FMO DATABASE

FMODB ID: 3K6LL

Calculation Name: 2A22-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A22

Chain ID: A

ChEMBL ID:

UniProt ID: Q5CYJ7

Base Structure: X-ray

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	193
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2180173.972901
FMO2-HF: Nuclear repulsion	2104578.358109
FMO2-HF: Total energy	-75595.614792
FMO2-MP2: Total energy	-75814.728981

3D Structure Molmil

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:4:ASP)

Summations of interaction energy for fragment #1(A:4:ASP)

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.
-14.362	-12.76	-0.006	-0.763	-0.833	0.001

Interaction energy analysis for fragmet #1(A:4:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.080 / q_NPA : -0.052

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	6	GLY	0	-0.009	0.007	3.858	1.332	3.039	-0.005	-0.752	-0.951	0.001
4	A	7	ASP	-1	-0.839	-0.901	5.060	-16.384	-16.489	-0.001	-0.011	0.118	0.000
5	A	8	LEU	0	-0.058	-0.040	7.608	2.225	2.225	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.024	0.008	10.313	-0.441	-0.441	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.007	0.009	13.193	0.534	0.534	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.004	-0.001	16.207	-0.124	-0.124	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.014	-0.006	19.456	0.199	0.199	0.000	0.000	0.000	0.000
10	A	13	GLY	0	0.097	0.036	22.284	-0.094	-0.094	0.000	0.000	0.000	0.000
11	A	14	ASP	-1	-0.729	-0.873	25.550	-0.738	-0.738	0.000	0.000	0.000	0.000
12	A	15	LEU	0	-0.009	0.022	25.123	0.063	0.063	0.000	0.000	0.000	0.000
13	A	16	LYS	1	0.881	0.928	29.383	0.703	0.703	0.000	0.000	0.000	0.000
14	A	17	ILE	0	-0.009	0.049	29.357	0.055	0.055	0.000	0.000	0.000	0.000
15	A	18	PRO	0	-0.005	-0.026	33.011	-0.035	-0.035	0.000	0.000	0.000	0.000
16	A	19	TYR	0	-0.057	-0.036	35.764	0.051	0.051	0.000	0.000	0.000	0.000
17	A	20	GLY	0	0.011	0.007	36.122	0.033	0.033	0.000	0.000	0.000	0.000
18	A	21	ALA	0	-0.009	-0.003	33.080	0.023	0.023	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.845	0.895	34.534	0.352	0.352	0.000	0.000	0.000	0.000
20	A	23	GLU	-1	-0.826	-0.889	30.617	-0.406	-0.406	0.000	0.000	0.000	0.000
21	A	24	LEU	0	0.034	0.012	24.049	0.000	0.000	0.000	0.000	0.000	0.000
22	A	25	PRO	0	0.013	0.013	27.303	0.043	0.043	0.000	0.000	0.000	0.000
23	A	26	SER	0	0.028	0.012	26.865	-0.024	-0.024	0.000	0.000	0.000	0.000
24	A	27	ASN	0	-0.017	-0.014	26.467	-0.020	-0.020	0.000	0.000	0.000	0.000
