FMO DATABASE

FMODB ID: GVK21

Calculation Name: 5ZW3-B-Xray547

Preferred Name:

Target Type:

Ligand Name: s-adenosyl-l-homocysteine | magnesium ion

Ligand 3-letter code: SAH | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5ZW3

Chain ID: B

ChEMBL ID:

UniProt ID: O32036

Base Structure: X-ray

Registration Date: 2025-10-06

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	193
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2277390.094186
FMO2-HF: Nuclear repulsion	2199897.358943
FMO2-HF: Total energy	-77492.735243
FMO2-MP2: Total energy	-77720.885686

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:3:ASP)

Summations of interaction energy for fragment #1(A:3:ASP)

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.
-27.286	-24.321	15.641	-7.935	-10.672	0.075

Interaction energy analysis for fragmet #1(A:3:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : -0.004

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	5	TYR	0	0.000	-0.006	1.944	-15.982	-13.619	8.545	-5.116	-5.793	0.049
4	A	6	GLU	-1	-0.836	-0.919	2.013	-12.898	-13.037	7.079	-2.657	-4.284	0.025
5	A	7	GLN	0	0.015	0.021	3.590	-3.371	-2.757	0.018	-0.155	-0.477	0.001
6	A	8	ILE	0	-0.054	-0.033	5.163	0.020	0.147	-0.001	-0.007	-0.118	0.000
7	A	9	ASN	0	0.027	0.014	6.765	-0.284	-0.284	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.856	-0.930	6.422	-5.465	-5.465	0.000	0.000	0.000	0.000
9	A	11	TYR	0	-0.103	-0.055	9.212	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	12	ILE	0	0.003	-0.005	11.109	0.060	0.060	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.796	-0.896	12.042	0.262	0.262	0.000	0.000	0.000	0.000
12	A	14	ALA	0	-0.068	-0.030	13.247	-0.065	-0.065	0.000	0.000	0.000	0.000
13	A	15	LEU	0	-0.065	-0.029	14.949	-0.010	-0.010	0.000	0.000	0.000	0.000
14	A	16	LEU	0	-0.025	0.008	15.989	0.093	0.093	0.000	0.000	0.000	0.000
15	A	17	LYS	1	0.955	0.985	18.941	-0.254	-0.254	0.000	0.000	0.000	0.000
16	A	18	PRO	0	-0.020	-0.006	21.957	0.056	0.056	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.847	0.889	19.110	-0.142	-0.142	0.000	0.000	0.000	0.000
18	A	20	PRO	0	0.026	-0.005	24.782	-0.064	-0.064	0.000	0.000	0.000	0.000
19	A	21	ASP	-1	-0.861	-0.946	26.926	-0.102	-0.102	0.000	0.000	0.000	0.000
20	A	22	ASN	0	-0.015	-0.003	28.084	-0.021	-0.021	0.000	0.000	0.000	0.000
21	A	23	VAL	0	0.038	0.022	23.744	0.017	0.017	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.870	0.947	22.769	0.132	0.132	0.000	0.000	0.000	0.000
23	A	25	ARG	1	0.936	0.974	23.828	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.009	0.022	24.867	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.733	-0.827	19.852	0.254	0.254	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.032	0.012	20.613	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	29	TYR	0	0.000	0.005	22.255	-0.023	-0.023	0.000	0.000	0.000	0.000
28	A	30	ALA	0	-0.012	-0.019	20.525	0.001	0.001	0.000	0.000	0.000	0.000
29	A	31	GLU	-1	-0.940	-0.960	16.810	-0.388	-0.388	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.930	-0.957	19.308	-0.283	-0.283	0.000	0.000	0.000	0.000
31	A	33	HIS	0	-0.118	-0.059	22.211	-0.029	-0.029	0.000	0.000	0.000	0.000
32	A	34	HIS	0	-0.089	-0.043	19.130	0.026	0.026	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.066	-0.034	20.353	0.098	0.098	0.000	0.000	0.000	0.000
34	A	36	PRO	0	-0.007	0.003	17.676	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	37	ILE	0	-0.029	-0.020	18.423	0.003	0.003	0.000	0.000	0.000	0.000
36	A	38	MET	0	0.022	0.021	17.193	0.094	0.094	0.000	0.000	0.000	0.000
37	A	39	GLU	-1	-0.819	-0.908	11.701	1.325	1.325	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.853	0.925	14.272	-0.145	-0.145	0.000	0.000	0.000	0.000
39	A	41	ALA	0	0.025	0.003	12.189	-0.091	-0.091	0.000	0.000	0.000	0.000
40	A	42	GLY	0	0.035	0.015	14.274	0.056	0.056	0.000	0.000	0.000	0.000
41	A	43	MET	0	-0.018	-0.002	15.683	-0.158	-0.158	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.846	-0.913	17.863	0.502	0.502	0.000	0.000	0.000	0.000
43	A	45	VAL	0	-0.021	-0.004	16.258	-0.083	-0.083	0.000	0.000	0.000	0.000
44	A	46	LEU	0	0.010	0.008	19.208	-0.084	-0.084	0.000	0.000	0.000	0.000
45	A	47	LEU	0	0.000	-0.004	21.555	-0.098	-0.098	0.000	0.000	0.000	0.000
46	A	48	GLN	0	0.024	0.014	22.336	-0.095	-0.095	0.000	0.000	0.000	0.000
47	A	49	ILE	0	-0.034	-0.023	20.783	-0.056	-0.056	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.010	-0.014	24.803	-0.068	-0.068	0.000	0.000	0.000	0.000
49	A	51	SER	0	-0.017	-0.027	27.127	-0.066	-0.066	0.000	0.000	0.000	0.000
50	A	52	VAL	0	-0.067	-0.021	27.179	-0.051	-0.051	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.823	0.912	29.059	-0.649	-0.649	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.082	-0.044	30.745	-0.056	-0.056	0.000	0.000	0.000	0.000
53	A	55	PRO	0	-0.027	-0.002	30.506	-0.025	-0.025	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.941	0.954	33.743	-0.378	-0.378	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.831	0.920	35.963	-0.427	-0.427	0.000	0.000	0.000	0.000
56	A	58	ILE	0	0.002	0.000	29.230	0.029	0.029	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.003	0.010	31.651	-0.040	-0.040	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.753	-0.833	26.451	0.727	0.727	0.000	0.000	0.000	0.000
59	A	61	ILE	0	-0.027	-0.017	27.619	-0.060	-0.060	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.030	0.011	25.599	0.082	0.082	0.000	0.000	0.000	0.000
61	A	63	THR	0	-0.022	-0.025	25.567	0.014	0.014	0.000	0.000	0.000	0.000
62	A	64	ALA	0	0.016	0.008	24.100	-0.018	-0.018	0.000	0.000	0.000	0.000
63	A	65	ILE	0	-0.015	-0.007	24.072	-0.048	-0.048	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.054	0.014	27.230	-0.051	-0.051	0.000	0.000	0.000	0.000
65	A	67	TYR	0	-0.051	-0.036	20.239	0.011	0.011	0.000	0.000	0.000	0.000
66	A	68	SER	0	0.046	-0.004	22.957	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	69	ALA	0	0.024	0.013	24.522	-0.017	-0.017	0.000	0.000	0.000	0.000
68	A	70	ILE	0	0.010	0.004	27.823	-0.024	-0.024	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.785	0.864	20.708	-0.585	-0.585	0.000	0.000	0.000	0.000
70	A	72	MET	0	-0.001	0.000	25.741	0.006	0.006	0.000	0.000	0.000	0.000
