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***  1asp_test  ***

elNémo ID: 181203223059140796

Job options:

ID        	=	 181203223059140796
JOBID     	=	 1asp_test
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1asp_test

data_1A2P
# 
_entry.id   1A2P 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1A2P         
WWPDB D_1000170318 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1A2P 
_pdbx_database_status.recvd_initial_deposition_date   1998-01-07 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Martin, C.'    1 
'Richard, V.'   2 
'Salem, M.'     3 
'Hartley, R.W.' 4 
'Mauguen, Y.'   5 
# 
_citation.id                        primary 
_citation.title                     'Refinement and structural analysis of barnase at 1.5 A resolution.' 
_citation.journal_abbrev            'Acta Crystallogr.,Sect.D' 
_citation.journal_volume            55 
_citation.page_first                386 
_citation.page_last                 398 
_citation.year                      1999 
_citation.journal_id_ASTM           ABCRE6 
_citation.country                   DK 
_citation.journal_id_ISSN           0907-4449 
_citation.journal_id_CSD            0766 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   10089345 
_citation.pdbx_database_id_DOI      10.1107/S0907444998010865 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Martin, C.'  1 
primary 'Richard, V.' 2 
primary 'Salem, M.'   3 
primary 'Hartley, R.' 4 
primary 'Mauguen, Y.' 5 
# 
_cell.entry_id           1A2P 
_cell.length_a           58.970 
_cell.length_b           58.970 
_cell.length_c           81.580 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              9 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1A2P 
_symmetry.space_group_name_H-M             'P 32' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                145 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man BARNASE    12398.721 3   3.1.27.- ? ? ? 
2 non-polymer syn 'ZINC ION' 65.409    3   ?        ? ? ? 
3 water       nat water      18.015    415 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTS
GFRNSDRILYSSDWLIYKTTDHYQTFTKIR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTS
GFRNSDRILYSSDWLIYKTTDHYQTFTKIR
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLN n 
1 3   VAL n 
1 4   ILE n 
1 5   ASN n 
1 6   THR n 
1 7   PHE n 
1 8   ASP n 
1 9   GLY n 
1 10  VAL n 
1 11  ALA n 
1 12  ASP n 
1 13  TYR n 
1 14  LEU n 
1 15  GLN n 
1 16  THR n 
1 17  TYR n 
1 18  HIS n 
1 19  LYS n 
1 20  LEU n 
1 21  PRO n 
1 22  ASP n 
1 23  ASN n 
1 24  TYR n 
1 25  ILE n 
1 26  THR n 
1 27  LYS n 
1 28  SER n 
1 29  GLU n 
1 30  ALA n 
1 31  GLN n 
1 32  ALA n 
1 33  LEU n 
1 34  GLY n 
1 35  TRP n 
1 36  VAL n 
1 37  ALA n 
1 38  SER n 
1 39  LYS n 
1 40  GLY n 
1 41  ASN n 
1 42  LEU n 
1 43  ALA n 
1 44  ASP n 
1 45  VAL n 
1 46  ALA n 
1 47  PRO n 
1 48  GLY n 
1 49  LYS n 
1 50  SER n 
1 51  ILE n 
1 52  GLY n 
1 53  GLY n 
1 54  ASP n 
1 55  ILE n 
1 56  PHE n 
1 57  SER n 
1 58  ASN n 
1 59  ARG n 
1 60  GLU n 
1 61  GLY n 
1 62  LYS n 
1 63  LEU n 
1 64  PRO n 
1 65  GLY n 
1 66  LYS n 
1 67  SER n 
1 68  GLY n 
1 69  ARG n 
1 70  THR n 
1 71  TRP n 
1 72  ARG n 
1 73  GLU n 
1 74  ALA n 
1 75  ASP n 
1 76  ILE n 
1 77  ASN n 
1 78  TYR n 
1 79  THR n 
1 80  SER n 
1 81  GLY n 
1 82  PHE n 
1 83  ARG n 
1 84  ASN n 
1 85  SER n 
1 86  ASP n 
1 87  ARG n 
1 88  ILE n 
1 89  LEU n 
1 90  TYR n 
1 91  SER n 
1 92  SER n 
1 93  ASP n 
1 94  TRP n 
1 95  LEU n 
1 96  ILE n 
1 97  TYR n 
1 98  LYS n 
1 99  THR n 
1 100 THR n 
1 101 ASP n 
1 102 HIS n 
1 103 TYR n 
1 104 GLN n 
1 105 THR n 
1 106 PHE n 
1 107 THR n 
1 108 LYS n 
1 109 ILE n 
1 110 ARG n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Bacillus 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Bacillus amyloliquefaciens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1390 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PMJ1002 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RNBR_BACAM 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00648 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;MMKMEGIALKKRLSWISVCLLVLVSAAGMLFSTAAKTETSSHKAHTEAQVINTFDGVADYLQTYHKLPDNYITKSEAQAL
GWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR
;
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1A2P A 1 ? 110 ? P00648 48 ? 157 ? 1 110 
2 1 1A2P B 1 ? 110 ? P00648 48 ? 157 ? 1 110 
3 1 1A2P C 1 ? 110 ? P00648 48 ? 157 ? 1 110 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1A2P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.24 
_exptl_crystal.density_percent_sol   45.0 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    'pH 7.5' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           287 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1993-11 
_diffrn_detector.details                'MULTILAYER MIRROR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'LURE BEAMLINE DW32' 
_diffrn_source.pdbx_synchrotron_site       LURE 
_diffrn_source.pdbx_synchrotron_beamline   DW32 
_diffrn_source.pdbx_wavelength             0.92 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1A2P 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             19.9 
_reflns.d_resolution_high            1.5 
_reflns.number_obs                   48463 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.0380000 
_reflns.pdbx_netI_over_sigmaI        11.9 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              2.5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.5 
_reflns_shell.d_res_low              1.58 
_reflns_shell.percent_possible_all   94.5 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.1580000 
_reflns_shell.meanI_over_sigI_obs    4.7 
_reflns_shell.pdbx_redundancy        1.9 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1A2P 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     48118 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             8.00 
_refine.ls_d_res_high                            1.50 
_refine.ls_percent_reflns_obs                    95.4 
_refine.ls_R_factor_obs                          0.1110000 
_refine.ls_R_factor_all                          0.1150000 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       0.1740000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.0 
_refine.ls_number_reflns_R_free                  4812 
_refine.ls_number_parameters                     27377 
_refine.ls_number_restraints                     33057 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.details                                  
;INITIAL POSITIONAL AND B-FACTOR REFINEMENT WAS CARRIED OUT WITH X-PLOR (BRUNGER, 1992) FOR DATA IN THE RESOLUTION RANGE 7.0 - 1.5 ANGSTROMS. AT R-VALUES OF R=0.174 FOR F.GREATER THAN 3 SIGMA(F), THE REFINEMENT WAS CONTINUED WITH THE PROGRAM SHELXL-93.

ANISOU RECORDS CONTAIN ANISOTROPIC DISPLACEMENT PARAMETERS
U11 U22 U33 U23 U13 U12 (ANGSTROMS**2) MULTIPLIED BY 10000.
ISOTROPIC EQUIVALENTS OF ANISOTROPIC TEMPERATURE FACTORS
ARE ALSO PRESENTED IN THIS ENTRY.
;
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'ENGH AND HUBER' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            'EVERY 10TH REFLECTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1A2P 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      10 
_refine_analyze.occupancy_sum_hydrogen          2417.5 
_refine_analyze.occupancy_sum_non_hydrogen      2972.0 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2624 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         3 
_refine_hist.number_atoms_solvent             415 
_refine_hist.number_atoms_total               3042 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        8.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d               0.013 ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d              1.76  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_dist         ?     ? ? ? 'X-RAY DIFFRACTION' ? 
s_from_restr_planes    ?     ? ? ? 'X-RAY DIFFRACTION' ? 
s_zero_chiral_vol      0.273 ? ? ? 'X-RAY DIFFRACTION' ? 
s_non_zero_chiral_vol  0.200 ? ? ? 'X-RAY DIFFRACTION' ? 
s_anti_bump_dis_restr  0.100 ? ? ? 'X-RAY DIFFRACTION' ? 
s_rigid_bond_adp_cmpnt 0.010 ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_adp_cmpnt    0.064 ? ? ? 'X-RAY DIFFRACTION' ? 
s_approx_iso_adps      0.100 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_refine.entry_id                                    1A2P 
_pdbx_refine.R_factor_all_no_cutoff                      0.1150000 
_pdbx_refine.R_factor_obs_no_cutoff                      0.1110000 
_pdbx_refine.free_R_factor_no_cutoff                     0.1740000 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     10.0 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            4812 
_pdbx_refine.R_factor_all_4sig_cutoff                    0.1110000 
_pdbx_refine.R_factor_obs_4sig_cutoff                    ? 
_pdbx_refine.free_R_factor_4sig_cutoff                   ? 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   ? 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          ? 
_pdbx_refine.number_reflns_obs_4sig_cutoff               44595 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? 0.757790 0.647480 0.080780 0.646210 -0.761860 0.044460 0.090330 0.018510 -0.995740 -58.48021 51.57518 98.15767 
2 given ? 0.589870 0.805830 0.051860 0.803110 -0.592140 0.066190 0.084050 0.002600 -0.996460 -30.43273 20.75484 81.77702 
# 
_struct.entry_id                  1A2P 
_struct.title                     'BARNASE WILDTYPE STRUCTURE AT 1.5 ANGSTROMS RESOLUTION' 
_struct.pdbx_descriptor           BARNASE 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1A2P 
_struct_keywords.pdbx_keywords   RIBONUCLEASE 
_struct_keywords.text            'RIBONUCLEASE, MICROBIAL RIBONUCLEASE, ALPHA/BETA PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
loop_
_struct_biol.id 
1 
2 
3 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  PHE A 7  ? TYR A 17 ? PHE A 7  TYR A 17 1 ? 11 
HELX_P HELX_P2  2  LYS A 27 ? LEU A 33 ? LYS A 27 LEU A 33 1 ? 7  
HELX_P HELX_P3  3  ALA A 37 ? LYS A 39 ? ALA A 37 LYS A 39 5 ? 3  
HELX_P HELX_P4  4  LEU A 42 ? VAL A 45 ? LEU A 42 VAL A 45 1 ? 4  
HELX_P HELX_P5  5  PHE B 7  ? TYR B 17 ? PHE B 7  TYR B 17 1 ? 11 
HELX_P HELX_P6  6  LYS B 27 ? LEU B 33 ? LYS B 27 LEU B 33 1 ? 7  
HELX_P HELX_P7  7  ALA B 37 ? LYS B 39 ? ALA B 37 LYS B 39 5 ? 3  
HELX_P HELX_P8  8  LEU B 42 ? VAL B 45 ? LEU B 42 VAL B 45 1 ? 4  
HELX_P HELX_P9  9  PHE C 7  ? TYR C 17 ? PHE C 7  TYR C 17 1 ? 11 
HELX_P HELX_P10 10 LYS C 27 ? LEU C 33 ? LYS C 27 LEU C 33 1 ? 7  
HELX_P HELX_P11 11 ALA C 37 ? LYS C 39 ? ALA C 37 LYS C 39 5 ? 3  
HELX_P HELX_P12 12 LEU C 42 ? VAL C 45 ? LEU C 42 VAL C 45 1 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1  metalc ? ? D ZN . ZN ? ? ? 1_555 A HIS 18 ND1 ? ? A ZN 112 A HIS 18  1_555 ? ? ? ? ? ? ? 2.360 ? 
metalc2  metalc ? ? E ZN . ZN ? ? ? 1_555 B GLU 60 OE1 ? ? B ZN 112 B GLU 60  1_555 ? ? ? ? ? ? ? 2.251 ? 
metalc3  metalc ? ? E ZN . ZN ? ? ? 1_555 B GLU 60 OE2 ? ? B ZN 112 B GLU 60  1_555 ? ? ? ? ? ? ? 2.324 ? 
metalc4  metalc ? ? F ZN . ZN ? ? ? 1_555 C GLU 60 OE1 ? ? C ZN 112 C GLU 60  1_555 ? ? ? ? ? ? ? 2.319 ? 
metalc5  metalc ? ? F ZN . ZN ? ? ? 1_555 C GLU 60 OE2 ? ? C ZN 112 C GLU 60  1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc6  metalc ? ? F ZN . ZN ? ? ? 1_555 C LYS 62 NZ  ? ? C ZN 112 C LYS 62  1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc7  metalc ? ? D ZN . ZN ? ? ? 1_555 G HOH .  O   ? ? A ZN 112 A HOH 227 1_555 ? ? ? ? ? ? ? 2.247 ? 
metalc8  metalc ? ? E ZN . ZN ? ? ? 1_555 H HOH .  O   ? ? B ZN 112 B HOH 260 1_555 ? ? ? ? ? ? ? 2.424 ? 
metalc9  metalc ? ? F ZN . ZN ? ? ? 1_555 I HOH .  O   ? ? C ZN 112 C HOH 139 1_555 ? ? ? ? ? ? ? 1.994 ? 
metalc10 metalc ? ? D ZN . ZN ? ? ? 1_555 A GLU 60 OE2 ? ? A ZN 112 A GLU 60  3_675 ? ? ? ? ? ? ? 2.214 ? 
metalc11 metalc ? ? E ZN . ZN ? ? ? 1_555 B HIS 18 ND1 ? ? B ZN 112 B HIS 18  3_565 ? ? ? ? ? ? ? 2.211 ? 
metalc12 metalc ? ? F ZN . ZN ? ? ? 1_555 C HIS 18 ND1 ? ? C ZN 112 C HIS 18  3_665 ? ? ? ? ? ? ? 2.059 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 4 ? 
C ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 96 ? THR A 99 ? ILE A 96 THR A 99 
A 2 ARG A 87 ? SER A 91 ? ARG A 87 SER A 91 
A 3 TRP A 71 ? ASP A 75 ? TRP A 71 ASP A 75 
A 4 GLY A 52 ? ILE A 55 ? GLY A 52 ILE A 55 
B 1 ILE B 96 ? THR B 99 ? ILE B 96 THR B 99 
B 2 ARG B 87 ? SER B 91 ? ARG B 87 SER B 91 
B 3 TRP B 71 ? ASP B 75 ? TRP B 71 ASP B 75 
B 4 GLY B 52 ? PHE B 56 ? GLY B 52 PHE B 56 
C 1 ILE C 96 ? THR C 99 ? ILE C 96 THR C 99 
C 2 ARG C 87 ? SER C 91 ? ARG C 87 SER C 91 
C 3 TRP C 71 ? ASP C 75 ? TRP C 71 ASP C 75 
C 4 GLY C 52 ? ILE C 55 ? GLY C 52 ILE C 55 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O TYR A 97 ? O TYR A 97 N LEU A 89 ? N LEU A 89 
A 2 3 O ILE A 88 ? O ILE A 88 N ALA A 74 ? N ALA A 74 
A 3 4 O GLU A 73 ? O GLU A 73 N ASP A 54 ? N ASP A 54 
B 1 2 O TYR B 97 ? O TYR B 97 N LEU B 89 ? N LEU B 89 
B 2 3 O ILE B 88 ? O ILE B 88 N ALA B 74 ? N ALA B 74 
B 3 4 O TRP B 71 ? O TRP B 71 N PHE B 56 ? N PHE B 56 
C 1 2 O TYR C 97 ? O TYR C 97 N LEU C 89 ? N LEU C 89 
C 2 3 O ILE C 88 ? O ILE C 88 N ALA C 74 ? N ALA C 74 
C 3 4 O GLU C 73 ? O GLU C 73 N ASP C 54 ? N ASP C 54 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 112' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 112' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 112' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 18 ? HIS A 18  . ? 1_555 ? 
2  AC1 4 GLU A 60 ? GLU A 60  . ? 3_675 ? 
3  AC1 4 LYS A 62 ? LYS A 62  . ? 3_675 ? 
4  AC1 4 HOH G .  ? HOH A 227 . ? 1_555 ? 
5  AC2 4 HIS B 18 ? HIS B 18  . ? 3_565 ? 
6  AC2 4 GLU B 60 ? GLU B 60  . ? 1_555 ? 
7  AC2 4 LYS B 62 ? LYS B 62  . ? 1_555 ? 
8  AC2 4 HOH H .  ? HOH B 260 . ? 1_555 ? 
9  AC3 4 HIS C 18 ? HIS C 18  . ? 3_665 ? 
10 AC3 4 GLU C 60 ? GLU C 60  . ? 1_555 ? 
11 AC3 4 LYS C 62 ? LYS C 62  . ? 1_555 ? 
12 AC3 4 HOH I .  ? HOH C 139 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1A2P 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1A2P 
_atom_sites.fract_transf_matrix[1][1]   0.016958 
_atom_sites.fract_transf_matrix[1][2]   0.009791 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019581 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.012258 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL A 1 3   ? 16.875  37.901 43.478 1.00 47.79 ? 3   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 3   ? 17.997  38.577 42.795 1.00 41.49 ? 3   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 3   ? 18.147  39.997 43.309 1.00 34.47 ? 3   VAL A C   1 
ATOM   4    O  O   . VAL A 1 3   ? 17.180  40.763 43.281 1.00 34.84 ? 3   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 3   ? 17.786  38.593 41.279 1.00 42.12 ? 3   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 3   ? 18.621  39.606 40.573 1.00 38.29 ? 3   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 3   ? 18.024  37.190 40.696 1.00 45.14 ? 3   VAL A CG2 1 
ATOM   8    N  N   . ILE A 1 4   ? 19.355  40.377 43.690 1.00 27.18 ? 4   ILE A N   1 
ATOM   9    C  CA  . ILE A 1 4   ? 19.568  41.805 44.109 1.00 24.08 ? 4   ILE A CA  1 
ATOM   10   C  C   . ILE A 1 4   ? 20.355  42.488 42.992 1.00 21.31 ? 4   ILE A C   1 
ATOM   11   O  O   . ILE A 1 4   ? 21.489  42.115 42.701 1.00 21.63 ? 4   ILE A O   1 
ATOM   12   C  CB  . ILE A 1 4   ? 20.430  41.800 45.396 1.00 24.83 ? 4   ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 4   ? 19.774  40.976 46.525 1.00 27.01 ? 4   ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 4   ? 20.779  43.192 45.823 1.00 24.93 ? 4   ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 4   ? 20.598  40.921 47.787 1.00 33.25 ? 4   ILE A CD1 1 
ATOM   16   N  N   . ASN A 1 5   ? 19.676  43.364 42.248 1.00 20.12 ? 5   ASN A N   1 
ATOM   17   C  CA  . ASN A 1 5   ? 20.308  43.996 41.102 1.00 19.67 ? 5   ASN A CA  1 
ATOM   18   C  C   . ASN A 1 5   ? 19.925  45.450 40.923 1.00 17.24 ? 5   ASN A C   1 
ATOM   19   O  O   . ASN A 1 5   ? 20.142  45.981 39.825 1.00 17.10 ? 5   ASN A O   1 
ATOM   20   C  CB  . ASN A 1 5   ? 20.074  43.224 39.803 1.00 20.04 ? 5   ASN A CB  1 
ATOM   21   C  CG  . ASN A 1 5   ? 18.623  43.365 39.320 1.00 20.89 ? 5   ASN A CG  1 
ATOM   22   O  OD1 . ASN A 1 5   ? 17.758  43.768 40.083 1.00 21.76 ? 5   ASN A OD1 1 
ATOM   23   N  ND2 . ASN A 1 5   ? 18.405  43.073 38.050 1.00 22.93 ? 5   ASN A ND2 1 
ATOM   24   N  N   . THR A 1 6   ? 19.502  46.115 41.979 1.00 15.82 ? 6   THR A N   1 
ATOM   25   C  CA  . THR A 1 6   ? 19.178  47.556 41.906 1.00 16.81 ? 6   THR A CA  1 
ATOM   26   C  C   . THR A 1 6   ? 20.299  48.405 42.457 1.00 14.04 ? 6   THR A C   1 
ATOM   27   O  O   . THR A 1 6   ? 21.154  47.941 43.191 1.00 14.38 ? 6   THR A O   1 
ATOM   28   C  CB  . THR A 1 6   ? 17.889  47.828 42.737 1.00 17.16 ? 6   THR A CB  1 
ATOM   29   O  OG1 . THR A 1 6   ? 18.098  47.384 44.059 1.00 23.19 ? 6   THR A OG1 1 
ATOM   30   C  CG2 . THR A 1 6   ? 16.696  47.101 42.162 1.00 22.55 ? 6   THR A CG2 1 
ATOM   31   N  N   . PHE A 1 7   ? 20.276  49.727 42.144 1.00 14.44 ? 7   PHE A N   1 
ATOM   32   C  CA  . PHE A 1 7   ? 21.281  50.600 42.712 1.00 14.94 ? 7   PHE A CA  1 
ATOM   33   C  C   . PHE A 1 7   ? 21.304  50.540 44.237 1.00 15.96 ? 7   PHE A C   1 
ATOM   34   O  O   . PHE A 1 7   ? 22.364  50.392 44.837 1.00 15.42 ? 7   PHE A O   1 
ATOM   35   C  CB  . PHE A 1 7   ? 21.193  52.025 42.242 1.00 15.65 ? 7   PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 7   ? 21.669  52.260 40.821 1.00 15.01 ? 7   PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 7   ? 23.019  52.178 40.526 1.00 15.42 ? 7   PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 7   ? 20.801  52.613 39.818 1.00 15.77 ? 7   PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 7   ? 23.466  52.380 39.234 1.00 17.19 ? 7   PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 7   ? 21.231  52.736 38.512 1.00 16.36 ? 7   PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 7   ? 22.588  52.649 38.217 1.00 16.36 ? 7   PHE A CZ  1 
ATOM   42   N  N   . ASP A 1 8   ? 20.153  50.663 44.861 1.00 16.64 ? 8   ASP A N   1 
ATOM   43   C  CA  . ASP A 1 8   ? 20.096  50.718 46.322 1.00 15.99 ? 8   ASP A CA  1 
ATOM   44   C  C   . ASP A 1 8   ? 20.397  49.363 46.940 1.00 17.56 ? 8   ASP A C   1 
ATOM   45   O  O   . ASP A 1 8   ? 21.150  49.259 47.909 1.00 16.79 ? 8   ASP A O   1 
ATOM   46   C  CB  . ASP A 1 8   ? 18.756  51.282 46.783 1.00 17.03 ? 8   ASP A CB  1 
ATOM   47   C  CG  . ASP A 1 8   ? 18.706  52.795 46.591 1.00 20.95 ? 8   ASP A CG  1 
