FMO DATABASE

FMODB ID: G7281

Calculation Name: 1FT5-A-Xray549

Preferred Name:

Target Type:

Ligand Name: protoporphyrin ix containing fe | phosphate ion

Ligand 3-letter code: HEM | PO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1FT5

Chain ID: A

ChEMBL ID:

UniProt ID: Q57142

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	211
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2381070.947961
FMO2-HF: Nuclear repulsion	2296672.876893
FMO2-HF: Total energy	-84398.071068
FMO2-MP2: Total energy	-84638.941874

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:ALA)

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

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.
162.361	163.594	-0.014	-0.494	-0.723	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.856 / q_NPA : 0.914

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	ALA	0	0.030	0.023	3.818	-0.278	0.904	-0.013	-0.491	-0.677	0.002
71	A	71	LYS	1	0.841	0.905	4.797	44.483	44.534	-0.001	-0.003	-0.046	0.000
4	A	4	PRO	0	-0.053	-0.037	6.206	2.055	2.055	0.000	0.000	0.000	0.000
5	A	5	PHE	0	0.041	0.025	8.840	0.915	0.915	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.806	-0.872	12.567	-18.925	-18.925	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.003	-0.001	15.386	1.149	1.149	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.871	0.928	18.610	12.877	12.877	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.955	0.981	21.182	12.811	12.811	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.898	0.932	17.220	16.944	16.944	0.000	0.000	0.000	0.000
11	A	11	CYS	0	0.076	0.047	18.598	0.268	0.268	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.030	-0.009	21.383	0.546	0.546	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.116	-0.061	23.688	0.523	0.523	0.000	0.000	0.000	0.000
14	A	14	CYS	0	-0.018	-0.009	23.500	0.393	0.393	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.004	0.011	21.461	0.846	0.846	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.952	0.976	26.307	10.338	10.338	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.020	0.034	29.408	0.189	0.189	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.076	0.033	26.278	0.332	0.332	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.014	0.003	26.418	0.048	0.048	0.000	0.000	0.000	0.000
20	A	20	GLN	0	0.006	-0.005	27.894	0.332	0.332	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.012	0.030	30.751	0.333	0.333	0.000	0.000	0.000	0.000
22	A	22	TRP	0	0.046	0.023	24.816	0.309	0.309	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.915	0.970	28.855	9.707	9.707	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.888	-0.947	30.608	-9.026	-9.026	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.003	0.004	29.143	0.165	0.165	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.003	-0.019	30.920	0.033	0.033	0.000	0.000	0.000	0.000
27	A	27	HIS	0	-0.002	-0.005	25.518	-0.204	-0.204	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.005	0.005	26.766	-0.271	-0.271	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.833	0.915	28.193	9.335	9.335	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.035	0.031	26.514	0.287	0.287	0.000	0.000	0.000	0.000
31	A	31	MET	0	0.058	0.037	25.897	0.304	0.304	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.830	-0.904	28.881	-9.301	-9.301	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.035	-0.019	31.215	0.377	0.377	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.006	0.012	27.300	0.204	0.204	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.852	0.922	31.843	9.538	9.538	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.047	0.034	34.626	0.077	0.077	0.000	0.000	0.000	0.000
