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.908	0.963	21.707	0.015	0.015	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.003	-0.003	25.356	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.046	0.034	27.466	0.000	0.000	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.010	0.004	22.294	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.887	0.948	26.431	0.005	0.005	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.963	-0.982	28.917	0.003	0.003	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.845	-0.886	28.296	0.025	0.025	0.000	0.000	0.000	0.000
47	A	54	VAL	0	-0.024	-0.026	19.554	0.003	0.003	0.000	0.000	0.000	0.000
48	A	55	LEU	0	0.015	0.012	18.144	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.905	0.948	14.556	-0.044	-0.044	0.000	0.000	0.000	0.000
50	A	57	GLY	0	0.024	0.020	14.290	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	58	LEU	0	-0.038	-0.020	10.777	-0.010	-0.010	0.000	0.000	0.000	0.000
52	A	59	LYS	1	0.828	0.897	6.297	-0.569	-0.569	0.000	0.000	0.000	0.000
53	A	60	ASN	0	-0.035	-0.025	3.058	-2.603	-1.264	0.477	-0.519	-1.296	-0.006
54	A	61	VAL	0	0.034	0.025	5.270	0.369	0.454	-0.001	-0.001	-0.082	0.000
55	A	62	ARG	1	0.830	0.882	8.510	0.082	0.082	0.000	0.000	0.000	0.000
56	A	63	ILE	0	-0.007	-0.009	10.383	0.035	0.035	0.000	0.000	0.000	0.000
57	A	64	HIS	0	-0.022	-0.014	11.854	-0.040	-0.040	0.000	0.000	0.000	0.000
58	A	65	GLU	-1	-0.863	-0.936	16.623	-0.022	-0.022	0.000	0.000	0.000	0.000
59	A	66	GLU	-1	-0.805	-0.890	20.399	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	67	ASN	0	-0.019	-0.021	22.362	0.004	0.004	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.814	-0.889	19.436	-0.077	-0.077	0.000	0.000	0.000	0.000
62	A	69	PHE	0	-0.022	-0.019	20.828	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	70	THR	0	-0.078	-0.053	21.007	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.022	0.008	16.074	-0.013	-0.013	0.000	0.000	0.000	0.000
65	A	72	PRO	0	-0.028	-0.033	13.215	0.002	0.002	0.000	0.000	0.000	0.000
66	A	73	LEU	0	0.029	0.016	12.522	0.007	0.007	0.000	0.000	0.000	0.000
67	A	74	ALA	0	-0.001	0.018	15.851	0.015	0.015	0.000	0.000	0.000	0.000
68	A	75	SER	0	-0.014	-0.011	17.629	0.009	0.009	0.000	0.000	0.000	0.000
69	A	76	GLY	0	0.067	0.027	17.277	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.002	-0.007	17.324	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	78	ARG	1	0.906	0.950	13.702	0.157	0.157	0.000	0.000	0.000	0.000
72	A	79	LEU	0	0.049	-0.001	12.915	-0.025	-0.025	0.000	0.000	0.000	0.000
73	A	80	VAL	0	0.024	0.012	13.745	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	81	HIS	0	-0.066	-0.014	10.012	0.056	0.056	0.000	0.000	0.000	0.000
75	A	82	TYR	0	-0.144	-0.091	9.333	-0.110	-0.110	0.000	0.000	0.000	0.000
76	A	83	ARG	1	0.847	0.925	7.165	-0.145	-0.145	0.000	0.000	0.000	0.000
77	A	84	GLY	0	0.017	-0.007	9.999	0.047	0.047	0.000	0.000	0.000	0.000
78	A	85	VAL	0	-0.048	-0.020	12.088	-0.020	-0.020	0.000	0.000	0.000	0.000
79	A	86	TYR	0	0.012	-0.012	11.637	0.006	0.006	0.000	0.000	0.000	0.000
80	A	87	VAL	0	-0.014	-0.013	15.933	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.013	0.028	17.696	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	89	PRO	0	0.056	0.019	19.524	0.004	0.004	0.000	0.000	0.000	0.000
83	A	90	CYS	0	0.016	0.009	22.583	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	91	SER	0	-0.009	-0.001	24.239	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	92	THR	0	0.084	0.023	27.789	0.000	0.000	0.000	0.000	0.000	0.000
86	A	93	ASN	0	-0.009	-0.004	30.405	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	94	THR	0	0.042	0.023	24.166	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	95	LEU	0	0.014	0.014	26.951	0.000	0.000	0.000	0.000	0.000	0.000
89	A	96	SER	0	0.002	0.000	27.899	0.001	0.001	0.000	0.000	0.000	0.000
90	A	97	CYS	0	-0.085	-0.038	28.483	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	98	ILE	0	0.048	0.022	22.998	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	99	ALA	0	-0.017	0.013	27.151	0.000	0.000	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.078	-0.055	29.564	0.001	0.001	0.000	0.000	0.000	0.000
94	A	101	GLY	0	0.011	0.027	28.986	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	102	ILE	0	-0.052	-0.012	30.073	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	103	ASN	0	0.008	-0.028	26.409	0.003	0.003	0.000	0.000	0.000	0.000
97	A	104	LYS	1	0.943	0.973	28.744	0.002	0.002	0.000	0.000	0.000	0.000
98	A	105	ASN	0	-0.035	-0.037	25.064	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	106	LEU	0	0.035	0.028	18.178	0.003	0.003	0.000	0.000	0.000	0.000
100	A	107	ILE	0	0.010	-0.009	20.503	0.001	0.001	0.000	0.000	0.000	0.000
101	A	108	HIS	0	-0.005	0.004	21.860	0.001	0.001	0.000	0.000	0.000	0.000
102	A	109	ARG	1	0.854	0.930	21.798	0.024	0.024	0.000	0.000	0.000	0.000
103	A	110	VAL	0	0.006	-0.011	16.819	0.000	0.000	0.000	0.000	0.000	0.000
104	A	111	GLY	0	0.023	0.022	19.705	0.003	0.003	0.000	0.000	0.000	0.000
105	A	112	GLU	-1	-0.821	-0.905	21.687	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	113	VAL	0	-0.031	-0.024	18.680	0.003	0.003	0.000	0.000	0.000	0.000
107	A	114	ALA	0	0.031	0.013	18.238	0.003	0.003	0.000	0.000	0.000	0.000
108	A	115	LEU	0	0.018	0.017	19.507	0.009	0.009	0.000	0.000	0.000	0.000
109	A	116	LYS	1	0.786	0.881	22.884	0.008	0.008	0.000	0.000	0.000	0.000
110	A	117	GLU	-1	-0.876	-0.914	19.086	0.008	0.008	0.000	0.000	0.000	0.000
111	A	118	ARG	1	0.875	0.946	19.497	-0.038	-0.038	0.000	0.000	0.000	0.000
112	A	119	VAL	0	-0.009	0.009	14.428	0.012	0.012	0.000	0.000	0.000	0.000
113	A	120	PRO	0	0.019	0.006	14.395	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	121	LEU	0	0.020	0.017	16.152	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	122	VAL	0	-0.017	-0.007	16.584	0.004	0.004	0.000	0.000	0.000	0.000
116	A	123	LEU	0	0.004	-0.009	18.927	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	124	LEU	0	0.009	0.014	21.081	0.002	0.002	0.000	0.000	0.000	0.000
118	A	125	VAL	0	-0.007	-0.004	22.855	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	126	ARG	1	0.922	0.967	26.558	-0.021	-0.021	0.000	0.000	0.000	0.000
120	A	127	GLU	-1	-0.884	-0.962	28.798	0.017	0.017	0.000	0.000	0.000	0.000
121	A	128	ALA	0	-0.056	0.005	32.438	0.002	0.002	0.000	0.000	0.000	0.000
122	A	129	PRO	0	0.036	0.003	35.816	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	130	TYR	0	-0.010	-0.006	31.203	0.000	0.000	0.000	0.000	0.000	0.000
124	A	131	ASN	0	0.041	0.018	36.827	0.000	0.000	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.852	-0.955	37.586	0.018	0.018	0.000	0.000	0.000	0.000
126	A	133	ILE	0	0.042	0.024	35.643	0.001	0.001	0.000	0.000	0.000	0.000
127	A	134	HIS	0	-0.009	-0.002	33.441	0.002	0.002	0.000	0.000	0.000	0.000
128	A	135	LEU	0	0.031	0.009	32.761	0.002	0.002	0.000	0.000	0.000	0.000
129	A	136	GLU	-1	-0.906	-0.951	33.648	0.023	0.023	0.000	0.000	0.000	0.000
130	A	137	ASN	0	-0.023	-0.016	30.871	0.001	0.001	0.000	0.000	0.000	0.000
131	A	138	MET	0	-0.024	-0.004	28.745	0.002	0.002	0.000	0.000	0.000	0.000
132	A	139	LEU	0	0.024	0.028	29.130	0.003	0.003	0.000	0.000	0.000	0.000
133	A	140	LYS	1	0.877	0.940	30.639	-0.018	-0.018	0.000	0.000	0.000	0.000
134	A	141	ILE	0	0.007	-0.001	24.655	0.001	0.001	0.000	0.000	0.000	0.000
135	A	142	THR	0	-0.021	-0.026	26.268	0.003	0.003	0.000	0.000	0.000	0.000
136	A	143	ARG	1	0.919	0.962	26.979	-0.030	-0.030	0.000	0.000	0.000	0.000
137	A	144	MET	0	-0.080	-0.030	26.650	0.000	0.000	0.000	0.000	0.000	0.000
138	A	145	GLY	0	-0.001	0.010	23.773	0.001	0.001	0.000	0.000	0.000	0.000
139	A	146	GLY	0	-0.024	0.004	21.835	0.005	0.005	0.000	0.000	0.000	0.000
140	A	147	VAL	0	-0.013	-0.017	20.566	0.001	0.001	0.000	0.000	0.000	0.000
141	A	148	VAL	0	0.000	-0.010	22.122	-0.002	-0.002	0.000	0.000	0.000	0.000
142	A	149	VAL	0	-0.015	-0.009	20.915	0.002	0.002	0.000	0.000	0.000	0.000
143	A	150	PRO	0	0.018	0.030	24.058	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	151	ALA	0	-0.003	-0.009	25.464	0.003	0.003	0.000	0.000	0.000	0.000
145	A	152	SER	0	-0.057	-0.041	26.379	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	153	PRO	0	-0.011	0.001	26.801	0.002	0.002	0.000	0.000	0.000	0.000
147	A	154	ALA	0	0.008	0.018	27.860	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	155	PHE	0	0.034	-0.011	29.547	0.000	0.000	0.000	0.000	0.000	0.000
149	A	156	TYR	0	-0.030	-0.012	28.214	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	157	HIS	0	0.010	-0.010	24.379	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	158	LYS	1	0.921	0.974	29.414	-0.035	-0.035	0.000	0.000	0.000	0.000
152	A	159	PRO	0	-0.003	0.017	28.786	0.000	0.000	0.000	0.000	0.000	0.000
153	A	160	GLN	0	0.014	0.000	30.144	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	161	SER	0	-0.014	-0.007	28.413	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	162	ILE	0	0.022	-0.017	27.740	0.002	0.002	0.000	0.000	0.000	0.000
156	A	163	ASP	-1	-0.783	-0.874	23.316	0.051	0.051	0.000	0.000	0.000	0.000
157	A	164	ASP	-1	-0.763	-0.869	24.131	0.043	0.043	0.000	0.000	0.000	0.000
158	A	165	MET	0	-0.052	-0.028	25.207	0.003	0.003	0.000	0.000	0.000	0.000
159	A	166	ILE	0	-0.021	-0.012	21.194	0.003	0.003	0.000	0.000	0.000	0.000
160	A	167	ASN	0	0.056	0.021	20.194	0.010	0.010	0.000	0.000	0.000	0.000
161	A	168	PHE	0	0.011	0.025	20.357	0.005	0.005	0.000	0.000	0.000	0.000
162	A	169	VAL	0	-0.007	-0.009	21.471	0.004	0.004	0.000	0.000	0.000	0.000
163	A	170	VAL	0	-0.001	-0.007	16.033	0.003	0.003	0.000	0.000	0.000	0.000
164	A	171	GLY	0	0.055	0.028	16.924	0.006	0.006	0.000	0.000	0.000	0.000
165	A	172	LYS	1	0.867	0.932	17.961	-0.074	-0.074	0.000	0.000	0.000	0.000
166	A	173	LEU	0	-0.004	-0.007	16.658	0.003	0.003	0.000	0.000	0.000	0.000
167	A	174	LEU	0	0.026	0.038	11.544	0.001	0.001	0.000	0.000	0.000	0.000
168	A	175	ASP	-1	-0.798	-0.882	14.445	0.106	0.106	0.000	0.000	0.000	0.000
169	A	176	VAL	0	-0.075	-0.026	16.910	0.010	0.010	0.000	0.000	0.000	0.000
170	A	177	LEU	0	-0.016	-0.003	12.194	0.004	0.004	0.000	0.000	0.000	0.000
171	A	178	ARG	1	0.877	0.926	12.358	-0.108	-0.108	0.000	0.000	0.000	0.000
172	A	179	ILE	0	-0.048	-0.010	9.068	0.034	0.034	0.000	0.000	0.000	0.000
173	A	180	GLU	-1	-0.930	-0.957	10.104	0.241	0.241	0.000	0.000	0.000	0.000
174	A	181	HIS	0	-0.008	-0.027	11.663	-0.015	-0.015	0.000	0.000	0.000	0.000
175	A	182	ASN	0	-0.002	-0.007	14.221	0.004	0.004	0.000	0.000	0.000	0.000
176	A	183	LEU	0	-0.030	0.005	15.685	-0.010	-0.010	0.000	0.000	0.000	0.000

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