FMO DATABASE

FMODB ID: JLRZ9

Calculation Name: 5U15-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5U15

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	212
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2101263.01797
FMO2-HF: Nuclear repulsion	2019297.698401
FMO2-HF: Total energy	-81965.319568
FMO2-MP2: Total energy	-82202.717612

3D Structure

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:1:GLN)

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

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.
-0.073	3.262	0.434	-1.161	-2.607	0

Interaction energy analysis for fragmet #1(A:1:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.015

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	3	GLN	0	0.017	0.007	2.471	-1.902	0.567	0.428	-0.919	-1.978
4	A	4	LEU	0	-0.027	-0.003	5.043	0.948	1.031	-0.001	-0.006	-0.076
5	A	5	VAL	0	0.022	0.009	8.105	0.165	0.165	0.000	0.000	0.000
6	A	6	GLN	0	-0.003	-0.029	10.786	0.092	0.092	0.000	0.000	0.000
7	A	7	SER	0	0.008	0.023	14.564	0.020	0.020	0.000	0.000	0.000
8	A	8	GLY	0	0.022	0.008	17.696	-0.010	-0.010	0.000	0.000	0.000
9	A	9	ALA	0	-0.028	-0.011	19.502	0.009	0.009	0.000	0.000	0.000
10	A	10	GLU	-1	-0.755	-0.870	22.297	-0.325	-0.325	0.000	0.000	0.000
11	A	11	VAL	0	-0.037	-0.015	25.445	0.015	0.015	0.000	0.000	0.000
12	A	12	LYS	1	0.812	0.897	27.961	0.308	0.308	0.000	0.000	0.000
13	A	13	LYS	1	0.858	0.919	31.990	0.178	0.178	0.000	0.000	0.000
14	A	14	PRO	0	0.024	-0.008	35.034	-0.007	-0.007	0.000	0.000	0.000
15	A	15	GLY	0	-0.026	-0.001	36.691	0.007	0.007	0.000	0.000	0.000
16	A	16	ALA	0	0.000	0.008	33.859	-0.001	-0.001	0.000	0.000	0.000
17	A	17	SER	0	0.018	-0.015	30.439	0.005	0.005	0.000	0.000	0.000
18	A	18	VAL	0	-0.040	-0.020	25.118	0.004	0.004	0.000	0.000	0.000
19	A	19	LYS	1	0.874	0.919	23.314	0.367	0.367	0.000	0.000	0.000
20	A	20	VAL	0	0.007	0.027	18.928	-0.013	-0.013	0.000	0.000	0.000
21	A	21	SER	0	0.031	0.002	17.302	0.002	0.002	0.000	0.000	0.000
22	A	22	CYS	0	-0.022	-0.012	13.419	-0.051	-0.051	0.000	0.000	0.000
23	A	23	LYS	1	0.862	0.945	9.940	1.603	1.603	0.000	0.000	0.000
24	A	24	ALA	0	0.025	0.015	9.099	-0.332	-0.332	0.000	0.000	0.000
25	A	25	SER	0	-0.043	-0.035	5.345	-0.175	-0.175	0.000	0.000	0.000
26	A	26	GLY	0	0.082	0.029	3.831	-1.733	-1.364	0.009	-0.194	-0.183
27	A	27	TYR	0	-0.007	-0.006	4.526	2.261	2.524	-0.001	-0.034	-0.228
28	A	28	THR	0	0.028	0.011	7.358	-0.295	-0.295	0.000	0.000	0.000
29	A	29	PHE	0	0.027	0.019	11.190	0.012	0.012	0.000	0.000	0.000
