FMO DATABASE

FMODB ID: 3Z22L

Calculation Name: 1F6F-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1F6F

Chain ID: A

ChEMBL ID:

UniProt ID: P16038

Base Structure: X-ray

Registration Date: 2025-10-05

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	194
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2160939.299742
FMO2-HF: Nuclear repulsion	2082332.116901
FMO2-HF: Total energy	-78607.182841
FMO2-MP2: Total energy	-78835.744493

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:1:ALA)

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

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.
68.572	71.176	0.142	-1.542	-1.204	-0.01

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.856 / q_NPA : 0.921

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	HIS	0	0.028	0.013	2.921	-16.388	-13.784	0.142	-1.542	-1.204	-0.010
4	A	4	PRO	0	0.026	0.008	5.600	3.888	3.888	0.000	0.000	0.000	0.000
5	A	5	PRO	0	0.026	0.007	9.240	0.126	0.126	0.000	0.000	0.000	0.000
6	A	6	TYR	0	0.067	0.020	12.019	0.526	0.526	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.036	-0.022	9.002	0.109	0.109	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.958	1.002	9.897	27.176	27.176	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.036	-0.039	12.180	2.843	2.843	0.000	0.000	0.000	0.000
10	A	10	GLN	0	0.053	0.028	13.789	-0.663	-0.663	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.006	0.011	15.463	-0.154	-0.154	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.067	0.031	12.461	-0.968	-0.968	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.911	0.963	11.516	16.956	16.956	0.000	0.000	0.000	0.000
14	A	15	GLN	0	-0.008	-0.009	10.938	0.868	0.868	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.006	0.009	13.697	-0.107	-0.107	0.000	0.000	0.000	0.000
16	A	17	PRO	0	0.036	0.014	15.493	0.870	0.870	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.071	0.031	18.495	0.048	0.048	0.000	0.000	0.000	0.000
18	A	19	GLN	0	0.055	0.032	22.022	0.405	0.405	0.000	0.000	0.000	0.000
19	A	20	SER	0	0.007	-0.003	18.816	-0.049	-0.049	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.043	-0.013	18.951	-0.271	-0.271	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.128	0.048	22.012	0.358	0.358	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.840	-0.904	23.103	-12.634	-12.634	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.911	0.953	16.149	17.724	17.724	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.036	0.024	24.115	0.346	0.346	0.000	0.000	0.000	0.000
25	A	26	THR	0	-0.011	-0.027	26.888	0.495	0.495	0.000	0.000	0.000	0.000
26	A	27	THR	0	-0.049	-0.027	26.047	0.393	0.393	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.053	0.025	25.992	0.343	0.343	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.024	0.015	28.951	0.360	0.360	0.000	0.000	0.000	0.000
29	A	30	ASN	0	-0.022	-0.011	31.865	0.609	0.609	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.058	-0.049	30.855	0.306	0.306	0.000	0.000	0.000	0.000
31	A	32	ASN	0	0.043	0.006	31.815	0.223	0.223	0.000	0.000	0.000	0.000
32	A	33	SER	0	0.008	0.003	34.747	0.359	0.359	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.884	0.955	35.560	8.961	8.961	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.040	0.024	33.998	0.264	0.264	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.023	0.010	38.080	0.218	0.218	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.029	0.017	40.681	0.223	0.223	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.885	-0.943	38.690	-8.173	-8.173	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.048	-0.016	39.563	0.181	0.181	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.027	-0.013	44.012	0.183	0.183	0.000	0.000	0.000	0.000
40	A	41	ASN	0	-0.005	0.009	45.902	0.200	0.200	0.000	0.000	0.000	0.000
41	A	42	ARG	1	0.918	0.971	44.793	7.139	7.139	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.015	-0.006	47.841	0.138	0.138	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.783	-0.903	49.899	-6.151	-6.151	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.940	-0.973	48.857	-6.559	-6.559	0.000	0.000	0.000	0.000
