FMO DATABASE

FMODB ID: R4848

Calculation Name: 5IT7-A-Other547

Preferred Name:

Target Type:

Ligand Name: phosphomethylphosphonic acid guanylate ester | (2s)-1-amino-n,n,n-trimethyl-1-oxobutan-2-aminium

Ligand 3-letter code: GCP | 6EM

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5IT7

Chain ID: A

ChEMBL ID:

UniProt ID: P38665

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	202
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2315347.832155
FMO2-HF: Nuclear repulsion	2232877.531095
FMO2-HF: Total energy	-82470.301059
FMO2-MP2: Total energy	-82718.164291

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:2:GLY)

Summations of interaction energy for fragment #1(A:2: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.
468.569	470.256	0.188	-0.614	-1.261	-0.003

Interaction energy analysis for fragmet #1(A:2:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.943 / q_NPA : 0.960

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	4	TYR	0	-0.001	-0.017	3.837	7.890	8.684	-0.003	-0.286	-0.505	-0.001
4	A	5	LYS	1	0.933	0.964	4.262	39.467	39.594	-0.001	-0.025	-0.101	0.000
5	A	6	TYR	0	0.088	0.055	2.554	-0.842	-0.076	0.192	-0.303	-0.655	-0.002
6	A	7	LEU	0	-0.025	-0.025	7.200	6.131	6.131	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.945	-0.981	9.140	-25.671	-25.671	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.771	-0.868	9.978	-22.579	-22.579	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.026	0.033	11.227	2.116	2.116	0.000	0.000	0.000	0.000
10	A	11	GLN	0	-0.070	-0.046	13.074	3.304	3.304	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.835	0.897	12.845	23.918	23.918	0.000	0.000	0.000	0.000
12	A	13	LYS	1	1.024	1.030	16.162	19.688	19.688	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.840	0.917	18.168	15.127	15.127	0.000	0.000	0.000	0.000
14	A	15	GLN	0	-0.008	-0.005	20.703	0.618	0.618	0.000	0.000	0.000	0.000
15	A	16	SER	0	0.033	0.013	19.197	0.262	0.262	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.796	-0.901	21.554	-12.944	-12.944	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.050	0.023	17.310	0.259	0.259	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.032	-0.023	16.712	-0.060	-0.060	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.910	0.960	20.604	12.401	12.401	0.000	0.000	0.000	0.000
20	A	21	PHE	0	0.046	0.037	22.277	0.536	0.536	0.000	0.000	0.000	0.000
21	A	22	LEU	0	0.009	-0.008	17.918	0.225	0.225	0.000	0.000	0.000	0.000
22	A	23	GLN	0	-0.061	-0.029	22.148	0.411	0.411	0.000	0.000	0.000	0.000
23	A	24	ARG	1	1.024	1.011	24.006	11.249	11.249	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.075	0.048	24.656	0.407	0.407	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.956	0.973	17.643	16.584	16.584	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.098	-0.041	25.403	0.285	0.285	0.000	0.000	0.000	0.000
27	A	28	TRP	0	0.065	0.039	28.399	0.254	0.254	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.744	-0.866	24.298	-12.741	-12.741	0.000	0.000	0.000	0.000
29	A	30	TYR	0	-0.075	-0.063	22.524	0.045	0.045	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.885	0.954	29.222	9.822	9.822	0.000	0.000	0.000	0.000
31	A	32	GLN	0	0.065	0.045	32.386	0.447	0.447	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.865	0.940	26.295	11.844	11.844	0.000	0.000	0.000	0.000
