FMO DATABASE

FMODB ID: JQ169

Calculation Name: 1VSC-A-Xray372

Preferred Name: Vascular cell adhesion protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1VSC

Chain ID: A

ChEMBL ID: CHEMBL3735

UniProt ID: P19320

Base Structure: X-ray

Registration Date: 2023-09-24

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	195
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1918310.411673
FMO2-HF: Nuclear repulsion	1840713.675147
FMO2-HF: Total energy	-77596.736526
FMO2-MP2: Total energy	-77819.868075

3D Structure

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:PHE)

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

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.
-36.495	-15.579	23.538	-14.462	-29.989	-0.04

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.020 / q_NPA : 0.016

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	0.031	0.026	2.935	-5.845	-1.220	0.268	-2.311	-2.581	0.002
4	A	4	GLU	-1	-0.942	-0.974	4.971	-0.790	-0.716	-0.001	-0.007	-0.065	0.000
5	A	5	THR	0	-0.014	-0.019	8.441	-0.102	-0.102	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.018	0.047	11.288	0.058	0.058	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.022	0.005	14.922	-0.017	-0.017	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.853	-0.942	13.634	-0.436	-0.436	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.006	-0.013	14.642	-0.019	-0.019	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.879	0.932	16.895	0.176	0.176	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.000	-0.008	19.757	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.028	0.050	21.981	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.034	-0.031	24.761	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.009	0.021	26.712	0.013	0.013	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.030	-0.026	29.460	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.044	-0.023	29.920	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.865	-0.932	27.771	-0.142	-0.142	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.025	-0.027	25.426	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.004	-0.002	20.794	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.006	-0.011	18.571	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.031	0.005	14.885	0.004	0.004	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.007	-0.023	13.017	-0.035	-0.035	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.035	-0.002	7.337	-0.108	-0.108	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.060	0.035	7.450	0.063	0.063	0.000	0.000	0.000	0.000
25	A	25	THR	0	0.008	0.005	2.479	-1.143	0.016	0.658	-0.474	-1.344	0.000
26	A	26	THR	0	-0.003	0.002	3.676	0.569	0.964	0.001	-0.105	-0.291	0.000
27	A	27	GLY	0	-0.066	-0.055	2.409	-4.376	-2.493	2.193	-1.698	-2.377	-0.020
28	A	28	CYS	-1	-0.822	-0.895	2.485	-2.342	0.612	1.353	-1.502	-2.806	-0.014
29	A	29	GLU	-1	-0.999	-0.981	3.865	0.317	0.383	0.015	-0.016	-0.065	0.000
30	A	30	SER	0	-0.062	-0.043	7.315	-0.119	-0.119	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.066	0.038	4.466	-0.039	0.157	-0.001	-0.014	-0.181	0.000
32	A	32	PHE	0	-0.089	-0.048	5.752	0.150	0.150	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.015	-0.008	5.518	-0.349	-0.349	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.051	-0.023	7.787	0.176	0.176	0.000	0.000	0.000	0.000
35	A	35	TRP	0	0.020	0.010	9.830	-0.081	-0.081	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.895	0.943	11.863	0.422	0.422	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.014	0.005	15.090	-0.014	-0.014	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.094	0.032	17.330	-0.016	-0.016	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.064	-0.025	18.312	0.014	0.014	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.912	-0.954	16.321	-0.264	-0.264	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.003	0.016	19.097	0.019	0.019	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.033	-0.030	20.435	-0.020	-0.020	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.054	0.036	15.825	0.002	0.002	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.061	-0.011	20.011	0.007	0.007	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.107	0.062	20.739	0.005	0.005	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.875	0.936	19.908	0.216	0.216	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.021	0.005	13.464	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.087	-0.038	15.648	0.032	0.032	0.000	0.000	0.000	0.000
49	A	49	ASN	0	0.033	0.024	11.445	-0.055	-0.055	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.942	-0.973	13.001	-0.361	-0.361	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.050	0.032	11.901	-0.040	-0.040	0.000	0.000	0.000	0.000
52	A	52	THR	0	0.025	0.013	7.101	0.020	0.020	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.021	0.000	7.663	-0.271	-0.271	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.045	-0.014	9.862	0.125	0.125	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.033	-0.004	11.288	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.041	-0.010	14.577	0.027	0.027	0.000	0.000	0.000	0.000
57	A	57	THR	0	0.004	-0.003	16.322	0.015	0.015	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.055	-0.035	19.604	0.009	0.009	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.012	0.047	22.593	0.012	0.012	0.000	0.000	0.000	0.000
60	A	60	PRO	0	-0.030	-0.012	25.950	0.002	0.002	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.006	0.005	24.961	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	62	SER	0	0.057	0.006	26.409	0.015	0.015	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.133	0.048	27.041	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.072	-0.026	26.342	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.018	-0.048	22.117	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.822	-0.871	22.871	-0.145	-0.145	0.000	0.000	0.000	0.000
67	A	67	HIS	1	0.863	0.932	20.231	0.207	0.207	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.021	0.027	17.392	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.049	-0.049	15.176	0.008	0.008	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.010	-0.030	11.774	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.050	-0.038	6.050	0.047	0.047	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.036	0.018	2.430	-0.517	-0.182	1.227	-0.557	-1.004	0.002
73	A	74	THR	0	-0.070	-0.051	2.610	-4.171	-2.303	0.986	-1.017	-1.837	-0.014
74	A	75	CYS	-1	-0.736	-0.861	2.634	-2.372	-0.731	7.717	-2.661	-6.696	-0.014
75	A	76	GLU	-1	-0.872	-0.933	3.908	1.960	2.394	0.008	0.074	-0.516	0.000
76	A	77	SER	0	-0.118	-0.071	6.495	-0.316	-0.316	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.825	0.917	2.281	-10.170	-9.498	4.043	-1.439	-3.276	0.011
78	A	79	LYS	1	0.957	0.993	2.621	-2.341	-1.137	2.249	-1.130	-2.323	-0.014
79	A	80	LEU	0	-0.055	-0.013	2.724	-2.966	0.307	2.822	-1.607	-4.488	0.021
80	A	81	GLU	-1	-0.867	-0.941	4.002	-1.134	-0.997	0.000	0.002	-0.139	0.000
81	A	82	LYS	1	0.881	0.937	7.362	0.652	0.652	0.000	0.000	0.000	0.000
82	A	83	GLY	0	-0.008	0.007	9.603	-0.058	-0.058	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.002	0.015	13.023	0.013	0.013	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.008	-0.002	15.856	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.035	-0.027	18.999	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.852	-0.922	21.514	-0.141	-0.141	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.032	-0.020	25.168	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	89	TYR	0	0.032	0.017	27.997	0.005	0.005	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.030	-0.021	31.762	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	91	PHE	0	0.054	0.012	34.684	0.004	0.004	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.027	-0.007	37.365	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.909	0.962	38.950	0.074	0.074	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.894	-0.935	42.785	-0.067	-0.067	0.000	0.000	0.000	0.000
94	A	95	PRO	0	0.061	0.013	45.784	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.985	-0.993	47.730	-0.052	-0.052	0.000	0.000	0.000	0.000
96	A	97	ILE	0	0.002	-0.004	50.948	0.001	0.001	0.000	0.000	0.000	0.000
97	A	98	HIS	0	-0.037	-0.027	54.353	0.001	0.001	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.001	-0.001	57.049	0.001	0.001	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.037	-0.025	60.631	0.000	0.000	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.025	-0.001	62.649	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.041	-0.019	65.296	0.000	0.000	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.025	0.039	66.221	0.000	0.000	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.913	-0.969	68.178	-0.026	-0.026	0.000	0.000	0.000	0.000
104	A	105	ALA	0	-0.011	-0.017	71.175	0.000	0.000	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.006	0.006	71.620	0.001	0.001	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.924	0.973	70.216	0.028	0.028	0.000	0.000	0.000	0.000
107	A	108	PRO	0	-0.069	-0.040	67.524	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.023	-0.015	63.637	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	THR	0	0.013	-0.040	59.171	0.000	0.000	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.013	0.004	56.527	0.000	0.000	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.935	0.960	52.517	0.047	0.047	0.000	0.000	0.000	0.000
112	A	113	CYS	-1	-0.902	-0.992	51.008	-0.052	-0.052	0.000	0.000	0.000	0.000
113	A	114	SER	0	0.032	-0.025	48.659	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	VAL	0	0.068	0.027	43.694	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	116	ALA	0	-0.013	-0.002	43.560	0.000	0.000	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.904	-0.973	38.560	-0.083	-0.083	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.036	0.014	38.045	-0.005	-0.005	0.000	0.000	0.000	0.000
118	A	119	TYR	0	-0.114	-0.059	30.255	0.003	0.003	0.000	0.000	0.000	0.000
119	A	120	PRO	0	0.007	-0.003	32.966	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	121	PHE	0	0.070	0.008	35.321	0.002	0.002	0.000	0.000	0.000	0.000
121	A	122	ASP	-1	-0.849	-0.931	35.961	-0.083	-0.083	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.882	0.969	34.591	0.089	0.089	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.059	-0.038	38.145	0.000	0.000	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.914	-0.949	41.276	-0.053	-0.053	0.000	0.000	0.000	0.000
125	A	126	ILE	0	-0.020	-0.013	44.739	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	127	ASP	-1	-0.840	-0.937	47.512	-0.050	-0.050	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.013	0.005	50.568	0.000	0.000	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.017	-0.034	52.041	0.001	0.001	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.893	0.953	55.999	0.032	0.032	0.000	0.000	0.000	0.000
130	A	131	GLY	0	-0.022	-0.004	58.628	0.001	0.001	0.000	0.000	0.000	0.000
131	A	132	ASP	-1	-0.939	-0.971	56.629	-0.038	-0.038	0.000	0.000	0.000	0.000
132	A	133	HIS	0	-0.063	-0.043	57.326	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	LEU	0	0.038	0.031	51.949	0.000	0.000	0.000	0.000	0.000	0.000
134	A	135	MET	0	-0.102	-0.035	56.211	0.002	0.002	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.888	0.933	53.740	0.043	0.043	0.000	0.000	0.000	0.000
136	A	137	SER	0	0.066	0.051	49.805	0.000	0.000	0.000	0.000	0.000	0.000
137	A	138	GLN	0	-0.074	-0.033	48.088	0.003	0.003	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.869	-0.926	44.759	-0.057	-0.057	0.000	0.000	0.000	0.000
139	A	140	PHE	0	-0.028	-0.039	42.616	0.002	0.002	0.000	0.000	0.000	0.000
140	A	141	LEU	0	-0.004	-0.002	40.819	-0.004	-0.004	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.950	-0.964	41.217	-0.056	-0.056	0.000	0.000	0.000	0.000
142	A	143	ASP	-1	-0.896	-0.976	39.967	-0.068	-0.068	0.000	0.000	0.000	0.000
143	A	144	ALA	0	-0.097	-0.045	40.566	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-0.849	-0.925	38.880	-0.074	-0.074	0.000	0.000	0.000	0.000
145	A	146	ARG	1	0.909	0.946	32.252	0.092	0.092	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.785	0.889	28.213	0.131	0.131	0.000	0.000	0.000	0.000
147	A	148	SER	0	0.003	0.027	34.520	-0.003	-0.003	0.000	0.000	0.000	0.000
148	A	149	LEU	0	-0.037	-0.002	35.833	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	150	GLU	-1	-0.928	-0.958	38.548	-0.063	-0.063	0.000	0.000	0.000	0.000
150	A	151	THR	0	-0.024	-0.027	42.215	-0.002	-0.002	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.859	0.965	42.596	0.068	0.068	0.000	0.000	0.000	0.000
152	A	153	SER	0	-0.009	-0.002	45.938	0.001	0.001	0.000	0.000	0.000	0.000
153	A	154	LEU	0	0.022	0.037	49.527	0.000	0.000	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.911	-0.962	51.897	-0.042	-0.042	0.000	0.000	0.000	0.000
155	A	156	VAL	0	-0.018	-0.006	55.652	0.001	0.001	0.000	0.000	0.000	0.000
156	A	157	THR	0	0.022	0.029	58.570	0.000	0.000	0.000	0.000	0.000	0.000
157	A	158	PHE	0	-0.039	-0.014	62.291	0.000	0.000	0.000	0.000	0.000	0.000
158	A	159	THR	0	0.007	0.019	64.725	0.000	0.000	0.000	0.000	0.000	0.000
159	A	160	PRO	0	0.008	0.035	66.692	0.000	0.000	0.000	0.000	0.000	0.000
160	A	161	VAL	0	0.018	-0.014	68.172	0.001	0.001	0.000	0.000	0.000	0.000
161	A	162	ILE	0	0.041	-0.002	70.395	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	163	GLU	-1	-0.920	-0.962	69.900	-0.026	-0.026	0.000	0.000	0.000	0.000
163	A	164	ASP	-1	-0.856	-0.948	66.262	-0.031	-0.031	0.000	0.000	0.000	0.000
164	A	165	ILE	0	-0.030	-0.003	66.339	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	166	GLY	0	0.042	0.032	66.375	0.001	0.001	0.000	0.000	0.000	0.000
166	A	167	LYS	1	0.825	0.929	63.033	0.030	0.030	0.000	0.000	0.000	0.000
167	A	168	VAL	0	0.014	-0.006	57.629	0.000	0.000	0.000	0.000	0.000	0.000
168	A	169	LEU	0	-0.021	-0.001	57.725	0.000	0.000	0.000	0.000	0.000	0.000
169	A	170	VAL	0	-0.066	-0.058	52.540	-0.001	-0.001	0.000	0.000	0.000	0.000
170	A	171	CYS	-1	-0.854	-0.806	50.655	-0.052	-0.052	0.000	0.000	0.000	0.000
171	A	172	ARG	1	0.890	0.897	47.850	0.050	0.050	0.000	0.000	0.000	0.000
172	A	173	ALA	0	0.048	0.040	44.100	0.001	0.001	0.000	0.000	0.000	0.000
173	A	174	LYS	1	0.895	0.929	42.819	0.054	0.054	0.000	0.000	0.000	0.000
174	A	175	LEU	0	0.025	0.006	35.713	0.000	0.000	0.000	0.000	0.000	0.000
175	A	176	HIS	0	-0.016	0.002	37.531	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	177	ILE	0	-0.007	-0.016	32.105	-0.001	-0.001	0.000	0.000	0.000	0.000
177	A	178	ASP	-1	-0.890	-0.953	31.840	-0.114	-0.114	0.000	0.000	0.000	0.000
178	A	179	GLU	-1	-0.901	-0.952	30.900	-0.091	-0.091	0.000	0.000	0.000	0.000
179	A	180	MET	0	-0.165	-0.070	28.040	0.001	0.001	0.000	0.000	0.000	0.000
180	A	181	ASP	-1	-0.816	-0.900	33.016	-0.079	-0.079	0.000	0.000	0.000	0.000
181	A	182	SER	0	-0.077	-0.040	36.212	0.003	0.003	0.000	0.000	0.000	0.000
182	A	183	VAL	0	-0.115	-0.062	39.540	0.004	0.004	0.000	0.000	0.000	0.000
183	A	184	PRO	0	0.028	0.020	39.101	-0.003	-0.003	0.000	0.000	0.000	0.000
184	A	185	THR	0	0.015	0.004	37.130	-0.001	-0.001	0.000	0.000	0.000	0.000
185	A	186	VAL	0	-0.070	-0.039	39.574	0.003	0.003	0.000	0.000	0.000	0.000
186	A	187	ARG	1	0.864	0.961	39.388	0.078	0.078	0.000	0.000	0.000	0.000
187	A	188	GLN	0	0.037	0.009	44.813	0.002	0.002	0.000	0.000	0.000	0.000
188	A	189	ALA	0	0.029	0.047	48.534	-0.001	-0.001	0.000	0.000	0.000	0.000
189	A	190	VAL	0	-0.006	-0.013	51.506	0.001	0.001	0.000	0.000	0.000	0.000
190	A	191	LYS	1	0.915	0.966	55.130	0.038	0.038	0.000	0.000	0.000	0.000
191	A	192	GLU	-1	-0.889	-0.958	58.369	-0.034	-0.034	0.000	0.000	0.000	0.000
192	A	193	LEU	0	-0.051	-0.015	61.747	0.000	0.000	0.000	0.000	0.000	0.000
193	A	194	GLN	0	-0.015	-0.017	64.593	0.002	0.002	0.000	0.000	0.000	0.000
194	A	195	VAL	0	-0.014	-0.023	67.135	0.000	0.000	0.000	0.000	0.000	0.000
195	A	196	ASP	-1	-0.982	-0.971	70.704	-0.026	-0.026	0.000	0.000	0.000	0.000

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