71	A	73	ALA	0	0.015	0.011	27.894	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	74	LEU	0	-0.064	-0.027	28.597	-0.046	-0.046	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.889	-0.917	27.214	0.464	0.464	0.000	0.000	0.000	0.000
74	A	76	LEU	0	-0.018	-0.004	29.584	-0.013	-0.013	0.000	0.000	0.000	0.000
75	A	77	PRO	0	-0.011	-0.013	32.582	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.052	-0.031	35.676	-0.023	-0.023	0.000	0.000	0.000	0.000
77	A	79	ALA	0	-0.026	0.010	33.776	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.807	-0.867	35.832	0.304	0.304	0.000	0.000	0.000	0.000
79	A	81	ILE	0	-0.038	-0.021	30.003	0.037	0.037	0.000	0.000	0.000	0.000
80	A	82	TYR	0	-0.037	-0.036	33.654	-0.035	-0.035	0.000	0.000	0.000	0.000
81	A	83	THR	0	-0.025	-0.042	29.345	0.041	0.041	0.000	0.000	0.000	0.000
82	A	84	ILE	0	0.020	0.025	30.822	-0.042	-0.042	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.804	-0.893	27.693	0.601	0.601	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.905	0.933	28.001	-0.622	-0.622	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.057	-0.033	29.517	-0.049	-0.049	0.000	0.000	0.000	0.000
86	A	88	GLU	-1	-0.878	-0.940	31.490	0.220	0.220	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.837	0.906	30.680	-0.155	-0.155	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.944	0.978	23.469	-0.533	-0.533	0.000	0.000	0.000	0.000
89	A	91	HIS	0	0.074	0.033	30.002	0.008	0.008	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.918	-0.953	32.879	0.144	0.144	0.000	0.000	0.000	0.000
91	A	93	GLU	-1	-0.862	-0.926	29.608	0.131	0.131	0.000	0.000	0.000	0.000
92	A	94	ALA	0	-0.020	0.003	30.066	-0.008	-0.008	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.012	0.000	31.299	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	96	ASN	0	-0.074	-0.041	34.468	-0.026	-0.026	0.000	0.000	0.000	0.000
95	A	97	ASN	0	0.027	0.007	29.231	-0.046	-0.046	0.000	0.000	0.000	0.000
96	A	98	ILE	0	-0.004	-0.006	31.754	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	99	LYS	1	0.968	0.998	33.765	-0.138	-0.138	0.000	0.000	0.000	0.000
98	A	100	GLU	-1	-1.005	-1.004	33.978	0.063	0.063	0.000	0.000	0.000	0.000
99	A	101	PHE	0	-0.086	-0.066	28.622	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	102	GLN	0	-0.086	-0.032	34.494	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.019	0.015	32.372	0.008	0.008	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.881	-0.945	36.309	0.222	0.222	0.000	0.000	0.000	0.000
103	A	105	ASP	-1	-0.934	-0.973	38.254	0.245	0.245	0.000	0.000	0.000	0.000
104	A	106	ARG	1	0.792	0.890	34.527	-0.307	-0.307	0.000	0.000	0.000	0.000
105	A	107	ILE	0	-0.020	-0.002	31.504	0.031	0.031	0.000	0.000	0.000	0.000
106	A	108	HIS	1	0.768	0.874	35.284	-0.338	-0.338	0.000	0.000	0.000	0.000
107	A	109	VAL	0	0.027	0.012	33.087	0.030	0.030	0.000	0.000	0.000	0.000
108	A	110	PHE	0	-0.020	-0.005	34.988	-0.028	-0.028	0.000	0.000	0.000	0.000
109	A	111	TYR	0	-0.016	-0.007	34.687	0.029	0.029	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.034	0.003	34.838	-0.018	-0.018	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.799	-0.904	32.562	0.599	0.599	0.000	0.000	0.000	0.000