37	A	37	ASN	0	-0.019	-0.022	37.830	0.198	0.198	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.009	0.021	36.130	0.205	0.205	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.923	0.943	33.409	9.328	9.328	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.904	0.955	38.618	7.338	7.338	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.859	-0.914	41.035	-7.380	-7.380	0.000	0.000	0.000	0.000
42	A	42	ALA	0	-0.016	-0.015	37.007	-0.017	-0.017	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.867	0.943	34.712	8.867	8.867	0.000	0.000	0.000	0.000
44	A	44	GLN	0	0.046	0.014	37.977	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.819	0.906	39.822	7.903	7.903	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.004	-0.003	35.243	0.035	0.035	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.905	0.963	36.652	7.362	7.362	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.006	0.014	33.145	-0.086	-0.086	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.796	-0.900	37.116	-7.710	-7.710	0.000	0.000	0.000	0.000
50	A	50	PRO	0	-0.040	-0.034	38.041	-0.176	-0.176	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.012	-0.022	40.186	-0.016	-0.016	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.878	0.946	32.779	9.418	9.418	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.855	-0.908	33.363	-9.632	-9.632	0.000	0.000	0.000	0.000
54	A	54	TYR	0	0.040	-0.001	30.680	0.013	0.013	0.000	0.000	0.000	0.000
55	A	55	THR	0	-0.084	-0.078	29.234	-0.481	-0.481	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.011	-0.014	27.465	-0.577	-0.577	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.816	-0.898	27.710	-10.660	-10.660	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.969	0.973	23.599	11.704	11.704	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.908	-0.944	23.977	-12.046	-12.046	0.000	0.000	0.000	0.000
60	A	60	CYS	0	-0.061	-0.023	26.414	0.236	0.236	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.004	-0.018	22.674	-0.331	-0.331	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.003	-0.008	20.648	-0.324	-0.324	0.000	0.000	0.000	0.000
63	A	63	CYS	0	-0.008	0.009	20.333	-0.715	-0.715	0.000	0.000	0.000	0.000
64	A	64	HIS	0	-0.061	-0.056	22.858	0.359	0.359	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.067	-0.028	19.777	0.412	0.412	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.805	-0.881	17.615	-16.568	-16.568	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.027	-0.005	14.547	-0.036	-0.036	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.020	0.021	14.695	-0.728	-0.728	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.038	0.021	14.976	-0.673	-0.673	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.039	-0.009	10.541	-3.544	-3.544	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.021	0.000	10.384	-0.981	-0.981	0.000	0.000	0.000	0.000
73	A	73	GLY	0	-0.025	-0.006	13.081	1.062	1.062	0.000	0.000	0.000	0.000
