FMO DATABASE

FMODB ID: 2RN3R

Calculation Name: 3K2C-B-Xray547

Preferred Name:

Target Type:

Ligand Name: 1-methoxy-2-[2-(2-methoxy-ethoxy]-ethane | 1,2-ethanediol

Ligand 3-letter code: PG5 | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3K2C

Chain ID: B

ChEMBL ID:

UniProt ID: Q8SRE1

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	175
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1832234.927352
FMO2-HF: Nuclear repulsion	1763626.112308
FMO2-HF: Total energy	-68608.815044
FMO2-MP2: Total energy	-68806.414233

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:-5:THR)

Summations of interaction energy for fragment #1(A:-5:THR)

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.
-31.226	-28.386	0.241	-1.529	-1.552	-0.014

Interaction energy analysis for fragmet #1(A:-5:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.851 / q_NPA : 0.910

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	GLY	0	0.050	0.020	2.878	-2.858	-0.017	0.242	-1.528	-1.556	-0.014
4	A	-2	PRO	0	-0.007	0.014	5.277	-0.982	-0.983	-0.001	-0.001	0.004	0.000
5	A	-1	GLY	0	0.024	0.012	7.914	-1.631	-1.631	0.000	0.000	0.000	0.000
6	A	0	SER	0	-0.026	-0.010	9.593	0.878	0.878	0.000	0.000	0.000	0.000
7	A	1	MET	0	0.002	0.002	12.602	0.021	0.021	0.000	0.000	0.000	0.000
8	A	2	ALA	0	0.002	0.005	15.464	-0.661	-0.661	0.000	0.000	0.000	0.000
9	A	3	LYS	1	0.974	0.980	17.355	12.835	12.835	0.000	0.000	0.000	0.000
10	A	4	GLU	-1	-0.874	-0.946	18.983	-15.686	-15.686	0.000	0.000	0.000	0.000
11	A	5	ALA	0	0.022	0.022	18.412	0.409	0.409	0.000	0.000	0.000	0.000
12	A	6	SER	0	-0.025	-0.005	20.401	0.428	0.428	0.000	0.000	0.000	0.000
13	A	7	GLY	0	-0.004	-0.005	22.211	0.350	0.350	0.000	0.000	0.000	0.000
14	A	8	ASN	0	-0.014	-0.007	22.845	1.152	1.152	0.000	0.000	0.000	0.000
15	A	9	VAL	0	0.011	-0.005	26.048	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	10	TYR	0	-0.041	-0.026	24.634	-0.243	-0.243	0.000	0.000	0.000	0.000
17	A	11	PHE	0	-0.024	-0.025	26.852	0.507	0.507	0.000	0.000	0.000	0.000
18	A	12	ASP	-1	-0.764	-0.843	25.255	-13.138	-13.138	0.000	0.000	0.000	0.000
19	A	13	VAL	0	-0.029	-0.029	28.125	0.467	0.467	0.000	0.000	0.000	0.000
20	A	14	TYR	0	0.003	-0.003	27.295	-0.333	-0.333	0.000	0.000	0.000	0.000
21	A	15	ALA	0	0.001	-0.001	32.890	0.339	0.339	0.000	0.000	0.000	0.000
22	A	16	ASN	0	-0.056	-0.053	35.950	0.057	0.057	0.000	0.000	0.000	0.000
23	A	17	GLU	-1	-0.788	-0.861	34.303	-9.223	-9.223	0.000	0.000	0.000	0.000
24	A	18	GLU	-1	-0.911	-0.937	30.544	-10.799	-10.799	0.000	0.000	0.000	0.000
25	A	19	SER	0	-0.032	-0.013	27.682	-0.023	-0.023	0.000	0.000	0.000	0.000
26	A	20	LEU	0	-0.019	-0.011	29.061	-0.088	-0.088	0.000	0.000	0.000	0.000
27	A	21	GLY	0	0.037	0.014	25.915	-0.316	-0.316	0.000	0.000	0.000	0.000
