FMO DATABASE

FMODB ID: Y7V22

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	184
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1686578.96866
FMO2-HF: Nuclear repulsion	1617136.913991
FMO2-HF: Total energy	-69442.054669
FMO2-MP2: Total energy	-69651.535172

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:3:ILE)

Summations of interaction energy for fragment #1(A:3: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.
258.47	261.885	0.354	-1.553	-2.215	-0.014

Interaction energy analysis for fragmet #1(A:3:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.844 / q_NPA : 0.906

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	5	HIS	0	-0.008	0.000	2.791	-1.273	2.073	0.355	-1.549	-2.151	-0.014
4	A	6	THR	0	0.087	0.049	5.253	3.743	3.812	-0.001	-0.004	-0.064	0.000
5	A	7	SER	0	-0.051	-0.028	8.042	2.573	2.573	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.931	0.954	9.049	16.967	16.967	0.000	0.000	0.000	0.000
7	A	9	GLN	0	0.086	0.035	5.960	5.282	5.282	0.000	0.000	0.000	0.000
8	A	10	HIS	0	0.021	0.011	9.987	2.484	2.484	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.901	0.974	12.776	20.666	20.666	0.000	0.000	0.000	0.000
10	A	12	ARG	1	0.996	0.988	15.256	14.990	14.990	0.000	0.000	0.000	0.000
11	A	13	SER	0	0.057	0.009	18.594	-0.181	-0.181	0.000	0.000	0.000	0.000
12	A	14	SER	0	-0.007	0.013	20.894	0.127	0.127	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.035	-0.020	22.751	0.987	0.987	0.000	0.000	0.000	0.000
14	A	16	ARG	1	0.823	0.909	25.463	9.415	9.415	0.000	0.000	0.000	0.000
15	A	17	THR	0	0.074	0.031	25.064	0.071	0.071	0.000	0.000	0.000	0.000
16	A	18	ALA	0	0.052	0.033	27.558	0.201	0.201	0.000	0.000	0.000	0.000
17	A	19	PRO	0	-0.022	0.004	30.552	-0.115	-0.115	0.000	0.000	0.000	0.000
18	A	20	LYS	1	0.936	0.961	29.639	10.262	10.262	0.000	0.000	0.000	0.000
19	A	21	SER	0	-0.082	-0.057	33.017	0.210	0.210	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.777	-0.885	36.688	-8.473	-8.473	0.000	0.000	0.000	0.000
21	A	23	ASN	0	-0.073	-0.033	38.391	0.151	0.151	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.127	0.062	40.397	-0.124	-0.124	0.000	0.000	0.000	0.000
23	A	25	TYR	0	0.083	0.039	41.657	-0.132	-0.132	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.038	-0.016	37.729	-0.030	-0.030	0.000	0.000	0.000	0.000
25	A	27	LYS	1	0.993	0.989	34.804	8.603	8.603	0.000	0.000	0.000	0.000
26	A	28	LEU	0	-0.009	-0.004	38.389	-0.168	-0.168	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.027	0.016	40.641	-0.059	-0.059	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.005	-0.016	34.509	-0.100	-0.100	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.939	0.978	36.237	7.735	7.735	0.000	0.000	0.000	0.000
30	A	32	LEU	0	0.038	0.031	37.302	-0.091	-0.091	0.000	0.000	0.000	0.000
31	A	33	TYR	0	0.033	-0.025	37.100	-0.086	-0.086	0.000	0.000	0.000	0.000