33	A	34	ASN	0	0.074	0.024	32.261	0.232	0.232	0.000	0.000	0.000	0.000
34	A	35	VAL	0	-0.029	0.002	32.230	-0.352	-0.352	0.000	0.000	0.000	0.000
35	A	36	ILE	0	-0.015	-0.016	30.907	-0.289	-0.289	0.000	0.000	0.000	0.000
36	A	37	HIS	0	-0.013	-0.012	27.670	-0.102	-0.102	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.980	0.991	24.223	11.739	11.739	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.012	0.013	22.101	0.051	0.051	0.000	0.000	0.000	0.000
39	A	40	SER	0	0.035	0.010	22.232	-0.097	-0.097	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.991	0.989	16.292	16.467	16.467	0.000	0.000	0.000	0.000
41	A	42	PRO	0	-0.019	0.009	15.306	0.434	0.434	0.000	0.000	0.000	0.000
42	A	43	THR	0	0.035	0.000	16.237	-0.724	-0.724	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.862	0.936	14.596	17.786	17.786	0.000	0.000	0.000	0.000
44	A	45	PRO	0	0.055	0.026	11.014	-0.014	-0.014	0.000	0.000	0.000	0.000
45	A	46	ASP	-1	-0.730	-0.833	9.210	-28.643	-28.643	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.917	0.968	10.692	18.640	18.640	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.010	-0.005	14.204	1.038	1.038	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.933	0.980	8.650	29.473	29.473	0.000	0.000	0.000	0.000
49	A	50	ARG	1	0.837	0.894	11.213	25.772	25.772	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.110	-0.050	13.757	1.152	1.152	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.042	0.020	16.084	1.049	1.049	0.000	0.000	0.000	0.000
52	A	53	TYR	0	0.002	-0.008	14.922	0.203	0.203	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.929	0.959	13.022	18.992	18.992	0.000	0.000	0.000	0.000
54	A	55	ALA	0	-0.011	-0.003	14.840	0.763	0.763	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.895	0.959	16.584	14.057	14.057	0.000	0.000	0.000	0.000
56	A	57	GLN	0	0.099	0.044	19.771	-0.255	-0.255	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.050	0.021	23.532	0.011	0.011	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.037	-0.013	20.252	0.102	0.102	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.011	-0.005	22.317	-0.046	-0.046	0.000	0.000	0.000	0.000
60	A	61	ILE	0	-0.013	-0.009	18.897	-0.379	-0.379	0.000	0.000	0.000	0.000
61	A	62	TYR	0	0.029	0.007	22.750	0.355	0.355	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.797	0.900	21.365	13.365	13.365	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.011	-0.008	26.413	0.466	0.466	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.871	0.963	28.789	9.118	9.118	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.059	-0.040	31.254	0.345	0.345	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.998	0.998	33.553	8.045	8.045	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.846	0.922	30.791	9.811	9.811	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.042	0.025	36.083	0.200	0.200	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.007	-0.002	38.658	-0.329	-0.329	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.909	0.958	41.302	7.162	7.162	0.000	0.000	0.000	0.000
71	A	72	LYS	1	1.004	1.013	42.894	6.497	6.497	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.879	0.946	46.450	6.323	6.323	0.000	0.000	0.000	0.000