30	A	30	THR	0	0.005	-0.008	12.598	0.000	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.026	0.021	13.797	0.055	0.055	0.000	0.000	0.000
32	A	32	TYR	0	-0.018	-0.018	10.346	0.053	0.053	0.000	0.000	0.000
33	A	33	TYR	0	-0.044	-0.033	14.473	-0.046	-0.046	0.000	0.000	0.000
34	A	34	MET	0	-0.035	0.000	12.273	-0.069	-0.069	0.000	0.000	0.000
35	A	35	HIS	0	0.032	0.008	16.664	0.088	0.088	0.000	0.000	0.000
36	A	36	TRP	0	0.000	-0.010	17.608	-0.110	-0.110	0.000	0.000	0.000
37	A	37	VAL	0	-0.002	-0.002	19.487	0.070	0.070	0.000	0.000	0.000
38	A	38	ARG	1	0.789	0.876	20.646	0.272	0.272	0.000	0.000	0.000
39	A	39	GLN	0	0.019	0.012	22.006	-0.022	-0.022	0.000	0.000	0.000
40	A	40	ALA	0	0.041	0.032	24.473	-0.006	-0.006	0.000	0.000	0.000
41	A	41	PRO	0	0.004	-0.018	27.427	-0.001	-0.001	0.000	0.000	0.000
42	A	42	GLY	0	0.006	0.008	27.744	0.017	0.017	0.000	0.000	0.000
43	A	43	GLN	0	-0.052	-0.004	28.185	0.019	0.019	0.000	0.000	0.000
44	A	44	GLY	0	0.039	0.015	26.318	-0.016	-0.016	0.000	0.000	0.000
45	A	45	LEU	0	-0.011	-0.007	20.304	-0.008	-0.008	0.000	0.000	0.000
46	A	46	GLU	-1	-0.775	-0.876	24.254	-0.248	-0.248	0.000	0.000	0.000
47	A	47	TRP	0	-0.012	-0.006	22.283	-0.008	-0.008	0.000	0.000	0.000
48	A	48	MET	0	-0.015	-0.008	23.733	0.020	0.020	0.000	0.000	0.000
49	A	49	GLY	0	0.004	-0.013	23.812	0.031	0.031	0.000	0.000	0.000
50	A	50	TRP	0	-0.002	0.021	20.783	-0.051	-0.051	0.000	0.000	0.000
51	A	51	ILE	0	-0.003	-0.006	19.129	0.042	0.042	0.000	0.000	0.000
52	A	52	ASN	0	0.045	0.036	19.440	-0.052	-0.052	0.000	0.000	0.000
53	A	53	PRO	0	0.010	-0.003	15.836	0.042	0.042	0.000	0.000	0.000
54	A	54	ASN	0	0.032	0.022	18.825	0.006	0.006	0.000	0.000	0.000
55	A	55	SER	0	0.007	0.013	20.267	0.007	0.007	0.000	0.000	0.000
56	A	56	GLY	0	-0.012	-0.009	22.716	0.014	0.014	0.000	0.000	0.000
57	A	57	GLY	0	0.001	0.010	23.866	0.004	0.004	0.000	0.000	0.000
58	A	58	THR	0	-0.016	-0.021	24.032	-0.028	-0.028	0.000	0.000	0.000
59	A	59	ASN	0	-0.028	-0.007	26.046	0.034	0.034	0.000	0.000	0.000
60	A	60	TYR	0	0.032	0.001	25.991	0.002	0.002	0.000	0.000	0.000
61	A	61	ALA	0	0.051	0.045	27.707	0.017	0.017	0.000	0.000	0.000
62	A	62	GLN	0	0.024	-0.013	29.420	0.001	0.001	0.000	0.000	0.000
63	A	63	LYS	1	0.860	0.934	31.077	0.242	0.242	0.000	0.000	0.000
64	A	64	PHE	0	-0.027	-0.018	28.220	0.003	0.003	0.000	0.000	0.000
65	A	65	GLN	0	0.081	0.054	31.475	-0.018	-0.018	0.000	0.000	0.000
66	A	66	GLY	0	0.039	0.028	32.941	0.014	0.014	0.000	0.000	0.000
