FMO DATABASE

FMODB ID: 9G9L2

Calculation Name: 1ZQ7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ZQ7

Chain ID: A

ChEMBL ID:

UniProt ID: Q8PZK8

Base Structure: X-ray

Registration Date: 2023-06-20

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	OptHSide
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	204
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2237031.315509
FMO2-HF: Nuclear repulsion	2157452.538623
FMO2-HF: Total energy	-79578.776886
FMO2-MP2: Total energy	-79809.570338

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:MET)

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

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.
-29.797	-30.376	25.759	-10.79	-14.39	-0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.020 / q_NPA : -0.005

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	THR	0	-0.023	-0.044	3.692	-0.852	0.773	-0.003	-0.768	-0.854	0.000
4	A	4	GLU	-1	-0.855	-0.941	5.958	0.228	0.228	0.000	0.000	0.000	0.000
5	A	5	THR	0	-0.052	-0.031	8.528	0.115	0.115	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.752	-0.815	7.099	-0.196	-0.196	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.057	0.022	8.097	0.228	0.228	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.926	0.955	8.713	-0.182	-0.182	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.005	-0.007	11.906	-0.002	-0.002	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.052	0.022	9.452	0.003	0.003	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.016	0.006	11.565	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.796	0.905	13.940	-0.382	-0.382	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.003	0.019	14.024	-0.053	-0.053	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.017	0.021	14.892	-0.037	-0.037	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.741	0.854	16.786	-0.333	-0.333	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.890	0.942	19.545	-0.307	-0.307	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.042	-0.031	18.851	-0.033	-0.033	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.010	0.001	19.930	-0.028	-0.028	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.827	-0.924	23.087	0.242	0.242	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.022	-0.013	23.769	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	PHE	0	-0.042	-0.008	25.282	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.008	0.003	26.414	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.075	-0.006	28.864	-0.021	-0.021	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.849	0.917	29.484	-0.229	-0.229	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.029	0.017	30.706	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.772	0.872	28.193	-0.256	-0.256	0.000	0.000	0.000	0.000
27	A	27	SER	0	0.072	0.013	24.048	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	28	PRO	0	-0.085	-0.010	23.861	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	29	ARG	0	0.150	0.139	19.561	0.046	0.046	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.002	-0.012	22.635	-0.027	-0.027	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.842	-0.936	25.115	0.226	0.226	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.014	-0.013	25.913	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.039	0.010	19.776	0.002	0.002	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.024	-0.001	22.342	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.054	-0.021	16.034	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.936	-0.964	17.009	0.235	0.235	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.036	-0.013	13.393	0.029	0.029	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.033	-0.053	9.614	0.031	0.031	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.067	0.000	10.710	0.100	0.100	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.034	0.036	5.212	0.131	0.131	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.035	-0.029	8.106	0.557	0.557	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.879	-0.940	10.655	0.643	0.643	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.900	-0.925	5.183	3.314	3.326	-0.001	-0.001	-0.010	0.000
44	A	44	TYR	0	-0.053	-0.020	9.439	0.064	0.064	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.805	0.860	1.911	-19.557	-26.431	14.866	-4.203	-3.790	0.025
46	A	46	GLY	0	0.010	0.037	8.992	-0.326	-0.326	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.004	-0.023	8.977	0.608	0.608	0.000	0.000	0.000	0.000
48	A	48	PHE	0	-0.006	0.000	10.926	-0.329	-0.329	0.000	0.000	0.000	0.000
49	A	49	VAL	0	0.000	0.012	12.698	0.099	0.099	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.020	-0.030	15.321	-0.061	-0.061	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.019	0.027	17.477	0.003	0.003	0.000	0.000	0.000	0.000
52	A	52	THR	0	0.027	0.006	19.996	-0.032	-0.032	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.801	-0.910	22.644	0.182	0.182	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.009	-0.001	26.080	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.036	-0.018	24.231	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.028	-0.007	24.654	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.028	-0.009	20.461	0.015	0.015	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.764	0.857	23.315	-0.229	-0.229	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.041	0.024	22.869	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	60	CYS	0	-0.102	-0.055	17.062	0.028	0.028	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.009	-0.002	18.430	-0.042	-0.042	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.039	0.008	15.520	0.066	0.066	0.000	0.000	0.000	0.000
63	A	63	HIS	0	-0.067	-0.018	14.619	-0.047	-0.047	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.005	-0.005	13.398	0.191	0.191	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.035	0.015	12.474	0.130	0.130	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.001	0.024	10.484	0.072	0.072	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.888	-0.962	12.364	0.644	0.644	0.000	0.000	0.000	0.000
68	A	68	SER	0	-0.069	-0.039	14.416	-0.143	-0.143	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.028	0.015	12.347	0.203	0.203	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.042	0.020	7.170	-0.118	-0.118	0.000	0.000	0.000	0.000
71	A	71	LYN	0	-0.033	-0.027	11.075	-0.148	-0.148	0.000	0.000	0.000	0.000
72	A	72	GLH	0	-0.082	-0.099	13.972	-0.098	-0.098	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.040	0.028	12.863	-0.089	-0.089	0.000	0.000	0.000	0.000
74	A	74	ILE	0	0.005	0.013	10.305	-0.084	-0.084	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.039	-0.021	14.456	-0.114	-0.114	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.861	-0.934	18.101	0.492	0.492	0.000	0.000	0.000	0.000
77	A	77	SER	0	0.012	0.004	15.751	-0.067	-0.067	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.002	-0.005	17.205	-0.062	-0.062	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.009	0.003	18.714	-0.059	-0.059	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.024	-0.014	21.041	-0.064	-0.064	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.034	-0.004	19.432	-0.041	-0.041	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.026	0.021	21.590	-0.034	-0.034	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.056	-0.052	24.383	-0.035	-0.035	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.862	0.926	23.359	-0.394	-0.394	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.691	-0.805	23.700	0.311	0.311	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.023	-0.020	25.916	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.778	0.864	21.417	-0.315	-0.315	0.000	0.000	0.000	0.000
88	A	88	PHE	0	-0.031	-0.015	24.504	-0.017	-0.017	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.007	0.016	29.515	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	THR	0	0.021	-0.003	29.274	0.013	0.013	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.029	0.001	25.691	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.905	-0.959	28.983	0.175	0.175	0.000	0.000	0.000	0.000
93	A	93	GLN	0	-0.021	-0.032	29.801	0.009	0.009	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.989	-0.996	29.855	0.153	0.153	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.689	-0.835	28.783	0.188	0.188	0.000	0.000	0.000	0.000