73	A	74	PRO	0	-0.033	-0.043	48.074	0.056	0.056	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.015	0.027	50.478	0.022	0.022	0.000	0.000	0.000	0.000
75	A	76	SER	0	0.088	0.049	54.157	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	77	LYS	1	1.005	0.991	56.452	5.291	5.291	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.027	0.003	55.020	0.011	0.011	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.018	0.015	56.022	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.084	-0.080	54.676	-0.060	-0.060	0.000	0.000	0.000	0.000
80	A	81	TYR	0	0.039	0.032	56.919	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.017	0.005	58.783	-0.058	-0.058	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.996	0.999	58.545	5.265	5.265	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.127	0.057	57.812	-0.133	-0.133	0.000	0.000	0.000	0.000
84	A	85	THR	0	0.016	0.019	53.291	-0.056	-0.056	0.000	0.000	0.000	0.000
85	A	86	ASN	0	-0.069	-0.041	53.135	-0.249	-0.249	0.000	0.000	0.000	0.000
86	A	87	GLN	0	0.066	0.033	54.167	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.012	0.031	51.345	-0.044	-0.044	0.000	0.000	0.000	0.000
88	A	89	VAL	0	0.014	-0.008	50.468	-0.082	-0.082	0.000	0.000	0.000	0.000
89	A	90	ASN	0	0.097	0.028	47.785	-0.178	-0.178	0.000	0.000	0.000	0.000
90	A	91	GLN	0	0.011	0.011	45.375	-0.123	-0.123	0.000	0.000	0.000	0.000
91	A	92	LEU	0	0.028	0.038	44.764	-0.136	-0.136	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.896	0.927	39.434	7.585	7.585	0.000	0.000	0.000	0.000
93	A	94	TYR	0	-0.017	-0.009	37.181	0.147	0.147	0.000	0.000	0.000	0.000
94	A	95	GLN	0	0.070	0.028	37.636	-0.361	-0.361	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.774	0.890	34.085	8.710	8.710	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.061	0.028	30.325	0.073	0.073	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.057	0.016	31.587	-0.031	-0.031	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.844	0.929	23.887	12.673	12.673	0.000	0.000	0.000	0.000
99	A	100	ALA	0	0.007	0.016	29.017	-0.088	-0.088	0.000	0.000	0.000	0.000
100	A	101	THR	0	0.006	-0.012	31.228	0.187	0.187	0.000	0.000	0.000	0.000
101	A	102	ALA	0	-0.007	0.000	28.982	0.165	0.165	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.721	-0.830	26.401	-11.658	-11.658	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.821	-0.908	29.535	-8.549	-8.549	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.949	0.978	33.262	8.969	8.969	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.003	-0.003	28.318	0.111	0.111	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.012	0.005	31.740	0.045	0.045	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.909	0.932	32.642	8.390	8.390	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.921	0.979	33.484	9.337	9.337	0.000	0.000	0.000	0.000
109	A	110	ALA	0	-0.016	-0.013	31.403	0.093	0.093	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.044	0.022	32.699	-0.233	-0.233	0.000	0.000	0.000	0.000
111	A	112	ASN	0	0.040	0.035	31.934	0.139	0.139	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.064	-0.032	27.162	-0.242	-0.242	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.841	0.923	28.263	9.955	9.955	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.007	-0.003	26.344	-0.478	-0.478	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.017	0.029	20.864	0.217	0.217	0.000	0.000	0.000	0.000
