FMO DATABASE

FMODB ID: 746LK

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	197
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1680009.691933
FMO2-HF: Nuclear repulsion	1603638.337275
FMO2-HF: Total energy	-76371.354658
FMO2-MP2: Total energy	-76600.80674

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:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
234.438	235.254	-0.004	-0.505	-0.307	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.865 / q_NPA : 0.915

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].
3	A	4	SER	0	-0.034	-0.028	3.837	-5.979	-5.163	-0.004	-0.505	-0.307
4	A	5	LYS	1	1.036	1.016	6.627	34.095	34.095	0.000	0.000	0.000
5	A	6	ASN	0	0.000	-0.001	10.268	-1.269	-1.269	0.000	0.000	0.000
6	A	7	LEU	0	0.059	0.041	9.207	0.949	0.949	0.000	0.000	0.000
7	A	8	PRO	0	0.008	0.017	11.380	-0.581	-0.581	0.000	0.000	0.000
8	A	9	ILE	0	0.027	0.003	9.699	-1.984	-1.984	0.000	0.000	0.000
9	A	10	LEU	0	-0.006	-0.003	9.111	2.012	2.012	0.000	0.000	0.000
10	A	11	LYS	1	0.936	0.969	9.742	16.499	16.499	0.000	0.000	0.000
11	A	12	ASN	0	0.039	0.013	10.118	3.015	3.015	0.000	0.000	0.000
12	A	13	HIS	0	-0.042	-0.020	11.626	-0.988	-0.988	0.000	0.000	0.000
13	A	14	PHE	0	0.006	-0.001	12.208	1.001	1.001	0.000	0.000	0.000
14	A	15	ARG	1	0.981	0.988	6.410	29.804	29.804	0.000	0.000	0.000
15	A	16	LYS	1	0.973	0.998	12.989	15.449	15.449	0.000	0.000	0.000
16	A	17	HIS	0	0.128	0.059	16.620	-0.850	-0.850	0.000	0.000	0.000
17	A	18	TRP	0	-0.004	-0.020	14.699	1.413	1.413	0.000	0.000	0.000
18	A	19	GLN	0	0.002	-0.003	17.695	0.713	0.713	0.000	0.000	0.000
19	A	20	GLU	-1	-0.883	-0.926	20.728	-12.078	-12.078	0.000	0.000	0.000
20	A	21	ARG	1	0.852	0.927	20.849	13.788	13.788	0.000	0.000	0.000
21	A	22	VAL	0	-0.012	0.007	21.537	0.026	0.026	0.000	0.000	0.000
22	A	23	LYS	1	0.893	0.946	24.089	10.227	10.227	0.000	0.000	0.000
23	A	24	VAL	0	0.037	0.022	25.486	-0.046	-0.046	0.000	0.000	0.000
24	A	25	HIS	0	0.030	0.024	28.001	0.565	0.565	0.000	0.000	0.000
25	A	26	PHE	0	0.086	0.026	28.380	0.220	0.220	0.000	0.000	0.000
26	A	27	ASP	-1	-0.815	-0.893	33.073	-8.678	-8.678	0.000	0.000	0.000
27	A	28	GLN	0	-0.021	-0.007	33.072	0.307	0.307	0.000	0.000	0.000
28	A	29	ALA	0	0.035	0.017	36.176	0.224	0.224	0.000	0.000	0.000
29	A	30	GLY	0	0.108	0.050	39.025	0.233	0.233	0.000	0.000	0.000
30	A	31	LYS	1	0.866	0.917	36.386	8.625	8.625	0.000	0.000	0.000
31	A	32	LYS	1	0.944	0.972	40.337	7.652	7.652	0.000	0.000	0.000
32	A	33	VAL	0	0.042	0.020	41.998	0.176	0.176	0.000	0.000	0.000
33	A	34	SER	0	0.040	0.020	43.455	0.197	0.197	0.000	0.000	0.000
34	A	35	ARG	1	0.906	0.943	37.515	8.015	8.015	0.000	0.000	0.000
35	A	36	ARG	1	0.912	0.961	45.265	6.573	6.573	0.000	0.000	0.000