32	A	34	ALA	0	-0.031	-0.025	32.944	-0.168	-0.168	0.000	0.000	0.000	0.000
33	A	35	PHE	0	-0.028	-0.010	33.734	-0.246	-0.246	0.000	0.000	0.000	0.000
34	A	36	LEU	0	0.066	0.034	35.820	-0.103	-0.103	0.000	0.000	0.000	0.000
35	A	37	ALA	0	-0.029	-0.007	32.962	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	38	ARG	1	0.935	0.977	30.382	9.163	9.163	0.000	0.000	0.000	0.000
37	A	39	ARG	1	0.963	0.981	32.726	7.969	7.969	0.000	0.000	0.000	0.000
38	A	40	THR	0	-0.051	-0.039	35.887	0.151	0.151	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.812	-0.895	32.201	-9.129	-9.129	0.000	0.000	0.000	0.000
40	A	42	ALA	0	0.027	0.026	34.999	0.033	0.033	0.000	0.000	0.000	0.000
41	A	43	PRO	0	0.020	-0.006	34.357	-0.159	-0.159	0.000	0.000	0.000	0.000
42	A	44	PHE	0	0.052	0.039	35.363	-0.149	-0.149	0.000	0.000	0.000	0.000
43	A	45	ASN	0	0.013	-0.011	36.564	0.016	0.016	0.000	0.000	0.000	0.000
44	A	46	LYS	1	0.858	0.921	30.352	9.220	9.220	0.000	0.000	0.000	0.000
45	A	47	VAL	0	-0.056	-0.008	32.619	-0.318	-0.318	0.000	0.000	0.000	0.000
46	A	48	ILE	0	0.038	0.023	35.005	-0.120	-0.120	0.000	0.000	0.000	0.000
47	A	49	LEU	0	0.033	0.034	30.725	-0.033	-0.033	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.929	0.960	28.469	10.033	10.033	0.000	0.000	0.000	0.000
49	A	51	SER	0	-0.087	-0.056	32.836	0.047	0.047	0.000	0.000	0.000	0.000
50	A	52	LEU	0	0.045	0.016	36.127	0.136	0.136	0.000	0.000	0.000	0.000
51	A	53	PHE	0	0.027	0.017	30.342	0.104	0.104	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.048	0.005	33.036	-0.144	-0.144	0.000	0.000	0.000	0.000
53	A	55	SER	0	0.022	0.003	34.988	0.210	0.210	0.000	0.000	0.000	0.000
54	A	56	LYS	1	1.037	1.003	36.573	7.101	7.101	0.000	0.000	0.000	0.000
55	A	57	ILE	0	0.005	0.005	37.252	0.116	0.116	0.000	0.000	0.000	0.000
56	A	58	ASN	0	-0.036	-0.027	34.042	0.023	0.023	0.000	0.000	0.000	0.000
57	A	59	ARG	1	0.893	0.958	37.464	7.886	7.886	0.000	0.000	0.000	0.000
58	A	60	PRO	0	-0.016	0.004	40.181	0.136	0.136	0.000	0.000	0.000	0.000
59	A	61	PRO	0	0.009	0.006	43.336	-0.034	-0.034	0.000	0.000	0.000	0.000
60	A	62	VAL	0	-0.018	-0.006	45.281	-0.018	-0.018	0.000	0.000	0.000	0.000
61	A	63	SER	0	-0.029	-0.011	47.879	0.024	0.024	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.068	0.028	51.501	-0.056	-0.056	0.000	0.000	0.000	0.000
63	A	65	SER	0	0.031	-0.010	53.939	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.897	0.963	46.289	6.665	6.665	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.009	0.003	50.038	-0.053	-0.053	0.000	0.000	0.000	0.000
66	A	68	SER	0	0.031	0.005	51.737	0.051	0.051	0.000	0.000	0.000	0.000
67	A	69	ARG	1	0.939	0.963	51.193	6.010	6.010	0.000	0.000	0.000	0.000
68	A	70	ALA	0	-0.008	-0.008	48.915	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.034	-0.003	50.526	-0.033	-0.033	0.000	0.000	0.000	0.000
70	A	72	LYS	1	0.921	0.954	53.565	5.484	5.484	0.000	0.000	0.000	0.000
