FMO DATABASE

FMODB ID: 5RMLZ

Calculation Name: 2DY0-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DY0

Chain ID: B

ChEMBL ID:

UniProt ID: P69503

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	181
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1833164.318404
FMO2-HF: Nuclear repulsion	1766187.992513
FMO2-HF: Total energy	-66976.32589
FMO2-MP2: Total energy	-67178.023798

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:ALA)

Summations of interaction energy for fragment #1(A:3: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.
-99.853	-96.055	9.458	-5.131	-8.124	-0.042

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.875 / q_NPA : 0.939

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	ALA	0	0.073	0.025	3.361	-2.046	-0.489	0.042	-0.777	-0.823	-0.001
5	A	7	GLN	0	0.020	0.017	2.277	-15.514	-14.017	3.640	-2.344	-2.793	-0.024
6	A	8	LEU	0	0.023	0.012	2.321	1.480	1.608	2.447	-0.755	-1.820	-0.006
7	A	9	GLU	-1	-0.949	-0.964	4.745	-20.398	-20.383	-0.001	-0.006	-0.008	0.000
45	A	47	LEU	0	-0.080	-0.055	2.293	-7.949	-7.838	3.329	-1.112	-2.327	-0.010
46	A	48	LEU	0	-0.024	-0.003	5.162	-3.827	-3.790	-0.001	-0.002	-0.034	0.000
173	A	175	TYR	0	-0.042	-0.017	3.810	-6.415	-6.069	0.002	-0.117	-0.231	-0.001
175	A	177	LEU	0	-0.051	-0.002	3.950	-3.578	-3.471	0.000	-0.018	-0.088	0.000
4	A	6	GLN	0	0.059	0.029	6.016	0.466	0.466	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.072	-0.074	7.395	2.415	2.415	0.000	0.000	0.000	0.000
9	A	11	LEU	0	0.010	0.006	5.023	2.196	2.196	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.878	0.954	8.413	24.547	24.547	0.000	0.000	0.000	0.000
11	A	13	ASN	0	-0.015	-0.016	10.441	2.279	2.279	0.000	0.000	0.000	0.000
12	A	14	SER	0	-0.027	-0.014	11.377	1.386	1.386	0.000	0.000	0.000	0.000
13	A	15	ILE	0	-0.029	0.013	11.384	1.022	1.022	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.982	0.998	14.865	14.269	14.269	0.000	0.000	0.000	0.000
15	A	17	SER	0	-0.004	-0.004	17.929	-0.425	-0.425	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.039	-0.008	20.236	0.398	0.398	0.000	0.000	0.000	0.000
17	A	19	GLN	0	0.037	0.003	23.952	-0.405	-0.405	0.000	0.000	0.000	0.000
18	A	20	ASP	-1	-0.892	-0.933	26.137	-9.838	-9.838	0.000	0.000	0.000	0.000
19	A	21	TYR	0	0.015	0.025	25.985	0.532	0.532	0.000	0.000	0.000	0.000
20	A	22	PRO	0	-0.020	-0.024	26.403	-0.439	-0.439	0.000	0.000	0.000	0.000
21	A	23	LYS	1	0.950	0.968	29.368	10.595	10.595	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.024	-0.007	29.636	-0.306	-0.306	0.000	0.000	0.000	0.000
23	A	25	GLY	0	-0.009	0.002	28.696	0.074	0.074	0.000	0.000	0.000	0.000
24	A	26	ILE	0	-0.063	-0.016	24.550	-0.198	-0.198	0.000	0.000	0.000	0.000
25	A	27	LEU	0	-0.003	-0.003	21.352	0.030	0.030	0.000	0.000	0.000	0.000
26	A	28	PHE	0	-0.005	0.008	21.298	-0.621	-0.621	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.873	0.921	16.705	15.478	15.478	0.000	0.000	0.000	0.000