ATOM   48   O  OD1 . ASP A 1 8   ? 19.571  53.503 47.112 1.00 21.91 ? 8   ASP A OD1 1 
ATOM   49   O  OD2 . ASP A 1 8   ? 17.795  53.254 45.873 1.00 22.61 ? 8   ASP A OD2 1 
ATOM   50   N  N   . GLY A 1 9   ? 19.913  48.292 46.302 1.00 18.86 ? 9   GLY A N   1 
ATOM   51   C  CA  . GLY A 1 9   ? 20.126  46.945 46.826 1.00 20.19 ? 9   GLY A CA  1 
ATOM   52   C  C   . GLY A 1 9   ? 21.580  46.537 46.842 1.00 18.58 ? 9   GLY A C   1 
ATOM   53   O  O   . GLY A 1 9   ? 22.105  46.026 47.839 1.00 19.40 ? 9   GLY A O   1 
ATOM   54   N  N   . VAL A 1 10  ? 22.248  46.736 45.696 1.00 16.97 ? 10  VAL A N   1 
ATOM   55   C  CA  . VAL A 1 10  ? 23.649  46.415 45.562 1.00 16.53 ? 10  VAL A CA  1 
ATOM   56   C  C   . VAL A 1 10  ? 24.524  47.334 46.400 1.00 15.21 ? 10  VAL A C   1 
ATOM   57   O  O   . VAL A 1 10  ? 25.443  46.858 47.074 1.00 15.57 ? 10  VAL A O   1 
ATOM   58   C  CB  . VAL A 1 10  ? 24.087  46.345 44.109 1.00 15.47 ? 10  VAL A CB  1 
ATOM   59   C  CG1 . VAL A 1 10  ? 25.562  45.981 43.977 1.00 16.57 ? 10  VAL A CG1 1 
ATOM   60   C  CG2 . VAL A 1 10  ? 23.226  45.294 43.368 1.00 17.03 ? 10  VAL A CG2 1 
ATOM   61   N  N   . ALA A 1 11  ? 24.256  48.622 46.409 1.00 15.54 ? 11  ALA A N   1 
ATOM   62   C  CA  . ALA A 1 11  ? 25.065  49.567 47.199 1.00 13.83 ? 11  ALA A CA  1 
ATOM   63   C  C   . ALA A 1 11  ? 25.039  49.171 48.677 1.00 18.78 ? 11  ALA A C   1 
ATOM   64   O  O   . ALA A 1 11  ? 26.051  49.157 49.362 1.00 18.74 ? 11  ALA A O   1 
ATOM   65   C  CB  . ALA A 1 11  ? 24.464  50.973 47.068 1.00 15.91 ? 11  ALA A CB  1 
ATOM   66   N  N   . ASP A 1 12  ? 23.834  48.873 49.177 1.00 19.06 ? 12  ASP A N   1 
ATOM   67   C  CA  . ASP A 1 12  ? 23.726  48.524 50.582 1.00 22.03 ? 12  ASP A CA  1 
ATOM   68   C  C   . ASP A 1 12  ? 24.334  47.159 50.888 1.00 23.78 ? 12  ASP A C   1 
ATOM   69   O  O   . ASP A 1 12  ? 24.933  46.981 51.939 1.00 22.94 ? 12  ASP A O   1 
ATOM   70   C  CB  . ASP A 1 12  ? 22.315  48.609 51.112 1.00 22.28 ? 12  ASP A CB  1 
ATOM   71   C  CG  . ASP A 1 12  ? 21.807  50.042 51.271 1.00 22.67 ? 12  ASP A CG  1 
ATOM   72   O  OD1 . ASP A 1 12  ? 22.633  50.960 51.336 1.00 26.27 ? 12  ASP A OD1 1 
ATOM   73   O  OD2 . ASP A 1 12  ? 20.584  50.220 51.156 1.00 25.64 ? 12  ASP A OD2 1 
ATOM   74   N  N   . TYR A 1 13  ? 24.253  46.232 49.937 1.00 22.66 ? 13  TYR A N   1 
ATOM   75   C  CA  . TYR A 1 13  ? 24.888  44.902 50.143 1.00 22.08 ? 13  TYR A CA  1 
ATOM   76   C  C   . TYR A 1 13  ? 26.393  45.040 50.199 1.00 22.77 ? 13  TYR A C   1 
ATOM   77   O  O   . TYR A 1 13  ? 27.049  44.481 51.062 1.00 23.52 ? 13  TYR A O   1 
ATOM   78   C  CB  . TYR A 1 13  ? 24.434  43.966 49.031 1.00 22.78 ? 13  TYR A CB  1 
ATOM   79   C  CG  . TYR A 1 13  ? 24.753  42.512 49.244 1.00 25.55 ? 13  TYR A CG  1 
ATOM   80   C  CD1 . TYR A 1 13  ? 26.033  41.994 49.022 1.00 25.49 ? 13  TYR A CD1 1 
ATOM   81   C  CD2 . TYR A 1 13  ? 23.762  41.624 49.621 1.00 29.01 ? 13  TYR A CD2 1 
ATOM   82   C  CE1 . TYR A 1 13  ? 26.295  40.649 49.212 1.00 27.24 ? 13  TYR A CE1 1 
ATOM   83   C  CE2 . TYR A 1 13  ? 24.019  40.283 49.832 1.00 31.36 ? 13  TYR A CE2 1 
ATOM   84   C  CZ  . TYR A 1 13  ? 25.295  39.800 49.601 1.00 30.49 ? 13  TYR A CZ  1 
ATOM   85   O  OH  . TYR A 1 13  ? 25.535  38.473 49.847 1.00 34.08 ? 13  TYR A OH  1 
ATOM   86   N  N   . LEU A 1 14  ? 26.983  45.832 49.302 1.00 23.45 ? 14  LEU A N   1 
ATOM   87   C  CA  . LEU A 1 14  ? 28.432  46.024 49.278 1.00 23.42 ? 14  LEU A CA  1 
ATOM   88   C  C   . LEU A 1 14  ? 28.948  46.628 50.562 1.00 22.83 ? 14  LEU A C   1 
ATOM   89   O  O   . LEU A 1 14  ? 29.991  46.250 51.112 1.00 23.07 ? 14  LEU A O   1 
ATOM   90   C  CB  . LEU A 1 14  ? 28.776  47.001 48.100 1.00 22.33 ? 14  LEU A CB  1 
ATOM   91   C  CG  . LEU A 1 14  ? 28.713  46.343 46.707 1.00 22.65 ? 14  LEU A CG  1 
ATOM   92   C  CD1 . LEU A 1 14  ? 28.674  47.413 45.615 1.00 21.22 ? 14  LEU A CD1 1 
ATOM   93   C  CD2 . LEU A 1 14  ? 29.926  45.426 46.535 1.00 22.24 ? 14  LEU A CD2 1 
ATOM   94   N  N   . GLN A 1 15  ? 28.274  47.685 51.058 1.00 23.85 ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 28.831  48.366 52.222 1.00 25.55 ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 28.710  47.530 53.484 1.00 27.95 ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 29.341  47.874 54.492 1.00 33.34 ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 28.183  49.734 52.409 1.00 23.08 ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 28.612  50.746 51.359 1.00 22.31 ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 28.340  52.167 51.799 1.00 21.02 ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 27.246  52.494 52.266 1.00 22.24 ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 29.303  53.040 51.577 1.00 19.61 ? 15  GLN A NE2 1 
ATOM   103  N  N   . THR A 1 16  ? 27.874  46.515 53.446 1.00 31.82 ? 16  THR A N   1 
ATOM   104  C  CA  . THR A 1 16  ? 27.596  45.638 54.566 1.00 32.67 ? 16  THR A CA  1 
ATOM   105  C  C   . THR A 1 16  ? 28.441  44.368 54.534 1.00 33.16 ? 16  THR A C   1 
ATOM   106  O  O   . THR A 1 16  ? 28.986  44.005 55.591 1.00 32.28 ? 16  THR A O   1 
ATOM   107  C  CB  . THR A 1 16  ? 26.099  45.203 54.585 1.00 34.89 ? 16  THR A CB  1 
ATOM   108  O  OG1 . THR A 1 16  ? 25.296  46.396 54.726 1.00 39.32 ? 16  THR A OG1 1 
ATOM   109  C  CG2 . THR A 1 16  ? 25.823  44.320 55.792 1.00 38.07 ? 16  THR A CG2 1 
ATOM   110  N  N   . TYR A 1 17  ? 28.487  43.698 53.397 1.00 27.51 ? 17  TYR A N   1 
ATOM   111  C  CA  . TYR A 1 17  ? 29.085  42.372 53.251 1.00 27.26 ? 17  TYR A CA  1 
ATOM   112  C  C   . TYR A 1 17  ? 30.474  42.451 52.595 1.00 26.76 ? 17  TYR A C   1 
ATOM   113  O  O   . TYR A 1 17  ? 31.179  41.423 52.554 1.00 27.90 ? 17  TYR A O   1 
ATOM   114  C  CB  . TYR A 1 17  ? 28.210  41.506 52.345 1.00 31.07 ? 17  TYR A CB  1 
ATOM   115  C  CG  . TYR A 1 17  ? 26.935  41.007 52.932 1.00 34.48 ? 17  TYR A CG  1 
ATOM   116  C  CD1 . TYR A 1 17  ? 25.781  41.773 52.971 1.00 36.48 ? 17  TYR A CD1 1 
ATOM   117  C  CD2 . TYR A 1 17  ? 26.869  39.692 53.411 0.30 36.61 ? 17  TYR A CD2 1 
ATOM   118  C  CE1 . TYR A 1 17  ? 24.608  41.263 53.516 1.00 39.05 ? 17  TYR A CE1 1 
ATOM   119  C  CE2 . TYR A 1 17  ? 25.713  39.187 53.946 0.80 39.75 ? 17  TYR A CE2 1 
ATOM   120  C  CZ  . TYR A 1 17  ? 24.580  39.978 53.997 0.50 39.88 ? 17  TYR A CZ  1 
ATOM   121  O  OH  . TYR A 1 17  ? 23.425  39.438 54.532 0.50 41.76 ? 17  TYR A OH  1 
ATOM   122  N  N   . HIS A 1 18  ? 30.790  43.584 52.015 1.00 24.69 ? 18  HIS A N   1 
ATOM   123  C  CA  . HIS A 1 18  ? 32.077  43.832 51.377 1.00 25.26 ? 18  HIS A CA  1 
ATOM   124  C  C   . HIS A 1 18  ? 32.339  42.866 50.238 1.00 23.85 ? 18  HIS A C   1 
ATOM   125  O  O   . HIS A 1 18  ? 33.477  42.490 49.976 1.00 26.01 ? 18  HIS A O   1 
ATOM   126  C  CB  . HIS A 1 18  ? 33.224  43.797 52.400 1.00 26.85 ? 18  HIS A CB  1 
ATOM   127  C  CG  . HIS A 1 18  ? 32.991  44.748 53.538 1.00 25.45 ? 18  HIS A CG  1 
ATOM   128  N  ND1 . HIS A 1 18  ? 33.016  44.372 54.853 1.00 23.27 ? 18  HIS A ND1 1 
ATOM   129  C  CD2 . HIS A 1 18  ? 32.614  46.056 53.525 1.00 26.66 ? 18  HIS A CD2 1 
ATOM   130  C  CE1 . HIS A 1 18  ? 32.701  45.402 55.613 1.00 24.47 ? 18  HIS A CE1 1 
ATOM   131  N  NE2 . HIS A 1 18  ? 32.446  46.439 54.820 1.00 24.12 ? 18  HIS A NE2 1 
ATOM   132  N  N   . LYS A 1 19  ? 31.258  42.503 49.554 1.00 22.82 ? 19  LYS A N   1 
ATOM   133  C  CA  . LYS A 1 19  ? 31.246  41.624 48.419 1.00 23.19 ? 19  LYS A CA  1 
ATOM   134  C  C   . LYS A 1 19  ? 29.982  41.803 47.599 1.00 23.98 ? 19  LYS A C   1 
ATOM   135  O  O   . LYS A 1 19  ? 28.964  42.309 48.081 1.00 22.78 ? 19  LYS A O   1 
ATOM   136  C  CB  . LYS A 1 19  ? 31.427  40.158 48.846 1.00 26.82 ? 19  LYS A CB  1 
ATOM   137  C  CG  . LYS A 1 19  ? 30.255  39.568 49.598 1.00 32.80 ? 19  LYS A CG  1 
ATOM   138  C  CD  . LYS A 1 19  ? 30.350  38.057 49.730 1.00 36.90 ? 19  LYS A CD  1 
ATOM   139  C  CE  . LYS A 1 19  ? 30.031  37.589 51.127 1.00 40.46 ? 19  LYS A CE  1 
ATOM   140  N  NZ  . LYS A 1 19  ? 28.765  36.817 51.229 1.00 53.44 ? 19  LYS A NZ  1 
ATOM   141  N  N   . LEU A 1 20  ? 30.025  41.352 46.333 1.00 21.22 ? 20  LEU A N   1 
ATOM   142  C  CA  . LEU A 1 20  ? 28.790  41.406 45.543 1.00 22.01 ? 20  LEU A CA  1 
ATOM   143  C  C   . LEU A 1 20  ? 27.888  40.236 45.925 1.00 21.56 ? 20  LEU A C   1 
ATOM   144  O  O   . LEU A 1 20  ? 28.354  39.167 46.348 1.00 23.54 ? 20  LEU A O   1 
ATOM   145  C  CB  . LEU A 1 20  ? 29.126  41.320 44.048 1.00 21.19 ? 20  LEU A CB  1 
ATOM   146  C  CG  . LEU A 1 20  ? 29.642  42.585 43.377 1.00 19.63 ? 20  LEU A CG  1 
ATOM   147  C  CD1 . LEU A 1 20  ? 30.254  42.256 42.019 1.00 19.39 ? 20  LEU A CD1 1 
ATOM   148  C  CD2 . LEU A 1 20  ? 28.602  43.669 43.278 1.00 19.28 ? 20  LEU A CD2 1 
ATOM   149  N  N   . PRO A 1 21  ? 26.581  40.396 45.744 1.00 22.14 ? 21  PRO A N   1 
ATOM   150  C  CA  . PRO A 1 21  ? 25.700  39.233 45.951 1.00 23.89 ? 21  PRO A CA  1 
ATOM   151  C  C   . PRO A 1 21  ? 26.038  38.117 44.946 1.00 24.39 ? 21  PRO A C   1 
ATOM   152  O  O   . PRO A 1 21  ? 26.682  38.344 43.922 1.00 22.07 ? 21  PRO A O   1 
ATOM   153  C  CB  . PRO A 1 21  ? 24.318  39.780 45.660 1.00 24.15 ? 21  PRO A CB  1 
ATOM   154  C  CG  . PRO A 1 21  ? 24.423  41.205 45.399 1.00 22.98 ? 21  PRO A CG  1 
ATOM   155  C  CD  . PRO A 1 21  ? 25.844  41.604 45.381 1.00 21.56 ? 21  PRO A CD  1 
ATOM   156  N  N   . ASP A 1 22  ? 25.537  36.929 45.226 1.00 24.36 ? 22  ASP A N   1 
ATOM   157  C  CA  . ASP A 1 22  ? 25.684  35.718 44.532 1.00 25.88 ? 22  ASP A CA  1 
ATOM   158  C  C   . ASP A 1 22  ? 25.255  35.639 43.099 1.00 23.95 ? 22  ASP A C   1 
ATOM   159  O  O   . ASP A 1 22  ? 25.589  34.678 42.364 1.00 28.97 ? 22  ASP A O   1 
ATOM   160  C  CB  . ASP A 1 22  ? 25.126  34.524 45.338 1.00 33.00 ? 22  ASP A CB  1 
ATOM   161  C  CG  . ASP A 1 22  ? 23.611  34.477 45.288 1.00 39.47 ? 22  ASP A CG  1 
ATOM   162  O  OD1 . ASP A 1 22  ? 23.063  34.652 44.164 0.50 40.60 ? 22  ASP A OD1 1 
ATOM   163  O  OD2 . ASP A 1 22  ? 22.968  34.271 46.324 0.50 48.30 ? 22  ASP A OD2 1 
ATOM   164  N  N   . ASN A 1 23  ? 24.443  36.574 42.625 1.00 23.62 ? 23  ASN A N   1 
ATOM   165  C  CA  . ASN A 1 23  ? 23.982  36.568 41.258 1.00 22.51 ? 23  ASN A CA  1 
ATOM   166  C  C   . ASN A 1 23  ? 24.969  37.232 40.305 1.00 22.21 ? 23  ASN A C   1 
ATOM   167  O  O   . ASN A 1 23  ? 24.660  37.348 39.116 1.00 22.47 ? 23  ASN A O   1 
ATOM   168  C  CB  . ASN A 1 23  ? 22.615  37.236 41.119 1.00 24.11 ? 23  ASN A CB  1 
ATOM   169  C  CG  . ASN A 1 23  ? 22.598  38.628 41.742 1.00 24.25 ? 23  ASN A CG  1 
ATOM   170  O  OD1 . ASN A 1 23  ? 22.844  38.720 42.951 1.00 27.96 ? 23  ASN A OD1 1 
ATOM   171  N  ND2 . ASN A 1 23  ? 22.343  39.657 40.983 1.00 24.60 ? 23  ASN A ND2 1 
ATOM   172  N  N   . TYR A 1 24  ? 26.138  37.653 40.787 1.00 19.12 ? 24  TYR A N   1 
ATOM   173  C  CA  . TYR A 1 24  ? 27.133  38.257 39.920 1.00 16.78 ? 24  TYR A CA  1 
ATOM   174  C  C   . TYR A 1 24  ? 28.235  37.285 39.514 1.00 18.03 ? 24  TYR A C   1 
ATOM   175  O  O   . TYR A 1 24  ? 28.753  36.520 40.340 1.00 19.18 ? 24  TYR A O   1 
ATOM   176  C  CB  . TYR A 1 24  ? 27.744  39.502 40.622 1.00 15.70 ? 24  TYR A CB  1 
ATOM   177  C  CG  . TYR A 1 24  ? 26.814  40.701 40.551 1.00 14.38 ? 24  TYR A CG  1 
ATOM   178  C  CD1 . TYR A 1 24  ? 26.745  41.501 39.415 1.00 13.39 ? 24  TYR A CD1 1 
ATOM   179  C  CD2 . TYR A 1 24  ? 25.939  41.003 41.587 1.00 14.54 ? 24  TYR A CD2 1 
ATOM   180  C  CE1 . TYR A 1 24  ? 25.886  42.578 39.322 1.00 13.84 ? 24  TYR A CE1 1 
ATOM   181  C  CE2 . TYR A 1 24  ? 25.036  42.054 41.483 1.00 14.96 ? 24  TYR A CE2 1 
ATOM   182  C  CZ  . TYR A 1 24  ? 25.006  42.833 40.357 1.00 13.51 ? 24  TYR A CZ  1 
ATOM   183  O  OH  . TYR A 1 24  ? 24.134  43.905 40.274 1.00 14.50 ? 24  TYR A OH  1 
ATOM   184  N  N   . ILE A 1 25  ? 28.650  37.354 38.259 1.00 16.05 ? 25  ILE A N   1 
ATOM   185  C  CA  . ILE A 1 25  ? 29.846  36.674 37.770 1.00 17.22 ? 25  ILE A CA  1 
ATOM   186  C  C   . ILE A 1 25  ? 30.745  37.629 37.016 1.00 16.20 ? 25  ILE A C   1 
ATOM   187  O  O   . ILE A 1 25  ? 30.260  38.631 36.451 1.00 16.75 ? 25  ILE A O   1 
ATOM   188  C  CB  . ILE A 1 25  ? 29.468  35.478 36.849 1.00 18.23 ? 25  ILE A CB  1 
ATOM   189  C  CG1 . ILE A 1 25  ? 28.563  35.946 35.693 1.00 18.49 ? 25  ILE A CG1 1 
ATOM   190  C  CG2 . ILE A 1 25  ? 28.761  34.434 37.706 1.00 21.88 ? 25  ILE A CG2 1 
ATOM   191  C  CD1 . ILE A 1 25  ? 28.230  34.794 34.745 1.00 19.54 ? 25  ILE A CD1 1 
ATOM   192  N  N   . THR A 1 26  ? 32.039  37.346 36.928 1.00 17.56 ? 26  THR A N   1 
ATOM   193  C  CA  . THR A 1 26  ? 32.931  38.271 36.209 1.00 19.93 ? 26  THR A CA  1 
ATOM   194  C  C   . THR A 1 26  ? 32.806  38.054 34.703 1.00 16.65 ? 26  THR A C   1 
ATOM   195  O  O   . THR A 1 26  ? 32.291  37.035 34.256 1.00 16.79 ? 26  THR A O   1 
ATOM   196  C  CB  . THR A 1 26  ? 34.396  38.073 36.601 1.00 19.08 ? 26  THR A CB  1 
ATOM   197  O  OG1 . THR A 1 26  ? 34.810  36.757 36.189 1.00 21.28 ? 26  THR A OG1 1 
ATOM   198  C  CG2 . THR A 1 26  ? 34.610  38.189 38.089 1.00 23.10 ? 26  THR A CG2 1 
ATOM   199  N  N   . LYS A 1 27  ? 33.385  38.997 33.926 1.00 16.97 ? 27  LYS A N   1 
ATOM   200  C  CA  . LYS A 1 27  ? 33.330  38.851 32.466 1.00 16.09 ? 27  LYS A CA  1 
ATOM   201  C  C   . LYS A 1 27  ? 34.018  37.561 32.017 1.00 16.03 ? 27  LYS A C   1 
ATOM   202  O  O   . LYS A 1 27  ? 33.513  36.901 31.116 1.00 17.02 ? 27  LYS A O   1 
ATOM   203  C  CB  . LYS A 1 27  ? 33.950  40.054 31.747 1.00 18.54 ? 27  LYS A CB  1 
ATOM   204  C  CG  . LYS A 1 27  ? 33.018  41.264 31.660 1.00 24.27 ? 27  LYS A CG  1 
ATOM   205  C  CD  . LYS A 1 27  ? 33.600  42.351 30.792 1.00 29.19 ? 27  LYS A CD  1 
ATOM   206  C  CE  . LYS A 1 27  ? 34.768  43.056 31.394 1.00 34.13 ? 27  LYS A CE  1 
ATOM   207  N  NZ  . LYS A 1 27  ? 34.448  43.939 32.547 1.00 39.24 ? 27  LYS A NZ  1 
ATOM   208  N  N   . SER A 1 28  ? 35.129  37.202 32.662 1.00 16.57 ? 28  SER A N   1 
ATOM   209  C  CA  . SER A 1 28  ? 35.883  35.991 32.293 1.00 18.89 ? 28  SER A CA  1 
ATOM   210  C  C   . SER A 1 28  ? 35.094  34.731 32.577 1.00 16.17 ? 28  SER A C   1 
ATOM   211  O  O   . SER A 1 28  ? 35.067  33.786 31.794 1.00 17.45 ? 28  SER A O   1 
ATOM   212  C  CB  A SER A 1 28  ? 37.212  35.963 33.077 0.50 20.70 ? 28  SER A CB  1 
ATOM   213  C  CB  B SER A 1 28  ? 37.182  35.960 33.149 0.50 20.32 ? 28  SER A CB  1 
ATOM   214  O  OG  A SER A 1 28  ? 37.920  34.770 32.764 0.50 22.79 ? 28  SER A OG  1 
ATOM   215  O  OG  B SER A 1 28  ? 38.218  36.566 32.408 0.50 28.61 ? 28  SER A OG  1 
ATOM   216  N  N   . GLU A 1 29  ? 34.386  34.742 33.705 1.00 16.57 ? 29  GLU A N   1 
ATOM   217  C  CA  . GLU A 1 29  ? 33.523  33.636 34.065 1.00 15.02 ? 29  GLU A CA  1 
ATOM   218  C  C   . GLU A 1 29  ? 32.356  33.496 33.099 1.00 14.20 ? 29  GLU A C   1 
ATOM   219  O  O   . GLU A 1 29  ? 32.048  32.360 32.668 1.00 13.77 ? 29  GLU A O   1 
ATOM   220  C  CB  . GLU A 1 29  ? 32.998  33.850 35.510 1.00 20.67 ? 29  GLU A CB  1 
ATOM   221  C  CG  . GLU A 1 29  ? 34.124  33.674 36.518 1.00 22.53 ? 29  GLU A CG  1 
ATOM   222  C  CD  . GLU A 1 29  ? 33.610  33.870 37.939 1.00 25.07 ? 29  GLU A CD  1 
ATOM   223  O  OE1 . GLU A 1 29  ? 32.796  34.773 38.162 1.00 24.78 ? 29  GLU A OE1 1 
ATOM   224  O  OE2 . GLU A 1 29  ? 34.078  33.111 38.813 1.00 29.03 ? 29  GLU A OE2 1 
ATOM   225  N  N   . ALA A 1 30  ? 31.756  34.596 32.701 1.00 13.59 ? 30  ALA A N   1 
ATOM   226  C  CA  . ALA A 1 30  ? 30.644  34.567 31.714 1.00 13.09 ? 30  ALA A CA  1 
ATOM   227  C  C   . ALA A 1 30  ? 31.133  34.062 30.380 1.00 11.94 ? 30  ALA A C   1 
ATOM   228  O  O   . ALA A 1 30  ? 30.469  33.238 29.731 1.00 12.45 ? 30  ALA A O   1 
ATOM   229  C  CB  . ALA A 1 30  ? 30.048  35.977 31.611 1.00 12.69 ? 30  ALA A CB  1 
ATOM   230  N  N   . GLN A 1 31  ? 32.280  34.565 29.910 1.00 13.57 ? 31  GLN A N   1 
ATOM   231  C  CA  . GLN A 1 31  ? 32.806  34.074 28.628 1.00 12.83 ? 31  GLN A CA  1 
ATOM   232  C  C   . GLN A 1 31  ? 33.025  32.575 28.662 1.00 13.43 ? 31  GLN A C   1 
ATOM   233  O  O   . GLN A 1 31  ? 32.737  31.881 27.678 1.00 13.31 ? 31  GLN A O   1 
ATOM   234  C  CB  A GLN A 1 31  ? 34.121  34.800 28.298 0.50 14.93 ? 31  GLN A CB  1 
ATOM   235  C  CB  B GLN A 1 31  ? 34.089  34.824 28.267 0.50 14.96 ? 31  GLN A CB  1 
ATOM   236  C  CG  A GLN A 1 31  ? 33.931  36.266 27.895 0.50 18.22 ? 31  GLN A CG  1 
ATOM   237  C  CG  B GLN A 1 31  ? 33.849  36.319 28.007 0.50 19.11 ? 31  GLN A CG  1 
ATOM   238  C  CD  A GLN A 1 31  ? 35.248  37.013 27.794 0.50 21.48 ? 31  GLN A CD  1 
ATOM   239  C  CD  B GLN A 1 31  ? 35.100  37.025 27.530 0.50 22.41 ? 31  GLN A CD  1 
ATOM   240  O  OE1 A GLN A 1 31  ? 36.187  36.774 28.552 0.50 22.62 ? 31  GLN A OE1 1 
ATOM   241  O  OE1 B GLN A 1 31  ? 35.825  36.527 26.657 0.50 22.37 ? 31  GLN A OE1 1 
ATOM   242  N  NE2 A GLN A 1 31  ? 35.376  37.916 26.823 0.50 25.73 ? 31  GLN A NE2 1 
ATOM   243  N  NE2 B GLN A 1 31  ? 35.375  38.209 28.073 0.50 27.83 ? 31  GLN A NE2 1 
ATOM   244  N  N   . ALA A 1 32  ? 33.563  32.060 29.773 1.00 13.39 ? 32  ALA A N   1 
ATOM   245  C  CA  . ALA A 1 32  ? 33.842  30.617 29.829 1.00 14.36 ? 32  ALA A CA  1 
ATOM   246  C  C   . ALA A 1 32  ? 32.565  29.811 29.725 1.00 13.16 ? 32  ALA A C   1 
ATOM   247  O  O   . ALA A 1 32  ? 32.604  28.674 29.197 1.00 13.34 ? 32  ALA A O   1 
ATOM   248  C  CB  . ALA A 1 32  ? 34.696  30.226 30.980 1.00 14.61 ? 32  ALA A CB  1 
ATOM   249  N  N   . LEU A 1 33  ? 31.478  30.300 30.279 1.00 12.44 ? 33  LEU A N   1 
ATOM   250  C  CA  . LEU A 1 33  ? 30.179  29.646 30.226 1.00 12.30 ? 33  LEU A CA  1 
ATOM   251  C  C   . LEU A 1 33  ? 29.500  29.717 28.887 1.00 11.98 ? 33  LEU A C   1 
ATOM   252  O  O   . LEU A 1 33  ? 28.469  29.068 28.637 1.00 14.07 ? 33  LEU A O   1 
ATOM   253  C  CB  . LEU A 1 33  ? 29.243  30.216 31.314 1.00 12.72 ? 33  LEU A CB  1 
ATOM   254  C  CG  . LEU A 1 33  ? 29.512  29.793 32.724 1.00 15.14 ? 33  LEU A CG  1 
ATOM   255  C  CD1 . LEU A 1 33  ? 29.008  30.699 33.798 1.00 16.96 ? 33  LEU A CD1 1 
ATOM   256  C  CD2 . LEU A 1 33  ? 29.096  28.344 32.960 1.00 21.14 ? 33  LEU A CD2 1 
ATOM   257  N  N   . GLY A 1 34  ? 30.010  30.521 27.948 1.00 10.85 ? 34  GLY A N   1 
ATOM   258  C  CA  . GLY A 1 34  ? 29.417  30.655 26.661 1.00 11.10 ? 34  GLY A CA  1 
ATOM   259  C  C   . GLY A 1 34  ? 28.848  32.003 26.308 1.00 9.73  ? 34  GLY A C   1 
ATOM   260  O  O   . GLY A 1 34  ? 28.189  32.125 25.263 1.00 9.98  ? 34  GLY A O   1 
ATOM   261  N  N   . TRP A 1 35  ? 29.019  33.030 27.143 1.00 9.98  ? 35  TRP A N   1 
ATOM   262  C  CA  . TRP A 1 35  ? 28.562  34.368 26.828 1.00 10.03 ? 35  TRP A CA  1 
ATOM   263  C  C   . TRP A 1 35  ? 29.345  34.918 25.618 1.00 9.77  ? 35  TRP A C   1 
ATOM   264  O  O   . TRP A 1 35  ? 30.561  34.996 25.627 1.00 11.96 ? 35  TRP A O   1 
ATOM   265  C  CB  . TRP A 1 35  ? 28.731  35.315 27.997 1.00 10.42 ? 35  TRP A CB  1 
ATOM   266  C  CG  . TRP A 1 35  ? 28.349  36.738 27.692 1.00 10.80 ? 35  TRP A CG  1 
ATOM   267  C  CD1 . TRP A 1 35  ? 27.179  37.220 27.176 1.00 11.56 ? 35  TRP A CD1 1 
ATOM   268  C  CD2 . TRP A 1 35  ? 29.165  37.891 27.954 1.00 10.24 ? 35  TRP A CD2 1 
ATOM   269  N  NE1 . TRP A 1 35  ? 27.196  38.583 27.100 1.00 11.40 ? 35  TRP A NE1 1 
ATOM   270  C  CE2 . TRP A 1 35  ? 28.418  39.035 27.534 1.00 11.16 ? 35  TRP A CE2 1 
ATOM   271  C  CE3 . TRP A 1 35  ? 30.450  38.069 28.453 1.00 11.38 ? 35  TRP A CE3 1 
ATOM   272  C  CZ2 . TRP A 1 35  ? 28.941  40.322 27.629 1.00 13.30 ? 35  TRP A CZ2 1 
ATOM   273  C  CZ3 . TRP A 1 35  ? 30.955  39.353 28.541 1.00 14.66 ? 35  TRP A CZ3 1 
ATOM   274  C  CH2 . TRP A 1 35  ? 30.209  40.451 28.137 1.00 14.80 ? 35  TRP A CH2 1 
ATOM   275  N  N   . VAL A 1 36  ? 28.575  35.366 24.657 1.00 10.30 ? 36  VAL A N   1 
ATOM   276  C  CA  . VAL A 1 36  ? 29.057  36.031 23.462 1.00 11.44 ? 36  VAL A CA  1 
ATOM   277  C  C   . VAL A 1 36  ? 28.386  37.405 23.391 1.00 10.12 ? 36  VAL A C   1 
ATOM   278  O  O   . VAL A 1 36  ? 27.197  37.504 23.129 1.00 12.00 ? 36  VAL A O   1 
ATOM   279  C  CB  . VAL A 1 36  ? 28.772  35.211 22.216 1.00 13.16 ? 36  VAL A CB  1 
ATOM   280  C  CG1 . VAL A 1 36  ? 29.278  35.948 20.973 1.00 15.35 ? 36  VAL A CG1 1 
ATOM   281  C  CG2 . VAL A 1 36  ? 29.420  33.822 22.343 1.00 15.70 ? 36  VAL A CG2 1 
ATOM   282  N  N   . ALA A 1 37  ? 29.186  38.442 23.664 1.00 11.46 ? 37  ALA A N   1 
ATOM   283  C  CA  . ALA A 1 37  ? 28.622  39.770 23.814 1.00 11.89 ? 37  ALA A CA  1 
ATOM   284  C  C   . ALA A 1 37  ? 27.738  40.156 22.651 1.00 11.89 ? 37  ALA A C   1 
ATOM   285  O  O   . ALA A 1 37  ? 26.695  40.790 22.789 1.00 11.19 ? 37  ALA A O   1 
ATOM   286  C  CB  . ALA A 1 37  ? 29.683  40.826 24.071 1.00 14.41 ? 37  ALA A CB  1 
ATOM   287  N  N   . SER A 1 38  ? 28.224  39.900 21.429 1.00 11.54 ? 38  SER A N   1 
ATOM   288  C  CA  . SER A 1 38  ? 27.536  40.357 20.243 1.00 12.39 ? 38  SER A CA  1 
ATOM   289  C  C   . SER A 1 38  ? 26.226  39.622 19.978 1.00 12.42 ? 38  SER A C   1 
ATOM   290  O  O   . SER A 1 38  ? 25.481  40.058 19.114 1.00 13.44 ? 38  SER A O   1 
ATOM   291  C  CB  A SER A 1 38  ? 28.441  40.228 19.005 0.50 12.91 ? 38  SER A CB  1 
ATOM   292  C  CB  B SER A 1 38  ? 28.450  40.187 19.006 0.50 12.02 ? 38  SER A CB  1 
ATOM   293  O  OG  A SER A 1 38  ? 29.486  41.180 19.027 0.50 12.45 ? 38  SER A OG  1 
ATOM   294  O  OG  B SER A 1 38  ? 28.744  38.805 18.871 0.50 14.16 ? 38  SER A OG  1 
ATOM   295  N  N   . LYS A 1 39  ? 25.965  38.519 20.677 1.00 13.31 ? 39  LYS A N   1 
ATOM   296  C  CA  . LYS A 1 39  ? 24.705  37.792 20.548 1.00 14.28 ? 39  LYS A CA  1 
ATOM   297  C  C   . LYS A 1 39  ? 23.722  38.118 21.651 1.00 14.79 ? 39  LYS A C   1 
ATOM   298  O  O   . LYS A 1 39  ? 22.606  37.611 21.679 1.00 13.44 ? 39  LYS A O   1 
ATOM   299  C  CB  . LYS A 1 39  ? 24.940  36.282 20.512 1.00 18.02 ? 39  LYS A CB  1 
ATOM   300  C  CG  . LYS A 1 39  ? 25.678  35.787 19.289 1.00 18.78 ? 39  LYS A CG  1 
ATOM   301  C  CD  . LYS A 1 39  ? 26.022  34.326 19.463 1.00 24.34 ? 39  LYS A CD  1 
ATOM   302  C  CE  . LYS A 1 39  ? 26.279  33.590 18.175 1.00 28.55 ? 39  LYS A CE  1 
ATOM   303  N  NZ  . LYS A 1 39  ? 26.017  32.130 18.329 1.00 40.73 ? 39  LYS A NZ  1 
ATOM   304  N  N   . GLY A 1 40  ? 24.145  38.902 22.656 1.00 11.90 ? 40  GLY A N   1 
ATOM   305  C  CA  . GLY A 1 40  ? 23.188  39.271 23.716 1.00 11.88 ? 40  GLY A CA  1 
ATOM   306  C  C   . GLY A 1 40  ? 22.638  38.091 24.476 1.00 12.38 ? 40  GLY A C   1 
ATOM   307  O  O   . GLY A 1 40  ? 21.446  38.142 24.893 1.00 11.97 ? 40  GLY A O   1 
ATOM   308  N  N   . ASN A 1 41  ? 23.419  37.055 24.711 1.00 10.36 ? 41  ASN A N   1 
ATOM   309  C  CA  . ASN A 1 41  ? 22.957  35.782 25.205 1.00 9.76  ? 41  ASN A CA  1 
ATOM   310  C  C   . ASN A 1 41  ? 23.226  35.464 26.639 1.00 9.17  ? 41  ASN A C   1 
ATOM   311  O  O   . ASN A 1 41  ? 23.081  34.322 27.093 1.00 11.10 ? 41  ASN A O   1 
ATOM   312  C  CB  . ASN A 1 41  ? 23.460  34.623 24.286 1.00 10.43 ? 41  ASN A CB  1 
ATOM   313  C  CG  . ASN A 1 41  ? 24.945  34.349 24.494 1.00 11.02 ? 41  ASN A CG  1 
ATOM   314  O  OD1 . ASN A 1 41  ? 25.654  35.174 25.091 1.00 11.11 ? 41  ASN A OD1 1 
ATOM   315  N  ND2 . ASN A 1 41  ? 25.448  33.259 23.933 1.00 13.81 ? 41  ASN A ND2 1 
ATOM   316  N  N   . LEU A 1 42  ? 23.583  36.452 27.480 1.00 10.76 ? 42  LEU A N   1 
ATOM   317  C  CA  . LEU A 1 42  ? 23.941  36.128 28.861 1.00 10.63 ? 42  LEU A CA  1 
ATOM   318  C  C   . LEU A 1 42  ? 22.890  35.354 29.604 1.00 11.33 ? 42  LEU A C   1 
ATOM   319  O  O   . LEU A 1 42  ? 23.154  34.395 30.324 1.00 12.42 ? 42  LEU A O   1 
ATOM   320  C  CB  . LEU A 1 42  ? 24.329  37.422 29.627 1.00 11.60 ? 42  LEU A CB  1 
ATOM   321  C  CG  . LEU A 1 42  ? 24.851  37.229 31.027 1.00 11.35 ? 42  LEU A CG  1 
ATOM   322  C  CD1 . LEU A 1 42  ? 26.154  36.386 30.999 1.00 12.40 ? 42  LEU A CD1 1 
ATOM   323  C  CD2 . LEU A 1 42  ? 25.123  38.574 31.700 1.00 12.49 ? 42  LEU A CD2 1 
ATOM   324  N  N   . ALA A 1 43  ? 21.610  35.746 29.481 1.00 12.31 ? 43  ALA A N   1 
ATOM   325  C  CA  . ALA A 1 43  ? 20.551  35.125 30.244 1.00 13.73 ? 43  ALA A CA  1 
ATOM   326  C  C   . ALA A 1 43  ? 20.242  33.707 29.800 1.00 13.92 ? 43  ALA A C   1 
ATOM   327  O  O   . ALA A 1 43  ? 19.668  32.915 30.575 1.00 17.39 ? 43  ALA A O   1 
ATOM   328  C  CB  . ALA A 1 43  ? 19.286  35.964 30.218 1.00 16.02 ? 43  ALA A CB  1 
ATOM   329  N  N   . ASP A 1 44  ? 20.678  33.335 28.624 1.00 13.85 ? 44  ASP A N   1 
ATOM   330  C  CA  . ASP A 1 44  ? 20.502  31.962 28.156 1.00 13.56 ? 44  ASP A CA  1 
ATOM   331  C  C   . ASP A 1 44  ? 21.581  31.018 28.703 1.00 14.45 ? 44  ASP A C   1 
ATOM   332  O  O   . ASP A 1 44  ? 21.337  29.814 28.935 1.00 14.29 ? 44  ASP A O   1 
ATOM   333  C  CB  . ASP A 1 44  ? 20.553  31.897 26.633 1.00 20.23 ? 44  ASP A CB  1 
ATOM   334  C  CG  . ASP A 1 44  ? 19.444  32.664 25.956 1.00 20.02 ? 44  ASP A CG  1 
ATOM   335  O  OD1 . ASP A 1 44  ? 18.299  32.583 26.452 1.00 26.75 ? 44  ASP A OD1 1 
ATOM   336  O  OD2 . ASP A 1 44  ? 19.693  33.268 24.897 1.00 27.73 ? 44  ASP A OD2 1 
ATOM   337  N  N   . VAL A 1 45  ? 22.795  31.534 28.826 1.00 11.38 ? 45  VAL A N   1 
ATOM   338  C  CA  . VAL A 1 45  ? 23.944  30.700 29.196 1.00 11.67 ? 45  VAL A CA  1 
ATOM   339  C  C   . VAL A 1 45  ? 24.238  30.699 30.663 1.00 11.24 ? 45  VAL A C   1 
ATOM   340  O  O   . VAL A 1 45  ? 24.949  29.820 31.168 1.00 12.28 ? 45  VAL A O   1 
ATOM   341  C  CB  . VAL A 1 45  ? 25.182  31.059 28.371 1.00 11.02 ? 45  VAL A CB  1 
ATOM   342  C  CG1 . VAL A 1 45  ? 24.890  31.029 26.894 1.00 16.15 ? 45  VAL A CG1 1 
ATOM   343  C  CG2 . VAL A 1 45  ? 25.781  32.387 28.824 1.00 16.39 ? 45  VAL A CG2 1 
ATOM   344  N  N   . ALA A 1 46  ? 23.757  31.743 31.357 1.00 12.49 ? 46  ALA A N   1 
ATOM   345  C  CA  . ALA A 1 46  ? 24.001  31.898 32.790 1.00 13.30 ? 46  ALA A CA  1 
ATOM   346  C  C   . ALA A 1 46  ? 22.736  32.521 33.421 1.00 12.88 ? 46  ALA A C   1 
ATOM   347  O  O   . ALA A 1 46  ? 22.723  33.683 33.780 1.00 12.95 ? 46  ALA A O   1 
ATOM   348  C  CB  . ALA A 1 46  ? 25.186  32.816 33.045 1.00 13.61 ? 46  ALA A CB  1 
ATOM   349  N  N   . PRO A 1 47  ? 21.673  31.739 33.465 1.00 16.12 ? 47  PRO A N   1 
ATOM   350  C  CA  . PRO A 1 47  ? 20.380  32.226 33.919 1.00 16.44 ? 47  PRO A CA  1 
ATOM   351  C  C   . PRO A 1 47  ? 20.476  32.863 35.309 1.00 16.37 ? 47  PRO A C   1 
ATOM   352  O  O   . PRO A 1 47  ? 21.052  32.276 36.223 1.00 18.11 ? 47  PRO A O   1 
ATOM   353  C  CB  . PRO A 1 47  ? 19.515  30.955 34.020 1.00 18.87 ? 47  PRO A CB  1 
ATOM   354  C  CG  . PRO A 1 47  ? 20.219  29.916 33.257 1.00 20.71 ? 47  PRO A CG  1 
ATOM   355  C  CD  . PRO A 1 47  ? 21.625  30.331 33.039 1.00 18.73 ? 47  PRO A CD  1 
ATOM   356  N  N   . GLY A 1 48  ? 19.905  34.044 35.447 1.00 15.97 ? 48  GLY A N   1 
ATOM   357  C  CA  . GLY A 1 48  ? 19.815  34.761 36.691 1.00 16.89 ? 48  GLY A CA  1 
ATOM   358  C  C   . GLY A 1 48  ? 21.073  35.511 37.065 1.00 16.89 ? 48  GLY A C   1 
ATOM   359  O  O   . GLY A 1 48  ? 21.102  36.174 38.097 1.00 19.14 ? 48  GLY A O   1 
ATOM   360  N  N   . LYS A 1 49  ? 22.096  35.475 36.210 1.00 16.21 ? 49  LYS A N   1 
ATOM   361  C  CA  . LYS A 1 49  ? 23.344  36.151 36.471 1.00 15.45 ? 49  LYS A CA  1 
ATOM   362  C  C   . LYS A 1 49  ? 23.484  37.516 35.810 1.00 15.51 ? 49  LYS A C   1 
ATOM   363  O  O   . LYS A 1 49  ? 22.875  37.759 34.786 1.00 15.15 ? 49  LYS A O   1 
ATOM   364  C  CB  . LYS A 1 49  ? 24.543  35.277 36.173 1.00 17.43 ? 49  LYS A CB  1 
ATOM   365  C  CG  . LYS A 1 49  ? 24.553  33.922 36.837 1.00 20.02 ? 49  LYS A CG  1 
ATOM   366  C  CD  . LYS A 1 49  ? 24.672  33.954 38.332 1.00 26.36 ? 49  LYS A CD  1 
ATOM   367  C  CE  . LYS A 1 49  ? 25.129  32.623 38.917 1.00 27.97 ? 49  LYS A CE  1 
ATOM   368  N  NZ  . LYS A 1 49  ? 24.668  32.442 40.323 1.00 34.81 ? 49  LYS A NZ  1 
ATOM   369  N  N   . SER A 1 50  ? 24.273  38.401 36.428 1.00 13.94 ? 50  SER A N   1 
ATOM   370  C  CA  . SER A 1 50  ? 24.649  39.681 35.870 1.00 13.08 ? 50  SER A CA  1 
ATOM   371  C  C   . SER A 1 50  ? 26.197  39.789 35.888 1.00 12.20 ? 50  SER A C   1 
ATOM   372  O  O   . SER A 1 50  ? 26.791  39.119 36.714 1.00 13.27 ? 50  SER A O   1 
ATOM   373  C  CB  . SER A 1 50  ? 24.127  40.854 36.727 1.00 13.95 ? 50  SER A CB  1 
ATOM   374  O  OG  . SER A 1 50  ? 22.716  40.956 36.639 1.00 14.40 ? 50  SER A OG  1 
ATOM   375  N  N   . ILE A 1 51  ? 26.768  40.561 34.976 1.00 13.24 ? 51  ILE A N   1 
ATOM   376  C  CA  . ILE A 1 51  ? 28.227  40.759 35.002 1.00 13.41 ? 51  ILE A CA  1 
ATOM   377  C  C   . ILE A 1 51  ? 28.595  41.750 36.114 1.00 13.36 ? 51  ILE A C   1 
ATOM   378  O  O   . ILE A 1 51  ? 27.996  42.821 36.265 1.00 13.98 ? 51  ILE A O   1 
ATOM   379  C  CB  . ILE A 1 51  ? 28.679  41.405 33.650 1.00 14.71 ? 51  ILE A CB  1 
ATOM   380  C  CG1 . ILE A 1 51  ? 28.351  40.598 32.400 1.00 16.48 ? 51  ILE A CG1 1 
ATOM   381  C  CG2 . ILE A 1 51  ? 30.191  41.674 33.736 1.00 16.64 ? 51  ILE A CG2 1 
ATOM   382  C  CD1 . ILE A 1 51  ? 28.956  39.259 32.425 1.00 19.44 ? 51  ILE A CD1 1 
ATOM   383  N  N   . GLY A 1 52  ? 29.633  41.423 36.874 1.00 13.20 ? 52  GLY A N   1 
ATOM   384  C  CA  . GLY A 1 52  ? 30.119  42.327 37.916 1.00 13.83 ? 52  GLY A CA  1 
ATOM   385  C  C   . GLY A 1 52  ? 31.352  41.815 38.606 1.00 14.19 ? 52  GLY A C   1 
ATOM   386  O  O   . GLY A 1 52  ? 31.602  40.606 38.651 1.00 16.98 ? 52  GLY A O   1 
ATOM   387  N  N   . GLY A 1 53  ? 32.142  42.732 39.188 1.00 14.92 ? 53  GLY A N   1 
ATOM   388  C  CA  . GLY A 1 53  ? 33.276  42.391 39.986 1.00 16.20 ? 53  GLY A CA  1 
ATOM   389  C  C   . GLY A 1 53  ? 34.624  42.633 39.361 1.00 18.25 ? 53  GLY A C   1 
ATOM   390  O  O   . GLY A 1 53  ? 35.651  42.459 40.015 1.00 19.64 ? 53  GLY A O   1 
ATOM   391  N  N   . ASP A 1 54  ? 34.663  43.080 38.105 1.00 19.50 ? 54  ASP A N   1 
ATOM   392  C  CA  . ASP A 1 54  ? 35.890  43.398 37.427 1.00 21.32 ? 54  ASP A CA  1 
ATOM   393  C  C   . ASP A 1 54  ? 36.470  44.740 37.856 1.00 19.77 ? 54  ASP A C   1 
ATOM   394  O  O   . ASP A 1 54  ? 35.750  45.691 38.205 1.00 19.70 ? 54  ASP A O   1 
ATOM   395  C  CB  . ASP A 1 54  ? 35.766  43.324 35.912 1.00 20.87 ? 54  ASP A CB  1 
ATOM   396  C  CG  . ASP A 1 54  ? 35.431  41.935 35.407 1.00 22.92 ? 54  ASP A CG  1 
ATOM   397  O  OD1 . ASP A 1 54  ? 36.254  41.038 35.646 1.00 27.93 ? 54  ASP A OD1 1 
ATOM   398  O  OD2 . ASP A 1 54  ? 34.350  41.737 34.818 1.00 24.19 ? 54  ASP A OD2 1 
ATOM   399  N  N   . ILE A 1 55  ? 37.787  44.830 37.789 1.00 21.91 ? 55  ILE A N   1 
ATOM   400  C  CA  . ILE A 1 55  ? 38.484  46.081 38.041 1.00 24.26 ? 55  ILE A CA  1 
ATOM   401  C  C   . ILE A 1 55  ? 38.180  47.102 36.939 1.00 23.86 ? 55  ILE A C   1 
ATOM   402  O  O   . ILE A 1 55  ? 38.128  46.771 35.753 1.00 24.90 ? 55  ILE A O   1 
ATOM   403  C  CB  . ILE A 1 55  ? 40.024  45.845 38.073 1.00 26.11 ? 55  ILE A CB  1 
ATOM   404  C  CG1 . ILE A 1 55  ? 40.426  44.998 39.299 1.00 26.93 ? 55  ILE A CG1 1 
ATOM   405  C  CG2 . ILE A 1 55  ? 40.720  47.205 38.143 1.00 30.14 ? 55  ILE A CG2 1 
ATOM   406  C  CD1 . ILE A 1 55  ? 41.821  45.319 39.797 1.00 31.50 ? 55  ILE A CD1 1 
ATOM   407  N  N   . PHE A 1 56  ? 37.870  48.306 37.378 1.00 22.83 ? 56  PHE A N   1 
ATOM   408  C  CA  . PHE A 1 56  ? 37.642  49.446 36.484 1.00 24.68 ? 56  PHE A CA  1 
ATOM   409  C  C   . PHE A 1 56  ? 38.884  50.362 36.556 1.00 26.75 ? 56  PHE A C   1 
ATOM   410  O  O   . PHE A 1 56  ? 39.256  50.781 37.644 1.00 27.76 ? 56  PHE A O   1 
ATOM   411  C  CB  . PHE A 1 56  ? 36.427  50.231 37.020 1.00 24.50 ? 56  PHE A CB  1 
ATOM   412  C  CG  . PHE A 1 56  ? 36.119  51.459 36.192 1.00 24.27 ? 56  PHE A CG  1 
ATOM   413  C  CD1 . PHE A 1 56  ? 35.537  51.313 34.937 1.00 25.66 ? 56  PHE A CD1 1 
ATOM   414  C  CD2 . PHE A 1 56  ? 36.401  52.724 36.673 1.00 24.28 ? 56  PHE A CD2 1 
ATOM   415  C  CE1 . PHE A 1 56  ? 35.175  52.434 34.215 1.00 26.88 ? 56  PHE A CE1 1 
ATOM   416  C  CE2 . PHE A 1 56  ? 36.122  53.848 35.897 1.00 25.62 ? 56  PHE A CE2 1 
ATOM   417  C  CZ  . PHE A 1 56  ? 35.574  53.687 34.642 1.00 26.47 ? 56  PHE A CZ  1 
ATOM   418  N  N   . SER A 1 57  ? 39.541  50.592 35.437 1.00 27.27 ? 57  SER A N   1 
ATOM   419  C  CA  . SER A 1 57  ? 40.767  51.317 35.370 1.00 28.58 ? 57  SER A CA  1 
ATOM   420  C  C   . SER A 1 57  ? 40.763  52.725 35.881 1.00 31.53 ? 57  SER A C   1 
ATOM   421  O  O   . SER A 1 57  ? 41.834  53.193 36.359 1.00 32.73 ? 57  SER A O   1 
ATOM   422  C  CB  . SER A 1 57  ? 41.440  51.259 33.989 1.00 32.50 ? 57  SER A CB  1 
ATOM   423  O  OG  . SER A 1 57  ? 42.480  52.221 33.915 1.00 42.69 ? 57  SER A OG  1 
ATOM   424  N  N   . ASN A 1 58  ? 39.716  53.477 35.690 1.00 32.30 ? 58  ASN A N   1 
ATOM   425  C  CA  . ASN A 1 58  ? 39.654  54.897 36.058 1.00 35.12 ? 58  ASN A CA  1 
ATOM   426  C  C   . ASN A 1 58  ? 40.737  55.685 35.308 1.00 34.49 ? 58  ASN A C   1 
ATOM   427  O  O   . ASN A 1 58  ? 41.336  56.596 35.896 1.00 36.23 ? 58  ASN A O   1 
ATOM   428  C  CB  . ASN A 1 58  ? 39.840  55.116 37.555 1.00 34.67 ? 58  ASN A CB  1 
ATOM   429  C  CG  . ASN A 1 58  ? 39.370  56.488 38.005 1.00 34.08 ? 58  ASN A CG  1 
ATOM   430  O  OD1 . ASN A 1 58  ? 38.495  57.097 37.376 1.00 33.82 ? 58  ASN A OD1 1 
ATOM   431  N  ND2 . ASN A 1 58  ? 39.981  57.015 39.067 1.00 32.88 ? 58  ASN A ND2 1 
ATOM   432  N  N   . ARG A 1 59  ? 40.973  55.327 34.066 0.50 35.56 ? 59  ARG A N   1 
ATOM   433  C  CA  . ARG A 1 59  ? 41.962  55.950 33.217 0.50 39.38 ? 59  ARG A CA  1 
ATOM   434  C  C   . ARG A 1 59  ? 41.767  57.466 33.108 0.50 40.97 ? 59  ARG A C   1 
ATOM   435  O  O   . ARG A 1 59  ? 42.747  58.204 33.257 0.50 43.04 ? 59  ARG A O   1 
ATOM   436  C  CB  . ARG A 1 59  ? 41.957  55.330 31.817 0.00 39.75 ? 59  ARG A CB  1 
ATOM   437  C  CG  . ARG A 1 59  ? 41.180  54.026 31.720 0.00 39.65 ? 59  ARG A CG  1 
ATOM   438  C  CD  . ARG A 1 59  ? 40.039  54.137 30.724 0.00 39.63 ? 59  ARG A CD  1 
ATOM   439  N  NE  . ARG A 1 59  ? 40.223  53.249 29.579 0.00 39.61 ? 59  ARG A NE  1 
ATOM   440  C  CZ  . ARG A 1 59  ? 39.339  53.088 28.604 0.00 39.58 ? 59  ARG A CZ  1 
ATOM   441  N  NH1 . ARG A 1 59  ? 38.755  54.143 28.052 0.00 39.61 ? 59  ARG A NH1 1 
ATOM   442  N  NH2 . ARG A 1 59  ? 39.034  51.871 28.175 0.00 39.55 ? 59  ARG A NH2 1 
ATOM   443  N  N   . GLU A 1 60  ? 40.552  57.887 32.815 1.00 41.02 ? 60  GLU A N   1 
ATOM   444  C  CA  . GLU A 1 60  ? 40.154  59.258 32.621 1.00 41.67 ? 60  GLU A CA  1 
ATOM   445  C  C   . GLU A 1 60  ? 40.240  60.090 33.895 1.00 40.83 ? 60  GLU A C   1 
ATOM   446  O  O   . GLU A 1 60  ? 40.055  61.308 33.871 1.00 41.53 ? 60  GLU A O   1 
ATOM   447  C  CB  . GLU A 1 60  ? 38.735  59.356 32.048 1.00 40.92 ? 60  GLU A CB  1 
ATOM   448  C  CG  . GLU A 1 60  ? 38.577  58.774 30.651 1.00 44.10 ? 60  GLU A CG  1 
ATOM   449  C  CD  . GLU A 1 60  ? 37.129  58.755 30.191 1.00 43.55 ? 60  GLU A CD  1 
ATOM   450  O  OE1 . GLU A 1 60  ? 36.227  58.900 31.045 0.50 40.93 ? 60  GLU A OE1 1 
ATOM   451  O  OE2 . GLU A 1 60  ? 36.897  58.615 28.972 0.50 43.79 ? 60  GLU A OE2 1 
ATOM   452  N  N   . GLY A 1 61  ? 40.447  59.416 35.024 1.00 36.76 ? 61  GLY A N   1 
ATOM   453  C  CA  . GLY A 1 61  ? 40.555  60.064 36.306 1.00 36.48 ? 61  GLY A CA  1 
ATOM   454  C  C   . GLY A 1 61  ? 39.296  60.751 36.749 1.00 35.94 ? 61  GLY A C   1 
ATOM   455  O  O   . GLY A 1 61  ? 39.334  61.724 37.514 1.00 36.85 ? 61  GLY A O   1 
ATOM   456  N  N   . LYS A 1 62  ? 38.139  60.259 36.296 1.00 30.38 ? 62  LYS A N   1 
ATOM   457  C  CA  . LYS A 1 62  ? 36.881  60.920 36.685 1.00 29.82 ? 62  LYS A CA  1 
ATOM   458  C  C   . LYS A 1 62  ? 36.529  60.613 38.121 1.00 29.74 ? 62  LYS A C   1 
ATOM   459  O  O   . LYS A 1 62  ? 36.080  61.456 38.908 1.00 30.04 ? 62  LYS A O   1 
ATOM   460  C  CB  . LYS A 1 62  ? 35.776  60.523 35.723 1.00 30.86 ? 62  LYS A CB  1 
ATOM   461  C  CG  . LYS A 1 62  ? 36.141  60.686 34.247 1.00 39.17 ? 62  LYS A CG  1 
ATOM   462  C  CD  . LYS A 1 62  ? 35.011  61.267 33.453 1.00 39.15 ? 62  LYS A CD  1 
ATOM   463  C  CE  . LYS A 1 62  ? 34.338  60.212 32.574 1.00 43.67 ? 62  LYS A CE  1 
ATOM   464  N  NZ  . LYS A 1 62  ? 34.395  60.601 31.120 1.00 46.84 ? 62  LYS A NZ  1 
ATOM   465  N  N   . LEU A 1 63  ? 36.814  59.389 38.558 1.00 26.33 ? 63  LEU A N   1 
ATOM   466  C  CA  . LEU A 1 63  ? 36.478  59.064 39.964 1.00 26.04 ? 63  LEU A CA  1 
ATOM   467  C  C   . LEU A 1 63  ? 37.657  59.477 40.845 1.00 25.25 ? 63  LEU A C   1 
ATOM   468  O  O   . LEU A 1 63  ? 38.808  59.392 40.422 1.00 25.93 ? 63  LEU A O   1 
ATOM   469  C  CB  . LEU A 1 63  ? 36.259  57.548 40.081 1.00 23.12 ? 63  LEU A CB  1 
ATOM   470  C  CG  . LEU A 1 63  ? 35.020  57.013 39.335 1.00 22.79 ? 63  LEU A CG  1 
ATOM   471  C  CD1 . LEU A 1 63  ? 35.138  55.493 39.264 1.00 30.30 ? 63  LEU A CD1 1 
ATOM   472  C  CD2 . LEU A 1 63  ? 33.750  57.405 40.071 1.00 22.23 ? 63  LEU A CD2 1 
ATOM   473  N  N   . PRO A 1 64  ? 37.364  59.871 42.072 1.00 27.45 ? 64  PRO A N   1 
ATOM   474  C  CA  . PRO A 1 64  ? 38.416  60.294 42.990 1.00 28.54 ? 64  PRO A CA  1 
ATOM   475  C  C   . PRO A 1 64  ? 39.454  59.201 43.224 1.00 29.53 ? 64  PRO A C   1 
ATOM   476  O  O   . PRO A 1 64  ? 39.114  58.059 43.545 1.00 25.46 ? 64  PRO A O   1 
ATOM   477  C  CB  . PRO A 1 64  ? 37.695  60.613 44.278 1.00 28.76 ? 64  PRO A CB  1 
ATOM   478  C  CG  . PRO A 1 64  ? 36.319  60.109 44.144 1.00 28.36 ? 64  PRO A CG  1 
ATOM   479  C  CD  . PRO A 1 64  ? 36.030  59.913 42.685 1.00 26.15 ? 64  PRO A CD  1 
ATOM   480  N  N   . GLY A 1 65  ? 40.712  59.609 43.100 1.00 33.23 ? 65  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 65  ? 41.845  58.759 43.236 1.00 33.22 ? 65  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 65  ? 42.564  58.898 44.564 1.00 33.72 ? 65  GLY A C   1 
ATOM   483  O  O   . GLY A 1 65  ? 42.542  59.958 45.196 1.00 38.12 ? 65  GLY A O   1 
ATOM   484  N  N   . LYS A 1 66  ? 43.205  57.816 44.975 1.00 34.34 ? 66  LYS A N   1 
ATOM   485  C  CA  . LYS A 1 66  ? 44.002  57.846 46.222 1.00 34.40 ? 66  LYS A CA  1 
ATOM   486  C  C   . LYS A 1 66  ? 44.966  56.666 46.213 1.00 35.61 ? 66  LYS A C   1 
ATOM   487  O  O   . LYS A 1 66  ? 44.656  55.613 45.641 1.00 34.49 ? 66  LYS A O   1 
ATOM   488  C  CB  . LYS A 1 66  ? 43.008  57.693 47.398 1.00 34.58 ? 66  LYS A CB  1 
ATOM   489  C  CG  . LYS A 1 66  ? 43.630  57.866 48.754 1.00 33.43 ? 66  LYS A CG  1 
ATOM   490  C  CD  . LYS A 1 66  ? 42.630  57.606 49.886 1.00 34.07 ? 66  LYS A CD  1 
ATOM   491  C  CE  . LYS A 1 66  ? 43.322  57.840 51.227 0.50 34.52 ? 66  LYS A CE  1 
ATOM   492  N  NZ  . LYS A 1 66  ? 42.405  57.716 52.375 0.50 36.00 ? 66  LYS A NZ  1 
ATOM   493  N  N   . SER A 1 67  ? 46.145  56.847 46.803 1.00 38.01 ? 67  SER A N   1 
ATOM   494  C  CA  . SER A 1 67  ? 47.110  55.738 46.878 1.00 39.15 ? 67  SER A CA  1 
ATOM   495  C  C   . SER A 1 67  ? 46.448  54.512 47.511 1.00 37.81 ? 67  SER A C   1 
ATOM   496  O  O   . SER A 1 67  ? 45.785  54.612 48.544 1.00 36.27 ? 67  SER A O   1 
ATOM   497  C  CB  . SER A 1 67  ? 48.336  56.147 47.697 1.00 40.52 ? 67  SER A CB  1 
ATOM   498  O  OG  . SER A 1 67  ? 48.342  57.535 47.973 1.00 49.44 ? 67  SER A OG  1 
ATOM   499  N  N   . GLY A 1 68  ? 46.581  53.366 46.848 1.00 36.25 ? 68  GLY A N   1 
ATOM   500  C  CA  . GLY A 1 68  ? 46.013  52.121 47.328 1.00 30.85 ? 68  GLY A CA  1 
ATOM   501  C  C   . GLY A 1 68  ? 44.543  51.967 47.140 1.00 28.89 ? 68  GLY A C   1 
ATOM   502  O  O   . GLY A 1 68  ? 43.928  50.979 47.589 1.00 31.77 ? 68  GLY A O   1 
ATOM   503  N  N   . ARG A 1 69  ? 43.879  52.879 46.412 1.00 28.03 ? 69  ARG A N   1 
ATOM   504  C  CA  . ARG A 1 69  ? 42.469  52.700 46.140 1.00 25.96 ? 69  ARG A CA  1 
ATOM   505  C  C   . ARG A 1 69  ? 42.256  52.074 44.754 1.00 24.78 ? 69  ARG A C   1 
ATOM   506  O  O   . ARG A 1 69  ? 42.770  52.588 43.758 1.00 27.30 ? 69  ARG A O   1 
ATOM   507  C  CB  . ARG A 1 69  ? 41.690  53.992 46.274 1.00 24.68 ? 69  ARG A CB  1 
ATOM   508  C  CG  . ARG A 1 69  ? 40.248  53.893 45.810 1.00 22.23 ? 69  ARG A CG  1 
ATOM   509  C  CD  . ARG A 1 69  ? 39.599  55.276 45.756 1.00 23.67 ? 69  ARG A CD  1 
ATOM   510  N  NE  . ARG A 1 69  ? 39.316  55.767 47.088 1.00 22.09 ? 69  ARG A NE  1 
ATOM   511  C  CZ  . ARG A 1 69  ? 39.323  57.034 47.471 1.00 21.85 ? 69  ARG A CZ  1 
ATOM   512  N  NH1 . ARG A 1 69  ? 39.357  57.987 46.548 1.00 25.96 ? 69  ARG A NH1 1 
ATOM   513  N  NH2 . ARG A 1 69  ? 39.117  57.340 48.733 1.00 25.99 ? 69  ARG A NH2 1 
ATOM   514  N  N   . THR A 1 70  ? 41.532  50.990 44.741 1.00 22.99 ? 70  THR A N   1 
ATOM   515  C  CA  . THR A 1 70  ? 41.138  50.235 43.562 1.00 21.85 ? 70  THR A CA  1 
ATOM   516  C  C   . THR A 1 70  ? 39.624  50.427 43.342 1.00 21.81 ? 70  THR A C   1 
ATOM   517  O  O   . THR A 1 70  ? 38.855  50.489 44.312 1.00 22.33 ? 70  THR A O   1 
ATOM   518  C  CB  . THR A 1 70  ? 41.412  48.719 43.771 1.00 23.89 ? 70  THR A CB  1 
ATOM   519  O  OG1 . THR A 1 70  ? 42.842  48.505 43.830 1.00 29.49 ? 70  THR A OG1 1 
ATOM   520  C  CG2 . THR A 1 70  ? 40.955  47.906 42.576 1.00 26.48 ? 70  THR A CG2 1 
ATOM   521  N  N   . TRP A 1 71  ? 39.230  50.539 42.089 1.00 20.46 ? 71  TRP A N   1 
ATOM   522  C  CA  . TRP A 1 71  ? 37.821  50.625 41.710 1.00 20.70 ? 71  TRP A CA  1 
ATOM   523  C  C   . TRP A 1 71  ? 37.395  49.337 40.990 1.00 18.50 ? 71  TRP A C   1 
ATOM   524  O  O   . TRP A 1 71  ? 38.162  48.781 40.223 1.00 18.82 ? 71  TRP A O   1 
ATOM   525  C  CB  . TRP A 1 71  ? 37.607  51.830 40.755 1.00 20.31 ? 71  TRP A CB  1 
ATOM   526  C  CG  . TRP A 1 71  ? 37.715  53.145 41.478 1.00 19.20 ? 71  TRP A CG  1 
ATOM   527  C  CD1 . TRP A 1 71  ? 38.809  53.938 41.576 1.00 19.14 ? 71  TRP A CD1 1 
ATOM   528  C  CD2 . TRP A 1 71  ? 36.669  53.792 42.219 1.00 18.30 ? 71  TRP A CD2 1 
ATOM   529  N  NE1 . TRP A 1 71  ? 38.519  55.059 42.323 1.00 19.34 ? 71  TRP A NE1 1 
ATOM   530  C  CE2 . TRP A 1 71  ? 37.213  55.003 42.729 1.00 18.59 ? 71  TRP A CE2 1 
ATOM   531  C  CE3 . TRP A 1 71  ? 35.340  53.505 42.493 1.00 17.00 ? 71  TRP A CE3 1 
ATOM   532  C  CZ2 . TRP A 1 71  ? 36.468  55.901 43.493 1.00 18.88 ? 71  TRP A CZ2 1 
ATOM   533  C  CZ3 . TRP A 1 71  ? 34.594  54.385 43.259 1.00 17.34 ? 71  TRP A CZ3 1 
ATOM   534  C  CH2 . TRP A 1 71  ? 35.167  55.570 43.760 1.00 16.87 ? 71  TRP A CH2 1 
ATOM   535  N  N   . ARG A 1 72  ? 36.162  48.940 41.228 1.00 16.50 ? 72  ARG A N   1 
ATOM   536  C  CA  . ARG A 1 72  ? 35.509  47.836 40.546 1.00 15.27 ? 72  ARG A CA  1 
ATOM   537  C  C   . ARG A 1 72  ? 34.104  48.247 40.126 1.00 15.39 ? 72  ARG A C   1 
ATOM   538  O  O   . ARG A 1 72  ? 33.551  49.229 40.623 1.00 15.08 ? 72  ARG A O   1 
ATOM   539  C  CB  . ARG A 1 72  ? 35.444  46.596 41.446 1.00 16.24 ? 72  ARG A CB  1 
ATOM   540  C  CG  . ARG A 1 72  ? 36.801  46.007 41.779 1.00 18.83 ? 72  ARG A CG  1 
ATOM   541  C  CD  . ARG A 1 72  ? 36.722  44.792 42.655 1.00 21.89 ? 72  ARG A CD  1 
ATOM   542  N  NE  . ARG A 1 72  ? 38.003  44.195 42.893 1.00 25.56 ? 72  ARG A NE  1 
ATOM   543  C  CZ  . ARG A 1 72  ? 38.716  43.410 42.138 1.00 23.20 ? 72  ARG A CZ  1 
ATOM   544  N  NH1 . ARG A 1 72  ? 38.183  42.826 41.050 1.00 29.44 ? 72  ARG A NH1 1 
ATOM   545  N  NH2 . ARG A 1 72  ? 39.987  43.133 42.457 1.00 31.78 ? 72  ARG A NH2 1 
ATOM   546  N  N   . GLU A 1 73  ? 33.552  47.491 39.172 1.00 13.40 ? 73  GLU A N   1 
ATOM   547  C  CA  . GLU A 1 73  ? 32.251  47.799 38.616 1.00 13.62 ? 73  GLU A CA  1 
ATOM   548  C  C   . GLU A 1 73  ? 31.320  46.597 38.647 1.00 13.26 ? 73  GLU A C   1 
ATOM   549  O  O   . GLU A 1 73  ? 31.776  45.453 38.685 1.00 13.95 ? 73  GLU A O   1 
ATOM   550  C  CB  . GLU A 1 73  ? 32.393  48.305 37.172 1.00 14.21 ? 73  GLU A CB  1 
ATOM   551  C  CG  . GLU A 1 73  ? 33.074  47.318 36.230 1.00 15.49 ? 73  GLU A CG  1 
ATOM   552  C  CD  . GLU A 1 73  ? 32.856  47.705 34.769 1.00 17.41 ? 73  GLU A CD  1 
ATOM   553  O  OE1 . GLU A 1 73  ? 31.677  47.799 34.359 1.00 19.05 ? 73  GLU A OE1 1 
ATOM   554  O  OE2 . GLU A 1 73  ? 33.842  47.915 34.055 1.00 23.91 ? 73  GLU A OE2 1 
ATOM   555  N  N   . ALA A 1 74  ? 30.033  46.874 38.548 1.00 12.04 ? 74  ALA A N   1 
ATOM   556  C  CA  . ALA A 1 74  ? 29.023  45.824 38.369 1.00 10.65 ? 74  ALA A CA  1 
ATOM   557  C  C   . ALA A 1 74  ? 27.802  46.375 37.626 1.00 10.64 ? 74  ALA A C   1 
ATOM   558  O  O   . ALA A 1 74  ? 27.473  47.566 37.741 1.00 11.25 ? 74  ALA A O   1 
ATOM   559  C  CB  . ALA A 1 74  ? 28.606  45.273 39.717 1.00 12.85 ? 74  ALA A CB  1 
ATOM   560  N  N   . ASP A 1 75  ? 27.199  45.515 36.827 1.00 9.96  ? 75  ASP A N   1 
ATOM   561  C  CA  . ASP A 1 75  ? 26.023  45.885 36.049 1.00 9.59  ? 75  ASP A CA  1 
ATOM   562  C  C   . ASP A 1 75  ? 24.793  45.992 36.975 1.00 10.08 ? 75  ASP A C   1 
ATOM   563  O  O   . ASP A 1 75  ? 24.593  45.136 37.823 1.00 11.03 ? 75  ASP A O   1 
ATOM   564  C  CB  . ASP A 1 75  ? 25.736  44.837 34.984 1.00 9.60  ? 75  ASP A CB  1 
ATOM   565  C  CG  . ASP A 1 75  ? 26.655  44.878 33.806 1.00 10.58 ? 75  ASP A CG  1 
ATOM   566  O  OD1 . ASP A 1 75  ? 27.771  45.399 33.891 1.00 11.28 ? 75  ASP A OD1 1 
ATOM   567  O  OD2 . ASP A 1 75  ? 26.230  44.306 32.745 1.00 11.43 ? 75  ASP A OD2 1 
ATOM   568  N  N   . ILE A 1 76  ? 23.952  46.980 36.692 1.00 9.92  ? 76  ILE A N   1 
ATOM   569  C  CA  . ILE A 1 76  ? 22.729  47.200 37.466 1.00 10.89 ? 76  ILE A CA  1 
ATOM   570  C  C   . ILE A 1 76  ? 21.505  47.148 36.571 1.00 11.54 ? 76  ILE A C   1 
ATOM   571  O  O   . ILE A 1 76  ? 21.562  47.530 35.376 1.00 11.88 ? 76  ILE A O   1 
ATOM   572  C  CB  . ILE A 1 76  ? 22.822  48.530 38.213 1.00 10.63 ? 76  ILE A CB  1 
ATOM   573  C  CG1 . ILE A 1 76  ? 23.977  48.549 39.224 1.00 11.17 ? 76  ILE A CG1 1 
ATOM   574  C  CG2 . ILE A 1 76  ? 21.533  49.036 38.791 1.00 11.74 ? 76  ILE A CG2 1 
ATOM   575  C  CD1 . ILE A 1 76  ? 23.733  47.645 40.411 1.00 14.19 ? 76  ILE A CD1 1 
ATOM   576  N  N   . ASN A 1 77  ? 20.395  46.640 37.093 1.00 12.72 ? 77  ASN A N   1 
ATOM   577  C  CA  . ASN A 1 77  ? 19.152  46.550 36.366 1.00 13.16 ? 77  ASN A CA  1 
ATOM   578  C  C   . ASN A 1 77  ? 19.148  45.563 35.221 1.00 13.65 ? 77  ASN A C   1 
ATOM   579  O  O   . ASN A 1 77  ? 18.254  45.624 34.355 1.00 14.54 ? 77  ASN A O   1 
ATOM   580  C  CB  . ASN A 1 77  ? 18.670  47.921 35.894 1.00 14.76 ? 77  ASN A CB  1 
ATOM   581  C  CG  . ASN A 1 77  ? 18.337  48.891 36.988 1.00 15.28 ? 77  ASN A CG  1 
ATOM   582  O  OD1 . ASN A 1 77  ? 17.820  48.498 38.030 1.00 18.52 ? 77  ASN A OD1 1 
ATOM   583  N  ND2 . ASN A 1 77  ? 18.618  50.172 36.762 1.00 18.53 ? 77  ASN A ND2 1 
ATOM   584  N  N   . TYR A 1 78  ? 20.084  44.628 35.158 1.00 12.62 ? 78  TYR A N   1 
ATOM   585  C  CA  . TYR A 1 78  ? 20.085  43.667 34.048 1.00 12.04 ? 78  TYR A CA  1 
ATOM   586  C  C   . TYR A 1 78  ? 19.173  42.488 34.326 1.00 12.99 ? 78  TYR A C   1 
ATOM   587  O  O   . TYR A 1 78  ? 19.223  41.883 35.405 1.00 14.11 ? 78  TYR A O   1 
ATOM   588  C  CB  . TYR A 1 78  ? 21.560  43.132 33.890 1.00 12.14 ? 78  TYR A CB  1 
ATOM   589  C  CG  . TYR A 1 78  ? 21.630  42.147 32.736 1.00 11.71 ? 78  TYR A CG  1 
ATOM   590  C  CD1 . TYR A 1 78  ? 21.570  42.594 31.428 1.00 11.82 ? 78  TYR A CD1 1 
ATOM   591  C  CD2 . TYR A 1 78  ? 21.592  40.783 32.971 1.00 12.35 ? 78  TYR A CD2 1 
ATOM   592  C  CE1 . TYR A 1 78  ? 21.561  41.704 30.348 1.00 11.32 ? 78  TYR A CE1 1 
ATOM   593  C  CE2 . TYR A 1 78  ? 21.525  39.900 31.916 1.00 11.94 ? 78  TYR A CE2 1 
ATOM   594  C  CZ  . TYR A 1 78  ? 21.518  40.343 30.623 1.00 11.01 ? 78  TYR A CZ  1 
ATOM   595  O  OH  . TYR A 1 78  ? 21.506  39.423 29.613 1.00 10.74 ? 78  TYR A OH  1 
ATOM   596  N  N   . THR A 1 79  ? 18.393  42.087 33.328 1.00 12.78 ? 79  THR A N   1 
ATOM   597  C  CA  . THR A 1 79  ? 17.623  40.866 33.371 1.00 16.35 ? 79  THR A CA  1 
ATOM   598  C  C   . THR A 1 79  ? 17.921  39.962 32.191 1.00 15.21 ? 79  THR A C   1 
ATOM   599  O  O   . THR A 1 79  ? 18.090  38.748 32.342 1.00 15.67 ? 79  THR A O   1 
ATOM   600  C  CB  . THR A 1 79  ? 16.114  41.103 33.489 1.00 17.82 ? 79  THR A CB  1 
ATOM   601  O  OG1 . THR A 1 79  ? 15.695  41.935 32.416 1.00 19.65 ? 79  THR A OG1 1 
ATOM   602  C  CG2 . THR A 1 79  ? 15.770  41.830 34.760 1.00 18.47 ? 79  THR A CG2 1 
ATOM   603  N  N   . SER A 1 80  ? 17.883  40.487 30.976 1.00 11.95 ? 80  SER A N   1 
ATOM   604  C  CA  . SER A 1 80  ? 18.072  39.656 29.786 1.00 12.04 ? 80  SER A CA  1 
ATOM   605  C  C   . SER A 1 80  ? 18.465  40.546 28.609 1.00 10.89 ? 80  SER A C   1 
ATOM   606  O  O   . SER A 1 80  ? 18.291  41.762 28.651 1.00 13.93 ? 80  SER A O   1 
ATOM   607  C  CB  . SER A 1 80  ? 16.829  38.849 29.447 1.00 15.22 ? 80  SER A CB  1 
ATOM   608  O  OG  . SER A 1 80  ? 15.748  39.662 29.099 1.00 17.95 ? 80  SER A OG  1 
ATOM   609  N  N   . GLY A 1 81  ? 18.992  39.928 27.564 1.00 11.25 ? 81  GLY A N   1 
ATOM   610  C  CA  . GLY A 1 81  ? 19.406  40.644 26.380 1.00 10.96 ? 81  GLY A CA  1 
ATOM   611  C  C   . GLY A 1 81  ? 20.803  41.208 26.451 1.00 8.92  ? 81  GLY A C   1 
ATOM   612  O  O   . GLY A 1 81  ? 21.649  40.774 27.211 1.00 9.54  ? 81  GLY A O   1 
ATOM   613  N  N   . PHE A 1 82  ? 21.038  42.222 25.603 1.00 11.10 ? 82  PHE A N   1 
ATOM   614  C  CA  . PHE A 1 82  ? 22.309  42.916 25.637 1.00 12.09 ? 82  PHE A CA  1 
ATOM   615  C  C   . PHE A 1 82  ? 22.463  43.632 26.968 1.00 10.20 ? 82  PHE A C   1 
ATOM   616  O  O   . PHE A 1 82  ? 21.474  44.026 27.598 1.00 11.13 ? 82  PHE A O   1 
ATOM   617  C  CB  . PHE A 1 82  ? 22.380  43.926 24.483 1.00 10.60 ? 82  PHE A CB  1 
ATOM   618  C  CG  . PHE A 1 82  ? 22.528  43.258 23.121 1.00 11.12 ? 82  PHE A CG  1 
ATOM   619  C  CD1 . PHE A 1 82  ? 23.772  42.918 22.638 1.00 11.21 ? 82  PHE A CD1 1 
ATOM   620  C  CD2 . PHE A 1 82  ? 21.422  42.951 22.350 1.00 11.71 ? 82  PHE A CD2 1 
ATOM   621  C  CE1 . PHE A 1 82  ? 23.915  42.280 21.428 1.00 11.86 ? 82  PHE A CE1 1 
ATOM   622  C  CE2 . PHE A 1 82  ? 21.549  42.267 21.164 1.00 13.03 ? 82  PHE A CE2 1 
ATOM   623  C  CZ  . PHE A 1 82  ? 22.808  41.935 20.694 1.00 12.21 ? 82  PHE A CZ  1 
ATOM   624  N  N   . ARG A 1 83  ? 23.691  43.879 27.402 1.00 11.02 ? 83  ARG A N   1 
ATOM   625  C  CA  . ARG A 1 83  ? 23.909  44.707 28.580 1.00 11.54 ? 83  ARG A CA  1 
ATOM   626  C  C   . ARG A 1 83  ? 23.401  46.127 28.376 1.00 11.11 ? 83  ARG A C   1 
ATOM   627  O  O   . ARG A 1 83  ? 23.337  46.653 27.280 1.00 13.20 ? 83  ARG A O   1 
ATOM   628  C  CB  . ARG A 1 83  ? 25.395  44.722 28.950 1.00 11.86 ? 83  ARG A CB  1 
ATOM   629  C  CG  . ARG A 1 83  ? 25.930  43.345 29.333 1.00 12.53 ? 83  ARG A CG  1 
ATOM   630  C  CD  . ARG A 1 83  ? 27.446  43.306 29.404 1.00 12.84 ? 83  ARG A CD  1 
ATOM   631  N  NE  . ARG A 1 83  ? 27.974  44.076 30.505 1.00 13.33 ? 83  ARG A NE  1 
ATOM   632  C  CZ  . ARG A 1 83  ? 29.227  44.480 30.652 1.00 15.19 ? 83  ARG A CZ  1 
ATOM   633  N  NH1 . ARG A 1 83  ? 30.071  44.370 29.626 1.00 17.20 ? 83  ARG A NH1 1 
ATOM   634  N  NH2 . ARG A 1 83  ? 29.601  45.151 31.724 1.00 16.82 ? 83  ARG A NH2 1 
ATOM   635  N  N   . ASN A 1 84  ? 22.994  46.747 29.472 1.00 10.79 ? 84  ASN A N   1 
ATOM   636  C  CA  . ASN A 1 84  ? 22.495  48.118 29.438 1.00 12.47 ? 84  ASN A CA  1 
ATOM   637  C  C   . ASN A 1 84  ? 23.620  49.106 29.755 1.00 12.98 ? 84  ASN A C   1 
ATOM   638  O  O   . ASN A 1 84  ? 24.810  48.745 29.675 1.00 14.07 ? 84  ASN A O   1 
ATOM   639  C  CB  . ASN A 1 84  ? 21.315  48.259 30.407 1.00 12.26 ? 84  ASN A CB  1 
ATOM   640  C  CG  . ASN A 1 84  ? 21.707  47.949 31.845 1.00 11.88 ? 84  ASN A CG  1 
ATOM   641  O  OD1 . ASN A 1 84  ? 22.874  48.117 32.210 1.00 13.50 ? 84  ASN A OD1 1 
ATOM   642  N  ND2 . ASN A 1 84  ? 20.737  47.554 32.646 1.00 15.93 ? 84  ASN A ND2 1 
ATOM   643  N  N   . SER A 1 85  ? 23.293  50.320 30.113 1.00 12.40 ? 85  SER A N   1 
ATOM   644  C  CA  . SER A 1 85  ? 24.215  51.406 30.348 1.00 14.94 ? 85  SER A CA  1 
ATOM   645  C  C   . SER A 1 85  ? 24.400  51.755 31.819 1.00 13.95 ? 85  SER A C   1 
ATOM   646  O  O   . SER A 1 85  ? 25.062  52.741 32.136 1.00 16.60 ? 85  SER A O   1 
ATOM   647  C  CB  A SER A 1 85  ? 23.780  52.657 29.570 0.50 16.95 ? 85  SER A CB  1 
ATOM   648  C  CB  B SER A 1 85  ? 23.738  52.663 29.587 0.50 15.92 ? 85  SER A CB  1 
ATOM   649  O  OG  A SER A 1 85  ? 22.561  53.163 30.077 0.50 19.20 ? 85  SER A OG  1 
ATOM   650  O  OG  B SER A 1 85  ? 23.943  52.472 28.194 0.50 22.18 ? 85  SER A OG  1 
ATOM   651  N  N   . ASP A 1 86  ? 23.807  50.958 32.689 1.00 11.96 ? 86  ASP A N   1 
ATOM   652  C  CA  . ASP A 1 86  ? 23.785  51.236 34.118 1.00 10.56 ? 86  ASP A CA  1 
ATOM   653  C  C   . ASP A 1 86  ? 24.859  50.422 34.841 1.00 10.75 ? 86  ASP A C   1 
ATOM   654  O  O   . ASP A 1 86  ? 24.920  49.213 34.747 1.00 11.00 ? 86  ASP A O   1 
ATOM   655  C  CB  . ASP A 1 86  ? 22.422  50.871 34.699 1.00 12.76 ? 86  ASP A CB  1 
ATOM   656  C  CG  . ASP A 1 86  ? 21.253  51.693 34.206 1.00 14.93 ? 86  ASP A CG  1 
ATOM   657  O  OD1 . ASP A 1 86  ? 21.454  52.751 33.585 1.00 19.19 ? 86  ASP A OD1 1 
ATOM   658  O  OD2 . ASP A 1 86  ? 20.092  51.265 34.445 1.00 19.15 ? 86  ASP A OD2 1 
ATOM   659  N  N   . ARG A 1 87  ? 25.652  51.116 35.668 1.00 10.04 ? 87  ARG A N   1 
ATOM   660  C  CA  . ARG A 1 87  ? 26.719  50.464 36.390 1.00 9.90  ? 87  ARG A CA  1 
ATOM   661  C  C   . ARG A 1 87  ? 26.854  51.127 37.789 1.00 9.18  ? 87  ARG A C   1 
ATOM   662  O  O   . ARG A 1 87  ? 26.684  52.319 37.936 1.00 11.19 ? 87  ARG A O   1 
ATOM   663  C  CB  . ARG A 1 87  ? 28.091  50.564 35.712 1.00 10.61 ? 87  ARG A CB  1 
ATOM   664  C  CG  . ARG A 1 87  ? 28.128  50.129 34.275 1.00 11.81 ? 87  ARG A CG  1 
ATOM   665  C  CD  . ARG A 1 87  ? 28.193  48.652 34.044 1.00 11.15 ? 87  ARG A CD  1 
ATOM   666  N  NE  . ARG A 1 87  ? 28.305  48.321 32.619 1.00 11.78 ? 87  ARG A NE  1 
ATOM   667  C  CZ  . ARG A 1 87  ? 27.292  48.176 31.795 1.00 11.84 ? 87  ARG A CZ  1 
ATOM   668  N  NH1 . ARG A 1 87  ? 26.016  48.170 32.271 1.00 13.04 ? 87  ARG A NH1 1 
ATOM   669  N  NH2 . ARG A 1 87  ? 27.476  47.936 30.525 1.00 15.27 ? 87  ARG A NH2 1 
ATOM   670  N  N   . ILE A 1 88  ? 27.256  50.282 38.720 1.00 10.57 ? 88  ILE A N   1 
ATOM   671  C  CA  . ILE A 1 88  ? 27.701  50.725 40.044 1.00 11.19 ? 88  ILE A CA  1 
ATOM   672  C  C   . ILE A 1 88  ? 29.227  50.639 40.063 1.00 10.18 ? 88  ILE A C   1 
ATOM   673  O  O   . ILE A 1 88  ? 29.783  49.672 39.508 1.00 11.68 ? 88  ILE A O   1 
ATOM   674  C  CB  . ILE A 1 88  ? 27.052  49.954 41.168 1.00 12.86 ? 88  ILE A CB  1 
ATOM   675  C  CG1 . ILE A 1 88  ? 26.833  50.623 42.470 1.00 15.93 ? 88  ILE A CG1 1 
ATOM   676  C  CG2 . ILE A 1 88  ? 27.491  48.527 41.236 1.00 18.43 ? 88  ILE A CG2 1 
ATOM   677  C  CD1 . ILE A 1 88  ? 26.009  49.949 43.523 1.00 16.61 ? 88  ILE A CD1 1 
ATOM   678  N  N   . LEU A 1 89  ? 29.852  51.655 40.639 1.00 10.80 ? 89  LEU A N   1 
ATOM   679  C  CA  . LEU A 1 89  ? 31.310  51.741 40.770 1.00 12.15 ? 89  LEU A CA  1 
ATOM   680  C  C   . LEU A 1 89  ? 31.603  51.790 42.268 1.00 12.67 ? 89  LEU A C   1 
ATOM   681  O  O   . LEU A 1 89  ? 31.058  52.622 42.983 1.00 13.69 ? 89  LEU A O   1 
ATOM   682  C  CB  . LEU A 1 89  ? 31.852  52.986 40.058 1.00 15.13 ? 89  LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 89  ? 32.111  52.895 38.571 1.00 16.78 ? 89  LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 89  ? 33.290  52.024 38.207 1.00 17.34 ? 89  LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 89  ? 30.879  52.547 37.777 1.00 21.29 ? 89  LEU A CD2 1 
ATOM   686  N  N   . TYR A 1 90  ? 32.414  50.838 42.759 1.00 13.10 ? 90  TYR A N   1 
ATOM   687  C  CA  . TYR A 1 90  ? 32.742  50.761 44.158 1.00 13.64 ? 90  TYR A CA  1 
ATOM   688  C  C   . TYR A 1 90  ? 34.241  50.653 44.391 1.00 14.29 ? 90  TYR A C   1 
ATOM   689  O  O   . TYR A 1 90  ? 34.929  49.939 43.666 1.00 15.57 ? 90  TYR A O   1 