36	A	37	HIS	0	0.101	0.061	48.052	0.124	0.124	0.000	0.000	0.000
37	A	38	ALA	0	0.039	0.028	47.553	0.127	0.127	0.000	0.000	0.000
38	A	39	ARG	1	0.886	0.948	44.994	6.755	6.755	0.000	0.000	0.000
39	A	40	ALA	0	0.066	0.040	50.993	0.101	0.101	0.000	0.000	0.000
40	A	41	SER	0	0.016	-0.002	52.257	0.104	0.104	0.000	0.000	0.000
41	A	42	LYS	1	0.835	0.913	49.511	6.329	6.329	0.000	0.000	0.000
42	A	43	ALA	0	0.037	0.007	54.755	0.079	0.079	0.000	0.000	0.000
43	A	44	ALA	0	0.082	0.040	56.892	0.088	0.088	0.000	0.000	0.000
44	A	45	LYS	1	0.913	0.960	56.614	5.501	5.501	0.000	0.000	0.000
45	A	46	ILE	0	-0.114	-0.056	56.729	0.040	0.040	0.000	0.000	0.000
46	A	47	ALA	0	0.057	0.035	59.965	0.071	0.071	0.000	0.000	0.000
47	A	48	PRO	0	0.060	0.046	61.934	-0.061	-0.061	0.000	0.000	0.000
48	A	49	ARG	1	0.896	0.951	58.437	5.235	5.235	0.000	0.000	0.000
49	A	50	PRO	0	0.032	0.020	57.060	-0.058	-0.058	0.000	0.000	0.000
50	A	51	LEU	0	-0.066	-0.042	51.884	-0.038	-0.038	0.000	0.000	0.000
51	A	52	ASP	-1	-0.942	-0.942	50.832	-6.204	-6.204	0.000	0.000	0.000
52	A	53	LEU	0	-0.011	-0.005	53.658	0.081	0.081	0.000	0.000	0.000
53	A	54	LEU	0	0.031	0.026	54.160	-0.154	-0.154	0.000	0.000	0.000
54	A	55	ARG	1	0.871	0.932	50.661	6.104	6.104	0.000	0.000	0.000
55	A	56	PRO	0	-0.055	0.013	52.707	0.034	0.034	0.000	0.000	0.000
56	A	57	VAL	0	0.080	0.025	52.456	-0.173	-0.173	0.000	0.000	0.000
57	A	58	VAL	0	-0.027	-0.019	48.339	0.051	0.051	0.000	0.000	0.000
58	A	59	ARG	1	0.936	0.968	48.902	6.108	6.108	0.000	0.000	0.000
59	A	60	ALA	0	-0.064	-0.022	43.693	-0.035	-0.035	0.000	0.000	0.000
60	A	61	PRO	0	0.070	0.018	42.783	0.043	0.043	0.000	0.000	0.000
61	A	62	THR	0	-0.009	-0.017	39.285	-0.215	-0.215	0.000	0.000	0.000
62	A	63	VAL	0	0.087	0.033	41.037	0.085	0.085	0.000	0.000	0.000
63	A	64	LYS	1	0.966	1.009	33.992	8.918	8.918	0.000	0.000	0.000
64	A	65	TYR	0	0.001	-0.017	36.516	-0.110	-0.110	0.000	0.000	0.000
65	A	66	ASN	0	0.053	0.051	42.470	0.039	0.039	0.000	0.000	0.000
66	A	67	ARG	1	0.997	0.995	40.717	7.521	7.521	0.000	0.000	0.000
67	A	68	LYS	1	0.888	0.965	42.894	7.181	7.181	0.000	0.000	0.000
68	A	69	VAL	0	0.039	0.015	46.735	-0.002	-0.002	0.000	0.000	0.000
69	A	70	ARG	1	0.876	0.929	44.419	6.763	6.763	0.000	0.000	0.000
70	A	71	ALA	0	0.096	0.059	47.608	0.109	0.109	0.000	0.000	0.000
71	A	72	GLY	0	-0.017	-0.012	47.690	-0.173	-0.173	0.000	0.000	0.000
72	A	73	ARG	1	0.936	0.967	47.654	6.370	6.370	0.000	0.000	0.000
73	A	74	GLY	0	0.050	-0.013	50.265	0.023	0.023	0.000	0.000	0.000
74	A	75	PHE	0	0.078	0.024	54.105	-0.072	-0.072	0.000	0.000	0.000
75	A	76	THR	0	-0.019	0.020	55.793	0.091	0.091	0.000	0.000	0.000
76	A	77	LEU	0	0.012	-0.016	58.021	0.051	0.051	0.000	0.000	0.000
77	A	78	ALA	0	-0.002	0.015	60.869	0.093	0.093	0.000	0.000	0.000
