FMO DATABASE

FMODB ID: J2MV9

Calculation Name: 1LGV-A-Xray372

Preferred Name:

Target Type:

Ligand Name: pyroglutamic acid

ligand 3-letter code: PCA

PDB ID: 1LGV

Chain ID: A

ChEMBL ID:

UniProt ID: Q6PJG0

Base Structure: X-ray

Registration Date: 2023-09-26

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	OptH
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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1964304.581838
FMO2-HF: Nuclear repulsion	1885734.717088
FMO2-HF: Total energy	-78569.86475
FMO2-MP2: Total energy	-78800.418245

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:PCA)

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

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.
-4.302	-1.11	0.096	-1.686	-1.602	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / q_NPA : -0.019

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	ALA	0	0.001	0.000	3.078	-3.620	-0.468	0.097	-1.683	-1.566
4	A	4	LEU	0	0.001	-0.007	5.332	0.641	0.681	-0.001	-0.003	-0.036
5	A	5	THR	0	-0.003	-0.015	8.859	-0.028	-0.028	0.000	0.000	0.000
6	A	6	GLN	0	0.013	-0.014	11.142	-0.053	-0.053	0.000	0.000	0.000
7	A	7	PRO	0	-0.029	0.008	12.851	0.058	0.058	0.000	0.000	0.000
8	A	8	ALA	0	0.101	0.048	13.421	-0.010	-0.010	0.000	0.000	0.000
9	A	9	SER	0	-0.077	-0.039	14.381	0.051	0.051	0.000	0.000	0.000
10	A	10	VAL	0	0.031	0.027	17.738	-0.034	-0.034	0.000	0.000	0.000
11	A	11	SER	0	-0.017	-0.019	21.004	0.030	0.030	0.000	0.000	0.000
12	A	12	GLY	0	0.062	0.034	24.312	-0.017	-0.017	0.000	0.000	0.000
13	A	13	SER	0	-0.043	-0.012	27.681	0.019	0.019	0.000	0.000	0.000
14	A	14	PRO	0	0.019	-0.011	30.928	-0.013	-0.013	0.000	0.000	0.000
15	A	15	GLY	0	-0.016	0.004	32.317	0.002	0.002	0.000	0.000	0.000
16	A	16	GLN	0	-0.010	-0.003	30.211	-0.009	-0.009	0.000	0.000	0.000
17	A	17	SER	0	0.039	0.016	28.645	0.000	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.000	0.014	22.506	0.008	0.008	0.000	0.000	0.000
19	A	19	THR	0	0.009	0.006	22.475	-0.010	-0.010	0.000	0.000	0.000
20	A	20	VAL	0	-0.012	0.005	16.777	0.014	0.014	0.000	0.000	0.000
21	A	21	SER	0	-0.016	-0.007	17.883	-0.034	-0.034	0.000	0.000	0.000
22	A	22	CYS	0	0.045	0.026	12.264	-0.029	-0.029	0.000	0.000	0.000
23	A	23	THR	0	-0.044	-0.014	13.925	-0.009	-0.009	0.000	0.000	0.000
24	A	24	GLY	0	0.040	0.015	12.189	-0.197	-0.197	0.000	0.000	0.000
25	A	25	VAL	0	-0.026	-0.007	12.522	-0.118	-0.118	0.000	0.000	0.000
26	A	26	SER	0	-0.013	-0.023	14.421	0.029	0.029	0.000	0.000	0.000