45	A	46	GLN	0	-0.053	-0.023	50.305	-0.031	-0.031	0.000	0.000	0.000	0.000
46	A	47	TYR	0	-0.019	-0.017	53.992	0.166	0.166	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.012	0.013	54.144	0.091	0.091	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.044	0.029	55.097	0.036	0.036	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.056	0.032	55.931	0.035	0.035	0.000	0.000	0.000	0.000
50	A	51	ILE	0	0.035	0.023	56.672	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.024	0.009	59.901	0.060	0.060	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.044	-0.026	56.197	0.035	0.035	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.780	-0.885	54.558	-5.990	-5.990	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.051	-0.032	57.707	0.054	0.054	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.817	0.902	59.407	5.379	5.379	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.003	0.010	55.527	-0.056	-0.056	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.047	-0.002	50.010	-0.069	-0.069	0.000	0.000	0.000	0.000
58	A	59	ASN	0	-0.031	-0.031	51.672	-0.220	-0.220	0.000	0.000	0.000	0.000
59	A	60	CYS	0	-0.029	0.010	46.192	0.043	0.043	0.000	0.000	0.000	0.000
60	A	61	HIS	0	0.030	0.014	43.224	0.236	0.236	0.000	0.000	0.000	0.000
61	A	62	THR	0	-0.041	-0.055	42.585	0.086	0.086	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.073	-0.033	45.593	-0.034	-0.034	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.012	-0.006	47.424	0.005	0.005	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.018	-0.005	41.440	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	66	THR	0	0.000	-0.003	45.336	0.056	0.056	0.000	0.000	0.000	0.000
66	A	67	THR	0	-0.031	-0.008	42.320	-0.127	-0.127	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.020	0.031	42.287	0.154	0.154	0.000	0.000	0.000	0.000
68	A	69	ASN	0	0.025	0.011	44.380	-0.274	-0.274	0.000	0.000	0.000	0.000
69	A	70	SER	0	0.009	0.012	46.977	0.060	0.060	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.981	0.975	43.809	6.994	6.994	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.023	0.006	44.476	-0.147	-0.147	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.822	-0.910	45.516	-6.803	-6.803	0.000	0.000	0.000	0.000
73	A	74	ALA	0	0.003	0.010	41.547	-0.133	-0.133	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.043	-0.028	40.458	-0.215	-0.215	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.021	0.007	40.938	-0.240	-0.240	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.042	-0.010	40.065	0.031	0.031	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.833	-0.923	37.935	-8.360	-8.360	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.797	-0.910	32.854	-9.521	-9.521	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.902	0.953	34.270	8.857	8.857	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.021	0.018	35.621	-0.063	-0.063	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.031	-0.012	35.641	0.001	0.001	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.001	-0.012	29.152	-0.127	-0.127	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.860	0.934	33.910	8.700	8.700	0.000	0.000	0.000	0.000
84	A	85	LEU	0	0.005	0.028	36.577	0.073	0.073	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.021	-0.013	32.751	0.041	0.041	0.000	0.000	0.000	0.000
86	A	87	ILE	0	-0.013	-0.001	30.752	-0.035	-0.035	0.000	0.000	0.000	0.000
87	A	88	SER	0	0.003	-0.010	34.155	0.097	0.097	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.009	0.005	37.743	0.141	0.141	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.020	-0.017	31.898	0.090	0.090	0.000	0.000	0.000	0.000
90	A	91	HIS	0	0.014	0.005	31.847	0.147	0.147	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.017	-0.020	36.485	0.198	0.198	0.000	0.000	0.000	0.000