78	A	79	GLU	-1	-0.749	-0.891	57.529	-5.483	-5.483	0.000	0.000	0.000
79	A	80	ILE	0	0.006	-0.005	59.748	0.046	0.046	0.000	0.000	0.000
80	A	81	LYS	1	0.969	0.990	63.481	4.714	4.714	0.000	0.000	0.000
81	A	82	ALA	0	0.003	0.001	65.431	0.078	0.078	0.000	0.000	0.000
82	A	83	ALA	0	-0.009	0.001	64.901	0.051	0.051	0.000	0.000	0.000
83	A	84	GLY	0	0.033	0.036	66.937	0.033	0.033	0.000	0.000	0.000
84	A	85	LEU	0	-0.026	-0.005	64.811	0.035	0.035	0.000	0.000	0.000
85	A	86	THR	0	0.057	0.023	66.880	-0.062	-0.062	0.000	0.000	0.000
86	A	87	PRO	0	0.028	0.000	61.777	-0.043	-0.043	0.000	0.000	0.000
87	A	88	ALA	0	-0.001	-0.007	62.169	-0.080	-0.080	0.000	0.000	0.000
88	A	89	TYR	0	0.053	0.022	64.152	-0.037	-0.037	0.000	0.000	0.000
89	A	90	ALA	0	0.072	0.036	62.004	-0.029	-0.029	0.000	0.000	0.000
90	A	91	ARG	1	0.894	0.945	56.701	5.363	5.363	0.000	0.000	0.000
91	A	92	THR	0	-0.081	-0.046	60.965	-0.014	-0.014	0.000	0.000	0.000
92	A	93	ILE	0	0.033	0.032	63.672	0.008	0.008	0.000	0.000	0.000
93	A	94	GLY	0	0.044	0.034	59.587	-0.022	-0.022	0.000	0.000	0.000
94	A	95	ILE	0	0.014	0.020	58.544	-0.105	-0.105	0.000	0.000	0.000
95	A	96	ALA	0	-0.050	-0.012	53.978	-0.016	-0.016	0.000	0.000	0.000
96	A	97	VAL	0	0.008	0.012	56.108	-0.003	-0.003	0.000	0.000	0.000
97	A	98	ASP	-1	-0.919	-0.967	51.739	-6.162	-6.162	0.000	0.000	0.000
98	A	99	HIS	0	0.040	0.008	53.958	0.055	0.055	0.000	0.000	0.000
99	A	100	ARG	1	0.935	0.968	49.396	6.237	6.237	0.000	0.000	0.000
100	A	101	ARG	1	0.764	0.896	51.747	5.740	5.740	0.000	0.000	0.000
101	A	102	GLN	0	0.059	0.024	53.505	0.088	0.088	0.000	0.000	0.000
102	A	103	ASN	0	-0.046	-0.038	55.186	-0.085	-0.085	0.000	0.000	0.000
103	A	104	ARG	1	0.986	0.985	53.991	5.776	5.776	0.000	0.000	0.000
104	A	105	ASN	0	0.033	0.007	55.713	0.021	0.021	0.000	0.000	0.000
105	A	106	GLN	0	0.115	0.060	58.003	-0.081	-0.081	0.000	0.000	0.000
106	A	107	GLU	-1	-0.837	-0.912	58.105	-5.148	-5.148	0.000	0.000	0.000
107	A	108	ILE	0	-0.112	-0.056	53.632	-0.082	-0.082	0.000	0.000	0.000
108	A	109	LEU	0	-0.040	-0.018	57.236	-0.020	-0.020	0.000	0.000	0.000
109	A	110	ASP	-1	-0.787	-0.887	60.180	-4.869	-4.869	0.000	0.000	0.000
110	A	111	LEU	0	-0.025	-0.007	55.826	-0.008	-0.008	0.000	0.000	0.000
111	A	112	ASN	0	-0.074	-0.047	55.417	-0.062	-0.062	0.000	0.000	0.000
112	A	113	ILE	0	0.021	-0.006	59.348	0.031	0.031	0.000	0.000	0.000
113	A	114	GLN	0	0.006	0.001	62.778	0.102	0.102	0.000	0.000	0.000
114	A	115	ARG	1	0.822	0.912	54.504	5.711	5.711	0.000	0.000	0.000
115	A	116	LEU	0	-0.044	-0.025	60.386	-0.008	-0.008	0.000	0.000	0.000
116	A	117	LYS	1	0.952	0.990	62.944	4.740	4.740	0.000	0.000	0.000
117	A	118	GLU	-1	-0.867	-0.935	62.927	-5.041	-5.041	0.000	0.000	0.000
118	A	119	TYR	0	-0.079	-0.060	60.530	-0.022	-0.022	0.000	0.000	0.000