ATOM   690  C  CB  . TYR A 1 90  ? 31.991  49.643 44.858 1.00 13.47 ? 90  TYR A CB  1 
ATOM   691  C  CG  . TYR A 1 90  ? 32.251  48.255 44.318 1.00 15.86 ? 90  TYR A CG  1 
ATOM   692  C  CD1 . TYR A 1 90  ? 31.605  47.780 43.183 1.00 16.58 ? 90  TYR A CD1 1 
ATOM   693  C  CD2 . TYR A 1 90  ? 33.071  47.380 45.017 1.00 16.05 ? 90  TYR A CD2 1 
ATOM   694  C  CE1 . TYR A 1 90  ? 31.823  46.507 42.709 1.00 18.04 ? 90  TYR A CE1 1 
ATOM   695  C  CE2 . TYR A 1 90  ? 33.282  46.084 44.537 1.00 17.45 ? 90  TYR A CE2 1 
ATOM   696  C  CZ  . TYR A 1 90  ? 32.670  45.657 43.394 1.00 18.19 ? 90  TYR A CZ  1 
ATOM   697  O  OH  . TYR A 1 90  ? 32.853  44.348 42.927 1.00 19.13 ? 90  TYR A OH  1 
ATOM   698  N  N   . SER A 1 91  ? 34.726  51.367 45.395 1.00 16.53 ? 91  SER A N   1 
ATOM   699  C  CA  . SER A 1 91  ? 36.151  51.404 45.698 1.00 16.94 ? 91  SER A CA  1 
ATOM   700  C  C   . SER A 1 91  ? 36.489  50.455 46.843 1.00 17.17 ? 91  SER A C   1 
ATOM   701  O  O   . SER A 1 91  ? 35.587  49.958 47.532 1.00 16.81 ? 91  SER A O   1 
ATOM   702  C  CB  . SER A 1 91  ? 36.586  52.827 46.061 1.00 16.27 ? 91  SER A CB  1 
ATOM   703  O  OG  . SER A 1 91  ? 35.998  53.194 47.336 1.00 17.78 ? 91  SER A OG  1 
ATOM   704  N  N   . SER A 1 92  ? 37.767  50.221 47.032 1.00 18.11 ? 92  SER A N   1 
ATOM   705  C  CA  . SER A 1 92  ? 38.284  49.342 48.058 1.00 18.36 ? 92  SER A CA  1 
ATOM   706  C  C   . SER A 1 92  ? 38.041  49.920 49.451 1.00 19.91 ? 92  SER A C   1 
ATOM   707  O  O   . SER A 1 92  ? 38.030  49.181 50.443 1.00 23.28 ? 92  SER A O   1 
ATOM   708  C  CB  . SER A 1 92  ? 39.777  49.076 47.858 1.00 20.49 ? 92  SER A CB  1 
ATOM   709  O  OG  . SER A 1 92  ? 40.449  50.239 47.486 1.00 27.50 ? 92  SER A OG  1 
ATOM   710  N  N   . ASP A 1 93  ? 37.670  51.190 49.491 1.00 19.65 ? 93  ASP A N   1 
ATOM   711  C  CA  . ASP A 1 93  ? 37.288  51.858 50.714 1.00 19.47 ? 93  ASP A CA  1 
ATOM   712  C  C   . ASP A 1 93  ? 35.823  52.181 50.786 1.00 18.67 ? 93  ASP A C   1 
ATOM   713  O  O   . ASP A 1 93  ? 35.352  52.975 51.591 1.00 17.88 ? 93  ASP A O   1 
ATOM   714  C  CB  . ASP A 1 93  ? 38.187  52.996 51.090 1.00 20.58 ? 93  ASP A CB  1 
ATOM   715  C  CG  . ASP A 1 93  ? 38.342  54.104 50.095 1.00 21.73 ? 93  ASP A CG  1 
ATOM   716  O  OD1 . ASP A 1 93  ? 38.025  53.906 48.911 1.00 19.83 ? 93  ASP A OD1 1 
ATOM   717  O  OD2 . ASP A 1 93  ? 38.842  55.207 50.493 1.00 24.26 ? 93  ASP A OD2 1 
ATOM   718  N  N   . TRP A 1 94  ? 35.005  51.560 49.918 1.00 16.89 ? 94  TRP A N   1 
ATOM   719  C  CA  . TRP A 1 94  ? 33.585  51.604 50.050 1.00 17.13 ? 94  TRP A CA  1 
ATOM   720  C  C   . TRP A 1 94  ? 32.859  52.853 49.721 1.00 16.24 ? 94  TRP A C   1 
ATOM   721  O  O   . TRP A 1 94  ? 31.681  53.071 50.084 1.00 17.68 ? 94  TRP A O   1 
ATOM   722  C  CB  . TRP A 1 94  ? 33.081  50.848 51.268 1.00 20.14 ? 94  TRP A CB  1 
ATOM   723  C  CG  . TRP A 1 94  ? 33.759  49.506 51.378 1.00 22.03 ? 94  TRP A CG  1 
ATOM   724  C  CD1 . TRP A 1 94  ? 34.700  49.131 52.294 1.00 22.23 ? 94  TRP A CD1 1 
ATOM   725  C  CD2 . TRP A 1 94  ? 33.605  48.402 50.478 1.00 24.21 ? 94  TRP A CD2 1 
ATOM   726  N  NE1 . TRP A 1 94  ? 35.117  47.850 52.028 1.00 24.16 ? 94  TRP A NE1 1 
ATOM   727  C  CE2 . TRP A 1 94  ? 34.449  47.375 50.927 1.00 25.63 ? 94  TRP A CE2 1 
ATOM   728  C  CE3 . TRP A 1 94  ? 32.811  48.175 49.350 1.00 25.72 ? 94  TRP A CE3 1 
ATOM   729  C  CZ2 . TRP A 1 94  ? 34.528  46.144 50.284 1.00 27.25 ? 94  TRP A CZ2 1 
ATOM   730  C  CZ3 . TRP A 1 94  ? 32.885  46.945 48.711 1.00 27.39 ? 94  TRP A CZ3 1 
ATOM   731  C  CH2 . TRP A 1 94  ? 33.736  45.939 49.185 1.00 28.37 ? 94  TRP A CH2 1 
ATOM   732  N  N   . LEU A 1 95  ? 33.462  53.668 48.843 1.00 16.63 ? 95  LEU A N   1 
ATOM   733  C  CA  . LEU A 1 95  ? 32.736  54.759 48.180 1.00 15.78 ? 95  LEU A CA  1 
ATOM   734  C  C   . LEU A 1 95  ? 31.932  54.165 47.013 1.00 16.02 ? 95  LEU A C   1 
ATOM   735  O  O   . LEU A 1 95  ? 32.433  53.212 46.350 1.00 16.65 ? 95  LEU A O   1 
ATOM   736  C  CB  . LEU A 1 95  ? 33.759  55.732 47.602 1.00 17.28 ? 95  LEU A CB  1 
ATOM   737  C  CG  . LEU A 1 95  ? 34.725  56.433 48.533 1.00 20.23 ? 95  LEU A CG  1 
ATOM   738  C  CD1 . LEU A 1 95  ? 35.655  57.339 47.697 1.00 24.99 ? 95  LEU A CD1 1 
ATOM   739  C  CD2 . LEU A 1 95  ? 33.986  57.294 49.548 1.00 22.76 ? 95  LEU A CD2 1 
ATOM   740  N  N   . ILE A 1 96  ? 30.723  54.622 46.813 1.00 13.46 ? 96  ILE A N   1 
ATOM   741  C  CA  . ILE A 1 96  ? 29.869  54.035 45.760 1.00 12.81 ? 96  ILE A CA  1 
ATOM   742  C  C   . ILE A 1 96  ? 29.335  55.142 44.842 1.00 11.36 ? 96  ILE A C   1 
ATOM   743  O  O   . ILE A 1 96  ? 28.756  56.096 45.329 1.00 11.74 ? 96  ILE A O   1 
ATOM   744  C  CB  A ILE A 1 96  ? 28.623  53.376 46.423 0.50 13.28 ? 96  ILE A CB  1 
ATOM   745  C  CB  B ILE A 1 96  ? 28.716  53.221 46.329 0.50 13.18 ? 96  ILE A CB  1 
ATOM   746  C  CG1 A ILE A 1 96  ? 28.976  52.574 47.680 0.50 14.18 ? 96  ILE A CG1 1 
ATOM   747  C  CG1 B ILE A 1 96  ? 29.162  52.165 47.360 0.50 13.90 ? 96  ILE A CG1 1 
ATOM   748  C  CG2 A ILE A 1 96  ? 27.901  52.505 45.412 0.50 14.91 ? 96  ILE A CG2 1 
ATOM   749  C  CG2 B ILE A 1 96  ? 27.910  52.556 45.217 0.50 13.78 ? 96  ILE A CG2 1 
ATOM   750  C  CD1 A ILE A 1 96  ? 29.596  51.228 47.356 0.50 14.47 ? 96  ILE A CD1 1 
ATOM   751  C  CD1 B ILE A 1 96  ? 28.036  51.337 47.902 0.50 17.78 ? 96  ILE A CD1 1 
ATOM   752  N  N   . TYR A 1 97  ? 29.557  54.974 43.556 1.00 10.22 ? 97  TYR A N   1 
ATOM   753  C  CA  . TYR A 1 97  ? 29.127  55.886 42.523 1.00 10.88 ? 97  TYR A CA  1 
ATOM   754  C  C   . TYR A 1 97  ? 28.232  55.128 41.538 1.00 11.72 ? 97  TYR A C   1 
ATOM   755  O  O   . TYR A 1 97  ? 28.293  53.906 41.391 1.00 12.21 ? 97  TYR A O   1 
ATOM   756  C  CB  . TYR A 1 97  ? 30.327  56.512 41.782 1.00 12.41 ? 97  TYR A CB  1 
ATOM   757  C  CG  . TYR A 1 97  ? 31.008  57.600 42.569 1.00 11.71 ? 97  TYR A CG  1 
ATOM   758  C  CD1 . TYR A 1 97  ? 31.861  57.282 43.633 1.00 11.99 ? 97  TYR A CD1 1 
ATOM   759  C  CD2 . TYR A 1 97  ? 30.825  58.949 42.286 1.00 12.71 ? 97  TYR A CD2 1 
ATOM   760  C  CE1 . TYR A 1 97  ? 32.477  58.253 44.403 1.00 13.43 ? 97  TYR A CE1 1 
ATOM   761  C  CE2 . TYR A 1 97  ? 31.464  59.915 43.052 1.00 14.09 ? 97  TYR A CE2 1 
ATOM   762  C  CZ  . TYR A 1 97  ? 32.329  59.571 44.056 1.00 14.00 ? 97  TYR A CZ  1 
ATOM   763  O  OH  . TYR A 1 97  ? 32.913  60.557 44.840 1.00 14.92 ? 97  TYR A OH  1 
ATOM   764  N  N   . LYS A 1 98  ? 27.439  55.905 40.842 1.00 11.31 ? 98  LYS A N   1 
ATOM   765  C  CA  . LYS A 1 98  ? 26.570  55.380 39.791 1.00 14.92 ? 98  LYS A CA  1 
ATOM   766  C  C   . LYS A 1 98  ? 26.864  56.075 38.476 1.00 11.02 ? 98  LYS A C   1 
ATOM   767  O  O   . LYS A 1 98  ? 27.154  57.276 38.444 1.00 14.20 ? 98  LYS A O   1 
ATOM   768  C  CB  . LYS A 1 98  ? 25.141  55.574 40.212 1.00 19.73 ? 98  LYS A CB  1 
ATOM   769  C  CG  . LYS A 1 98  ? 24.180  56.287 39.373 1.00 22.04 ? 98  LYS A CG  1 
ATOM   770  C  CD  . LYS A 1 98  ? 22.767  56.173 39.905 1.00 23.86 ? 98  LYS A CD  1 
ATOM   771  C  CE  . LYS A 1 98  ? 22.158  57.511 40.237 1.00 25.31 ? 98  LYS A CE  1 
ATOM   772  N  NZ  . LYS A 1 98  ? 20.653  57.400 40.132 1.00 32.15 ? 98  LYS A NZ  1 
ATOM   773  N  N   . THR A 1 99  ? 26.703  55.332 37.396 1.00 11.21 ? 99  THR A N   1 
ATOM   774  C  CA  . THR A 1 99  ? 26.631  55.867 36.065 1.00 13.28 ? 99  THR A CA  1 
ATOM   775  C  C   . THR A 1 99  ? 25.416  55.268 35.345 1.00 13.45 ? 99  THR A C   1 
ATOM   776  O  O   . THR A 1 99  ? 25.129  54.072 35.519 1.00 13.47 ? 99  THR A O   1 
ATOM   777  C  CB  . THR A 1 99  ? 27.894  55.709 35.235 1.00 13.61 ? 99  THR A CB  1 
ATOM   778  O  OG1 . THR A 1 99  ? 27.742  56.188 33.910 1.00 14.56 ? 99  THR A OG1 1 
ATOM   779  C  CG2 . THR A 1 99  ? 28.291  54.230 35.090 1.00 13.95 ? 99  THR A CG2 1 
ATOM   780  N  N   . THR A 1 100 ? 24.715  56.060 34.566 1.00 14.21 ? 100 THR A N   1 
ATOM   781  C  CA  . THR A 1 100 ? 23.619  55.522 33.745 1.00 15.00 ? 100 THR A CA  1 
ATOM   782  C  C   . THR A 1 100 ? 23.861  55.860 32.280 1.00 15.62 ? 100 THR A C   1 
ATOM   783  O  O   . THR A 1 100 ? 22.961  55.769 31.450 1.00 18.33 ? 100 THR A O   1 
ATOM   784  C  CB  . THR A 1 100 ? 22.255  56.088 34.187 1.00 15.50 ? 100 THR A CB  1 
ATOM   785  O  OG1 . THR A 1 100 ? 22.323  57.510 34.193 1.00 19.63 ? 100 THR A OG1 1 
ATOM   786  C  CG2 . THR A 1 100 ? 21.916  55.646 35.595 1.00 18.50 ? 100 THR A CG2 1 
ATOM   787  N  N   . ASP A 1 101 ? 25.092  56.285 31.982 1.00 17.78 ? 101 ASP A N   1 
ATOM   788  C  CA  . ASP A 1 101 ? 25.448  56.719 30.639 1.00 18.50 ? 101 ASP A CA  1 
ATOM   789  C  C   . ASP A 1 101 ? 26.698  56.096 30.100 1.00 18.57 ? 101 ASP A C   1 
ATOM   790  O  O   . ASP A 1 101 ? 27.512  56.725 29.412 1.00 21.06 ? 101 ASP A O   1 
ATOM   791  C  CB  . ASP A 1 101 ? 25.473  58.242 30.555 1.00 18.97 ? 101 ASP A CB  1 
ATOM   792  C  CG  . ASP A 1 101 ? 26.502  58.918 31.411 1.00 18.39 ? 101 ASP A CG  1 
ATOM   793  O  OD1 . ASP A 1 101 ? 27.330  58.261 32.057 1.00 18.63 ? 101 ASP A OD1 1 
ATOM   794  O  OD2 . ASP A 1 101 ? 26.501  60.183 31.418 1.00 22.23 ? 101 ASP A OD2 1 
ATOM   795  N  N   . HIS A 1 102 ? 26.937  54.822 30.461 1.00 19.35 ? 102 HIS A N   1 
ATOM   796  C  CA  . HIS A 1 102 ? 28.104  54.110 29.968 1.00 18.33 ? 102 HIS A CA  1 
ATOM   797  C  C   . HIS A 1 102 ? 29.412  54.793 30.363 1.00 17.70 ? 102 HIS A C   1 
ATOM   798  O  O   . HIS A 1 102 ? 30.316  54.941 29.549 1.00 20.81 ? 102 HIS A O   1 
ATOM   799  C  CB  . HIS A 1 102 ? 28.066  53.916 28.440 1.00 23.18 ? 102 HIS A CB  1 
ATOM   800  C  CG  . HIS A 1 102 ? 27.578  52.571 28.033 1.00 26.09 ? 102 HIS A CG  1 
ATOM   801  N  ND1 . HIS A 1 102 ? 26.337  52.378 27.444 1.00 30.22 ? 102 HIS A ND1 1 
ATOM   802  C  CD2 . HIS A 1 102 ? 28.104  51.325 28.205 1.00 28.68 ? 102 HIS A CD2 1 
ATOM   803  C  CE1 . HIS A 1 102 ? 26.132  51.100 27.275 1.00 33.19 ? 102 HIS A CE1 1 
ATOM   804  N  NE2 . HIS A 1 102 ? 27.185  50.440 27.744 1.00 32.82 ? 102 HIS A NE2 1 
ATOM   805  N  N   . TYR A 1 103 ? 29.534  55.160 31.633 1.00 17.45 ? 103 TYR A N   1 
ATOM   806  C  CA  . TYR A 1 103 ? 30.778  55.637 32.213 1.00 19.43 ? 103 TYR A CA  1 
ATOM   807  C  C   . TYR A 1 103 ? 31.152  57.036 31.801 1.00 20.70 ? 103 TYR A C   1 
ATOM   808  O  O   . TYR A 1 103 ? 32.322  57.451 31.990 1.00 22.74 ? 103 TYR A O   1 
ATOM   809  C  CB  . TYR A 1 103 ? 31.941  54.690 31.970 1.00 20.36 ? 103 TYR A CB  1 
ATOM   810  C  CG  . TYR A 1 103 ? 31.699  53.215 32.088 1.00 19.16 ? 103 TYR A CG  1 
ATOM   811  C  CD1 . TYR A 1 103 ? 31.786  52.519 33.276 1.00 17.53 ? 103 TYR A CD1 1 
ATOM   812  C  CD2 . TYR A 1 103 ? 31.517  52.456 30.912 1.00 21.63 ? 103 TYR A CD2 1 
ATOM   813  C  CE1 . TYR A 1 103 ? 31.599  51.129 33.312 1.00 15.87 ? 103 TYR A CE1 1 
ATOM   814  C  CE2 . TYR A 1 103 ? 31.280  51.108 30.953 1.00 19.00 ? 103 TYR A CE2 1 
ATOM   815  C  CZ  . TYR A 1 103 ? 31.347  50.437 32.168 1.00 15.41 ? 103 TYR A CZ  1 
ATOM   816  O  OH  . TYR A 1 103 ? 31.143  49.061 32.161 1.00 18.13 ? 103 TYR A OH  1 
ATOM   817  N  N   . GLN A 1 104 ? 30.238  57.807 31.221 1.00 19.88 ? 104 GLN A N   1 
ATOM   818  C  CA  . GLN A 1 104 ? 30.617  59.181 30.831 1.00 21.35 ? 104 GLN A CA  1 
ATOM   819  C  C   . GLN A 1 104 ? 30.586  60.118 32.026 1.00 21.37 ? 104 GLN A C   1 
ATOM   820  O  O   . GLN A 1 104 ? 31.447  60.985 32.169 1.00 24.13 ? 104 GLN A O   1 
ATOM   821  C  CB  . GLN A 1 104 ? 29.657  59.691 29.760 1.00 21.71 ? 104 GLN A CB  1 
ATOM   822  C  CG  . GLN A 1 104 ? 29.776  58.921 28.453 1.00 32.05 ? 104 GLN A CG  1 
ATOM   823  C  CD  . GLN A 1 104 ? 28.840  59.460 27.391 1.00 32.02 ? 104 GLN A CD  1 
ATOM   824  O  OE1 . GLN A 1 104 ? 29.242  60.269 26.570 1.00 32.95 ? 104 GLN A OE1 1 
ATOM   825  N  NE2 . GLN A 1 104 ? 27.583  59.008 27.445 1.00 35.06 ? 104 GLN A NE2 1 
ATOM   826  N  N   . THR A 1 105 ? 29.555  59.966 32.856 1.00 21.35 ? 105 THR A N   1 
ATOM   827  C  CA  . THR A 1 105 ? 29.432  60.791 34.054 1.00 22.99 ? 105 THR A CA  1 
ATOM   828  C  C   . THR A 1 105 ? 29.050  59.899 35.245 1.00 18.49 ? 105 THR A C   1 
ATOM   829  O  O   . THR A 1 105 ? 28.453  58.859 35.090 1.00 15.88 ? 105 THR A O   1 
ATOM   830  C  CB  . THR A 1 105 ? 28.388  61.894 33.902 1.00 25.14 ? 105 THR A CB  1 
ATOM   831  O  OG1 . THR A 1 105 ? 27.090  61.367 33.781 1.00 23.71 ? 105 THR A OG1 1 
ATOM   832  C  CG2 . THR A 1 105 ? 28.656  62.762 32.683 1.00 24.95 ? 105 THR A CG2 1 
ATOM   833  N  N   . PHE A 1 106 ? 29.443  60.377 36.418 1.00 16.86 ? 106 PHE A N   1 
ATOM   834  C  CA  . PHE A 1 106 ? 29.228  59.634 37.647 1.00 14.44 ? 106 PHE A CA  1 
ATOM   835  C  C   . PHE A 1 106 ? 28.630  60.571 38.706 1.00 13.97 ? 106 PHE A C   1 
ATOM   836  O  O   . PHE A 1 106 ? 29.004  61.739 38.750 1.00 17.83 ? 106 PHE A O   1 
ATOM   837  C  CB  . PHE A 1 106 ? 30.584  59.122 38.171 1.00 15.80 ? 106 PHE A CB  1 
ATOM   838  C  CG  . PHE A 1 106 ? 31.277  58.166 37.234 1.00 16.33 ? 106 PHE A CG  1 
ATOM   839  C  CD1 . PHE A 1 106 ? 30.988  56.812 37.196 1.00 16.79 ? 106 PHE A CD1 1 
ATOM   840  C  CD2 . PHE A 1 106 ? 32.234  58.675 36.352 1.00 16.89 ? 106 PHE A CD2 1 
ATOM   841  C  CE1 . PHE A 1 106 ? 31.595  55.960 36.282 1.00 16.81 ? 106 PHE A CE1 1 
ATOM   842  C  CE2 . PHE A 1 106 ? 32.853  57.816 35.462 1.00 17.23 ? 106 PHE A CE2 1 
ATOM   843  C  CZ  . PHE A 1 106 ? 32.576  56.472 35.473 1.00 17.40 ? 106 PHE A CZ  1 
ATOM   844  N  N   . THR A 1 107 ? 27.826  59.993 39.569 1.00 13.00 ? 107 THR A N   1 
ATOM   845  C  CA  . THR A 1 107 ? 27.361  60.727 40.752 1.00 13.97 ? 107 THR A CA  1 
ATOM   846  C  C   . THR A 1 107 ? 27.481  59.830 41.978 1.00 13.43 ? 107 THR A C   1 
ATOM   847  O  O   . THR A 1 107 ? 27.308  58.600 41.877 1.00 11.77 ? 107 THR A O   1 
ATOM   848  C  CB  . THR A 1 107 ? 25.901  61.175 40.593 1.00 14.59 ? 107 THR A CB  1 
ATOM   849  O  OG1 . THR A 1 107 ? 25.065  60.072 40.377 1.00 19.65 ? 107 THR A OG1 1 
ATOM   850  C  CG2 . THR A 1 107 ? 25.764  62.162 39.467 1.00 16.06 ? 107 THR A CG2 1 
ATOM   851  N  N   . LYS A 1 108 ? 27.772  60.423 43.111 1.00 11.11 ? 108 LYS A N   1 
ATOM   852  C  CA  . LYS A 1 108 ? 27.924  59.599 44.349 1.00 10.65 ? 108 LYS A CA  1 
ATOM   853  C  C   . LYS A 1 108 ? 26.552  59.170 44.858 1.00 10.00 ? 108 LYS A C   1 
ATOM   854  O  O   . LYS A 1 108 ? 25.592  59.958 44.873 1.00 11.99 ? 108 LYS A O   1 
ATOM   855  C  CB  . LYS A 1 108 ? 28.537  60.542 45.403 1.00 12.38 ? 108 LYS A CB  1 
ATOM   856  C  CG  . LYS A 1 108 ? 28.868  59.876 46.714 1.00 12.26 ? 108 LYS A CG  1 
ATOM   857  C  CD  . LYS A 1 108 ? 29.582  60.886 47.647 1.00 15.49 ? 108 LYS A CD  1 
ATOM   858  C  CE  . LYS A 1 108 ? 29.741  60.298 49.034 1.00 14.76 ? 108 LYS A CE  1 
ATOM   859  N  NZ  . LYS A 1 108 ? 30.747  59.205 49.066 1.00 18.56 ? 108 LYS A NZ  1 
ATOM   860  N  N   . ILE A 1 109 ? 26.435  57.920 45.294 1.00 10.25 ? 109 ILE A N   1 
ATOM   861  C  CA  . ILE A 1 109 ? 25.209  57.445 45.913 1.00 10.96 ? 109 ILE A CA  1 
ATOM   862  C  C   . ILE A 1 109 ? 25.423  56.879 47.315 1.00 11.60 ? 109 ILE A C   1 
ATOM   863  O  O   . ILE A 1 109 ? 24.428  56.729 48.032 1.00 12.61 ? 109 ILE A O   1 
ATOM   864  C  CB  . ILE A 1 109 ? 24.488  56.412 45.036 1.00 11.43 ? 109 ILE A CB  1 
ATOM   865  C  CG1 . ILE A 1 109 ? 25.244  55.151 44.716 1.00 12.61 ? 109 ILE A CG1 1 
ATOM   866  C  CG2 . ILE A 1 109 ? 23.931  57.101 43.806 1.00 12.56 ? 109 ILE A CG2 1 
ATOM   867  C  CD1 . ILE A 1 109 ? 24.460  53.993 44.160 1.00 13.99 ? 109 ILE A CD1 1 
ATOM   868  N  N   . ARG A 1 110 ? 26.646  56.621 47.736 1.00 12.10 ? 110 ARG A N   1 
ATOM   869  C  CA  . ARG A 1 110 ? 27.033  56.297 49.061 1.00 12.73 ? 110 ARG A CA  1 
ATOM   870  C  C   . ARG A 1 110 ? 28.442  56.843 49.414 1.00 14.19 ? 110 ARG A C   1 
ATOM   871  O  O   . ARG A 1 110 ? 28.707  57.047 50.614 1.00 20.57 ? 110 ARG A O   1 
ATOM   872  C  CB  . ARG A 1 110 ? 26.957  54.879 49.506 1.00 13.31 ? 110 ARG A CB  1 
ATOM   873  C  CG  . ARG A 1 110 ? 25.692  54.073 49.245 1.00 13.37 ? 110 ARG A CG  1 
ATOM   874  C  CD  . ARG A 1 110 ? 24.573  54.428 50.204 1.00 14.07 ? 110 ARG A CD  1 
ATOM   875  N  NE  . ARG A 1 110 ? 23.404  53.563 50.069 1.00 14.69 ? 110 ARG A NE  1 
ATOM   876  C  CZ  . ARG A 1 110 ? 22.439  53.681 49.181 1.00 13.99 ? 110 ARG A CZ  1 
ATOM   877  N  NH1 . ARG A 1 110 ? 22.472  54.683 48.314 1.00 14.54 ? 110 ARG A NH1 1 
ATOM   878  N  NH2 . ARG A 1 110 ? 21.426  52.821 49.119 1.00 16.55 ? 110 ARG A NH2 1 
ATOM   879  O  OXT . ARG A 1 110 ? 29.332  56.795 48.546 1.00 14.66 ? 110 ARG A OXT 1 
ATOM   880  N  N   . VAL B 1 3   ? -17.297 34.921 57.728 0.00 35.21 ? 3   VAL B N   1 
ATOM   881  C  CA  . VAL B 1 3   ? -15.997 35.558 57.909 1.00 29.99 ? 3   VAL B CA  1 
ATOM   882  C  C   . VAL B 1 3   ? -14.868 34.655 57.423 1.00 30.05 ? 3   VAL B C   1 
ATOM   883  O  O   . VAL B 1 3   ? -15.027 33.427 57.376 1.00 35.82 ? 3   VAL B O   1 
ATOM   884  C  CB  . VAL B 1 3   ? -15.746 35.867 59.414 1.00 31.20 ? 3   VAL B CB  1 
ATOM   885  C  CG1 . VAL B 1 3   ? -17.005 36.280 60.111 1.00 32.55 ? 3   VAL B CG1 1 
ATOM   886  C  CG2 . VAL B 1 3   ? -15.081 34.680 60.080 1.00 34.75 ? 3   VAL B CG2 1 
ATOM   887  N  N   . ILE B 1 4   ? -13.701 35.226 57.118 1.00 22.20 ? 4   ILE B N   1 
ATOM   888  C  CA  . ILE B 1 4   ? -12.550 34.355 56.756 1.00 20.52 ? 4   ILE B CA  1 
ATOM   889  C  C   . ILE B 1 4   ? -11.611 34.326 57.968 1.00 19.66 ? 4   ILE B C   1 
ATOM   890  O  O   . ILE B 1 4   ? -11.014 35.333 58.311 1.00 19.67 ? 4   ILE B O   1 
ATOM   891  C  CB  . ILE B 1 4   ? -11.781 34.947 55.554 1.00 21.92 ? 4   ILE B CB  1 
ATOM   892  C  CG1 . ILE B 1 4   ? -12.634 35.216 54.330 1.00 22.02 ? 4   ILE B CG1 1 
ATOM   893  C  CG2 . ILE B 1 4   ? -10.584 34.064 55.215 1.00 22.88 ? 4   ILE B CG2 1 
ATOM   894  C  CD1 . ILE B 1 4   ? -11.955 35.880 53.180 1.00 29.45 ? 4   ILE B CD1 1 
ATOM   895  N  N   . ASN B 1 5   ? -11.580 33.181 58.642 1.00 16.71 ? 5   ASN B N   1 
ATOM   896  C  CA  . ASN B 1 5   ? -10.778 33.049 59.854 1.00 15.80 ? 5   ASN B CA  1 
ATOM   897  C  C   . ASN B 1 5   ? -10.174 31.667 60.014 1.00 16.61 ? 5   ASN B C   1 
ATOM   898  O  O   . ASN B 1 5   ? -9.814  31.323 61.139 1.00 16.39 ? 5   ASN B O   1 
ATOM   899  C  CB  . ASN B 1 5   ? -11.646 33.408 61.069 1.00 16.35 ? 5   ASN B CB  1 
ATOM   900  C  CG  . ASN B 1 5   ? -12.636 32.323 61.415 1.00 19.11 ? 5   ASN B CG  1 
ATOM   901  O  OD1 . ASN B 1 5   ? -13.002 31.498 60.575 1.00 22.34 ? 5   ASN B OD1 1 
ATOM   902  N  ND2 . ASN B 1 5   ? -13.127 32.379 62.649 1.00 22.05 ? 5   ASN B ND2 1 
ATOM   903  N  N   . THR B 1 6   ? -10.022 30.924 58.918 1.00 14.70 ? 6   THR B N   1 