28	A	30	ASP	-1	-0.846	-0.912	18.700	-14.047	-14.047	0.000	0.000	0.000	0.000
29	A	31	VAL	0	0.022	0.000	14.811	-0.578	-0.578	0.000	0.000	0.000	0.000
30	A	32	THR	0	-0.033	-0.035	16.881	-0.376	-0.376	0.000	0.000	0.000	0.000
31	A	33	SER	0	0.013	-0.027	16.602	0.096	0.096	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.037	-0.008	10.652	-0.333	-0.333	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.041	-0.028	14.549	-0.543	-0.543	0.000	0.000	0.000	0.000
34	A	36	GLU	-1	-0.983	-0.980	16.995	-13.126	-13.126	0.000	0.000	0.000	0.000
35	A	37	ASP	-1	-0.777	-0.869	13.586	-19.258	-19.258	0.000	0.000	0.000	0.000
36	A	38	PRO	0	-0.005	-0.008	14.761	-1.079	-1.079	0.000	0.000	0.000	0.000
37	A	39	LYS	1	0.874	0.961	9.703	23.978	23.978	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.007	-0.007	10.000	-2.326	-2.326	0.000	0.000	0.000	0.000
39	A	41	TYR	0	-0.015	-0.015	10.263	-1.630	-1.630	0.000	0.000	0.000	0.000
40	A	42	ALA	0	0.032	0.029	11.436	-1.209	-1.209	0.000	0.000	0.000	0.000
41	A	43	LEU	0	0.007	0.005	4.867	-2.045	-2.045	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.058	-0.051	6.511	-4.444	-4.444	0.000	0.000	0.000	0.000
43	A	45	ILE	0	0.008	0.008	8.073	-1.037	-1.037	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.872	-0.937	8.021	-28.709	-28.709	0.000	0.000	0.000	0.000
47	A	49	VAL	0	0.031	0.012	7.921	0.900	0.900	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.841	-0.909	5.481	-34.250	-34.250	0.000	0.000	0.000	0.000
49	A	51	ARG	1	0.823	0.924	5.605	31.347	31.347	0.000	0.000	0.000	0.000
50	A	52	TYR	0	-0.020	-0.026	7.127	1.896	1.896	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.850	0.924	9.144	32.955	32.955	0.000	0.000	0.000	0.000
52	A	54	ASN	0	-0.013	-0.010	11.926	2.067	2.067	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.026	-0.004	12.830	0.900	0.900	0.000	0.000	0.000	0.000
54	A	56	GLY	0	0.014	0.008	14.692	0.941	0.941	0.000	0.000	0.000	0.000
55	A	57	ILE	0	-0.033	-0.012	15.066	0.700	0.700	0.000	0.000	0.000	0.000
56	A	58	THR	0	-0.002	-0.031	18.146	0.006	0.006	0.000	0.000	0.000	0.000
57	A	59	LYS	1	0.793	0.878	20.568	12.679	12.679	0.000	0.000	0.000	0.000
58	A	60	VAL	0	0.010	0.017	16.302	-0.653	-0.653	0.000	0.000	0.000	0.000
59	A	61	VAL	0	-0.009	-0.005	19.090	0.850	0.850	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.052	0.018	18.922	-1.028	-1.028	0.000	0.000	0.000	0.000
61	A	63	THR	0	0.021	0.015	20.175	0.653	0.653	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.834	-0.877	21.778	-11.018	-11.018	0.000	0.000	0.000	0.000
63	A	65	ALA	0	-0.039	-0.031	23.830	0.049	0.049	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.884	0.899	19.013	14.137	14.137	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.108	0.071	17.542	-0.694	-0.694	0.000	0.000	0.000	0.000
66	A	68	PHE	0	-0.070	-0.036	17.688	-0.450	-0.450	0.000	0.000	0.000	0.000
