FMO DATABASE

FMODB ID: LGKJ9

Calculation Name: 6E3A-A-Xray547

Preferred Name:

Target Type:

Ligand Name: coenzyme a | [[(2~{r},3~{s},4~{r},5~{r})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{r},3~{s},4~{r},5~{r})-3,4-bis(oxidanyl)-5-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate

Ligand 3-letter code: COA | HQG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6E3A

Chain ID: A

ChEMBL ID:

UniProt ID: A3DJX6

Base Structure: X-ray

Registration Date: 2025-10-04

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	180
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1976104.814527
FMO2-HF: Nuclear repulsion	1904120.457124
FMO2-HF: Total energy	-71984.357403
FMO2-MP2: Total energy	-72198.63361

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:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
77.99	80.034	0.007	-0.757	-1.293	-0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.881 / q_NPA : 0.929

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	ASP	-1	-0.802	-0.886	3.520	-31.235	-29.522	0.009	-0.734	-0.987	-0.002
4	A	6	TYR	0	0.062	-0.010	4.486	2.221	2.431	-0.001	-0.008	-0.201	0.000
49	A	51	LYS	1	0.881	0.947	4.462	46.167	46.288	-0.001	-0.015	-0.105	0.000
5	A	7	SER	0	-0.009	0.008	7.864	3.779	3.779	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.834	0.889	9.586	31.346	31.346	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.051	0.040	9.322	1.738	1.738	0.000	0.000	0.000	0.000
8	A	10	SER	0	0.038	0.008	11.269	2.483	2.483	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.883	0.945	13.574	21.322	21.322	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.785	-0.853	14.359	-18.867	-18.867	0.000	0.000	0.000	0.000
11	A	13	VAL	0	0.068	0.022	14.720	1.114	1.114	0.000	0.000	0.000	0.000
12	A	14	ALA	0	-0.055	-0.016	17.121	1.095	1.095	0.000	0.000	0.000	0.000
13	A	15	TYR	0	-0.013	-0.014	19.215	1.077	1.077	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.057	0.026	19.754	0.784	0.784	0.000	0.000	0.000	0.000
15	A	17	LEU	0	0.004	0.001	19.895	0.622	0.622	0.000	0.000	0.000	0.000
16	A	18	ARG	1	0.790	0.903	21.253	14.017	14.017	0.000	0.000	0.000	0.000
17	A	19	HIS	0	-0.053	-0.050	23.175	0.218	0.218	0.000	0.000	0.000	0.000
18	A	20	ALA	0	0.062	0.031	24.853	0.496	0.496	0.000	0.000	0.000	0.000
19	A	21	PRO	0	0.012	0.025	24.603	-0.361	-0.361	0.000	0.000	0.000	0.000
20	A	22	TRP	0	0.082	0.026	25.444	-0.209	-0.209	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.968	-0.969	24.333	-11.907	-11.907	0.000	0.000	0.000	0.000
22	A	24	TYR	0	-0.094	-0.066	18.414	-0.294	-0.294	0.000	0.000	0.000	0.000
23	A	25	GLY	0	0.028	0.031	23.167	-0.252	-0.252	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.084	-0.038	21.287	0.085	0.085	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.916	-0.964	25.971	-9.464	-9.464	0.000	0.000	0.000	0.000
26	A	28	LEU	0	-0.094	-0.039	25.073	-0.292	-0.292	0.000	0.000	0.000	0.000
