FMO DATABASE

FMODB ID: N7NLQ

Calculation Name: 4AIG-A-Xray549

Preferred Name:

Target Type:

Ligand Name: n-[(furan-2-yl)carbonyl]-(s)-leucyl-(r)-[1-amino-2(1h-indol-3-yl)ethyl]-phosphonic acid | calcium ion

Ligand 3-letter code: FLX | CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4AIG

Chain ID: A

ChEMBL ID:

UniProt ID: P34179

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	199
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2456334.015897
FMO2-HF: Nuclear repulsion	2374711.580554
FMO2-HF: Total energy	-81622.435343
FMO2-MP2: Total energy	-81857.489744

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:2:ASN)

Summations of interaction energy for fragment #1(A:2:ASN)

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.
48.379	49.454	7.312	-3.814	-4.575	0.014

Interaction energy analysis for fragmet #1(A:2:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.853 / 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	4	PRO	0	-0.030	0.006	3.862	-3.109	-1.919	-0.002	-0.417	-0.772	0.001
181	A	183	MET	0	-0.032	-0.012	4.990	-1.596	-1.501	-0.001	-0.001	-0.093	0.000
185	A	187	GLN	0	-0.025	-0.033	1.975	-18.072	-18.282	7.315	-3.396	-3.710	0.013
4	A	5	GLN	0	-0.008	0.003	5.677	3.987	3.987	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.849	0.931	8.979	30.627	30.627	0.000	0.000	0.000	0.000
6	A	7	TYR	0	0.049	0.008	11.930	0.244	0.244	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.041	0.020	14.917	0.058	0.058	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.763	-0.829	18.166	-13.142	-13.142	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.004	0.000	21.295	0.294	0.294	0.000	0.000	0.000	0.000
10	A	11	VAL	0	-0.026	-0.007	23.014	0.343	0.343	0.000	0.000	0.000	0.000
11	A	12	VAL	0	0.001	0.004	25.878	-0.132	-0.132	0.000	0.000	0.000	0.000
12	A	13	VAL	0	0.003	0.003	28.087	0.258	0.258	0.000	0.000	0.000	0.000
13	A	14	ALA	0	0.020	0.011	31.407	-0.095	-0.095	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.700	-0.847	33.928	-7.937	-7.937	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.916	0.942	36.815	6.997	6.997	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.823	0.929	38.487	7.627	7.627	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.000	-0.001	34.041	0.067	0.067	0.000	0.000	0.000	0.000
18	A	19	PHE	0	0.009	0.003	37.374	0.083	0.083	0.000	0.000	0.000	0.000
19	A	20	MET	0	-0.011	-0.012	39.921	0.093	0.093	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.835	0.922	35.441	8.358	8.358	0.000	0.000	0.000	0.000
21	A	22	TYR	0	-0.089	-0.073	34.749	0.024	0.024	0.000	0.000	0.000	0.000
22	A	23	ASN	0	-0.001	0.000	40.270	0.083	0.083	0.000	0.000	0.000	0.000
23	A	24	SER	0	-0.005	-0.002	42.753	0.169	0.169	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.833	-0.896	41.019	-7.469	-7.469	0.000	0.000	0.000	0.000
25	A	26	LEU	0	0.018	-0.010	37.543	-0.217	-0.217	0.000	0.000	0.000	0.000
26	A	27	ASN	0	-0.021	-0.022	37.419	-0.339	-0.339	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.010	0.020	36.523	-0.303	-0.303	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.000	0.004	34.447	-0.289	-0.289	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.891	0.938	32.103	8.954	8.954	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.028	-0.019	31.736	-0.380	-0.380	0.000	0.000	0.000	0.000