25	A	28	PHE	0	0.015	-0.006	23.435	0.043	0.043	0.000	0.000	0.000	0.000
26	A	29	ARG	1	0.959	0.986	22.077	0.269	0.269	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.938	-0.978	20.055	-0.116	-0.116	0.000	0.000	0.000	0.000
28	A	31	LEU	0	-0.053	-0.018	18.175	-0.030	-0.030	0.000	0.000	0.000	0.000
29	A	32	LEU	0	-0.003	-0.013	17.273	-0.174	-0.174	0.000	0.000	0.000	0.000
30	A	33	ALA	0	-0.012	0.008	17.441	-0.206	-0.206	0.000	0.000	0.000	0.000
31	A	34	THR	0	-0.019	0.001	13.054	0.083	0.083	0.000	0.000	0.000	0.000
32	A	35	ASP	-1	-0.865	-0.942	10.307	-0.991	-0.991	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.872	0.929	8.085	-3.284	-3.284	0.000	0.000	0.000	0.000
34	A	37	ILE	0	0.004	0.023	8.644	-1.131	-1.131	0.000	0.000	0.000	0.000
35	A	38	ASN	0	-0.014	-0.011	5.355	2.290	2.290	0.000	0.000	0.000	0.000
36	A	39	TYR	0	-0.019	-0.013	8.165	0.229	0.229	0.000	0.000	0.000	0.000
37	A	40	VAL	0	0.012	0.011	11.848	0.493	0.493	0.000	0.000	0.000	0.000
38	A	41	LEU	0	-0.020	-0.005	15.602	-0.059	-0.059	0.000	0.000	0.000	0.000
39	A	42	CYS	0	0.001	0.010	18.393	0.253	0.253	0.000	0.000	0.000	0.000
40	A	43	THR	0	0.025	0.000	21.735	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	44	GLY	0	0.071	0.046	24.985	0.094	0.094	0.000	0.000	0.000	0.000
42	A	45	ASN	0	-0.159	-0.109	27.120	0.041	0.041	0.000	0.000	0.000	0.000
43	A	46	VAL	0	0.003	-0.005	25.372	0.026	0.026	0.000	0.000	0.000	0.000
44	A	47	CYS	0	-0.098	-0.041	28.441	0.051	0.051	0.000	0.000	0.000	0.000
45	A	48	SER	0	0.032	0.025	30.490	0.021	0.021	0.000	0.000	0.000	0.000
46	A	49	GLN	0	0.048	0.010	27.672	-0.045	-0.045	0.000	0.000	0.000	0.000
47	A	50	GLU	-1	-0.917	-0.952	27.641	-0.774	-0.774	0.000	0.000	0.000	0.000
48	A	51	TYR	0	0.022	-0.012	25.948	-0.061	-0.061	0.000	0.000	0.000	0.000
49	A	52	VAL	0	0.001	0.008	24.391	-0.112	-0.112	0.000	0.000	0.000	0.000
50	A	53	GLU	-1	-0.886	-0.943	22.975	-1.225	-1.225	0.000	0.000	0.000	0.000
51	A	54	MET	0	-0.028	0.005	21.048	-0.135	-0.135	0.000	0.000	0.000	0.000
52	A	55	LEU	0	0.023	-0.005	20.135	-0.134	-0.134	0.000	0.000	0.000	0.000
53	A	56	LYS	1	0.759	0.856	18.433	2.061	2.061	0.000	0.000	0.000	0.000
54	A	57	ASN	0	-0.064	-0.038	17.950	-0.238	-0.238	0.000	0.000	0.000	0.000
55	A	58	ILE	0	-0.032	0.005	14.442	-0.044	-0.044	0.000	0.000	0.000	0.000
56	A	59	THR	0	-0.017	-0.023	10.376	-0.485	-0.485	0.000	0.000	0.000	0.000
57	A	60	LYS	1	0.943	0.984	10.413	6.926	6.926	0.000	0.000	0.000	0.000
58	A	61	ASN	0	-0.052	-0.028	9.072	0.936	0.936	0.000	0.000	0.000	0.000
59	A	62	VAL	0	0.017	0.018	13.100	0.071	0.071	0.000	0.000	0.000	0.000