96	A	96	MET	0	0.065	0.045	22.066	0.005	0.005	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.791	0.918	25.485	-0.130	-0.130	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.063	-0.043	27.545	-0.021	-0.021	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.011	0.029	22.284	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.050	-0.021	19.992	0.002	0.002	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.002	-0.010	16.057	0.020	0.020	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.830	-0.919	14.269	0.400	0.400	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.008	0.000	9.955	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	104	THR	0	-0.007	0.003	8.745	0.025	0.025	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.024	-0.012	5.100	-0.181	-0.181	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.000	0.006	5.298	0.890	0.890	0.000	0.000	0.000	0.000
107	A	107	THR	0	0.010	-0.001	2.116	0.876	0.299	5.515	-1.434	-3.504	0.004
108	A	108	GLN	0	-0.038	-0.034	4.185	-2.838	-2.687	0.003	-0.077	-0.077	0.000
109	A	109	PRO	0	-0.043	-0.021	6.761	-0.597	-0.597	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.911	-0.949	6.887	-1.052	-1.052	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.812	0.900	10.266	-0.141	-0.141	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.049	0.027	12.378	-0.086	-0.086	0.000	0.000	0.000	0.000
113	A	113	ASN	0	-0.070	-0.047	14.472	0.098	0.098	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.015	0.008	17.469	-0.034	-0.034	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.056	-0.034	19.548	0.038	0.038	0.000	0.000	0.000	0.000
116	A	116	PRO	0	0.057	0.000	21.551	-0.020	-0.020	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.860	0.917	22.498	0.101	0.101	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.723	-0.836	19.787	-0.255	-0.255	0.000	0.000	0.000	0.000
119	A	119	LEU	0	-0.024	0.006	17.053	-0.036	-0.036	0.000	0.000	0.000	0.000
120	A	120	PRO	0	0.012	-0.001	16.933	-0.040	-0.040	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.907	-0.952	17.533	-0.324	-0.324	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.772	0.876	13.909	0.316	0.316	0.000	0.000	0.000	0.000
123	A	123	VAL	0	-0.020	0.004	12.461	-0.094	-0.094	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.817	-0.900	9.359	-1.451	-1.451	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.002	-0.004	10.688	-0.079	-0.079	0.000	0.000	0.000	0.000
126	A	126	GLY	0	0.018	0.009	10.888	-0.043	-0.043	0.000	0.000	0.000	0.000
127	A	127	LYS	1	0.784	0.905	5.185	2.224	2.224	0.000	0.000	0.000	0.000
128	A	128	HIS	0	0.016	0.005	6.408	0.199	0.199	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.034	0.036	8.482	0.155	0.155	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.037	-0.031	10.208	-0.048	-0.048	0.000	0.000	0.000	0.000
131	A	131	ILE	0	0.031	0.004	12.297	0.085	0.085	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.038	-0.008	15.067	-0.056	-0.056	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.892	0.926	18.342	-0.194	-0.194	0.000	0.000	0.000	0.000
134	A	134	GLN	0	0.003	-0.009	20.375	-0.045	-0.045	0.000	0.000	0.000	0.000
135	A	135	GLY	0	-0.015	-0.002	24.022	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	136	TYR	0	-0.022	-0.027	23.647	0.021	0.021	0.000	0.000	0.000	0.000
137	A	137	CYS	0	-0.035	0.003	24.458	0.012	0.012	0.000	0.000	0.000	0.000
138	A	138	GLN	0	0.063	0.010	17.597	0.016	0.016	0.000	0.000	0.000	0.000
139	A	139	GLY	0	-0.015	-0.008	19.295	-0.004	-0.004	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.012	0.002	13.649	-0.013	-0.013	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.033	-0.006	14.935	0.004	0.004	0.000	0.000	0.000	0.000
142	A	142	LEU	0	0.013	0.000	11.611	0.005	0.005	0.000	0.000	0.000	0.000
143	A	143	PRO	0	0.071	0.022	7.564	0.005	0.005	0.000	0.000	0.000	0.000
144	A	144	GLN	0	0.034	0.032	10.332	-0.091	-0.091	0.000	0.000	0.000	0.000
145	A	145	VAL	0	-0.050	-0.028	12.747	0.002	0.002	0.000	0.000	0.000	0.000
146	A	146	ALA	0	0.040	0.013	14.254	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	147	PRO	0	0.009	0.015	12.541	0.007	0.007	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.829	-0.914	15.550	0.026	0.026	0.000	0.000	0.000	0.000