112	A	114	ALA	0	0.034	0.028	31.216	-0.017	-0.017	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.043	-0.031	31.609	0.001	0.001	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.985	-0.988	34.810	0.378	0.378	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.031	-0.009	35.360	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	118	ALA	0	0.036	0.028	37.802	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	119	ASP	-1	-0.893	-0.959	38.690	0.368	0.368	0.000	0.000	0.000	0.000
118	A	120	ALA	0	-0.044	-0.030	40.640	-0.011	-0.011	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.012	0.019	35.648	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	122	HIS	0	0.048	0.019	38.955	0.019	0.019	0.000	0.000	0.000	0.000
121	A	123	VAL	0	-0.067	-0.025	41.111	-0.010	-0.010	0.000	0.000	0.000	0.000
122	A	124	THR	0	-0.011	-0.007	39.220	-0.019	-0.019	0.000	0.000	0.000	0.000
123	A	125	ALA	0	0.030	0.050	39.064	0.017	0.017	0.000	0.000	0.000	0.000
124	A	126	PRO	0	-0.086	-0.053	38.390	-0.028	-0.028	0.000	0.000	0.000	0.000
125	A	127	TYR	0	-0.010	-0.015	33.893	-0.018	-0.018	0.000	0.000	0.000	0.000
126	A	128	ASP	-1	-0.829	-0.898	34.026	0.517	0.517	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.008	-0.019	27.510	0.034	0.034	0.000	0.000	0.000	0.000
128	A	130	ILE	0	0.003	0.016	28.689	-0.048	-0.048	0.000	0.000	0.000	0.000
129	A	131	PHE	0	-0.011	-0.010	21.059	0.066	0.066	0.000	0.000	0.000	0.000
130	A	132	ILE	0	-0.034	-0.022	24.087	-0.087	-0.087	0.000	0.000	0.000	0.000
131	A	133	ASP	-1	-0.846	-0.928	20.152	1.441	1.441	0.000	0.000	0.000	0.000
132	A	134	ALA	0	0.073	0.024	22.431	-0.126	-0.126	0.000	0.000	0.000	0.000
133	A	135	ALA	0	-0.050	-0.031	22.309	0.087	0.087	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.878	0.925	16.144	-2.150	-2.150	0.000	0.000	0.000	0.000
135	A	137	GLY	0	-0.051	-0.020	21.904	0.039	0.039	0.000	0.000	0.000	0.000
136	A	138	GLN	0	-0.017	-0.012	24.419	-0.082	-0.082	0.000	0.000	0.000	0.000
137	A	139	TYR	0	0.004	-0.004	20.031	-0.142	-0.142	0.000	0.000	0.000	0.000
138	A	140	GLN	0	-0.005	-0.002	25.602	-0.080	-0.080	0.000	0.000	0.000	0.000
139	A	141	ASN	0	-0.029	-0.017	27.945	-0.050	-0.050	0.000	0.000	0.000	0.000
140	A	142	PHE	0	0.009	-0.004	26.179	-0.048	-0.048	0.000	0.000	0.000	0.000
141	A	143	PHE	0	0.042	0.014	26.720	-0.043	-0.043	0.000	0.000	0.000	0.000
142	A	144	HIS	0	-0.031	-0.021	29.653	-0.021	-0.021	0.000	0.000	0.000	0.000
143	A	145	LEU	0	-0.045	-0.006	32.905	-0.039	-0.039	0.000	0.000	0.000	0.000
144	A	146	TYR	0	-0.006	-0.041	32.005	-0.044	-0.044	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.859	-0.903	31.746	0.631	0.631	0.000	0.000	0.000	0.000
146	A	148	PRO	0	-0.010	0.000	33.496	-0.021	-0.021	0.000	0.000	0.000	0.000
147	A	149	MET	0	-0.065	-0.006	36.022	-0.035	-0.035	0.000	0.000	0.000	0.000
148	A	150	LEU	0	-0.034	0.001	31.385	-0.011	-0.011	0.000	0.000	0.000	0.000
149	A	151	SER	0	-0.027	-0.045	35.112	-0.026	-0.026	0.000	0.000	0.000	0.000
150	A	152	PRO	0	-0.015	-0.015	35.635	0.033	0.033	0.000	0.000	0.000	0.000
151	A	153	ASP	-1	-0.845	-0.916	34.633	0.583	0.583	0.000	0.000	0.000	0.000
152	A	154	GLY	0	-0.019	-0.004	32.890	0.010	0.010	0.000	0.000	0.000	0.000
