FMO DATABASE

FMODB ID: MZGNZ

Calculation Name: 1VCA-A-Xray549

Preferred Name: Vascular cell adhesion protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VCA

Chain ID: A

ChEMBL ID: CHEMBL3735

UniProt ID: P19320

Base Structure: X-ray

Registration Date: 2025-10-11

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	196
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1961450.108148
FMO2-HF: Nuclear repulsion	1882726.892649
FMO2-HF: Total energy	-78723.215499
FMO2-MP2: Total energy	-78949.339103

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: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.
-191.905	-169.799	26.823	-17.739	-31.195	-0.124

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 : 1 / q_Mulliken : 0.766 / q_NPA : 0.877

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	0.021	0.012	3.532	-4.532	-1.821	0.030	-1.000	-1.740	0.000
4	A	4	GLU	-1	-0.950	-0.969	5.091	-28.236	-28.187	-0.001	-0.007	-0.042	0.000
25	A	25	THR	0	-0.019	-0.017	2.217	-4.901	-4.326	1.565	-0.474	-1.667	-0.005
26	A	26	THR	0	0.054	0.034	3.980	-0.632	-0.247	-0.001	-0.121	-0.264	0.000
27	A	27	GLY	0	-0.003	-0.012	2.228	-29.509	-27.344	6.161	-4.668	-3.658	-0.047
28	A	28	CYS	0	-0.051	-0.032	1.943	-39.548	-33.864	13.210	-7.077	-11.818	-0.052
29	A	29	GLU	-1	-0.897	-0.930	4.311	-23.800	-23.719	0.001	-0.056	-0.026	0.000
31	A	31	PRO	0	-0.049	-0.002	3.959	-0.159	0.075	0.000	-0.030	-0.204	0.000
72	A	73	ALA	0	0.024	0.020	2.879	0.172	0.919	0.228	-0.277	-0.698	-0.002
73	A	74	THR	0	-0.029	-0.023	2.601	-6.041	-3.936	0.782	-1.290	-1.597	-0.020
74	A	76	GLU	-1	-0.815	-0.907	4.369	-37.427	-37.093	0.007	-0.018	-0.324	0.001
76	A	78	ARG	1	0.852	0.926	2.629	47.118	49.608	0.980	-0.875	-2.596	-0.001
77	A	79	LYS	1	0.936	0.946	3.140	22.369	23.727	0.288	-0.412	-1.233	-0.004
78	A	80	LEU	0	-0.030	-0.001	2.536	-3.736	-0.727	3.573	-1.435	-5.147	0.006
79	A	81	GLU	-1	-0.832	-0.915	3.973	-21.011	-20.832	0.000	0.001	-0.181	0.000
5	A	5	THR	0	0.011	-0.011	8.481	-0.478	-0.478	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.000	0.046	11.251	0.447	0.447	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.031	0.011	14.803	0.251	0.251	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.836	-0.907	14.518	-21.324	-21.324	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.001	-0.023	14.641	-0.686	-0.686	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.759	0.842	17.028	11.653	11.653	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.009	-0.008	20.115	-0.390	-0.390	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.059	0.038	21.989	0.149	0.149	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.061	-0.039	24.211	0.009	0.009	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.017	0.005	26.261	0.420	0.420	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.029	-0.028	29.299	-0.152	-0.152	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.038	-0.019	30.679	0.247	0.247	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.846	-0.902	28.533	-9.447	-9.447	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.063	-0.036	25.782	-0.319	-0.319	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.032	0.017	21.319	-0.109	-0.109	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.032	-0.021	18.387	-0.055	-0.055	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.013	0.033	15.061	-0.091	-0.091	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.026	-0.032	12.867	-0.567	-0.567	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.034	0.010	7.729	-1.451	-1.451	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.043	0.032	7.496	0.710	0.710	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.005	-0.017	7.409	3.952	3.952	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.002	0.003	5.609	2.855	2.855	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.010	-0.006	5.553	-2.414	-2.414	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.031	-0.011	7.972	2.230	2.230	0.000	0.000	0.000	0.000
35	A	35	TRP	0	0.039	-0.001	9.808	-1.123	-1.123	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.846	0.925	10.473	18.801	18.801	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.048	0.014	14.980	-0.423	-0.423	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.001	-0.021	17.436	-0.173	-0.173	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.047	-0.013	18.594	0.230	0.230	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.918	-0.952	17.024	-13.543	-13.543	0.000	0.000	0.000	0.000
41	A	41	SER	0	0.002	0.021	19.609	0.350	0.350	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.020	-0.019	20.444	-0.454	-0.454	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.028	0.012	16.337	0.092	0.092	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.055	-0.021	20.452	0.098	0.098	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.076	0.041	20.968	0.159	0.159	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.887	0.959	19.890	12.363	12.363	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.060	0.029	14.067	-0.254	-0.254	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.085	-0.054	15.349	0.930	0.930	0.000	0.000	0.000	0.000
49	A	49	ASN	0	-0.002	0.017	11.111	-0.614	-0.614	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.911	-0.957	12.055	-15.078	-15.078	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.018	0.016	11.852	-0.859	-0.859	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.036	-0.024	7.342	-0.152	-0.152	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.005	-0.025	7.592	-2.114	-2.114	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.013	-0.001	9.545	1.321	1.321	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.015	0.001	11.029	-0.190	-0.190	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.014	0.003	14.367	0.341	0.341	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.007	-0.015	16.516	0.066	0.066	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.037	-0.011	20.139	0.224	0.224	0.000	0.000	0.000	0.000
59	A	59	ASN	0	0.000	0.010	22.966	0.304	0.304	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.001	0.009	26.288	0.057	0.057	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.007	-0.005	24.852	-0.168	-0.168	0.000	0.000	0.000	0.000
62	A	62	SER	0	0.003	-0.009	27.299	0.475	0.475	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.081	0.011	28.084	-0.265	-0.265	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.033	0.001	27.286	-0.081	-0.081	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.007	-0.025	22.846	0.047	0.047	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.806	-0.867	23.536	-10.109	-10.109	0.000	0.000	0.000	0.000
67	A	67	HIS	0	-0.001	0.002	20.217	-0.154	-0.154	0.000	0.000	0.000	0.000
68	A	68	SER	0	-0.005	0.004	18.157	-0.526	-0.526	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.016	-0.015	15.668	0.078	0.078	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.013	-0.011	11.990	-0.604	-0.604	0.000	0.000	0.000	0.000
71	A	72	THR	0	0.001	-0.022	6.015	-0.391	-0.391	0.000	0.000	0.000	0.000
75	A	77	SER	0	-0.010	-0.003	7.222	0.583	0.583	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.819	0.904	6.963	22.081	22.081	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.021	0.020	9.933	0.424	0.424	0.000	0.000	0.000	0.000
82	A	84	ILE	0	-0.027	-0.021	13.004	-0.350	-0.350	0.000	0.000	0.000	0.000
83	A	85	GLN	0	-0.017	-0.010	16.109	0.742	0.742	0.000	0.000	0.000	0.000
84	A	86	VAL	0	-0.019	-0.015	19.557	-0.058	-0.058	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.770	-0.839	22.007	-10.972	-10.972	0.000	0.000	0.000	0.000
86	A	88	ILE	0	-0.050	-0.020	25.573	-0.065	-0.065	0.000	0.000	0.000	0.000
87	A	89	TYR	0	0.022	0.005	28.189	0.348	0.348	0.000	0.000	0.000	0.000
88	A	90	SER	0	-0.042	-0.041	31.608	-0.153	-0.153	0.000	0.000	0.000	0.000
89	A	91	PHE	0	0.027	0.011	34.356	0.245	0.245	0.000	0.000	0.000	0.000
90	A	92	PRO	0	0.058	0.042	36.120	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.832	0.903	37.172	7.166	7.166	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.842	-0.904	40.768	-7.378	-7.378	0.000	0.000	0.000	0.000
93	A	95	PRO	0	-0.040	-0.024	43.297	0.080	0.080	0.000	0.000	0.000	0.000
94	A	96	GLU	-1	-0.931	-0.954	46.270	-6.171	-6.171	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.041	-0.032	49.401	0.048	0.048	0.000	0.000	0.000	0.000
96	A	98	HIS	0	-0.029	-0.016	51.309	0.176	0.176	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.008	-0.016	55.803	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	100	SER	0	0.014	0.009	59.445	0.001	0.001	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.007	0.006	62.608	0.086	0.086	0.000	0.000	0.000	0.000
100	A	102	PRO	0	0.002	0.005	63.281	-0.088	-0.088	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.033	0.010	61.383	0.029	0.029	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.811	-0.877	65.679	-4.337	-4.337	0.000	0.000	0.000	0.000
103	A	105	ALA	0	-0.006	-0.010	69.299	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	106	GLY	0	-0.034	-0.017	70.546	0.066	0.066	0.000	0.000	0.000	0.000
105	A	107	LYS	1	0.813	0.899	70.355	4.344	4.344	0.000	0.000	0.000	0.000
106	A	108	PRO	0	-0.015	-0.007	67.216	-0.058	-0.058	0.000	0.000	0.000	0.000
107	A	109	ILE	0	-0.022	-0.007	62.237	0.010	0.010	0.000	0.000	0.000	0.000
108	A	110	THR	0	-0.015	-0.026	59.776	-0.016	-0.016	0.000	0.000	0.000	0.000
109	A	111	VAL	0	-0.016	-0.015	55.631	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.899	0.939	53.196	5.619	5.619	0.000	0.000	0.000	0.000
111	A	113	CYS	0	-0.084	-0.012	49.285	-0.013	-0.013	0.000	0.000	0.000	0.000
112	A	114	SER	0	0.002	-0.009	48.771	0.048	0.048	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.037	0.016	42.297	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.025	0.008	43.530	0.042	0.042	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.863	-0.923	38.695	-7.410	-7.410	0.000	0.000	0.000	0.000
116	A	118	VAL	0	0.028	0.019	38.074	-0.242	-0.242	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.004	0.015	31.732	0.179	0.179	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.034	0.019	33.345	-0.176	-0.176	0.000	0.000	0.000	0.000
119	A	121	PHE	0	0.058	-0.009	36.254	0.034	0.034	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.849	-0.920	37.766	-7.814	-7.814	0.000	0.000	0.000	0.000
121	A	123	ARG	1	0.860	0.930	35.518	8.118	8.118	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.036	0.000	38.936	-0.034	-0.034	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.795	-0.892	41.493	-6.810	-6.810	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.053	-0.028	44.240	-0.063	-0.063	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.754	-0.851	46.864	-6.456	-6.456	0.000	0.000	0.000	0.000
126	A	128	LEU	0	-0.005	-0.019	49.311	-0.021	-0.021	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.023	-0.011	50.149	0.070	0.070	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.847	0.914	54.183	5.126	5.126	0.000	0.000	0.000	0.000
129	A	131	GLY	0	-0.017	-0.008	56.842	0.087	0.087	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.932	-0.969	53.761	-5.929	-5.929	0.000	0.000	0.000	0.000
131	A	133	HIS	0	-0.035	-0.015	54.656	-0.038	-0.038	0.000	0.000	0.000	0.000
132	A	134	LEU	0	-0.014	-0.008	51.426	0.016	0.016	0.000	0.000	0.000	0.000
133	A	135	MET	0	-0.043	-0.017	54.851	0.128	0.128	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.875	0.933	53.794	5.693	5.693	0.000	0.000	0.000	0.000
135	A	137	SER	0	0.004	-0.012	48.756	-0.082	-0.082	0.000	0.000	0.000	0.000
136	A	138	GLN	0	-0.073	-0.037	49.252	0.250	0.250	0.000	0.000	0.000	0.000
137	A	139	GLU	-1	-0.870	-0.919	45.416	-6.887	-6.887	0.000	0.000	0.000	0.000
138	A	140	PHE	0	-0.028	-0.045	44.207	0.208	0.208	0.000	0.000	0.000	0.000
139	A	141	LEU	0	0.015	0.017	43.481	-0.068	-0.068	0.000	0.000	0.000	0.000
140	A	142	GLU	-1	-0.981	-0.986	44.423	-6.524	-6.524	0.000	0.000	0.000	0.000
141	A	143	ASP	-1	-0.916	-0.965	40.663	-7.285	-7.285	0.000	0.000	0.000	0.000
142	A	144	ALA	0	-0.025	-0.005	38.612	0.103	0.103	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.920	-0.955	39.350	-7.120	-7.120	0.000	0.000	0.000	0.000
144	A	146	ARG	1	0.883	0.932	36.919	7.393	7.393	0.000	0.000	0.000	0.000
145	A	147	LYS	1	0.810	0.889	30.699	9.106	9.106	0.000	0.000	0.000	0.000
146	A	148	SER	0	-0.032	-0.045	35.782	-0.068	-0.068	0.000	0.000	0.000	0.000
147	A	149	LEU	0	-0.030	-0.015	35.067	-0.098	-0.098	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.851	-0.892	38.801	-6.788	-6.788	0.000	0.000	0.000	0.000
149	A	151	THR	0	-0.047	-0.025	42.098	-0.051	-0.051	0.000	0.000	0.000	0.000
150	A	152	LYS	1	0.888	0.973	44.101	6.771	6.771	0.000	0.000	0.000	0.000
151	A	153	SER	0	0.004	-0.011	46.619	-0.006	-0.006	0.000	0.000	0.000	0.000
152	A	154	LEU	0	-0.014	0.014	49.594	0.048	0.048	0.000	0.000	0.000	0.000
153	A	155	GLU	-1	-0.837	-0.912	51.985	-5.403	-5.403	0.000	0.000	0.000	0.000
154	A	156	VAL	0	-0.017	-0.014	55.745	0.000	0.000	0.000	0.000	0.000	0.000
155	A	157	THR	0	0.009	0.016	58.525	0.029	0.029	0.000	0.000	0.000	0.000
156	A	158	PHE	0	0.007	0.005	60.555	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	159	THR	0	0.004	0.011	63.911	0.063	0.063	0.000	0.000	0.000	0.000
158	A	160	PRO	0	-0.009	0.010	64.957	-0.031	-0.031	0.000	0.000	0.000	0.000
159	A	161	VAL	0	0.021	0.013	66.638	0.091	0.091	0.000	0.000	0.000	0.000
160	A	162	ILE	0	0.063	0.027	67.845	-0.049	-0.049	0.000	0.000	0.000	0.000
161	A	163	GLU	-1	-0.885	-0.950	67.616	-4.589	-4.589	0.000	0.000	0.000	0.000
162	A	164	ASP	-1	-0.819	-0.923	63.580	-5.076	-5.076	0.000	0.000	0.000	0.000
163	A	165	ILE	0	-0.020	0.000	63.170	-0.090	-0.090	0.000	0.000	0.000	0.000
164	A	166	GLY	0	-0.013	-0.004	61.825	0.000	0.000	0.000	0.000	0.000	0.000
165	A	167	LYS	1	0.844	0.940	59.466	4.961	4.961	0.000	0.000	0.000	0.000
166	A	168	VAL	0	0.032	0.014	53.896	0.020	0.020	0.000	0.000	0.000	0.000
167	A	169	LEU	0	-0.005	-0.003	55.272	0.020	0.020	0.000	0.000	0.000	0.000
168	A	170	VAL	0	0.005	-0.007	50.163	-0.065	-0.065	0.000	0.000	0.000	0.000
169	A	172	ARG	1	0.898	0.925	44.954	6.548	6.548	0.000	0.000	0.000	0.000
170	A	173	ALA	0	0.004	0.012	42.890	0.070	0.070	0.000	0.000	0.000	0.000
171	A	174	LYS	1	0.829	0.909	40.561	6.768	6.768	0.000	0.000	0.000	0.000
172	A	175	LEU	0	0.016	0.009	35.148	0.126	0.126	0.000	0.000	0.000	0.000
173	A	176	HIS	0	-0.026	-0.025	36.210	-0.400	-0.400	0.000	0.000	0.000	0.000
174	A	177	ILE	0	-0.019	-0.014	31.152	-0.018	-0.018	0.000	0.000	0.000	0.000
175	A	178	ASP	-1	-0.877	-0.939	29.013	-9.864	-9.864	0.000	0.000	0.000	0.000
176	A	179	GLU	-1	-0.838	-0.867	29.507	-9.169	-9.169	0.000	0.000	0.000	0.000
177	A	180	MET	0	-0.036	-0.023	24.673	-0.630	-0.630	0.000	0.000	0.000	0.000
178	A	181	ASP	-1	-0.911	-0.951	27.984	-9.583	-9.583	0.000	0.000	0.000	0.000
179	A	182	SER	0	-0.057	-0.040	28.006	-0.407	-0.407	0.000	0.000	0.000	0.000
180	A	183	VAL	0	-0.039	0.003	28.745	0.211	0.211	0.000	0.000	0.000	0.000
181	A	184	PRO	0	-0.030	-0.017	31.372	-0.029	-0.029	0.000	0.000	0.000	0.000
182	A	185	THR	0	0.033	-0.011	34.827	0.050	0.050	0.000	0.000	0.000	0.000
183	A	186	VAL	0	-0.060	-0.031	36.408	0.236	0.236	0.000	0.000	0.000	0.000
184	A	187	ARG	1	0.836	0.922	36.882	7.796	7.796	0.000	0.000	0.000	0.000
185	A	188	GLN	0	-0.033	-0.035	41.562	0.134	0.134	0.000	0.000	0.000	0.000
186	A	189	ALA	0	0.009	0.029	45.295	-0.039	-0.039	0.000	0.000	0.000	0.000
187	A	190	VAL	0	0.016	-0.009	48.266	0.066	0.066	0.000	0.000	0.000	0.000
188	A	191	LYS	1	0.907	0.957	51.504	5.655	5.655	0.000	0.000	0.000	0.000
189	A	192	GLU	-1	-0.901	-0.943	55.181	-5.543	-5.543	0.000	0.000	0.000	0.000
190	A	193	LEU	0	-0.044	-0.024	57.867	0.057	0.057	0.000	0.000	0.000	0.000
191	A	194	GLN	0	0.022	0.012	61.082	0.085	0.085	0.000	0.000	0.000	0.000
192	A	195	VAL	0	-0.045	-0.023	64.113	-0.014	-0.014	0.000	0.000	0.000	0.000
193	A	196	TYR	0	-0.014	-0.008	66.095	0.058	0.058	0.000	0.000	0.000	0.000
194	A	197	ILE	0	0.012	-0.003	70.137	-0.005	-0.005	0.000	0.000	0.000	0.000
195	A	198	SER	0	-0.016	-0.031	73.653	0.006	0.006	0.000	0.000	0.000	0.000
196	A	199	PRO	-1	-0.970	-0.964	76.006	-3.942	-3.942	0.000	0.000	0.000	0.000

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