FMO DATABASE

FMODB ID: LJ959

Calculation Name: 2IFT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1964662.837964
FMO2-HF: Nuclear repulsion	1894560.355512
FMO2-HF: Total energy	-70102.482453
FMO2-MP2: Total energy	-70309.690184

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: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.
1.441	5.84	1.48	-2.796	-3.082	-0.011

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 : 0.079 / 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	13	VAL	0	0.013	0.018	3.853	0.151	2.193	-0.014	-1.210	-0.817	0.004
4	A	14	ARG	1	0.845	0.901	7.373	0.606	0.606	0.000	0.000	0.000	0.000
5	A	15	ILE	0	0.017	0.029	10.480	0.109	0.109	0.000	0.000	0.000	0.000
6	A	16	ILE	0	0.004	-0.001	13.670	0.034	0.034	0.000	0.000	0.000	0.000
7	A	17	ALA	0	-0.012	-0.018	16.650	0.046	0.046	0.000	0.000	0.000	0.000
8	A	18	GLY	0	0.074	0.049	19.425	-0.035	-0.035	0.000	0.000	0.000	0.000
9	A	19	LEU	0	-0.002	-0.005	21.186	-0.019	-0.019	0.000	0.000	0.000	0.000
10	A	20	TRP	0	-0.012	-0.012	16.932	-0.038	-0.038	0.000	0.000	0.000	0.000
11	A	21	ARG	1	0.861	0.941	16.562	0.240	0.240	0.000	0.000	0.000	0.000
12	A	22	GLY	0	-0.004	-0.001	15.270	0.040	0.040	0.000	0.000	0.000	0.000
13	A	23	ARG	1	0.929	0.977	12.794	0.739	0.739	0.000	0.000	0.000	0.000
14	A	24	LYS	1	0.815	0.891	7.836	1.537	1.537	0.000	0.000	0.000	0.000
15	A	25	LEU	0	-0.001	0.000	8.271	0.234	0.234	0.000	0.000	0.000	0.000
16	A	26	PRO	0	0.024	0.027	4.850	-0.668	-0.668	0.000	0.000	0.000	0.000
17	A	27	VAL	0	0.008	0.014	3.104	1.580	2.195	0.066	-0.240	-0.440	0.000
18	A	28	LEU	0	0.005	0.009	2.393	-3.695	-1.953	1.428	-1.346	-1.825	-0.015
19	A	38	ASP	-1	-0.770	-0.841	17.262	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	39	ARG	1	0.872	0.895	18.822	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	40	VAL	0	-0.048	-0.036	22.301	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	41	LYS	1	0.879	0.926	15.449	0.115	0.115	0.000	0.000	0.000	0.000
23	A	42	GLU	-1	-0.813	-0.877	20.194	-0.241	-0.241	0.000	0.000	0.000	0.000
24	A	43	THR	0	-0.037	-0.029	22.226	0.001	0.001	0.000	0.000	0.000	0.000
25	A	44	LEU	0	0.025	0.032	22.094	0.004	0.004	0.000	0.000	0.000	0.000
26	A	45	PHE	0	0.033	0.004	18.571	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	46	ASN	0	-0.017	-0.016	24.298	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	47	TRP	0	-0.027	-0.018	27.371	0.007	0.007	0.000	0.000	0.000	0.000
29	A	48	LEU	0	0.054	0.032	24.409	0.003	0.003	0.000	0.000	0.000	0.000
30	A	49	MET	0	-0.030	-0.008	26.322	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	50	PRO	0	-0.047	-0.018	28.642	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	51	TYR	0	0.002	-0.005	30.732	0.005	0.005	0.000	0.000	0.000	0.000