27	A	27	SER	0	0.020	0.040	15.465	-0.068	-0.068	0.000	0.000	0.000
28	A	28	ILE	0	-0.035	-0.013	14.651	0.074	0.074	0.000	0.000	0.000
29	A	29	VAL	0	-0.064	0.066	17.313	0.077	0.077	0.000	0.000	0.000
30	A	30	GLY	0	0.058	0.019	19.294	-0.012	-0.012	0.000	0.000	0.000
31	A	31	SER	0	-0.003	-0.025	21.143	-0.032	-0.032	0.000	0.000	0.000
32	A	32	TYR	0	-0.026	-0.006	17.369	0.074	0.074	0.000	0.000	0.000
33	A	33	ASN	0	0.010	-0.008	19.770	-0.056	-0.056	0.000	0.000	0.000
34	A	34	LEU	0	-0.007	-0.013	17.263	0.050	0.050	0.000	0.000	0.000
35	A	35	VAL	0	0.021	0.021	15.884	-0.085	-0.085	0.000	0.000	0.000
36	A	36	SER	0	-0.014	-0.010	15.698	0.135	0.135	0.000	0.000	0.000
37	A	37	TRP	0	-0.001	0.013	15.530	-0.111	-0.111	0.000	0.000	0.000
38	A	38	TYR	0	-0.016	-0.017	14.072	0.029	0.029	0.000	0.000	0.000
39	A	39	GLN	0	0.011	0.001	16.708	-0.007	-0.007	0.000	0.000	0.000
40	A	40	GLN	0	-0.028	-0.030	13.927	-0.009	-0.009	0.000	0.000	0.000
41	A	41	HIS	0	0.009	0.022	17.494	0.029	0.029	0.000	0.000	0.000
42	A	42	PRO	0	0.026	-0.010	18.523	0.006	0.006	0.000	0.000	0.000
43	A	43	GLY	0	0.013	0.012	18.234	-0.016	-0.016	0.000	0.000	0.000
44	A	44	LYS	1	0.924	0.977	19.062	0.000	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.028	0.018	17.309	0.011	0.011	0.000	0.000	0.000
46	A	46	PRO	0	0.011	0.001	13.770	0.009	0.009	0.000	0.000	0.000
47	A	47	LYS	1	0.955	0.988	16.905	0.159	0.159	0.000	0.000	0.000
48	A	48	LEU	0	-0.024	-0.004	18.383	-0.016	-0.016	0.000	0.000	0.000
49	A	49	LEU	0	-0.040	-0.020	19.596	0.043	0.043	0.000	0.000	0.000
50	A	50	THR	0	0.013	-0.022	20.403	0.011	0.011	0.000	0.000	0.000
51	A	51	TYR	0	0.054	0.016	19.848	-0.046	-0.046	0.000	0.000	0.000
52	A	52	GLU	-1	-0.882	-0.942	20.374	-0.358	-0.358	0.000	0.000	0.000
53	A	53	VAL	0	-0.047	-0.010	20.508	0.035	0.035	0.000	0.000	0.000
54	A	54	ASN	0	-0.048	-0.031	21.646	0.006	0.006	0.000	0.000	0.000
55	A	55	LYS	1	0.888	0.974	24.330	0.383	0.383	0.000	0.000	0.000
56	A	56	ARG	1	0.936	0.969	24.382	0.181	0.181	0.000	0.000	0.000
57	A	57	PRO	0	-0.027	0.004	23.457	0.016	0.016	0.000	0.000	0.000
58	A	58	SER	0	0.060	0.023	26.607	0.009	0.009	0.000	0.000	0.000
59	A	59	GLY	0	0.014	0.008	28.726	-0.002	-0.002	0.000	0.000	0.000
60	A	60	VAL	0	-0.112	-0.047	24.765	0.014	0.014	0.000	0.000	0.000
61	A	61	SER	0	0.038	0.025	27.962	-0.003	-0.003	0.000	0.000	0.000
62	A	62	ASP	-1	-0.895	-0.970	28.406	-0.163	-0.163	0.000	0.000	0.000
63	A	63	ARG	1	0.847	0.923	28.049	0.100	0.100	0.000	0.000	0.000
64	A	64	PHE	0	-0.054	-0.015	23.484	-0.008	-0.008	0.000	0.000	0.000