27	A	29	ASP	-1	-0.734	-0.874	28.635	-10.155	-10.155	0.000	0.000	0.000	0.000
28	A	30	ALA	0	0.033	0.003	31.160	-0.130	-0.130	0.000	0.000	0.000	0.000
29	A	31	GLU	-1	-0.913	-0.953	30.863	-9.438	-9.438	0.000	0.000	0.000	0.000
30	A	32	GLY	0	-0.033	-0.023	27.817	-0.279	-0.279	0.000	0.000	0.000	0.000
31	A	33	TRP	0	-0.044	-0.035	24.346	-0.828	-0.828	0.000	0.000	0.000	0.000
32	A	34	VAL	0	0.022	0.018	22.328	0.424	0.424	0.000	0.000	0.000	0.000
33	A	35	ASP	-1	-0.795	-0.909	23.199	-13.492	-13.492	0.000	0.000	0.000	0.000
34	A	36	ILE	0	-0.002	-0.009	16.958	-0.453	-0.453	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.002	-0.002	18.618	-1.545	-1.545	0.000	0.000	0.000	0.000
36	A	38	GLN	0	0.004	0.002	19.987	-0.425	-0.425	0.000	0.000	0.000	0.000
37	A	39	LEU	0	0.009	0.013	17.291	-0.366	-0.366	0.000	0.000	0.000	0.000
38	A	40	LEU	0	-0.038	-0.034	13.638	-1.017	-1.017	0.000	0.000	0.000	0.000
39	A	41	SER	0	0.010	0.009	16.260	-0.837	-0.837	0.000	0.000	0.000	0.000
40	A	42	SER	0	0.027	-0.006	18.450	-0.405	-0.405	0.000	0.000	0.000	0.000
41	A	43	LEU	0	-0.069	-0.038	13.548	-0.668	-0.668	0.000	0.000	0.000	0.000
42	A	44	HIS	1	0.783	0.894	12.412	20.903	20.903	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.810	-0.888	15.487	-15.210	-15.210	0.000	0.000	0.000	0.000
44	A	46	CYS	0	-0.080	-0.033	14.619	-0.511	-0.511	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.809	-0.899	11.866	-24.372	-24.372	0.000	0.000	0.000	0.000
46	A	48	LYS	1	0.887	0.946	9.377	21.126	21.126	0.000	0.000	0.000	0.000
47	A	49	TRP	0	-0.080	-0.080	7.547	-6.773	-6.773	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.911	0.957	10.496	20.105	20.105	0.000	0.000	0.000	0.000
50	A	52	VAL	0	-0.059	-0.007	8.344	-1.917	-1.917	0.000	0.000	0.000	0.000
51	A	53	SER	0	0.015	-0.025	9.294	3.486	3.486	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.791	-0.928	11.333	-16.835	-16.835	0.000	0.000	0.000	0.000
53	A	55	HIS	0	0.030	0.018	9.102	1.781	1.781	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.798	-0.865	6.911	-37.174	-37.174	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.005	-0.001	9.707	-0.195	-0.195	0.000	0.000	0.000	0.000
56	A	58	HIS	0	0.020	0.009	13.040	0.906	0.906	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.006	0.001	8.045	0.553	0.553	0.000	0.000	0.000	0.000
58	A	60	MET	0	-0.070	-0.026	10.477	-0.070	-0.070	0.000	0.000	0.000	0.000
59	A	61	ILE	0	-0.059	-0.025	11.284	0.997	0.997	0.000	0.000	0.000	0.000
60	A	62	GLU	-1	-0.812	-0.884	12.384	-20.986	-20.986	0.000	0.000	0.000	0.000
61	A	63	LYS	1	0.801	0.878	8.748	23.943	23.943	0.000	0.000	0.000	0.000
62	A	64	SER	0	-0.056	-0.029	12.011	-0.361	-0.361	0.000	0.000	0.000	0.000
63	A	65	ASP	-1	-0.826	-0.903	14.487	-15.588	-15.588	0.000	0.000	0.000	0.000
64	A	66	LYS	1	0.870	0.934	16.959	14.994	14.994	0.000	0.000	0.000	0.000
65	A	67	LYS	1	1.011	1.039	18.440	11.743	11.743	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.794	0.881	16.587	17.485	17.485	0.000	0.000	0.000	0.000