67	A	69	LEU	0	0.002	0.015	17.781	-0.142	-0.142	0.000	0.000	0.000	0.000
68	A	70	PHE	0	0.062	0.031	12.736	-0.588	-0.588	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.048	0.012	14.529	-0.729	-0.729	0.000	0.000	0.000	0.000
70	A	72	ALA	0	-0.003	0.004	16.485	-0.041	-0.041	0.000	0.000	0.000	0.000
71	A	73	PRO	0	0.005	-0.007	14.775	0.116	0.116	0.000	0.000	0.000	0.000
72	A	74	VAL	0	0.024	0.016	11.381	-0.545	-0.545	0.000	0.000	0.000	0.000
73	A	75	ALA	0	-0.012	-0.012	14.078	-0.183	-0.183	0.000	0.000	0.000	0.000
74	A	76	LEU	0	-0.017	-0.008	17.520	0.270	0.270	0.000	0.000	0.000	0.000
75	A	77	GLY	0	-0.014	-0.005	14.505	0.324	0.324	0.000	0.000	0.000	0.000
76	A	78	LEU	0	-0.049	-0.024	12.144	-0.711	-0.711	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.021	0.011	15.581	0.581	0.581	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.060	-0.018	17.942	0.889	0.889	0.000	0.000	0.000	0.000
79	A	81	GLY	0	-0.011	-0.004	20.518	0.110	0.110	0.000	0.000	0.000	0.000
80	A	82	PHE	0	0.012	0.002	19.369	-0.355	-0.355	0.000	0.000	0.000	0.000
81	A	83	VAL	0	-0.027	-0.017	22.111	0.784	0.784	0.000	0.000	0.000	0.000
82	A	84	PRO	0	-0.036	-0.010	23.248	-0.362	-0.362	0.000	0.000	0.000	0.000
83	A	85	VAL	0	0.010	0.006	24.352	0.452	0.452	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.800	0.870	25.720	10.522	10.522	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.926	0.953	28.510	10.174	10.174	0.000	0.000	0.000	0.000
86	A	88	PRO	0	0.015	0.011	31.454	0.011	0.011	0.000	0.000	0.000	0.000
87	A	89	GLY	0	-0.009	0.010	34.940	0.061	0.061	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.901	0.959	31.568	9.393	9.393	0.000	0.000	0.000	0.000
89	A	91	LEU	0	-0.031	-0.018	29.664	-0.082	-0.082	0.000	0.000	0.000	0.000
90	A	92	PRO	0	-0.012	-0.003	33.800	0.178	0.178	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.925	0.963	32.234	9.524	9.524	0.000	0.000	0.000	0.000
92	A	94	GLU	-1	-0.862	-0.934	36.380	-8.269	-8.269	0.000	0.000	0.000	0.000
93	A	95	THR	0	-0.047	-0.025	33.254	-0.243	-0.243	0.000	0.000	0.000	0.000
94	A	96	ILE	0	-0.015	0.011	31.567	0.277	0.277	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.024	0.002	32.744	-0.336	-0.336	0.000	0.000	0.000	0.000
96	A	98	GLU	-1	-0.841	-0.913	30.100	-9.700	-9.700	0.000	0.000	0.000	0.000
97	A	99	THR	0	-0.021	-0.011	32.247	0.092	0.092	0.000	0.000	0.000	0.000
98	A	100	TYR	0	-0.034	-0.016	28.160	-0.206	-0.206	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.888	-0.943	30.976	-9.381	-9.381	0.000	0.000	0.000	0.000
100	A	102	LEU	0	-0.059	-0.041	29.434	-0.452	-0.452	0.000	0.000	0.000	0.000
101	A	103	GLU	-1	-0.928	-0.959	31.977	-9.108	-9.108	0.000	0.000	0.000	0.000
102	A	104	TYR	0	-0.049	-0.027	33.597	0.321	0.321	0.000	0.000	0.000	0.000
103	A	105	GLY	0	-0.002	-0.004	35.808	0.243	0.243	0.000	0.000	0.000	0.000
104	A	106	THR	0	-0.045	-0.015	33.877	-0.164	-0.164	0.000	0.000	0.000	0.000