31	A	32	ARG	1	0.817	0.884	30.555	8.980	8.980	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.005	-0.006	27.947	-0.352	-0.352	0.000	0.000	0.000	0.000
33	A	34	HIS	0	0.008	0.005	27.154	-0.321	-0.321	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.874	-0.933	26.247	-10.162	-10.162	0.000	0.000	0.000	0.000
35	A	36	ILE	0	-0.028	-0.008	24.552	-0.422	-0.422	0.000	0.000	0.000	0.000
36	A	37	VAL	0	0.013	-0.009	21.998	-0.535	-0.535	0.000	0.000	0.000	0.000
37	A	38	ASN	0	-0.024	0.000	21.424	-0.932	-0.932	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.048	0.022	20.775	-0.575	-0.575	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.022	-0.012	18.223	-0.605	-0.605	0.000	0.000	0.000	0.000
40	A	41	ASN	0	-0.039	-0.038	16.892	-1.778	-1.778	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.950	-0.962	15.808	-14.769	-14.769	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.005	-0.002	14.975	-0.813	-0.813	0.000	0.000	0.000	0.000
43	A	44	TYR	0	0.009	-0.006	11.921	-1.476	-1.476	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.984	1.006	10.228	20.668	20.668	0.000	0.000	0.000	0.000
45	A	46	SER	0	-0.100	-0.054	9.422	-1.912	-1.912	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.002	-0.010	6.947	-2.574	-2.574	0.000	0.000	0.000	0.000
47	A	48	ASN	0	-0.049	-0.034	5.681	2.363	2.363	0.000	0.000	0.000	0.000
48	A	49	ILE	0	0.003	0.007	8.645	-0.082	-0.082	0.000	0.000	0.000	0.000
49	A	50	ARG	1	0.825	0.919	12.127	16.568	16.568	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.000	-0.010	15.586	0.050	0.050	0.000	0.000	0.000	0.000
51	A	52	SER	0	0.011	0.006	18.463	0.277	0.277	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.006	-0.004	21.916	0.077	0.077	0.000	0.000	0.000	0.000
53	A	54	THR	0	-0.003	0.007	24.405	0.245	0.245	0.000	0.000	0.000	0.000
54	A	55	ASP	0	-0.101	-0.113	26.822	0.467	0.467	0.000	0.000	0.000	0.000
55	A	56	LEU	0	0.029	0.013	28.889	-0.316	-0.316	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.845	-0.863	31.420	-8.609	-8.609	0.000	0.000	0.000	0.000
57	A	58	ILE	0	0.023	-0.003	33.954	-0.091	-0.091	0.000	0.000	0.000	0.000
58	A	59	TRP	0	-0.009	0.011	35.414	0.224	0.224	0.000	0.000	0.000	0.000
59	A	60	SER	0	0.015	-0.005	39.244	0.145	0.145	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.015	0.026	42.234	0.179	0.179	0.000	0.000	0.000	0.000
61	A	62	GLN	0	-0.011	-0.016	43.213	0.208	0.208	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.771	-0.895	39.566	-7.817	-7.817	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.020	-0.012	38.194	0.154	0.154	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.018	-0.004	34.259	-0.083	-0.083	0.000	0.000	0.000	0.000
65	A	66	THR	0	0.003	0.002	38.538	0.055	0.055	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.028	-0.009	35.615	-0.105	-0.105	0.000	0.000	0.000	0.000
67	A	68	GLN	0	-0.008	0.000	37.224	0.271	0.271	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.022	-0.013	37.014	-0.178	-0.178	0.000	0.000	0.000	0.000
69	A	70	SER	0	0.069	0.043	36.096	-0.304	-0.304	0.000	0.000	0.000	0.000
70	A	71	SER	0	0.053	0.021	31.032	-0.050	-0.050	0.000	0.000	0.000	0.000
71	A	72	SER	0	0.002	-0.016	31.498	-0.358	-0.358	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.001	-0.006	32.565	-0.280	-0.280	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.017	0.021	32.985	0.058	0.058	0.000	0.000	0.000	0.000
74	A	75	LEU	0	0.006	0.009	26.600	-0.028	-0.028	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.023	-0.011	30.584	-0.328	-0.328	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.006	-0.017	32.277	0.055	0.055	0.000	0.000	0.000	0.000
77	A	78	PHE	0	-0.008	-0.011	27.659	0.085	0.085	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.042	0.021	29.301	-0.130	-0.130	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.844	-0.908	30.121	-8.458	-8.458	0.000	0.000	0.000	0.000
80	A	81	TRP	0	0.057	0.022	31.573	-0.056	-0.056	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.805	0.889	24.861	11.875	11.875	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.913	-0.972	30.728	-9.954	-9.954	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.859	0.914	31.787	8.136	8.136	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.019	-0.006	34.697	0.193	0.193	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.004	0.008	29.482	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.018	-0.012	27.871	-0.174	-0.174	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.025	-0.005	31.069	-0.035	-0.035	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.873	0.933	32.975	8.923	8.923	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.901	0.960	29.232	9.959	9.959	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.868	0.901	23.459	13.216	13.216	0.000	0.000	0.000	0.000
91	A	92	HIS	0	-0.008	-0.016	24.426	-0.032	-0.032	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.748	-0.862	19.839	-15.268	-15.268	0.000	0.000	0.000	0.000
93	A	94	ASN	0	-0.039	-0.019	20.620	0.218	0.218	0.000	0.000	0.000	0.000
94	A	95	ALA	0	0.016	0.020	22.757	0.195	0.195	0.000	0.000	0.000	0.000
95	A	96	GLN	0	-0.006	-0.019	22.001	0.235	0.235	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.020	0.002	25.977	0.243	0.243	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.027	-0.009	28.922	-0.137	-0.137	0.000	0.000	0.000	0.000
98	A	99	THR	0	-0.003	-0.036	30.833	0.312	0.312	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.002	-0.004	33.758	-0.137	-0.137	0.000	0.000	0.000	0.000
100	A	101	ILE	0	-0.022	0.002	35.482	0.252	0.252	0.000	0.000	0.000	0.000
101	A	102	ASN	0	-0.026	-0.025	36.080	-0.357	-0.357	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.001	-0.001	31.249	0.122	0.122	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.864	-0.907	35.914	-7.510	-7.510	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.012	-0.014	35.028	-0.222	-0.222	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.925	0.956	33.585	8.084	8.084	0.000	0.000	0.000	0.000
106	A	107	ILE	0	-0.026	0.010	29.343	-0.206	-0.206	0.000	0.000	0.000	0.000
107	A	108	ILE	0	0.009	-0.007	26.702	0.220	0.220	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.015	0.010	26.112	-0.062	-0.062	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.917	0.967	25.787	10.247	10.247	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.075	0.048	22.157	0.155	0.155	0.000	0.000	0.000	0.000
111	A	112	TYR	0	-0.042	-0.009	23.478	0.216	0.216	0.000	0.000	0.000	0.000
112	A	113	THR	0	0.028	0.002	18.279	-0.403	-0.403	0.000	0.000	0.000	0.000
113	A	114	SER	0	-0.041	-0.021	16.928	-0.075	-0.075	0.000	0.000	0.000	0.000
114	A	115	SER	0	-0.035	-0.022	17.936	0.029	0.029	0.000	0.000	0.000	0.000
115	A	116	MET	0	0.021	0.014	16.205	0.753	0.753	0.000	0.000	0.000	0.000
116	A	117	CYS	0	-0.085	-0.025	16.765	-0.621	-0.621	0.000	0.000	0.000	0.000
117	A	118	ASN	0	-0.004	0.022	20.855	0.873	0.873	0.000	0.000	0.000	0.000
118	A	119	PRO	0	0.036	0.014	23.632	0.047	0.047	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.965	1.012	27.129	9.901	9.901	0.000	0.000	0.000	0.000
120	A	121	SER	0	0.014	-0.009	24.685	0.173	0.173	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.053	-0.016	21.491	-0.542	-0.542	0.000	0.000	0.000	0.000
122	A	123	VAL	0	-0.014	-0.021	23.014	0.164	0.164	0.000	0.000	0.000	0.000
123	A	124	GLY	0	0.058	0.029	24.069	-0.257	-0.257	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.079	-0.023	24.990	0.311	0.311	0.000	0.000	0.000	0.000
125	A	126	VAL	0	0.023	0.005	25.210	-0.176	-0.176	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.912	0.967	28.167	8.619	8.619	0.000	0.000	0.000	0.000
127	A	128	ASP	-1	-0.718	-0.825	30.214	-9.153	-9.153	0.000	0.000	0.000	0.000
128	A	129	HIS	0	-0.107	-0.086	27.367	0.616	0.616	0.000	0.000	0.000	0.000
129	A	130	SER	0	0.052	0.037	30.632	0.213	0.213	0.000	0.000	0.000	0.000
130	A	131	PRO	0	0.042	0.024	32.383	-0.132	-0.132	0.000	0.000	0.000	0.000
131	A	132	ILE	0	0.005	0.009	28.813	-0.105	-0.105	0.000	0.000	0.000	0.000
132	A	133	ASN	0	0.057	0.017	27.650	-0.072	-0.072	0.000	0.000	0.000	0.000
133	A	134	LEU	0	0.053	0.030	22.610	-0.239	-0.239	0.000	0.000	0.000	0.000
134	A	135	LEU	0	0.020	0.013	24.232	-0.326	-0.326	0.000	0.000	0.000	0.000
135	A	136	VAL	0	-0.005	0.016	25.511	-0.184	-0.184	0.000	0.000	0.000	0.000
136	A	137	ALA	0	0.038	0.022	22.418	-0.218	-0.218	0.000	0.000	0.000	0.000
137	A	138	VAL	0	0.008	0.005	20.545	-0.520	-0.520	0.000	0.000	0.000	0.000
138	A	139	THR	0	-0.024	-0.016	20.836	-0.218	-0.218	0.000	0.000	0.000	0.000
139	A	140	MET	0	0.014	-0.001	22.115	-0.245	-0.245	0.000	0.000	0.000	0.000
140	A	141	ALA	0	0.000	0.001	17.291	-0.401	-0.401	0.000	0.000	0.000	0.000
141	A	142	HIS	0	0.058	0.026	17.260	-0.563	-0.563	0.000	0.000	0.000	0.000
142	A	143	GLU	-1	-0.878	-0.958	18.715	-12.260	-12.260	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.006	0.000	16.994	-0.238	-0.238	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.080	0.025	14.861	-0.738	-0.738	0.000	0.000	0.000	0.000
145	A	146	HIS	1	0.792	0.892	15.363	13.141	13.141	0.000	0.000	0.000	0.000
146	A	147	ASN	0	0.015	0.004	17.677	-0.174	-0.174	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.052	-0.023	12.572	-0.384	-0.384	0.000	0.000	0.000	0.000
148	A	149	GLY	0	0.028	0.010	12.875	-1.320	-1.320	0.000	0.000	0.000	0.000
149	A	150	MET	0	-0.100	-0.035	10.926	-0.265	-0.265	0.000	0.000	0.000	0.000
150	A	151	GLU	-1	-0.897	-0.934	14.283	-13.682	-13.682	0.000	0.000	0.000	0.000
151	A	152	HIS	0	-0.043	-0.034	16.173	-0.615	-0.615	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.783	-0.862	15.119	-16.609	-16.609	0.000	0.000	0.000	0.000
153	A	154	GLY	0	0.022	-0.004	17.670	0.688	0.688	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.938	0.944	20.092	9.976	9.976	0.000	0.000	0.000	0.000
155	A	156	ASP	-1	-0.891	-0.948	23.004	-10.589	-10.589	0.000	0.000	0.000	0.000
156	A	157	CYS	0	-0.074	-0.018	15.869	-0.742	-0.742	0.000	0.000	0.000	0.000
157	A	158	LEU	0	0.019	0.006	19.153	0.312	0.312	0.000	0.000	0.000	0.000
158	A	159	ARG	1	0.804	0.865	9.731	20.969	20.969	0.000	0.000	0.000	0.000
159	A	160	GLY	0	0.027	0.016	16.673	-0.008	-0.008	0.000	0.000	0.000	0.000
160	A	161	ALA	0	0.008	-0.005	19.182	0.494	0.494	0.000	0.000	0.000	0.000
161	A	162	SER	0	-0.062	-0.027	17.640	0.820	0.820	0.000	0.000	0.000	0.000
162	A	163	LEU	0	-0.010	-0.003	19.283	-0.132	-0.132	0.000	0.000	0.000	0.000
163	A	165	ILE	0	-0.009	-0.002	15.321	0.661	0.661	0.000	0.000	0.000	0.000
164	A	166	MET	0	-0.024	0.026	14.677	0.528	0.528	0.000	0.000	0.000	0.000
165	A	167	ARG	1	0.898	0.971	17.495	12.186	12.186	0.000	0.000	0.000	0.000
166	A	168	PRO	0	-0.006	-0.018	20.503	0.241	0.241	0.000	0.000	0.000	0.000
167	A	169	GLY	0	-0.001	0.007	23.144	0.364	0.364	0.000	0.000	0.000	0.000
168	A	170	LEU	0	-0.031	-0.004	24.324	-0.159	-0.159	0.000	0.000	0.000	0.000
169	A	171	THR	0	0.001	0.009	25.119	0.424	0.424	0.000	0.000	0.000	0.000
170	A	172	PRO	0	0.005	0.006	25.834	-0.356	-0.356	0.000	0.000	0.000	0.000
171	A	173	GLY	0	0.043	0.012	25.864	0.056	0.056	0.000	0.000	0.000	0.000
172	A	174	ARG	1	0.935	0.957	25.742	10.300	10.300	0.000	0.000	0.000	0.000
173	A	175	SER	0	0.014	0.009	20.974	0.129	0.129	0.000	0.000	0.000	0.000
174	A	176	TYR	0	-0.032	-0.029	19.215	0.300	0.300	0.000	0.000	0.000	0.000
175	A	177	GLU	-1	-0.806	-0.877	13.935	-17.677	-17.677	0.000	0.000	0.000	0.000
176	A	178	PHE	0	0.008	-0.002	10.926	0.484	0.484	0.000	0.000	0.000	0.000
177	A	179	SER	0	0.022	-0.018	11.657	-0.893	-0.893	0.000	0.000	0.000	0.000
178	A	180	ASP	-1	-0.777	-0.883	7.819	-24.047	-24.047	0.000	0.000	0.000	0.000
179	A	181	ASP	-1	-0.869	-0.927	7.846	-20.654	-20.654	0.000	0.000	0.000	0.000
180	A	182	SER	0	-0.029	-0.031	10.179	-0.050	-0.050	0.000	0.000	0.000	0.000
182	A	184	GLY	0	0.006	0.008	6.155	-2.010	-2.010	0.000	0.000	0.000	0.000
183	A	185	TYR	0	-0.002	-0.017	7.152	-0.649	-0.649	0.000	0.000	0.000	0.000
184	A	186	TYR	0	0.078	0.041	7.056	0.882	0.882	0.000	0.000	0.000	0.000
186	A	188	LYS	1	0.884	0.956	6.777	18.012	18.012	0.000	0.000	0.000	0.000
187	A	189	PHE	0	0.011	0.019	10.092	0.565	0.565	0.000	0.000	0.000	0.000
188	A	190	LEU	0	-0.012	-0.014	7.253	0.412	0.412	0.000	0.000	0.000	0.000
189	A	191	ASN	0	-0.052	-0.040	6.444	0.437	0.437	0.000	0.000	0.000	0.000
190	A	192	GLN	0	-0.010	0.002	10.602	1.633	1.633	0.000	0.000	0.000	0.000
191	A	193	TYR	0	0.015	-0.001	14.186	1.258	1.258	0.000	0.000	0.000	0.000
192	A	194	LYS	1	0.834	0.940	10.275	27.543	27.543	0.000	0.000	0.000	0.000
193	A	195	PRO	0	0.013	0.006	12.931	0.754	0.754	0.000	0.000	0.000	0.000
194	A	196	GLN	0	0.041	-0.002	15.199	-0.290	-0.290	0.000	0.000	0.000	0.000
195	A	198	ILE	0	0.069	0.032	13.273	-0.105	-0.105	0.000	0.000	0.000	0.000
196	A	199	LEU	0	-0.019	-0.010	12.217	-1.929	-1.929	0.000	0.000	0.000	0.000
197	A	200	ASN	0	-0.071	-0.034	14.758	-0.255	-0.255	0.000	0.000	0.000	0.000
198	A	201	LYS	1	0.913	0.951	16.619	17.698	17.698	0.000	0.000	0.000	0.000
199	A	202	PRO	-1	-0.851	-0.889	18.206	-13.823	-13.823	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASN)