FMO DATABASE

FMODB ID: J3789

Calculation Name: 2IFT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2IFT

Chain ID: A

ChEMBL ID:

UniProt ID: P44869

Base Structure: X-ray

Registration Date: 2023-06-19

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
Remarks

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	-1965566.981582
FMO2-HF: Nuclear repulsion	1895466.113268
FMO2-HF: Total energy	-70100.868314
FMO2-MP2: Total energy	-70308.285429

3D Structure Molmil

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:11:GLY)

Summations of interaction energy for fragment #1(A:11:GLY)

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.
0.662	4.622	1.748	-2.695	-3.014	-0.008

Interaction energy analysis for fragmet #1(A:11:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.072 / q_NPA : 0.040

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	13	VAL	0	0.028	0.013	3.804	0.434	2.411	-0.018	-1.140	-0.819	0.004
4	A	14	ARG	1	0.862	0.920	7.139	0.614	0.614	0.000	0.000	0.000	0.000
5	A	15	ILE	0	0.017	0.030	10.028	0.149	0.149	0.000	0.000	0.000	0.000
6	A	16	ILE	0	0.014	0.022	13.278	0.028	0.028	0.000	0.000	0.000	0.000
7	A	17	ALA	0	-0.033	-0.036	15.810	0.045	0.045	0.000	0.000	0.000	0.000
8	A	18	GLY	0	0.064	0.077	18.659	-0.040	-0.040	0.000	0.000	0.000	0.000
9	A	19	LEU	0	-0.006	-0.012	20.899	-0.012	-0.012	0.000	0.000	0.000	0.000
10	A	20	TRP	0	-0.019	-0.016	16.351	-0.039	-0.039	0.000	0.000	0.000	0.000
11	A	21	ARG	1	0.899	0.981	16.004	0.218	0.218	0.000	0.000	0.000	0.000
12	A	22	GLY	0	-0.030	-0.025	14.837	0.030	0.030	0.000	0.000	0.000	0.000
13	A	23	ARG	1	0.958	0.988	12.237	0.756	0.756	0.000	0.000	0.000	0.000
14	A	24	LYS	1	0.821	0.895	7.777	1.531	1.531	0.000	0.000	0.000	0.000
15	A	25	LEU	0	-0.033	-0.013	8.114	0.149	0.149	0.000	0.000	0.000	0.000
16	A	26	PRO	0	0.012	0.021	5.213	-0.886	-0.886	0.000	0.000	0.000	0.000
17	A	27	VAL	0	0.005	0.018	2.318	2.003	1.789	1.278	-0.226	-0.838	0.002
18	A	28	LEU	0	0.042	0.029	2.802	-4.943	-2.746	0.488	-1.329	-1.357	-0.014
19	A	38	ASP	-1	-0.755	-0.870	16.790	0.049	0.049	0.000	0.000	0.000	0.000
20	A	39	ARG	1	0.861	0.900	18.374	-0.077	-0.077	0.000	0.000	0.000	0.000
21	A	40	VAL	0	-0.006	-0.012	21.996	-0.017	-0.017	0.000	0.000	0.000	0.000
22	A	41	LYS	1	1.025	1.005	14.443	0.071	0.071	0.000	0.000	0.000	0.000
23	A	42	GLU	-1	-0.839	-0.912	19.542	-0.180	-0.180	0.000	0.000	0.000	0.000
24	A	43	THR	0	-0.065	-0.028	22.315	0.000	0.000	0.000	0.000	0.000	0.000
25	A	44	LEU	0	0.018	0.032	21.621	0.002	0.002	0.000	0.000	0.000	0.000
26	A	45	PHE	0	0.051	-0.001	18.590	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	46	ASN	0	-0.062	-0.028	24.208	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	47	TRP	0	-0.014	-0.023	27.138	0.003	0.003	0.000	0.000	0.000	0.000
29	A	48	LEU	0	0.063	0.043	24.336	0.001	0.001	0.000	0.000	0.000	0.000