ATOM   904  C  CA  . THR B 1 6   ? -9.349  29.617 58.956 1.00 15.00 ? 6   THR B CA  1 
ATOM   905  C  C   . THR B 1 6   ? -7.895  29.735 58.533 1.00 14.02 ? 6   THR B C   1 
ATOM   906  O  O   . THR B 1 6   ? -7.498  30.711 57.861 1.00 13.44 ? 6   THR B O   1 
ATOM   907  C  CB  . THR B 1 6   ? -10.035 28.581 58.043 1.00 16.44 ? 6   THR B CB  1 
ATOM   908  O  OG1 . THR B 1 6   ? -10.063 29.066 56.710 1.00 18.33 ? 6   THR B OG1 1 
ATOM   909  C  CG2 . THR B 1 6   ? -11.474 28.358 58.490 1.00 19.59 ? 6   THR B CG2 1 
ATOM   910  N  N   . PHE B 1 7   ? -7.086  28.748 58.886 1.00 14.12 ? 7   PHE B N   1 
ATOM   911  C  CA  . PHE B 1 7   ? -5.661  28.820 58.494 1.00 14.03 ? 7   PHE B CA  1 
ATOM   912  C  C   . PHE B 1 7   ? -5.544  28.927 56.970 1.00 13.08 ? 7   PHE B C   1 
ATOM   913  O  O   . PHE B 1 7   ? -4.785  29.740 56.464 1.00 14.34 ? 7   PHE B O   1 
ATOM   914  C  CB  . PHE B 1 7   ? -4.919  27.572 58.968 1.00 14.48 ? 7   PHE B CB  1 
ATOM   915  C  CG  . PHE B 1 7   ? -4.530  27.607 60.423 1.00 14.65 ? 7   PHE B CG  1 
ATOM   916  C  CD1 . PHE B 1 7   ? -3.618  28.577 60.884 1.00 14.13 ? 7   PHE B CD1 1 
ATOM   917  C  CD2 . PHE B 1 7   ? -5.049  26.719 61.333 1.00 15.74 ? 7   PHE B CD2 1 
ATOM   918  C  CE1 . PHE B 1 7   ? -3.265  28.621 62.188 1.00 15.19 ? 7   PHE B CE1 1 
ATOM   919  C  CE2 . PHE B 1 7   ? -4.698  26.775 62.665 1.00 16.68 ? 7   PHE B CE2 1 
ATOM   920  C  CZ  . PHE B 1 7   ? -3.807  27.726 63.099 1.00 15.72 ? 7   PHE B CZ  1 
ATOM   921  N  N   . ASP B 1 8   ? -6.255  28.047 56.246 1.00 13.87 ? 8   ASP B N   1 
ATOM   922  C  CA  . ASP B 1 8   ? -6.118  28.049 54.774 1.00 15.11 ? 8   ASP B CA  1 
ATOM   923  C  C   . ASP B 1 8   ? -6.745  29.288 54.166 1.00 15.00 ? 8   ASP B C   1 
ATOM   924  O  O   . ASP B 1 8   ? -6.184  29.892 53.253 1.00 16.65 ? 8   ASP B O   1 
ATOM   925  C  CB  . ASP B 1 8   ? -6.736  26.782 54.194 1.00 19.11 ? 8   ASP B CB  1 
ATOM   926  C  CG  . ASP B 1 8   ? -5.872  25.554 54.355 1.00 23.86 ? 8   ASP B CG  1 
ATOM   927  O  OD1 . ASP B 1 8   ? -4.680  25.583 54.006 1.00 21.59 ? 8   ASP B OD1 1 
ATOM   928  O  OD2 . ASP B 1 8   ? -6.361  24.577 54.966 1.00 27.25 ? 8   ASP B OD2 1 
ATOM   929  N  N   . GLY B 1 9   ? -7.892  29.729 54.699 1.00 15.34 ? 9   GLY B N   1 
ATOM   930  C  CA  . GLY B 1 9   ? -8.560  30.912 54.119 1.00 16.02 ? 9   GLY B CA  1 
ATOM   931  C  C   . GLY B 1 9   ? -7.760  32.179 54.310 1.00 13.87 ? 9   GLY B C   1 
ATOM   932  O  O   . GLY B 1 9   ? -7.551  32.960 53.362 1.00 14.95 ? 9   GLY B O   1 
ATOM   933  N  N   . VAL B 1 10  ? -7.204  32.377 55.508 1.00 13.27 ? 10  VAL B N   1 
ATOM   934  C  CA  . VAL B 1 10  ? -6.375  33.550 55.755 1.00 12.86 ? 10  VAL B CA  1 
ATOM   935  C  C   . VAL B 1 10  ? -5.037  33.461 55.058 1.00 13.33 ? 10  VAL B C   1 
ATOM   936  O  O   . VAL B 1 10  ? -4.558  34.463 54.480 1.00 13.76 ? 10  VAL B O   1 
ATOM   937  C  CB  . VAL B 1 10  ? -6.229  33.816 57.268 1.00 13.78 ? 10  VAL B CB  1 
ATOM   938  C  CG1 . VAL B 1 10  ? -5.375  35.069 57.498 1.00 14.70 ? 10  VAL B CG1 1 
ATOM   939  C  CG2 . VAL B 1 10  ? -7.632  34.070 57.857 1.00 13.98 ? 10  VAL B CG2 1 
ATOM   940  N  N   . ALA B 1 11  ? -4.422  32.289 55.000 1.00 13.04 ? 11  ALA B N   1 
ATOM   941  C  CA  . ALA B 1 11  ? -3.158  32.111 54.309 1.00 13.33 ? 11  ALA B CA  1 
ATOM   942  C  C   . ALA B 1 11  ? -3.264  32.499 52.839 1.00 14.11 ? 11  ALA B C   1 
ATOM   943  O  O   . ALA B 1 11  ? -2.429  33.254 52.307 1.00 15.16 ? 11  ALA B O   1 
ATOM   944  C  CB  . ALA B 1 11  ? -2.626  30.699 54.433 1.00 13.79 ? 11  ALA B CB  1 
ATOM   945  N  N   . ASP B 1 12  ? -4.311  32.029 52.197 1.00 13.82 ? 12  ASP B N   1 
ATOM   946  C  CA  . ASP B 1 12  ? -4.542  32.284 50.770 1.00 15.33 ? 12  ASP B CA  1 
ATOM   947  C  C   . ASP B 1 12  ? -4.846  33.749 50.515 1.00 14.71 ? 12  ASP B C   1 
ATOM   948  O  O   . ASP B 1 12  ? -4.318  34.328 49.575 1.00 16.91 ? 12  ASP B O   1 
ATOM   949  C  CB  . ASP B 1 12  ? -5.567  31.367 50.188 1.00 17.59 ? 12  ASP B CB  1 
ATOM   950  C  CG  . ASP B 1 12  ? -5.089  29.933 50.031 1.00 22.40 ? 12  ASP B CG  1 
ATOM   951  O  OD1 . ASP B 1 12  ? -3.859  29.706 50.123 1.00 24.16 ? 12  ASP B OD1 1 
ATOM   952  O  OD2 . ASP B 1 12  ? -5.958  29.070 49.841 1.00 29.38 ? 12  ASP B OD2 1 
ATOM   953  N  N   . TYR B 1 13  ? -5.646  34.340 51.421 1.00 15.17 ? 13  TYR B N   1 
ATOM   954  C  CA  . TYR B 1 13  ? -5.997  35.766 51.284 1.00 15.51 ? 13  TYR B CA  1 
ATOM   955  C  C   . TYR B 1 13  ? -4.759  36.634 51.408 1.00 16.14 ? 13  TYR B C   1 
ATOM   956  O  O   . TYR B 1 13  ? -4.540  37.553 50.607 1.00 16.58 ? 13  TYR B O   1 
ATOM   957  C  CB  . TYR B 1 13  ? -7.058  36.157 52.294 1.00 15.55 ? 13  TYR B CB  1 
ATOM   958  C  CG  . TYR B 1 13  ? -7.754  37.476 52.060 1.00 16.34 ? 13  TYR B CG  1 
ATOM   959  C  CD1 . TYR B 1 13  ? -7.198  38.691 52.444 1.00 19.16 ? 13  TYR B CD1 1 
ATOM   960  C  CD2 . TYR B 1 13  ? -9.024  37.513 51.479 1.00 17.20 ? 13  TYR B CD2 1 
ATOM   961  C  CE1 . TYR B 1 13  ? -7.868  39.896 52.219 1.00 20.50 ? 13  TYR B CE1 1 
ATOM   962  C  CE2 . TYR B 1 13  ? -9.704  38.691 51.307 1.00 19.27 ? 13  TYR B CE2 1 
ATOM   963  C  CZ  . TYR B 1 13  ? -9.125  39.887 51.656 1.00 21.18 ? 13  TYR B CZ  1 
ATOM   964  O  OH  . TYR B 1 13  ? -9.821  41.084 51.508 1.00 23.87 ? 13  TYR B OH  1 
ATOM   965  N  N   . LEU B 1 14  ? -3.908  36.370 52.387 1.00 15.34 ? 14  LEU B N   1 
ATOM   966  C  CA  . LEU B 1 14  ? -2.670  37.108 52.571 1.00 15.36 ? 14  LEU B CA  1 
ATOM   967  C  C   . LEU B 1 14  ? -1.754  37.049 51.368 1.00 15.91 ? 14  LEU B C   1 
ATOM   968  O  O   . LEU B 1 14  ? -1.191  38.058 50.948 1.00 17.17 ? 14  LEU B O   1 
ATOM   969  C  CB  . LEU B 1 14  ? -1.920  36.626 53.810 1.00 15.73 ? 14  LEU B CB  1 
ATOM   970  C  CG  . LEU B 1 14  ? -2.472  37.065 55.155 1.00 16.12 ? 14  LEU B CG  1 
ATOM   971  C  CD1 . LEU B 1 14  ? -1.906  36.170 56.258 1.00 16.47 ? 14  LEU B CD1 1 
ATOM   972  C  CD2 . LEU B 1 14  ? -2.253  38.538 55.438 1.00 18.47 ? 14  LEU B CD2 1 
ATOM   973  N  N   . GLN B 1 15  ? -1.550  35.849 50.813 1.00 15.90 ? 15  GLN B N   1 
ATOM   974  C  CA  . GLN B 1 15  ? -0.611  35.706 49.682 1.00 17.07 ? 15  GLN B CA  1 
ATOM   975  C  C   . GLN B 1 15  ? -1.130  36.372 48.424 1.00 16.88 ? 15  GLN B C   1 
ATOM   976  O  O   . GLN B 1 15  ? -0.349  36.808 47.577 1.00 19.47 ? 15  GLN B O   1 
ATOM   977  C  CB  . GLN B 1 15  ? -0.285  34.241 49.444 1.00 17.26 ? 15  GLN B CB  1 
ATOM   978  C  CG  . GLN B 1 15  ? 0.520   33.590 50.552 1.00 18.34 ? 15  GLN B CG  1 
ATOM   979  C  CD  . GLN B 1 15  ? 1.306   32.383 50.087 1.00 18.72 ? 15  GLN B CD  1 
ATOM   980  O  OE1 . GLN B 1 15  ? 0.740   31.441 49.499 1.00 22.92 ? 15  GLN B OE1 1 
ATOM   981  N  NE2 . GLN B 1 15  ? 2.597   32.370 50.359 1.00 21.07 ? 15  GLN B NE2 1 
ATOM   982  N  N   . THR B 1 16  ? -2.439  36.476 48.274 1.00 18.25 ? 16  THR B N   1 
ATOM   983  C  CA  . THR B 1 16  ? -3.085  37.045 47.123 1.00 18.11 ? 16  THR B CA  1 
ATOM   984  C  C   . THR B 1 16  ? -3.287  38.554 47.204 1.00 19.59 ? 16  THR B C   1 
ATOM   985  O  O   . THR B 1 16  ? -3.039  39.266 46.218 1.00 21.99 ? 16  THR B O   1 
ATOM   986  C  CB  . THR B 1 16  ? -4.457  36.391 46.838 1.00 21.71 ? 16  THR B CB  1 
ATOM   987  O  OG1 . THR B 1 16  ? -4.295  34.960 46.727 1.00 28.19 ? 16  THR B OG1 1 
ATOM   988  C  CG2 . THR B 1 16  ? -5.037  36.871 45.531 1.00 22.18 ? 16  THR B CG2 1 
ATOM   989  N  N   . TYR B 1 17  ? -3.790  39.042 48.343 1.00 19.41 ? 17  TYR B N   1 
ATOM   990  C  CA  . TYR B 1 17  ? -4.140  40.426 48.527 1.00 19.68 ? 17  TYR B CA  1 
ATOM   991  C  C   . TYR B 1 17  ? -3.231  41.226 49.419 1.00 19.50 ? 17  TYR B C   1 
ATOM   992  O  O   . TYR B 1 17  ? -3.352  42.475 49.509 1.00 22.22 ? 17  TYR B O   1 
ATOM   993  C  CB  . TYR B 1 17  ? -5.612  40.587 48.952 1.00 21.87 ? 17  TYR B CB  1 
ATOM   994  C  CG  . TYR B 1 17  ? -6.556  39.849 48.029 1.00 25.07 ? 17  TYR B CG  1 
ATOM   995  C  CD1 . TYR B 1 17  ? -6.705  40.263 46.705 1.00 30.60 ? 17  TYR B CD1 1 
ATOM   996  C  CD2 . TYR B 1 17  ? -7.249  38.733 48.454 1.00 24.78 ? 17  TYR B CD2 1 
ATOM   997  C  CE1 . TYR B 1 17  ? -7.561  39.589 45.841 1.00 32.93 ? 17  TYR B CE1 1 
ATOM   998  C  CE2 . TYR B 1 17  ? -8.103  38.054 47.603 1.00 29.41 ? 17  TYR B CE2 1 
ATOM   999  C  CZ  . TYR B 1 17  ? -8.253  38.490 46.302 1.00 33.42 ? 17  TYR B CZ  1 
ATOM   1000 O  OH  . TYR B 1 17  ? -9.089  37.790 45.447 1.00 41.94 ? 17  TYR B OH  1 
ATOM   1001 N  N   . HIS B 1 18  ? -2.329  40.590 50.129 1.00 19.22 ? 18  HIS B N   1 
ATOM   1002 C  CA  . HIS B 1 18  ? -1.281  41.242 50.886 1.00 20.19 ? 18  HIS B CA  1 
ATOM   1003 C  C   . HIS B 1 18  ? -1.800  42.114 52.006 1.00 19.90 ? 18  HIS B C   1 
ATOM   1004 O  O   . HIS B 1 18  ? -1.192  43.120 52.382 1.00 23.27 ? 18  HIS B O   1 
ATOM   1005 C  CB  . HIS B 1 18  ? -0.371  42.062 49.967 1.00 24.02 ? 18  HIS B CB  1 
ATOM   1006 C  CG  . HIS B 1 18  ? 0.013   41.296 48.734 1.00 24.00 ? 18  HIS B CG  1 
ATOM   1007 N  ND1 . HIS B 1 18  ? -0.243  41.715 47.450 1.00 25.40 ? 18  HIS B ND1 1 
ATOM   1008 C  CD2 . HIS B 1 18  ? 0.570   40.051 48.645 1.00 24.79 ? 18  HIS B CD2 1 
ATOM   1009 C  CE1 . HIS B 1 18  ? 0.182   40.779 46.616 1.00 25.26 ? 18  HIS B CE1 1 
ATOM   1010 N  NE2 . HIS B 1 18  ? 0.669   39.768 47.315 1.00 25.72 ? 18  HIS B NE2 1 
ATOM   1011 N  N   . LYS B 1 19  ? -2.900  41.693 52.588 1.00 20.48 ? 19  LYS B N   1 
ATOM   1012 C  CA  . LYS B 1 19  ? -3.470  42.341 53.773 1.00 21.34 ? 19  LYS B CA  1 
ATOM   1013 C  C   . LYS B 1 19  ? -4.427  41.322 54.404 1.00 17.52 ? 19  LYS B C   1 
ATOM   1014 O  O   . LYS B 1 19  ? -4.768  40.326 53.743 1.00 20.08 ? 19  LYS B O   1 
ATOM   1015 C  CB  . LYS B 1 19  ? -4.234  43.601 53.381 1.00 23.97 ? 19  LYS B CB  1 
ATOM   1016 C  CG  . LYS B 1 19  ? -5.443  43.403 52.485 1.00 24.78 ? 19  LYS B CG  1 
ATOM   1017 C  CD  . LYS B 1 19  ? -5.986  44.783 52.048 1.00 25.99 ? 19  LYS B CD  1 
ATOM   1018 C  CE  . LYS B 1 19  ? -7.390  44.662 51.497 0.50 26.16 ? 19  LYS B CE  1 
ATOM   1019 N  NZ  . LYS B 1 19  ? -7.457  43.665 50.380 0.50 31.03 ? 19  LYS B NZ  1 
ATOM   1020 N  N   . LEU B 1 20  ? -4.837  41.580 55.634 1.00 17.45 ? 20  LEU B N   1 
ATOM   1021 C  CA  . LEU B 1 20  ? -5.816  40.704 56.268 1.00 18.43 ? 20  LEU B CA  1 
ATOM   1022 C  C   . LEU B 1 20  ? -7.216  41.026 55.742 1.00 17.47 ? 20  LEU B C   1 
ATOM   1023 O  O   . LEU B 1 20  ? -7.516  42.184 55.409 1.00 21.05 ? 20  LEU B O   1 
ATOM   1024 C  CB  . LEU B 1 20  ? -5.781  40.848 57.788 1.00 15.96 ? 20  LEU B CB  1 
ATOM   1025 C  CG  . LEU B 1 20  ? -4.549  40.293 58.514 1.00 16.41 ? 20  LEU B CG  1 
ATOM   1026 C  CD1 . LEU B 1 20  ? -4.425  40.918 59.897 1.00 16.83 ? 20  LEU B CD1 1 
ATOM   1027 C  CD2 . LEU B 1 20  ? -4.553  38.794 58.592 1.00 15.75 ? 20  LEU B CD2 1 
ATOM   1028 N  N   . PRO B 1 21  ? -8.095  40.045 55.844 1.00 18.84 ? 21  PRO B N   1 
ATOM   1029 C  CA  . PRO B 1 21  ? -9.520  40.255 55.545 1.00 19.40 ? 21  PRO B CA  1 
ATOM   1030 C  C   . PRO B 1 21  ? -10.135 41.270 56.506 1.00 19.89 ? 21  PRO B C   1 
ATOM   1031 O  O   . PRO B 1 21  ? -9.566  41.613 57.544 1.00 18.98 ? 21  PRO B O   1 
ATOM   1032 C  CB  . PRO B 1 21  ? -10.131 38.887 55.687 1.00 21.19 ? 21  PRO B CB  1 
ATOM   1033 C  CG  . PRO B 1 21  ? -9.048  37.921 55.921 1.00 21.48 ? 21  PRO B CG  1 
ATOM   1034 C  CD  . PRO B 1 21  ? -7.806  38.668 56.231 1.00 18.87 ? 21  PRO B CD  1 
ATOM   1035 N  N   . ASP B 1 22  ? -11.301 41.784 56.125 1.00 20.35 ? 22  ASP B N   1 
ATOM   1036 C  CA  . ASP B 1 22  ? -11.949 42.855 56.815 1.00 21.29 ? 22  ASP B CA  1 
ATOM   1037 C  C   . ASP B 1 22  ? -12.428 42.592 58.203 1.00 21.52 ? 22  ASP B C   1 
ATOM   1038 O  O   . ASP B 1 22  ? -12.738 43.551 58.960 1.00 24.77 ? 22  ASP B O   1 
ATOM   1039 C  CB  . ASP B 1 22  ? -13.022 43.512 55.921 1.00 21.58 ? 22  ASP B CB  1 
ATOM   1040 C  CG  . ASP B 1 22  ? -12.378 44.074 54.658 1.00 27.32 ? 22  ASP B CG  1 
ATOM   1041 O  OD1 . ASP B 1 22  ? -11.495 44.974 54.826 1.00 40.07 ? 22  ASP B OD1 1 
ATOM   1042 O  OD2 . ASP B 1 22  ? -12.765 43.688 53.555 0.30 38.37 ? 22  ASP B OD2 1 
ATOM   1043 N  N   . ASN B 1 23  ? -12.484 41.352 58.644 1.00 20.51 ? 23  ASN B N   1 
ATOM   1044 C  CA  . ASN B 1 23  ? -12.894 40.966 59.977 1.00 18.55 ? 23  ASN B CA  1 
ATOM   1045 C  C   . ASN B 1 23  ? -11.802 41.086 61.025 1.00 17.95 ? 23  ASN B C   1 
ATOM   1046 O  O   . ASN B 1 23  ? -12.062 40.785 62.214 1.00 20.51 ? 23  ASN B O   1 
ATOM   1047 C  CB  . ASN B 1 23  ? -13.531 39.578 59.999 1.00 21.14 ? 23  ASN B CB  1 
ATOM   1048 C  CG  . ASN B 1 23  ? -12.621 38.512 59.422 1.00 21.07 ? 23  ASN B CG  1 
ATOM   1049 O  OD1 . ASN B 1 23  ? -12.189 38.685 58.280 1.00 24.05 ? 23  ASN B OD1 1 
ATOM   1050 N  ND2 . ASN B 1 23  ? -12.273 37.519 60.181 1.00 22.47 ? 23  ASN B ND2 1 
ATOM   1051 N  N   . TYR B 1 24  ? -10.622 41.569 60.682 1.00 16.31 ? 24  TYR B N   1 
ATOM   1052 C  CA  . TYR B 1 24  ? -9.523  41.764 61.600 1.00 14.79 ? 24  TYR B CA  1 
ATOM   1053 C  C   . TYR B 1 24  ? -9.354  43.204 62.072 1.00 15.15 ? 24  TYR B C   1 
ATOM   1054 O  O   . TYR B 1 24  ? -9.431  44.158 61.289 1.00 18.30 ? 24  TYR B O   1 
ATOM   1055 C  CB  . TYR B 1 24  ? -8.196  41.237 61.035 1.00 15.61 ? 24  TYR B CB  1 
ATOM   1056 C  CG  . TYR B 1 24  ? -8.140  39.717 61.038 1.00 13.03 ? 24  TYR B CG  1 
ATOM   1057 C  CD1 . TYR B 1 24  ? -7.712  39.016 62.165 1.00 12.55 ? 24  TYR B CD1 1 
ATOM   1058 C  CD2 . TYR B 1 24  ? -8.587  38.984 59.948 1.00 13.59 ? 24  TYR B CD2 1 
ATOM   1059 C  CE1 . TYR B 1 24  ? -7.695  37.630 62.184 1.00 11.91 ? 24  TYR B CE1 1 
ATOM   1060 C  CE2 . TYR B 1 24  ? -8.555  37.596 59.953 1.00 12.66 ? 24  TYR B CE2 1 
ATOM   1061 C  CZ  . TYR B 1 24  ? -8.113  36.923 61.068 1.00 11.87 ? 24  TYR B CZ  1 
ATOM   1062 O  OH  . TYR B 1 24  ? -8.091  35.542 61.065 1.00 15.66 ? 24  TYR B OH  1 
ATOM   1063 N  N   . ILE B 1 25  ? -9.102  43.352 63.363 1.00 14.60 ? 25  ILE B N   1 
ATOM   1064 C  CA  . ILE B 1 25  ? -8.671  44.641 63.949 1.00 13.68 ? 25  ILE B CA  1 
ATOM   1065 C  C   . ILE B 1 25  ? -7.458  44.392 64.832 1.00 13.80 ? 25  ILE B C   1 
ATOM   1066 O  O   . ILE B 1 25  ? -7.278  43.306 65.385 1.00 13.11 ? 25  ILE B O   1 
ATOM   1067 C  CB  . ILE B 1 25  ? -9.813  45.266 64.780 1.00 14.61 ? 25  ILE B CB  1 
ATOM   1068 C  CG1 . ILE B 1 25  ? -10.335 44.337 65.893 1.00 16.77 ? 25  ILE B CG1 1 
ATOM   1069 C  CG2 . ILE B 1 25  ? -10.964 45.721 63.874 1.00 16.27 ? 25  ILE B CG2 1 
ATOM   1070 C  CD1 . ILE B 1 25  ? -11.387 45.022 66.753 1.00 16.75 ? 25  ILE B CD1 1 
ATOM   1071 N  N   . THR B 1 26  ? -6.626  45.417 65.048 1.00 15.27 ? 26  THR B N   1 
ATOM   1072 C  CA  . THR B 1 26  ? -5.454  45.232 65.895 1.00 15.05 ? 26  THR B CA  1 
ATOM   1073 C  C   . THR B 1 26  ? -5.823  45.300 67.374 1.00 14.45 ? 26  THR B C   1 
ATOM   1074 O  O   . THR B 1 26  ? -6.892  45.720 67.749 1.00 14.60 ? 26  THR B O   1 
ATOM   1075 C  CB  . THR B 1 26  ? -4.399  46.316 65.650 1.00 17.61 ? 26  THR B CB  1 
ATOM   1076 O  OG1 . THR B 1 26  ? -4.952  47.563 66.054 1.00 18.07 ? 26  THR B OG1 1 
ATOM   1077 C  CG2 . THR B 1 26  ? -4.016  46.413 64.180 1.00 18.83 ? 26  THR B CG2 1 
ATOM   1078 N  N   . LYS B 1 27  ? -4.853  44.875 68.225 1.00 14.66 ? 27  LYS B N   1 
ATOM   1079 C  CA  . LYS B 1 27  ? -5.077  44.882 69.655 1.00 15.02 ? 27  LYS B CA  1 
ATOM   1080 C  C   . LYS B 1 27  ? -5.429  46.286 70.151 1.00 13.82 ? 27  LYS B C   1 
ATOM   1081 O  O   . LYS B 1 27  ? -6.337  46.451 70.946 1.00 13.78 ? 27  LYS B O   1 
ATOM   1082 C  CB  . LYS B 1 27  ? -3.888  44.342 70.454 1.00 15.51 ? 27  LYS B CB  1 
ATOM   1083 C  CG  . LYS B 1 27  ? -3.704  42.859 70.399 1.00 22.12 ? 27  LYS B CG  1 
ATOM   1084 C  CD  . LYS B 1 27  ? -2.624  42.338 71.301 1.00 23.27 ? 27  LYS B CD  1 
ATOM   1085 C  CE  . LYS B 1 27  ? -1.216  42.535 70.752 1.00 25.87 ? 27  LYS B CE  1 
ATOM   1086 N  NZ  . LYS B 1 27  ? -1.078  42.066 69.345 1.00 31.70 ? 27  LYS B NZ  1 
ATOM   1087 N  N   . SER B 1 28  ? -4.703  47.281 69.647 1.00 15.26 ? 28  SER B N   1 
ATOM   1088 C  CA  . SER B 1 28  ? -4.973  48.659 70.047 1.00 17.35 ? 28  SER B CA  1 
ATOM   1089 C  C   . SER B 1 28  ? -6.314  49.168 69.571 1.00 16.38 ? 28  SER B C   1 
ATOM   1090 O  O   . SER B 1 28  ? -7.022  49.872 70.292 1.00 16.83 ? 28  SER B O   1 
ATOM   1091 C  CB  A SER B 1 28  ? -3.844  49.592 69.663 0.50 19.65 ? 28  SER B CB  1 
ATOM   1092 C  CB  B SER B 1 28  ? -3.845  49.574 69.548 0.50 18.81 ? 28  SER B CB  1 
ATOM   1093 O  OG  A SER B 1 28  ? -2.662  49.301 70.374 0.50 20.73 ? 28  SER B OG  1 
ATOM   1094 O  OG  B SER B 1 28  ? -3.841  49.632 68.127 0.50 24.23 ? 28  SER B OG  1 
ATOM   1095 N  N   . GLU B 1 29  ? -6.731  48.787 68.350 1.00 15.95 ? 29  GLU B N   1 
ATOM   1096 C  CA  . GLU B 1 29  ? -8.070  49.185 67.898 1.00 15.27 ? 29  GLU B CA  1 
ATOM   1097 C  C   . GLU B 1 29  ? -9.134  48.534 68.771 1.00 15.12 ? 29  GLU B C   1 
ATOM   1098 O  O   . GLU B 1 29  ? -10.163 49.142 69.076 1.00 14.74 ? 29  GLU B O   1 
ATOM   1099 C  CB  . GLU B 1 29  ? -8.283  48.737 66.440 1.00 16.68 ? 29  GLU B CB  1 
ATOM   1100 C  CG  . GLU B 1 29  ? -7.623  49.662 65.453 1.00 23.60 ? 29  GLU B CG  1 
ATOM   1101 C  CD  . GLU B 1 29  ? -7.435  49.141 64.061 1.00 28.98 ? 29  GLU B CD  1 
ATOM   1102 O  OE1 . GLU B 1 29  ? -7.676  47.939 63.771 1.00 23.36 ? 29  GLU B OE1 1 
ATOM   1103 O  OE2 . GLU B 1 29  ? -7.024  49.959 63.211 1.00 30.39 ? 29  GLU B OE2 1 
ATOM   1104 N  N   . ALA B 1 30  ? -8.924  47.258 69.097 1.00 11.80 ? 30  ALA B N   1 
ATOM   1105 C  CA  . ALA B 1 30  ? -9.880  46.574 69.943 1.00 10.60 ? 30  ALA B CA  1 
ATOM   1106 C  C   . ALA B 1 30  ? -9.992  47.259 71.304 1.00 9.99  ? 30  ALA B C   1 
ATOM   1107 O  O   . ALA B 1 30  ? -11.102 47.449 71.791 1.00 10.75 ? 30  ALA B O   1 
ATOM   1108 C  CB  . ALA B 1 30  ? -9.575  45.103 70.080 1.00 12.01 ? 30  ALA B CB  1 
ATOM   1109 N  N   . GLN B 1 31  ? -8.839  47.564 71.898 1.00 12.06 ? 31  GLN B N   1 
ATOM   1110 C  CA  . GLN B 1 31  ? -8.854  48.279 73.205 1.00 13.80 ? 31  GLN B CA  1 
ATOM   1111 C  C   . GLN B 1 31  ? -9.632  49.571 73.119 1.00 15.25 ? 31  GLN B C   1 
ATOM   1112 O  O   . GLN B 1 31  ? -10.378 49.898 74.075 1.00 14.98 ? 31  GLN B O   1 
ATOM   1113 C  CB  . GLN B 1 31  ? -7.408  48.533 73.650 1.00 15.71 ? 31  GLN B CB  1 
ATOM   1114 C  CG  . GLN B 1 31  ? -6.703  47.239 74.075 1.00 19.09 ? 31  GLN B CG  1 
ATOM   1115 C  CD  . GLN B 1 31  ? -5.237  47.430 74.382 1.00 23.68 ? 31  GLN B CD  1 
ATOM   1116 O  OE1 . GLN B 1 31  ? -4.625  48.413 73.952 1.00 32.43 ? 31  GLN B OE1 1 
ATOM   1117 N  NE2 . GLN B 1 31  ? -4.632  46.458 75.020 1.00 24.68 ? 31  GLN B NE2 1 