116	A	117	ASN	0	0.027	-0.007	21.266	0.449	0.449	0.000	0.000	0.000	0.000
117	A	118	SER	0	-0.041	-0.041	22.702	0.109	0.109	0.000	0.000	0.000	0.000
118	A	119	TYR	0	-0.075	-0.080	18.048	-0.606	-0.606	0.000	0.000	0.000	0.000
119	A	120	TRP	0	0.034	0.031	21.472	0.054	0.054	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.025	-0.010	20.950	-0.944	-0.944	0.000	0.000	0.000	0.000
121	A	122	ASN	0	0.053	0.016	22.283	-0.223	-0.223	0.000	0.000	0.000	0.000
122	A	123	GLN	0	-0.031	-0.025	25.112	0.434	0.434	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.652	-0.789	28.774	-9.975	-9.975	0.000	0.000	0.000	0.000
124	A	125	SER	0	0.059	0.033	31.906	-0.091	-0.091	0.000	0.000	0.000	0.000
125	A	126	THR	0	-0.004	-0.014	35.068	0.164	0.164	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.019	-0.029	32.341	0.196	0.196	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.879	0.948	28.912	10.352	10.352	0.000	0.000	0.000	0.000
128	A	129	TYR	0	-0.006	-0.020	26.317	0.200	0.200	0.000	0.000	0.000	0.000
129	A	130	PHE	0	-0.036	-0.033	24.735	-0.519	-0.519	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.685	-0.794	19.755	-15.262	-15.262	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.023	-0.023	22.499	-0.335	-0.335	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.032	0.003	19.266	-0.032	-0.032	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.005	-0.019	22.269	0.353	0.353	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.013	0.003	22.752	-0.503	-0.503	0.000	0.000	0.000	0.000
135	A	136	ASP	-1	-0.791	-0.885	25.343	-9.810	-9.810	0.000	0.000	0.000	0.000
136	A	137	PRO	0	-0.041	-0.005	28.271	-0.160	-0.160	0.000	0.000	0.000	0.000
137	A	138	SER	0	0.006	-0.024	30.316	0.213	0.213	0.000	0.000	0.000	0.000
138	A	139	HIS	0	0.025	0.011	26.164	-0.178	-0.178	0.000	0.000	0.000	0.000
139	A	140	LYS	1	1.023	0.990	28.637	8.893	8.893	0.000	0.000	0.000	0.000
140	A	141	ALA	0	0.062	0.035	23.775	-0.059	-0.059	0.000	0.000	0.000	0.000
141	A	142	ILE	0	-0.082	-0.033	23.519	-0.592	-0.592	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.918	0.945	25.536	9.298	9.298	0.000	0.000	0.000	0.000
143	A	144	ARG	1	0.991	1.028	27.242	10.284	10.284	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-0.790	-0.904	21.940	-13.392	-13.392	0.000	0.000	0.000	0.000
145	A	146	ALA	0	0.079	0.031	24.162	-0.224	-0.224	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.959	0.976	17.037	16.615	16.615	0.000	0.000	0.000	0.000
147	A	148	TYR	0	-0.042	-0.041	17.640	-0.772	-0.772	0.000	0.000	0.000	0.000
148	A	149	ASN	0	0.060	0.041	23.405	0.418	0.418	0.000	0.000	0.000	0.000
149	A	150	TRP	0	0.024	0.023	22.912	0.590	0.590	0.000	0.000	0.000	0.000
150	A	151	ILE	0	-0.052	-0.030	25.473	0.394	0.394	0.000	0.000	0.000	0.000
151	A	152	CYS	0	0.017	-0.012	27.870	0.324	0.324	0.000	0.000	0.000	0.000
152	A	153	ASN	0	0.029	0.044	30.729	0.533	0.533	0.000	0.000	0.000	0.000
153	A	154	PRO	0	0.080	0.042	33.331	-0.164	-0.164	0.000	0.000	0.000	0.000
154	A	155	VAL	0	0.048	0.020	33.554	0.017	0.017	0.000	0.000	0.000	0.000
155	A	156	HIS	0	-0.021	-0.003	29.913	-0.198	-0.198	0.000	0.000	0.000	0.000
156	A	157	LYS	1	0.998	1.004	31.823	7.811	7.811	0.000	0.000	0.000	0.000
157	A	158	HIS	0	0.018	0.001	33.585	0.242	0.242	0.000	0.000	0.000	0.000
