FMO DATABASE

FMODB ID: VQMR1

Calculation Name: 1Z9S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1Z9S

Chain ID: A

ChEMBL ID:

UniProt ID: P26926

Base Structure: X-ray

Registration Date: 2023-09-24

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	205
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2217450.200392
FMO2-HF: Nuclear repulsion	2138013.937741
FMO2-HF: Total energy	-79436.262651
FMO2-MP2: Total energy	-79671.411834

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:9:SER)

Summations of interaction energy for fragment #1(A:9:SER)

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.
1.036	4.197	-0.012	-1.583	-1.567	0.006

Interaction energy analysis for fragmet #1(A:9:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.019 / q_NPA : 0.017

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	11	GLU	-1	-0.816	-0.894	3.738	1.582	4.743	-0.012	-1.583	-1.567	0.006
4	A	12	TYR	0	-0.049	-0.035	6.178	-0.507	-0.507	0.000	0.000	0.000	0.000
5	A	13	GLY	0	0.016	0.017	9.495	0.132	0.132	0.000	0.000	0.000	0.000
6	A	14	VAL	0	-0.010	-0.003	12.610	-0.054	-0.054	0.000	0.000	0.000	0.000
7	A	15	THR	0	-0.006	0.002	16.322	0.033	0.033	0.000	0.000	0.000	0.000
8	A	16	ILE	0	-0.028	-0.009	19.102	-0.018	-0.018	0.000	0.000	0.000	0.000
9	A	17	GLY	0	-0.013	-0.020	22.689	0.009	0.009	0.000	0.000	0.000	0.000
10	A	18	GLU	-1	-0.893	-0.938	25.379	0.006	0.006	0.000	0.000	0.000	0.000
11	A	19	SER	0	0.012	-0.010	25.112	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	20	ARG	1	0.817	0.905	26.056	-0.033	-0.033	0.000	0.000	0.000	0.000
13	A	21	ILE	0	0.074	0.047	29.114	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	22	ILE	0	-0.006	0.007	31.986	0.001	0.001	0.000	0.000	0.000	0.000
15	A	23	TYR	0	0.003	-0.017	35.610	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	24	PRO	0	-0.010	-0.002	37.461	0.001	0.001	0.000	0.000	0.000	0.000
17	A	25	LEU	0	-0.017	-0.009	41.226	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	26	ASP	-1	-0.820	-0.899	43.000	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	27	ALA	0	-0.038	0.002	41.075	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	28	ALA	0	0.012	0.001	42.002	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	29	GLY	0	-0.006	-0.022	38.265	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	30	VAL	0	-0.053	-0.008	33.746	0.001	0.001	0.000	0.000	0.000	0.000
23	A	31	MET	0	-0.019	-0.010	32.513	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	32	VAL	0	0.060	0.044	27.067	0.003	0.003	0.000	0.000	0.000	0.000
25	A	33	SER	0	-0.011	-0.002	25.878	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	34	VAL	0	0.035	0.022	21.443	0.007	0.007	0.000	0.000	0.000	0.000