119	A	120	GLN	0	-0.050	-0.058	63.571	-0.038	-0.038	0.000	0.000	0.000
120	A	121	SER	0	-0.034	0.014	66.915	0.056	0.056	0.000	0.000	0.000
121	A	122	LYS	1	0.896	0.936	62.156	5.083	5.083	0.000	0.000	0.000
122	A	123	ILE	0	-0.061	-0.009	63.663	-0.021	-0.021	0.000	0.000	0.000
123	A	124	ILE	0	0.069	0.036	66.472	0.068	0.068	0.000	0.000	0.000
124	A	125	VAL	0	-0.051	-0.028	68.112	-0.067	-0.067	0.000	0.000	0.000
125	A	126	PHE	0	0.033	0.016	67.165	0.075	0.075	0.000	0.000	0.000
126	A	127	PRO	0	0.001	-0.006	70.908	-0.009	-0.009	0.000	0.000	0.000
127	A	128	ARG	1	0.955	0.960	69.151	4.501	4.501	0.000	0.000	0.000
128	A	129	LYS	1	0.962	0.985	73.480	3.972	3.972	0.000	0.000	0.000
129	A	130	GLY	0	0.068	0.038	75.897	0.043	0.043	0.000	0.000	0.000
130	A	131	LYS	1	0.900	0.966	74.999	4.185	4.185	0.000	0.000	0.000
131	A	132	ALA	0	0.081	0.036	71.001	-0.014	-0.014	0.000	0.000	0.000
132	A	133	PRO	0	-0.070	-0.041	72.921	0.011	0.011	0.000	0.000	0.000
133	A	134	GLU	-1	-0.906	-0.963	66.102	-4.839	-4.839	0.000	0.000	0.000
134	A	135	ALA	0	-0.005	-0.005	68.312	0.055	0.055	0.000	0.000	0.000
135	A	136	GLU	-1	-0.916	-0.943	63.432	-5.080	-5.080	0.000	0.000	0.000
136	A	137	GLN	0	-0.025	-0.012	59.318	-0.027	-0.027	0.000	0.000	0.000
137	A	138	THR	0	0.039	0.023	59.721	-0.049	-0.049	0.000	0.000	0.000
138	A	139	LEU	0	-0.002	-0.013	55.074	-0.082	-0.082	0.000	0.000	0.000
139	A	140	SER	0	-0.074	-0.063	52.506	-0.089	-0.089	0.000	0.000	0.000
140	A	141	ALA	0	0.089	0.040	54.907	0.054	0.054	0.000	0.000	0.000
141	A	142	ALA	0	-0.031	-0.026	51.425	0.034	0.034	0.000	0.000	0.000
142	A	143	ALA	0	-0.013	-0.005	53.501	-0.024	-0.024	0.000	0.000	0.000
143	A	144	SER	0	0.028	0.024	54.886	0.042	0.042	0.000	0.000	0.000
144	A	145	PHE	0	-0.010	0.000	56.494	0.069	0.069	0.000	0.000	0.000
145	A	146	PRO	0	0.072	0.051	53.214	-0.126	-0.126	0.000	0.000	0.000
146	A	147	ILE	0	-0.084	-0.052	50.056	0.051	0.051	0.000	0.000	0.000
147	A	148	VAL	0	0.047	0.025	51.202	-0.144	-0.144	0.000	0.000	0.000
148	A	149	GLN	0	-0.036	-0.027	48.477	-0.067	-0.067	0.000	0.000	0.000
149	A	150	PRO	0	-0.018	-0.023	52.278	0.046	0.046	0.000	0.000	0.000
150	A	151	VAL	0	0.064	0.041	54.448	-0.100	-0.100	0.000	0.000	0.000
151	A	152	THR	0	-0.074	-0.041	53.930	0.011	0.011	0.000	0.000	0.000
152	A	153	ASP	-1	-0.893	-0.950	56.458	-5.546	-5.546	0.000	0.000	0.000
153	A	154	SER	0	-0.034	-0.028	57.809	0.092	0.092	0.000	0.000	0.000
154	A	155	GLU	-1	-0.924	-0.931	58.495	-5.370	-5.370	0.000	0.000	0.000
155	A	156	THR	0	-0.019	-0.006	59.618	-0.006	-0.006	0.000	0.000	0.000
156	A	157	ARG	1	0.904	0.943	58.796	5.351	5.351	0.000	0.000	0.000
157	A	158	ALA	0	0.036	0.028	63.479	-0.009	-0.009	0.000	0.000	0.000
158	A	159	VAL	0	-0.032	-0.025	60.745	-0.091	-0.091	0.000	0.000	0.000
