FMO DATABASE

FMODB ID: N6GKQ

Calculation Name: 1H6F-A-Xray549

Preferred Name:

Target Type:

Ligand Name: magnesium ion

Ligand 3-letter code: MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1H6F

Chain ID: A

ChEMBL ID:

UniProt ID: O15119

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	184
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2115637.46738
FMO2-HF: Nuclear repulsion	2039173.179702
FMO2-HF: Total energy	-76464.287678
FMO2-MP2: Total energy	-76684.870871

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:102:ASP)

Summations of interaction energy for fragment #1(A:102: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.
5.771	8.749	0.338	-1.293	-2.024	0.003

Interaction energy analysis for fragmet #1(A:102:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.033 / q_NPA : -0.022

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	104	LYS	1	0.940	0.968	2.665	11.709	14.195	0.335	-1.006	-1.816	0.004
41	A	142	GLY	0	0.046	0.011	4.564	-0.788	-0.790	-0.001	-0.019	0.022	0.000
42	A	143	LEU	0	-0.020	-0.016	3.523	-7.173	-6.863	0.004	-0.233	-0.081	-0.001
148	A	249	ARG	1	0.935	0.977	3.781	-3.746	-3.562	0.000	-0.035	-0.149	0.000
4	A	105	VAL	0	-0.007	0.001	5.943	-0.471	-0.471	0.000	0.000	0.000	0.000
5	A	106	HIS	0	-0.022	-0.009	9.637	0.495	0.495	0.000	0.000	0.000	0.000
6	A	107	LEU	0	0.025	0.016	12.501	-0.020	-0.020	0.000	0.000	0.000	0.000
7	A	108	GLU	-1	-0.883	-0.956	15.880	-1.424	-1.424	0.000	0.000	0.000	0.000
8	A	109	ALA	0	0.004	-0.012	18.866	0.113	0.113	0.000	0.000	0.000	0.000
9	A	110	LYS	1	0.859	0.909	17.150	0.142	0.142	0.000	0.000	0.000	0.000
10	A	111	GLU	-1	-0.844	-0.922	20.440	-0.451	-0.451	0.000	0.000	0.000	0.000
11	A	112	LEU	0	-0.045	-0.018	23.623	0.061	0.061	0.000	0.000	0.000	0.000
12	A	113	TRP	0	0.001	-0.011	21.204	0.088	0.088	0.000	0.000	0.000	0.000
13	A	114	ASP	-1	-0.801	-0.891	21.510	0.011	0.011	0.000	0.000	0.000	0.000
14	A	115	GLN	0	-0.025	0.006	24.180	0.072	0.072	0.000	0.000	0.000	0.000
15	A	116	PHE	0	0.009	-0.012	26.796	0.026	0.026	0.000	0.000	0.000	0.000
16	A	117	HIS	0	0.051	0.031	22.742	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	118	LYS	1	0.942	0.976	26.311	0.001	0.001	0.000	0.000	0.000	0.000
18	A	119	ARG	1	0.783	0.877	28.482	0.062	0.062	0.000	0.000	0.000	0.000
19	A	120	GLY	0	0.021	0.023	29.192	0.006	0.006	0.000	0.000	0.000	0.000
20	A	121	THR	0	0.005	-0.003	25.877	-0.031	-0.031	0.000	0.000	0.000	0.000
21	A	122	GLU	-1	-0.687	-0.823	28.984	0.056	0.056	0.000	0.000	0.000	0.000
22	A	123	MET	0	-0.076	-0.023	26.569	-0.052	-0.052	0.000	0.000	0.000	0.000
23	A	124	VAL	0	0.025	0.030	31.568	0.017	0.017	0.000	0.000	0.000	0.000
24	A	125	ILE	0	-0.037	-0.015	32.498	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	126	THR	0	0.022	-0.007	35.086	0.000	0.000	0.000	0.000	0.000	0.000
26	A	127	LYS	1	1.040	1.044	37.212	0.070	0.070	0.000	0.000	0.000	0.000