67	A	69	TYR	0	0.007	-0.020	15.996	0.830	0.830	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.845	-0.918	20.284	-11.958	-11.958	0.000	0.000	0.000	0.000
69	A	71	ILE	0	0.023	0.009	16.764	0.073	0.073	0.000	0.000	0.000	0.000
70	A	72	SER	0	-0.013	-0.008	21.350	0.206	0.206	0.000	0.000	0.000	0.000
71	A	73	ASN	0	0.008	0.006	24.450	-0.057	-0.057	0.000	0.000	0.000	0.000
72	A	74	GLY	0	0.074	0.049	22.156	0.267	0.267	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.857	0.943	22.775	10.963	10.963	0.000	0.000	0.000	0.000
74	A	76	ILE	0	-0.005	-0.010	17.792	-0.326	-0.326	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.841	0.945	22.022	11.398	11.398	0.000	0.000	0.000	0.000
76	A	78	ALA	0	-0.020	-0.008	22.099	-0.584	-0.584	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.016	-0.002	23.150	0.524	0.524	0.000	0.000	0.000	0.000
78	A	80	TYR	0	0.004	-0.011	21.966	0.450	0.450	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.005	0.002	24.790	-0.586	-0.586	0.000	0.000	0.000	0.000
80	A	82	HIS	0	0.037	0.032	26.343	0.072	0.072	0.000	0.000	0.000	0.000
81	A	83	SER	0	-0.007	-0.004	28.069	0.140	0.140	0.000	0.000	0.000	0.000
82	A	84	ILE	0	-0.006	0.030	28.555	0.185	0.185	0.000	0.000	0.000	0.000
83	A	85	PRO	0	0.032	0.012	31.263	0.141	0.141	0.000	0.000	0.000	0.000
84	A	86	GLN	0	0.043	0.037	33.926	0.299	0.299	0.000	0.000	0.000	0.000
85	A	87	ARG	1	0.827	0.896	33.551	7.991	7.991	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.009	0.010	29.634	0.089	0.089	0.000	0.000	0.000	0.000
87	A	89	ILE	0	0.007	0.008	33.024	0.196	0.196	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.840	0.921	28.830	10.061	10.061	0.000	0.000	0.000	0.000
89	A	91	GLU	-1	-0.803	-0.891	34.067	-8.614	-8.614	0.000	0.000	0.000	0.000
90	A	92	GLN	0	0.000	-0.011	35.878	-0.021	-0.021	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.839	0.912	34.064	8.873	8.873	0.000	0.000	0.000	0.000
92	A	94	CYS	0	-0.004	0.017	38.977	0.067	0.067	0.000	0.000	0.000	0.000
93	A	95	PRO	0	-0.041	-0.015	38.546	-0.196	-0.196	0.000	0.000	0.000	0.000
94	A	96	PRO	0	0.022	-0.002	36.450	0.175	0.175	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.925	-0.963	39.778	-6.848	-6.848	0.000	0.000	0.000	0.000
96	A	98	VAL	0	-0.020	-0.016	38.373	0.073	0.073	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.026	0.000	34.517	-0.228	-0.228	0.000	0.000	0.000	0.000
98	A	100	TYR	0	0.047	0.020	33.539	0.130	0.130	0.000	0.000	0.000	0.000
99	A	101	HIS	0	-0.036	-0.035	32.885	-0.243	-0.243	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.014	0.033	31.815	0.224	0.224	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.004	-0.016	31.705	-0.306	-0.306	0.000	0.000	0.000	0.000
102	A	104	ALA	0	-0.009	-0.009	32.536	-0.042	-0.042	0.000	0.000	0.000	0.000
103	A	105	ARG	1	0.911	0.912	34.196	8.795	8.795	0.000	0.000	0.000	0.000