65	A	65	SER	0	0.003	-0.009	25.449	0.001	0.001	0.000	0.000	0.000
66	A	66	GLY	0	0.014	0.022	22.406	-0.008	-0.008	0.000	0.000	0.000
67	A	67	SER	0	0.004	-0.005	22.298	0.024	0.024	0.000	0.000	0.000
68	A	68	LYS	1	0.949	0.968	19.047	0.626	0.626	0.000	0.000	0.000
69	A	69	SER	0	-0.025	-0.006	21.446	0.047	0.047	0.000	0.000	0.000
70	A	70	GLY	0	0.051	0.030	21.743	-0.024	-0.024	0.000	0.000	0.000
71	A	71	ASN	0	0.025	0.002	15.580	-0.076	-0.076	0.000	0.000	0.000
72	A	72	SER	0	0.010	-0.004	16.692	-0.128	-0.128	0.000	0.000	0.000
73	A	73	ALA	0	0.054	0.031	16.976	0.060	0.060	0.000	0.000	0.000
74	A	74	SER	0	-0.059	-0.042	18.336	0.001	0.001	0.000	0.000	0.000
75	A	75	LEU	0	0.025	0.032	19.464	0.010	0.010	0.000	0.000	0.000
76	A	76	THR	0	-0.025	-0.023	21.120	0.011	0.011	0.000	0.000	0.000
77	A	77	ILE	0	-0.032	-0.015	21.744	0.000	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.022	-0.005	25.846	0.015	0.015	0.000	0.000	0.000
79	A	79	GLY	0	0.007	0.004	29.645	0.003	0.003	0.000	0.000	0.000
80	A	80	LEU	0	-0.066	-0.031	25.340	0.005	0.005	0.000	0.000	0.000
81	A	81	GLN	0	-0.022	-0.038	28.580	0.007	0.007	0.000	0.000	0.000
82	A	82	ALA	0	0.069	0.036	28.051	-0.001	-0.001	0.000	0.000	0.000
83	A	83	GLU	-1	-0.842	-0.908	27.158	-0.026	-0.026	0.000	0.000	0.000
84	A	84	ASP	-1	-0.779	-0.865	24.473	-0.102	-0.102	0.000	0.000	0.000
85	A	85	GLU	-1	-0.871	-0.904	22.764	0.049	0.049	0.000	0.000	0.000
86	A	86	ALA	0	-0.039	-0.022	19.517	0.011	0.011	0.000	0.000	0.000
87	A	87	ASP	-1	-0.822	-0.887	14.134	0.175	0.175	0.000	0.000	0.000
88	A	88	TYR	0	-0.036	-0.058	15.555	-0.047	-0.047	0.000	0.000	0.000
89	A	89	TYR	0	-0.017	0.015	9.226	0.012	0.012	0.000	0.000	0.000
90	A	91	SER	0	0.017	-0.003	11.026	-0.194	-0.194	0.000	0.000	0.000
91	A	92	SER	0	0.014	-0.005	11.363	0.262	0.262	0.000	0.000	0.000
92	A	93	TYR	0	-0.025	0.013	11.898	-0.170	-0.170	0.000	0.000	0.000
93	A	94	ASP	-1	-0.762	-0.905	10.394	-1.783	-1.783	0.000	0.000	0.000
94	A	95	GLY	0	0.006	-0.076	12.938	0.096	0.096	0.000	0.000	0.000
95	A	96	SER	0	-0.078	-0.045	12.312	0.031	0.031	0.000	0.000	0.000
96	A	97	SER	0	0.035	0.014	9.828	0.089	0.089	0.000	0.000	0.000
97	A	98	THR	0	-0.026	-0.008	11.762	0.065	0.065	0.000	0.000	0.000
98	A	99	SER	0	0.012	0.019	9.544	0.156	0.156	0.000	0.000	0.000
99	A	100	VAL	0	-0.010	-0.004	9.924	0.017	0.017	0.000	0.000	0.000
100	A	101	VAL	0	0.007	0.018	5.935	-0.316	-0.316	0.000	0.000	0.000
101	A	102	PHE	0	0.003	-0.018	6.516	0.593	0.593	0.000	0.000	0.000
102	A	103	GLY	0	0.004	0.008	6.651	-0.764	-0.764	0.000	0.000	0.000