67	A	67	ARG	1	0.700	0.808	32.146	0.253	0.253	0.000	0.000	0.000
68	A	68	VAL	0	-0.005	0.004	26.435	-0.009	-0.009	0.000	0.000	0.000
69	A	69	THR	0	-0.015	-0.002	26.847	0.024	0.024	0.000	0.000	0.000
70	A	70	MET	0	-0.044	0.001	22.370	-0.030	-0.030	0.000	0.000	0.000
71	A	71	THR	0	0.010	0.005	22.213	0.024	0.024	0.000	0.000	0.000
72	A	72	ARG	1	0.832	0.896	18.576	0.306	0.306	0.000	0.000	0.000
73	A	73	ASP	-1	-0.801	-0.873	18.302	-0.409	-0.409	0.000	0.000	0.000
74	A	74	THR	0	0.018	-0.008	16.669	-0.092	-0.092	0.000	0.000	0.000
75	A	75	SER	0	-0.054	-0.030	16.030	-0.044	-0.044	0.000	0.000	0.000
76	A	76	ILE	0	0.054	0.033	14.970	-0.023	-0.023	0.000	0.000	0.000
77	A	77	SER	0	-0.052	-0.026	11.910	-0.178	-0.178	0.000	0.000	0.000
78	A	78	THR	0	-0.016	0.000	12.358	-0.285	-0.285	0.000	0.000	0.000
79	A	79	ALA	0	0.005	0.005	14.849	0.141	0.141	0.000	0.000	0.000
80	A	80	TYR	0	-0.005	-0.021	17.091	-0.069	-0.069	0.000	0.000	0.000
81	A	81	MET	0	-0.035	0.001	19.966	0.047	0.047	0.000	0.000	0.000
82	A	82	GLU	-1	-0.832	-0.904	22.542	-0.342	-0.342	0.000	0.000	0.000
83	A	83	LEU	0	0.006	0.003	25.949	0.018	0.018	0.000	0.000	0.000
84	A	84	SER	0	0.036	0.009	28.672	0.006	0.006	0.000	0.000	0.000
85	A	85	ARG	1	0.877	0.934	32.241	0.201	0.201	0.000	0.000	0.000
86	A	86	LEU	0	-0.018	0.016	29.539	0.004	0.004	0.000	0.000	0.000
87	A	87	ARG	1	0.865	0.885	33.363	0.226	0.226	0.000	0.000	0.000
88	A	88	SER	0	0.063	0.025	33.278	-0.013	-0.013	0.000	0.000	0.000
89	A	89	ASP	-1	-0.819	-0.870	32.914	-0.225	-0.225	0.000	0.000	0.000
90	A	90	ASP	-1	-0.728	-0.821	29.603	-0.271	-0.271	0.000	0.000	0.000
91	A	91	THR	0	-0.014	0.008	28.286	-0.027	-0.027	0.000	0.000	0.000
92	A	92	ALA	0	0.002	-0.006	25.265	0.013	0.013	0.000	0.000	0.000
93	A	93	VAL	0	0.010	0.022	19.509	-0.009	-0.009	0.000	0.000	0.000
94	A	94	TYR	0	-0.021	-0.038	20.762	0.021	0.021	0.000	0.000	0.000
95	A	95	TYR	0	0.024	0.002	15.973	-0.052	-0.052	0.000	0.000	0.000
96	A	97	ALA	0	0.057	0.011	13.289	-0.127	-0.127	0.000	0.000	0.000
97	A	98	ARG	1	0.763	0.869	7.681	1.039	1.039	0.000	0.000	0.000
98	A	99	GLY	0	0.052	0.023	12.839	0.031	0.031	0.000	0.000	0.000
99	A	100	GLY	0	0.015	0.006	14.253	-0.001	-0.001	0.000	0.000	0.000
100	A	101	TRP	0	0.016	0.001	13.899	-0.039	-0.039	0.000	0.000	0.000
101	A	102	ILE	0	-0.063	-0.037	15.823	0.016	0.016	0.000	0.000	0.000
102	A	103	SER	0	-0.016	-0.005	18.549	0.038	0.038	0.000	0.000	0.000
103	A	104	LEU	0	0.013	0.007	21.105	-0.013	-0.013	0.000	0.000	0.000