27	A	35	LYS	1	0.924	0.954	18.161	0.040	0.040	0.000	0.000	0.000	0.000
28	A	36	ASN	0	-0.012	-0.012	15.518	0.024	0.024	0.000	0.000	0.000	0.000
29	A	37	THR	0	-0.055	-0.041	13.109	-0.018	-0.018	0.000	0.000	0.000	0.000
30	A	38	GLN	0	0.017	0.030	8.992	0.072	0.072	0.000	0.000	0.000	0.000
31	A	39	ASP	-1	-0.857	-0.944	10.093	-0.371	-0.371	0.000	0.000	0.000	0.000
32	A	40	TYR	0	-0.036	-0.049	9.454	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	41	PRO	0	-0.032	-0.004	14.200	0.054	0.054	0.000	0.000	0.000	0.000
34	A	42	VAL	0	0.016	0.005	15.184	-0.038	-0.038	0.000	0.000	0.000	0.000
35	A	43	LEU	0	-0.007	-0.005	17.951	0.025	0.025	0.000	0.000	0.000	0.000
36	A	44	ILE	0	0.002	0.005	19.625	0.000	0.000	0.000	0.000	0.000	0.000
37	A	45	GLN	0	-0.005	-0.016	21.756	0.006	0.006	0.000	0.000	0.000	0.000
38	A	46	SER	0	0.014	0.004	23.289	0.006	0.006	0.000	0.000	0.000	0.000
39	A	47	ARG	1	0.898	0.954	25.529	0.050	0.050	0.000	0.000	0.000	0.000
40	A	48	ILE	0	0.039	0.022	27.711	0.004	0.004	0.000	0.000	0.000	0.000
41	A	49	TYR	0	-0.051	-0.025	26.150	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	50	ASP	-1	-0.704	-0.861	31.102	0.005	0.005	0.000	0.000	0.000	0.000
43	A	51	GLU	-1	-0.920	-0.959	32.101	0.017	0.017	0.000	0.000	0.000	0.000
44	A	52	ASN	0	-0.030	-0.003	32.558	0.007	0.007	0.000	0.000	0.000	0.000
45	A	53	LYS	1	0.821	0.922	25.423	-0.020	-0.020	0.000	0.000	0.000	0.000
46	A	54	GLU	-1	-0.899	-0.960	29.936	0.002	0.002	0.000	0.000	0.000	0.000
47	A	55	LYS	1	0.692	0.826	30.018	0.026	0.026	0.000	0.000	0.000	0.000
48	A	56	GLU	-1	-0.755	-0.866	33.059	-0.026	-0.026	0.000	0.000	0.000	0.000
49	A	57	SER	0	-0.037	-0.021	36.696	0.002	0.002	0.000	0.000	0.000	0.000
50	A	58	GLU	-1	-0.894	-0.940	38.812	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	59	ASP	-1	-0.923	-0.966	39.269	-0.023	-0.023	0.000	0.000	0.000	0.000
52	A	60	PRO	0	-0.013	0.012	36.244	0.000	0.000	0.000	0.000	0.000	0.000
53	A	61	PHE	0	-0.002	-0.007	34.932	0.001	0.001	0.000	0.000	0.000	0.000
54	A	62	VAL	0	0.030	0.017	34.776	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	63	VAL	0	-0.018	-0.014	28.779	0.001	0.001	0.000	0.000	0.000	0.000
56	A	64	THR	0	-0.061	0.000	32.094	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	65	PRO	0	0.030	-0.012	29.007	0.003	0.003	0.000	0.000	0.000	0.000
58	A	66	PRO	0	0.051	0.025	28.712	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	67	LEU	0	-0.008	-0.031	23.902	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	68	PHE	0	0.001	0.011	24.842	0.002	0.002	0.000	0.000	0.000	0.000
61	A	69	ARG	1	0.906	0.956	21.056	0.206	0.206	0.000	0.000	0.000	0.000
62	A	70	LEU	0	-0.032	-0.002	20.557	0.013	0.013	0.000	0.000	0.000	0.000