60	A	63	TYR	0	0.016	0.005	14.470	0.301	0.301	0.000	0.000	0.000	0.000
61	A	64	ILE	0	0.002	-0.009	18.958	0.085	0.085	0.000	0.000	0.000	0.000
62	A	65	VAL	0	-0.053	-0.005	22.525	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.012	-0.008	25.507	0.053	0.053	0.000	0.000	0.000	0.000
64	A	67	GLY	0	0.006	-0.024	29.170	0.010	0.010	0.000	0.000	0.000	0.000
65	A	68	ASP	-1	-0.851	-0.915	31.320	-0.666	-0.666	0.000	0.000	0.000	0.000
66	A	69	LEU	0	0.005	-0.009	34.033	0.043	0.043	0.000	0.000	0.000	0.000
67	A	70	ASP	-1	-0.730	-0.845	29.687	-0.975	-0.975	0.000	0.000	0.000	0.000
68	A	71	SER	0	-0.036	-0.019	32.909	-0.016	-0.016	0.000	0.000	0.000	0.000
69	A	72	ALA	0	-0.022	-0.010	34.317	0.021	0.021	0.000	0.000	0.000	0.000
70	A	73	ILE	0	-0.041	-0.005	28.114	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	74	PHE	0	-0.015	0.002	28.537	0.023	0.023	0.000	0.000	0.000	0.000
72	A	75	ASN	0	-0.011	-0.023	23.987	-0.125	-0.125	0.000	0.000	0.000	0.000
73	A	76	PRO	0	-0.002	-0.005	22.770	0.034	0.034	0.000	0.000	0.000	0.000
74	A	77	ASP	-1	-0.821	-0.890	20.756	-2.278	-2.278	0.000	0.000	0.000	0.000
75	A	78	PRO	0	-0.005	-0.008	22.667	0.112	0.112	0.000	0.000	0.000	0.000
76	A	79	GLU	-1	-0.929	-0.966	24.480	-1.430	-1.430	0.000	0.000	0.000	0.000
77	A	80	SER	0	-0.065	-0.033	25.824	0.116	0.116	0.000	0.000	0.000	0.000
78	A	81	ASN	0	-0.059	-0.032	27.664	0.116	0.116	0.000	0.000	0.000	0.000
79	A	82	GLY	0	0.064	0.031	28.975	0.082	0.082	0.000	0.000	0.000	0.000
80	A	83	VAL	0	-0.042	-0.014	29.775	0.022	0.022	0.000	0.000	0.000	0.000
81	A	84	PHE	0	0.044	0.019	23.952	-0.115	-0.115	0.000	0.000	0.000	0.000
82	A	85	PRO	0	-0.012	0.006	23.946	0.095	0.095	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.845	-0.916	27.220	-0.899	-0.899	0.000	0.000	0.000	0.000
84	A	87	TYR	0	-0.037	-0.042	25.632	0.024	0.024	0.000	0.000	0.000	0.000
85	A	88	VAL	0	-0.002	0.001	19.581	-0.033	-0.033	0.000	0.000	0.000	0.000
86	A	89	VAL	0	-0.022	-0.014	20.201	0.084	0.084	0.000	0.000	0.000	0.000
87	A	90	VAL	0	-0.026	-0.006	14.308	-0.083	-0.083	0.000	0.000	0.000	0.000
88	A	91	GLN	0	-0.041	-0.013	12.942	0.457	0.457	0.000	0.000	0.000	0.000
89	A	92	ILE	0	-0.035	-0.023	10.279	-0.624	-0.624	0.000	0.000	0.000	0.000
90	A	93	GLY	0	0.041	0.028	9.434	0.648	0.648	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.941	-0.974	10.307	-2.467	-2.467	0.000	0.000	0.000	0.000