103	A	104	GLY	0	-0.012	-0.010	6.913	-0.053	-0.053	0.000	0.000	0.000
104	A	105	GLY	0	-0.012	-0.003	7.883	0.441	0.441	0.000	0.000	0.000
105	A	106	THR	0	-0.067	-0.034	11.139	0.029	0.029	0.000	0.000	0.000
106	A	107	LYS	1	0.870	0.919	14.593	-0.295	-0.295	0.000	0.000	0.000
107	A	108	LEU	0	-0.026	-0.009	16.897	-0.006	-0.006	0.000	0.000	0.000
108	A	109	THR	0	-0.034	-0.026	20.463	0.033	0.033	0.000	0.000	0.000
109	A	110	VAL	0	0.001	-0.009	23.511	-0.021	-0.021	0.000	0.000	0.000
110	A	111	LEU	0	0.006	0.011	26.802	0.018	0.018	0.000	0.000	0.000
111	A	112	GLY	0	0.028	0.001	29.346	-0.012	-0.012	0.000	0.000	0.000
112	A	113	GLN	0	-0.050	-0.040	28.880	-0.009	-0.009	0.000	0.000	0.000
113	A	114	PRO	0	-0.038	-0.004	33.756	0.006	0.006	0.000	0.000	0.000
114	A	115	LYS	1	0.955	0.978	36.712	-0.072	-0.072	0.000	0.000	0.000
115	A	116	ALA	0	-0.041	-0.027	37.614	-0.007	-0.007	0.000	0.000	0.000
116	A	117	ALA	0	0.033	0.012	38.568	0.008	0.008	0.000	0.000	0.000
117	A	118	PRO	0	-0.013	-0.002	38.951	-0.003	-0.003	0.000	0.000	0.000
118	A	119	SER	0	0.050	0.033	40.599	-0.004	-0.004	0.000	0.000	0.000
119	A	120	VAL	0	-0.028	-0.021	41.772	0.006	0.006	0.000	0.000	0.000
120	A	121	THR	0	-0.028	-0.017	43.857	-0.007	-0.007	0.000	0.000	0.000
121	A	122	LEU	0	-0.028	-0.007	44.822	0.006	0.006	0.000	0.000	0.000
122	A	123	PHE	0	-0.034	-0.013	44.452	-0.005	-0.005	0.000	0.000	0.000
123	A	124	PRO	0	0.007	-0.007	48.277	0.005	0.005	0.000	0.000	0.000
124	A	125	PRO	0	0.041	0.040	49.819	0.000	0.000	0.000	0.000	0.000
125	A	126	SER	0	0.010	0.004	50.633	-0.003	-0.003	0.000	0.000	0.000
126	A	127	SER	0	0.039	-0.011	52.458	0.002	0.002	0.000	0.000	0.000
127	A	128	GLU	-1	-0.912	-0.951	52.131	0.056	0.056	0.000	0.000	0.000
128	A	129	GLU	-1	-0.769	-0.855	47.819	0.093	0.093	0.000	0.000	0.000
129	A	130	LEU	0	-0.001	-0.011	51.595	0.002	0.002	0.000	0.000	0.000
130	A	131	GLN	0	-0.026	-0.005	54.571	0.001	0.001	0.000	0.000	0.000
131	A	132	ALA	0	-0.062	-0.014	51.420	-0.001	-0.001	0.000	0.000	0.000
132	A	133	ASN	0	-0.041	-0.027	52.537	0.002	0.002	0.000	0.000	0.000
133	A	134	LYS	1	0.854	0.919	45.413	-0.093	-0.093	0.000	0.000	0.000
134	A	135	ALA	0	0.003	-0.013	49.920	-0.005	-0.005	0.000	0.000	0.000
135	A	136	THR	0	-0.042	-0.031	43.861	0.008	0.008	0.000	0.000	0.000
136	A	137	LEU	0	-0.053	0.001	46.382	-0.006	-0.006	0.000	0.000	0.000
137	A	138	VAL	0	0.051	0.020	41.596	0.008	0.008	0.000	0.000	0.000
138	A	139	CYS	0	-0.072	-0.010	42.175	-0.001	-0.001	0.000	0.000	0.000
139	A	140	LEU	0	0.006	-0.013	39.034	0.008	0.008	0.000	0.000	0.000