30	A	49	MET	0	-0.063	-0.010	26.103	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	50	PRO	0	-0.043	-0.012	28.462	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	51	TYR	0	0.039	0.003	30.630	0.003	0.003	0.000	0.000	0.000	0.000
33	A	52	ILE	0	-0.029	-0.005	23.717	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	53	HIS	0	0.068	0.037	27.431	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	54	GLN	0	-0.094	-0.056	29.152	0.002	0.002	0.000	0.000	0.000	0.000
36	A	55	SER	0	-0.062	-0.018	26.704	0.006	0.006	0.000	0.000	0.000	0.000
37	A	56	GLU	-1	-0.943	-0.985	26.204	-0.162	-0.162	0.000	0.000	0.000	0.000
38	A	57	CYS	0	-0.046	-0.037	21.875	0.012	0.012	0.000	0.000	0.000	0.000
39	A	58	LEU	0	0.024	0.024	21.408	-0.013	-0.013	0.000	0.000	0.000	0.000
40	A	59	ASP	-1	-0.885	-0.948	15.245	-0.258	-0.258	0.000	0.000	0.000	0.000
41	A	60	GLY	0	0.011	-0.009	18.263	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	61	PHE	0	0.015	0.001	16.102	0.018	0.018	0.000	0.000	0.000	0.000
43	A	62	ALA	0	0.037	0.037	13.640	0.004	0.004	0.000	0.000	0.000	0.000
44	A	63	GLY	0	0.074	0.047	10.723	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	64	SER	0	-0.061	-0.052	6.876	-0.138	-0.138	0.000	0.000	0.000	0.000
46	A	65	GLY	0	0.054	0.031	8.252	-0.229	-0.229	0.000	0.000	0.000	0.000
47	A	66	SER	0	-0.026	-0.022	9.934	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	67	LEU	0	0.014	0.018	11.366	0.005	0.005	0.000	0.000	0.000	0.000
49	A	68	GLY	0	0.089	0.044	14.958	0.012	0.012	0.000	0.000	0.000	0.000
50	A	69	PHE	0	0.002	-0.027	10.608	0.000	0.000	0.000	0.000	0.000	0.000
51	A	70	GLU	-1	-0.840	-0.906	14.934	-0.418	-0.418	0.000	0.000	0.000	0.000
52	A	71	ALA	0	0.033	0.002	16.471	0.031	0.031	0.000	0.000	0.000	0.000
53	A	72	LEU	0	-0.020	-0.005	17.011	0.011	0.011	0.000	0.000	0.000	0.000
54	A	73	SER	0	-0.066	-0.071	17.475	0.021	0.021	0.000	0.000	0.000	0.000
55	A	74	ARG	1	0.805	0.890	18.685	0.268	0.268	0.000	0.000	0.000	0.000
56	A	75	GLN	0	-0.028	-0.019	22.412	0.032	0.032	0.000	0.000	0.000	0.000
57	A	76	ALA	0	0.016	0.019	22.923	0.022	0.022	0.000	0.000	0.000	0.000
58	A	77	LYS	1	0.910	0.984	24.647	0.130	0.130	0.000	0.000	0.000	0.000
59	A	78	LYS	1	0.946	0.959	24.295	0.184	0.184	0.000	0.000	0.000	0.000
60	A	79	VAL	0	-0.018	0.021	18.373	0.013	0.013	0.000	0.000	0.000	0.000
61	A	80	THR	0	0.005	0.005	21.258	-0.017	-0.017	0.000	0.000	0.000	0.000
62	A	81	PHE	0	-0.039	-0.042	14.689	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	82	LEU	0	-0.002	0.012	18.204	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	83	GLU	-1	-0.859	-0.944	13.562	-0.131	-0.131	0.000	0.000	0.000	0.000
65	A	84	LEU	0	0.001	0.007	16.745	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	85	ASP	-1	-0.813	-0.900	13.630	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	86	LYS	1	0.955	0.966	14.809	0.129	0.129	0.000	0.000	0.000	0.000