63	A	71	ASP	-1	-0.778	-0.898	19.591	-0.216	-0.216	0.000	0.000	0.000	0.000
64	A	72	ALA	0	0.048	0.023	15.914	0.018	0.018	0.000	0.000	0.000	0.000
65	A	73	LYS	1	0.825	0.914	12.588	0.154	0.154	0.000	0.000	0.000	0.000
66	A	74	GLN	0	-0.021	0.005	17.910	0.037	0.037	0.000	0.000	0.000	0.000
67	A	75	GLN	0	-0.011	-0.019	20.775	0.013	0.013	0.000	0.000	0.000	0.000
68	A	76	ASN	0	0.013	0.009	23.391	0.002	0.002	0.000	0.000	0.000	0.000
69	A	77	SER	0	-0.034	-0.018	26.339	0.008	0.008	0.000	0.000	0.000	0.000
70	A	78	LEU	0	-0.012	0.011	25.805	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	79	ARG	1	0.993	0.990	29.772	0.029	0.029	0.000	0.000	0.000	0.000
72	A	80	ILE	0	-0.034	-0.016	30.041	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	81	ALA	0	0.023	-0.007	33.948	0.002	0.002	0.000	0.000	0.000	0.000
74	A	82	GLN	0	0.033	0.032	37.565	0.000	0.000	0.000	0.000	0.000	0.000
75	A	83	ALA	0	-0.025	-0.017	39.790	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	84	GLY	0	0.008	0.021	41.521	0.000	0.000	0.000	0.000	0.000	0.000
77	A	85	GLY	0	0.040	0.007	43.525	0.001	0.001	0.000	0.000	0.000	0.000
78	A	86	VAL	0	-0.012	-0.012	44.632	0.000	0.000	0.000	0.000	0.000	0.000
79	A	87	PHE	0	-0.004	-0.009	39.666	0.001	0.001	0.000	0.000	0.000	0.000
80	A	88	PRO	0	-0.034	0.001	43.441	0.000	0.000	0.000	0.000	0.000	0.000
81	A	89	ARG	1	0.866	0.875	45.420	0.002	0.002	0.000	0.000	0.000	0.000
82	A	90	ASP	-1	-0.887	-0.935	47.700	0.009	0.009	0.000	0.000	0.000	0.000
83	A	91	LYS	1	0.914	0.923	43.372	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	92	GLU	-1	-0.733	-0.847	38.430	0.014	0.014	0.000	0.000	0.000	0.000
85	A	93	SER	0	-0.020	-0.007	39.206	0.000	0.000	0.000	0.000	0.000	0.000
86	A	94	LEU	0	-0.044	-0.010	31.588	0.000	0.000	0.000	0.000	0.000	0.000
87	A	95	LYS	1	0.920	0.979	33.166	0.001	0.001	0.000	0.000	0.000	0.000
88	A	96	TRP	0	-0.042	-0.024	25.957	0.007	0.007	0.000	0.000	0.000	0.000
89	A	97	LEU	0	0.055	0.036	26.233	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	98	CYS	0	-0.105	-0.041	19.614	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	99	VAL	0	0.047	0.012	21.027	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	100	LYS	1	0.966	0.978	17.973	0.103	0.103	0.000	0.000	0.000	0.000
93	A	101	GLY	0	0.003	0.010	16.635	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	102	ILE	0	-0.066	-0.044	15.698	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	103	PRO	0	0.014	0.006	12.322	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	104	PRO	0	-0.001	0.015	13.465	0.002	0.002	0.000	0.000	0.000	0.000
97	A	125	ASP	-1	-0.935	-0.977	17.206	0.120	0.120	0.000	0.000	0.000	0.000
98	A	126	VAL	0	-0.031	-0.013	16.135	-0.022	-0.022	0.000	0.000	0.000	0.000
99	A	127	GLY	0	0.021	0.022	14.106	0.031	0.031	0.000	0.000	0.000	0.000
100	A	128	VAL	0	-0.002	-0.009	10.756	-0.033	-0.033	0.000	0.000	0.000	0.000
101	A	129	PHE	0	0.008	-0.006	8.728	-0.051	-0.051	0.000	0.000	0.000	0.000
102	A	130	VAL	0	0.036	0.026	8.141	0.021	0.021	0.000	0.000	0.000	0.000
103	A	131	GLN	0	0.017	0.010	8.557	-0.246	-0.246	0.000	0.000	0.000	0.000
104	A	132	PHE	0	-0.001	0.003	7.659	0.117	0.117	0.000	0.000	0.000	0.000
105	A	133	ALA	0	0.019	-0.010	11.299	-0.055	-0.055	0.000	0.000	0.000	0.000
106	A	134	ILE	0	0.011	0.027	11.458	0.033	0.033	0.000	0.000	0.000	0.000
107	A	135	ASN	0	0.021	-0.012	14.665	-0.024	-0.024	0.000	0.000	0.000	0.000
108	A	136	ASN	0	-0.015	0.003	18.296	0.019	0.019	0.000	0.000	0.000	0.000
109	A	138	ILE	0	0.024	0.019	23.175	0.010	0.010	0.000	0.000	0.000	0.000
110	A	139	LYS	1	0.835	0.916	25.837	-0.042	-0.042	0.000	0.000	0.000	0.000
111	A	140	LEU	0	0.025	0.030	29.478	0.000	0.000	0.000	0.000	0.000	0.000
112	A	141	LEU	0	-0.021	-0.026	32.165	0.001	0.001	0.000	0.000	0.000	0.000
113	A	142	VAL	0	0.014	0.018	35.277	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	143	ARG	1	0.774	0.831	37.643	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	144	PRO	0	0.020	0.024	41.095	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	145	ASN	0	0.025	0.010	44.828	0.002	0.002	0.000	0.000	0.000	0.000
117	A	146	GLU	-1	-0.843	-0.926	46.634	0.002	0.002	0.000	0.000	0.000	0.000
118	A	147	LEU	0	-0.071	-0.017	43.169	0.001	0.001	0.000	0.000	0.000	0.000
119	A	148	LYS	1	0.937	0.966	46.843	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	149	GLY	0	0.012	0.005	45.441	0.001	0.001	0.000	0.000	0.000	0.000
121	A	150	THR	0	-0.002	0.001	39.865	0.000	0.000	0.000	0.000	0.000	0.000
122	A	151	PRO	0	0.060	0.022	37.333	0.001	0.001	0.000	0.000	0.000	0.000
123	A	152	ILE	0	0.045	0.003	37.741	0.001	0.001	0.000	0.000	0.000	0.000
124	A	153	GLN	0	-0.047	-0.014	40.130	0.000	0.000	0.000	0.000	0.000	0.000
125	A	154	PHE	0	0.020	0.008	42.588	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	155	ALA	0	0.016	0.022	39.160	0.001	0.001	0.000	0.000	0.000	0.000
127	A	156	GLU	-1	-0.916	-0.959	40.896	0.029	0.029	0.000	0.000	0.000	0.000
128	A	157	ASN	0	-0.073	-0.074	43.394	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	158	LEU	0	-0.012	0.027	38.513	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	159	SER	0	-0.025	0.003	43.158	0.001	0.001	0.000	0.000	0.000	0.000
131	A	160	TRP	0	0.068	0.010	36.888	0.002	0.002	0.000	0.000	0.000	0.000
132	A	161	LYS	1	0.990	0.990	43.378	-0.027	-0.027	0.000	0.000	0.000	0.000
133	A	162	VAL	0	-0.007	0.005	42.142	0.002	0.002	0.000	0.000	0.000	0.000