104	A	106	ARG	1	0.867	0.928	31.233	9.608	9.608	0.000	0.000	0.000	0.000
105	A	107	PHE	0	-0.021	-0.016	32.792	0.008	0.008	0.000	0.000	0.000	0.000
106	A	108	VAL	0	0.033	0.022	38.475	0.130	0.130	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.960	0.998	40.611	6.727	6.727	0.000	0.000	0.000	0.000
108	A	110	SER	0	0.032	0.001	41.085	0.112	0.112	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.019	-0.005	37.130	0.018	0.018	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.944	0.991	41.713	6.996	6.996	0.000	0.000	0.000	0.000
111	A	113	GLU	-1	-0.918	-0.953	45.076	-6.552	-6.552	0.000	0.000	0.000	0.000
112	A	114	LYS	1	0.932	0.967	43.413	7.194	7.194	0.000	0.000	0.000	0.000
113	A	115	GLY	0	0.062	0.041	43.137	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.063	-0.022	36.232	-0.142	-0.142	0.000	0.000	0.000	0.000
115	A	117	GLN	0	0.023	0.002	38.184	0.006	0.006	0.000	0.000	0.000	0.000
116	A	118	PRO	0	0.038	0.009	35.092	-0.206	-0.206	0.000	0.000	0.000	0.000
117	A	119	GLN	0	-0.062	-0.032	33.893	-0.227	-0.227	0.000	0.000	0.000	0.000
118	A	120	GLY	0	0.021	0.024	31.966	0.088	0.088	0.000	0.000	0.000	0.000
119	A	121	ARG	1	0.738	0.864	25.188	11.072	11.072	0.000	0.000	0.000	0.000
120	A	122	GLN	0	0.027	0.007	31.739	0.255	0.255	0.000	0.000	0.000	0.000
121	A	123	TYR	0	-0.022	-0.019	32.357	0.311	0.311	0.000	0.000	0.000	0.000
122	A	124	VAL	0	-0.016	0.007	33.076	-0.279	-0.279	0.000	0.000	0.000	0.000
123	A	125	HIS	0	-0.031	-0.032	27.880	-0.524	-0.524	0.000	0.000	0.000	0.000
124	A	126	LEU	0	0.002	0.011	31.701	0.138	0.138	0.000	0.000	0.000	0.000
125	A	127	SER	0	-0.049	-0.037	29.484	-0.476	-0.476	0.000	0.000	0.000	0.000
126	A	128	ALA	0	0.048	0.029	30.402	0.296	0.296	0.000	0.000	0.000	0.000
127	A	129	ASP	-1	-0.786	-0.851	28.522	-10.237	-10.237	0.000	0.000	0.000	0.000
128	A	130	VAL	0	0.076	0.027	31.081	-0.181	-0.181	0.000	0.000	0.000	0.000
129	A	131	GLU	-1	-0.822	-0.889	26.397	-10.747	-10.747	0.000	0.000	0.000	0.000
130	A	132	THR	0	-0.095	-0.106	25.597	-0.547	-0.547	0.000	0.000	0.000	0.000
131	A	133	ALA	0	0.014	0.012	27.269	-0.220	-0.220	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.027	0.007	29.611	-0.088	-0.088	0.000	0.000	0.000	0.000
133	A	135	GLN	0	-0.044	-0.040	24.134	-0.352	-0.352	0.000	0.000	0.000	0.000
134	A	136	VAL	0	-0.068	-0.020	25.497	-0.487	-0.487	0.000	0.000	0.000	0.000
135	A	137	GLY	0	0.051	0.036	27.234	-0.083	-0.083	0.000	0.000	0.000	0.000
136	A	138	LYS	1	0.936	0.953	25.877	10.797	10.797	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.823	0.915	23.100	11.869	11.869	0.000	0.000	0.000	0.000
138	A	140	ARG	1	0.905	0.964	25.620	10.370	10.370	0.000	0.000	0.000	0.000
139	A	141	ASP	-1	-0.742	-0.851	28.966	-8.729	-8.729	0.000	0.000	0.000	0.000
140	A	142	ILE	0	0.076	0.047	28.448	-0.151	-0.151	0.000	0.000	0.000	0.000
141	A	143	LYS	1	0.897	0.948	30.559	8.392	8.392	0.000	0.000	0.000	0.000
142	A	144	PRO	0	-0.044	-0.004	30.244	0.228	0.228	0.000	0.000	0.000	0.000