33	A	52	ILE	0	-0.022	0.000	23.835	0.000	0.000	0.000	0.000	0.000	0.000
34	A	53	HIS	0	0.056	0.027	27.680	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	54	GLN	0	-0.087	-0.067	29.553	0.008	0.008	0.000	0.000	0.000	0.000
36	A	55	SER	0	-0.008	0.011	26.457	0.006	0.006	0.000	0.000	0.000	0.000
37	A	56	GLU	-1	-0.800	-0.874	26.690	-0.164	-0.164	0.000	0.000	0.000	0.000
38	A	57	CYS	0	-0.060	-0.033	22.453	0.012	0.012	0.000	0.000	0.000	0.000
39	A	58	LEU	0	0.021	0.019	21.414	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	59	ASP	-1	-0.848	-0.938	15.402	-0.354	-0.354	0.000	0.000	0.000	0.000
41	A	60	GLY	0	0.053	0.023	18.320	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	61	PHE	0	0.021	-0.001	16.279	0.034	0.034	0.000	0.000	0.000	0.000
43	A	62	ALA	0	0.037	0.046	13.734	0.006	0.006	0.000	0.000	0.000	0.000
44	A	63	GLY	0	0.089	0.057	10.557	-0.052	-0.052	0.000	0.000	0.000	0.000
45	A	64	SER	0	-0.066	-0.054	6.441	-0.181	-0.181	0.000	0.000	0.000	0.000
46	A	65	GLY	0	0.034	0.004	8.281	-0.259	-0.259	0.000	0.000	0.000	0.000
47	A	66	SER	0	-0.031	-0.023	9.795	0.004	0.004	0.000	0.000	0.000	0.000
48	A	67	LEU	0	0.025	0.019	11.621	0.018	0.018	0.000	0.000	0.000	0.000
49	A	68	GLY	0	0.084	0.034	15.238	0.027	0.027	0.000	0.000	0.000	0.000
50	A	69	PHE	0	-0.020	-0.032	10.703	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	70	GLU	-1	-0.758	-0.845	15.044	-0.443	-0.443	0.000	0.000	0.000	0.000
52	A	71	ALA	0	0.014	-0.001	16.579	0.040	0.040	0.000	0.000	0.000	0.000
53	A	72	LEU	0	-0.007	-0.002	17.437	0.018	0.018	0.000	0.000	0.000	0.000
54	A	73	SER	0	-0.037	-0.032	17.670	0.018	0.018	0.000	0.000	0.000	0.000
55	A	74	ARG	1	0.726	0.823	19.000	0.314	0.314	0.000	0.000	0.000	0.000
56	A	75	GLN	0	-0.045	-0.029	22.521	0.041	0.041	0.000	0.000	0.000	0.000
57	A	76	ALA	0	0.025	0.018	22.546	0.023	0.023	0.000	0.000	0.000	0.000
58	A	77	LYS	1	0.788	0.923	24.545	0.134	0.134	0.000	0.000	0.000	0.000
59	A	78	LYS	1	0.825	0.888	24.476	0.209	0.209	0.000	0.000	0.000	0.000
60	A	79	VAL	0	-0.041	-0.008	18.784	0.010	0.010	0.000	0.000	0.000	0.000
61	A	80	THR	0	-0.021	-0.030	21.065	-0.027	-0.027	0.000	0.000	0.000	0.000
62	A	81	PHE	0	-0.048	-0.028	14.709	0.002	0.002	0.000	0.000	0.000	0.000
63	A	82	LEU	0	-0.026	-0.003	18.382	0.006	0.006	0.000	0.000	0.000	0.000
64	A	83	GLU	-1	-0.823	-0.910	13.460	-0.156	-0.156	0.000	0.000	0.000	0.000
65	A	84	LEU	0	-0.009	-0.005	16.725	0.002	0.002	0.000	0.000	0.000	0.000
66	A	85	ASP	-1	-0.793	-0.888	13.087	0.018	0.018	0.000	0.000	0.000	0.000
67	A	86	LYS	1	0.943	0.970	14.567	0.094	0.094	0.000	0.000	0.000	0.000
68	A	87	THR	0	-0.033	-0.037	10.808	-0.062	-0.062	0.000	0.000	0.000	0.000
69	A	88	VAL	0	-0.004	0.007	9.551	-0.181	-0.181	0.000	0.000	0.000	0.000
70	A	89	ALA	0	0.024	0.013	11.181	-0.154	-0.154	0.000	0.000	0.000	0.000