104	A	105	TYR	0	-0.014	-0.010	24.569	0.005	0.005	0.000	0.000	0.000
105	A	106	TYR	0	0.014	0.013	23.726	0.008	0.008	0.000	0.000	0.000
106	A	107	ASP	-1	-0.757	-0.839	23.620	-0.258	-0.258	0.000	0.000	0.000
107	A	108	SER	0	-0.015	-0.010	19.872	0.012	0.012	0.000	0.000	0.000
108	A	109	SER	0	-0.083	-0.068	20.433	-0.039	-0.039	0.000	0.000	0.000
109	A	110	GLY	0	0.008	-0.004	21.563	-0.036	-0.036	0.000	0.000	0.000
110	A	111	TYR	0	-0.023	-0.008	18.732	0.010	0.010	0.000	0.000	0.000
111	A	112	PRO	0	0.011	0.010	19.431	-0.045	-0.045	0.000	0.000	0.000
112	A	113	ASN	0	-0.030	-0.014	16.040	-0.015	-0.015	0.000	0.000	0.000
113	A	114	PHE	0	-0.022	-0.029	14.830	-0.030	-0.030	0.000	0.000	0.000
114	A	115	ASP	-1	-0.744	-0.832	9.699	-1.029	-1.029	0.000	0.000	0.000
115	A	116	TYR	0	-0.016	-0.001	4.520	-0.603	-0.452	-0.001	-0.008	-0.142
116	A	117	TRP	0	-0.008	-0.024	9.525	0.254	0.254	0.000	0.000	0.000
117	A	118	GLY	0	0.027	0.015	9.731	-0.342	-0.342	0.000	0.000	0.000
118	A	119	GLN	0	-0.026	-0.008	11.576	-0.030	-0.030	0.000	0.000	0.000
119	A	120	GLY	0	0.003	0.012	12.864	0.152	0.152	0.000	0.000	0.000
120	A	121	THR	0	-0.045	-0.035	16.375	-0.030	-0.030	0.000	0.000	0.000
121	A	122	LEU	0	-0.019	0.003	19.309	0.032	0.032	0.000	0.000	0.000
122	A	123	VAL	0	-0.003	0.009	22.598	0.001	0.001	0.000	0.000	0.000
123	A	124	THR	0	-0.003	-0.010	25.635	0.018	0.018	0.000	0.000	0.000
124	A	125	VAL	0	-0.014	-0.001	29.165	0.007	0.007	0.000	0.000	0.000
125	A	126	SER	0	0.040	0.011	32.378	0.012	0.012	0.000	0.000	0.000
126	A	127	GLY	0	0.030	0.004	35.834	0.001	0.001	0.000	0.000	0.000
127	A	128	ALA	0	-0.017	0.015	39.266	0.006	0.006	0.000	0.000	0.000
128	A	129	SER	0	-0.001	-0.008	40.043	-0.005	-0.005	0.000	0.000	0.000
129	A	130	THR	0	0.007	-0.001	42.261	-0.001	-0.001	0.000	0.000	0.000
130	A	131	LYS	1	0.898	0.966	43.592	0.114	0.114	0.000	0.000	0.000
131	A	132	GLY	0	0.077	0.045	45.314	-0.003	-0.003	0.000	0.000	0.000
132	A	133	PRO	0	-0.041	-0.014	46.482	0.000	0.000	0.000	0.000	0.000
133	A	134	SER	0	0.012	0.019	48.369	0.005	0.005	0.000	0.000	0.000
134	A	135	VAL	0	-0.002	-0.018	50.232	-0.003	-0.003	0.000	0.000	0.000
135	A	136	PHE	0	-0.013	-0.005	52.432	0.004	0.004	0.000	0.000	0.000
136	A	137	PRO	0	-0.018	-0.002	53.334	-0.001	-0.001	0.000	0.000	0.000
137	A	138	LEU	0	0.019	0.010	50.155	0.000	0.000	0.000	0.000	0.000
138	A	149	THR	0	-0.025	-0.019	55.067	0.001	0.001	0.000	0.000	0.000
139	A	150	ALA	0	-0.042	-0.029	57.279	0.000	0.000	0.000	0.000	0.000
140	A	151	ALA	0	0.018	0.010	52.849	-0.001	-0.001	0.000	0.000	0.000
