FMO DATABASE

FMODB ID: YV8K2

Calculation Name: 4INK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4INK

Chain ID: A

ChEMBL ID:

UniProt ID: Q2FXC5

Base Structure: X-ray

Registration Date: 2023-09-23

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	203
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2299339.197808
FMO2-HF: Nuclear repulsion	2222599.887033
FMO2-HF: Total energy	-76739.310775
FMO2-MP2: Total energy	-76965.515951

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:GLU)

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

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.
-69.596	-67.253	0.183	-1.278	-1.247	-0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.929 / q_NPA : -0.965

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	SER	0	-0.009	0.001	3.005	0.453	2.796	0.183	-1.278	-1.247	-0.002
4	A	4	VAL	0	0.012	0.003	5.490	-2.741	-2.741	0.000	0.000	0.000	0.000
5	A	5	LYS	1	0.929	0.963	6.077	-27.016	-27.016	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.033	0.026	11.798	-0.699	-0.699	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.031	-0.013	14.602	0.054	0.054	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.032	0.011	17.260	-0.716	-0.716	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.028	0.002	19.575	-0.920	-0.920	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.006	-0.007	20.806	0.183	0.183	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.076	-0.047	22.160	-0.401	-0.401	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.037	0.023	20.235	-0.405	-0.405	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.037	0.040	21.428	0.327	0.327	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.018	-0.003	16.801	0.207	0.207	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.014	-0.022	13.919	-0.574	-0.574	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.013	-0.025	20.337	-0.169	-0.169	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.010	0.005	22.945	-0.533	-0.533	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.021	-0.003	19.948	-0.169	-0.169	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.042	-0.049	23.421	-0.290	-0.290	0.000	0.000	0.000	0.000
20	A	20	TRP	0	-0.018	0.009	23.621	0.497	0.497	0.000	0.000	0.000	0.000
21	A	21	MET	0	0.016	0.017	27.179	-0.442	-0.442	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.031	0.016	29.557	-0.249	-0.249	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.007	-0.020	28.882	0.065	0.065	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.024	0.009	25.116	0.261	0.261	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.007	0.007	21.067	-0.189	-0.189	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.025	0.028	24.033	-0.311	-0.311	0.000	0.000	0.000	0.000
27	A	27	PHE	0	-0.008	-0.007	23.106	0.372	0.372	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.005	0.014	25.231	-0.341	-0.341	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.049	0.020	26.606	0.252	0.252	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.011	-0.023	28.935	-0.212	-0.212	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.091	-0.074	31.970	0.216	0.216	0.000	0.000	0.000	0.000
32	A	32	HIS	1	0.775	0.864	34.745	-7.770	-7.770	0.000	0.000	0.000	0.000
33	A	33	THR	0	0.018	-0.007	32.337	-0.186	-0.186	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.014	-0.010	28.488	0.230	0.230	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.011	0.018	26.234	-0.283	-0.283	0.000	0.000	0.000	0.000
36	A	36	THR	0	0.024	-0.012	26.193	0.306	0.306	0.000	0.000	0.000	0.000
37	A	37	ASN	0	-0.010	-0.027	24.252	0.184	0.184	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.871	0.935	27.873	-9.555	-9.555	0.000	0.000	0.000	0.000
39	A	39	HIS	0	-0.071	-0.047	24.914	-0.111	-0.111	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.060	-0.017	26.766	-0.044	-0.044	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.003	-0.050	30.029	-0.102	-0.102	0.000	0.000	0.000	0.000
42	A	42	TYR	0	-0.025	0.010	33.345	-0.273	-0.273	0.000	0.000	0.000	0.000
43	A	43	HIS	0	0.034	-0.002	34.045	-0.381	-0.381	0.000	0.000	0.000	0.000