71	A	90	ASN	0	-0.042	-0.030	13.039	-0.012	-0.012	0.000	0.000	0.000	0.000
72	A	91	GLN	0	-0.014	-0.017	6.676	0.316	0.316	0.000	0.000	0.000	0.000
73	A	92	LEU	0	0.009	0.013	10.587	-0.147	-0.147	0.000	0.000	0.000	0.000
74	A	93	LYS	1	0.953	0.978	12.672	0.305	0.305	0.000	0.000	0.000	0.000
75	A	94	LYS	1	0.880	0.940	9.675	1.399	1.399	0.000	0.000	0.000	0.000
76	A	95	ASN	0	0.007	-0.002	8.350	0.070	0.070	0.000	0.000	0.000	0.000
77	A	96	LEU	0	0.034	0.026	12.780	0.037	0.037	0.000	0.000	0.000	0.000
78	A	97	GLN	0	-0.031	-0.008	15.795	0.020	0.020	0.000	0.000	0.000	0.000
79	A	98	THR	0	-0.027	-0.018	12.525	-0.034	-0.034	0.000	0.000	0.000	0.000
80	A	99	LEU	0	-0.048	-0.020	14.672	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	100	LYS	1	0.834	0.908	17.285	0.433	0.433	0.000	0.000	0.000	0.000
82	A	101	CYS	0	0.027	0.045	19.073	0.024	0.024	0.000	0.000	0.000	0.000
83	A	102	SER	0	0.021	0.016	21.673	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	103	SER	0	0.049	0.005	23.838	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	104	GLU	-1	-0.879	-0.933	25.197	-0.209	-0.209	0.000	0.000	0.000	0.000
86	A	105	GLN	0	0.007	0.018	23.055	0.002	0.002	0.000	0.000	0.000	0.000
87	A	106	ALA	0	-0.018	-0.024	19.560	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	107	GLU	-1	-0.822	-0.868	20.839	-0.193	-0.193	0.000	0.000	0.000	0.000
89	A	108	VAL	0	-0.019	-0.011	16.279	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	109	ILE	0	-0.006	0.009	19.450	0.012	0.012	0.000	0.000	0.000	0.000
91	A	110	ASN	0	-0.070	-0.045	18.586	-0.031	-0.031	0.000	0.000	0.000	0.000
92	A	111	GLN	0	0.008	-0.005	20.333	0.031	0.031	0.000	0.000	0.000	0.000
93	A	112	SER	0	0.039	0.018	20.542	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	113	SER	0	0.036	-0.022	20.827	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	114	LEU	0	-0.004	0.015	22.555	0.002	0.002	0.000	0.000	0.000	0.000
96	A	115	ASP	-1	-0.862	-0.909	25.152	0.005	0.005	0.000	0.000	0.000	0.000
97	A	116	PHE	0	0.034	0.004	24.817	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	117	LEU	0	0.001	-0.005	25.130	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	118	LYS	1	0.836	0.904	28.297	0.009	0.009	0.000	0.000	0.000	0.000
100	A	119	GLN	0	-0.013	0.020	30.820	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	120	PRO	0	0.050	0.024	32.709	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	121	GLN	0	-0.057	-0.014	32.004	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	122	ASN	0	-0.002	-0.013	35.289	0.006	0.006	0.000	0.000	0.000	0.000
104	A	123	GLN	0	-0.030	-0.012	35.549	0.005	0.005	0.000	0.000	0.000	0.000
105	A	124	PRO	0	0.016	0.027	33.394	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	125	HIS	1	0.760	0.862	29.316	0.100	0.100	0.000	0.000	0.000	0.000