141	A	152	LEU	0	-0.019	0.008	53.867	0.001	0.001	0.000	0.000	0.000
142	A	153	GLY	0	0.056	0.008	51.614	-0.002	-0.002	0.000	0.000	0.000
143	A	154	CYS	0	-0.091	-0.026	50.722	0.001	0.001	0.000	0.000	0.000
144	A	155	LEU	0	0.020	0.030	47.999	-0.003	-0.003	0.000	0.000	0.000
145	A	156	VAL	0	0.001	-0.011	45.460	0.003	0.003	0.000	0.000	0.000
146	A	157	LYS	1	0.907	0.923	46.333	0.090	0.090	0.000	0.000	0.000
147	A	158	ASP	-1	-0.799	-0.886	45.331	-0.104	-0.104	0.000	0.000	0.000
148	A	159	TYR	0	-0.053	-0.038	40.561	0.006	0.006	0.000	0.000	0.000
149	A	160	PHE	0	0.027	0.009	36.738	-0.009	-0.009	0.000	0.000	0.000
150	A	161	PRO	0	0.009	0.017	37.015	0.006	0.006	0.000	0.000	0.000
151	A	162	GLU	-1	-0.714	-0.848	35.883	-0.122	-0.122	0.000	0.000	0.000
152	A	163	PRO	0	-0.033	-0.013	36.611	-0.004	-0.004	0.000	0.000	0.000
153	A	164	VAL	0	-0.011	-0.010	38.568	0.006	0.006	0.000	0.000	0.000
154	A	165	THR	0	-0.059	-0.027	41.086	0.000	0.000	0.000	0.000	0.000
155	A	166	VAL	0	0.022	0.003	43.520	0.002	0.002	0.000	0.000	0.000
156	A	167	SER	0	-0.014	-0.001	45.975	0.002	0.002	0.000	0.000	0.000
157	A	168	TRP	0	0.049	0.022	48.765	0.001	0.001	0.000	0.000	0.000
158	A	169	ASN	0	0.010	-0.020	52.022	0.000	0.000	0.000	0.000	0.000
159	A	170	SER	0	-0.016	-0.012	52.749	0.001	0.001	0.000	0.000	0.000
160	A	171	GLY	0	0.012	0.013	50.318	0.000	0.000	0.000	0.000	0.000
161	A	172	ALA	0	-0.029	-0.001	51.270	0.001	0.001	0.000	0.000	0.000
162	A	173	LEU	0	-0.030	-0.008	52.282	0.002	0.002	0.000	0.000	0.000
163	A	174	THR	0	0.027	0.001	47.513	-0.002	-0.002	0.000	0.000	0.000
164	A	175	SER	0	0.035	0.013	48.114	-0.003	-0.003	0.000	0.000	0.000
165	A	176	GLY	0	0.059	0.027	48.863	0.000	0.000	0.000	0.000	0.000
166	A	177	VAL	0	-0.049	-0.015	46.658	-0.002	-0.002	0.000	0.000	0.000
167	A	178	HIS	0	0.004	0.008	40.648	0.001	0.001	0.000	0.000	0.000
168	A	179	THR	0	0.008	0.007	41.646	0.003	0.003	0.000	0.000	0.000
169	A	180	PHE	0	-0.011	0.005	41.009	-0.003	-0.003	0.000	0.000	0.000
170	A	181	PRO	0	0.023	-0.005	36.062	0.000	0.000	0.000	0.000	0.000
171	A	182	ALA	0	-0.006	0.008	38.130	0.003	0.003	0.000	0.000	0.000
172	A	183	VAL	0	-0.008	0.001	37.467	-0.009	-0.009	0.000	0.000	0.000
173	A	184	LEU	0	-0.029	-0.016	34.282	0.004	0.004	0.000	0.000	0.000
174	A	185	GLN	0	-0.045	-0.033	37.981	0.000	0.000	0.000	0.000	0.000
175	A	186	SER	0	0.025	0.003	39.161	-0.005	-0.005	0.000	0.000	0.000
176	A	187	SER	0	-0.011	-0.006	40.233	-0.005	-0.005	0.000	0.000	0.000