28	A	22	ARG	1	0.840	0.891	21.401	14.219	14.219	0.000	0.000	0.000	0.000
29	A	23	ILE	0	-0.034	-0.012	25.269	-0.108	-0.108	0.000	0.000	0.000	0.000
30	A	24	VAL	0	0.046	0.015	22.237	0.133	0.133	0.000	0.000	0.000	0.000
31	A	25	MET	0	-0.050	-0.024	25.629	0.331	0.331	0.000	0.000	0.000	0.000
32	A	26	LYS	1	0.899	0.946	26.532	10.756	10.756	0.000	0.000	0.000	0.000
33	A	27	LEU	0	-0.037	-0.021	28.117	0.429	0.429	0.000	0.000	0.000	0.000
34	A	28	GLU	-1	-0.832	-0.904	30.784	-10.523	-10.523	0.000	0.000	0.000	0.000
35	A	29	ASP	-1	-0.786	-0.873	31.959	-9.456	-9.456	0.000	0.000	0.000	0.000
36	A	30	ASP	-1	-0.926	-0.963	32.303	-9.483	-9.483	0.000	0.000	0.000	0.000
37	A	31	ILE	0	-0.024	-0.002	35.362	0.214	0.214	0.000	0.000	0.000	0.000
38	A	32	VAL	0	-0.052	-0.022	37.159	0.304	0.304	0.000	0.000	0.000	0.000
39	A	33	PRO	0	0.052	0.042	36.968	-0.106	-0.106	0.000	0.000	0.000	0.000
40	A	34	LYS	1	0.868	0.923	37.939	7.436	7.436	0.000	0.000	0.000	0.000
41	A	35	THR	0	0.019	-0.018	39.090	0.060	0.060	0.000	0.000	0.000	0.000
42	A	36	ALA	0	0.017	0.025	34.055	-0.070	-0.070	0.000	0.000	0.000	0.000
43	A	37	LYS	1	0.988	0.995	35.033	7.967	7.967	0.000	0.000	0.000	0.000
44	A	38	ASN	0	-0.017	-0.005	36.512	0.033	0.033	0.000	0.000	0.000	0.000
45	A	39	PHE	0	0.053	0.016	32.020	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	40	ARG	1	0.813	0.868	29.434	10.201	10.201	0.000	0.000	0.000	0.000
47	A	41	THR	0	-0.007	-0.018	32.985	-0.073	-0.073	0.000	0.000	0.000	0.000
48	A	42	LEU	0	-0.064	-0.031	35.333	0.074	0.074	0.000	0.000	0.000	0.000
49	A	43	CYS	0	-0.054	-0.019	30.688	0.002	0.002	0.000	0.000	0.000	0.000
50	A	44	GLU	-1	-0.895	-0.950	30.163	-10.194	-10.194	0.000	0.000	0.000	0.000
51	A	45	ARG	1	0.909	0.976	32.184	8.055	8.055	0.000	0.000	0.000	0.000
52	A	46	PRO	0	0.012	0.012	34.751	-0.197	-0.197	0.000	0.000	0.000	0.000
53	A	47	LYS	1	0.891	0.936	34.707	8.995	8.995	0.000	0.000	0.000	0.000
54	A	48	GLY	0	-0.018	-0.001	37.790	0.151	0.151	0.000	0.000	0.000	0.000
55	A	49	GLU	-1	-0.957	-0.981	39.347	-7.506	-7.506	0.000	0.000	0.000	0.000
56	A	50	GLY	0	0.024	-0.006	37.038	-0.031	-0.031	0.000	0.000	0.000	0.000
57	A	51	TYR	0	-0.078	-0.053	34.565	0.156	0.156	0.000	0.000	0.000	0.000
58	A	52	LYS	1	0.956	0.995	30.056	10.267	10.267	0.000	0.000	0.000	0.000
59	A	53	GLY	0	-0.058	-0.040	34.858	0.257	0.257	0.000	0.000	0.000	0.000
60	A	54	SER	0	-0.077	-0.049	37.140	0.284	0.284	0.000	0.000	0.000	0.000
61	A	55	THR	0	-0.006	-0.025	37.616	-0.142	-0.142	0.000	0.000	0.000	0.000
62	A	56	PHE	0	0.030	0.011	34.134	0.054	0.054	0.000	0.000	0.000	0.000
63	A	57	HIS	0	0.003	0.015	39.479	-0.051	-0.051	0.000	0.000	0.000	0.000
64	A	58	ARG	1	0.892	0.944	42.561	7.176	7.176	0.000	0.000	0.000	0.000