ATOM   1118 N  N   . ALA B 1 32  ? -9.521  50.304 72.018 1.00 15.41 ? 32  ALA B N   1 
ATOM   1119 C  CA  . ALA B 1 32  ? -10.247 51.573 71.874 1.00 17.15 ? 32  ALA B CA  1 
ATOM   1120 C  C   . ALA B 1 32  ? -11.754 51.402 71.843 1.00 15.58 ? 32  ALA B C   1 
ATOM   1121 O  O   . ALA B 1 32  ? -12.487 52.380 72.154 1.00 17.31 ? 32  ALA B O   1 
ATOM   1122 C  CB  . ALA B 1 32  ? -9.781  52.332 70.641 1.00 16.66 ? 32  ALA B CB  1 
ATOM   1123 N  N   . LEU B 1 33  ? -12.234 50.240 71.458 1.00 14.55 ? 33  LEU B N   1 
ATOM   1124 C  CA  . LEU B 1 33  ? -13.636 49.910 71.391 1.00 15.35 ? 33  LEU B CA  1 
ATOM   1125 C  C   . LEU B 1 33  ? -14.223 49.478 72.701 1.00 14.89 ? 33  LEU B C   1 
ATOM   1126 O  O   . LEU B 1 33  ? -15.420 49.232 72.823 1.00 19.83 ? 33  LEU B O   1 
ATOM   1127 C  CB  . LEU B 1 33  ? -13.966 48.909 70.277 1.00 16.17 ? 33  LEU B CB  1 
ATOM   1128 C  CG  . LEU B 1 33  ? -13.662 49.353 68.860 1.00 17.79 ? 33  LEU B CG  1 
ATOM   1129 C  CD1 . LEU B 1 33  ? -13.847 48.199 67.873 1.00 18.55 ? 33  LEU B CD1 1 
ATOM   1130 C  CD2 . LEU B 1 33  ? -14.561 50.527 68.461 1.00 19.09 ? 33  LEU B CD2 1 
ATOM   1131 N  N   . GLY B 1 34  ? -13.360 49.147 73.674 1.00 13.96 ? 34  GLY B N   1 
ATOM   1132 C  CA  . GLY B 1 34  ? -13.819 48.648 74.925 1.00 13.65 ? 34  GLY B CA  1 
ATOM   1133 C  C   . GLY B 1 34  ? -13.505 47.193 75.175 1.00 11.49 ? 34  GLY B C   1 
ATOM   1134 O  O   . GLY B 1 34  ? -14.035 46.620 76.131 1.00 13.15 ? 34  GLY B O   1 
ATOM   1135 N  N   . TRP B 1 35  ? -12.679 46.557 74.357 1.00 11.68 ? 35  TRP B N   1 
ATOM   1136 C  CA  . TRP B 1 35  ? -12.256 45.173 74.635 1.00 11.01 ? 35  TRP B CA  1 
ATOM   1137 C  C   . TRP B 1 35  ? -11.392 45.159 75.921 1.00 11.03 ? 35  TRP B C   1 
ATOM   1138 O  O   . TRP B 1 35  ? -10.448 45.942 76.037 1.00 13.00 ? 35  TRP B O   1 
ATOM   1139 C  CB  . TRP B 1 35  ? -11.342 44.708 73.489 1.00 11.33 ? 35  TRP B CB  1 
ATOM   1140 C  CG  . TRP B 1 35  ? -10.756 43.332 73.697 1.00 10.58 ? 35  TRP B CG  1 
ATOM   1141 C  CD1 . TRP B 1 35  ? -11.407 42.196 74.049 1.00 12.08 ? 35  TRP B CD1 1 
ATOM   1142 C  CD2 . TRP B 1 35  ? -9.372  42.978 73.579 1.00 10.94 ? 35  TRP B CD2 1 
ATOM   1143 N  NE1 . TRP B 1 35  ? -10.535 41.137 74.155 1.00 12.32 ? 35  TRP B NE1 1 
ATOM   1144 C  CE2 . TRP B 1 35  ? -9.275  41.590 73.838 1.00 10.48 ? 35  TRP B CE2 1 
ATOM   1145 C  CE3 . TRP B 1 35  ? -8.213  43.678 73.240 1.00 13.02 ? 35  TRP B CE3 1 
ATOM   1146 C  CZ2 . TRP B 1 35  ? -8.063  40.910 73.787 1.00 12.26 ? 35  TRP B CZ2 1 
ATOM   1147 C  CZ3 . TRP B 1 35  ? -7.007  42.978 73.173 1.00 13.66 ? 35  TRP B CZ3 1 
ATOM   1148 C  CH2 . TRP B 1 35  ? -6.957  41.619 73.441 1.00 13.07 ? 35  TRP B CH2 1 
ATOM   1149 N  N   . VAL B 1 36  ? -11.722 44.268 76.806 1.00 10.19 ? 36  VAL B N   1 
ATOM   1150 C  CA  . VAL B 1 36  ? -10.987 43.983 78.034 1.00 11.15 ? 36  VAL B CA  1 
ATOM   1151 C  C   . VAL B 1 36  ? -10.527 42.509 77.997 1.00 10.82 ? 36  VAL B C   1 
ATOM   1152 O  O   . VAL B 1 36  ? -11.325 41.598 78.097 1.00 10.72 ? 36  VAL B O   1 
ATOM   1153 C  CB  . VAL B 1 36  ? -11.837 44.235 79.284 1.00 11.19 ? 36  VAL B CB  1 
ATOM   1154 C  CG1 . VAL B 1 36  ? -11.024 43.978 80.549 1.00 13.16 ? 36  VAL B CG1 1 
ATOM   1155 C  CG2 . VAL B 1 36  ? -12.479 45.579 79.268 1.00 13.74 ? 36  VAL B CG2 1 
ATOM   1156 N  N   . ALA B 1 37  ? -9.216  42.354 77.752 1.00 11.33 ? 37  ALA B N   1 
ATOM   1157 C  CA  . ALA B 1 37  ? -8.673  41.014 77.552 1.00 10.23 ? 37  ALA B CA  1 
ATOM   1158 C  C   . ALA B 1 37  ? -9.083  40.081 78.666 1.00 9.59  ? 37  ALA B C   1 
ATOM   1159 O  O   . ALA B 1 37  ? -9.408  38.907 78.455 1.00 11.78 ? 37  ALA B O   1 
ATOM   1160 C  CB  . ALA B 1 37  ? -7.189  41.043 77.319 1.00 11.92 ? 37  ALA B CB  1 
ATOM   1161 N  N   . SER B 1 38  ? -9.001  40.568 79.904 1.00 10.41 ? 38  SER B N   1 
ATOM   1162 C  CA  . SER B 1 38  ? -9.278  39.770 81.076 1.00 11.18 ? 38  SER B CA  1 
ATOM   1163 C  C   . SER B 1 38  ? -10.725 39.355 81.231 1.00 12.08 ? 38  SER B C   1 
ATOM   1164 O  O   . SER B 1 38  ? -11.009 38.459 82.039 1.00 13.69 ? 38  SER B O   1 
ATOM   1165 C  CB  A SER B 1 38  ? -8.761  40.456 82.344 0.50 11.57 ? 38  SER B CB  1 
ATOM   1166 C  CB  B SER B 1 38  ? -8.783  40.463 82.351 0.50 11.42 ? 38  SER B CB  1 
ATOM   1167 O  OG  A SER B 1 38  ? -7.352  40.674 82.319 0.50 11.96 ? 38  SER B OG  1 
ATOM   1168 O  OG  B SER B 1 38  ? -9.563  41.614 82.590 0.50 15.37 ? 38  SER B OG  1 
ATOM   1169 N  N   . LYS B 1 39  ? -11.671 39.938 80.475 1.00 12.21 ? 39  LYS B N   1 
ATOM   1170 C  CA  . LYS B 1 39  ? -13.052 39.523 80.489 1.00 13.31 ? 39  LYS B CA  1 
ATOM   1171 C  C   . LYS B 1 39  ? -13.416 38.610 79.336 1.00 13.64 ? 39  LYS B C   1 
ATOM   1172 O  O   . LYS B 1 39  ? -14.524 38.054 79.259 1.00 15.72 ? 39  LYS B O   1 
ATOM   1173 C  CB  . LYS B 1 39  ? -14.006 40.763 80.412 1.00 15.40 ? 39  LYS B CB  1 
ATOM   1174 C  CG  . LYS B 1 39  ? -14.073 41.583 81.654 1.00 23.83 ? 39  LYS B CG  1 
ATOM   1175 C  CD  . LYS B 1 39  ? -14.752 42.949 81.441 1.00 25.26 ? 39  LYS B CD  1 
ATOM   1176 C  CE  . LYS B 1 39  ? -16.222 42.838 81.775 1.00 29.36 ? 39  LYS B CE  1 
ATOM   1177 N  NZ  . LYS B 1 39  ? -16.986 44.073 81.627 1.00 33.82 ? 39  LYS B NZ  1 
ATOM   1178 N  N   . GLY B 1 40  ? -12.547 38.546 78.310 1.00 11.24 ? 40  GLY B N   1 
ATOM   1179 C  CA  . GLY B 1 40  ? -12.884 37.675 77.179 1.00 12.24 ? 40  GLY B CA  1 
ATOM   1180 C  C   . GLY B 1 40  ? -14.068 38.176 76.384 1.00 12.12 ? 40  GLY B C   1 
ATOM   1181 O  O   . GLY B 1 40  ? -14.857 37.348 75.903 1.00 13.42 ? 40  GLY B O   1 
ATOM   1182 N  N   . ASN B 1 41  ? -14.207 39.487 76.223 1.00 11.30 ? 41  ASN B N   1 
ATOM   1183 C  CA  . ASN B 1 41  ? -15.390 40.117 75.704 1.00 11.24 ? 41  ASN B CA  1 
ATOM   1184 C  C   . ASN B 1 41  ? -15.300 40.656 74.309 1.00 10.98 ? 41  ASN B C   1 
ATOM   1185 O  O   . ASN B 1 41  ? -16.190 41.440 73.880 1.00 11.02 ? 41  ASN B O   1 
ATOM   1186 C  CB  . ASN B 1 41  ? -15.896 41.223 76.665 1.00 11.85 ? 41  ASN B CB  1 
ATOM   1187 C  CG  . ASN B 1 41  ? -15.022 42.452 76.623 1.00 12.33 ? 41  ASN B CG  1 
ATOM   1188 O  OD1 . ASN B 1 41  ? -13.916 42.416 76.096 1.00 13.80 ? 41  ASN B OD1 1 
ATOM   1189 N  ND2 . ASN B 1 41  ? -15.466 43.592 77.177 1.00 15.44 ? 41  ASN B ND2 1 
ATOM   1190 N  N   . LEU B 1 42  ? -14.314 40.218 73.519 1.00 11.00 ? 42  LEU B N   1 
ATOM   1191 C  CA  . LEU B 1 42  ? -14.191 40.772 72.170 1.00 11.64 ? 42  LEU B CA  1 
ATOM   1192 C  C   . LEU B 1 42  ? -15.464 40.679 71.370 1.00 12.22 ? 42  LEU B C   1 
ATOM   1193 O  O   . LEU B 1 42  ? -15.888 41.657 70.725 1.00 12.33 ? 42  LEU B O   1 
ATOM   1194 C  CB  . LEU B 1 42  ? -13.001 40.220 71.400 1.00 11.68 ? 42  LEU B CB  1 
ATOM   1195 C  CG  . LEU B 1 42  ? -12.666 40.811 70.040 1.00 11.91 ? 42  LEU B CG  1 
ATOM   1196 C  CD1 . LEU B 1 42  ? -12.271 42.278 70.116 1.00 17.11 ? 42  LEU B CD1 1 
ATOM   1197 C  CD2 . LEU B 1 42  ? -11.535 40.013 69.376 1.00 12.42 ? 42  LEU B CD2 1 
ATOM   1198 N  N   . ALA B 1 43  ? -16.096 39.493 71.337 1.00 13.34 ? 43  ALA B N   1 
ATOM   1199 C  CA  . ALA B 1 43  ? -17.269 39.312 70.493 1.00 14.98 ? 43  ALA B CA  1 
ATOM   1200 C  C   . ALA B 1 43  ? -18.475 40.111 70.950 1.00 15.34 ? 43  ALA B C   1 
ATOM   1201 O  O   . ALA B 1 43  ? -19.415 40.352 70.188 1.00 15.94 ? 43  ALA B O   1 
ATOM   1202 C  CB  . ALA B 1 43  ? -17.628 37.816 70.422 1.00 17.70 ? 43  ALA B CB  1 
ATOM   1203 N  N   . ASP B 1 44  ? -18.517 40.534 72.210 1.00 13.88 ? 44  ASP B N   1 
ATOM   1204 C  CA  . ASP B 1 44  ? -19.613 41.379 72.680 1.00 13.88 ? 44  ASP B CA  1 
ATOM   1205 C  C   . ASP B 1 44  ? -19.420 42.834 72.246 1.00 14.32 ? 44  ASP B C   1 
ATOM   1206 O  O   . ASP B 1 44  ? -20.389 43.538 71.926 1.00 15.84 ? 44  ASP B O   1 
ATOM   1207 C  CB  . ASP B 1 44  ? -19.613 41.334 74.213 1.00 16.67 ? 44  ASP B CB  1 
ATOM   1208 C  CG  . ASP B 1 44  ? -20.052 40.001 74.775 1.00 25.69 ? 44  ASP B CG  1 
ATOM   1209 O  OD1 . ASP B 1 44  ? -20.861 39.292 74.157 1.00 29.14 ? 44  ASP B OD1 1 
ATOM   1210 O  OD2 . ASP B 1 44  ? -19.693 39.773 75.946 1.00 38.96 ? 44  ASP B OD2 1 
ATOM   1211 N  N   . VAL B 1 45  ? -18.166 43.286 72.275 1.00 12.02 ? 45  VAL B N   1 
ATOM   1212 C  CA  . VAL B 1 45  ? -17.867 44.669 71.947 1.00 13.14 ? 45  VAL B CA  1 
ATOM   1213 C  C   . VAL B 1 45  ? -17.793 44.915 70.452 1.00 12.87 ? 45  VAL B C   1 
ATOM   1214 O  O   . VAL B 1 45  ? -18.260 45.950 69.971 1.00 12.96 ? 45  VAL B O   1 
ATOM   1215 C  CB  . VAL B 1 45  ? -16.627 45.191 72.662 1.00 16.56 ? 45  VAL B CB  1 
ATOM   1216 C  CG1 . VAL B 1 45  ? -16.763 45.098 74.169 1.00 18.93 ? 45  VAL B CG1 1 
ATOM   1217 C  CG2 . VAL B 1 45  ? -15.335 44.673 72.134 1.00 18.98 ? 45  VAL B CG2 1 
ATOM   1218 N  N   . ALA B 1 46  ? -17.269 43.944 69.707 1.00 13.88 ? 46  ALA B N   1 
ATOM   1219 C  CA  . ALA B 1 46  ? -17.096 44.079 68.256 1.00 13.19 ? 46  ALA B CA  1 
ATOM   1220 C  C   . ALA B 1 46  ? -17.493 42.774 67.563 1.00 12.11 ? 46  ALA B C   1 
ATOM   1221 O  O   . ALA B 1 46  ? -16.641 41.972 67.166 1.00 12.06 ? 46  ALA B O   1 
ATOM   1222 C  CB  . ALA B 1 46  ? -15.638 44.432 67.941 1.00 16.34 ? 46  ALA B CB  1 
ATOM   1223 N  N   . PRO B 1 47  ? -18.792 42.506 67.519 1.00 13.09 ? 47  PRO B N   1 
ATOM   1224 C  CA  . PRO B 1 47  ? -19.258 41.228 66.927 1.00 15.23 ? 47  PRO B CA  1 
ATOM   1225 C  C   . PRO B 1 47  ? -18.639 41.014 65.557 1.00 15.14 ? 47  PRO B C   1 
ATOM   1226 O  O   . PRO B 1 47  ? -18.550 41.938 64.731 1.00 16.80 ? 47  PRO B O   1 
ATOM   1227 C  CB  . PRO B 1 47  ? -20.767 41.385 66.853 1.00 16.62 ? 47  PRO B CB  1 
ATOM   1228 C  CG  . PRO B 1 47  ? -21.115 42.555 67.677 1.00 15.71 ? 47  PRO B CG  1 
ATOM   1229 C  CD  . PRO B 1 47  ? -19.910 43.331 67.990 1.00 13.47 ? 47  PRO B CD  1 
ATOM   1230 N  N   . GLY B 1 48  ? -18.194 39.793 65.329 1.00 15.23 ? 48  GLY B N   1 
ATOM   1231 C  CA  . GLY B 1 48  ? -17.619 39.316 64.125 1.00 15.75 ? 48  GLY B CA  1 
ATOM   1232 C  C   . GLY B 1 48  ? -16.173 39.600 63.881 1.00 15.48 ? 48  GLY B C   1 
ATOM   1233 O  O   . GLY B 1 48  ? -15.625 39.286 62.822 1.00 15.78 ? 48  GLY B O   1 
ATOM   1234 N  N   . LYS B 1 49  ? -15.520 40.344 64.787 1.00 13.19 ? 49  LYS B N   1 
ATOM   1235 C  CA  . LYS B 1 49  ? -14.134 40.716 64.606 1.00 12.40 ? 49  LYS B CA  1 
ATOM   1236 C  C   . LYS B 1 49  ? -13.177 39.730 65.284 1.00 12.15 ? 49  LYS B C   1 
ATOM   1237 O  O   . LYS B 1 49  ? -13.557 39.114 66.286 1.00 13.13 ? 49  LYS B O   1 
ATOM   1238 C  CB  . LYS B 1 49  ? -13.900 42.126 65.172 1.00 14.59 ? 49  LYS B CB  1 
ATOM   1239 C  CG  . LYS B 1 49  ? -14.625 43.227 64.400 1.00 16.64 ? 49  LYS B CG  1 
ATOM   1240 C  CD  . LYS B 1 49  ? -14.333 43.224 62.941 1.00 25.07 ? 49  LYS B CD  1 
ATOM   1241 C  CE  . LYS B 1 49  ? -14.835 44.460 62.215 1.00 24.58 ? 49  LYS B CE  1 
ATOM   1242 N  NZ  . LYS B 1 49  ? -16.229 44.765 62.563 1.00 30.77 ? 49  LYS B NZ  1 
ATOM   1243 N  N   . SER B 1 50  ? -11.958 39.620 64.790 1.00 11.22 ? 50  SER B N   1 
ATOM   1244 C  CA  . SER B 1 50  ? -10.884 38.901 65.419 1.00 11.25 ? 50  SER B CA  1 
ATOM   1245 C  C   . SER B 1 50  ? -9.653  39.850 65.563 1.00 12.05 ? 50  SER B C   1 
ATOM   1246 O  O   . SER B 1 50  ? -9.517  40.772 64.757 1.00 12.70 ? 50  SER B O   1 
ATOM   1247 C  CB  . SER B 1 50  ? -10.425 37.711 64.531 1.00 12.39 ? 50  SER B CB  1 
ATOM   1248 O  OG  . SER B 1 50  ? -11.442 36.700 64.477 1.00 13.02 ? 50  SER B OG  1 
ATOM   1249 N  N   . ILE B 1 51  ? -8.753  39.554 66.479 1.00 11.41 ? 51  ILE B N   1 
ATOM   1250 C  CA  . ILE B 1 51  ? -7.518  40.334 66.610 1.00 11.26 ? 51  ILE B CA  1 
ATOM   1251 C  C   . ILE B 1 51  ? -6.500  39.875 65.557 1.00 10.35 ? 51  ILE B C   1 
ATOM   1252 O  O   . ILE B 1 51  ? -6.267  38.651 65.412 1.00 11.16 ? 51  ILE B O   1 
ATOM   1253 C  CB  . ILE B 1 51  ? -6.872  40.099 68.001 1.00 13.85 ? 51  ILE B CB  1 
ATOM   1254 C  CG1 . ILE B 1 51  ? -7.776  40.450 69.163 1.00 13.90 ? 51  ILE B CG1 1 
ATOM   1255 C  CG2 . ILE B 1 51  ? -5.537  40.786 68.102 1.00 12.50 ? 51  ILE B CG2 1 
ATOM   1256 C  CD1 . ILE B 1 51  ? -8.097  41.879 69.282 1.00 16.39 ? 51  ILE B CD1 1 
ATOM   1257 N  N   . GLY B 1 52  ? -5.880  40.826 64.879 1.00 12.15 ? 52  GLY B N   1 
ATOM   1258 C  CA  . GLY B 1 52  ? -4.772  40.513 63.976 1.00 12.14 ? 52  GLY B CA  1 
ATOM   1259 C  C   . GLY B 1 52  ? -4.152  41.747 63.355 1.00 12.00 ? 52  GLY B C   1 
ATOM   1260 O  O   . GLY B 1 52  ? -4.760  42.846 63.312 1.00 14.41 ? 52  GLY B O   1 
ATOM   1261 N  N   . GLY B 1 53  ? -2.920  41.608 62.880 1.00 13.03 ? 53  GLY B N   1 
ATOM   1262 C  CA  . GLY B 1 53  ? -2.184  42.632 62.211 1.00 13.20 ? 53  GLY B CA  1 
ATOM   1263 C  C   . GLY B 1 53  ? -1.071  43.284 62.984 1.00 15.38 ? 53  GLY B C   1 
ATOM   1264 O  O   . GLY B 1 53  ? -0.304  44.120 62.450 1.00 17.73 ? 53  GLY B O   1 
ATOM   1265 N  N   . ASP B 1 54  ? -0.883  42.922 64.260 1.00 14.33 ? 54  ASP B N   1 
ATOM   1266 C  CA  . ASP B 1 54  ? 0.197   43.505 65.045 1.00 15.66 ? 54  ASP B CA  1 
ATOM   1267 C  C   . ASP B 1 54  ? 1.538   42.887 64.654 1.00 16.08 ? 54  ASP B C   1 
ATOM   1268 O  O   . ASP B 1 54  ? 1.654   41.732 64.249 1.00 15.64 ? 54  ASP B O   1 
ATOM   1269 C  CB  . ASP B 1 54  ? -0.070  43.344 66.531 1.00 16.16 ? 54  ASP B CB  1 
ATOM   1270 C  CG  . ASP B 1 54  ? -1.244  44.146 67.029 1.00 16.24 ? 54  ASP B CG  1 
ATOM   1271 O  OD1 . ASP B 1 54  ? -1.144  45.394 67.028 1.00 25.06 ? 54  ASP B OD1 1 
ATOM   1272 O  OD2 . ASP B 1 54  ? -2.299  43.527 67.341 1.00 18.11 ? 54  ASP B OD2 1 
ATOM   1273 N  N   . ILE B 1 55  ? 2.608   43.649 64.854 1.00 19.30 ? 55  ILE B N   1 
ATOM   1274 C  CA  . ILE B 1 55  ? 3.963   43.154 64.686 1.00 19.79 ? 55  ILE B CA  1 
ATOM   1275 C  C   . ILE B 1 55  ? 4.303   42.087 65.714 1.00 19.96 ? 55  ILE B C   1 
ATOM   1276 O  O   . ILE B 1 55  ? 3.940   42.177 66.888 1.00 21.19 ? 55  ILE B O   1 
ATOM   1277 C  CB  . ILE B 1 55  ? 4.987   44.330 64.785 1.00 21.63 ? 55  ILE B CB  1 
ATOM   1278 C  CG1 . ILE B 1 55  ? 4.915   45.179 63.498 1.00 24.60 ? 55  ILE B CG1 1 
ATOM   1279 C  CG2 . ILE B 1 55  ? 6.396   43.742 64.923 1.00 24.67 ? 55  ILE B CG2 1 
ATOM   1280 C  CD1 . ILE B 1 55  ? 5.630   46.485 63.537 1.00 30.76 ? 55  ILE B CD1 1 
ATOM   1281 N  N   . PHE B 1 56  ? 4.948   41.027 65.274 1.00 20.75 ? 56  PHE B N   1 
ATOM   1282 C  CA  . PHE B 1 56  ? 5.448   39.977 66.144 1.00 21.39 ? 56  PHE B CA  1 
ATOM   1283 C  C   . PHE B 1 56  ? 6.992   40.029 66.151 1.00 21.12 ? 56  PHE B C   1 
ATOM   1284 O  O   . PHE B 1 56  ? 7.626   39.909 65.108 1.00 21.97 ? 56  PHE B O   1 
ATOM   1285 C  CB  . PHE B 1 56  ? 4.985   38.610 65.630 1.00 23.00 ? 56  PHE B CB  1 
ATOM   1286 C  CG  . PHE B 1 56  ? 5.440   37.453 66.504 1.00 22.24 ? 56  PHE B CG  1 
ATOM   1287 C  CD1 . PHE B 1 56  ? 4.780   37.166 67.684 1.00 23.09 ? 56  PHE B CD1 1 
ATOM   1288 C  CD2 . PHE B 1 56  ? 6.522   36.672 66.129 1.00 23.07 ? 56  PHE B CD2 1 
ATOM   1289 C  CE1 . PHE B 1 56  ? 5.154   36.079 68.456 1.00 23.41 ? 56  PHE B CE1 1 
ATOM   1290 C  CE2 . PHE B 1 56  ? 6.887   35.577 66.885 1.00 23.37 ? 56  PHE B CE2 1 
ATOM   1291 C  CZ  . PHE B 1 56  ? 6.192   35.268 68.046 1.00 24.00 ? 56  PHE B CZ  1 
ATOM   1292 N  N   . SER B 1 57  ? 7.553   40.306 67.314 1.00 25.76 ? 57  SER B N   1 
ATOM   1293 C  CA  . SER B 1 57  ? 8.942   40.589 67.494 1.00 26.35 ? 57  SER B CA  1 
ATOM   1294 C  C   . SER B 1 57  ? 9.925   39.570 67.049 1.00 26.96 ? 57  SER B C   1 
ATOM   1295 O  O   . SER B 1 57  ? 11.058  39.922 66.605 1.00 31.88 ? 57  SER B O   1 
ATOM   1296 C  CB  . SER B 1 57  ? 9.258   41.205 68.839 1.00 27.91 ? 57  SER B CB  1 
ATOM   1297 O  OG  . SER B 1 57  ? 9.639   40.231 69.791 1.00 36.83 ? 57  SER B OG  1 
ATOM   1298 N  N   . ASN B 1 58  ? 9.654   38.282 67.199 1.00 28.85 ? 58  ASN B N   1 
ATOM   1299 C  CA  . ASN B 1 58  ? 10.552  37.220 66.861 1.00 29.34 ? 58  ASN B CA  1 
ATOM   1300 C  C   . ASN B 1 58  ? 11.805  37.139 67.680 1.00 29.73 ? 58  ASN B C   1 
ATOM   1301 O  O   . ASN B 1 58  ? 12.834  36.598 67.291 1.00 31.22 ? 58  ASN B O   1 
ATOM   1302 C  CB  . ASN B 1 58  ? 10.748  37.000 65.386 1.00 28.88 ? 58  ASN B CB  1 
ATOM   1303 C  CG  . ASN B 1 58  ? 11.341  35.653 65.034 1.00 28.00 ? 58  ASN B CG  1 
ATOM   1304 O  OD1 . ASN B 1 58  ? 10.975  34.631 65.621 1.00 27.69 ? 58  ASN B OD1 1 
ATOM   1305 N  ND2 . ASN B 1 58  ? 12.252  35.646 64.073 1.00 28.28 ? 58  ASN B ND2 1 
ATOM   1306 N  N   . ARG B 1 59  ? 11.736  37.619 68.946 1.00 32.58 ? 59  ARG B N   1 
ATOM   1307 C  CA  . ARG B 1 59  ? 12.858  37.550 69.851 0.50 32.41 ? 59  ARG B CA  1 
ATOM   1308 C  C   . ARG B 1 59  ? 13.355  36.148 70.134 1.00 33.66 ? 59  ARG B C   1 
ATOM   1309 O  O   . ARG B 1 59  ? 14.561  35.922 70.290 1.00 34.10 ? 59  ARG B O   1 
ATOM   1310 C  CB  . ARG B 1 59  ? 12.577  38.300 71.162 0.50 31.73 ? 59  ARG B CB  1 
ATOM   1311 C  CG  . ARG B 1 59  ? 13.396  39.568 71.330 0.00 31.78 ? 59  ARG B CG  1 
ATOM   1312 C  CD  . ARG B 1 59  ? 12.619  40.793 70.873 0.00 31.79 ? 59  ARG B CD  1 
ATOM   1313 N  NE  . ARG B 1 59  ? 11.575  41.164 71.824 0.00 31.80 ? 59  ARG B NE  1 
ATOM   1314 C  CZ  . ARG B 1 59  ? 10.870  42.286 71.763 0.00 31.81 ? 59  ARG B CZ  1 
ATOM   1315 N  NH1 . ARG B 1 59  ? 11.279  43.290 70.998 0.00 31.79 ? 59  ARG B NH1 1 
ATOM   1316 N  NH2 . ARG B 1 59  ? 9.753   42.411 72.467 0.00 31.82 ? 59  ARG B NH2 1 
ATOM   1317 N  N   . GLU B 1 60  ? 12.456  35.176 70.268 1.00 33.82 ? 60  GLU B N   1 
ATOM   1318 C  CA  . GLU B 1 60  ? 12.870  33.804 70.576 1.00 33.27 ? 60  GLU B CA  1 
ATOM   1319 C  C   . GLU B 1 60  ? 13.613  33.166 69.406 1.00 33.51 ? 60  GLU B C   1 
ATOM   1320 O  O   . GLU B 1 60  ? 14.238  32.106 69.568 1.00 34.72 ? 60  GLU B O   1 
ATOM   1321 C  CB  . GLU B 1 60  ? 11.691  33.001 71.114 0.50 34.67 ? 60  GLU B CB  1 
ATOM   1322 C  CG  . GLU B 1 60  ? 11.578  32.960 72.656 0.50 35.48 ? 60  GLU B CG  1 
ATOM   1323 C  CD  . GLU B 1 60  ? 10.649  31.849 73.045 0.50 38.57 ? 60  GLU B CD  1 
ATOM   1324 O  OE1 . GLU B 1 60  ? 9.440   31.844 72.590 0.50 44.09 ? 60  GLU B OE1 1 
ATOM   1325 O  OE2 . GLU B 1 60  ? 11.069  30.914 73.806 0.50 37.22 ? 60  GLU B OE2 1 
ATOM   1326 N  N   . GLY B 1 61  ? 13.532  33.778 68.238 1.00 34.02 ? 61  GLY B N   1 
ATOM   1327 C  CA  . GLY B 1 61  ? 14.215  33.338 67.043 1.00 34.03 ? 61  GLY B CA  1 
ATOM   1328 C  C   . GLY B 1 61  ? 13.660  32.084 66.425 1.00 33.71 ? 61  GLY B C   1 
ATOM   1329 O  O   . GLY B 1 61  ? 14.349  31.421 65.622 1.00 32.97 ? 61  GLY B O   1 
ATOM   1330 N  N   . LYS B 1 62  ? 12.433  31.721 66.754 1.00 28.17 ? 62  LYS B N   1 
ATOM   1331 C  CA  . LYS B 1 62  ? 11.788  30.530 66.263 1.00 27.24 ? 62  LYS B CA  1 
ATOM   1332 C  C   . LYS B 1 62  ? 11.363  30.582 64.800 1.00 27.28 ? 62  LYS B C   1 