143	A	145	VAL	0	0.011	-0.002	33.290	0.128	0.128	0.000	0.000	0.000	0.000
144	A	146	LEU	0	0.004	0.001	33.987	-0.223	-0.223	0.000	0.000	0.000	0.000
145	A	147	LEU	0	-0.024	-0.003	36.148	0.201	0.201	0.000	0.000	0.000	0.000
146	A	148	ILE	0	0.008	-0.003	37.235	-0.257	-0.257	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.002	0.001	38.442	0.191	0.191	0.000	0.000	0.000	0.000
148	A	150	ASN	0	0.065	0.033	40.761	-0.218	-0.218	0.000	0.000	0.000	0.000
149	A	151	ALA	0	-0.007	-0.011	39.563	0.102	0.102	0.000	0.000	0.000	0.000
150	A	152	LEU	0	0.037	0.025	41.639	0.048	0.048	0.000	0.000	0.000	0.000
151	A	153	GLU	-1	-0.814	-0.893	44.242	-6.327	-6.327	0.000	0.000	0.000	0.000
152	A	154	ALA	0	0.034	0.010	43.295	0.084	0.084	0.000	0.000	0.000	0.000
153	A	155	TRP	0	-0.011	-0.011	42.736	0.058	0.058	0.000	0.000	0.000	0.000
154	A	156	SER	0	-0.079	-0.041	44.974	0.110	0.110	0.000	0.000	0.000	0.000
155	A	157	GLU	-1	-0.788	-0.847	48.229	-6.047	-6.047	0.000	0.000	0.000	0.000
156	A	158	GLY	0	0.035	0.033	47.635	0.036	0.036	0.000	0.000	0.000	0.000
157	A	159	ILE	0	-0.086	-0.045	41.559	-0.112	-0.112	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.872	0.946	40.684	7.109	7.109	0.000	0.000	0.000	0.000
159	A	161	PHE	0	0.044	-0.004	37.390	-0.186	-0.186	0.000	0.000	0.000	0.000
160	A	162	TYR	0	-0.045	-0.056	34.610	0.107	0.107	0.000	0.000	0.000	0.000
161	A	163	LEU	0	0.012	0.014	30.392	-0.164	-0.164	0.000	0.000	0.000	0.000
162	A	164	GLY	0	0.014	0.007	28.990	-0.149	-0.149	0.000	0.000	0.000	0.000
163	A	165	ASN	0	-0.080	-0.063	23.965	-0.082	-0.082	0.000	0.000	0.000	0.000
164	A	166	ASP	-1	-0.838	-0.915	27.537	-10.444	-10.444	0.000	0.000	0.000	0.000
165	A	167	LYS	1	0.897	0.951	23.673	12.061	12.061	0.000	0.000	0.000	0.000
166	A	168	VAL	0	-0.078	-0.029	25.263	0.124	0.124	0.000	0.000	0.000	0.000
167	A	169	TRP	0	0.078	0.042	28.435	0.078	0.078	0.000	0.000	0.000	0.000
168	A	170	LEU	0	-0.031	-0.020	29.695	-0.174	-0.174	0.000	0.000	0.000	0.000
169	A	171	ALA	0	0.038	0.025	33.269	0.210	0.210	0.000	0.000	0.000	0.000
170	A	172	ASP	-1	-0.743	-0.839	36.492	-8.085	-8.085	0.000	0.000	0.000	0.000
171	A	173	ALA	0	-0.016	-0.023	39.198	-0.073	-0.073	0.000	0.000	0.000	0.000
172	A	174	ILE	0	0.011	0.012	38.039	0.129	0.129	0.000	0.000	0.000	0.000
173	A	175	PRO	0	0.019	0.005	42.074	-0.043	-0.043	0.000	0.000	0.000	0.000
174	A	176	SER	0	0.023	-0.030	44.798	-0.053	-0.053	0.000	0.000	0.000	0.000
175	A	177	LYS	1	0.812	0.907	45.829	6.167	6.167	0.000	0.000	0.000	0.000
176	A	178	TYR	0	-0.023	-0.031	44.155	-0.013	-0.013	0.000	0.000	0.000	0.000
177	A	179	ILE	0	-0.076	-0.033	40.732	-0.187	-0.187	0.000	0.000	0.000	0.000
178	A	180	ARG	1	0.950	0.980	42.968	7.182	7.182	0.000	0.000	0.000	0.000
179	A	181	PHE	0	-0.041	-0.063	41.632	-0.268	-0.268	0.000	0.000	0.000	0.000
180	A	182	GLU	-2	-1.878	-1.918	42.958	-13.718	-13.718	0.000	0.000	0.000	0.000

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