134	A	163	ASP	-1	-0.920	-0.962	43.454	0.027	0.027	0.000	0.000	0.000	0.000
135	A	164	GLY	0	0.067	0.038	43.124	0.001	0.001	0.000	0.000	0.000	0.000
136	A	165	GLY	0	-0.047	-0.015	41.785	0.001	0.001	0.000	0.000	0.000	0.000
137	A	166	LYS	1	0.883	0.927	36.505	-0.041	-0.041	0.000	0.000	0.000	0.000
138	A	167	LEU	0	-0.013	0.011	36.892	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	168	ILE	0	0.003	0.000	38.637	0.001	0.001	0.000	0.000	0.000	0.000
140	A	169	ALA	0	-0.015	0.000	38.652	0.000	0.000	0.000	0.000	0.000	0.000
141	A	170	GLU	-1	-0.883	-0.948	40.691	0.022	0.022	0.000	0.000	0.000	0.000
142	A	171	ASN	0	-0.034	-0.012	40.057	0.000	0.000	0.000	0.000	0.000	0.000
143	A	172	PRO	0	0.033	0.019	42.906	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	173	SER	0	-0.005	-0.015	42.529	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	174	PRO	0	0.010	-0.015	44.066	0.000	0.000	0.000	0.000	0.000	0.000
146	A	175	PHE	0	0.024	0.000	39.594	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	176	TYR	0	-0.032	-0.034	35.455	0.002	0.002	0.000	0.000	0.000	0.000
148	A	177	MET	0	-0.017	0.018	36.818	0.002	0.002	0.000	0.000	0.000	0.000
149	A	178	ASN	0	0.032	-0.011	31.211	0.003	0.003	0.000	0.000	0.000	0.000
150	A	179	ILE	0	-0.002	0.007	31.872	0.001	0.001	0.000	0.000	0.000	0.000
151	A	180	GLY	0	0.003	-0.019	28.870	0.002	0.002	0.000	0.000	0.000	0.000
152	A	181	GLU	-1	-0.904	-0.958	28.436	0.075	0.075	0.000	0.000	0.000	0.000
153	A	182	LEU	0	0.015	0.013	30.727	-0.006	-0.006	0.000	0.000	0.000	0.000
154	A	183	THR	0	-0.021	-0.001	32.217	0.007	0.007	0.000	0.000	0.000	0.000
155	A	184	PHE	0	0.025	0.008	34.627	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	185	GLY	0	0.011	-0.019	37.011	0.002	0.002	0.000	0.000	0.000	0.000
157	A	186	GLY	0	-0.013	-0.004	36.478	0.001	0.001	0.000	0.000	0.000	0.000
158	A	187	LYS	1	0.910	0.968	33.209	-0.067	-0.067	0.000	0.000	0.000	0.000
159	A	188	SER	0	0.049	0.022	29.135	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	189	ILE	0	-0.038	-0.014	30.733	0.003	0.003	0.000	0.000	0.000	0.000
161	A	190	PRO	0	-0.011	-0.002	26.595	0.001	0.001	0.000	0.000	0.000	0.000
162	A	191	SER	0	0.022	0.007	28.045	-0.005	-0.005	0.000	0.000	0.000	0.000
163	A	192	HIS	1	0.887	0.938	28.712	-0.039	-0.039	0.000	0.000	0.000	0.000
164	A	193	TYR	0	-0.022	0.003	30.787	0.001	0.001	0.000	0.000	0.000	0.000
165	A	194	ILE	0	-0.002	0.018	33.274	0.000	0.000	0.000	0.000	0.000	0.000
166	A	195	PRO	0	0.022	0.005	37.011	-0.001	-0.001	0.000	0.000	0.000	0.000
167	A	196	PRO	0	-0.011	0.006	38.716	0.001	0.001	0.000	0.000	0.000	0.000
168	A	197	LYS	1	0.859	0.945	41.818	-0.013	-0.013	0.000	0.000	0.000	0.000
169	A	198	SER	0	0.025	0.034	41.676	0.000	0.000	0.000	0.000	0.000	0.000