159	A	160	GLU	-1	-0.934	-0.968	62.733	-4.752	-4.752	0.000	0.000	0.000
160	A	161	ASP	-1	-0.946	-0.968	60.587	-5.379	-5.379	0.000	0.000	0.000
161	A	162	ASN	0	-0.019	-0.033	61.768	0.009	0.009	0.000	0.000	0.000
162	A	163	GLY	0	0.023	0.018	60.891	0.028	0.028	0.000	0.000	0.000
163	A	164	GLU	-1	-0.892	-0.922	58.159	-5.390	-5.390	0.000	0.000	0.000
164	A	165	SER	0	-0.013	-0.011	54.860	-0.147	-0.147	0.000	0.000	0.000
165	A	166	ALA	0	0.081	0.036	52.181	-0.063	-0.063	0.000	0.000	0.000
166	A	167	TYR	0	0.027	0.004	46.225	-0.141	-0.141	0.000	0.000	0.000
167	A	168	ARG	1	0.988	0.991	50.730	5.666	5.666	0.000	0.000	0.000
168	A	169	THR	0	0.070	0.035	53.302	-0.001	-0.001	0.000	0.000	0.000
169	A	170	LEU	0	-0.009	-0.009	47.810	-0.041	-0.041	0.000	0.000	0.000
170	A	171	ARG	1	0.883	0.942	44.705	6.662	6.662	0.000	0.000	0.000
171	A	172	LEU	0	0.024	0.044	49.850	-0.065	-0.065	0.000	0.000	0.000
172	A	173	ALA	0	0.087	0.048	51.292	-0.020	-0.020	0.000	0.000	0.000
173	A	174	ARG	1	0.904	0.942	42.433	7.011	7.011	0.000	0.000	0.000
174	A	175	SER	0	-0.066	-0.052	48.327	-0.114	-0.114	0.000	0.000	0.000
175	A	176	ASP	-1	-0.767	-0.874	50.336	-5.739	-5.739	0.000	0.000	0.000
176	A	177	LYS	1	0.906	0.961	45.775	6.602	6.602	0.000	0.000	0.000
177	A	178	ARG	1	0.830	0.921	43.368	6.815	6.815	0.000	0.000	0.000
178	A	179	TYR	0	0.028	-0.012	47.875	-0.051	-0.051	0.000	0.000	0.000
179	A	180	LYS	1	0.962	1.002	51.198	6.038	6.038	0.000	0.000	0.000
180	A	181	GLY	0	0.051	0.043	51.471	0.070	0.070	0.000	0.000	0.000
181	A	182	ILE	0	-0.033	-0.023	51.049	0.046	0.046	0.000	0.000	0.000
182	A	183	ARG	1	0.846	0.910	53.345	5.678	5.678	0.000	0.000	0.000
183	A	184	GLU	-1	-0.838	-0.947	54.918	-5.603	-5.603	0.000	0.000	0.000
184	A	185	LYS	1	0.785	0.880	54.021	5.648	5.648	0.000	0.000	0.000
185	A	186	ARG	1	0.899	0.938	53.884	5.695	5.695	0.000	0.000	0.000
186	A	187	ALA	0	0.066	0.053	58.983	0.048	0.048	0.000	0.000	0.000
187	A	188	LYS	1	0.988	0.996	57.810	5.403	5.403	0.000	0.000	0.000
188	A	189	ASP	-1	-0.819	-0.894	58.494	-5.375	-5.375	0.000	0.000	0.000
189	A	190	LYS	1	0.903	0.942	61.422	5.070	5.070	0.000	0.000	0.000
190	A	191	ALA	0	-0.022	-0.007	64.459	0.061	0.061	0.000	0.000	0.000
191	A	192	GLU	-1	-0.865	-0.924	65.347	-4.613	-4.613	0.000	0.000	0.000
192	A	193	ALA	0	-0.036	-0.039	65.340	-0.040	-0.040	0.000	0.000	0.000
193	A	194	GLU	-1	-1.004	-1.005	65.894	-4.612	-4.612	0.000	0.000	0.000
194	A	195	ALA	0	-0.018	-0.022	67.898	0.056	0.056	0.000	0.000	0.000
195	A	196	GLU	-1	-0.820	-0.897	68.624	-4.551	-4.551	0.000	0.000	0.000
196	A	197	LYS	1	0.853	0.935	70.138	4.542	4.542	0.000	0.000	0.000
197	A	198	LYS	0	-0.057	-0.002	69.234	0.390	0.390	0.000	0.000	0.000

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