74	A	74	TYR	0	-0.029	-0.014	15.349	0.545	0.545	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.006	-0.007	17.883	-0.211	-0.211	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.022	-0.006	20.279	0.307	0.307	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.902	-0.936	22.888	-12.405	-12.405	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.043	-0.020	21.394	0.312	0.312	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.034	0.040	21.927	-0.736	-0.736	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.988	0.983	18.120	16.133	16.133	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.084	0.044	23.237	-0.314	-0.314	0.000	0.000	0.000	0.000
82	A	82	MET	0	-0.153	-0.062	19.462	0.220	0.220	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.000	0.010	16.919	-0.400	-0.400	0.000	0.000	0.000	0.000
84	A	84	THR	0	0.020	0.015	21.047	-0.090	-0.090	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.015	0.024	24.256	0.341	0.341	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.018	0.015	21.542	-0.563	-0.563	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.040	0.004	21.320	0.528	0.528	0.000	0.000	0.000	0.000
88	A	88	CYS	0	-0.064	-0.047	19.755	-0.137	-0.137	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.675	-0.836	14.434	-20.848	-20.848	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.025	-0.028	15.706	-1.205	-1.205	0.000	0.000	0.000	0.000
91	A	91	CYS	0	-0.017	0.003	17.400	-0.360	-0.360	0.000	0.000	0.000	0.000
92	A	92	HIS	0	0.008	-0.003	17.140	-1.126	-1.126	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.061	0.043	13.055	-1.059	-1.059	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.073	-0.031	9.276	1.613	1.613	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.093	0.026	11.085	-1.426	-1.426	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.773	0.890	10.109	23.508	23.508	0.000	0.000	0.000	0.000
97	A	97	ASN	0	0.004	-0.012	5.838	3.758	3.758	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.078	0.055	10.220	1.729	1.729	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.840	0.887	12.807	20.735	20.735	0.000	0.000	0.000	0.000
100	A	100	GLY	0	-0.026	-0.009	14.594	1.291	1.291	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.740	-0.858	13.615	-20.786	-20.786	0.000	0.000	0.000	0.000
102	A	102	HIS	0	-0.005	0.000	16.395	1.770	1.770	0.000	0.000	0.000	0.000
103	A	103	ARG	1	0.880	0.937	19.067	14.354	14.354	0.000	0.000	0.000	0.000
104	A	104	LYS	0	0.008	0.017	18.373	0.841	0.841	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.032	0.013	18.863	0.481	0.481	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.031	0.024	21.487	0.580	0.580	0.000	0.000	0.000	0.000
107	A	107	GLN	0	-0.002	-0.011	23.593	0.166	0.166	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.040	0.014	23.740	0.516	0.516	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.013	0.023	25.423	0.412	0.412	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.869	-0.924	27.257	-10.011	-10.011	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.762	0.871	28.375	11.074	11.074	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.046	-0.035	28.051	0.119	0.119	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.048	0.036	30.128	0.088	0.088	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.902	0.949	24.177	12.135	12.135	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.919	0.975	24.137	11.220	11.220	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.004	-0.012	17.652	0.072	0.072	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.025	0.013	17.078	0.204	0.204	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.887	0.951	16.889	13.901	13.901	0.000	0.000	0.000	0.000
119	A	119	LYS	1	0.980	0.993	13.188	17.422	17.422	0.000	0.000	0.000	0.000