92	A	95	PHE	0	-0.034	-0.008	13.675	0.393	0.393	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.893	0.964	15.196	1.149	1.149	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.011	-0.019	15.356	0.324	0.324	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.019	0.007	18.726	-0.096	-0.096	0.000	0.000	0.000	0.000
96	A	99	LEU	0	-0.008	-0.005	20.165	0.041	0.041	0.000	0.000	0.000	0.000
97	A	100	MET	0	0.008	-0.003	22.829	0.009	0.009	0.000	0.000	0.000	0.000
98	A	101	HIS	1	0.788	0.910	26.417	0.910	0.910	0.000	0.000	0.000	0.000
99	A	102	GLY	0	0.048	0.014	28.788	0.026	0.026	0.000	0.000	0.000	0.000
100	A	103	ASN	0	-0.014	-0.009	30.929	0.016	0.016	0.000	0.000	0.000	0.000
101	A	104	GLN	0	0.027	-0.008	31.051	0.049	0.049	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.061	-0.005	31.364	0.011	0.011	0.000	0.000	0.000	0.000
103	A	106	LEU	0	-0.007	0.009	34.518	0.032	0.032	0.000	0.000	0.000	0.000
104	A	107	PRO	0	0.035	-0.002	38.250	0.004	0.004	0.000	0.000	0.000	0.000
105	A	108	TRP	0	0.039	0.015	35.676	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	109	ASP	-1	-0.774	-0.864	31.735	-0.597	-0.597	0.000	0.000	0.000	0.000
107	A	110	ASP	-1	-0.852	-0.903	34.028	-0.452	-0.452	0.000	0.000	0.000	0.000
108	A	111	PRO	0	0.013	-0.012	33.145	-0.040	-0.040	0.000	0.000	0.000	0.000
109	A	112	GLY	0	0.001	0.016	33.424	-0.025	-0.025	0.000	0.000	0.000	0.000
110	A	113	SER	0	0.002	-0.015	34.804	-0.051	-0.051	0.000	0.000	0.000	0.000
111	A	114	LEU	0	0.016	-0.003	29.201	-0.048	-0.048	0.000	0.000	0.000	0.000
112	A	115	GLU	-1	-0.794	-0.866	30.164	-0.605	-0.605	0.000	0.000	0.000	0.000
113	A	116	GLN	0	-0.045	-0.040	30.971	-0.029	-0.029	0.000	0.000	0.000	0.000
114	A	117	TRP	0	0.018	-0.004	29.538	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	118	GLN	0	0.008	-0.012	25.696	0.017	0.017	0.000	0.000	0.000	0.000
116	A	119	ARG	1	0.827	0.904	26.875	0.562	0.562	0.000	0.000	0.000	0.000
117	A	120	ARG	1	0.870	0.951	29.276	0.793	0.793	0.000	0.000	0.000	0.000
118	A	121	LEU	0	0.000	-0.011	24.728	-0.025	-0.025	0.000	0.000	0.000	0.000
119	A	122	ASP	-1	-0.935	-0.956	24.356	-1.310	-1.310	0.000	0.000	0.000	0.000
120	A	123	CYS	0	-0.015	0.017	21.600	-0.075	-0.075	0.000	0.000	0.000	0.000
121	A	124	ASP	-1	-0.816	-0.910	19.304	-1.389	-1.389	0.000	0.000	0.000	0.000
122	A	125	ILE	0	-0.021	-0.015	17.443	0.156	0.156	0.000	0.000	0.000	0.000
123	A	126	LEU	0	-0.020	-0.012	21.420	-0.115	-0.115	0.000	0.000	0.000	0.000
124	A	127	VAL	0	-0.024	-0.010	20.115	0.100	0.100	0.000	0.000	0.000	0.000
125	A	128	THR	0	-0.002	-0.010	23.576	-0.019	-0.019	0.000	0.000	0.000	0.000
126	A	129	GLY	0	0.043	0.017	26.883	0.020	0.020	0.000	0.000	0.000	0.000