71	A	73	GLN	0	-0.044	-0.008	47.337	-0.035	-0.035	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.789	-0.901	52.574	-5.616	-5.616	0.000	0.000	0.000	0.000
73	A	75	GLY	0	0.019	0.031	51.673	-0.133	-0.133	0.000	0.000	0.000	0.000
74	A	76	ALA	0	-0.091	-0.065	50.326	-0.121	-0.121	0.000	0.000	0.000	0.000
75	A	77	ALA	0	0.037	0.022	52.099	-0.035	-0.035	0.000	0.000	0.000	0.000
76	A	78	GLN	0	0.021	0.010	54.424	0.021	0.021	0.000	0.000	0.000	0.000
77	A	79	LYS	1	0.847	0.948	47.893	6.308	6.308	0.000	0.000	0.000	0.000
78	A	80	THR	0	0.008	0.008	48.741	0.036	0.036	0.000	0.000	0.000	0.000
79	A	81	ILE	0	0.009	0.008	47.897	-0.187	-0.187	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.012	-0.002	43.047	0.011	0.011	0.000	0.000	0.000	0.000
81	A	83	VAL	0	-0.008	-0.005	44.368	-0.134	-0.134	0.000	0.000	0.000	0.000
82	A	84	VAL	0	0.019	0.005	39.426	0.025	0.025	0.000	0.000	0.000	0.000
83	A	85	GLY	0	-0.011	-0.032	41.288	-0.208	-0.208	0.000	0.000	0.000	0.000
84	A	86	THR	0	-0.053	-0.013	43.796	0.057	0.057	0.000	0.000	0.000	0.000
85	A	87	VAL	0	0.057	0.030	47.410	-0.055	-0.055	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.023	-0.032	50.067	0.018	0.018	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.816	-0.910	52.569	-5.411	-5.411	0.000	0.000	0.000	0.000
88	A	90	ASP	-1	-0.809	-0.864	54.995	-5.835	-5.835	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.001	-0.010	57.113	-0.013	-0.013	0.000	0.000	0.000	0.000
90	A	92	ARG	1	0.877	0.914	53.471	5.794	5.794	0.000	0.000	0.000	0.000
91	A	93	ILE	0	-0.033	0.000	57.631	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	94	PHE	0	0.046	0.024	60.658	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.850	-0.932	63.261	-4.949	-4.949	0.000	0.000	0.000	0.000
94	A	96	PHE	0	-0.074	-0.048	55.215	-0.117	-0.117	0.000	0.000	0.000	0.000
95	A	97	PRO	0	0.009	0.009	57.498	0.065	0.065	0.000	0.000	0.000	0.000
96	A	98	LYS	1	0.990	0.998	58.796	4.897	4.897	0.000	0.000	0.000	0.000
97	A	99	THR	0	-0.010	-0.008	55.069	-0.064	-0.064	0.000	0.000	0.000	0.000
98	A	100	THR	0	-0.007	-0.003	52.461	0.026	0.026	0.000	0.000	0.000	0.000
99	A	101	VAL	0	-0.037	-0.025	50.330	-0.109	-0.109	0.000	0.000	0.000	0.000
100	A	102	ALA	0	0.042	0.025	47.441	0.040	0.040	0.000	0.000	0.000	0.000
101	A	103	ALA	0	-0.027	-0.015	46.811	-0.109	-0.109	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.050	-0.020	41.160	-0.024	-0.024	0.000	0.000	0.000	0.000
103	A	105	ARG	1	0.919	0.955	44.398	6.929	6.929	0.000	0.000	0.000	0.000
104	A	106	PHE	0	0.051	0.033	48.769	-0.035	-0.035	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.003	-0.005	52.085	0.012	0.012	0.000	0.000	0.000	0.000
106	A	108	ALA	0	0.066	0.025	54.450	0.015	0.015	0.000	0.000	0.000	0.000
107	A	109	GLY	0	0.070	0.046	58.050	0.067	0.067	0.000	0.000	0.000	0.000