177	A	188	GLY	0	-0.007	-0.004	38.483	0.000	0.000	0.000	0.000	0.000
178	A	189	LEU	0	-0.068	-0.025	39.496	0.000	0.000	0.000	0.000	0.000
179	A	190	TYR	0	0.039	0.021	34.356	-0.003	-0.003	0.000	0.000	0.000
180	A	191	SER	0	-0.005	-0.014	40.980	0.009	0.009	0.000	0.000	0.000
181	A	192	LEU	0	0.007	0.030	41.199	-0.005	-0.005	0.000	0.000	0.000
182	A	193	SER	0	0.007	-0.014	43.714	0.006	0.006	0.000	0.000	0.000
183	A	194	SER	0	0.000	-0.003	44.973	-0.004	-0.004	0.000	0.000	0.000
184	A	195	VAL	0	0.004	-0.017	47.005	0.003	0.003	0.000	0.000	0.000
185	A	196	VAL	0	-0.005	-0.004	48.781	-0.001	-0.001	0.000	0.000	0.000
186	A	197	THR	0	-0.018	0.000	49.930	0.000	0.000	0.000	0.000	0.000
187	A	198	VAL	0	0.007	0.008	52.548	0.002	0.002	0.000	0.000	0.000
188	A	199	PRO	0	0.050	0.030	56.176	0.000	0.000	0.000	0.000	0.000
189	A	200	SER	0	0.028	-0.009	59.537	0.000	0.000	0.000	0.000	0.000
190	A	201	SER	0	-0.031	-0.018	61.890	0.001	0.001	0.000	0.000	0.000
191	A	202	SER	0	0.044	0.020	62.541	0.001	0.001	0.000	0.000	0.000
192	A	203	LEU	0	-0.011	-0.001	64.486	-0.001	-0.001	0.000	0.000	0.000
193	A	204	GLY	0	0.007	0.006	65.621	-0.001	-0.001	0.000	0.000	0.000
194	A	205	THR	0	-0.038	-0.019	65.971	0.001	0.001	0.000	0.000	0.000
195	A	206	GLN	0	0.016	0.024	60.483	0.001	0.001	0.000	0.000	0.000
196	A	207	THR	0	-0.036	-0.004	61.186	-0.001	-0.001	0.000	0.000	0.000
197	A	208	TYR	0	0.046	0.011	56.783	0.000	0.000	0.000	0.000	0.000
198	A	209	ILE	0	-0.018	-0.017	55.884	-0.001	-0.001	0.000	0.000	0.000
199	A	211	ASN	0	0.048	0.030	50.844	0.000	0.000	0.000	0.000	0.000
200	A	212	VAL	0	-0.010	-0.009	48.053	-0.002	-0.002	0.000	0.000	0.000
201	A	213	ASN	0	-0.003	-0.015	46.291	0.004	0.004	0.000	0.000	0.000
202	A	214	HIS	0	0.000	0.007	41.729	0.002	0.002	0.000	0.000	0.000
203	A	215	LYS	1	0.971	0.975	41.996	0.088	0.088	0.000	0.000	0.000
204	A	216	PRO	0	0.005	0.010	40.242	0.003	0.003	0.000	0.000	0.000
205	A	217	SER	0	-0.018	-0.032	42.742	0.000	0.000	0.000	0.000	0.000
206	A	218	ASN	0	-0.024	-0.017	46.275	0.001	0.001	0.000	0.000	0.000
207	A	219	THR	0	0.010	0.020	47.996	0.005	0.005	0.000	0.000	0.000
208	A	220	LYS	1	0.832	0.888	48.818	0.060	0.060	0.000	0.000	0.000
209	A	221	VAL	0	-0.007	0.000	51.210	0.002	0.002	0.000	0.000	0.000
210	A	222	ASP	-1	-0.813	-0.886	52.993	-0.058	-0.058	0.000	0.000	0.000
211	A	223	LYS	1	0.933	0.973	54.378	0.062	0.062	0.000	0.000	0.000
212	A	224	ARG	1	0.962	0.994	55.508	0.050	0.050	0.000	0.000	0.000

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