153	A	155	VAL	0	-0.066	-0.038	26.337	0.021	0.021	0.000	0.000	0.000	0.000
154	A	156	ILE	0	0.011	0.012	25.882	-0.030	-0.030	0.000	0.000	0.000	0.000
155	A	157	ILE	0	-0.011	-0.010	21.498	0.073	0.073	0.000	0.000	0.000	0.000
156	A	158	THR	0	-0.020	-0.003	20.610	-0.124	-0.124	0.000	0.000	0.000	0.000
157	A	159	ASP	-1	-0.774	-0.885	16.212	2.401	2.401	0.000	0.000	0.000	0.000
158	A	160	ASN	0	-0.073	-0.015	15.620	-0.143	-0.143	0.000	0.000	0.000	0.000
159	A	161	VAL	0	-0.036	-0.025	15.664	-0.178	-0.178	0.000	0.000	0.000	0.000
160	A	162	LEU	0	-0.084	-0.034	10.395	0.043	0.043	0.000	0.000	0.000	0.000
161	A	163	PHE	-1	-0.797	-0.875	6.900	3.291	3.291	0.000	0.000	0.000	0.000
162	A	186	ILE	0	0.036	0.008	16.527	-0.072	-0.072	0.000	0.000	0.000	0.000
163	A	187	ASP	-1	-0.866	-0.935	17.501	2.112	2.112	0.000	0.000	0.000	0.000
164	A	188	GLU	-1	-0.910	-0.950	19.466	0.958	0.958	0.000	0.000	0.000	0.000
165	A	189	TYR	0	-0.008	-0.013	21.249	-0.124	-0.124	0.000	0.000	0.000	0.000
166	A	190	ASN	0	0.019	-0.006	16.668	-0.192	-0.192	0.000	0.000	0.000	0.000
167	A	191	HIS	0	-0.064	-0.032	19.956	-0.125	-0.125	0.000	0.000	0.000	0.000
168	A	192	TRP	0	-0.004	0.003	23.232	-0.067	-0.067	0.000	0.000	0.000	0.000
169	A	193	LEU	0	-0.021	-0.007	22.210	-0.072	-0.072	0.000	0.000	0.000	0.000
170	A	194	MET	0	-0.051	-0.023	21.039	-0.011	-0.011	0.000	0.000	0.000	0.000
171	A	195	ASN	0	-0.109	-0.060	24.318	-0.099	-0.099	0.000	0.000	0.000	0.000
172	A	196	HIS	0	0.074	0.060	27.755	-0.077	-0.077	0.000	0.000	0.000	0.000
173	A	197	PRO	0	-0.017	-0.010	29.872	0.001	0.001	0.000	0.000	0.000	0.000
174	A	198	ASP	-1	-0.904	-0.955	33.199	0.624	0.624	0.000	0.000	0.000	0.000
175	A	199	TYR	0	-0.023	-0.043	28.640	-0.008	-0.008	0.000	0.000	0.000	0.000
176	A	200	GLN	0	-0.041	-0.005	27.530	-0.011	-0.011	0.000	0.000	0.000	0.000
177	A	201	THR	0	0.038	0.011	21.521	-0.043	-0.043	0.000	0.000	0.000	0.000
178	A	202	ALA	0	-0.025	0.003	20.342	0.016	0.016	0.000	0.000	0.000	0.000
179	A	203	ILE	0	0.041	0.005	14.803	-0.048	-0.048	0.000	0.000	0.000	0.000
180	A	204	ILE	0	-0.026	-0.009	14.282	0.090	0.090	0.000	0.000	0.000	0.000
181	A	205	PRO	0	-0.028	-0.016	9.542	0.019	0.019	0.000	0.000	0.000	0.000
182	A	206	VAL	0	0.002	-0.009	10.346	0.505	0.505	0.000	0.000	0.000	0.000
183	A	207	GLY	0	0.043	0.031	10.648	-0.455	-0.455	0.000	0.000	0.000	0.000
184	A	208	ASP	-1	-0.808	-0.893	10.327	4.417	4.417	0.000	0.000	0.000	0.000
185	A	209	GLY	0	-0.027	-0.013	12.621	-0.018	-0.018	0.000	0.000	0.000	0.000
186	A	210	LEU	0	0.033	0.012	13.538	-0.450	-0.450	0.000	0.000	0.000	0.000
187	A	211	ALA	0	-0.004	0.003	16.984	0.080	0.080	0.000	0.000	0.000	0.000
188	A	212	ILE	0	-0.023	-0.014	19.636	-0.159	-0.159	0.000	0.000	0.000	0.000
189	A	213	SER	0	0.040	-0.007	22.416	0.038	0.038	0.000	0.000	0.000	0.000
190	A	214	LYS	1	0.873	0.945	25.686	-0.747	-0.747	0.000	0.000	0.000	0.000
191	A	215	LYS	1	0.933	0.974	29.245	-0.602	-0.602	0.000	0.000	0.000	0.000
192	A	216	LYS	1	0.749	0.847	30.624	-0.842	-0.842	0.000	0.000	0.000	0.000
193	A	217	ARG	0	-0.004	0.025	32.819	-0.016	-0.016	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ASP)