44	A	44	MET	0	-0.028	0.032	32.906	-0.097	-0.097	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.812	0.892	36.466	-8.071	-8.071	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.000	-0.001	39.332	0.118	0.118	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.018	0.012	41.074	-0.162	-0.162	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.814	-0.889	36.949	8.007	8.007	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.826	-0.886	35.975	7.829	7.829	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.016	0.007	31.001	0.230	0.230	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.834	0.907	29.203	-9.886	-9.886	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.027	0.010	28.689	0.366	0.366	0.000	0.000	0.000	0.000
53	A	53	HIS	1	0.846	0.934	24.070	-10.825	-10.825	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.031	0.006	25.552	-0.018	-0.018	0.000	0.000	0.000	0.000
55	A	55	ASN	0	0.002	-0.005	21.531	0.727	0.727	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.054	0.031	24.862	-0.222	-0.222	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.015	-0.007	26.214	-0.319	-0.319	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.023	-0.004	28.796	-0.192	-0.192	0.000	0.000	0.000	0.000
59	A	59	ASN	0	0.007	0.026	28.364	-0.154	-0.154	0.000	0.000	0.000	0.000
60	A	60	ASN	0	0.041	-0.002	30.324	0.203	0.203	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.057	0.048	28.366	-0.055	-0.055	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.001	0.006	29.147	-0.306	-0.306	0.000	0.000	0.000	0.000
63	A	63	GLY	0	-0.029	-0.024	30.891	-0.365	-0.365	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.014	0.005	32.558	0.264	0.264	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.026	-0.019	33.162	-0.260	-0.260	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.896	0.947	36.139	-7.212	-7.212	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.007	0.006	35.628	0.026	0.026	0.000	0.000	0.000	0.000
68	A	68	THR	0	-0.009	-0.019	38.192	-0.145	-0.145	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.847	0.929	38.495	-7.875	-7.875	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.038	0.015	35.670	0.240	0.240	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.024	-0.013	35.842	-0.248	-0.248	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.782	-0.877	34.103	9.016	9.016	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.080	-0.032	31.887	-0.334	-0.334	0.000	0.000	0.000	0.000
74	A	74	PRO	0	0.002	-0.004	34.270	0.062	0.062	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.013	0.029	34.399	-0.108	-0.108	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.873	0.905	30.395	-9.749	-9.749	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.758	-0.860	27.723	10.299	10.299	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.745	-0.861	26.885	10.551	10.551	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.044	-0.014	26.796	0.413	0.413	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.041	0.021	28.969	-0.396	-0.396	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.041	-0.015	30.177	0.306	0.306	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.006	0.002	32.398	-0.246	-0.246	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.065	-0.043	33.720	-0.037	-0.037	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.037	0.019	34.326	-0.027	-0.027	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.883	-0.946	37.252	6.970	6.970	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.811	-0.885	38.031	7.590	7.590	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.792	0.901	38.661	-7.089	-7.089	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.012	-0.026	37.042	0.006	0.006	0.000	0.000	0.000	0.000
89	A	89	THR	0	-0.008	-0.036	38.409	-0.251	-0.251	0.000	0.000	0.000	0.000
90	A	90	GLN	0	0.000	0.013	37.897	-0.290	-0.290	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.015	0.011	35.795	0.254	0.254	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.956	0.980	38.832	-7.016	-7.016	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.033	0.017	40.681	0.060	0.060	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.863	0.933	32.788	-8.666	-8.666	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.919	0.949	37.035	-7.428	-7.428	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.063	0.027	30.778	0.159	0.159	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.855	0.919	32.690	-7.552	-7.552	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.847	-0.892	32.616	8.023	8.023	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.000	-0.005	31.369	0.046	0.046	0.000	0.000	0.000	0.000
