FMO DATABASE

FMODB ID: 1942Z

Calculation Name: 1P3C-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1P3C

Chain ID: A

ChEMBL ID:

UniProt ID: Q9EXR9

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	214
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2437246.548552
FMO2-HF: Nuclear repulsion	2356564.352622
FMO2-HF: Total energy	-80682.19593
FMO2-MP2: Total energy	-80915.954973

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:VAL)

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

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.
-43.44	-38.594	29.188	-16.041	-17.988	-0.181

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.722 / q_NPA : 0.840

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	ILE	0	-0.043	-0.017	2.528	-2.347	0.487	0.829	-1.317	-2.346	-0.006
4	A	4	GLY	0	0.016	0.019	4.846	3.915	4.022	-0.001	-0.011	-0.094	0.000
164	A	165	ASP	-1	-0.747	-0.876	4.762	-54.056	-53.913	-0.001	-0.029	-0.113	0.000
165	A	166	THR	0	-0.032	-0.032	2.250	-9.740	-7.314	2.905	-2.485	-2.846	-0.030
166	A	167	PHE	0	-0.024	-0.001	1.950	-31.266	-32.095	7.232	-3.184	-3.219	-0.050
167	A	168	SER	0	0.030	0.013	4.246	3.415	3.487	-0.001	-0.013	-0.058	0.000
185	A	186	HIS	0	0.049	0.054	4.082	4.515	4.644	-0.001	-0.009	-0.118	0.000
188	A	189	GLY	0	0.012	0.012	2.568	-9.066	-8.411	0.762	-0.638	-0.779	0.001
189	A	190	TYR	0	-0.011	-0.031	3.360	10.843	10.756	0.012	0.405	-0.329	-0.001
190	A	191	SER	0	0.007	-0.007	5.197	-0.814	-0.754	-0.001	0.000	-0.059	0.000
192	A	193	GLY	0	0.016	0.021	2.576	0.046	0.421	0.574	-0.327	-0.622	0.001
193	A	194	THR	0	-0.020	-0.019	2.510	-6.563	-5.428	1.283	-0.885	-1.532	-0.020
194	A	195	ILE	0	-0.043	-0.011	4.076	2.432	2.606	0.000	-0.030	-0.144	0.000
195	A	196	ASN	0	-0.028	-0.012	1.760	-40.516	-42.996	15.597	-7.473	-5.643	-0.076
196	A	197	GLY	0	0.092	0.027	4.587	7.261	7.393	-0.001	-0.045	-0.086	0.000
5	A	5	ASP	-1	-0.914	-0.952	8.552	-23.086	-23.086	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.826	-0.894	8.882	-34.927	-34.927	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.050	0.023	9.729	2.903	2.903	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.634	0.762	6.487	39.952	39.952	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.009	-0.004	10.954	1.871	1.871	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.824	0.899	14.113	14.782	14.782	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.001	-0.002	15.569	0.877	0.877	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.024	0.008	17.977	0.484	0.484	0.000	0.000	0.000	0.000
13	A	13	ASN	0	0.007	-0.009	21.618	0.529	0.529	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.007	-0.011	19.364	-0.136	-0.136	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.983	0.989	22.145	11.175	11.175	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.021	0.002	23.794	0.420	0.420	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.019	0.037	23.076	-0.607	-0.607	0.000	0.000	0.000	0.000
18	A	18	PRO	0	0.001	-0.008	18.802	0.193	0.193	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.043	-0.049	16.936	0.245	0.245	0.000	0.000	0.000	0.000
20	A	20	ASN	0	0.032	0.016	19.621	-0.792	-0.792	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.033	-0.009	21.016	0.114	0.114	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.018	-0.004	14.816	-0.346	-0.346	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.017	0.004	17.592	0.419	0.419	0.000	0.000	0.000	0.000
24	A	24	TYR	0	0.009	0.012	14.795	-0.860	-0.860	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.018	-0.023	15.809	1.301	1.301	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.028	0.003	16.697	-1.058	-1.058	0.000	0.000	0.000	0.000
27	A	27	PHE	0	0.037	0.007	16.019	0.583	0.583	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.005	-0.010	20.333	-0.168	-0.168	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.015	0.014	19.705	0.443	0.443	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.053	-0.023	14.649	-0.626	-0.626	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.016	0.008	13.512	1.202	1.202	0.000	0.000	0.000	0.000
32	A	32	CYS	0	-0.172	-0.060	11.976	-3.321	-3.321	0.000	0.000	0.000	0.000
33	A	33	THR	0	0.044	0.030	11.032	1.185	1.185	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.028	0.021	13.208	-0.110	-0.110	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.015	-0.005	15.553	0.046	0.046	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.005	0.009	18.001	0.346	0.346	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.002	-0.005	20.699	-0.014	-0.014	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.006	-0.007	23.442	0.460	0.460	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.019	0.012	26.492	-0.328	-0.328	0.000	0.000	0.000	0.000
40	A	40	ASN	0	0.022	0.016	27.725	-0.225	-0.225	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.782	0.891	24.717	10.958	10.958	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.014	0.017	18.748	-0.286	-0.286	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.006	0.010	16.966	0.223	0.223	0.000	0.000	0.000	0.000
44	A	44	THR	0	0.032	-0.014	14.327	-1.101	-1.101	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.019	-0.036	10.472	-1.826	-1.826	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.055	0.032	14.035	0.970	0.970	0.000	0.000	0.000	0.000
47	A	47	HIS	1	0.803	0.861	9.301	29.127	29.127	0.000	0.000	0.000	0.000
48	A	49	VAL	0	0.001	0.024	14.983	0.783	0.783	0.000	0.000	0.000	0.000
49	A	50	TYR	0	0.009	0.006	17.809	1.118	1.118	0.000	0.000	0.000	0.000
50	A	51	ASN	0	0.014	0.013	17.349	-1.000	-1.000	0.000	0.000	0.000	0.000
51	A	52	THR	0	0.044	0.004	17.062	0.645	0.645	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.006	0.010	17.768	0.672	0.672	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.010	-0.017	19.705	0.538	0.538	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.939	0.973	21.721	12.159	12.159	0.000	0.000	0.000	0.000
55	A	56	SER	0	0.003	0.017	22.344	0.757	0.757	0.000	0.000	0.000	0.000
56	A	57	TYR	0	0.000	-0.011	21.461	-0.850	-0.850	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.044	-0.036	18.098	0.227	0.227	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.000	0.002	21.132	0.494	0.494	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.873	0.921	22.590	10.836	10.836	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.062	0.019	23.081	0.293	0.293	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.039	-0.008	22.516	0.493	0.493	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.014	-0.006	20.934	-0.937	-0.937	0.000	0.000	0.000	0.000
63	A	64	TYR	0	0.036	0.005	20.517	0.670	0.670	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.006	-0.004	20.337	-0.872	-0.872	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.061	0.035	20.100	0.636	0.636	0.000	0.000	0.000	0.000
66	A	67	MET	0	-0.057	0.009	19.393	0.218	0.218	0.000	0.000	0.000	0.000
67	A	68	ASN	0	0.055	0.004	18.763	-1.828	-1.828	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.793	-0.864	20.078	-13.761	-13.761	0.000	0.000	0.000	0.000
69	A	70	SER	0	0.028	-0.003	20.479	0.311	0.311	0.000	0.000	0.000	0.000
70	A	71	THR	0	0.012	0.027	21.921	0.620	0.620	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.019	0.006	23.495	-0.507	-0.507	0.000	0.000	0.000	0.000
72	A	73	VAL	0	-0.039	-0.021	24.075	0.587	0.587	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.066	-0.047	23.828	0.883	0.883	0.000	0.000	0.000	0.000
74	A	75	GLY	0	0.027	0.026	26.987	0.206	0.206	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.040	-0.040	25.479	-0.530	-0.530	0.000	0.000	0.000	0.000
76	A	77	ALA	0	-0.027	0.004	25.490	0.462	0.462	0.000	0.000	0.000	0.000
77	A	78	ASN	0	0.012	-0.014	25.542	-0.816	-0.816	0.000	0.000	0.000	0.000
78	A	79	MET	0	-0.044	0.007	19.756	0.136	0.136	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.020	-0.001	25.747	0.194	0.194	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.868	-0.933	27.403	-10.628	-10.628	0.000	0.000	0.000	0.000
81	A	82	PHE	0	-0.020	-0.021	22.102	-0.583	-0.583	0.000	0.000	0.000	0.000
82	A	83	TYR	0	0.058	0.024	23.654	0.394	0.394	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.019	0.003	19.899	-0.754	-0.754	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.017	0.023	20.258	0.730	0.730	0.000	0.000	0.000	0.000
85	A	86	SER	0	0.064	0.013	22.501	-0.440	-0.440	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.030	0.028	22.718	0.064	0.064	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.021	0.004	14.418	-0.112	-0.112	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.009	-0.001	19.985	-0.256	-0.256	0.000	0.000	0.000	0.000
89	A	90	ASN	0	-0.016	-0.013	22.539	0.090	0.090	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.042	-0.038	20.383	-0.067	-0.067	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.009	0.004	17.190	-0.372	-0.372	0.000	0.000	0.000	0.000
92	A	93	ALA	0	-0.014	0.001	15.336	-1.387	-1.387	0.000	0.000	0.000	0.000
93	A	94	SER	0	0.042	-0.012	11.278	0.649	0.649	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.008	0.001	14.009	-0.181	-0.181	0.000	0.000	0.000	0.000
95	A	96	TYR	0	0.010	0.008	17.032	0.881	0.881	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.744	-0.816	11.864	-24.125	-24.125	0.000	0.000	0.000	0.000
97	A	98	PHE	0	-0.062	-0.034	13.983	-1.683	-1.683	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.008	-0.003	16.630	0.922	0.922	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.013	-0.003	18.963	-0.530	-0.530	0.000	0.000	0.000	0.000
100	A	101	ILE	0	-0.012	-0.008	19.102	0.311	0.311	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.848	0.916	22.949	10.031	10.031	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.010	-0.021	24.911	-0.227	-0.227	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.788	-0.896	27.341	-10.333	-10.333	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.001	0.007	29.774	0.304	0.304	0.000	0.000	0.000	0.000
105	A	106	ASN	0	-0.011	-0.002	29.427	-0.583	-0.583	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.060	0.030	25.847	0.097	0.097	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.030	0.017	26.665	-0.099	-0.099	0.000	0.000	0.000	0.000
108	A	109	ASN	0	-0.036	-0.038	27.472	-0.131	-0.131	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.059	-0.015	29.835	0.336	0.336	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.038	-0.022	24.395	0.057	0.057	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.015	0.027	26.067	-0.240	-0.240	0.000	0.000	0.000	0.000
112	A	113	TYR	0	-0.046	-0.040	23.995	-0.414	-0.414	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.847	0.918	19.864	14.008	14.008	0.000	0.000	0.000	0.000
114	A	115	SER	0	0.007	0.000	23.080	0.208	0.208	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.005	-0.014	21.094	-0.758	-0.758	0.000	0.000	0.000	0.000
116	A	117	ARG	1	0.846	0.926	21.449	14.703	14.703	0.000	0.000	0.000	0.000
117	A	118	GLN	0	0.041	0.013	22.197	-0.504	-0.504	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.051	-0.030	19.250	0.313	0.313	0.000	0.000	0.000	0.000
119	A	120	THR	0	-0.008	0.005	22.577	-0.138	-0.138	0.000	0.000	0.000	0.000
120	A	121	ASN	0	-0.013	-0.014	19.980	-0.961	-0.961	0.000	0.000	0.000	0.000
121	A	122	LEU	0	0.019	-0.011	15.791	0.249	0.249	0.000	0.000	0.000	0.000
122	A	123	THR	0	-0.055	-0.047	16.629	-0.643	-0.643	0.000	0.000	0.000	0.000
123	A	124	GLY	0	-0.002	0.008	17.051	1.003	1.003	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.069	-0.039	17.807	0.627	0.627	0.000	0.000	0.000	0.000
125	A	126	THR	0	-0.024	-0.012	16.508	-1.389	-1.389	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.035	-0.021	11.574	0.948	0.948	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.834	0.913	13.795	17.051	17.051	0.000	0.000	0.000	0.000
128	A	129	ILE	0	0.000	0.008	7.709	0.106	0.106	0.000	0.000	0.000	0.000
129	A	130	SER	0	0.004	-0.023	11.098	-0.213	-0.213	0.000	0.000	0.000	0.000
130	A	131	GLY	0	0.019	-0.001	11.028	0.222	0.222	0.000	0.000	0.000	0.000
131	A	132	TYR	0	-0.034	-0.024	11.196	0.555	0.555	0.000	0.000	0.000	0.000
132	A	133	PRO	0	-0.034	0.003	7.411	-0.728	-0.728	0.000	0.000	0.000	0.000
133	A	134	GLY	0	0.067	0.006	9.011	2.412	2.412	0.000	0.000	0.000	0.000
134	A	135	ASP	-1	-0.806	-0.880	7.519	-34.883	-34.883	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.908	0.962	9.690	29.541	29.541	0.000	0.000	0.000	0.000
136	A	137	MET	0	-0.047	0.017	12.000	2.329	2.329	0.000	0.000	0.000	0.000
137	A	138	ARG	1	0.959	0.977	9.188	26.911	26.911	0.000	0.000	0.000	0.000
138	A	139	SER	0	-0.019	-0.017	13.390	0.488	0.488	0.000	0.000	0.000	0.000
139	A	140	THR	0	-0.072	-0.050	15.140	1.153	1.153	0.000	0.000	0.000	0.000
140	A	141	GLY	0	0.024	0.022	17.633	0.932	0.932	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.841	0.919	18.069	15.198	15.198	0.000	0.000	0.000	0.000
142	A	143	VAL	0	0.043	0.029	16.135	-1.248	-1.248	0.000	0.000	0.000	0.000
143	A	144	SER	0	-0.045	-0.037	15.606	1.452	1.452	0.000	0.000	0.000	0.000
144	A	145	GLN	0	0.014	0.020	14.407	-1.635	-1.635	0.000	0.000	0.000	0.000
145	A	146	TRP	0	-0.001	-0.017	11.060	0.586	0.586	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.731	-0.836	11.624	-19.797	-19.797	0.000	0.000	0.000	0.000
147	A	148	MET	0	0.018	0.048	9.334	-1.530	-1.530	0.000	0.000	0.000	0.000
148	A	149	SER	0	-0.019	-0.028	11.741	0.991	0.991	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.051	0.030	12.853	-0.348	-0.348	0.000	0.000	0.000	0.000
150	A	151	SER	0	0.005	0.009	13.790	0.235	0.235	0.000	0.000	0.000	0.000
151	A	152	VAL	0	-0.017	0.006	12.564	-2.010	-2.010	0.000	0.000	0.000	0.000
152	A	153	THR	0	-0.006	-0.011	10.626	1.416	1.416	0.000	0.000	0.000	0.000
153	A	154	ARG	1	0.951	0.982	10.150	25.288	25.288	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.722	-0.814	13.229	-18.618	-18.618	0.000	0.000	0.000	0.000
155	A	156	ASP	-1	-0.764	-0.852	14.591	-19.148	-19.148	0.000	0.000	0.000	0.000
156	A	157	THR	0	0.028	0.000	17.111	0.078	0.078	0.000	0.000	0.000	0.000
157	A	158	ASN	0	-0.059	-0.020	17.385	0.772	0.772	0.000	0.000	0.000	0.000
158	A	159	LEU	0	-0.039	-0.018	11.807	-0.356	-0.356	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.025	0.010	12.809	1.201	1.201	0.000	0.000	0.000	0.000
160	A	161	TYR	0	-0.056	-0.060	8.180	-2.826	-2.826	0.000	0.000	0.000	0.000
161	A	162	TYR	0	0.036	-0.020	6.196	4.832	4.832	0.000	0.000	0.000	0.000
162	A	163	THR	0	0.022	-0.002	6.006	-4.744	-4.744	0.000	0.000	0.000	0.000
163	A	164	ILE	0	0.013	0.024	6.734	-1.094	-1.094	0.000	0.000	0.000	0.000
168	A	169	GLY	0	0.073	0.039	6.999	1.386	1.386	0.000	0.000	0.000	0.000
169	A	170	ASN	0	0.013	0.005	5.466	-1.197	-1.197	0.000	0.000	0.000	0.000
170	A	171	SER	0	0.005	0.021	7.606	0.312	0.312	0.000	0.000	0.000	0.000
171	A	172	GLY	0	0.057	0.032	9.062	2.098	2.098	0.000	0.000	0.000	0.000
172	A	173	SER	0	-0.038	-0.037	8.973	1.928	1.928	0.000	0.000	0.000	0.000
173	A	174	ALA	0	-0.010	0.001	11.082	-1.077	-1.077	0.000	0.000	0.000	0.000
174	A	175	MET	0	-0.048	-0.002	10.572	-0.343	-0.343	0.000	0.000	0.000	0.000
175	A	176	LEU	0	-0.019	-0.006	13.799	1.756	1.756	0.000	0.000	0.000	0.000
176	A	177	ASP	-1	-0.721	-0.861	16.711	-14.918	-14.918	0.000	0.000	0.000	0.000
177	A	178	GLN	0	0.023	0.000	19.345	0.045	0.045	0.000	0.000	0.000	0.000
178	A	179	ASN	0	-0.058	-0.017	21.866	0.771	0.771	0.000	0.000	0.000	0.000
179	A	180	GLN	0	-0.025	-0.018	20.771	0.319	0.319	0.000	0.000	0.000	0.000
180	A	181	GLN	0	0.024	0.021	21.760	0.385	0.385	0.000	0.000	0.000	0.000
181	A	182	ILE	0	-0.026	-0.012	16.907	-0.713	-0.713	0.000	0.000	0.000	0.000
182	A	183	VAL	0	0.026	0.007	16.389	0.840	0.840	0.000	0.000	0.000	0.000
183	A	184	GLY	0	0.083	0.027	15.044	0.165	0.165	0.000	0.000	0.000	0.000
184	A	185	VAL	0	-0.059	-0.017	12.016	0.322	0.322	0.000	0.000	0.000	0.000
186	A	187	ASN	0	-0.055	-0.037	8.247	0.646	0.646	0.000	0.000	0.000	0.000
187	A	188	ALA	0	0.001	0.007	5.287	-0.729	-0.729	0.000	0.000	0.000	0.000
191	A	192	ASN	0	0.015	0.009	6.898	-0.796	-0.796	0.000	0.000	0.000	0.000
197	A	198	GLY	0	0.014	0.021	7.712	-3.086	-3.086	0.000	0.000	0.000	0.000
198	A	199	PRO	0	-0.021	0.004	10.541	1.271	1.271	0.000	0.000	0.000	0.000
199	A	200	LYS	1	0.828	0.891	14.396	16.666	16.666	0.000	0.000	0.000	0.000
200	A	201	ALA	0	-0.013	-0.002	16.762	0.498	0.498	0.000	0.000	0.000	0.000
201	A	202	THR	0	0.024	0.007	19.845	0.862	0.862	0.000	0.000	0.000	0.000
202	A	203	ALA	0	0.030	0.009	22.253	0.046	0.046	0.000	0.000	0.000	0.000
203	A	204	ALA	0	0.076	0.042	23.574	0.074	0.074	0.000	0.000	0.000	0.000
204	A	205	PHE	0	-0.035	-0.005	17.034	0.008	0.008	0.000	0.000	0.000	0.000
205	A	206	VAL	0	0.019	-0.006	22.273	0.105	0.105	0.000	0.000	0.000	0.000
206	A	207	GLU	-1	-0.911	-0.953	24.899	-10.869	-10.869	0.000	0.000	0.000	0.000
207	A	208	PHE	0	0.011	0.004	22.478	0.244	0.244	0.000	0.000	0.000	0.000
208	A	209	ILE	0	0.001	-0.014	20.634	0.142	0.142	0.000	0.000	0.000	0.000
209	A	210	ASN	0	-0.023	-0.024	24.759	0.099	0.099	0.000	0.000	0.000	0.000
210	A	211	TYR	0	0.009	0.016	27.355	0.407	0.407	0.000	0.000	0.000	0.000
211	A	212	ALA	0	0.030	0.014	25.347	0.258	0.258	0.000	0.000	0.000	0.000
212	A	213	LYS	1	0.880	0.939	25.180	12.263	12.263	0.000	0.000	0.000	0.000
213	A	214	ALA	0	-0.021	-0.005	28.459	0.161	0.161	0.000	0.000	0.000	0.000
214	A	215	GLN	-1	-0.852	-0.861	29.815	-9.634	-9.634	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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