92	A	93	TRP	0	-0.059	-0.043	38.282	0.278	0.278	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.807	-0.889	35.420	-9.021	-9.021	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.797	-0.902	37.973	-7.321	-7.321	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.019	0.014	41.393	0.107	0.107	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.017	-0.004	37.541	0.109	0.109	0.000	0.000	0.000	0.000
97	A	98	HIS	0	0.017	0.008	39.606	-0.147	-0.147	0.000	0.000	0.000	0.000
98	A	99	HIS	0	-0.034	-0.005	40.902	0.203	0.203	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.003	-0.002	43.051	0.117	0.117	0.000	0.000	0.000	0.000
100	A	101	VAL	0	-0.007	-0.012	38.838	0.082	0.082	0.000	0.000	0.000	0.000
101	A	102	THR	0	-0.011	-0.008	42.141	0.029	0.029	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.769	-0.875	44.318	-6.270	-6.270	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.042	-0.028	43.734	0.099	0.099	0.000	0.000	0.000	0.000
104	A	105	ALA	0	0.005	0.011	42.810	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	ASN	0	-0.071	-0.028	44.668	0.159	0.159	0.000	0.000	0.000	0.000
106	A	107	SER	0	0.058	0.030	48.332	0.183	0.183	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.895	0.936	45.654	6.808	6.808	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.017	0.024	49.417	0.111	0.111	0.000	0.000	0.000	0.000
109	A	110	THR	0	0.002	-0.016	48.302	-0.016	-0.016	0.000	0.000	0.000	0.000
110	A	111	SER	0	0.027	0.009	45.202	-0.085	-0.085	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.056	-0.005	43.133	-0.173	-0.173	0.000	0.000	0.000	0.000
112	A	113	ALA	0	-0.013	-0.028	42.378	-0.179	-0.179	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.011	0.017	42.991	-0.105	-0.105	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.004	0.009	40.536	-0.168	-0.168	0.000	0.000	0.000	0.000
115	A	116	THR	0	0.012	0.015	36.815	-0.214	-0.214	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.882	0.925	36.850	8.008	8.008	0.000	0.000	0.000	0.000
117	A	118	ALA	0	0.054	0.020	37.588	-0.161	-0.161	0.000	0.000	0.000	0.000
118	A	119	GLN	0	0.014	0.001	35.494	-0.135	-0.135	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.778	-0.852	30.892	-10.745	-10.745	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.013	-0.004	32.698	-0.314	-0.314	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.825	0.924	34.273	8.793	8.793	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.871	-0.934	29.768	-10.240	-10.240	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.834	0.888	27.554	10.646	10.646	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.018	0.003	30.007	-0.224	-0.224	0.000	0.000	0.000	0.000
125	A	126	LYS	1	0.892	0.934	29.671	10.130	10.130	0.000	0.000	0.000	0.000
126	A	127	VAL	0	-0.021	-0.008	24.530	-0.334	-0.334	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.048	-0.017	26.163	-0.377	-0.377	0.000	0.000	0.000	0.000
128	A	129	VAL	0	0.011	0.004	28.223	-0.120	-0.120	0.000	0.000	0.000	0.000
129	A	130	ASP	-1	-0.909	-0.930	22.867	-13.705	-13.705	0.000	0.000	0.000	0.000
130	A	131	GLY	0	0.025	0.006	23.549	-0.311	-0.311	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.016	-0.025	24.590	-0.146	-0.146	0.000	0.000	0.000	0.000
132	A	133	GLU	-1	-0.825	-0.910	27.111	-10.703	-10.703	0.000	0.000	0.000	0.000
133	A	134	VAL	0	-0.049	-0.018	20.600	-0.155	-0.155	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.060	-0.036	23.872	-0.215	-0.215	0.000	0.000	0.000	0.000
135	A	136	GLN	0	0.013	0.004	25.203	-0.082	-0.082	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.879	0.931	25.134	11.739	11.739	0.000	0.000	0.000	0.000
137	A	138	ARG	1	0.815	0.921	17.979	15.883	15.883	0.000	0.000	0.000	0.000
138	A	139	ILE	0	-0.031	-0.009	24.039	-0.190	-0.190	0.000	0.000	0.000	0.000
139	A	140	HIS	0	-0.033	-0.034	27.214	0.260	0.260	0.000	0.000	0.000	0.000
140	A	141	PRO	0	0.007	-0.007	26.008	0.092	0.092	0.000	0.000	0.000	0.000
141	A	142	GLY	0	-0.011	-0.002	28.396	0.297	0.297	0.000	0.000	0.000	0.000
142	A	143	GLU	-1	-0.805	-0.883	31.101	-8.650	-8.650	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.918	0.961	32.006	8.742	8.742	0.000	0.000	0.000	0.000
144	A	145	ASN	0	-0.013	-0.014	31.834	0.316	0.316	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.869	-0.927	35.806	-7.807	-7.807	0.000	0.000	0.000	0.000
146	A	147	PRO	0	-0.038	-0.021	39.189	-0.129	-0.129	0.000	0.000	0.000	0.000
147	A	148	TYR	0	-0.004	0.002	37.471	0.075	0.075	0.000	0.000	0.000	0.000
148	A	149	PRO	0	-0.024	0.001	42.055	0.075	0.075	0.000	0.000	0.000	0.000
149	A	150	VAL	0	0.064	0.023	43.688	-0.142	-0.142	0.000	0.000	0.000	0.000
150	A	151	TRP	0	-0.060	-0.047	45.924	0.087	0.087	0.000	0.000	0.000	0.000
151	A	152	SER	0	0.024	0.004	48.023	-0.021	-0.021	0.000	0.000	0.000	0.000
152	A	153	GLU	-1	-0.795	-0.876	50.825	-5.968	-5.968	0.000	0.000	0.000	0.000
153	A	154	GLN	0	-0.028	-0.004	45.618	-0.021	-0.021	0.000	0.000	0.000	0.000
154	A	155	SER	0	0.041	0.017	49.620	-0.041	-0.041	0.000	0.000	0.000	0.000
155	A	156	SER	0	-0.037	-0.027	51.729	0.036	0.036	0.000	0.000	0.000	0.000
156	A	157	LEU	0	-0.023	-0.018	47.084	0.075	0.075	0.000	0.000	0.000	0.000
157	A	158	THR	0	-0.034	-0.030	49.990	0.023	0.023	0.000	0.000	0.000	0.000
158	A	159	SER	0	-0.043	-0.014	52.541	0.119	0.119	0.000	0.000	0.000	0.000
159	A	160	GLN	0	0.030	0.004	56.246	0.044	0.044	0.000	0.000	0.000	0.000
160	A	161	ASP	-1	-0.837	-0.892	58.939	-5.209	-5.209	0.000	0.000	0.000	0.000
161	A	162	GLU	0	0.032	0.001	58.427	-0.087	-0.087	0.000	0.000	0.000	0.000
162	A	163	ASN	0	-0.069	-0.046	58.369	-0.023	-0.023	0.000	0.000	0.000	0.000
163	A	164	VAL	0	0.030	0.006	57.224	-0.087	-0.087	0.000	0.000	0.000	0.000
164	A	165	ARG	1	0.846	0.915	51.531	6.060	6.060	0.000	0.000	0.000	0.000
165	A	166	ARG	1	0.858	0.936	53.580	5.368	5.368	0.000	0.000	0.000	0.000
166	A	167	VAL	0	0.024	0.014	53.874	-0.105	-0.105	0.000	0.000	0.000	0.000
167	A	168	ALA	0	0.028	0.028	51.962	-0.091	-0.091	0.000	0.000	0.000	0.000
168	A	169	PHE	0	0.017	-0.001	46.544	-0.154	-0.154	0.000	0.000	0.000	0.000
169	A	170	TYR	0	-0.050	-0.035	49.175	-0.137	-0.137	0.000	0.000	0.000	0.000
170	A	171	ARG	1	0.833	0.884	50.104	5.999	5.999	0.000	0.000	0.000	0.000
171	A	172	LEU	0	0.028	0.022	44.241	-0.107	-0.107	0.000	0.000	0.000	0.000
172	A	173	PHE	0	0.019	-0.004	43.705	-0.151	-0.151	0.000	0.000	0.000	0.000
173	A	174	HIS	1	0.852	0.902	45.365	6.305	6.305	0.000	0.000	0.000	0.000
174	A	176	LEU	0	0.045	0.033	39.413	-0.109	-0.109	0.000	0.000	0.000	0.000
175	A	177	HIS	0	0.017	0.016	41.236	-0.328	-0.328	0.000	0.000	0.000	0.000
176	A	178	ARG	1	0.920	0.969	42.238	6.527	6.527	0.000	0.000	0.000	0.000
177	A	179	ASP	-1	-0.744	-0.859	40.585	-7.575	-7.575	0.000	0.000	0.000	0.000
178	A	180	SER	0	-0.016	-0.015	37.766	-0.301	-0.301	0.000	0.000	0.000	0.000
179	A	181	SER	0	-0.020	-0.005	37.670	-0.282	-0.282	0.000	0.000	0.000	0.000
180	A	182	LYS	1	0.904	0.963	39.338	7.163	7.163	0.000	0.000	0.000	0.000
181	A	183	ILE	0	0.026	0.015	33.984	-0.153	-0.153	0.000	0.000	0.000	0.000
182	A	184	TYR	0	0.020	-0.003	32.896	-0.322	-0.322	0.000	0.000	0.000	0.000
183	A	185	THR	0	-0.058	-0.038	35.256	-0.117	-0.117	0.000	0.000	0.000	0.000
184	A	186	TYR	0	0.005	-0.021	36.451	-0.099	-0.099	0.000	0.000	0.000	0.000
185	A	187	LEU	0	0.014	0.014	29.892	-0.173	-0.173	0.000	0.000	0.000	0.000
186	A	188	ARG	1	0.875	0.945	31.744	8.463	8.463	0.000	0.000	0.000	0.000
187	A	189	ILE	0	-0.013	0.000	33.708	-0.077	-0.077	0.000	0.000	0.000	0.000
188	A	190	LEU	0	-0.015	-0.001	31.239	-0.049	-0.049	0.000	0.000	0.000	0.000
189	A	191	LYS	1	0.869	0.949	27.151	11.321	11.321	0.000	0.000	0.000	0.000
190	A	197	CYS	-1	-0.944	-0.980	29.088	-10.544	-10.544	0.000	0.000	0.000	0.000
191	A	193	ARG	1	0.807	0.914	32.867	8.712	8.712	0.000	0.000	0.000	0.000
192	A	194	LEU	0	-0.015	-0.010	29.193	0.002	0.002	0.000	0.000	0.000	0.000
193	A	195	THR	0	-0.136	-0.076	25.432	-0.649	-0.649	0.000	0.000	0.000	0.000
194	A	196	SER	0	0.003	0.012	26.905	0.364	0.364	0.000	0.000	0.000	0.000

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