120	A	120	ASP	-1	-0.898	-0.948	12.196	-22.645	-22.645	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.040	-0.021	11.661	-2.150	-2.150	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.014	0.018	11.428	-1.807	-1.807	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.915	0.955	7.817	26.361	26.361	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.767	0.871	6.918	19.047	19.047	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.021	0.000	8.529	0.103	0.103	0.000	0.000	0.000	0.000
126	A	126	GLN	0	-0.016	0.006	9.147	1.429	1.429	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.794	-0.897	12.719	-22.090	-22.090	0.000	0.000	0.000	0.000
128	A	128	PHE	0	-0.019	-0.032	14.551	1.274	1.274	0.000	0.000	0.000	0.000
129	A	129	HIS	0	-0.015	-0.005	16.500	0.449	0.449	0.000	0.000	0.000	0.000
130	A	130	PHE	0	0.028	-0.008	17.187	1.071	1.071	0.000	0.000	0.000	0.000
131	A	131	GLU	-1	-0.893	-0.927	18.607	-13.995	-13.995	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.818	-0.897	14.523	-17.896	-17.896	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.857	0.918	10.567	24.938	24.938	0.000	0.000	0.000	0.000
134	A	134	CYS	0	-0.057	-0.023	17.246	0.692	0.692	0.000	0.000	0.000	0.000
135	A	135	SER	0	0.006	-0.011	19.924	0.874	0.874	0.000	0.000	0.000	0.000
136	A	136	ALA	0	-0.019	-0.013	17.130	0.424	0.424	0.000	0.000	0.000	0.000
137	A	137	CYS	0	-0.059	-0.024	19.224	0.127	0.127	0.000	0.000	0.000	0.000
138	A	138	HIS	0	-0.035	-0.025	22.305	0.788	0.788	0.000	0.000	0.000	0.000
139	A	139	LEU	0	-0.023	-0.003	23.458	0.575	0.575	0.000	0.000	0.000	0.000
140	A	140	ASN	0	0.050	0.047	21.597	-0.462	-0.462	0.000	0.000	0.000	0.000
141	A	141	TYR	0	0.019	-0.007	23.674	0.282	0.282	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.882	-0.943	26.680	-10.613	-10.613	0.000	0.000	0.000	0.000
143	A	143	GLY	0	0.005	-0.005	28.631	0.240	0.240	0.000	0.000	0.000	0.000
144	A	144	SER	0	-0.059	-0.024	25.158	0.186	0.186	0.000	0.000	0.000	0.000
145	A	145	PRO	0	-0.029	-0.017	26.545	-0.160	-0.160	0.000	0.000	0.000	0.000
146	A	146	TRP	0	-0.064	-0.026	17.089	-0.072	-0.072	0.000	0.000	0.000	0.000
147	A	147	LYS	1	0.976	0.966	20.998	12.229	12.229	0.000	0.000	0.000	0.000
148	A	148	GLY	0	0.039	0.037	18.148	-0.348	-0.348	0.000	0.000	0.000	0.000
149	A	149	ALA	0	-0.033	-0.007	18.833	-0.378	-0.378	0.000	0.000	0.000	0.000
150	A	150	LYS	1	0.811	0.902	17.961	16.539	16.539	0.000	0.000	0.000	0.000
151	A	151	ALA	0	0.032	0.036	22.357	-0.043	-0.043	0.000	0.000	0.000	0.000
152	A	152	PRO	0	-0.018	-0.011	21.755	-0.547	-0.547	0.000	0.000	0.000	0.000
153	A	153	TYR	0	0.027	0.004	23.785	-0.602	-0.602	0.000	0.000	0.000	0.000
154	A	154	THR	0	-0.005	0.002	26.284	0.253	0.253	0.000	0.000	0.000	0.000
155	A	155	PRO	0	0.002	-0.008	27.833	0.208	0.208	0.000	0.000	0.000	0.000
156	A	156	PHE	0	-0.070	-0.028	30.710	0.420	0.420	0.000	0.000	0.000	0.000
157	A	157	THR	0	0.082	0.034	30.622	-0.257	-0.257	0.000	0.000	0.000	0.000
158	A	158	PRO	0	-0.003	-0.027	31.551	0.263	0.263	0.000	0.000	0.000	0.000
159	A	159	GLU	-1	-0.925	-0.947	34.767	-8.732	-8.732	0.000	0.000	0.000	0.000
160	A	160	VAL	0	-0.040	0.004	35.787	0.276	0.276	0.000	0.000	0.000	0.000
161	A	161	ASP	-1	-0.853	-0.960	36.684	-7.857	-7.857	0.000	0.000	0.000	0.000
162	A	162	ALA	0	0.088	0.067	36.186	-0.282	-0.282	0.000	0.000	0.000	0.000
163	A	163	LYS	1	0.902	0.968	36.082	8.110	8.110	0.000	0.000	0.000	0.000
164	A	164	TYR	0	-0.065	-0.034	32.126	-0.144	-0.144	0.000	0.000	0.000	0.000
165	A	165	THR	0	-0.037	-0.025	31.370	-0.347	-0.347	0.000	0.000	0.000	0.000
166	A	166	PHE	0	0.033	0.007	24.381	0.026	0.026	0.000	0.000	0.000	0.000
167	A	167	LYS	1	0.959	0.966	28.738	10.050	10.050	0.000	0.000	0.000	0.000
168	A	168	PHE	0	0.049	0.028	22.177	0.051	0.051	0.000	0.000	0.000	0.000
169	A	169	ASP	-1	-0.801	-0.906	26.277	-12.034	-12.034	0.000	0.000	0.000	0.000
170	A	170	GLU	-1	-0.889	-0.933	28.222	-9.423	-9.423	0.000	0.000	0.000	0.000
171	A	171	MET	0	-0.013	-0.012	28.452	-0.094	-0.094	0.000	0.000	0.000	0.000
172	A	172	VAL	0	-0.035	-0.015	24.104	-0.143	-0.143	0.000	0.000	0.000	0.000
173	A	173	LYS	1	0.808	0.879	27.014	10.252	10.252	0.000	0.000	0.000	0.000
174	A	174	GLU	-1	-0.855	-0.887	30.182	-9.051	-9.051	0.000	0.000	0.000	0.000
175	A	175	VAL	0	0.005	-0.009	30.585	-0.282	-0.282	0.000	0.000	0.000	0.000
176	A	176	LYS	0	-0.028	-0.032	31.574	-0.232	-0.232	0.000	0.000	0.000	0.000
177	A	177	ALA	0	-0.039	-0.020	29.366	-0.009	-0.009	0.000	0.000	0.000	0.000
178	A	178	MET	0	-0.071	-0.011	25.558	-0.712	-0.712	0.000	0.000	0.000	0.000
179	A	179	HIS	0	-0.062	-0.066	25.379	-0.722	-0.722	0.000	0.000	0.000	0.000
180	A	180	GLU	-1	-0.802	-0.884	29.430	-9.437	-9.437	0.000	0.000	0.000	0.000
181	A	181	HIS	0	0.023	0.021	26.685	-0.523	-0.523	0.000	0.000	0.000	0.000
182	A	182	TYR	0	-0.008	-0.020	29.738	0.592	0.592	0.000	0.000	0.000	0.000
183	A	183	LYS	1	0.853	0.921	29.857	9.577	9.577	0.000	0.000	0.000	0.000
184	A	184	LEU	0	-0.038	-0.017	24.992	-0.235	-0.235	0.000	0.000	0.000	0.000
185	A	185	GLU	-1	-0.905	-0.956	28.984	-9.812	-9.812	0.000	0.000	0.000	0.000
186	A	186	GLY	0	-0.012	0.003	26.758	0.103	0.103	0.000	0.000	0.000	0.000
187	A	187	VAL	0	-0.029	-0.015	22.583	-0.104	-0.104	0.000	0.000	0.000	0.000
188	A	188	PHE	0	-0.009	-0.009	18.297	-0.380	-0.380	0.000	0.000	0.000	0.000
189	A	189	GLU	-1	-0.899	-0.959	21.733	-12.214	-12.214	0.000	0.000	0.000	0.000
190	A	190	GLY	0	0.015	-0.001	20.733	-0.808	-0.808	0.000	0.000	0.000	0.000
191	A	191	GLU	-1	-0.815	-0.891	19.016	-15.060	-15.060	0.000	0.000	0.000	0.000
192	A	192	PRO	0	-0.066	-0.044	14.230	-0.608	-0.608	0.000	0.000	0.000	0.000
193	A	193	LYS	1	0.831	0.879	17.535	12.187	12.187	0.000	0.000	0.000	0.000
194	A	194	PHE	0	0.015	0.019	20.558	0.120	0.120	0.000	0.000	0.000	0.000
195	A	195	LYS	1	0.859	0.916	21.992	13.231	13.231	0.000	0.000	0.000	0.000
196	A	196	PHE	0	0.055	0.036	24.851	0.422	0.422	0.000	0.000	0.000	0.000
197	A	197	HIS	0	-0.041	-0.025	23.627	-0.079	-0.079	0.000	0.000	0.000	0.000
198	A	198	ASP	-1	-0.782	-0.885	26.239	-11.485	-11.485	0.000	0.000	0.000	0.000
199	A	199	GLU	-1	-0.800	-0.870	29.418	-9.893	-9.893	0.000	0.000	0.000	0.000
200	A	200	PHE	0	0.022	0.000	26.219	0.245	0.245	0.000	0.000	0.000	0.000
201	A	201	GLN	0	0.002	-0.022	28.023	0.569	0.569	0.000	0.000	0.000	0.000
202	A	202	ALA	0	-0.006	0.012	30.968	0.235	0.235	0.000	0.000	0.000	0.000
203	A	203	SER	0	-0.002	0.005	33.841	0.277	0.277	0.000	0.000	0.000	0.000
204	A	204	ALA	0	-0.032	0.003	31.593	0.121	0.121	0.000	0.000	0.000	0.000
205	A	205	LYS	1	0.811	0.899	33.714	9.340	9.340	0.000	0.000	0.000	0.000
206	A	206	PRO	0	0.063	0.015	34.467	-0.316	-0.316	0.000	0.000	0.000	0.000
207	A	207	ALA	0	0.014	0.009	33.537	-0.104	-0.104	0.000	0.000	0.000	0.000
208	A	208	LYS	1	0.972	1.001	34.455	9.190	9.190	0.000	0.000	0.000	0.000
209	A	209	LYS	1	0.891	0.918	34.455	8.792	8.792	0.000	0.000	0.000	0.000
210	A	210	GLY	0	-0.061	-0.042	32.704	-0.323	-0.323	0.000	0.000	0.000	0.000
211	A	211	LYS	0	0.072	0.057	29.948	1.168	1.168	0.000	0.000	0.000	0.000

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