127	A	130	HIS	0	-0.061	-0.016	28.634	0.031	0.031	0.000	0.000	0.000	0.000
128	A	131	THR	0	-0.021	-0.059	32.196	0.034	0.034	0.000	0.000	0.000	0.000
129	A	132	HIS	0	0.009	0.030	31.431	0.016	0.016	0.000	0.000	0.000	0.000
130	A	133	LYS	1	0.962	0.985	32.315	0.430	0.430	0.000	0.000	0.000	0.000
131	A	134	LEU	0	-0.013	0.008	26.286	-0.029	-0.029	0.000	0.000	0.000	0.000
132	A	135	ARG	1	0.767	0.869	27.957	0.638	0.638	0.000	0.000	0.000	0.000
133	A	136	VAL	0	0.053	0.026	24.473	-0.087	-0.087	0.000	0.000	0.000	0.000
134	A	137	PHE	0	-0.062	-0.029	26.885	0.080	0.080	0.000	0.000	0.000	0.000
135	A	138	GLU	-1	-0.834	-0.914	26.312	-0.528	-0.528	0.000	0.000	0.000	0.000
136	A	139	LYS	1	0.869	0.930	27.763	0.522	0.522	0.000	0.000	0.000	0.000
137	A	140	ASN	0	-0.085	-0.057	29.022	-0.016	-0.016	0.000	0.000	0.000	0.000
138	A	141	GLY	0	0.009	0.014	26.437	-0.028	-0.028	0.000	0.000	0.000	0.000
139	A	142	LYS	1	0.867	0.960	24.267	0.791	0.791	0.000	0.000	0.000	0.000
140	A	143	LEU	0	0.009	0.013	20.341	0.094	0.094	0.000	0.000	0.000	0.000
141	A	144	PHE	0	-0.023	-0.013	23.760	-0.134	-0.134	0.000	0.000	0.000	0.000
142	A	145	LEU	0	-0.012	-0.016	20.770	0.083	0.083	0.000	0.000	0.000	0.000
143	A	146	ASN	0	0.040	0.013	24.868	-0.084	-0.084	0.000	0.000	0.000	0.000
144	A	147	PRO	0	0.030	0.016	23.126	0.077	0.077	0.000	0.000	0.000	0.000
145	A	148	GLY	0	0.037	0.036	25.178	0.062	0.062	0.000	0.000	0.000	0.000
146	A	149	THR	0	-0.026	-0.011	28.020	-0.050	-0.050	0.000	0.000	0.000	0.000
147	A	150	ALA	0	0.023	0.004	25.321	0.045	0.045	0.000	0.000	0.000	0.000
148	A	151	THR	0	-0.061	-0.064	27.005	0.032	0.032	0.000	0.000	0.000	0.000
149	A	152	GLY	0	0.000	0.013	30.208	0.048	0.048	0.000	0.000	0.000	0.000
150	A	153	ALA	0	-0.007	0.021	32.731	0.035	0.035	0.000	0.000	0.000	0.000
151	A	154	PHE	0	0.010	-0.009	34.750	-0.009	-0.009	0.000	0.000	0.000	0.000
152	A	155	SER	0	0.015	0.000	36.152	-0.021	-0.021	0.000	0.000	0.000	0.000
153	A	156	ALA	0	0.004	-0.005	38.123	0.021	0.021	0.000	0.000	0.000	0.000
154	A	157	LEU	0	-0.063	-0.022	36.944	0.018	0.018	0.000	0.000	0.000	0.000
155	A	158	THR	0	-0.050	-0.040	34.746	0.012	0.012	0.000	0.000	0.000	0.000
156	A	159	PRO	0	-0.030	-0.002	37.250	-0.012	-0.012	0.000	0.000	0.000	0.000
157	A	160	ASP	-1	-0.913	-0.969	38.503	-0.270	-0.270	0.000	0.000	0.000	0.000
158	A	161	ALA	0	-0.030	-0.001	33.346	0.014	0.014	0.000	0.000	0.000	0.000
159	A	162	PRO	0	-0.015	-0.004	31.399	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	163	PRO	0	-0.010	-0.001	29.399	-0.040	-0.040	0.000	0.000	0.000	0.000