65	A	59	ILE	0	-0.002	0.017	39.051	-0.142	-0.142	0.000	0.000	0.000	0.000
66	A	60	ILE	0	-0.006	0.009	41.895	0.161	0.161	0.000	0.000	0.000	0.000
67	A	61	PRO	0	0.032	0.008	40.311	-0.151	-0.151	0.000	0.000	0.000	0.000
68	A	62	GLY	0	-0.004	0.004	39.795	0.173	0.173	0.000	0.000	0.000	0.000
69	A	63	PHE	0	-0.020	-0.007	41.010	0.083	0.083	0.000	0.000	0.000	0.000
70	A	64	MET	0	-0.044	-0.010	39.107	-0.173	-0.173	0.000	0.000	0.000	0.000
71	A	65	VAL	0	0.016	0.011	35.800	0.130	0.130	0.000	0.000	0.000	0.000
72	A	66	GLN	0	0.040	0.008	38.674	-0.070	-0.070	0.000	0.000	0.000	0.000
73	A	67	GLY	0	0.029	0.012	39.395	0.009	0.009	0.000	0.000	0.000	0.000
74	A	68	GLY	0	0.045	0.023	39.400	0.094	0.094	0.000	0.000	0.000	0.000
75	A	69	ASP	-1	-0.739	-0.864	40.182	-6.881	-6.881	0.000	0.000	0.000	0.000
76	A	70	TYR	0	0.003	-0.021	40.415	0.028	0.028	0.000	0.000	0.000	0.000
77	A	71	THR	0	-0.017	0.000	42.345	0.015	0.015	0.000	0.000	0.000	0.000
78	A	72	ALA	0	-0.051	-0.030	46.010	0.111	0.111	0.000	0.000	0.000	0.000
79	A	73	HIS	0	-0.071	-0.021	41.979	-0.051	-0.051	0.000	0.000	0.000	0.000
80	A	74	ASN	0	0.026	0.023	45.398	-0.035	-0.035	0.000	0.000	0.000	0.000
81	A	75	GLY	0	-0.007	0.000	47.065	0.046	0.046	0.000	0.000	0.000	0.000
82	A	76	THR	0	-0.078	-0.051	47.987	0.077	0.077	0.000	0.000	0.000	0.000
83	A	77	GLY	0	-0.003	0.006	48.172	0.095	0.095	0.000	0.000	0.000	0.000
84	A	78	GLY	0	0.027	0.019	44.775	-0.092	-0.092	0.000	0.000	0.000	0.000
85	A	79	ARG	1	0.836	0.906	44.373	6.765	6.765	0.000	0.000	0.000	0.000
86	A	80	SER	0	0.032	0.021	43.203	-0.211	-0.211	0.000	0.000	0.000	0.000
87	A	81	ILE	0	-0.015	-0.013	38.997	0.109	0.109	0.000	0.000	0.000	0.000
88	A	82	TYR	0	-0.083	-0.058	40.805	0.009	0.009	0.000	0.000	0.000	0.000
89	A	83	GLY	0	-0.018	0.012	45.784	0.156	0.156	0.000	0.000	0.000	0.000
90	A	84	GLU	-1	-0.895	-0.956	48.119	-5.996	-5.996	0.000	0.000	0.000	0.000
91	A	85	LYS	1	0.880	0.962	48.203	5.875	5.875	0.000	0.000	0.000	0.000
92	A	86	PHE	0	-0.020	-0.013	42.132	0.078	0.078	0.000	0.000	0.000	0.000
93	A	87	PRO	0	0.038	-0.010	47.865	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	88	ASP	-1	-0.802	-0.893	46.164	-6.929	-6.929	0.000	0.000	0.000	0.000
95	A	89	GLU	-1	-0.807	-0.874	41.202	-7.730	-7.730	0.000	0.000	0.000	0.000
96	A	90	ASN	0	0.022	0.002	41.421	0.000	0.000	0.000	0.000	0.000	0.000
97	A	91	PHE	0	0.015	0.003	43.946	-0.068	-0.068	0.000	0.000	0.000	0.000
98	A	92	GLU	-1	-0.914	-0.945	39.833	-7.843	-7.843	0.000	0.000	0.000	0.000
99	A	93	LEU	0	-0.002	0.007	36.188	-0.050	-0.050	0.000	0.000	0.000	0.000
100	A	94	LYS	1	0.883	0.933	39.494	7.470	7.470	0.000	0.000	0.000	0.000
101	A	95	HIS	0	-0.017	-0.017	38.816	-0.304	-0.304	0.000	0.000	0.000	0.000
102	A	96	THR	0	-0.025	-0.035	36.564	0.045	0.045	0.000	0.000	0.000	0.000