108	A	110	ALA	0	-0.006	-0.012	54.438	0.038	0.038	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.958	0.978	53.999	5.804	5.804	0.000	0.000	0.000	0.000
110	A	112	ALA	0	0.048	0.032	57.354	0.039	0.039	0.000	0.000	0.000	0.000
111	A	113	LYS	1	0.869	0.941	58.896	5.303	5.303	0.000	0.000	0.000	0.000
112	A	114	ILE	0	-0.046	-0.028	54.215	0.018	0.018	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.014	-0.010	58.633	0.028	0.028	0.000	0.000	0.000	0.000
114	A	116	LYS	1	0.986	0.999	61.157	4.838	4.838	0.000	0.000	0.000	0.000
115	A	117	ALA	0	-0.030	0.000	61.176	0.075	0.075	0.000	0.000	0.000	0.000
116	A	118	GLY	0	0.042	0.024	63.317	0.031	0.031	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.017	-0.014	59.152	-0.029	-0.029	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.760	-0.848	55.922	-5.587	-5.587	0.000	0.000	0.000	0.000
119	A	121	ALA	0	-0.041	-0.016	54.230	-0.107	-0.107	0.000	0.000	0.000	0.000
120	A	122	ILE	0	-0.011	0.007	49.677	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	123	THR	0	-0.026	-0.040	48.252	-0.037	-0.037	0.000	0.000	0.000	0.000
122	A	124	LEU	0	0.015	-0.019	42.277	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	125	ASP	-1	-0.817	-0.870	44.928	-6.669	-6.669	0.000	0.000	0.000	0.000
124	A	126	GLN	0	0.066	0.021	46.190	0.090	0.090	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.034	-0.013	44.469	0.053	0.053	0.000	0.000	0.000	0.000
126	A	128	ALA	0	-0.027	-0.016	43.617	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	VAL	0	0.007	0.001	45.183	-0.033	-0.033	0.000	0.000	0.000	0.000
128	A	130	ARG	1	0.843	0.899	48.284	5.898	5.898	0.000	0.000	0.000	0.000
129	A	131	ALA	0	-0.017	-0.004	46.120	0.048	0.048	0.000	0.000	0.000	0.000
130	A	132	PRO	0	0.030	0.031	43.630	-0.200	-0.200	0.000	0.000	0.000	0.000
131	A	133	LYS	1	0.932	0.956	40.128	7.112	7.112	0.000	0.000	0.000	0.000
132	A	134	GLY	0	-0.023	-0.017	41.464	-0.131	-0.131	0.000	0.000	0.000	0.000
133	A	135	GLN	0	0.069	0.025	43.472	-0.102	-0.102	0.000	0.000	0.000	0.000
134	A	136	ASN	0	0.050	0.015	46.419	0.034	0.034	0.000	0.000	0.000	0.000
135	A	137	THR	0	-0.019	0.010	43.734	0.075	0.075	0.000	0.000	0.000	0.000
136	A	138	LEU	0	0.061	0.022	45.377	-0.057	-0.057	0.000	0.000	0.000	0.000
137	A	139	ILE	0	-0.021	-0.006	39.627	0.019	0.019	0.000	0.000	0.000	0.000
138	A	140	VAL	0	0.019	0.019	43.375	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	141	ARG	1	0.942	0.956	35.426	8.183	8.183	0.000	0.000	0.000	0.000
140	A	142	GLY	0	0.061	0.036	42.603	0.132	0.132	0.000	0.000	0.000	0.000
141	A	143	PRO	0	-0.013	-0.013	41.961	-0.215	-0.215	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.896	0.934	34.756	8.645	8.645	0.000	0.000	0.000	0.000
143	A	145	ALA	0	0.017	0.005	39.293	-0.088	-0.088	0.000	0.000	0.000	0.000
144	A	146	SER	0	-0.015	0.005	40.579	0.087	0.087	0.000	0.000	0.000	0.000
145	A	147	ARG	1	0.940	0.965	37.853	8.144	8.144	0.000	0.000	0.000	0.000