105	A	107	ASP	-1	-0.807	-0.876	31.300	-9.462	-9.462	0.000	0.000	0.000	0.000
106	A	108	GLN	0	-0.045	-0.039	32.326	0.004	0.004	0.000	0.000	0.000	0.000
107	A	109	LEU	0	-0.038	-0.022	25.822	-0.262	-0.262	0.000	0.000	0.000	0.000
108	A	110	GLU	-1	-0.835	-0.925	29.967	-8.800	-8.800	0.000	0.000	0.000	0.000
109	A	111	ILE	0	0.022	0.002	26.112	-0.415	-0.415	0.000	0.000	0.000	0.000
110	A	112	HIS	0	-0.011	-0.012	29.735	0.553	0.553	0.000	0.000	0.000	0.000
111	A	113	VAL	0	0.042	0.015	30.998	-0.358	-0.358	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.903	-0.954	32.569	-9.108	-9.108	0.000	0.000	0.000	0.000
113	A	115	ALA	0	-0.062	-0.025	27.868	-0.098	-0.098	0.000	0.000	0.000	0.000
114	A	116	ILE	0	-0.016	-0.003	24.717	-0.499	-0.499	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.872	0.932	28.110	10.183	10.183	0.000	0.000	0.000	0.000
116	A	118	PRO	0	0.028	-0.002	28.659	-0.354	-0.354	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.004	0.010	27.556	0.163	0.163	0.000	0.000	0.000	0.000
118	A	120	ASP	-1	-0.791	-0.842	24.606	-12.405	-12.405	0.000	0.000	0.000	0.000
119	A	121	LYS	1	0.872	0.955	17.645	17.025	17.025	0.000	0.000	0.000	0.000
120	A	122	VAL	0	-0.021	-0.019	20.238	-0.387	-0.387	0.000	0.000	0.000	0.000
121	A	123	LEU	0	-0.008	0.014	12.805	-0.370	-0.370	0.000	0.000	0.000	0.000
122	A	124	VAL	0	-0.008	-0.012	16.990	0.742	0.742	0.000	0.000	0.000	0.000
123	A	125	VAL	0	-0.022	-0.017	13.156	-1.317	-1.317	0.000	0.000	0.000	0.000
124	A	126	ASP	-1	-0.834	-0.935	14.991	-14.218	-14.218	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.838	-0.909	14.428	-17.343	-17.343	0.000	0.000	0.000	0.000
126	A	128	LEU	0	-0.033	-0.021	14.107	-1.445	-1.445	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.017	0.014	15.173	1.032	1.032	0.000	0.000	0.000	0.000
128	A	130	ALA	0	0.069	0.019	16.834	-0.072	-0.072	0.000	0.000	0.000	0.000
129	A	131	THR	0	0.045	0.018	20.102	-0.250	-0.250	0.000	0.000	0.000	0.000
130	A	132	GLY	0	0.048	0.012	20.872	0.252	0.252	0.000	0.000	0.000	0.000
131	A	133	GLY	0	-0.010	0.004	21.796	0.055	0.055	0.000	0.000	0.000	0.000
132	A	134	THR	0	0.061	0.029	22.123	0.229	0.229	0.000	0.000	0.000	0.000
133	A	135	ILE	0	0.022	0.020	18.841	0.161	0.161	0.000	0.000	0.000	0.000
134	A	136	GLU	-1	-0.801	-0.878	21.982	-11.260	-11.260	0.000	0.000	0.000	0.000
135	A	137	ALA	0	0.030	0.009	24.706	0.286	0.286	0.000	0.000	0.000	0.000
136	A	138	THR	0	0.022	-0.011	22.190	0.280	0.280	0.000	0.000	0.000	0.000
137	A	139	VAL	0	-0.014	-0.006	21.941	0.089	0.089	0.000	0.000	0.000	0.000
138	A	140	LYS	1	0.860	0.945	24.538	10.912	10.912	0.000	0.000	0.000	0.000
139	A	141	LEU	0	-0.022	-0.014	27.231	0.244	0.244	0.000	0.000	0.000	0.000
140	A	142	ILE	0	-0.001	-0.001	22.342	0.215	0.215	0.000	0.000	0.000	0.000
141	A	143	ARG	1	0.825	0.902	22.778	13.296	13.296	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.811	0.887	28.207	9.731	9.731	0.000	0.000	0.000	0.000