107	A	126	PHE	0	0.020	0.017	25.533	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	127	ASP	-1	-0.776	-0.865	28.336	-0.117	-0.117	0.000	0.000	0.000	0.000
109	A	128	VAL	0	0.006	-0.003	23.195	0.006	0.006	0.000	0.000	0.000	0.000
110	A	129	VAL	0	0.011	0.008	23.117	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	130	PHE	0	-0.040	-0.018	18.406	0.006	0.006	0.000	0.000	0.000	0.000
112	A	131	LEU	0	0.001	-0.007	19.936	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	132	ASP	-1	-0.867	-0.939	14.535	-0.103	-0.103	0.000	0.000	0.000	0.000
114	A	133	PRO	0	-0.006	0.019	15.978	0.021	0.021	0.000	0.000	0.000	0.000
115	A	134	PRO	0	-0.006	-0.020	15.586	0.019	0.019	0.000	0.000	0.000	0.000
116	A	135	PHE	0	0.015	0.017	17.771	-0.023	-0.023	0.000	0.000	0.000	0.000
117	A	136	HIS	0	-0.035	-0.028	20.510	0.014	0.014	0.000	0.000	0.000	0.000
118	A	137	PHE	0	-0.010	-0.008	21.566	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	138	ASN	0	-0.005	-0.014	24.808	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	139	LEU	0	0.018	0.017	19.928	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	140	ALA	0	0.037	0.014	22.309	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	141	GLU	-1	-0.794	-0.925	23.729	0.003	0.003	0.000	0.000	0.000	0.000
123	A	142	GLN	0	-0.034	-0.016	26.399	-0.009	-0.009	0.000	0.000	0.000	0.000
124	A	143	ALA	0	-0.003	0.003	24.260	-0.008	-0.008	0.000	0.000	0.000	0.000
125	A	144	ILE	0	-0.024	-0.010	25.920	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	145	SER	0	-0.011	-0.016	28.548	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	146	LEU	0	0.009	0.012	28.174	-0.006	-0.006	0.000	0.000	0.000	0.000
128	A	147	LEU	0	-0.025	-0.029	25.972	-0.008	-0.008	0.000	0.000	0.000	0.000
129	A	148	CYS	0	-0.047	-0.016	30.140	-0.006	-0.006	0.000	0.000	0.000	0.000
130	A	149	GLU	-1	-0.869	-0.925	33.671	-0.014	-0.014	0.000	0.000	0.000	0.000
131	A	150	ASN	0	-0.061	-0.027	32.394	0.001	0.001	0.000	0.000	0.000	0.000
132	A	151	ASN	0	-0.013	-0.013	34.133	-0.007	-0.007	0.000	0.000	0.000	0.000
133	A	152	TRP	0	0.033	0.012	28.356	-0.015	-0.015	0.000	0.000	0.000	0.000
134	A	153	LEU	0	-0.031	-0.006	28.467	-0.013	-0.013	0.000	0.000	0.000	0.000
135	A	154	LYS	1	0.831	0.885	31.278	0.129	0.129	0.000	0.000	0.000	0.000
136	A	155	PRO	0	0.041	0.012	33.615	0.002	0.002	0.000	0.000	0.000	0.000
137	A	156	ASN	0	-0.019	-0.023	34.554	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	157	ALA	0	-0.006	0.021	29.595	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	158	LEU	0	-0.023	-0.015	27.437	0.010	0.010	0.000	0.000	0.000	0.000
140	A	159	ILE	0	-0.007	-0.004	25.534	-0.013	-0.013	0.000	0.000	0.000	0.000
141	A	160	TYR	0	-0.069	-0.071	18.273	0.008	0.008	0.000	0.000	0.000	0.000