146	A	148	GLU	-1	-0.764	-0.877	43.460	-6.819	-6.819	0.000	0.000	0.000	0.000
147	A	149	ALA	0	0.000	0.008	39.928	-0.041	-0.041	0.000	0.000	0.000	0.000
148	A	150	ALA	0	-0.034	-0.015	39.309	-0.122	-0.122	0.000	0.000	0.000	0.000
149	A	151	ARG	1	0.908	0.939	40.304	6.583	6.583	0.000	0.000	0.000	0.000
150	A	152	HIS	0	-0.013	-0.020	41.240	0.049	0.049	0.000	0.000	0.000	0.000
151	A	153	PHE	0	-0.056	-0.030	35.594	-0.159	-0.159	0.000	0.000	0.000	0.000
152	A	154	GLY	0	0.058	0.031	36.223	0.055	0.055	0.000	0.000	0.000	0.000
153	A	155	PHE	0	-0.001	-0.005	36.938	0.129	0.129	0.000	0.000	0.000	0.000
154	A	156	GLY	0	0.053	0.032	39.051	-0.210	-0.210	0.000	0.000	0.000	0.000
155	A	157	PRO	0	0.059	0.039	40.600	0.120	0.120	0.000	0.000	0.000	0.000
156	A	158	HIS	0	0.007	-0.017	40.468	-0.377	-0.377	0.000	0.000	0.000	0.000
157	A	159	LYS	1	0.849	0.917	37.046	8.511	8.511	0.000	0.000	0.000	0.000
158	A	160	GLY	0	0.039	0.034	41.824	-0.006	-0.006	0.000	0.000	0.000	0.000
159	A	161	LYS	1	0.831	0.924	38.607	8.090	8.090	0.000	0.000	0.000	0.000
160	A	162	ALA	0	-0.018	-0.013	44.250	0.144	0.144	0.000	0.000	0.000	0.000
161	A	163	PRO	0	0.020	0.036	44.286	-0.200	-0.200	0.000	0.000	0.000	0.000
162	A	164	ARG	1	0.910	0.941	38.009	8.173	8.173	0.000	0.000	0.000	0.000
163	A	165	ILE	0	0.042	0.021	45.728	-0.003	-0.003	0.000	0.000	0.000	0.000
164	A	166	GLN	0	0.029	0.019	48.933	0.109	0.109	0.000	0.000	0.000	0.000
165	A	167	SER	0	0.013	0.007	51.281	0.144	0.144	0.000	0.000	0.000	0.000
166	A	168	THR	0	0.084	0.014	53.981	-0.065	-0.065	0.000	0.000	0.000	0.000
167	A	169	GLY	0	0.008	0.027	55.931	-0.036	-0.036	0.000	0.000	0.000	0.000
168	A	170	ARG	1	0.983	0.990	57.129	5.021	5.021	0.000	0.000	0.000	0.000
169	A	171	LYS	1	0.932	0.959	58.787	5.440	5.440	0.000	0.000	0.000	0.000
170	A	172	PHE	0	0.065	0.042	54.012	-0.014	-0.014	0.000	0.000	0.000	0.000
171	A	173	GLU	-1	-0.856	-0.933	48.414	-6.716	-6.716	0.000	0.000	0.000	0.000
172	A	174	ARG	1	0.873	0.934	52.734	5.890	5.890	0.000	0.000	0.000	0.000
173	A	175	ALA	0	0.034	0.006	54.847	0.107	0.107	0.000	0.000	0.000	0.000
174	A	176	ARG	1	1.006	0.994	48.716	6.421	6.421	0.000	0.000	0.000	0.000
175	A	177	GLY	0	0.069	0.054	50.580	-0.114	-0.114	0.000	0.000	0.000	0.000
176	A	178	ARG	1	0.839	0.922	48.469	6.431	6.431	0.000	0.000	0.000	0.000
177	A	179	ARG	1	0.868	0.925	52.979	5.630	5.630	0.000	0.000	0.000	0.000
178	A	180	ARG	1	1.067	1.036	54.697	5.741	5.741	0.000	0.000	0.000	0.000
179	A	181	SER	0	0.039	0.029	56.942	-0.024	-0.024	0.000	0.000	0.000	0.000
180	A	182	ARG	1	0.888	0.937	56.728	5.391	5.391	0.000	0.000	0.000	0.000
181	A	183	ALA	0	0.094	0.050	54.250	-0.128	-0.128	0.000	0.000	0.000	0.000
182	A	184	PHE	0	0.036	0.029	47.981	0.008	0.008	0.000	0.000	0.000	0.000
183	A	185	LYS	1	0.858	0.926	50.744	6.350	6.350	0.000	0.000	0.000	0.000
184	A	186	VAL	-1	-0.805	-0.887	45.411	-6.959	-6.959	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ILE)