140	A	141	ILE	0	0.001	-0.004	37.851	-0.006	-0.006	0.000	0.000	0.000
141	A	142	SER	0	0.024	-0.001	37.362	0.007	0.007	0.000	0.000	0.000
142	A	143	ASP	-1	-0.874	-0.945	36.846	0.051	0.051	0.000	0.000	0.000
143	A	144	PHE	0	0.029	0.028	33.494	-0.003	-0.003	0.000	0.000	0.000
144	A	145	TYR	0	0.014	0.003	29.258	0.005	0.005	0.000	0.000	0.000
145	A	146	PRO	0	0.071	0.018	31.600	-0.009	-0.009	0.000	0.000	0.000
146	A	147	GLY	0	0.022	0.010	30.311	-0.002	-0.002	0.000	0.000	0.000
147	A	148	ALA	0	-0.014	0.000	30.420	0.019	0.019	0.000	0.000	0.000
148	A	149	VAL	0	-0.013	-0.011	32.441	-0.013	-0.013	0.000	0.000	0.000
149	A	150	THR	0	-0.006	0.013	35.022	0.015	0.015	0.000	0.000	0.000
150	A	151	VAL	0	0.007	-0.001	37.572	-0.011	-0.011	0.000	0.000	0.000
151	A	152	ALA	0	-0.010	0.003	39.909	0.007	0.007	0.000	0.000	0.000
152	A	153	TRP	0	0.037	0.007	41.610	-0.011	-0.011	0.000	0.000	0.000
153	A	154	LYS	1	0.794	0.884	45.599	-0.082	-0.082	0.000	0.000	0.000
154	A	155	ALA	0	0.044	0.031	49.245	-0.002	-0.002	0.000	0.000	0.000
155	A	156	ASP	-1	-0.810	-0.920	52.046	0.073	0.073	0.000	0.000	0.000
156	A	157	SER	0	-0.037	-0.023	53.373	0.001	0.001	0.000	0.000	0.000
157	A	158	SER	0	-0.007	-0.001	52.278	0.002	0.002	0.000	0.000	0.000
158	A	159	PRO	0	-0.013	-0.020	46.924	0.002	0.002	0.000	0.000	0.000
159	A	160	VAL	0	0.015	0.018	45.561	-0.001	-0.001	0.000	0.000	0.000
160	A	161	LYS	1	0.917	0.950	44.788	-0.123	-0.123	0.000	0.000	0.000
161	A	162	ALA	0	0.001	0.006	43.179	0.007	0.007	0.000	0.000	0.000
162	A	163	GLY	0	0.075	0.028	42.735	-0.006	-0.006	0.000	0.000	0.000
163	A	164	VAL	0	-0.034	-0.002	39.138	-0.005	-0.005	0.000	0.000	0.000
164	A	165	GLU	-1	-0.893	-0.927	35.557	0.207	0.207	0.000	0.000	0.000
165	A	166	THR	0	-0.004	0.001	34.928	-0.018	-0.018	0.000	0.000	0.000
166	A	167	THR	0	-0.013	0.005	32.005	0.012	0.012	0.000	0.000	0.000
167	A	168	LYS	1	0.925	0.955	25.670	-0.300	-0.300	0.000	0.000	0.000
168	A	169	PRO	0	0.013	0.006	29.370	-0.007	-0.007	0.000	0.000	0.000
169	A	170	SER	0	-0.017	-0.008	28.041	0.019	0.019	0.000	0.000	0.000
170	A	171	LYS	1	0.849	0.935	26.010	-0.058	-0.058	0.000	0.000	0.000
171	A	172	GLN	0	0.026	0.011	29.053	0.008	0.008	0.000	0.000	0.000
172	A	173	SER	0	0.007	-0.011	31.341	-0.004	-0.004	0.000	0.000	0.000
173	A	174	ASN	0	-0.003	0.007	32.494	-0.005	-0.005	0.000	0.000	0.000
174	A	175	ASN	0	-0.041	-0.040	29.779	0.002	0.002	0.000	0.000	0.000
175	A	176	LYS	1	0.933	1.010	31.626	-0.035	-0.035	0.000	0.000	0.000
176	A	177	TYR	0	-0.009	-0.001	27.448	0.007	0.007	0.000	0.000	0.000