161	A	164	SER	0	-0.057	-0.056	26.695	0.073	0.073	0.000	0.000	0.000	0.000
162	A	165	PHE	0	-0.025	-0.008	19.309	-0.077	-0.077	0.000	0.000	0.000	0.000
163	A	166	MET	0	-0.036	-0.013	20.114	0.097	0.097	0.000	0.000	0.000	0.000
164	A	167	LEU	0	-0.005	0.012	14.624	-0.194	-0.194	0.000	0.000	0.000	0.000
165	A	168	MET	0	0.013	0.011	14.825	0.262	0.262	0.000	0.000	0.000	0.000
166	A	169	ALA	0	0.000	0.007	11.333	-0.543	-0.543	0.000	0.000	0.000	0.000
167	A	170	LEU	0	-0.008	0.001	10.827	0.504	0.504	0.000	0.000	0.000	0.000
168	A	171	GLN	0	-0.004	-0.019	8.226	-0.370	-0.370	0.000	0.000	0.000	0.000
169	A	172	GLY	0	0.044	0.030	10.301	0.784	0.784	0.000	0.000	0.000	0.000
170	A	173	ASN	0	0.023	0.005	12.103	-0.393	-0.393	0.000	0.000	0.000	0.000
171	A	174	LYS	1	0.911	0.952	13.938	-0.131	-0.131	0.000	0.000	0.000	0.000
172	A	175	VAL	0	0.066	0.033	14.320	-0.380	-0.380	0.000	0.000	0.000	0.000
173	A	176	VAL	0	-0.005	-0.002	14.864	0.270	0.270	0.000	0.000	0.000	0.000
174	A	177	LEU	0	-0.018	-0.005	15.919	-0.230	-0.230	0.000	0.000	0.000	0.000
175	A	178	TYR	0	-0.001	-0.007	15.388	0.275	0.275	0.000	0.000	0.000	0.000
176	A	179	VAL	0	0.038	0.011	19.639	-0.166	-0.166	0.000	0.000	0.000	0.000
177	A	180	TYR	0	0.006	-0.004	17.943	0.197	0.197	0.000	0.000	0.000	0.000
178	A	181	ASP	-1	-0.774	-0.879	24.120	-0.294	-0.294	0.000	0.000	0.000	0.000
179	A	182	LEU	0	-0.039	-0.006	27.801	0.058	0.058	0.000	0.000	0.000	0.000
180	A	183	ARG	1	0.908	0.933	30.107	0.141	0.141	0.000	0.000	0.000	0.000
181	A	184	ASP	-1	-0.890	-0.948	33.575	-0.087	-0.087	0.000	0.000	0.000	0.000
182	A	185	GLY	0	-0.026	-0.004	34.151	0.027	0.027	0.000	0.000	0.000	0.000
183	A	186	LYS	1	0.902	0.950	29.468	-0.074	-0.074	0.000	0.000	0.000	0.000
184	A	187	THR	0	0.024	0.009	24.592	-0.034	-0.034	0.000	0.000	0.000	0.000
185	A	188	ASN	0	-0.121	-0.073	27.113	0.129	0.129	0.000	0.000	0.000	0.000
186	A	189	VAL	0	0.029	0.003	20.974	-0.057	-0.057	0.000	0.000	0.000	0.000
187	A	190	ALA	0	-0.029	0.005	24.400	0.084	0.084	0.000	0.000	0.000	0.000
188	A	191	MET	0	-0.012	0.007	19.900	-0.106	-0.106	0.000	0.000	0.000	0.000
189	A	192	SER	0	-0.059	-0.038	21.286	0.001	0.001	0.000	0.000	0.000	0.000
190	A	193	GLU	-1	-0.930	-0.966	18.664	0.295	0.295	0.000	0.000	0.000	0.000
191	A	194	PHE	0	0.004	-0.005	19.665	0.008	0.008	0.000	0.000	0.000	0.000
192	A	195	SER	0	-0.050	-0.038	18.983	0.040	0.040	0.000	0.000	0.000	0.000
193	A	196	LYS	0	0.036	0.041	19.298	-0.501	-0.501	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASP)