FMO DATABASE

FMODB ID: 196JZ

Calculation Name: 2A31-A-Xray547

Preferred Name: Trypsin

Target Type: SINGLE PROTEIN

Ligand Name: guanidine-3-propanol | borate ion

Ligand 3-letter code: PG3 | BO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A31

Chain ID: A

ChEMBL ID: CHEMBL2366

UniProt ID: P00761

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	217
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2548159.962007
FMO2-HF: Nuclear repulsion	2463376.826626
FMO2-HF: Total energy	-84783.135381
FMO2-MP2: Total energy	-85022.455636

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:16:ILE)

Summations of interaction energy for fragment #1(A:16:ILE)

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.
-138.75	-123.533	38.377	-22.008	-31.58	-0.231

Interaction energy analysis for fragmet #1(A:16:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.728 / q_NPA : 0.859

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	18	GLY	0	0.046	0.013	3.388	3.642	5.303	0.063	-0.672	-1.052	-0.001
4	A	19	GLY	0	-0.042	-0.018	2.403	3.741	4.496	1.034	-0.746	-1.043	0.000
5	A	20	TYR	0	-0.025	-0.015	3.211	4.480	4.037	0.028	0.651	-0.236	0.000
7	A	22	CYS	0	-0.075	-0.022	2.743	-1.187	0.870	0.733	-1.007	-1.783	-0.014
117	A	138	ILE	0	0.003	0.015	2.574	0.512	0.942	0.857	-0.207	-1.080	0.001
118	A	139	SER	0	-0.003	-0.034	2.521	-2.584	-1.389	0.762	-0.594	-1.362	-0.002
119	A	140	GLY	0	0.004	-0.002	2.885	0.819	1.869	0.906	-0.273	-1.684	-0.009
120	A	141	TRP	0	-0.001	0.001	3.235	-6.660	-5.840	0.101	-0.249	-0.672	-0.004
121	A	142	GLY	0	0.032	0.010	2.987	9.503	10.166	0.047	-0.261	-0.448	-0.001
122	A	143	ASN	0	-0.023	-0.030	2.563	-18.402	-16.381	1.801	-1.944	-1.879	-0.021
123	A	144	THR	0	0.031	-0.005	1.921	-29.281	-29.244	6.665	-3.661	-3.040	-0.045
124	A	145	LYS	1	0.857	0.944	4.213	33.036	33.144	-0.001	-0.026	-0.081	0.000
131	A	152	PRO	0	-0.041	0.007	3.823	4.874	5.030	-0.001	-0.017	-0.138	0.000
135	A	156	GLN	0	-0.051	-0.038	2.334	1.154	1.828	2.358	-0.952	-2.080	-0.004
136	A	158	LEU	0	0.012	0.002	2.264	-2.077	-1.434	2.854	-0.849	-2.648	-0.005
137	A	159	LYS	1	0.906	0.964	3.695	24.138	24.279	0.011	0.010	-0.161	0.000
168	A	189	ASP	-1	-0.753	-0.868	4.284	-32.237	-32.006	-0.001	-0.028	-0.202	0.000
169	A	190	SER	0	-0.042	0.003	2.248	-16.073	-12.909	1.889	-2.496	-2.557	-0.015
170	A	191	CYS	0	-0.048	-0.030	3.277	7.603	7.814	0.019	0.342	-0.571	-0.001
171	A	192	GLN	0	0.105	0.026	4.813	-2.273	-2.145	-0.001	-0.004	-0.122	0.000
172	A	193	GLY	0	0.023	0.021	5.177	-7.148	-7.126	-0.001	-0.001	-0.019	0.000
173	A	194	ASP	-1	-0.766	-0.868	1.921	-132.915	-133.621	18.256	-8.988	-8.562	-0.110
174	A	195	SER	0	0.002	-0.015	4.676	4.039	4.139	-0.001	-0.028	-0.071	0.000
187	A	213	VAL	0	-0.048	-0.025	4.312	0.875	0.974	-0.001	-0.008	-0.089	0.000
6	A	21	THR	0	0.050	0.026	5.264	-4.632	-4.632	0.000	0.000	0.000	0.000
8	A	23	ALA	0	0.056	0.023	8.273	1.107	1.107	0.000	0.000	0.000	0.000
9	A	24	ALA	0	0.066	0.039	11.430	-0.808	-0.808	0.000	0.000	0.000	0.000
10	A	25	ASN	0	-0.013	-0.013	12.362	2.004	2.004	0.000	0.000	0.000	0.000
11	A	26	SER	0	-0.056	-0.041	10.999	0.288	0.288	0.000	0.000	0.000	0.000
12	A	27	ILE	0	-0.025	-0.007	7.377	0.395	0.395	0.000	0.000	0.000	0.000
13	A	28	PRO	0	0.047	0.028	10.801	-0.678	-0.678	0.000	0.000	0.000	0.000
14	A	29	TYR	0	0.026	0.021	9.102	1.192	1.192	0.000	0.000	0.000	0.000
15	A	30	GLN	0	-0.008	0.004	6.177	-2.196	-2.196	0.000	0.000	0.000	0.000
16	A	31	VAL	0	-0.015	0.000	10.078	1.376	1.376	0.000	0.000	0.000	0.000
17	A	32	SER	0	-0.005	-0.015	9.677	-2.022	-2.022	0.000	0.000	0.000	0.000
18	A	33	LEU	0	-0.033	-0.011	11.185	2.683	2.683	0.000	0.000	0.000	0.000
19	A	34	ASN	0	0.047	0.011	12.854	-0.279	-0.279	0.000	0.000	0.000	0.000
20	A	37	SER	0	-0.021	-0.028	15.413	0.792	0.792	0.000	0.000	0.000	0.000
21	A	38	GLY	0	0.005	0.016	18.066	0.543	0.543	0.000	0.000	0.000	0.000
22	A	39	SER	0	0.014	0.007	14.021	0.176	0.176	0.000	0.000	0.000	0.000
23	A	40	HIS	0	0.041	0.032	6.964	4.037	4.037	0.000	0.000	0.000	0.000
24	A	41	PHE	0	-0.024	-0.030	10.682	-0.701	-0.701	0.000	0.000	0.000	0.000
25	A	42	CYS	0	-0.083	-0.016	8.944	-2.380	-2.380	0.000	0.000	0.000	0.000
26	A	43	GLY	0	0.042	0.033	7.141	0.255	0.255	0.000	0.000	0.000	0.000
27	A	44	GLY	0	0.023	0.005	8.160	2.170	2.170	0.000	0.000	0.000	0.000
28	A	45	SER	0	-0.015	-0.008	9.704	-1.328	-1.328	0.000	0.000	0.000	0.000
29	A	46	LEU	0	-0.014	0.000	11.738	1.058	1.058	0.000	0.000	0.000	0.000
30	A	47	ILE	0	-0.020	-0.020	15.087	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	48	ASN	0	0.015	0.003	17.586	0.834	0.834	0.000	0.000	0.000	0.000
32	A	49	SER	0	0.057	0.033	20.219	-0.444	-0.444	0.000	0.000	0.000	0.000
33	A	50	GLN	0	0.028	0.007	22.391	-0.035	-0.035	0.000	0.000	0.000	0.000
34	A	51	TRP	0	0.029	0.015	20.072	-0.055	-0.055	0.000	0.000	0.000	0.000
35	A	52	VAL	0	0.030	0.021	13.692	-0.265	-0.265	0.000	0.000	0.000	0.000
36	A	53	VAL	0	-0.026	-0.005	13.355	0.718	0.718	0.000	0.000	0.000	0.000
37	A	54	SER	0	0.015	-0.002	11.187	-1.306	-1.306	0.000	0.000	0.000	0.000
38	A	55	ALA	0	0.057	0.031	11.414	1.039	1.039	0.000	0.000	0.000	0.000
39	A	56	ALA	0	-0.040	-0.018	13.190	0.425	0.425	0.000	0.000	0.000	0.000
40	A	57	HIS	0	-0.045	-0.041	10.864	-1.106	-1.106	0.000	0.000	0.000	0.000
41	A	59	TYR	0	0.013	0.002	14.543	0.404	0.404	0.000	0.000	0.000	0.000
42	A	60	LYS	1	0.891	0.954	15.464	19.229	19.229	0.000	0.000	0.000	0.000
43	A	61	SER	0	0.010	0.011	20.139	-0.021	-0.021	0.000	0.000	0.000	0.000
44	A	62	ARG	1	0.936	0.962	21.985	12.302	12.302	0.000	0.000	0.000	0.000
45	A	63	ILE	0	0.020	0.013	16.540	-0.595	-0.595	0.000	0.000	0.000	0.000
46	A	64	GLN	0	0.008	0.019	18.518	0.301	0.301	0.000	0.000	0.000	0.000
47	A	65	VAL	0	0.015	0.005	15.179	-1.303	-1.303	0.000	0.000	0.000	0.000
48	A	66	ARG	1	0.850	0.939	14.236	19.098	19.098	0.000	0.000	0.000	0.000
49	A	67	LEU	0	0.044	0.010	13.902	-1.541	-1.541	0.000	0.000	0.000	0.000
50	A	69	GLY	0	0.050	0.019	15.063	0.604	0.604	0.000	0.000	0.000	0.000
51	A	70	GLU	-1	-0.855	-0.948	12.120	-20.469	-20.469	0.000	0.000	0.000	0.000
52	A	71	HIS	0	-0.086	-0.040	9.456	-1.247	-1.247	0.000	0.000	0.000	0.000
53	A	72	ASN	0	0.008	-0.019	10.572	-3.974	-3.974	0.000	0.000	0.000	0.000
54	A	73	ILE	0	0.026	0.027	9.355	1.218	1.218	0.000	0.000	0.000	0.000
55	A	74	ASP	-1	-0.890	-0.915	12.354	-23.315	-23.315	0.000	0.000	0.000	0.000
56	A	75	VAL	0	-0.099	-0.060	14.990	1.403	1.403	0.000	0.000	0.000	0.000
57	A	76	LEU	0	-0.023	0.000	17.403	-0.338	-0.338	0.000	0.000	0.000	0.000
58	A	77	GLU	-1	-0.839	-0.938	15.237	-19.517	-19.517	0.000	0.000	0.000	0.000
59	A	78	GLY	0	-0.037	-0.013	19.622	0.648	0.648	0.000	0.000	0.000	0.000
60	A	79	ASN	0	-0.050	-0.033	18.485	1.020	1.020	0.000	0.000	0.000	0.000
61	A	80	GLU	-1	-0.789	-0.869	16.602	-16.345	-16.345	0.000	0.000	0.000	0.000
62	A	81	GLN	0	-0.022	-0.020	18.396	1.045	1.045	0.000	0.000	0.000	0.000
63	A	82	PHE	0	-0.009	-0.008	17.125	-0.680	-0.680	0.000	0.000	0.000	0.000
64	A	83	ILE	0	-0.006	0.003	19.768	0.767	0.767	0.000	0.000	0.000	0.000
65	A	84	ASN	0	0.025	0.010	20.323	-1.146	-1.146	0.000	0.000	0.000	0.000
66	A	85	ALA	0	0.031	0.027	20.381	0.331	0.331	0.000	0.000	0.000	0.000
67	A	86	ALA	0	-0.031	-0.015	22.189	0.419	0.419	0.000	0.000	0.000	0.000
68	A	87	LYS	1	0.776	0.867	23.816	10.888	10.888	0.000	0.000	0.000	0.000
69	A	88	ILE	0	0.008	0.006	19.418	-0.526	-0.526	0.000	0.000	0.000	0.000
70	A	89	ILE	0	-0.005	0.003	21.063	0.417	0.417	0.000	0.000	0.000	0.000
71	A	90	THR	0	0.051	0.025	19.181	-0.566	-0.566	0.000	0.000	0.000	0.000
72	A	91	HIS	0	0.018	0.013	20.173	0.664	0.664	0.000	0.000	0.000	0.000
73	A	92	PRO	0	-0.031	-0.014	22.047	-0.090	-0.090	0.000	0.000	0.000	0.000
74	A	93	ASN	0	0.006	0.000	24.526	0.420	0.420	0.000	0.000	0.000	0.000
75	A	94	PHE	0	-0.014	-0.001	17.838	-0.287	-0.287	0.000	0.000	0.000	0.000
76	A	95	ASN	0	0.017	0.013	21.591	0.146	0.146	0.000	0.000	0.000	0.000
77	A	96	GLY	0	0.014	-0.001	20.068	-0.567	-0.567	0.000	0.000	0.000	0.000
78	A	97	ASN	0	-0.077	-0.024	20.461	-0.504	-0.504	0.000	0.000	0.000	0.000
79	A	98	THR	0	0.047	-0.002	20.518	-0.489	-0.489	0.000	0.000	0.000	0.000
80	A	99	LEU	0	0.019	0.019	15.182	-0.493	-0.493	0.000	0.000	0.000	0.000
81	A	100	ASP	-1	-0.797	-0.870	17.519	-13.801	-13.801	0.000	0.000	0.000	0.000
82	A	101	ASN	0	-0.014	-0.003	19.380	0.267	0.267	0.000	0.000	0.000	0.000
83	A	102	ASP	-1	-0.690	-0.792	13.880	-20.265	-20.265	0.000	0.000	0.000	0.000
84	A	103	ILE	0	-0.063	-0.014	14.672	-1.167	-1.167	0.000	0.000	0.000	0.000
85	A	104	MET	0	-0.007	-0.006	15.325	1.278	1.278	0.000	0.000	0.000	0.000
86	A	105	LEU	0	-0.019	-0.003	16.298	-0.746	-0.746	0.000	0.000	0.000	0.000
87	A	106	ILE	0	0.007	-0.003	15.814	0.370	0.370	0.000	0.000	0.000	0.000
88	A	107	LYS	1	0.862	0.938	19.388	10.653	10.653	0.000	0.000	0.000	0.000
89	A	108	LEU	0	-0.012	-0.018	18.560	-0.116	-0.116	0.000	0.000	0.000	0.000
90	A	109	SER	0	-0.036	-0.045	22.516	0.575	0.575	0.000	0.000	0.000	0.000
91	A	110	SER	0	0.021	0.011	24.792	0.536	0.536	0.000	0.000	0.000	0.000
92	A	111	PRO	0	-0.038	-0.032	24.112	-0.497	-0.497	0.000	0.000	0.000	0.000
93	A	112	ALA	0	0.033	0.024	20.222	0.031	0.031	0.000	0.000	0.000	0.000
94	A	113	THR	0	-0.034	-0.017	22.149	0.530	0.530	0.000	0.000	0.000	0.000
95	A	114	LEU	0	-0.009	-0.009	20.305	-0.420	-0.420	0.000	0.000	0.000	0.000
96	A	115	ASN	0	0.012	0.000	20.598	0.162	0.162	0.000	0.000	0.000	0.000
97	A	116	SER	0	-0.002	-0.010	20.010	-0.483	-0.483	0.000	0.000	0.000	0.000
98	A	117	ARG	1	0.912	0.963	16.525	13.901	13.901	0.000	0.000	0.000	0.000
99	A	118	VAL	0	-0.015	0.004	15.971	-1.023	-1.023	0.000	0.000	0.000	0.000
100	A	119	ALA	0	0.015	0.006	16.545	1.044	1.044	0.000	0.000	0.000	0.000
101	A	120	THR	0	-0.012	0.005	16.210	-0.626	-0.626	0.000	0.000	0.000	0.000
102	A	121	VAL	0	-0.009	-0.003	12.793	0.191	0.191	0.000	0.000	0.000	0.000
103	A	122	SER	0	-0.041	-0.013	15.871	0.810	0.810	0.000	0.000	0.000	0.000
104	A	123	LEU	0	0.057	0.026	16.491	-0.856	-0.856	0.000	0.000	0.000	0.000
105	A	124	PRO	0	-0.065	-0.037	16.776	0.472	0.472	0.000	0.000	0.000	0.000
106	A	125	ARG	1	0.952	0.970	19.269	13.231	13.231	0.000	0.000	0.000	0.000
107	A	127	SER	0	0.017	0.014	21.568	0.580	0.580	0.000	0.000	0.000	0.000
108	A	128	CYS	0	-0.071	-0.024	16.460	0.094	0.094	0.000	0.000	0.000	0.000
109	A	129	ALA	0	0.016	0.014	16.174	0.429	0.429	0.000	0.000	0.000	0.000
110	A	130	ALA	0	0.027	0.026	18.259	0.144	0.144	0.000	0.000	0.000	0.000
111	A	132	ALA	0	0.039	0.021	17.590	-0.773	-0.773	0.000	0.000	0.000	0.000
112	A	133	GLY	0	-0.006	-0.004	16.932	0.629	0.629	0.000	0.000	0.000	0.000
113	A	134	THR	0	-0.088	-0.056	15.195	0.266	0.266	0.000	0.000	0.000	0.000
114	A	135	GLU	-1	-0.874	-0.947	12.064	-20.683	-20.683	0.000	0.000	0.000	0.000
115	A	136	CYS	0	-0.037	-0.010	9.281	0.398	0.398	0.000	0.000	0.000	0.000
116	A	137	LEU	0	-0.052	-0.033	6.089	-0.504	-0.504	0.000	0.000	0.000	0.000
125	A	146	SER	0	0.049	0.028	6.884	-1.916	-1.916	0.000	0.000	0.000	0.000
126	A	147	SER	0	-0.015	-0.020	9.036	3.576	3.576	0.000	0.000	0.000	0.000
127	A	148	GLY	0	0.012	0.017	11.383	0.254	0.254	0.000	0.000	0.000	0.000
128	A	149	SER	0	0.003	-0.006	8.713	-3.841	-3.841	0.000	0.000	0.000	0.000
129	A	150	SER	0	0.005	-0.015	7.546	5.169	5.169	0.000	0.000	0.000	0.000
130	A	151	TYR	0	0.022	0.024	5.924	-8.550	-8.550	0.000	0.000	0.000	0.000
132	A	153	SER	0	0.067	0.003	6.957	-1.039	-1.039	0.000	0.000	0.000	0.000
133	A	154	LEU	0	-0.050	-0.019	9.126	0.791	0.791	0.000	0.000	0.000	0.000
134	A	155	LEU	0	-0.008	0.015	5.419	-5.215	-5.215	0.000	0.000	0.000	0.000
138	A	160	ALA	0	0.031	0.009	6.932	-0.932	-0.932	0.000	0.000	0.000	0.000
139	A	161	PRO	0	0.072	0.059	8.926	0.432	0.432	0.000	0.000	0.000	0.000
140	A	162	VAL	0	-0.009	-0.012	11.971	-0.972	-0.972	0.000	0.000	0.000	0.000
141	A	163	LEU	0	-0.021	-0.003	12.766	1.240	1.240	0.000	0.000	0.000	0.000
142	A	164	SER	0	0.028	0.010	15.558	0.235	0.235	0.000	0.000	0.000	0.000
143	A	165	ASP	-1	-0.860	-0.933	19.001	-13.528	-13.528	0.000	0.000	0.000	0.000
144	A	166	SER	0	-0.001	0.001	20.939	-0.271	-0.271	0.000	0.000	0.000	0.000
145	A	167	SER	0	0.029	0.025	17.504	0.120	0.120	0.000	0.000	0.000	0.000
146	A	168	CYS	0	-0.006	0.030	12.545	-1.290	-1.290	0.000	0.000	0.000	0.000
147	A	169	LYS	1	0.980	0.971	17.933	12.403	12.403	0.000	0.000	0.000	0.000
148	A	170	SER	0	-0.062	-0.038	21.170	0.173	0.173	0.000	0.000	0.000	0.000
149	A	171	SER	0	-0.006	-0.008	16.610	-0.109	-0.109	0.000	0.000	0.000	0.000
150	A	172	TYR	0	-0.060	-0.044	12.727	0.016	0.016	0.000	0.000	0.000	0.000
151	A	173	PRO	0	0.038	0.016	19.463	0.307	0.307	0.000	0.000	0.000	0.000
152	A	174	GLY	0	-0.017	-0.009	23.273	0.082	0.082	0.000	0.000	0.000	0.000
153	A	175	GLN	0	-0.014	-0.007	19.236	0.035	0.035	0.000	0.000	0.000	0.000
154	A	176	ILE	0	-0.019	-0.004	16.621	-0.279	-0.279	0.000	0.000	0.000	0.000
155	A	177	THR	0	0.021	-0.023	19.792	0.601	0.601	0.000	0.000	0.000	0.000
156	A	178	GLY	0	-0.009	-0.012	20.625	-0.287	-0.287	0.000	0.000	0.000	0.000
157	A	179	ASN	0	-0.036	-0.024	19.505	0.227	0.227	0.000	0.000	0.000	0.000
158	A	180	MET	0	-0.031	0.036	16.161	-0.885	-0.885	0.000	0.000	0.000	0.000
159	A	181	ILE	0	-0.010	-0.005	12.708	0.914	0.914	0.000	0.000	0.000	0.000
160	A	183	VAL	0	-0.015	-0.010	8.954	1.115	1.115	0.000	0.000	0.000	0.000
161	A	184	GLY	0	0.023	0.017	8.667	-2.300	-2.300	0.000	0.000	0.000	0.000
162	A	184	PHE	0	-0.018	-0.019	7.340	1.689	1.689	0.000	0.000	0.000	0.000
163	A	185	LEU	0	0.030	0.016	11.340	-0.168	-0.168	0.000	0.000	0.000	0.000
164	A	186	GLU	-1	-0.868	-0.942	12.908	-17.912	-17.912	0.000	0.000	0.000	0.000
165	A	187	GLY	0	-0.021	-0.007	11.961	-1.173	-1.173	0.000	0.000	0.000	0.000
166	A	188	GLY	0	-0.032	-0.026	9.233	0.663	0.663	0.000	0.000	0.000	0.000
167	A	188	LYS	1	0.901	0.954	5.564	24.000	24.000	0.000	0.000	0.000	0.000
175	A	196	GLY	0	0.011	-0.013	7.962	0.646	0.646	0.000	0.000	0.000	0.000
176	A	197	GLY	0	-0.021	0.001	5.338	2.060	2.060	0.000	0.000	0.000	0.000
177	A	198	PRO	0	-0.017	-0.008	5.518	2.210	2.210	0.000	0.000	0.000	0.000
178	A	199	VAL	0	0.022	0.015	5.667	-3.116	-3.116	0.000	0.000	0.000	0.000
179	A	200	VAL	0	-0.028	-0.014	8.157	2.369	2.369	0.000	0.000	0.000	0.000
180	A	202	ASN	0	0.023	0.005	13.136	0.595	0.595	0.000	0.000	0.000	0.000
181	A	203	GLY	0	0.016	0.013	15.190	0.747	0.747	0.000	0.000	0.000	0.000
182	A	204	GLN	0	-0.041	-0.024	15.376	0.880	0.880	0.000	0.000	0.000	0.000
183	A	209	LEU	0	0.012	0.011	10.511	-0.828	-0.828	0.000	0.000	0.000	0.000
184	A	210	GLN	0	0.013	-0.021	12.673	0.929	0.929	0.000	0.000	0.000	0.000
185	A	211	GLY	0	-0.002	0.002	11.021	0.856	0.856	0.000	0.000	0.000	0.000
186	A	212	ILE	0	-0.011	-0.001	9.169	-0.596	-0.596	0.000	0.000	0.000	0.000
188	A	214	SER	0	-0.030	-0.031	7.633	0.850	0.850	0.000	0.000	0.000	0.000
189	A	215	TRP	0	0.000	-0.031	10.799	-0.424	-0.424	0.000	0.000	0.000	0.000
190	A	216	GLY	0	0.080	0.035	10.542	-1.190	-1.190	0.000	0.000	0.000	0.000
191	A	217	TYR	0	-0.036	-0.014	12.015	1.265	1.265	0.000	0.000	0.000	0.000
192	A	219	GLY	0	-0.014	-0.001	11.546	-0.029	-0.029	0.000	0.000	0.000	0.000
193	A	221	ALA	0	-0.025	-0.010	6.700	1.434	1.434	0.000	0.000	0.000	0.000
194	A	221	GLN	0	0.057	0.027	8.611	3.048	3.048	0.000	0.000	0.000	0.000
195	A	222	LYS	1	0.951	0.965	12.405	15.726	15.726	0.000	0.000	0.000	0.000
196	A	223	ASN	0	-0.070	-0.042	15.158	0.734	0.734	0.000	0.000	0.000	0.000
197	A	224	LYS	1	0.850	0.933	13.441	18.123	18.123	0.000	0.000	0.000	0.000
198	A	225	PRO	0	0.021	0.037	10.413	-1.653	-1.653	0.000	0.000	0.000	0.000
199	A	226	GLY	0	0.082	0.063	8.140	0.996	0.996	0.000	0.000	0.000	0.000
200	A	227	VAL	0	-0.020	-0.030	9.160	2.107	2.107	0.000	0.000	0.000	0.000
201	A	228	TYR	0	-0.038	-0.038	5.734	-0.437	-0.437	0.000	0.000	0.000	0.000
202	A	229	THR	0	-0.013	-0.022	11.540	1.412	1.412	0.000	0.000	0.000	0.000
203	A	230	LYS	1	0.937	0.969	13.632	13.387	13.387	0.000	0.000	0.000	0.000
204	A	231	VAL	0	0.025	0.009	13.544	1.087	1.087	0.000	0.000	0.000	0.000
205	A	233	ASN	0	-0.021	-0.018	19.467	0.597	0.597	0.000	0.000	0.000	0.000
206	A	234	TYR	0	-0.033	-0.040	18.065	0.250	0.250	0.000	0.000	0.000	0.000
207	A	235	VAL	0	-0.005	0.007	20.117	0.130	0.130	0.000	0.000	0.000	0.000
208	A	236	ASN	0	0.036	0.017	21.943	0.042	0.042	0.000	0.000	0.000	0.000
209	A	237	TRP	0	0.045	0.022	19.135	0.066	0.066	0.000	0.000	0.000	0.000
210	A	238	ILE	0	0.024	0.016	17.985	0.075	0.075	0.000	0.000	0.000	0.000
211	A	239	GLN	0	0.003	0.002	22.111	0.218	0.218	0.000	0.000	0.000	0.000
212	A	240	GLN	0	-0.003	-0.016	25.048	0.223	0.223	0.000	0.000	0.000	0.000
213	A	241	THR	0	-0.022	-0.010	23.645	0.307	0.307	0.000	0.000	0.000	0.000
214	A	242	ILE	0	-0.036	-0.025	21.191	0.120	0.120	0.000	0.000	0.000	0.000
215	A	243	ALA	0	-0.021	-0.015	25.465	0.200	0.200	0.000	0.000	0.000	0.000
216	A	244	ALA	0	-0.017	0.008	28.781	0.349	0.349	0.000	0.000	0.000	0.000
217	A	245	ASN	-1	-0.842	-0.873	27.161	-10.258	-10.258	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:ILE)