FMO DATABASE

FMODB ID: VR4J1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1866604.146822
FMO2-HF: Nuclear repulsion	1798016.489247
FMO2-HF: Total energy	-68587.657575
FMO2-MP2: Total energy	-68787.307632

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.
-16.4	-17.304	24.699	-11.232	-12.562	-0.001

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 : 0.039 / q_NPA : 0.064

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	0.963	0.991	3.318	-1.177	0.998	0.039	-1.102	-1.113	0.002
4	A	4	ILE	0	0.009	0.011	6.005	-0.074	-0.074	0.000	0.000	0.000	0.000
5	A	5	ALA	0	-0.005	0.011	8.554	0.129	0.129	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.001	0.006	11.852	-0.025	-0.025	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.023	-0.004	14.090	-0.014	-0.014	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.043	0.031	16.877	-0.006	-0.006	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.050	-0.045	20.178	-0.015	-0.015	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.024	-0.003	23.828	0.001	0.001	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.036	-0.024	26.490	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.040	-0.034	26.886	0.003	0.003	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.039	-0.001	26.204	0.002	0.002	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.031	-0.025	23.078	0.009	0.009	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.020	0.012	21.527	0.011	0.011	0.000	0.000	0.000	0.000
16	A	16	TYR	0	0.026	0.006	20.638	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.036	0.025	17.760	0.012	0.012	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.048	-0.027	16.455	0.024	0.024	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.849	0.906	16.431	-0.062	-0.062	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.016	0.007	13.247	0.012	0.012	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.027	-0.022	11.185	0.031	0.031	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.008	0.011	11.268	0.059	0.059	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.079	0.036	11.474	0.037	0.037	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.014	-0.014	8.237	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.818	-0.897	6.900	0.443	0.443	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.940	-0.983	7.803	0.094	0.094	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.054	-0.016	7.938	-0.059	-0.059	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.897	-0.933	3.585	0.101	0.470	0.008	-0.110	-0.267	0.000
29	A	29	PHE	0	-0.027	-0.015	2.537	-5.263	-2.671	3.103	-2.469	-3.226	-0.026
30	A	30	SER	0	-0.050	-0.072	2.152	-4.531	-12.281	19.956	-6.926	-5.279	0.032
31	A	31	VAL	0	-0.015	-0.005	4.070	-1.833	-2.232	0.083	0.538	-0.222	0.005
32	A	32	ASP	-1	-0.759	-0.793	7.758	-0.021	-0.021	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.003	-0.006	10.490	-0.030	-0.030	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.011	0.005	13.516	-0.044	-0.044	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.020	0.005	16.557	0.005	0.005	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.003	0.003	19.848	-0.015	-0.015	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.915	0.921	23.574	-0.019	-0.019	0.000	0.000	0.000	0.000
38	A	38	ASN	0	0.008	-0.003	26.021	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.054	0.032	22.995	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.801	0.900	21.038	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.031	-0.004	24.790	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.071	0.036	27.228	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.021	-0.013	21.731	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.848	0.925	25.983	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.930	-0.967	28.619	0.015	0.015	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.849	-0.881	27.735	0.044	0.044	0.000	0.000	0.000	0.000
47	A	54	VAL	0	-0.020	-0.023	19.206	0.004	0.004	0.000	0.000	0.000	0.000
48	A	55	LEU	0	0.012	0.009	17.807	0.000	0.000	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.889	0.934	14.293	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	57	GLY	0	0.020	0.011	13.629	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	58	LEU	0	-0.028	-0.003	10.264	-0.029	-0.029	0.000	0.000	0.000	0.000
52	A	59	LYS	1	0.829	0.891	5.713	-0.403	-0.403	0.000	0.000	0.000	0.000
53	A	60	ASN	0	-0.015	-0.019	2.868	-4.169	-2.196	1.511	-1.151	-2.333	-0.014
54	A	61	VAL	0	0.015	0.023	4.547	0.642	0.778	-0.001	-0.012	-0.122	0.000
55	A	62	ARG	1	0.837	0.881	8.070	-0.204	-0.204	0.000	0.000	0.000	0.000
56	A	63	ILE	0	-0.003	-0.005	9.741	0.038	0.038	0.000	0.000	0.000	0.000
57	A	64	HIS	0	-0.006	0.001	11.757	-0.075	-0.075	0.000	0.000	0.000	0.000
58	A	65	GLU	-1	-0.765	-0.891	16.282	0.022	0.022	0.000	0.000	0.000	0.000
59	A	66	GLU	-1	-0.812	-0.882	19.957	0.029	0.029	0.000	0.000	0.000	0.000
60	A	67	ASN	0	-0.011	-0.008	22.264	0.003	0.003	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.808	-0.881	18.727	-0.029	-0.029	0.000	0.000	0.000	0.000
62	A	69	PHE	0	-0.021	-0.029	20.440	0.005	0.005	0.000	0.000	0.000	0.000
63	A	70	THR	0	-0.078	-0.053	20.754	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.033	0.020	15.623	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	72	PRO	0	-0.053	-0.053	12.793	0.002	0.002	0.000	0.000	0.000	0.000
66	A	73	LEU	0	0.039	0.021	12.518	0.005	0.005	0.000	0.000	0.000	0.000
67	A	74	ALA	0	0.009	0.019	15.799	0.007	0.007	0.000	0.000	0.000	0.000
68	A	75	SER	0	-0.010	-0.007	17.272	-0.005	-0.005	0.000	0.000	0.000	0.000
69	A	76	GLY	0	0.073	0.033	17.035	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	77	SER	0	-0.006	-0.006	17.054	0.003	0.003	0.000	0.000	0.000	0.000
71	A	78	ARG	1	0.893	0.950	13.357	0.075	0.075	0.000	0.000	0.000	0.000
72	A	79	LEU	0	0.053	0.012	12.641	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	80	VAL	0	0.034	0.007	13.544	0.007	0.007	0.000	0.000	0.000	0.000
74	A	81	HIS	0	-0.089	-0.021	9.800	0.036	0.036	0.000	0.000	0.000	0.000
75	A	82	TYR	0	-0.112	-0.085	8.874	-0.149	-0.149	0.000	0.000	0.000	0.000
76	A	83	ARG	1	0.833	0.915	7.631	-0.233	-0.233	0.000	0.000	0.000	0.000
77	A	84	GLY	0	0.027	0.001	10.243	0.022	0.022	0.000	0.000	0.000	0.000
78	A	85	VAL	0	-0.034	-0.016	11.799	0.012	0.012	0.000	0.000	0.000	0.000
79	A	86	TYR	0	0.009	-0.017	11.708	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	87	VAL	0	-0.017	-0.027	15.892	0.002	0.002	0.000	0.000	0.000	0.000
81	A	88	VAL	0	0.007	0.026	17.478	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	89	PRO	0	0.049	0.022	19.524	0.008	0.008	0.000	0.000	0.000	0.000
83	A	90	CYS	0	-0.027	0.002	22.645	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	91	SER	0	0.020	-0.003	24.374	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	92	THR	0	0.042	-0.002	27.829	0.001	0.001	0.000	0.000	0.000	0.000
86	A	93	ASN	0	-0.017	-0.009	30.180	0.000	0.000	0.000	0.000	0.000	0.000
87	A	94	THR	0	0.055	0.032	24.043	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	95	LEU	0	0.009	0.009	26.982	0.001	0.001	0.000	0.000	0.000	0.000
89	A	96	SER	0	-0.004	0.001	27.901	0.000	0.000	0.000	0.000	0.000	0.000
90	A	97	CYS	0	-0.077	-0.028	28.189	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	98	ILE	0	0.028	0.013	22.633	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	99	ALA	0	-0.003	0.015	26.728	0.000	0.000	0.000	0.000	0.000	0.000
93	A	100	ASN	0	-0.093	-0.060	29.179	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	101	GLY	0	0.036	0.039	28.584	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	102	ILE	0	-0.025	-0.006	29.670	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	103	ASN	0	-0.021	-0.040	26.363	0.005	0.005	0.000	0.000	0.000	0.000
97	A	104	LYS	1	0.945	0.976	28.252	-0.021	-0.021	0.000	0.000	0.000	0.000
98	A	105	ASN	0	-0.035	-0.037	24.807	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	106	LEU	0	0.023	0.015	17.906	0.003	0.003	0.000	0.000	0.000	0.000
100	A	107	ILE	0	0.008	-0.007	20.189	0.004	0.004	0.000	0.000	0.000	0.000
101	A	108	HIS	0	-0.030	-0.020	21.576	0.001	0.001	0.000	0.000	0.000	0.000
102	A	109	ARG	1	0.858	0.929	21.540	-0.017	-0.017	0.000	0.000	0.000	0.000
103	A	110	VAL	0	0.004	-0.009	16.342	0.000	0.000	0.000	0.000	0.000	0.000
104	A	111	GLY	0	0.025	0.015	19.544	0.005	0.005	0.000	0.000	0.000	0.000
105	A	112	GLU	-1	-0.818	-0.892	21.618	0.029	0.029	0.000	0.000	0.000	0.000
106	A	113	VAL	0	-0.018	-0.016	18.501	0.000	0.000	0.000	0.000	0.000	0.000
107	A	114	ALA	0	0.007	0.000	18.011	0.001	0.001	0.000	0.000	0.000	0.000
108	A	115	LEU	0	0.018	0.005	19.393	0.003	0.003	0.000	0.000	0.000	0.000
109	A	116	LYS	1	0.804	0.898	22.803	-0.032	-0.032	0.000	0.000	0.000	0.000
110	A	117	GLU	-1	-0.863	-0.930	18.861	0.041	0.041	0.000	0.000	0.000	0.000
111	A	118	ARG	1	0.850	0.937	19.999	-0.060	-0.060	0.000	0.000	0.000	0.000
112	A	119	VAL	0	0.002	0.028	14.380	0.010	0.010	0.000	0.000	0.000	0.000
113	A	120	PRO	0	0.022	0.008	14.885	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	121	LEU	0	0.020	0.016	16.023	0.001	0.001	0.000	0.000	0.000	0.000
115	A	122	VAL	0	-0.015	-0.003	16.877	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	123	LEU	0	-0.001	-0.006	18.937	0.004	0.004	0.000	0.000	0.000	0.000
117	A	124	LEU	0	-0.003	0.009	21.038	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	125	VAL	0	-0.003	0.004	22.739	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	126	ARG	1	0.896	0.944	26.453	-0.040	-0.040	0.000	0.000	0.000	0.000
120	A	127	GLU	-1	-0.864	-0.929	28.705	0.034	0.034	0.000	0.000	0.000	0.000
121	A	128	ALA	0	-0.022	0.004	32.387	0.001	0.001	0.000	0.000	0.000	0.000
122	A	129	PRO	0	0.025	0.005	35.678	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	130	TYR	0	-0.005	0.002	31.175	0.001	0.001	0.000	0.000	0.000	0.000
124	A	131	ASN	0	0.040	0.007	36.642	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.860	-0.941	37.245	0.029	0.029	0.000	0.000	0.000	0.000
126	A	133	ILE	0	0.046	0.029	35.700	0.002	0.002	0.000	0.000	0.000	0.000
127	A	134	HIS	0	0.013	0.007	33.195	0.003	0.003	0.000	0.000	0.000	0.000
128	A	135	LEU	0	0.028	0.008	32.792	0.003	0.003	0.000	0.000	0.000	0.000
129	A	136	GLU	-1	-0.906	-0.950	33.612	0.037	0.037	0.000	0.000	0.000	0.000
130	A	137	ASN	0	-0.028	-0.020	30.821	0.002	0.002	0.000	0.000	0.000	0.000
131	A	138	MET	0	-0.014	-0.003	28.820	0.004	0.004	0.000	0.000	0.000	0.000
132	A	139	LEU	0	0.012	0.015	29.090	0.004	0.004	0.000	0.000	0.000	0.000
133	A	140	LYS	1	0.870	0.935	30.702	-0.036	-0.036	0.000	0.000	0.000	0.000
134	A	141	ILE	0	0.013	-0.002	24.490	0.002	0.002	0.000	0.000	0.000	0.000
135	A	142	THR	0	-0.037	-0.023	26.119	0.004	0.004	0.000	0.000	0.000	0.000
136	A	143	ARG	1	0.909	0.948	27.301	-0.044	-0.044	0.000	0.000	0.000	0.000
137	A	144	MET	0	-0.065	-0.021	26.689	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	145	GLY	0	0.001	0.015	24.224	0.002	0.002	0.000	0.000	0.000	0.000
139	A	146	GLY	0	-0.011	0.007	21.690	0.007	0.007	0.000	0.000	0.000	0.000
140	A	147	VAL	0	-0.028	-0.026	20.682	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	148	VAL	0	0.001	-0.004	22.287	0.001	0.001	0.000	0.000	0.000	0.000
142	A	149	VAL	0	0.004	0.002	21.093	0.000	0.000	0.000	0.000	0.000	0.000
143	A	150	PRO	0	0.021	0.020	24.228	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	151	ALA	0	-0.004	-0.009	25.625	0.003	0.003	0.000	0.000	0.000	0.000
145	A	152	SER	0	-0.053	-0.036	26.611	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	153	PRO	0	-0.001	0.008	26.754	0.003	0.003	0.000	0.000	0.000	0.000
147	A	154	ALA	0	-0.009	0.002	27.912	-0.004	-0.004	0.000	0.000	0.000	0.000
148	A	155	PHE	0	0.045	-0.002	29.361	0.001	0.001	0.000	0.000	0.000	0.000
149	A	156	TYR	0	-0.029	-0.010	28.754	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	157	HIS	0	0.023	-0.002	24.152	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	158	LYS	1	0.913	0.967	29.406	-0.040	-0.040	0.000	0.000	0.000	0.000
152	A	159	PRO	0	-0.012	0.015	28.680	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	160	GLN	0	0.024	0.008	30.185	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	161	SER	0	-0.036	-0.026	28.210	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	162	ILE	0	0.040	-0.009	27.461	0.003	0.003	0.000	0.000	0.000	0.000
156	A	163	ASP	-1	-0.778	-0.862	22.961	0.064	0.064	0.000	0.000	0.000	0.000
157	A	164	ASP	-1	-0.779	-0.868	23.905	0.051	0.051	0.000	0.000	0.000	0.000
158	A	165	MET	0	-0.032	-0.016	24.800	0.005	0.005	0.000	0.000	0.000	0.000
159	A	166	ILE	0	-0.004	-0.004	21.010	0.005	0.005	0.000	0.000	0.000	0.000
160	A	167	ASN	0	0.024	0.001	20.142	0.016	0.016	0.000	0.000	0.000	0.000
161	A	168	PHE	0	0.012	0.013	20.346	0.008	0.008	0.000	0.000	0.000	0.000
162	A	169	VAL	0	-0.013	-0.005	21.488	0.006	0.006	0.000	0.000	0.000	0.000
163	A	170	VAL	0	-0.004	-0.008	15.972	0.006	0.006	0.000	0.000	0.000	0.000
164	A	171	GLY	0	0.054	0.026	16.912	0.011	0.011	0.000	0.000	0.000	0.000
165	A	172	LYS	1	0.866	0.928	17.790	-0.090	-0.090	0.000	0.000	0.000	0.000
166	A	173	LEU	0	-0.004	-0.003	16.759	0.002	0.002	0.000	0.000	0.000	0.000
167	A	174	LEU	0	0.009	0.032	11.586	0.007	0.007	0.000	0.000	0.000	0.000
168	A	175	ASP	-1	-0.791	-0.885	14.598	0.128	0.128	0.000	0.000	0.000	0.000
169	A	176	VAL	0	-0.069	-0.018	17.212	0.006	0.006	0.000	0.000	0.000	0.000
170	A	177	LEU	0	0.001	0.010	11.705	0.002	0.002	0.000	0.000	0.000	0.000
171	A	178	ARG	1	0.884	0.926	12.680	-0.127	-0.127	0.000	0.000	0.000	0.000
172	A	179	ILE	0	-0.051	-0.013	9.256	0.029	0.029	0.000	0.000	0.000	0.000
173	A	180	GLU	-1	-0.924	-0.959	10.311	0.275	0.275	0.000	0.000	0.000	0.000
174	A	181	HIS	0	-0.010	-0.027	11.696	-0.010	-0.010	0.000	0.000	0.000	0.000
175	A	182	ASN	0	-0.007	-0.004	14.328	-0.002	-0.002	0.000	0.000	0.000	0.000
176	A	183	LEU	0	-0.043	-0.004	16.188	-0.013	-0.013	0.000	0.000	0.000	0.000

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