100	A	100	THR	0	-0.058	-0.030	28.159	0.317	0.317	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.043	0.023	24.669	-0.091	-0.091	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.820	0.940	25.790	-8.792	-8.792	0.000	0.000	0.000	0.000
103	A	103	PHE	0	0.019	0.010	19.422	0.103	0.103	0.000	0.000	0.000	0.000
104	A	104	ASN	0	0.002	0.006	24.023	-0.554	-0.554	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.034	-0.019	23.302	0.465	0.465	0.000	0.000	0.000	0.000
106	A	106	ALA	0	0.028	0.027	20.580	-0.260	-0.260	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.009	-0.032	22.693	-0.327	-0.327	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.921	-0.938	21.644	11.398	11.398	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.005	-0.001	17.769	0.398	0.398	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.860	0.913	15.820	-16.274	-16.274	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.841	-0.922	15.218	17.912	17.912	0.000	0.000	0.000	0.000
112	A	112	ASN	0	-0.012	-0.022	11.267	2.045	2.045	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.870	-0.896	10.466	17.543	17.543	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.005	0.003	7.971	0.679	0.679	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.073	-0.034	9.218	-1.903	-1.903	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.058	-0.059	9.468	1.546	1.546	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.044	0.020	11.739	-1.295	-1.295	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.015	-0.009	14.041	0.653	0.653	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.031	-0.001	16.594	-0.804	-0.804	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.045	-0.043	18.698	0.318	0.318	0.000	0.000	0.000	0.000
121	A	121	PRO	0	0.030	0.030	15.326	-0.481	-0.481	0.000	0.000	0.000	0.000
122	A	122	ASN	0	0.006	0.011	18.209	-0.856	-0.856	0.000	0.000	0.000	0.000
123	A	123	PRO	0	0.008	0.013	20.508	-0.018	-0.018	0.000	0.000	0.000	0.000
124	A	124	ASN	0	0.049	0.016	23.200	-0.435	-0.435	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.009	0.015	21.501	-0.336	-0.336	0.000	0.000	0.000	0.000
126	A	126	ASN	0	0.027	-0.002	16.949	-0.082	-0.082	0.000	0.000	0.000	0.000
127	A	127	LYS	1	0.877	0.946	20.990	-11.972	-11.972	0.000	0.000	0.000	0.000
128	A	128	LEU	0	-0.001	-0.002	23.552	-0.352	-0.352	0.000	0.000	0.000	0.000
129	A	129	GLN	0	-0.017	-0.004	20.392	-0.267	-0.267	0.000	0.000	0.000	0.000
130	A	130	MET	0	-0.033	0.009	18.406	0.328	0.328	0.000	0.000	0.000	0.000
131	A	131	TYR	0	-0.019	-0.033	13.648	0.312	0.312	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.744	-0.811	11.147	17.659	17.659	0.000	0.000	0.000	0.000
133	A	133	SER	0	-0.048	-0.036	10.002	1.906	1.906	0.000	0.000	0.000	0.000
134	A	134	THR	0	0.005	-0.021	6.265	-0.706	-0.706	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.053	0.019	6.077	2.895	2.895	0.000	0.000	0.000	0.000
136	A	136	LYS	1	0.884	0.942	6.944	-30.918	-30.918	0.000	0.000	0.000	0.000
137	A	137	VAL	0	-0.003	0.025	9.259	-0.316	-0.316	0.000	0.000	0.000	0.000
138	A	138	LEU	0	-0.047	-0.029	9.998	-0.034	-0.034	0.000	0.000	0.000	0.000
139	A	139	SER	0	-0.022	-0.016	13.634	-1.047	-1.047	0.000	0.000	0.000	0.000
140	A	140	VAL	0	0.046	0.013	17.419	0.275	0.275	0.000	0.000	0.000	0.000
141	A	141	ASN	0	-0.018	-0.003	20.250	-0.828	-0.828	0.000	0.000	0.000	0.000
142	A	142	GLY	0	0.019	0.013	23.552	-0.122	-0.122	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.061	-0.033	25.601	0.133	0.133	0.000	0.000	0.000	0.000
144	A	144	ILE	0	-0.008	0.006	20.850	0.075	0.075	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.011	0.014	16.232	0.111	0.111	0.000	0.000	0.000	0.000
146	A	146	THR	0	-0.026	-0.010	14.949	-0.239	-0.239	0.000	0.000	0.000	0.000
147	A	147	SER	0	0.006	-0.017	11.224	0.698	0.698	0.000	0.000	0.000	0.000