103	A	97	LYS	1	0.829	0.906	30.626	10.223	10.223	0.000	0.000	0.000	0.000
104	A	98	GLU	-1	-0.832	-0.901	31.055	-9.913	-9.913	0.000	0.000	0.000	0.000
105	A	99	GLY	0	0.065	0.013	31.584	-0.221	-0.221	0.000	0.000	0.000	0.000
106	A	100	ILE	0	-0.062	-0.018	32.457	-0.166	-0.166	0.000	0.000	0.000	0.000
107	A	101	LEU	0	-0.003	0.003	32.760	0.173	0.173	0.000	0.000	0.000	0.000
108	A	102	SER	0	0.008	-0.023	35.635	0.107	0.107	0.000	0.000	0.000	0.000
109	A	103	MET	0	0.009	0.019	39.246	-0.104	-0.104	0.000	0.000	0.000	0.000
110	A	104	ALA	0	-0.043	-0.019	41.891	0.156	0.156	0.000	0.000	0.000	0.000
111	A	105	ASN	0	-0.041	-0.030	44.416	0.069	0.069	0.000	0.000	0.000	0.000
112	A	106	CYS	0	-0.023	-0.024	47.869	0.021	0.021	0.000	0.000	0.000	0.000
113	A	107	GLY	0	0.039	0.022	50.977	0.169	0.169	0.000	0.000	0.000	0.000
114	A	108	ALA	0	0.017	0.024	50.983	-0.119	-0.119	0.000	0.000	0.000	0.000
115	A	109	HIS	0	-0.012	-0.004	49.896	0.027	0.027	0.000	0.000	0.000	0.000
116	A	110	THR	0	-0.065	-0.050	49.982	0.053	0.053	0.000	0.000	0.000	0.000
117	A	111	ASN	0	-0.018	-0.007	44.595	-0.091	-0.091	0.000	0.000	0.000	0.000
118	A	112	GLY	0	0.054	0.016	45.284	0.100	0.100	0.000	0.000	0.000	0.000
119	A	113	SER	0	0.016	0.000	40.946	-0.048	-0.048	0.000	0.000	0.000	0.000
120	A	114	GLN	0	-0.042	-0.020	40.673	-0.280	-0.280	0.000	0.000	0.000	0.000
121	A	115	PHE	0	0.022	0.024	35.847	0.044	0.044	0.000	0.000	0.000	0.000
122	A	116	PHE	0	-0.045	-0.034	39.125	0.087	0.087	0.000	0.000	0.000	0.000
123	A	117	ILE	0	0.043	0.031	32.579	-0.111	-0.111	0.000	0.000	0.000	0.000
124	A	118	THR	0	-0.041	-0.017	36.432	0.095	0.095	0.000	0.000	0.000	0.000
125	A	119	LEU	0	-0.031	-0.014	35.290	-0.296	-0.296	0.000	0.000	0.000	0.000
126	A	120	GLY	0	0.050	0.014	36.856	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	121	LYS	1	0.914	0.979	37.938	7.666	7.666	0.000	0.000	0.000	0.000
128	A	122	THR	0	0.004	-0.011	39.754	0.103	0.103	0.000	0.000	0.000	0.000
129	A	123	GLN	0	0.067	0.023	42.742	-0.070	-0.070	0.000	0.000	0.000	0.000
130	A	124	TRP	0	-0.004	0.010	44.338	0.099	0.099	0.000	0.000	0.000	0.000
131	A	125	LEU	0	-0.022	-0.012	43.248	0.178	0.178	0.000	0.000	0.000	0.000
132	A	126	ASP	-1	-0.750	-0.855	43.334	-7.540	-7.540	0.000	0.000	0.000	0.000
133	A	127	GLU	-1	-0.949	-0.984	45.807	-6.393	-6.393	0.000	0.000	0.000	0.000
134	A	128	LYS	1	0.802	0.907	47.622	6.679	6.679	0.000	0.000	0.000	0.000
135	A	129	HIS	1	0.828	0.920	43.781	7.069	7.069	0.000	0.000	0.000	0.000
136	A	130	VAL	0	0.029	0.035	40.723	-0.032	-0.032	0.000	0.000	0.000	0.000
137	A	131	VAL	0	0.009	0.013	37.209	-0.117	-0.117	0.000	0.000	0.000	0.000
138	A	132	PHE	0	-0.008	-0.025	34.986	0.096	0.096	0.000	0.000	0.000	0.000
139	A	133	GLY	0	0.051	0.029	32.831	-0.197	-0.197	0.000	0.000	0.000	0.000