149	A	149	ASN	0	-0.146	-0.090	17.786	0.038	0.038	0.000	0.000	0.000	0.000
150	A	150	ASP	-1	-0.975	-0.971	19.720	-0.141	-0.141	0.000	0.000	0.000	0.000
151	A	151	MET	0	-0.054	0.000	18.210	0.025	0.025	0.000	0.000	0.000	0.000
152	A	152	ASP	-1	-0.804	-0.905	18.003	-0.229	-0.229	0.000	0.000	0.000	0.000
153	A	153	SER	0	0.024	-0.016	16.858	0.015	0.015	0.000	0.000	0.000	0.000
154	A	154	ILE	0	-0.040	-0.019	18.090	0.028	0.028	0.000	0.000	0.000	0.000
155	A	155	ASP	-1	-0.848	-0.905	20.689	-0.083	-0.083	0.000	0.000	0.000	0.000
156	A	156	PHE	0	0.009	0.009	12.452	0.045	0.045	0.000	0.000	0.000	0.000
157	A	157	LEU	0	0.009	0.016	16.957	0.049	0.049	0.000	0.000	0.000	0.000
158	A	158	SER	0	-0.012	-0.012	19.113	0.042	0.042	0.000	0.000	0.000	0.000
159	A	159	HIS	0	0.027	-0.001	20.314	0.023	0.023	0.000	0.000	0.000	0.000
160	A	160	THR	0	-0.004	-0.018	16.509	0.041	0.041	0.000	0.000	0.000	0.000
161	A	161	CYS	0	-0.095	-0.025	19.497	0.034	0.034	0.000	0.000	0.000	0.000
162	A	162	MET	0	0.012	0.016	22.322	0.017	0.017	0.000	0.000	0.000	0.000
163	A	163	LYS	1	0.879	0.953	19.424	-0.205	-0.205	0.000	0.000	0.000	0.000
164	A	164	ALA	0	-0.030	-0.011	21.280	0.030	0.030	0.000	0.000	0.000	0.000
165	A	165	GLY	0	-0.040	-0.013	22.963	0.005	0.005	0.000	0.000	0.000	0.000
166	A	166	LEU	0	-0.083	-0.038	23.477	-0.012	-0.012	0.000	0.000	0.000	0.000
167	A	167	SER	0	-0.018	-0.038	26.856	-0.004	-0.004	0.000	0.000	0.000	0.000
168	A	168	PRO	0	0.075	0.022	25.501	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	169	ASP	-1	-0.848	-0.906	25.017	-0.014	-0.014	0.000	0.000	0.000	0.000
170	A	170	ALA	0	0.004	-0.006	24.570	-0.007	-0.007	0.000	0.000	0.000	0.000
171	A	171	TRP	0	0.062	0.004	21.001	-0.008	-0.008	0.000	0.000	0.000	0.000
172	A	172	VAL	0	-0.063	-0.024	22.858	-0.017	-0.017	0.000	0.000	0.000	0.000
173	A	173	LYS	1	0.835	0.911	25.553	0.000	0.000	0.000	0.000	0.000	0.000
174	A	174	GLY	0	-0.007	0.002	24.217	0.007	0.007	0.000	0.000	0.000	0.000
175	A	175	ALA	0	-0.033	0.006	22.650	0.010	0.010	0.000	0.000	0.000	0.000
176	A	176	GLU	-1	-0.819	-0.878	18.850	0.129	0.129	0.000	0.000	0.000	0.000
177	A	177	VAL	0	0.029	0.013	14.743	0.033	0.033	0.000	0.000	0.000	0.000
178	A	178	TYR	0	-0.069	-0.051	12.428	-0.038	-0.038	0.000	0.000	0.000	0.000
179	A	179	CYS	0	0.034	0.029	8.519	0.021	0.021	0.000	0.000	0.000	0.000
180	A	180	PHE	0	-0.031	-0.008	6.450	0.100	0.100	0.000	0.000	0.000	0.000
181	A	181	GLU	-1	-0.798	-0.917	2.472	-9.569	-8.236	2.255	-1.382	-2.207	-0.015
182	A	182	GLY	0	0.022	-0.009	3.542	2.046	2.462	0.009	-0.110	-0.314	0.000
183	A	183	GLN	0	-0.016	0.009	2.389	-5.192	-1.899	3.116	-2.806	-3.603	-0.025
184	A	184	ILE	0	0.015	0.007	5.391	0.127	0.169	-0.001	-0.009	-0.031	0.000
185	A	185	PHE	0	0.039	0.045	5.545	-0.168	-0.168	0.000	0.000	0.000	0.000
186	A	186	LYS	1	0.855	0.901	10.584	-0.326	-0.326	0.000	0.000	0.000	0.000
187	A	187	GLU	-1	-0.755	-0.866	14.350	0.278	0.278	0.000	0.000	0.000	0.000
188	A	188	LYS	1	0.911	0.962	17.568	-0.100	-0.100	0.000	0.000	0.000	0.000
189	A	189	GLU	-1	-0.941	-0.985	19.933	0.090	0.090	0.000	0.000	0.000	0.000
190	A	190	PRO	0	0.028	0.023	21.294	0.026	0.026	0.000	0.000	0.000	0.000
191	A	191	ASP	-1	-0.880	-0.944	21.026	0.239	0.239	0.000	0.000	0.000	0.000
192	A	192	GLY	0	-0.043	-0.016	21.393	-0.018	-0.018	0.000	0.000	0.000	0.000
193	A	193	GLU	-1	-0.980	-1.013	17.597	0.123	0.123	0.000	0.000	0.000	0.000
194	A	194	VAL	0	-0.050	-0.021	12.847	0.019	0.019	0.000	0.000	0.000	0.000
195	A	195	ILE	0	0.011	0.018	13.596	-0.034	-0.034	0.000	0.000	0.000	0.000
196	A	196	GLU	-1	-0.832	-0.919	6.105	1.272	1.272	0.000	0.000	0.000	0.000
197	A	197	GLU	-1	-0.926	-0.941	10.525	-0.161	-0.161	0.000	0.000	0.000	0.000
198	A	198	LYS	1	0.851	0.888	7.327	0.327	0.327	0.000	0.000	0.000	0.000
199	A	199	PHE	0	-0.047	-0.010	7.289	-0.329	-0.329	0.000	0.000	0.000	0.000
200	A	200	LEU	0	-0.017	-0.010	6.353	0.229	0.229	0.000	0.000	0.000	0.000
201	A	201	GLU	-1	-0.912	-0.961	9.725	-0.385	-0.385	0.000	0.000	0.000	0.000
202	A	202	HIS	0	-0.069	-0.023	12.687	-0.030	-0.030	0.000	0.000	0.000	0.000
203	A	203	HIS	0	-0.079	-0.043	16.001	-0.017	-0.017	0.000	0.000	0.000	0.000
204	A	204	HIS	0	-0.013	-0.003	13.043	0.052	0.052	0.000	0.000	0.000	0.000

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