27	A	128	SER	0	-0.025	-0.021	39.120	0.000	0.000	0.000	0.000	0.000	0.000
28	A	129	GLY	0	0.024	0.018	34.967	-0.023	-0.023	0.000	0.000	0.000	0.000
29	A	130	ARG	1	0.935	0.971	33.408	0.114	0.114	0.000	0.000	0.000	0.000
30	A	131	ARG	1	0.977	0.981	30.170	0.364	0.364	0.000	0.000	0.000	0.000
31	A	132	MET	0	0.014	0.017	23.217	0.018	0.018	0.000	0.000	0.000	0.000
32	A	133	PHE	0	-0.018	-0.001	28.422	-0.046	-0.046	0.000	0.000	0.000	0.000
33	A	134	PRO	0	0.113	0.053	24.610	0.043	0.043	0.000	0.000	0.000	0.000
34	A	135	PRO	0	-0.046	-0.015	25.034	0.023	0.023	0.000	0.000	0.000	0.000
35	A	136	PHE	0	0.053	0.019	16.332	-0.053	-0.053	0.000	0.000	0.000	0.000
36	A	137	LYS	1	0.940	0.985	19.835	0.665	0.665	0.000	0.000	0.000	0.000
37	A	138	VAL	0	0.060	0.040	14.194	0.043	0.043	0.000	0.000	0.000	0.000
38	A	139	ARG	1	0.975	1.000	14.051	2.230	2.230	0.000	0.000	0.000	0.000
39	A	140	CYS	0	0.006	0.017	9.959	0.044	0.044	0.000	0.000	0.000	0.000
40	A	141	SER	0	0.004	-0.008	8.099	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	144	ASP	-1	-0.792	-0.877	5.446	-8.146	-8.146	0.000	0.000	0.000	0.000
44	A	145	LYS	1	0.962	0.971	7.381	5.544	5.544	0.000	0.000	0.000	0.000
45	A	146	LYS	1	0.912	0.920	10.624	2.804	2.804	0.000	0.000	0.000	0.000
46	A	147	ALA	0	-0.018	0.014	9.991	0.507	0.507	0.000	0.000	0.000	0.000
47	A	148	LYS	1	0.901	0.944	12.007	1.455	1.455	0.000	0.000	0.000	0.000
48	A	149	TYR	0	0.011	0.001	6.921	-0.416	-0.416	0.000	0.000	0.000	0.000
49	A	150	ILE	0	0.027	0.024	13.579	0.055	0.055	0.000	0.000	0.000	0.000
50	A	151	LEU	0	-0.008	0.005	12.014	-0.050	-0.050	0.000	0.000	0.000	0.000
51	A	152	LEU	0	-0.036	-0.025	15.381	0.137	0.137	0.000	0.000	0.000	0.000
52	A	153	MET	0	-0.028	0.001	16.650	-0.080	-0.080	0.000	0.000	0.000	0.000
53	A	154	ASP	-1	-0.745	-0.835	19.213	0.191	0.191	0.000	0.000	0.000	0.000
54	A	155	ILE	0	-0.026	-0.011	20.943	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	156	ILE	0	0.015	0.014	20.648	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	157	ALA	0	0.052	0.019	24.036	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	158	ALA	0	-0.038	-0.025	23.691	0.048	0.048	0.000	0.000	0.000	0.000
58	A	159	ASP	-1	-0.780	-0.861	24.717	0.433	0.433	0.000	0.000	0.000	0.000
59	A	160	ASP	-1	-0.815	-0.907	27.497	0.393	0.393	0.000	0.000	0.000	0.000
60	A	161	CYS	0	-0.031	-0.018	30.755	-0.019	-0.019	0.000	0.000	0.000	0.000
61	A	162	ARG	1	0.960	1.004	32.830	-0.195	-0.195	0.000	0.000	0.000	0.000
62	A	163	TYR	0	-0.087	-0.087	29.793	0.002	0.002	0.000	0.000	0.000	0.000
63	A	164	LYS	1	0.925	0.959	36.000	-0.186	-0.186	0.000	0.000	0.000	0.000
64	A	165	PHE	0	0.049	0.028	36.644	0.014	0.014	0.000	0.000	0.000	0.000
65	A	166	HIS	0	-0.002	-0.016	39.049	0.001	0.001	0.000	0.000	0.000	0.000
66	A	167	ASN	0	0.006	-0.004	40.761	0.004	0.004	0.000	0.000	0.000	0.000
67	A	168	SER	0	0.009	0.003	40.328	0.006	0.006	0.000	0.000	0.000	0.000
68	A	169	ARG	1	0.943	0.981	36.604	-0.173	-0.173	0.000	0.000	0.000	0.000
69	A	170	TRP	0	0.004	-0.006	33.345	0.004	0.004	0.000	0.000	0.000	0.000
70	A	171	MET	0	-0.022	-0.011	34.721	0.028	0.028	0.000	0.000	0.000	0.000
71	A	172	VAL	0	0.041	0.023	33.355	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	173	ALA	0	-0.073	-0.049	35.936	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	174	GLY	0	0.008	0.005	37.488	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	175	LYS	1	0.837	0.924	33.357	-0.314	-0.314	0.000	0.000	0.000	0.000
75	A	176	ALA	0	-0.080	-0.034	33.181	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	177	ASP	-1	-0.849	-0.936	35.243	0.167	0.167	0.000	0.000	0.000	0.000
77	A	178	PRO	0	-0.021	-0.024	35.030	0.018	0.018	0.000	0.000	0.000	0.000
78	A	179	GLU	-1	-0.748	-0.821	30.324	0.165	0.165	0.000	0.000	0.000	0.000
79	A	180	MET	0	-0.011	0.003	32.501	0.010	0.010	0.000	0.000	0.000	0.000
80	A	181	PRO	0	0.021	0.002	29.448	0.012	0.012	0.000	0.000	0.000	0.000
81	A	182	LYS	1	0.798	0.905	25.738	-0.183	-0.183	0.000	0.000	0.000	0.000
82	A	183	ARG	1	0.819	0.906	26.170	0.227	0.227	0.000	0.000	0.000	0.000
83	A	184	MET	0	0.043	0.038	19.469	-0.053	-0.053	0.000	0.000	0.000	0.000
84	A	185	TYR	0	-0.060	-0.050	22.319	-0.040	-0.040	0.000	0.000	0.000	0.000
85	A	186	ILE	0	0.052	0.020	20.223	-0.050	-0.050	0.000	0.000	0.000	0.000
86	A	187	HIS	0	-0.016	-0.004	18.784	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	188	PRO	0	-0.019	-0.021	20.680	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	189	ASP	-1	-0.837	-0.899	19.938	-1.165	-1.165	0.000	0.000	0.000	0.000
89	A	190	SER	0	-0.089	-0.034	18.689	-0.172	-0.172	0.000	0.000	0.000	0.000
90	A	191	PRO	0	-0.015	0.006	17.838	0.107	0.107	0.000	0.000	0.000	0.000
91	A	192	ALA	0	0.064	0.021	16.348	0.029	0.029	0.000	0.000	0.000	0.000
92	A	193	THR	0	-0.030	-0.042	14.119	-0.120	-0.120	0.000	0.000	0.000	0.000
93	A	194	GLY	0	0.044	0.020	10.242	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	195	GLU	-1	-0.850	-0.911	11.094	-2.931	-2.931	0.000	0.000	0.000	0.000
95	A	196	GLN	0	0.057	0.037	13.453	0.058	0.058	0.000	0.000	0.000	0.000
96	A	197	TRP	0	-0.018	-0.012	12.365	0.217	0.217	0.000	0.000	0.000	0.000
97	A	198	MET	0	-0.074	-0.017	8.964	-0.566	-0.566	0.000	0.000	0.000	0.000
98	A	199	SER	0	-0.097	-0.036	12.829	0.265	0.265	0.000	0.000	0.000	0.000
99	A	200	LYS	1	0.884	0.942	16.194	1.817	1.817	0.000	0.000	0.000	0.000
100	A	201	VAL	0	-0.004	0.006	16.655	-0.183	-0.183	0.000	0.000	0.000	0.000
101	A	202	VAL	0	-0.024	-0.003	15.259	0.124	0.124	0.000	0.000	0.000	0.000
102	A	203	THR	0	-0.032	-0.048	18.218	0.122	0.122	0.000	0.000	0.000	0.000
103	A	204	PHE	0	0.051	0.017	17.731	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	205	HIS	0	0.021	0.004	23.382	0.124	0.124	0.000	0.000	0.000	0.000
105	A	206	LYS	1	0.933	0.963	26.642	0.472	0.472	0.000	0.000	0.000	0.000
106	A	207	LEU	0	-0.002	0.013	24.042	0.043	0.043	0.000	0.000	0.000	0.000
107	A	208	LYS	1	0.823	0.926	27.501	0.211	0.211	0.000	0.000	0.000	0.000
108	A	209	LEU	0	0.039	0.029	27.475	0.018	0.018	0.000	0.000	0.000	0.000
109	A	210	THR	0	-0.045	-0.052	31.380	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	211	ASN	0	0.094	0.051	34.210	0.002	0.002	0.000	0.000	0.000	0.000
111	A	212	ASN	0	-0.013	-0.009	36.947	0.024	0.024	0.000	0.000	0.000	0.000
112	A	213	ILE	0	0.079	0.025	36.719	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	214	SER	0	0.021	0.019	37.931	0.007	0.007	0.000	0.000	0.000	0.000
114	A	215	ASP	-1	-0.827	-0.908	35.213	-0.119	-0.119	0.000	0.000	0.000	0.000
115	A	216	LYS	1	0.932	0.966	36.747	0.061	0.061	0.000	0.000	0.000	0.000
116	A	217	HIS	1	0.825	0.897	35.045	0.122	0.122	0.000	0.000	0.000	0.000
117	A	218	GLY	0	0.028	0.034	31.741	-0.026	-0.026	0.000	0.000	0.000	0.000
118	A	219	PHE	0	-0.028	-0.018	30.290	-0.031	-0.031	0.000	0.000	0.000	0.000
119	A	220	THR	0	0.049	0.019	26.808	0.006	0.006	0.000	0.000	0.000	0.000
120	A	221	ILE	0	-0.004	0.012	29.640	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	222	LEU	0	-0.045	-0.016	28.057	0.021	0.021	0.000	0.000	0.000	0.000
122	A	223	ASN	0	0.031	0.005	32.093	-0.038	-0.038	0.000	0.000	0.000	0.000
123	A	224	SER	0	-0.014	-0.025	33.870	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	225	MET	0	-0.008	0.007	35.646	0.009	0.009	0.000	0.000	0.000	0.000
125	A	226	HIS	0	0.042	0.026	31.897	0.040	0.040	0.000	0.000	0.000	0.000
126	A	227	LYS	1	0.863	0.939	26.442	-0.375	-0.375	0.000	0.000	0.000	0.000
127	A	228	TYR	0	-0.048	-0.052	25.921	0.016	0.016	0.000	0.000	0.000	0.000
128	A	229	GLN	0	0.025	-0.007	19.207	0.041	0.041	0.000	0.000	0.000	0.000
129	A	230	PRO	0	-0.059	-0.026	19.981	0.002	0.002	0.000	0.000	0.000	0.000
130	A	231	ARG	1	0.858	0.901	16.666	-0.348	-0.348	0.000	0.000	0.000	0.000
131	A	232	PHE	0	0.007	0.001	11.683	-0.146	-0.146	0.000	0.000	0.000	0.000
132	A	233	HIS	0	0.001	0.000	13.026	0.274	0.274	0.000	0.000	0.000	0.000
133	A	234	ILE	0	-0.014	0.001	8.110	-0.403	-0.403	0.000	0.000	0.000	0.000
134	A	235	VAL	0	0.063	0.032	10.893	0.359	0.359	0.000	0.000	0.000	0.000
135	A	236	ARG	1	0.839	0.897	7.340	3.068	3.068	0.000	0.000	0.000	0.000
136	A	237	ALA	0	0.029	0.018	11.849	0.262	0.262	0.000	0.000	0.000	0.000
137	A	238	ASN	0	-0.005	-0.022	15.647	-0.080	-0.080	0.000	0.000	0.000	0.000
138	A	239	ASP	-1	-0.757	-0.890	18.511	-0.369	-0.369	0.000	0.000	0.000	0.000
139	A	240	ILE	0	0.011	0.005	20.575	0.030	0.030	0.000	0.000	0.000	0.000
140	A	241	LEU	0	0.023	0.007	22.273	0.070	0.070	0.000	0.000	0.000	0.000
141	A	242	LYS	1	0.917	0.953	19.579	0.515	0.515	0.000	0.000	0.000	0.000
142	A	243	LEU	0	-0.038	0.003	17.718	0.069	0.069	0.000	0.000	0.000	0.000
143	A	244	PRO	0	-0.011	-0.013	19.600	0.082	0.082	0.000	0.000	0.000	0.000
144	A	245	TYR	0	0.009	0.020	20.698	0.085	0.085	0.000	0.000	0.000	0.000
145	A	246	SER	0	-0.046	-0.028	15.493	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	247	THR	0	-0.006	-0.006	11.793	0.142	0.142	0.000	0.000	0.000	0.000
147	A	248	PHE	0	-0.011	-0.016	12.707	-0.297	-0.297	0.000	0.000	0.000	0.000
149	A	250	THR	0	0.011	-0.018	10.238	-0.528	-0.528	0.000	0.000	0.000	0.000
150	A	251	TYR	0	-0.047	-0.034	5.589	0.517	0.517	0.000	0.000	0.000	0.000
151	A	252	LEU	0	0.014	-0.004	11.732	-0.205	-0.205	0.000	0.000	0.000	0.000
152	A	253	PHE	0	0.041	0.022	12.075	0.033	0.033	0.000	0.000	0.000	0.000
153	A	254	PRO	0	0.070	0.055	15.922	-0.085	-0.085	0.000	0.000	0.000	0.000
154	A	255	GLU	-1	-0.798	-0.882	17.468	0.055	0.055	0.000	0.000	0.000	0.000
155	A	256	THR	0	-0.087	-0.080	19.152	-0.088	-0.088	0.000	0.000	0.000	0.000
156	A	257	GLU	-1	-0.858	-0.918	21.544	0.356	0.356	0.000	0.000	0.000	0.000
157	A	258	PHE	0	-0.060	-0.041	23.468	-0.047	-0.047	0.000	0.000	0.000	0.000
158	A	259	ILE	0	0.030	0.021	27.145	0.031	0.031	0.000	0.000	0.000	0.000
159	A	260	ALA	0	-0.028	-0.006	30.611	-0.040	-0.040	0.000	0.000	0.000	0.000
160	A	261	VAL	0	0.031	0.015	32.182	0.019	0.019	0.000	0.000	0.000	0.000
161	A	262	THR	0	0.006	-0.010	35.864	-0.015	-0.015	0.000	0.000	0.000	0.000
162	A	263	ALA	0	-0.006	-0.008	38.870	-0.018	-0.018	0.000	0.000	0.000	0.000
163	A	264	TYR	0	-0.012	-0.011	33.653	0.006	0.006	0.000	0.000	0.000	0.000
164	A	265	GLN	0	-0.054	-0.026	37.342	0.012	0.012	0.000	0.000	0.000	0.000
165	A	266	ASN	0	0.018	0.015	34.444	-0.009	-0.009	0.000	0.000	0.000	0.000
166	A	267	ASP	-1	-0.823	-0.914	37.099	-0.028	-0.028	0.000	0.000	0.000	0.000
167	A	268	LYS	1	0.913	0.947	35.759	-0.028	-0.028	0.000	0.000	0.000	0.000
168	A	269	ILE	0	-0.052	-0.016	31.169	-0.022	-0.022	0.000	0.000	0.000	0.000
169	A	270	THR	0	0.032	-0.003	34.417	-0.024	-0.024	0.000	0.000	0.000	0.000
170	A	271	GLN	0	0.036	0.018	37.181	-0.006	-0.006	0.000	0.000	0.000	0.000
171	A	272	LEU	0	0.000	0.018	30.487	-0.021	-0.021	0.000	0.000	0.000	0.000
172	A	273	LYS	1	0.754	0.864	30.246	0.082	0.082	0.000	0.000	0.000	0.000
173	A	274	ILE	0	0.019	0.011	34.239	-0.029	-0.029	0.000	0.000	0.000	0.000
174	A	275	ASP	-1	-0.797	-0.883	35.292	-0.173	-0.173	0.000	0.000	0.000	0.000
175	A	276	ASN	0	-0.085	-0.055	30.809	-0.046	-0.046	0.000	0.000	0.000	0.000
176	A	277	ASN	0	-0.029	-0.018	32.600	-0.057	-0.057	0.000	0.000	0.000	0.000
177	A	278	PRO	0	-0.004	-0.016	32.451	0.016	0.016	0.000	0.000	0.000	0.000
178	A	279	PHE	0	-0.040	-0.035	33.473	0.004	0.004	0.000	0.000	0.000	0.000
179	A	280	ALA	0	-0.016	0.006	36.895	0.016	0.016	0.000	0.000	0.000	0.000
180	A	281	LYS	1	0.973	0.979	38.097	0.302	0.302	0.000	0.000	0.000	0.000
181	A	282	GLY	0	-0.019	-0.001	40.047	0.004	0.004	0.000	0.000	0.000	0.000
182	A	283	PHE	0	-0.058	-0.030	41.314	0.009	0.009	0.000	0.000	0.000	0.000
183	A	284	ARG	1	0.818	0.912	35.486	0.240	0.240	0.000	0.000	0.000	0.000
184	A	285	ASP	-2	-1.844	-1.896	42.517	-0.257	-0.257	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:102:ASP)