FMO DATABASE

FMODB ID: G8721

Calculation Name: 1FNG-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-acetamido-2-deoxy-beta-d-glucopyranose

Ligand 3-letter code: NAG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1FNG

Chain ID: A

ChEMBL ID:

UniProt ID: P04224

Base Structure: X-ray

Registration Date: 2025-09-02

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	181
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1916119.819707
FMO2-HF: Nuclear repulsion	1842403.981574
FMO2-HF: Total energy	-73715.838132
FMO2-MP2: Total energy	-73933.143958

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:1:ILE)

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

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.
-196.789	-192.983	0.145	-1.59	-2.36	-0.009

Interaction energy analysis for fragmet #1(A:1:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.856 / q_NPA : 0.913

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	GLU	-1	-0.842	-0.901	3.034	-47.204	-43.471	0.146	-1.579	-2.299	-0.009
4	A	4	GLU	-1	-0.913	-0.947	4.589	-28.848	-28.775	-0.001	-0.011	-0.061	0.000
5	A	5	HIS	1	0.797	0.860	6.434	28.966	28.966	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.008	0.004	10.619	0.258	0.258	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.019	-0.008	14.204	0.068	0.068	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.015	-0.006	16.888	0.211	0.211	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.022	0.001	20.623	-0.057	-0.057	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.003	-0.006	23.642	0.128	0.128	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.776	-0.843	26.331	-9.822	-9.822	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.003	0.006	30.013	0.075	0.075	0.000	0.000	0.000	0.000
13	A	13	TYR	0	0.040	-0.004	33.537	0.160	0.160	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.016	0.029	37.249	-0.017	-0.017	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.090	-0.043	39.713	0.206	0.206	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.052	0.016	43.263	-0.056	-0.056	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.827	-0.935	41.943	-7.062	-7.062	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.872	0.936	43.008	6.450	6.450	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.952	0.988	38.475	7.212	7.212	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.031	0.012	36.430	-0.028	-0.028	0.000	0.000	0.000	0.000
21	A	21	GLU	0	-0.010	-0.021	29.531	0.125	0.125	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.016	0.003	26.858	-0.053	-0.053	0.000	0.000	0.000	0.000
23	A	23	MET	0	-0.034	-0.003	23.541	0.045	0.045	0.000	0.000	0.000	0.000
24	A	24	PHE	0	0.024	0.008	20.222	-0.164	-0.164	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.834	-0.921	19.145	-14.256	-14.256	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.010	-0.025	10.954	-0.617	-0.617	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.801	-0.882	11.670	-22.228	-22.228	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.039	0.035	15.216	0.016	0.016	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.920	-0.948	18.082	-13.717	-13.717	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.870	-0.938	19.700	-11.197	-11.197	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.017	-0.018	17.989	-0.123	-0.123	0.000	0.000	0.000	0.000
32	A	32	PHE	0	-0.019	-0.025	21.153	0.287	0.287	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.013	-0.011	24.827	0.149	0.149	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.042	-0.021	28.065	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.838	-0.916	31.189	-8.016	-8.016	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.034	-0.041	33.354	0.048	0.048	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.955	-0.972	36.584	-7.270	-7.270	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.845	0.933	37.708	8.059	8.059	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.052	-0.014	35.740	0.009	0.009	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.884	-0.945	33.921	-8.404	-8.404	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.027	-0.032	27.350	0.040	0.040	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.009	0.010	29.368	-0.056	-0.056	0.000	0.000	0.000	0.000
43	A	43	TRP	0	0.014	-0.005	21.777	-0.401	-0.401	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.883	0.955	23.082	11.578	11.578	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.000	0.001	20.437	0.241	0.241	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.907	-0.957	24.149	-10.214	-10.214	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.976	-0.991	19.847	-13.628	-13.628	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.035	0.012	18.463	-0.400	-0.400	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.032	0.023	21.779	-0.182	-0.182	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.825	0.922	21.340	13.091	13.091	0.000	0.000	0.000	0.000
51	A	51	PHE	0	-0.058	-0.036	18.737	-0.202	-0.202	0.000	0.000	0.000	0.000
52	A	52	ALA	0	-0.009	0.004	20.341	-0.405	-0.405	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.025	-0.012	22.280	0.555	0.555	0.000	0.000	0.000	0.000
54	A	54	PHE	0	0.046	0.011	24.848	-0.349	-0.349	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.952	-0.960	26.940	-8.810	-8.810	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.040	0.021	30.560	-0.011	-0.011	0.000	0.000	0.000	0.000
57	A	57	GLN	0	0.021	-0.009	32.331	0.227	0.227	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.019	0.014	31.362	0.136	0.136	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.028	0.018	30.445	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.003	0.003	32.020	0.144	0.144	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.024	-0.006	34.795	0.205	0.205	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.036	-0.030	30.156	0.274	0.274	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.021	0.012	33.015	0.150	0.150	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.033	-0.013	35.942	0.216	0.216	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.019	-0.010	35.879	0.206	0.206	0.000	0.000	0.000	0.000
66	A	66	ASP	0	-0.054	-0.078	32.724	0.123	0.123	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.904	0.963	36.825	7.082	7.082	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.030	-0.011	40.370	0.154	0.154	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.008	-0.007	36.155	0.273	0.273	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.003	0.012	39.682	0.075	0.075	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.907	-0.957	41.031	-6.717	-6.717	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.004	-0.002	42.523	0.112	0.112	0.000	0.000	0.000	0.000
73	A	73	MET	0	-0.020	-0.019	38.609	0.067	0.067	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.946	1.000	42.486	6.702	6.702	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.967	-0.969	45.359	-6.305	-6.305	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.911	0.952	39.880	7.599	7.599	0.000	0.000	0.000	0.000
77	A	77	SER	0	0.001	-0.008	44.072	0.033	0.033	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.054	-0.021	46.147	0.120	0.120	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.067	-0.052	47.477	0.041	0.041	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.022	-0.014	46.617	0.096	0.096	0.000	0.000	0.000	0.000
81	A	81	PRO	0	-0.048	-0.010	44.837	-0.141	-0.141	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.896	-0.948	40.704	-7.534	-7.534	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.054	-0.031	42.700	0.119	0.119	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.031	-0.011	41.099	-0.268	-0.268	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.018	-0.005	35.928	0.086	0.086	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.042	0.015	37.954	-0.119	-0.119	0.000	0.000	0.000	0.000