142	A	161	VAL	0	0.029	0.006	21.690	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	162	GLU	-1	-0.748	-0.839	16.538	-0.032	-0.032	0.000	0.000	0.000	0.000
144	A	163	THR	0	-0.019	-0.033	20.170	0.006	0.006	0.000	0.000	0.000	0.000
145	A	164	GLU	-1	-0.784	-0.871	21.768	0.172	0.172	0.000	0.000	0.000	0.000
146	A	165	LYS	1	0.793	0.876	23.119	-0.157	-0.157	0.000	0.000	0.000	0.000
147	A	166	ASP	-1	-0.815	-0.897	24.922	0.100	0.100	0.000	0.000	0.000	0.000
148	A	167	LYS	1	0.850	0.903	28.560	-0.106	-0.106	0.000	0.000	0.000	0.000
149	A	168	PRO	0	-0.039	0.000	26.627	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	169	LEU	0	-0.003	0.014	25.319	-0.002	-0.002	0.000	0.000	0.000	0.000
151	A	170	ILE	0	0.006	0.012	29.852	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	171	THR	0	-0.047	-0.034	32.550	-0.003	-0.003	0.000	0.000	0.000	0.000
153	A	172	PRO	0	0.035	0.031	32.110	0.003	0.003	0.000	0.000	0.000	0.000
154	A	173	GLU	-1	-0.930	-0.966	35.155	-0.014	-0.014	0.000	0.000	0.000	0.000
155	A	174	ASN	0	-0.024	-0.014	35.215	0.003	0.003	0.000	0.000	0.000	0.000
156	A	175	TRP	0	0.002	-0.007	28.445	-0.006	-0.006	0.000	0.000	0.000	0.000
157	A	176	THR	0	-0.012	-0.014	34.178	0.005	0.005	0.000	0.000	0.000	0.000
158	A	177	LEU	0	-0.017	-0.002	29.283	-0.007	-0.007	0.000	0.000	0.000	0.000
159	A	178	LEU	0	0.018	0.025	30.716	0.003	0.003	0.000	0.000	0.000	0.000
160	A	179	LYS	1	0.802	0.879	27.958	0.041	0.041	0.000	0.000	0.000	0.000
161	A	180	GLU	-1	-0.747	-0.853	27.424	0.015	0.015	0.000	0.000	0.000	0.000
162	A	181	LYS	1	0.853	0.932	24.665	0.029	0.029	0.000	0.000	0.000	0.000
163	A	182	THR	0	0.073	0.051	24.425	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	183	THR	0	-0.057	-0.025	20.940	-0.012	-0.012	0.000	0.000	0.000	0.000
165	A	184	GLY	0	0.008	0.004	21.246	0.012	0.012	0.000	0.000	0.000	0.000
166	A	185	ILE	0	0.013	-0.006	17.355	-0.003	-0.003	0.000	0.000	0.000	0.000
167	A	186	VAL	0	0.009	0.017	17.397	0.004	0.004	0.000	0.000	0.000	0.000
168	A	187	SER	0	-0.009	-0.014	20.873	-0.008	-0.008	0.000	0.000	0.000	0.000
169	A	188	TYR	0	-0.052	-0.027	17.652	0.000	0.000	0.000	0.000	0.000	0.000
170	A	189	ARG	1	0.836	0.894	22.831	-0.028	-0.028	0.000	0.000	0.000	0.000
171	A	190	LEU	0	-0.011	-0.003	24.509	-0.012	-0.012	0.000	0.000	0.000	0.000
172	A	191	TYR	0	0.029	0.006	26.790	0.007	0.007	0.000	0.000	0.000	0.000
173	A	192	GLN	0	-0.030	-0.015	29.265	-0.013	-0.013	0.000	0.000	0.000	0.000
174	A	193	ASN	0	-0.023	-0.030	32.011	0.012	0.012	0.000	0.000	0.000	0.000
175	A	194	LEU	0	-0.062	-0.034	33.715	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	195	GLU	-1	-0.823	-0.877	36.495	-0.046	-0.046	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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