158	A	159	ARG	1	0.853	0.931	25.916	11.523	11.523	0.000	0.000	0.000	0.000
159	A	160	GLU	-1	-0.803	-0.904	30.154	-9.663	-9.663	0.000	0.000	0.000	0.000
160	A	161	ALA	0	0.016	0.017	31.642	0.084	0.084	0.000	0.000	0.000	0.000
161	A	162	ARG	1	0.866	0.925	34.671	8.935	8.935	0.000	0.000	0.000	0.000
162	A	163	GLY	0	-0.010	0.000	32.496	0.063	0.063	0.000	0.000	0.000	0.000
163	A	164	LEU	0	-0.010	-0.014	30.745	-0.041	-0.041	0.000	0.000	0.000	0.000
164	A	165	THR	0	-0.021	-0.018	26.945	-0.284	-0.284	0.000	0.000	0.000	0.000
165	A	166	ALA	0	0.018	0.003	24.112	0.233	0.233	0.000	0.000	0.000	0.000
166	A	167	THR	0	0.020	0.004	26.168	0.178	0.178	0.000	0.000	0.000	0.000
167	A	168	GLY	0	0.004	0.031	28.186	0.371	0.371	0.000	0.000	0.000	0.000
168	A	169	LYS	1	0.983	0.987	28.094	11.142	11.142	0.000	0.000	0.000	0.000
169	A	170	LYS	1	1.005	1.007	28.022	10.774	10.774	0.000	0.000	0.000	0.000
170	A	171	SER	0	-0.049	-0.045	30.752	0.243	0.243	0.000	0.000	0.000	0.000
171	A	172	ARG	1	0.855	0.932	33.537	9.377	9.377	0.000	0.000	0.000	0.000
172	A	173	GLY	0	0.030	0.033	34.212	0.249	0.249	0.000	0.000	0.000	0.000
173	A	174	ILE	0	-0.067	-0.031	32.332	0.114	0.114	0.000	0.000	0.000	0.000
174	A	175	ASN	0	-0.037	-0.020	28.727	-0.345	-0.345	0.000	0.000	0.000	0.000
175	A	176	LYS	1	0.994	0.987	30.183	10.537	10.537	0.000	0.000	0.000	0.000
176	A	177	GLY	0	0.071	0.034	33.555	-0.196	-0.196	0.000	0.000	0.000	0.000
177	A	178	HIS	0	0.115	0.046	36.055	-0.063	-0.063	0.000	0.000	0.000	0.000
178	A	179	LYS	1	0.913	0.970	34.645	8.956	8.956	0.000	0.000	0.000	0.000
179	A	180	PHE	0	-0.089	-0.043	32.688	-0.100	-0.100	0.000	0.000	0.000	0.000
180	A	181	HIS	0	0.124	0.070	37.625	0.038	0.038	0.000	0.000	0.000	0.000
181	A	182	ASN	0	0.044	0.015	41.063	0.004	0.004	0.000	0.000	0.000	0.000
182	A	183	THR	0	-0.111	-0.071	37.753	0.130	0.130	0.000	0.000	0.000	0.000
183	A	184	GLN	0	0.094	0.053	36.869	0.026	0.026	0.000	0.000	0.000	0.000
184	A	185	ALA	0	0.024	0.013	36.429	-0.211	-0.211	0.000	0.000	0.000	0.000
185	A	186	GLY	0	-0.005	-0.020	38.490	-0.088	-0.088	0.000	0.000	0.000	0.000
186	A	187	ARG	1	0.960	0.985	39.552	7.498	7.498	0.000	0.000	0.000	0.000
187	A	188	ARG	1	0.948	0.974	42.079	7.372	7.372	0.000	0.000	0.000	0.000
188	A	189	LYS	1	0.994	1.015	41.661	7.661	7.661	0.000	0.000	0.000	0.000
189	A	190	THR	0	-0.023	-0.021	42.300	0.108	0.108	0.000	0.000	0.000	0.000
190	A	191	TRP	0	0.046	0.034	44.985	0.049	0.049	0.000	0.000	0.000	0.000
191	A	192	LYS	1	1.001	0.993	47.645	6.413	6.413	0.000	0.000	0.000	0.000
192	A	193	ARG	1	0.941	0.982	44.335	7.054	7.054	0.000	0.000	0.000	0.000
193	A	194	GLN	0	-0.023	-0.023	47.191	-0.045	-0.045	0.000	0.000	0.000	0.000
194	A	195	ASN	0	-0.003	0.000	50.851	-0.027	-0.027	0.000	0.000	0.000	0.000
195	A	196	THR	0	-0.043	-0.021	52.557	0.096	0.096	0.000	0.000	0.000	0.000
196	A	197	LEU	0	0.039	0.026	54.706	-0.048	-0.048	0.000	0.000	0.000	0.000
197	A	198	SER	0	-0.041	-0.028	54.991	0.051	0.051	0.000	0.000	0.000	0.000
198	A	199	LEU	0	0.003	0.007	57.211	0.063	0.063	0.000	0.000	0.000	0.000
199	A	200	TRP	0	0.028	0.023	55.186	-0.057	-0.057	0.000	0.000	0.000	0.000
200	A	201	ARG	1	0.908	0.948	61.458	5.034	5.034	0.000	0.000	0.000	0.000
201	A	202	TYR	0	0.057	0.032	64.308	0.047	0.047	0.000	0.000	0.000	0.000
202	A	203	ARG	0	0.049	0.028	63.896	-0.128	-0.128	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:GLY)