87	A	87	PRO	0	-0.010	0.005	35.622	-0.172	-0.172	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.833	-0.889	32.437	-9.242	-9.242	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.020	0.000	34.216	-0.177	-0.177	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.026	-0.008	31.007	0.201	0.201	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.004	-0.001	33.134	-0.115	-0.115	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.001	0.015	27.521	0.001	0.001	0.000	0.000	0.000	0.000
93	A	93	SER	0	0.017	0.006	31.072	0.074	0.074	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.946	0.974	24.593	10.887	10.887	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.047	-0.035	26.483	-0.492	-0.492	0.000	0.000	0.000	0.000
96	A	96	PRO	0	0.036	0.024	27.234	0.287	0.287	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.012	0.012	30.416	0.037	0.037	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.010	-0.001	32.622	0.165	0.165	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.014	0.003	36.237	0.043	0.043	0.000	0.000	0.000	0.000
100	A	100	GLY	0	-0.035	-0.012	39.893	0.026	0.026	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.900	-0.943	33.987	-8.738	-8.738	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.080	-0.049	34.865	-0.056	-0.056	0.000	0.000	0.000	0.000
103	A	103	ASN	0	-0.001	0.007	31.679	-0.420	-0.420	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.033	-0.029	29.885	0.127	0.127	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.017	0.030	31.781	-0.258	-0.258	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.026	-0.023	27.184	-0.059	-0.059	0.000	0.000	0.000	0.000
107	A	107	CYS	0	-0.056	-0.019	31.498	0.088	0.088	0.000	0.000	0.000	0.000
108	A	108	PHE	0	-0.018	-0.009	26.884	-0.129	-0.129	0.000	0.000	0.000	0.000
109	A	109	ILE	0	0.014	0.012	30.985	0.241	0.241	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.752	-0.889	28.687	-10.916	-10.916	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.777	0.875	29.636	10.197	10.197	0.000	0.000	0.000	0.000
112	A	112	PHE	0	0.027	0.032	32.030	0.234	0.234	0.000	0.000	0.000	0.000
113	A	113	SER	0	0.022	0.000	33.744	-0.203	-0.203	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.052	0.031	36.280	0.159	0.159	0.000	0.000	0.000	0.000
115	A	115	PRO	0	-0.033	-0.007	33.662	0.023	0.023	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.042	-0.033	35.583	0.033	0.033	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.005	-0.007	36.454	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	118	ASN	0	-0.048	0.004	39.310	-0.023	-0.023	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.027	0.002	37.044	-0.060	-0.060	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.055	-0.031	40.372	0.176	0.176	0.000	0.000	0.000	0.000
121	A	121	TRP	0	0.022	0.024	34.525	0.002	0.002	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.053	-0.030	41.230	0.203	0.203	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.957	0.980	41.183	6.985	6.985	0.000	0.000	0.000	0.000
124	A	124	ASN	0	-0.031	-0.025	44.854	0.109	0.109	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.021	0.006	47.164	0.176	0.176	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.837	0.920	48.150	6.197	6.197	0.000	0.000	0.000	0.000
127	A	127	PRO	0	0.042	0.012	45.811	-0.115	-0.115	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.064	-0.018	41.873	0.097	0.097	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.008	-0.033	42.396	-0.095	-0.095	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.895	-0.915	41.771	-7.063	-7.063	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.010	0.000	37.961	-0.037	-0.037	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.014	0.007	36.452	-0.210	-0.210	0.000	0.000	0.000	0.000
133	A	133	SER	0	-0.012	-0.010	32.102	-0.038	-0.038	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.879	-0.936	32.160	-8.376	-8.376	0.000	0.000	0.000	0.000
135	A	135	THR	0	-0.010	0.004	26.921	-0.133	-0.133	0.000	0.000	0.000	0.000
136	A	136	VAL	0	0.006	0.015	28.327	0.346	0.346	0.000	0.000	0.000	0.000
137	A	137	PHE	0	0.010	0.007	29.612	-0.171	-0.171	0.000	0.000	0.000	0.000
138	A	138	LEU	0	0.004	0.018	24.459	-0.117	-0.117	0.000	0.000	0.000	0.000
139	A	139	PRO	0	0.038	0.016	23.167	0.333	0.333	0.000	0.000	0.000	0.000
140	A	140	ARG	1	0.755	0.837	24.341	10.511	10.511	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.889	-0.942	21.120	-13.979	-13.979	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.852	-0.896	23.934	-10.491	-10.491	0.000	0.000	0.000	0.000
143	A	143	HIS	0	-0.022	-0.022	27.762	-0.280	-0.280	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.081	-0.022	29.782	0.383	0.383	0.000	0.000	0.000	0.000
145	A	145	PHE	0	-0.007	-0.018	29.128	-0.334	-0.334	0.000	0.000	0.000	0.000
146	A	146	ARG	1	0.809	0.908	21.995	12.671	12.671	0.000	0.000	0.000	0.000
147	A	147	LYS	1	0.745	0.861	29.346	8.850	8.850	0.000	0.000	0.000	0.000
148	A	148	PHE	0	0.023	0.011	24.782	0.028	0.028	0.000	0.000	0.000	0.000
149	A	149	HIS	0	0.073	0.042	30.265	0.055	0.055	0.000	0.000	0.000	0.000
150	A	150	TYR	0	0.002	-0.007	26.712	-0.248	-0.248	0.000	0.000	0.000	0.000
151	A	151	LEU	0	0.027	0.021	33.223	0.246	0.246	0.000	0.000	0.000	0.000
152	A	152	THR	0	-0.034	-0.021	34.978	-0.208	-0.208	0.000	0.000	0.000	0.000
153	A	153	PHE	0	-0.051	-0.036	34.341	0.263	0.263	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.007	0.010	37.204	-0.173	-0.173	0.000	0.000	0.000	0.000
155	A	155	PRO	0	-0.025	-0.004	36.687	0.184	0.184	0.000	0.000	0.000	0.000
156	A	156	SER	0	0.043	0.019	39.744	0.066	0.066	0.000	0.000	0.000	0.000
157	A	157	THR	0	0.036	0.008	43.009	-0.107	-0.107	0.000	0.000	0.000	0.000
158	A	158	ASP	-1	-0.991	-0.986	45.064	-6.234	-6.234	0.000	0.000	0.000	0.000
159	A	159	ASP	-1	-0.930	-0.947	43.615	-6.717	-6.717	0.000	0.000	0.000	0.000
160	A	160	PHE	0	-0.013	0.003	43.307	-0.049	-0.049	0.000	0.000	0.000	0.000
161	A	161	TYR	0	-0.001	-0.018	40.156	0.053	0.053	0.000	0.000	0.000	0.000
162	A	162	ASP	-1	-0.768	-0.877	41.359	-6.896	-6.896	0.000	0.000	0.000	0.000
163	A	164	GLU	-1	-0.901	-0.958	39.685	-6.653	-6.653	0.000	0.000	0.000	0.000
164	A	165	VAL	0	0.004	-0.012	37.476	-0.099	-0.099	0.000	0.000	0.000	0.000
165	A	166	ASP	-1	-0.851	-0.939	40.782	-6.717	-6.717	0.000	0.000	0.000	0.000
166	A	167	HIS	0	0.016	-0.005	38.371	-0.031	-0.031	0.000	0.000	0.000	0.000
167	A	168	TRP	0	-0.017	-0.003	42.217	0.173	0.173	0.000	0.000	0.000	0.000
168	A	169	GLY	0	0.000	-0.009	42.253	0.111	0.111	0.000	0.000	0.000	0.000
169	A	170	LEU	0	-0.081	-0.029	41.279	-0.050	-0.050	0.000	0.000	0.000	0.000
170	A	171	GLU	-1	-0.983	-0.985	44.711	-6.298	-6.298	0.000	0.000	0.000	0.000
171	A	172	GLU	-1	-0.977	-0.987	47.177	-6.108	-6.108	0.000	0.000	0.000	0.000
172	A	173	PRO	0	-0.008	-0.010	44.996	-0.155	-0.155	0.000	0.000	0.000	0.000
173	A	174	LEU	0	0.001	0.017	39.231	0.040	0.040	0.000	0.000	0.000	0.000
174	A	175	ARG	1	0.828	0.897	41.799	6.504	6.504	0.000	0.000	0.000	0.000
175	A	176	LYS	1	0.822	0.900	36.917	8.160	8.160	0.000	0.000	0.000	0.000
176	A	177	HIS	0	0.009	-0.020	40.097	-0.060	-0.060	0.000	0.000	0.000	0.000
177	A	178	TRP	0	-0.009	-0.012	35.208	-0.141	-0.141	0.000	0.000	0.000	0.000
178	A	179	GLU	-1	-0.858	-0.924	39.640	-6.792	-6.792	0.000	0.000	0.000	0.000
179	A	180	PHE	0	-0.014	-0.012	37.869	-0.180	-0.180	0.000	0.000	0.000	0.000
180	A	181	GLU	-1	-0.985	-0.990	37.595	-7.698	-7.698	0.000	0.000	0.000	0.000
181	A	182	GLU	-2	-1.950	-1.963	37.164	-15.742	-15.742	0.000	0.000	0.000	0.000

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