140	A	134	GLU	-1	-0.879	-0.919	29.193	-10.304	-10.304	0.000	0.000	0.000	0.000
141	A	135	VAL	0	-0.027	-0.016	27.492	-0.248	-0.248	0.000	0.000	0.000	0.000
142	A	136	VAL	0	-0.027	-0.009	23.877	0.026	0.026	0.000	0.000	0.000	0.000
143	A	137	GLU	-1	-0.913	-0.955	19.854	-16.563	-16.563	0.000	0.000	0.000	0.000
144	A	138	GLY	0	0.058	0.030	23.624	0.481	0.481	0.000	0.000	0.000	0.000
145	A	139	MET	0	-0.007	0.004	25.380	0.467	0.467	0.000	0.000	0.000	0.000
146	A	140	ASP	-1	-0.829	-0.933	25.533	-12.120	-12.120	0.000	0.000	0.000	0.000
147	A	141	VAL	0	-0.041	-0.010	26.360	0.404	0.404	0.000	0.000	0.000	0.000
148	A	142	VAL	0	0.015	0.011	29.147	0.422	0.422	0.000	0.000	0.000	0.000
149	A	143	HIS	0	-0.029	-0.035	30.907	0.560	0.560	0.000	0.000	0.000	0.000
150	A	144	LYS	1	0.796	0.901	26.436	12.204	12.204	0.000	0.000	0.000	0.000
151	A	145	ILE	0	-0.005	0.001	32.850	0.328	0.328	0.000	0.000	0.000	0.000
152	A	146	ALA	0	0.023	0.003	35.240	0.326	0.326	0.000	0.000	0.000	0.000
153	A	147	LYS	1	0.899	0.952	35.368	9.096	9.096	0.000	0.000	0.000	0.000
154	A	148	TYR	0	-0.041	-0.019	35.100	0.171	0.171	0.000	0.000	0.000	0.000
155	A	149	GLY	0	0.041	0.016	40.085	0.148	0.148	0.000	0.000	0.000	0.000
156	A	150	SER	0	-0.050	-0.028	42.435	0.133	0.133	0.000	0.000	0.000	0.000
157	A	151	GLU	-1	-0.844	-0.932	45.669	-6.892	-6.892	0.000	0.000	0.000	0.000
158	A	152	SER	0	-0.054	-0.031	47.761	0.061	0.061	0.000	0.000	0.000	0.000
159	A	153	GLY	0	0.001	-0.009	45.515	0.063	0.063	0.000	0.000	0.000	0.000
160	A	154	GLN	0	-0.020	0.000	45.507	-0.159	-0.159	0.000	0.000	0.000	0.000
161	A	155	VAL	0	0.063	0.049	41.896	-0.053	-0.053	0.000	0.000	0.000	0.000
162	A	156	LYS	1	0.938	0.969	41.670	7.738	7.738	0.000	0.000	0.000	0.000
163	A	157	LYS	1	0.881	0.921	44.328	6.635	6.635	0.000	0.000	0.000	0.000
164	A	158	GLY	0	0.034	0.016	45.112	-0.051	-0.051	0.000	0.000	0.000	0.000
165	A	159	TYR	0	-0.013	0.003	38.460	-0.188	-0.188	0.000	0.000	0.000	0.000
166	A	160	ARG	1	0.940	0.991	39.013	8.000	8.000	0.000	0.000	0.000	0.000
167	A	161	ILE	0	0.001	0.001	35.901	-0.174	-0.174	0.000	0.000	0.000	0.000
168	A	162	GLU	-1	-0.800	-0.895	35.388	-8.756	-8.756	0.000	0.000	0.000	0.000
169	A	163	ILE	0	0.016	0.023	31.994	-0.324	-0.324	0.000	0.000	0.000	0.000
170	A	164	ARG	1	0.715	0.820	30.887	9.532	9.532	0.000	0.000	0.000	0.000
171	A	165	ASP	-1	-0.824	-0.919	26.943	-11.075	-11.075	0.000	0.000	0.000	0.000
172	A	166	CYS	0	-0.068	-0.028	28.661	0.133	0.133	0.000	0.000	0.000	0.000
173	A	167	GLY	0	0.049	0.048	27.457	0.144	0.144	0.000	0.000	0.000	0.000
174	A	168	VAL	0	-0.029	-0.015	24.823	0.003	0.003	0.000	0.000	0.000	0.000
175	A	169	LEU	-1	-0.893	-0.945	20.304	-14.745	-14.745	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-5:THR)