177	A	178	ALA	0	-0.008	-0.007	32.621	-0.008	-0.008	0.000	0.000	0.000
178	A	179	ALA	0	-0.019	-0.006	32.975	0.014	0.014	0.000	0.000	0.000
179	A	180	SER	0	0.010	0.014	34.961	-0.012	-0.012	0.000	0.000	0.000
180	A	181	SER	0	0.021	-0.007	36.750	0.010	0.010	0.000	0.000	0.000
181	A	182	TYR	0	-0.005	-0.003	36.952	-0.012	-0.012	0.000	0.000	0.000
182	A	183	LEU	0	0.003	0.011	41.385	0.007	0.007	0.000	0.000	0.000
183	A	184	SER	0	-0.013	-0.003	42.898	-0.007	-0.007	0.000	0.000	0.000
184	A	185	LEU	0	-0.043	-0.027	45.415	0.003	0.003	0.000	0.000	0.000
185	A	186	THR	0	0.063	0.031	49.048	-0.001	-0.001	0.000	0.000	0.000
186	A	187	PRO	0	0.056	0.014	51.964	-0.001	-0.001	0.000	0.000	0.000
187	A	188	GLU	-1	-0.869	-0.931	54.808	0.077	0.077	0.000	0.000	0.000
188	A	189	GLN	0	-0.020	-0.003	50.140	-0.001	-0.001	0.000	0.000	0.000
189	A	190	TRP	0	0.024	0.010	52.887	-0.001	-0.001	0.000	0.000	0.000
190	A	191	LYS	1	0.947	0.947	54.410	-0.063	-0.063	0.000	0.000	0.000
191	A	192	SER	0	-0.092	-0.014	56.684	-0.002	-0.002	0.000	0.000	0.000
192	A	193	HIS	1	0.836	0.925	54.381	-0.082	-0.082	0.000	0.000	0.000
193	A	194	ARG	1	0.946	0.974	57.664	-0.060	-0.060	0.000	0.000	0.000
194	A	195	SER	0	-0.037	-0.016	55.321	-0.002	-0.002	0.000	0.000	0.000
195	A	196	TYR	0	0.054	0.025	49.496	0.002	0.002	0.000	0.000	0.000
196	A	197	SER	0	-0.001	-0.001	49.762	-0.005	-0.005	0.000	0.000	0.000
197	A	199	GLN	0	-0.024	-0.041	44.784	-0.003	-0.003	0.000	0.000	0.000
198	A	200	VAL	0	0.042	0.009	39.851	0.008	0.008	0.000	0.000	0.000
199	A	201	THR	0	-0.029	-0.025	40.083	-0.005	-0.005	0.000	0.000	0.000
200	A	202	HIS	0	-0.031	-0.036	35.382	0.006	0.006	0.000	0.000	0.000
201	A	203	GLU	-1	-0.909	-0.959	35.455	0.102	0.102	0.000	0.000	0.000
202	A	204	GLY	0	-0.001	-0.010	38.637	-0.007	-0.007	0.000	0.000	0.000
203	A	205	SER	0	-0.031	-0.001	41.524	-0.006	-0.006	0.000	0.000	0.000
204	A	206	THR	0	0.007	-0.004	42.956	0.006	0.006	0.000	0.000	0.000
205	A	207	VAL	0	0.005	0.031	44.332	-0.006	-0.006	0.000	0.000	0.000
206	A	208	GLU	-1	-0.808	-0.896	45.642	0.086	0.086	0.000	0.000	0.000
207	A	209	LYS	1	0.878	0.958	47.524	-0.067	-0.067	0.000	0.000	0.000
208	A	210	THR	0	0.026	-0.005	49.587	0.003	0.003	0.000	0.000	0.000
209	A	211	VAL	0	-0.016	-0.004	51.004	-0.004	-0.004	0.000	0.000	0.000
210	A	212	ALA	0	0.049	0.008	53.536	0.003	0.003	0.000	0.000	0.000
211	A	213	PRO	0	0.000	0.001	56.474	-0.002	-0.002	0.000	0.000	0.000
212	A	214	THR	0	-0.021	0.004	57.898	-0.001	-0.001	0.000	0.000	0.000

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