170	A	199	THR	0	-0.011	-0.012	41.362	0.001	0.001	0.000	0.000	0.000	0.000
171	A	200	TRP	0	0.032	-0.005	32.869	-0.002	-0.002	0.000	0.000	0.000	0.000
172	A	201	ALA	0	0.003	0.008	37.554	0.001	0.001	0.000	0.000	0.000	0.000
173	A	202	PHE	0	-0.033	-0.020	32.238	0.001	0.001	0.000	0.000	0.000	0.000
174	A	203	ASP	-1	-0.843	-0.928	32.768	0.051	0.051	0.000	0.000	0.000	0.000
175	A	204	LEU	0	-0.016	-0.014	34.037	0.003	0.003	0.000	0.000	0.000	0.000
176	A	205	PRO	0	-0.004	-0.012	34.347	0.004	0.004	0.000	0.000	0.000	0.000
177	A	206	LYS	1	0.919	0.991	28.551	-0.086	-0.086	0.000	0.000	0.000	0.000
178	A	207	GLY	0	0.004	-0.013	33.818	0.003	0.003	0.000	0.000	0.000	0.000
179	A	208	LEU	0	-0.005	-0.021	36.411	0.002	0.002	0.000	0.000	0.000	0.000
180	A	209	ALA	0	0.009	-0.003	39.496	-0.002	-0.002	0.000	0.000	0.000	0.000
181	A	210	GLY	0	0.042	0.035	42.418	-0.002	-0.002	0.000	0.000	0.000	0.000
182	A	211	ALA	0	-0.049	0.013	41.168	-0.001	-0.001	0.000	0.000	0.000	0.000
183	A	212	ARG	1	0.947	0.958	43.121	-0.034	-0.034	0.000	0.000	0.000	0.000
184	A	213	ASN	0	0.013	0.029	40.285	-0.003	-0.003	0.000	0.000	0.000	0.000
185	A	214	VAL	0	-0.006	0.003	38.419	0.003	0.003	0.000	0.000	0.000	0.000
186	A	215	SER	0	0.001	-0.006	36.995	-0.002	-0.002	0.000	0.000	0.000	0.000
187	A	216	TRP	0	-0.023	-0.021	35.223	0.004	0.004	0.000	0.000	0.000	0.000
188	A	217	ARG	1	0.944	0.990	32.329	-0.058	-0.058	0.000	0.000	0.000	0.000
189	A	218	ILE	0	0.011	0.010	33.203	0.003	0.003	0.000	0.000	0.000	0.000
190	A	219	ILE	0	-0.039	0.003	28.545	0.001	0.001	0.000	0.000	0.000	0.000
191	A	220	ASN	0	0.040	0.018	31.955	-0.004	-0.004	0.000	0.000	0.000	0.000
192	A	221	ASP	-1	-0.716	-0.855	32.573	0.019	0.019	0.000	0.000	0.000	0.000
193	A	222	GLN	0	0.016	0.005	32.070	0.001	0.001	0.000	0.000	0.000	0.000
194	A	223	GLY	0	-0.052	-0.031	28.654	0.002	0.002	0.000	0.000	0.000	0.000
195	A	224	GLY	0	-0.019	-0.004	28.304	0.007	0.007	0.000	0.000	0.000	0.000
196	A	225	LEU	0	-0.023	-0.025	28.537	-0.003	-0.003	0.000	0.000	0.000	0.000
197	A	226	ASP	-1	-0.855	-0.913	31.192	0.033	0.033	0.000	0.000	0.000	0.000
198	A	227	ARG	1	0.917	0.944	34.801	-0.026	-0.026	0.000	0.000	0.000	0.000
199	A	228	LEU	0	-0.051	-0.023	35.504	0.000	0.000	0.000	0.000	0.000	0.000
200	A	229	TYR	0	0.031	0.028	37.950	-0.003	-0.003	0.000	0.000	0.000	0.000
201	A	230	SER	0	0.017	-0.016	39.706	0.004	0.004	0.000	0.000	0.000	0.000
202	A	231	LYS	1	0.872	0.959	42.200	-0.030	-0.030	0.000	0.000	0.000	0.000
203	A	232	ASN	0	0.005	-0.012	43.641	0.003	0.003	0.000	0.000	0.000	0.000
204	A	233	VAL	0	-0.024	0.001	43.186	-0.001	-0.001	0.000	0.000	0.000	0.000
205	A	234	THR	0	-0.008	-0.015	45.784	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:SER)