148	A	148	ASP	-1	-0.784	-0.907	7.916	30.955	30.955	0.000	0.000	0.000	0.000
149	A	149	ALA	0	0.007	0.021	8.571	2.715	2.715	0.000	0.000	0.000	0.000
150	A	150	VAL	0	0.012	0.033	8.080	-2.267	-2.267	0.000	0.000	0.000	0.000
151	A	151	VAL	0	0.004	0.010	10.821	-1.204	-1.204	0.000	0.000	0.000	0.000
152	A	152	GLN	0	0.006	-0.016	14.116	-0.999	-0.999	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.027	0.007	17.245	-0.435	-0.435	0.000	0.000	0.000	0.000
154	A	154	GLY	0	0.037	0.021	21.117	-0.039	-0.039	0.000	0.000	0.000	0.000
155	A	155	SER	0	0.025	0.010	17.267	-0.122	-0.122	0.000	0.000	0.000	0.000
156	A	156	SER	0	0.004	0.018	19.602	0.418	0.418	0.000	0.000	0.000	0.000
157	A	157	GLY	0	0.027	0.021	22.545	-0.276	-0.276	0.000	0.000	0.000	0.000
158	A	158	SER	0	-0.044	-0.053	18.664	-0.192	-0.192	0.000	0.000	0.000	0.000
159	A	159	PRO	0	-0.032	0.008	19.157	0.034	0.034	0.000	0.000	0.000	0.000
160	A	160	ILE	0	0.012	-0.003	14.041	0.740	0.740	0.000	0.000	0.000	0.000
161	A	161	LEU	0	-0.054	-0.020	15.077	-0.981	-0.981	0.000	0.000	0.000	0.000
162	A	162	ASN	0	0.080	0.023	14.008	1.198	1.198	0.000	0.000	0.000	0.000
163	A	163	SER	0	0.038	0.009	12.821	-0.318	-0.318	0.000	0.000	0.000	0.000
164	A	164	LYS	1	0.816	0.910	14.150	-12.544	-12.544	0.000	0.000	0.000	0.000
165	A	165	ARG	1	0.791	0.872	13.464	-17.632	-17.632	0.000	0.000	0.000	0.000
166	A	166	GLU	-1	-0.785	-0.871	17.667	11.856	11.856	0.000	0.000	0.000	0.000
167	A	167	ALA	0	0.000	-0.007	18.671	0.701	0.701	0.000	0.000	0.000	0.000
168	A	168	ILE	0	0.020	-0.001	15.855	-0.596	-0.596	0.000	0.000	0.000	0.000
169	A	169	GLY	0	0.035	-0.001	20.030	-0.291	-0.291	0.000	0.000	0.000	0.000
170	A	170	VAL	0	-0.046	-0.014	20.760	0.181	0.181	0.000	0.000	0.000	0.000
171	A	171	MET	0	-0.005	0.012	16.060	-0.086	-0.086	0.000	0.000	0.000	0.000
172	A	172	TYR	0	-0.020	-0.002	20.258	-0.496	-0.496	0.000	0.000	0.000	0.000
173	A	173	ALA	0	-0.002	0.010	20.753	-0.390	-0.390	0.000	0.000	0.000	0.000
174	A	174	SER	0	0.012	-0.013	17.802	1.261	1.261	0.000	0.000	0.000	0.000
175	A	175	ASP	-1	-0.737	-0.852	15.683	18.922	18.922	0.000	0.000	0.000	0.000
176	A	176	LYS	1	0.820	0.908	16.045	-18.334	-18.334	0.000	0.000	0.000	0.000
177	A	177	PRO	0	0.034	0.032	19.089	0.113	0.113	0.000	0.000	0.000	0.000
178	A	178	THR	0	-0.014	-0.024	21.057	-0.273	-0.273	0.000	0.000	0.000	0.000
179	A	179	GLY	0	0.010	0.012	17.922	0.364	0.364	0.000	0.000	0.000	0.000
180	A	180	GLU	-1	-0.859	-0.926	11.285	23.673	23.673	0.000	0.000	0.000	0.000
181	A	181	SER	0	-0.024	-0.002	12.659	-0.083	-0.083	0.000	0.000	0.000	0.000
182	A	182	THR	0	-0.022	-0.013	10.715	1.839	1.839	0.000	0.000	0.000	0.000
183	A	183	ARG	1	0.857	0.920	9.605	-24.943	-24.943	0.000	0.000	0.000	0.000
184	A	184	SER	0	-0.022	-0.010	13.188	-1.520	-1.520	0.000	0.000	0.000	0.000
185	A	185	PHE	0	0.022	0.004	15.518	0.256	0.256	0.000	0.000	0.000	0.000
186	A	186	ALA	0	0.035	0.001	18.347	-0.338	-0.338	0.000	0.000	0.000	0.000
187	A	187	VAL	0	-0.003	0.006	20.158	-0.120	-0.120	0.000	0.000	0.000	0.000
188	A	188	TYR	0	0.012	0.002	21.173	0.123	0.123	0.000	0.000	0.000	0.000
189	A	189	PHE	0	-0.034	-0.006	22.861	-0.566	-0.566	0.000	0.000	0.000	0.000
190	A	190	SER	0	0.044	-0.001	25.035	-0.141	-0.141	0.000	0.000	0.000	0.000
191	A	191	PRO	0	0.030	-0.010	27.161	-0.139	-0.139	0.000	0.000	0.000	0.000
192	A	192	GLU	-1	-0.851	-0.911	30.701	9.301	9.301	0.000	0.000	0.000	0.000
193	A	193	ILE	0	0.022	0.016	27.273	-0.204	-0.204	0.000	0.000	0.000	0.000
194	A	194	LYS	1	0.830	0.909	25.657	-10.959	-10.959	0.000	0.000	0.000	0.000
195	A	195	LYS	1	0.898	0.946	30.139	-7.960	-7.960	0.000	0.000	0.000	0.000
196	A	196	PHE	0	0.010	0.006	31.598	-0.217	-0.217	0.000	0.000	0.000	0.000
197	A	197	ILE	0	0.037	0.020	27.674	-0.157	-0.157	0.000	0.000	0.000	0.000
198	A	198	ALA	0	0.006	0.000	32.049	-0.180	-0.180	0.000	0.000	0.000	0.000
199	A	199	ASP	-1	-0.837	-0.912	34.207	7.502	7.502	0.000	0.000	0.000	0.000
200	A	200	ASN	0	-0.009	-0.013	34.896	-0.387	-0.387	0.000	0.000	0.000	0.000
201	A	201	LEU	0	0.013	0.017	32.002	0.029	0.029	0.000	0.000	0.000	0.000
202	A	202	ASP	-1	-0.776	-0.863	34.816	8.283	8.283	0.000	0.000	0.000	0.000
203	A	203	LYS	1	0.871	0.965	37.214	-7.820	-7.820	0.000	0.000	0.000	0.000

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