143	A	145	LEU	0	-0.027	0.006	29.358	0.355	0.355	0.000	0.000	0.000	0.000
144	A	146	GLY	0	-0.020	-0.010	30.313	0.083	0.083	0.000	0.000	0.000	0.000
145	A	147	GLY	0	0.011	0.008	26.174	-0.095	-0.095	0.000	0.000	0.000	0.000
146	A	148	GLU	-1	-0.921	-0.969	21.627	-14.020	-14.020	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.006	-0.012	19.624	-0.387	-0.387	0.000	0.000	0.000	0.000
148	A	150	ALA	0	0.049	0.025	18.540	0.561	0.561	0.000	0.000	0.000	0.000
149	A	151	ASP	-1	-0.878	-0.937	13.616	-22.422	-22.422	0.000	0.000	0.000	0.000
150	A	152	ALA	0	-0.003	-0.005	14.820	1.064	1.064	0.000	0.000	0.000	0.000
151	A	153	ALA	0	-0.024	-0.015	10.249	-1.566	-1.566	0.000	0.000	0.000	0.000
152	A	154	PHE	0	0.034	0.011	10.710	1.725	1.725	0.000	0.000	0.000	0.000
153	A	155	ILE	0	0.011	0.007	9.632	-3.224	-3.224	0.000	0.000	0.000	0.000
154	A	156	ILE	0	-0.010	-0.012	10.012	-1.731	-1.731	0.000	0.000	0.000	0.000
155	A	157	ASN	0	-0.003	-0.007	12.270	1.735	1.735	0.000	0.000	0.000	0.000
156	A	158	LEU	0	0.014	0.012	13.871	-0.417	-0.417	0.000	0.000	0.000	0.000
157	A	159	PHE	0	0.039	0.011	14.172	0.511	0.511	0.000	0.000	0.000	0.000
158	A	160	ASP	-1	-0.832	-0.912	17.171	-14.101	-14.101	0.000	0.000	0.000	0.000
159	A	161	LEU	0	-0.061	-0.028	20.233	0.745	0.745	0.000	0.000	0.000	0.000
160	A	162	GLY	0	-0.002	0.012	20.545	0.387	0.387	0.000	0.000	0.000	0.000
161	A	163	GLY	0	0.017	0.003	20.096	0.205	0.205	0.000	0.000	0.000	0.000
162	A	164	GLU	-1	-0.916	-0.959	13.822	-21.081	-21.081	0.000	0.000	0.000	0.000
163	A	165	GLN	0	0.047	0.016	17.390	0.798	0.798	0.000	0.000	0.000	0.000
164	A	166	ARG	1	0.813	0.904	20.828	12.484	12.484	0.000	0.000	0.000	0.000
165	A	167	LEU	0	0.014	0.006	18.381	0.481	0.481	0.000	0.000	0.000	0.000
166	A	168	GLU	-1	-0.858	-0.928	18.225	-16.231	-16.231	0.000	0.000	0.000	0.000
167	A	169	LYS	1	0.806	0.898	21.080	13.640	13.640	0.000	0.000	0.000	0.000
168	A	170	GLN	0	-0.045	-0.017	23.269	0.182	0.182	0.000	0.000	0.000	0.000
169	A	171	GLY	0	0.009	0.008	22.085	0.180	0.180	0.000	0.000	0.000	0.000
170	A	172	ILE	0	-0.074	-0.030	17.442	-0.206	-0.206	0.000	0.000	0.000	0.000
171	A	173	THR	0	-0.002	0.002	12.970	-0.058	-0.058	0.000	0.000	0.000	0.000
172	A	174	SER	0	0.026	0.004	13.748	0.156	0.156	0.000	0.000	0.000	0.000
174	A	176	SER	0	0.012	-0.004	8.689	2.642	2.642	0.000	0.000	0.000	0.000
176	A	178	VAL	0	-0.009	-0.005	6.274	-1.857	-1.857	0.000	0.000	0.000	0.000
177	A	179	PRO	0	0.018	0.025	8.489	2.294	2.294	0.000	0.000	0.000	0.000
178	A	180	PHE	0	-0.029	-0.049	11.500	-0.057	-0.057	0.000	0.000	0.000	0.000
179	A	181	PRO	0	0.037	0.038	14.981	0.101	0.101	0.000	0.000	0.000	0.000
180	A	182	GLY	0	-0.049	-0.031	18.397	-0.036	-0.036	0.000	0.000	0.000	0.000
181	A	183	HIS	-1	-0.890	-0.947	21.081	-12.976	-12.976	0.000	0.000	0.000	0.000

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