68	A	87	THR	0	-0.028	-0.024	10.739	-0.083	-0.083	0.000	0.000	0.000	0.000
69	A	88	VAL	0	0.014	0.018	9.551	-0.163	-0.163	0.000	0.000	0.000	0.000
70	A	89	ALA	0	0.031	0.017	11.329	-0.146	-0.146	0.000	0.000	0.000	0.000
71	A	90	ASN	0	-0.047	-0.036	13.609	-0.015	-0.015	0.000	0.000	0.000	0.000
72	A	91	GLN	0	-0.033	-0.008	7.734	0.186	0.186	0.000	0.000	0.000	0.000
73	A	92	LEU	0	0.020	0.015	11.099	-0.114	-0.114	0.000	0.000	0.000	0.000
74	A	93	LYS	1	0.988	0.990	12.662	0.317	0.317	0.000	0.000	0.000	0.000
75	A	94	LYS	1	0.969	0.990	10.002	1.313	1.313	0.000	0.000	0.000	0.000
76	A	95	ASN	0	0.019	-0.007	8.621	-0.033	-0.033	0.000	0.000	0.000	0.000
77	A	96	LEU	0	0.018	0.010	13.047	0.038	0.038	0.000	0.000	0.000	0.000
78	A	97	GLN	0	-0.078	-0.019	16.255	0.015	0.015	0.000	0.000	0.000	0.000
79	A	98	THR	0	-0.074	-0.030	13.109	-0.021	-0.021	0.000	0.000	0.000	0.000
80	A	99	LEU	0	-0.063	-0.038	13.824	0.039	0.039	0.000	0.000	0.000	0.000
81	A	100	LYS	1	0.908	0.947	17.470	0.413	0.413	0.000	0.000	0.000	0.000
82	A	101	CYS	0	0.015	0.023	19.242	0.016	0.016	0.000	0.000	0.000	0.000
83	A	102	SER	0	-0.026	-0.002	21.783	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	103	SER	0	0.038	0.000	23.698	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	104	GLU	-1	-0.879	-0.940	25.102	-0.201	-0.201	0.000	0.000	0.000	0.000
86	A	105	GLN	0	-0.045	-0.004	22.703	0.004	0.004	0.000	0.000	0.000	0.000
87	A	106	ALA	0	-0.015	-0.021	19.307	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	107	GLU	-1	-0.920	-0.954	21.082	-0.191	-0.191	0.000	0.000	0.000	0.000
89	A	108	VAL	0	-0.046	-0.015	16.776	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	109	ILE	0	-0.003	0.006	19.481	0.013	0.013	0.000	0.000	0.000	0.000
91	A	110	ASN	0	-0.042	-0.035	18.744	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	111	GLN	0	0.028	0.004	20.231	0.030	0.030	0.000	0.000	0.000	0.000
93	A	112	SER	0	0.067	0.051	20.326	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	113	SER	0	0.034	-0.026	20.753	-0.007	-0.007	0.000	0.000	0.000	0.000
95	A	114	LEU	0	-0.027	-0.008	22.876	0.001	0.001	0.000	0.000	0.000	0.000
96	A	115	ASP	-1	-0.902	-0.960	25.032	0.000	0.000	0.000	0.000	0.000	0.000
97	A	116	PHE	0	-0.005	-0.008	24.600	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	117	LEU	0	-0.015	-0.017	24.889	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	118	LYS	1	0.918	0.978	28.087	0.005	0.005	0.000	0.000	0.000	0.000
100	A	119	GLN	0	-0.001	0.022	30.710	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	120	PRO	0	0.021	0.017	32.616	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	121	GLN	0	-0.080	-0.045	31.711	-0.009	-0.009	0.000	0.000	0.000	0.000
103	A	122	ASN	0	0.018	0.007	35.014	0.006	0.006	0.000	0.000	0.000	0.000
104	A	123	GLN	0	-0.031	-0.012	35.980	0.005	0.005	0.000	0.000	0.000	0.000
105	A	124	PRO	0	0.047	0.044	33.415	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	125	HIS	1	0.787	0.870	28.965	0.091	0.091	0.000	0.000	0.000	0.000
107	A	126	PHE	0	-0.005	-0.004	25.280	-0.010	-0.010	0.000	0.000	0.000	0.000
108	A	127	ASP	-1	-0.810	-0.898	27.947	-0.104	-0.104	0.000	0.000	0.000	0.000
109	A	128	VAL	0	-0.001	-0.019	23.056	0.009	0.009	0.000	0.000	0.000	0.000
110	A	129	VAL	0	0.016	0.019	23.075	-0.012	-0.012	0.000	0.000	0.000	0.000
111	A	130	PHE	0	-0.041	-0.019	18.272	0.011	0.011	0.000	0.000	0.000	0.000
112	A	131	LEU	0	-0.007	-0.014	19.627	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	132	ASP	-1	-0.899	-0.960	14.285	-0.019	-0.019	0.000	0.000	0.000	0.000
114	A	133	PRO	0	-0.011	0.020	15.874	0.018	0.018	0.000	0.000	0.000	0.000
115	A	134	PRO	0	0.012	-0.008	15.412	0.022	0.022	0.000	0.000	0.000	0.000
116	A	135	PHE	0	0.016	0.005	17.556	-0.027	-0.027	0.000	0.000	0.000	0.000
117	A	136	HIS	0	-0.051	-0.043	20.397	0.006	0.006	0.000	0.000	0.000	0.000
118	A	137	PHE	0	0.029	0.024	21.920	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	138	ASN	0	0.004	-0.003	24.712	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	139	LEU	0	0.031	0.018	20.632	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	140	ALA	0	0.037	0.014	22.321	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	141	GLU	-1	-0.873	-0.941	23.829	0.026	0.026	0.000	0.000	0.000	0.000
123	A	142	GLN	0	-0.039	-0.025	26.458	-0.016	-0.016	0.000	0.000	0.000	0.000
124	A	143	ALA	0	-0.003	-0.003	24.176	-0.009	-0.009	0.000	0.000	0.000	0.000
125	A	144	ILE	0	-0.006	0.004	25.972	-0.012	-0.012	0.000	0.000	0.000	0.000
126	A	145	SER	0	0.011	0.011	28.375	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	146	LEU	0	0.023	0.014	27.713	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	147	LEU	0	-0.060	-0.025	25.832	-0.008	-0.008	0.000	0.000	0.000	0.000
129	A	148	CYS	0	-0.039	-0.021	29.954	-0.005	-0.005	0.000	0.000	0.000	0.000
130	A	149	GLU	-1	-0.940	-0.973	33.382	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	150	ASN	0	-0.068	-0.035	31.965	0.000	0.000	0.000	0.000	0.000	0.000
132	A	151	ASN	0	-0.014	-0.008	33.893	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	152	TRP	0	0.033	0.012	28.752	-0.014	-0.014	0.000	0.000	0.000	0.000
134	A	153	LEU	0	-0.028	-0.008	28.197	-0.012	-0.012	0.000	0.000	0.000	0.000
135	A	154	LYS	1	0.937	0.988	31.146	0.108	0.108	0.000	0.000	0.000	0.000
136	A	155	PRO	0	0.030	0.009	33.199	0.002	0.002	0.000	0.000	0.000	0.000
137	A	156	ASN	0	-0.020	-0.021	34.169	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	157	ALA	0	0.002	0.028	29.205	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	158	LEU	0	-0.024	-0.013	26.883	0.010	0.010	0.000	0.000	0.000	0.000
140	A	159	ILE	0	0.002	-0.009	25.247	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	160	TYR	0	-0.122	-0.121	18.048	0.008	0.008	0.000	0.000	0.000	0.000
142	A	161	VAL	0	0.022	0.006	21.822	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	162	GLU	-1	-0.823	-0.854	16.391	0.060	0.060	0.000	0.000	0.000	0.000
144	A	163	THR	0	-0.007	-0.020	20.384	0.006	0.006	0.000	0.000	0.000	0.000
145	A	164	GLU	-1	-0.816	-0.877	21.877	0.230	0.230	0.000	0.000	0.000	0.000
146	A	165	LYS	1	0.773	0.871	22.913	-0.196	-0.196	0.000	0.000	0.000	0.000
147	A	166	ASP	-1	-0.851	-0.916	24.747	0.127	0.127	0.000	0.000	0.000	0.000
148	A	167	LYS	1	0.860	0.896	28.223	-0.125	-0.125	0.000	0.000	0.000	0.000
149	A	168	PRO	0	-0.057	0.005	26.981	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	169	LEU	0	0.013	0.011	26.384	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	170	ILE	0	0.032	0.031	30.216	0.000	0.000	0.000	0.000	0.000	0.000
152	A	171	THR	0	-0.062	-0.032	32.556	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	172	PRO	0	0.045	0.046	31.858	0.001	0.001	0.000	0.000	0.000	0.000
154	A	173	GLU	-1	-0.913	-0.982	34.856	-0.005	-0.005	0.000	0.000	0.000	0.000
155	A	174	ASN	0	0.000	0.025	35.723	0.004	0.004	0.000	0.000	0.000	0.000
156	A	175	TRP	0	-0.002	-0.014	28.568	-0.005	-0.005	0.000	0.000	0.000	0.000
157	A	176	THR	0	0.001	-0.002	34.086	0.003	0.003	0.000	0.000	0.000	0.000
158	A	177	LEU	0	-0.012	-0.003	29.412	-0.005	-0.005	0.000	0.000	0.000	0.000
159	A	178	LEU	0	-0.008	0.003	30.326	0.001	0.001	0.000	0.000	0.000	0.000
160	A	179	LYS	1	0.833	0.893	27.350	0.017	0.017	0.000	0.000	0.000	0.000
161	A	180	GLU	-1	-0.793	-0.902	27.262	0.041	0.041	0.000	0.000	0.000	0.000
162	A	181	LYS	1	0.847	0.948	24.518	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	182	THR	0	0.095	0.048	24.323	0.001	0.001	0.000	0.000	0.000	0.000
164	A	183	THR	0	-0.055	-0.026	20.335	-0.009	-0.009	0.000	0.000	0.000	0.000
165	A	184	GLY	0	0.009	0.003	20.915	0.018	0.018	0.000	0.000	0.000	0.000
166	A	185	ILE	0	0.040	-0.022	17.573	-0.009	-0.009	0.000	0.000	0.000	0.000
167	A	186	VAL	0	0.025	0.031	17.489	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	187	SER	0	-0.018	-0.012	20.931	-0.010	-0.010	0.000	0.000	0.000	0.000
169	A	188	TYR	0	-0.038	-0.022	17.736	-0.001	-0.001	0.000	0.000	0.000	0.000
170	A	189	ARG	1	0.876	0.932	22.900	-0.054	-0.054	0.000	0.000	0.000	0.000
171	A	190	LEU	0	-0.019	-0.004	24.522	-0.010	-0.010	0.000	0.000	0.000	0.000
172	A	191	TYR	0	0.040	0.009	26.799	0.008	0.008	0.000	0.000	0.000	0.000
173	A	192	GLN	0	-0.022	-0.013	29.222	-0.014	-0.014	0.000	0.000	0.000	0.000
174	A	193	ASN	0	-0.059	-0.045	31.917	0.012	0.012	0.000	0.000	0.000	0.000
175	A	194	LEU	0	-0.037	-0.015	33.641	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	195	GLU	-1	-0.846	-0.914	36.281	-0.037	-0.037	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:GLY)