ATOM   1333 O  O   . LYS B 1 62  ? 11.112  29.526 64.200 1.00 29.68 ? 62  LYS B O   1 
ATOM   1334 C  CB  . LYS B 1 62  ? 10.617  30.141 67.150 1.00 31.97 ? 62  LYS B CB  1 
ATOM   1335 C  CG  . LYS B 1 62  ? 11.024  29.775 68.590 1.00 36.84 ? 62  LYS B CG  1 
ATOM   1336 C  CD  . LYS B 1 62  ? 9.900   28.921 69.195 1.00 42.98 ? 62  LYS B CD  1 
ATOM   1337 C  CE  . LYS B 1 62  ? 9.801   29.076 70.685 1.00 45.42 ? 62  LYS B CE  1 
ATOM   1338 N  NZ  . LYS B 1 62  ? 9.834   27.750 71.396 1.00 50.23 ? 62  LYS B NZ  1 
ATOM   1339 N  N   . LEU B 1 63  ? 11.208  31.766 64.248 1.00 24.10 ? 63  LEU B N   1 
ATOM   1340 C  CA  . LEU B 1 63  ? 10.862  31.957 62.838 1.00 23.92 ? 63  LEU B CA  1 
ATOM   1341 C  C   . LEU B 1 63  ? 12.098  32.434 62.085 1.00 23.94 ? 63  LEU B C   1 
ATOM   1342 O  O   . LEU B 1 63  ? 12.987  33.039 62.695 1.00 27.39 ? 63  LEU B O   1 
ATOM   1343 C  CB  . LEU B 1 63  ? 9.736   32.989 62.712 1.00 23.34 ? 63  LEU B CB  1 
ATOM   1344 C  CG  . LEU B 1 63  ? 8.415   32.619 63.371 1.00 21.85 ? 63  LEU B CG  1 
ATOM   1345 C  CD1 . LEU B 1 63  ? 7.461   33.798 63.413 1.00 24.98 ? 63  LEU B CD1 1 
ATOM   1346 C  CD2 . LEU B 1 63  ? 7.782   31.415 62.692 1.00 25.38 ? 63  LEU B CD2 1 
ATOM   1347 N  N   . PRO B 1 64  ? 12.233  32.080 60.812 1.00 25.24 ? 64  PRO B N   1 
ATOM   1348 C  CA  . PRO B 1 64  ? 13.437  32.439 60.073 1.00 24.87 ? 64  PRO B CA  1 
ATOM   1349 C  C   . PRO B 1 64  ? 13.578  33.938 59.844 1.00 27.85 ? 64  PRO B C   1 
ATOM   1350 O  O   . PRO B 1 64  ? 12.658  34.619 59.427 1.00 27.67 ? 64  PRO B O   1 
ATOM   1351 C  CB  . PRO B 1 64  ? 13.270  31.715 58.737 1.00 26.29 ? 64  PRO B CB  1 
ATOM   1352 C  CG  . PRO B 1 64  ? 11.780  31.540 58.610 1.00 26.34 ? 64  PRO B CG  1 
ATOM   1353 C  CD  . PRO B 1 64  ? 11.302  31.272 60.014 1.00 24.55 ? 64  PRO B CD  1 
ATOM   1354 N  N   . GLY B 1 65  ? 14.798  34.442 60.069 1.00 34.20 ? 65  GLY B N   1 
ATOM   1355 C  CA  . GLY B 1 65  ? 15.052  35.857 59.819 1.00 35.80 ? 65  GLY B CA  1 
ATOM   1356 C  C   . GLY B 1 65  ? 15.728  36.048 58.454 1.00 38.16 ? 65  GLY B C   1 
ATOM   1357 O  O   . GLY B 1 65  ? 16.221  35.086 57.870 1.00 38.95 ? 65  GLY B O   1 
ATOM   1358 N  N   . LYS B 1 66  ? 15.702  37.264 57.981 1.00 37.44 ? 66  LYS B N   1 
ATOM   1359 C  CA  . LYS B 1 66  ? 16.273  37.699 56.724 1.00 36.36 ? 66  LYS B CA  1 
ATOM   1360 C  C   . LYS B 1 66  ? 16.284  39.245 56.731 1.00 38.10 ? 66  LYS B C   1 
ATOM   1361 O  O   . LYS B 1 66  ? 15.367  39.834 57.318 1.00 39.67 ? 66  LYS B O   1 
ATOM   1362 C  CB  . LYS B 1 66  ? 15.401  37.229 55.539 1.00 39.84 ? 66  LYS B CB  1 
ATOM   1363 C  CG  . LYS B 1 66  ? 15.864  37.818 54.203 1.00 44.08 ? 66  LYS B CG  1 
ATOM   1364 C  CD  . LYS B 1 66  ? 15.108  37.197 53.046 1.00 45.33 ? 66  LYS B CD  1 
ATOM   1365 C  CE  . LYS B 1 66  ? 15.988  36.976 51.833 0.50 44.86 ? 66  LYS B CE  1 
ATOM   1366 N  NZ  . LYS B 1 66  ? 15.265  37.224 50.555 0.50 43.72 ? 66  LYS B NZ  1 
ATOM   1367 N  N   . SER B 1 67  ? 17.309  39.811 56.140 0.50 39.30 ? 67  SER B N   1 
ATOM   1368 C  CA  . SER B 1 67  ? 17.447  41.268 56.088 0.50 39.90 ? 67  SER B CA  1 
ATOM   1369 C  C   . SER B 1 67  ? 16.209  41.892 55.463 1.00 38.19 ? 67  SER B C   1 
ATOM   1370 O  O   . SER B 1 67  ? 15.755  41.470 54.390 1.00 42.65 ? 67  SER B O   1 
ATOM   1371 C  CB  . SER B 1 67  ? 18.694  41.651 55.287 0.00 39.99 ? 67  SER B CB  1 
ATOM   1372 O  OG  . SER B 1 67  ? 19.875  41.297 55.986 0.00 40.02 ? 67  SER B OG  1 
ATOM   1373 N  N   . GLY B 1 68  ? 15.600  42.819 56.177 1.00 38.74 ? 68  GLY B N   1 
ATOM   1374 C  CA  . GLY B 1 68  ? 14.425  43.513 55.734 1.00 37.74 ? 68  GLY B CA  1 
ATOM   1375 C  C   . GLY B 1 68  ? 13.115  42.839 56.019 1.00 34.25 ? 68  GLY B C   1 
ATOM   1376 O  O   . GLY B 1 68  ? 12.063  43.386 55.650 1.00 36.97 ? 68  GLY B O   1 
ATOM   1377 N  N   . ARG B 1 69  ? 13.124  41.648 56.613 1.00 31.18 ? 69  ARG B N   1 
ATOM   1378 C  CA  . ARG B 1 69  ? 11.897  40.912 56.879 1.00 27.84 ? 69  ARG B CA  1 
ATOM   1379 C  C   . ARG B 1 69  ? 11.303  41.246 58.246 1.00 28.43 ? 69  ARG B C   1 
ATOM   1380 O  O   . ARG B 1 69  ? 11.984  41.123 59.271 1.00 28.75 ? 69  ARG B O   1 
ATOM   1381 C  CB  . ARG B 1 69  ? 12.215  39.385 56.873 1.00 27.61 ? 69  ARG B CB  1 
ATOM   1382 C  CG  . ARG B 1 69  ? 10.967  38.545 57.172 1.00 27.36 ? 69  ARG B CG  1 
ATOM   1383 C  CD  . ARG B 1 69  ? 11.337  37.054 57.202 1.00 28.24 ? 69  ARG B CD  1 
ATOM   1384 N  NE  . ARG B 1 69  ? 11.509  36.513 55.855 1.00 29.25 ? 69  ARG B NE  1 
ATOM   1385 C  CZ  . ARG B 1 69  ? 12.228  35.464 55.513 1.00 28.90 ? 69  ARG B CZ  1 
ATOM   1386 N  NH1 . ARG B 1 69  ? 12.810  34.712 56.439 1.00 29.52 ? 69  ARG B NH1 1 
ATOM   1387 N  NH2 . ARG B 1 69  ? 12.331  35.114 54.228 1.00 30.45 ? 69  ARG B NH2 1 
ATOM   1388 N  N   . THR B 1 70  ? 10.015  41.558 58.251 1.00 27.13 ? 70  THR B N   1 
ATOM   1389 C  CA  . THR B 1 70  ? 9.275   41.727 59.502 1.00 26.91 ? 70  THR B CA  1 
ATOM   1390 C  C   . THR B 1 70  ? 8.189   40.667 59.593 1.00 22.42 ? 70  THR B C   1 
ATOM   1391 O  O   . THR B 1 70  ? 7.716   40.178 58.555 1.00 26.04 ? 70  THR B O   1 
ATOM   1392 C  CB  . THR B 1 70  ? 8.643   43.133 59.577 1.00 29.62 ? 70  THR B CB  1 
ATOM   1393 O  OG1 . THR B 1 70  ? 7.955   43.391 58.344 1.00 30.21 ? 70  THR B OG1 1 
ATOM   1394 C  CG2 . THR B 1 70  ? 9.709   44.204 59.695 1.00 34.79 ? 70  THR B CG2 1 
ATOM   1395 N  N   . TRP B 1 71  ? 7.775   40.339 60.813 1.00 18.76 ? 71  TRP B N   1 
ATOM   1396 C  CA  . TRP B 1 71  ? 6.708   39.337 61.002 1.00 18.38 ? 71  TRP B CA  1 
ATOM   1397 C  C   . TRP B 1 71  ? 5.517   40.019 61.695 1.00 17.94 ? 71  TRP B C   1 
ATOM   1398 O  O   . TRP B 1 71  ? 5.673   40.881 62.559 1.00 18.34 ? 71  TRP B O   1 
ATOM   1399 C  CB  . TRP B 1 71  ? 7.226   38.210 61.902 1.00 18.97 ? 71  TRP B CB  1 
ATOM   1400 C  CG  . TRP B 1 71  ? 8.201   37.296 61.232 1.00 18.01 ? 71  TRP B CG  1 
ATOM   1401 C  CD1 . TRP B 1 71  ? 9.554   37.391 61.229 1.00 18.86 ? 71  TRP B CD1 1 
ATOM   1402 C  CD2 . TRP B 1 71  ? 7.874   36.159 60.406 1.00 17.50 ? 71  TRP B CD2 1 
ATOM   1403 N  NE1 . TRP B 1 71  ? 10.096  36.363 60.482 1.00 18.59 ? 71  TRP B NE1 1 
ATOM   1404 C  CE2 . TRP B 1 71  ? 9.083   35.594 59.979 1.00 18.38 ? 71  TRP B CE2 1 
ATOM   1405 C  CE3 . TRP B 1 71  ? 6.674   35.542 60.027 1.00 17.25 ? 71  TRP B CE3 1 
ATOM   1406 C  CZ2 . TRP B 1 71  ? 9.144   34.461 59.168 1.00 18.27 ? 71  TRP B CZ2 1 
ATOM   1407 C  CZ3 . TRP B 1 71  ? 6.738   34.416 59.223 1.00 16.38 ? 71  TRP B CZ3 1 
ATOM   1408 C  CH2 . TRP B 1 71  ? 7.964   33.883 58.809 1.00 17.44 ? 71  TRP B CH2 1 
ATOM   1409 N  N   . ARG B 1 72  ? 4.340   39.546 61.313 1.00 15.63 ? 72  ARG B N   1 
ATOM   1410 C  CA  . ARG B 1 72  ? 3.096   39.973 61.952 1.00 15.43 ? 72  ARG B CA  1 
ATOM   1411 C  C   . ARG B 1 72  ? 2.253   38.730 62.275 1.00 13.98 ? 72  ARG B C   1 
ATOM   1412 O  O   . ARG B 1 72  ? 2.480   37.660 61.695 1.00 13.98 ? 72  ARG B O   1 
ATOM   1413 C  CB  . ARG B 1 72  ? 2.344   40.929 61.041 1.00 16.53 ? 72  ARG B CB  1 
ATOM   1414 C  CG  . ARG B 1 72  ? 2.971   42.317 60.930 1.00 19.90 ? 72  ARG B CG  1 
ATOM   1415 C  CD  . ARG B 1 72  ? 2.252   43.146 59.881 1.00 21.33 ? 72  ARG B CD  1 
ATOM   1416 N  NE  . ARG B 1 72  ? 2.794   44.454 59.701 1.00 27.36 ? 72  ARG B NE  1 
ATOM   1417 C  CZ  . ARG B 1 72  ? 2.757   45.505 60.473 1.00 29.28 ? 72  ARG B CZ  1 
ATOM   1418 N  NH1 . ARG B 1 72  ? 1.818   45.671 61.406 1.00 29.42 ? 72  ARG B NH1 1 
ATOM   1419 N  NH2 . ARG B 1 72  ? 3.637   46.481 60.283 1.00 40.88 ? 72  ARG B NH2 1 
ATOM   1420 N  N   . GLU B 1 73  ? 1.280   38.906 63.153 1.00 13.87 ? 73  GLU B N   1 
ATOM   1421 C  CA  . GLU B 1 73  ? 0.432   37.789 63.583 1.00 12.99 ? 73  GLU B CA  1 
ATOM   1422 C  C   . GLU B 1 73  ? -1.035  38.108 63.378 1.00 12.09 ? 73  GLU B C   1 
ATOM   1423 O  O   . GLU B 1 73  ? -1.436  39.260 63.321 1.00 11.83 ? 73  GLU B O   1 
ATOM   1424 C  CB  . GLU B 1 73  ? 0.729   37.438 65.031 1.00 12.80 ? 73  GLU B CB  1 
ATOM   1425 C  CG  . GLU B 1 73  ? 0.557   38.630 65.984 1.00 13.50 ? 73  GLU B CG  1 
ATOM   1426 C  CD  . GLU B 1 73  ? 0.494   38.140 67.429 1.00 17.94 ? 73  GLU B CD  1 
ATOM   1427 O  OE1 . GLU B 1 73  ? -0.306  37.224 67.683 1.00 17.74 ? 73  GLU B OE1 1 
ATOM   1428 O  OE2 . GLU B 1 73  ? 1.272   38.657 68.247 1.00 24.80 ? 73  GLU B OE2 1 
ATOM   1429 N  N   . ALA B 1 74  ? -1.856  37.041 63.390 1.00 10.05 ? 74  ALA B N   1 
ATOM   1430 C  CA  . ALA B 1 74  ? -3.285  37.169 63.390 1.00 10.42 ? 74  ALA B CA  1 
ATOM   1431 C  C   . ALA B 1 74  ? -3.912  35.934 64.066 1.00 10.31 ? 74  ALA B C   1 
ATOM   1432 O  O   . ALA B 1 74  ? -3.450  34.813 63.872 1.00 11.81 ? 74  ALA B O   1 
ATOM   1433 C  CB  . ALA B 1 74  ? -3.861  37.293 61.988 1.00 12.20 ? 74  ALA B CB  1 
ATOM   1434 N  N   . ASP B 1 75  ? -5.008  36.172 64.779 1.00 10.51 ? 75  ASP B N   1 
ATOM   1435 C  CA  . ASP B 1 75  ? -5.736  35.097 65.416 1.00 9.74  ? 75  ASP B CA  1 
ATOM   1436 C  C   . ASP B 1 75  ? -6.504  34.254 64.396 1.00 11.44 ? 75  ASP B C   1 
ATOM   1437 O  O   . ASP B 1 75  ? -7.171  34.815 63.528 1.00 11.39 ? 75  ASP B O   1 
ATOM   1438 C  CB  . ASP B 1 75  ? -6.721  35.612 66.471 1.00 9.44  ? 75  ASP B CB  1 
ATOM   1439 C  CG  . ASP B 1 75  ? -6.041  36.142 67.713 1.00 10.18 ? 75  ASP B CG  1 
ATOM   1440 O  OD1 . ASP B 1 75  ? -4.853  36.497 67.706 1.00 10.62 ? 75  ASP B OD1 1 
ATOM   1441 O  OD2 . ASP B 1 75  ? -6.781  36.273 68.719 1.00 10.36 ? 75  ASP B OD2 1 
ATOM   1442 N  N   . ILE B 1 76  ? -6.537  32.954 64.619 1.00 10.67 ? 76  ILE B N   1 
ATOM   1443 C  CA  . ILE B 1 76  ? -7.291  32.032 63.738 1.00 11.36 ? 76  ILE B CA  1 
ATOM   1444 C  C   . ILE B 1 76  ? -8.307  31.251 64.560 1.00 11.37 ? 76  ILE B C   1 
ATOM   1445 O  O   . ILE B 1 76  ? -8.073  30.945 65.730 1.00 12.67 ? 76  ILE B O   1 
ATOM   1446 C  CB  . ILE B 1 76  ? -6.259  31.097 63.075 1.00 11.47 ? 76  ILE B CB  1 
ATOM   1447 C  CG1 . ILE B 1 76  ? -5.317  31.876 62.137 1.00 12.29 ? 76  ILE B CG1 1 
ATOM   1448 C  CG2 . ILE B 1 76  ? -6.877  29.937 62.338 1.00 12.92 ? 76  ILE B CG2 1 
ATOM   1449 C  CD1 . ILE B 1 76  ? -6.048  32.470 60.950 1.00 13.83 ? 76  ILE B CD1 1 
ATOM   1450 N  N   . ASN B 1 77  ? -9.425  30.881 63.953 1.00 12.92 ? 77  ASN B N   1 
ATOM   1451 C  CA  . ASN B 1 77  ? -10.458 30.086 64.566 1.00 13.90 ? 77  ASN B CA  1 
ATOM   1452 C  C   . ASN B 1 77  ? -11.186 30.761 65.712 1.00 14.13 ? 77  ASN B C   1 
ATOM   1453 O  O   . ASN B 1 77  ? -11.798 30.055 66.543 1.00 16.07 ? 77  ASN B O   1 
ATOM   1454 C  CB  . ASN B 1 77  ? -9.965  28.706 65.000 1.00 18.62 ? 77  ASN B CB  1 
ATOM   1455 C  CG  . ASN B 1 77  ? -9.531  27.812 63.878 1.00 18.98 ? 77  ASN B CG  1 
ATOM   1456 O  OD1 . ASN B 1 77  ? -10.087 27.830 62.777 1.00 20.29 ? 77  ASN B OD1 1 
ATOM   1457 N  ND2 . ASN B 1 77  ? -8.491  27.012 64.121 1.00 20.14 ? 77  ASN B ND2 1 
ATOM   1458 N  N   . TYR B 1 78  ? -11.134 32.084 65.779 1.00 13.04 ? 78  TYR B N   1 
ATOM   1459 C  CA  . TYR B 1 78  ? -11.828 32.809 66.855 1.00 13.24 ? 78  TYR B CA  1 
ATOM   1460 C  C   . TYR B 1 78  ? -13.280 33.094 66.511 1.00 12.32 ? 78  TYR B C   1 
ATOM   1461 O  O   . TYR B 1 78  ? -13.561 33.586 65.430 1.00 13.87 ? 78  TYR B O   1 
ATOM   1462 C  CB  . TYR B 1 78  ? -11.084 34.118 67.166 1.00 12.93 ? 78  TYR B CB  1 
ATOM   1463 C  CG  . TYR B 1 78  ? -11.746 34.877 68.300 1.00 12.43 ? 78  TYR B CG  1 
ATOM   1464 C  CD1 . TYR B 1 78  ? -11.546 34.499 69.617 1.00 11.84 ? 78  TYR B CD1 1 
ATOM   1465 C  CD2 . TYR B 1 78  ? -12.677 35.883 68.042 1.00 12.02 ? 78  TYR B CD2 1 
ATOM   1466 C  CE1 . TYR B 1 78  ? -12.176 35.159 70.655 1.00 12.25 ? 78  TYR B CE1 1 
ATOM   1467 C  CE2 . TYR B 1 78  ? -13.323 36.547 69.077 1.00 12.45 ? 78  TYR B CE2 1 
ATOM   1468 C  CZ  . TYR B 1 78  ? -13.082 36.170 70.365 1.00 11.67 ? 78  TYR B CZ  1 
ATOM   1469 O  OH  . TYR B 1 78  ? -13.704 36.827 71.399 1.00 13.25 ? 78  TYR B OH  1 
ATOM   1470 N  N   . THR B 1 79  ? -14.184 32.774 67.441 1.00 11.75 ? 79  THR B N   1 
ATOM   1471 C  CA  . THR B 1 79  ? -15.581 33.110 67.362 1.00 13.87 ? 79  THR B CA  1 
ATOM   1472 C  C   . THR B 1 79  ? -16.071 33.963 68.518 1.00 12.95 ? 79  THR B C   1 
ATOM   1473 O  O   . THR B 1 79  ? -16.652 35.034 68.323 1.00 16.26 ? 79  THR B O   1 
ATOM   1474 C  CB  . THR B 1 79  ? -16.484 31.904 67.186 1.00 16.67 ? 79  THR B CB  1 
ATOM   1475 O  OG1 . THR B 1 79  ? -16.254 30.948 68.254 1.00 23.08 ? 79  THR B OG1 1 
ATOM   1476 C  CG2 . THR B 1 79  ? -16.210 31.174 65.922 1.00 18.13 ? 79  THR B CG2 1 
ATOM   1477 N  N   . SER B 1 80  ? -15.750 33.555 69.740 1.00 14.05 ? 80  SER B N   1 
ATOM   1478 C  CA  . SER B 1 80  ? -16.069 34.318 70.923 1.00 14.55 ? 80  SER B CA  1 
ATOM   1479 C  C   . SER B 1 80  ? -15.188 33.907 72.114 1.00 14.56 ? 80  SER B C   1 
ATOM   1480 O  O   . SER B 1 80  ? -14.572 32.822 72.091 1.00 15.84 ? 80  SER B O   1 
ATOM   1481 C  CB  . SER B 1 80  ? -17.539 34.123 71.336 1.00 15.45 ? 80  SER B CB  1 
ATOM   1482 O  OG  . SER B 1 80  ? -17.777 32.867 71.864 1.00 24.20 ? 80  SER B OG  1 
ATOM   1483 N  N   . GLY B 1 81  ? -15.291 34.674 73.176 1.00 13.57 ? 81  GLY B N   1 
ATOM   1484 C  CA  . GLY B 1 81  ? -14.654 34.409 74.447 1.00 15.38 ? 81  GLY B CA  1 
ATOM   1485 C  C   . GLY B 1 81  ? -13.211 34.845 74.488 1.00 12.74 ? 81  GLY B C   1 
ATOM   1486 O  O   . GLY B 1 81  ? -12.790 35.787 73.788 1.00 11.67 ? 81  GLY B O   1 
ATOM   1487 N  N   . PHE B 1 82  ? -12.428 34.251 75.359 1.00 12.90 ? 82  PHE B N   1 
ATOM   1488 C  CA  . PHE B 1 82  ? -10.986 34.515 75.430 1.00 12.61 ? 82  PHE B CA  1 
ATOM   1489 C  C   . PHE B 1 82  ? -10.330 34.127 74.111 1.00 13.39 ? 82  PHE B C   1 
ATOM   1490 O  O   . PHE B 1 82  ? -10.750 33.222 73.420 1.00 15.26 ? 82  PHE B O   1 
ATOM   1491 C  CB  . PHE B 1 82  ? -10.370 33.720 76.589 1.00 12.78 ? 82  PHE B CB  1 
ATOM   1492 C  CG  . PHE B 1 82  ? -10.738 34.250 77.955 1.00 11.10 ? 82  PHE B CG  1 
ATOM   1493 C  CD1 . PHE B 1 82  ? -10.188 35.397 78.467 1.00 12.10 ? 82  PHE B CD1 1 
ATOM   1494 C  CD2 . PHE B 1 82  ? -11.655 33.557 78.756 1.00 13.60 ? 82  PHE B CD2 1 
ATOM   1495 C  CE1 . PHE B 1 82  ? -10.530 35.879 79.718 1.00 12.31 ? 82  PHE B CE1 1 
ATOM   1496 C  CE2 . PHE B 1 82  ? -12.011 34.038 79.989 1.00 18.05 ? 82  PHE B CE2 1 
ATOM   1497 C  CZ  . PHE B 1 82  ? -11.468 35.221 80.479 1.00 14.36 ? 82  PHE B CZ  1 
ATOM   1498 N  N   . ARG B 1 83  ? -9.207  34.825 73.808 1.00 12.82 ? 83  ARG B N   1 
ATOM   1499 C  CA  . ARG B 1 83  ? -8.428  34.433 72.656 1.00 12.76 ? 83  ARG B CA  1 
ATOM   1500 C  C   . ARG B 1 83  ? -7.921  33.002 72.819 1.00 13.26 ? 83  ARG B C   1 
ATOM   1501 O  O   . ARG B 1 83  ? -7.690  32.535 73.943 1.00 15.75 ? 83  ARG B O   1 
ATOM   1502 C  CB  . ARG B 1 83  ? -7.260  35.374 72.358 1.00 11.61 ? 83  ARG B CB  1 
ATOM   1503 C  CG  . ARG B 1 83  ? -7.715  36.807 72.048 1.00 11.37 ? 83  ARG B CG  1 
ATOM   1504 C  CD  . ARG B 1 83  ? -6.575  37.798 72.054 1.00 11.85 ? 83  ARG B CD  1 
ATOM   1505 N  NE  . ARG B 1 83  ? -5.619  37.573 70.996 1.00 11.42 ? 83  ARG B NE  1 
ATOM   1506 C  CZ  . ARG B 1 83  ? -4.378  37.992 70.966 1.00 13.02 ? 83  ARG B CZ  1 
ATOM   1507 N  NH1 . ARG B 1 83  ? -3.896  38.637 72.034 1.00 13.57 ? 83  ARG B NH1 1 
ATOM   1508 N  NH2 . ARG B 1 83  ? -3.602  37.746 69.929 1.00 14.36 ? 83  ARG B NH2 1 
ATOM   1509 N  N   . ASN B 1 84  ? -7.848  32.299 71.709 1.00 13.35 ? 84  ASN B N   1 
ATOM   1510 C  CA  . ASN B 1 84  ? -7.460  30.886 71.748 1.00 14.48 ? 84  ASN B CA  1 
ATOM   1511 C  C   . ASN B 1 84  ? -5.970  30.749 71.491 1.00 13.97 ? 84  ASN B C   1 
ATOM   1512 O  O   . ASN B 1 84  ? -5.227  31.717 71.644 1.00 15.50 ? 84  ASN B O   1 
ATOM   1513 C  CB  . ASN B 1 84  ? -8.298  30.117 70.747 1.00 14.22 ? 84  ASN B CB  1 
ATOM   1514 C  CG  . ASN B 1 84  ? -8.034  30.537 69.317 1.00 13.94 ? 84  ASN B CG  1 
ATOM   1515 O  OD1 . ASN B 1 84  ? -6.986  31.100 68.995 1.00 14.31 ? 84  ASN B OD1 1 
ATOM   1516 N  ND2 . ASN B 1 84  ? -9.014  30.265 68.454 1.00 16.51 ? 84  ASN B ND2 1 
ATOM   1517 N  N   . SER B 1 85  ? -5.520  29.535 71.214 1.00 15.48 ? 85  SER B N   1 
ATOM   1518 C  CA  . SER B 1 85  ? -4.101  29.269 71.072 1.00 14.99 ? 85  SER B CA  1 
ATOM   1519 C  C   . SER B 1 85  ? -3.587  29.331 69.655 1.00 15.57 ? 85  SER B C   1 
ATOM   1520 O  O   . SER B 1 85  ? -2.380  29.052 69.434 1.00 15.04 ? 85  SER B O   1 
ATOM   1521 C  CB  . SER B 1 85  ? -3.740  27.911 71.706 1.00 18.00 ? 85  SER B CB  1 
ATOM   1522 O  OG  . SER B 1 85  ? -4.423  26.879 71.040 1.00 26.67 ? 85  SER B OG  1 
ATOM   1523 N  N   . ASP B 1 86  ? -4.440  29.631 68.695 1.00 14.92 ? 86  ASP B N   1 
ATOM   1524 C  CA  . ASP B 1 86  ? -4.154  29.505 67.290 1.00 12.94 ? 86  ASP B CA  1 
ATOM   1525 C  C   . ASP B 1 86  ? -3.783  30.843 66.649 1.00 10.97 ? 86  ASP B C   1 
ATOM   1526 O  O   . ASP B 1 86  ? -4.541  31.814 66.707 1.00 12.07 ? 86  ASP B O   1 
ATOM   1527 C  CB  . ASP B 1 86  ? -5.368  28.911 66.565 1.00 15.54 ? 86  ASP B CB  1 
ATOM   1528 C  CG  . ASP B 1 86  ? -5.702  27.504 66.979 1.00 19.19 ? 86  ASP B CG  1 
ATOM   1529 O  OD1 . ASP B 1 86  ? -4.871  26.836 67.659 1.00 20.15 ? 86  ASP B OD1 1 
ATOM   1530 O  OD2 . ASP B 1 86  ? -6.780  26.990 66.581 1.00 22.78 ? 86  ASP B OD2 1 
ATOM   1531 N  N   . ARG B 1 87  ? -2.661  30.841 65.926 1.00 10.55 ? 87  ARG B N   1 
ATOM   1532 C  CA  . ARG B 1 87  ? -2.247  32.058 65.235 1.00 11.68 ? 87  ARG B CA  1 
ATOM   1533 C  C   . ARG B 1 87  ? -1.611  31.746 63.878 1.00 10.78 ? 87  ARG B C   1 
ATOM   1534 O  O   . ARG B 1 87  ? -0.964  30.715 63.710 1.00 12.23 ? 87  ARG B O   1 
ATOM   1535 C  CB  . ARG B 1 87  ? -1.151  32.805 66.051 1.00 11.16 ? 87  ARG B CB  1 
ATOM   1536 C  CG  . ARG B 1 87  ? -1.539  33.082 67.481 1.00 11.58 ? 87  ARG B CG  1 
ATOM   1537 C  CD  . ARG B 1 87  ? -2.370  34.269 67.714 1.00 11.58 ? 87  ARG B CD  1 
ATOM   1538 N  NE  . ARG B 1 87  ? -2.623  34.541 69.140 1.00 12.24 ? 87  ARG B NE  1 
ATOM   1539 C  CZ  . ARG B 1 87  ? -3.597  33.997 69.853 1.00 11.75 ? 87  ARG B CZ  1 
ATOM   1540 N  NH1 . ARG B 1 87  ? -4.436  33.138 69.292 1.00 13.36 ? 87  ARG B NH1 1 
ATOM   1541 N  NH2 . ARG B 1 87  ? -3.728  34.243 71.148 1.00 14.88 ? 87  ARG B NH2 1 
ATOM   1542 N  N   . ILE B 1 88  ? -1.780  32.663 62.959 1.00 11.66 ? 88  ILE B N   1 
ATOM   1543 C  CA  . ILE B 1 88  ? -1.041  32.704 61.719 1.00 12.43 ? 88  ILE B CA  1 
ATOM   1544 C  C   . ILE B 1 88  ? 0.066   33.758 61.826 1.00 10.92 ? 88  ILE B C   1 
ATOM   1545 O  O   . ILE B 1 88  ? -0.194  34.832 62.374 1.00 11.72 ? 88  ILE B O   1 
ATOM   1546 C  CB  . ILE B 1 88  ? -1.898  32.921 60.492 1.00 12.04 ? 88  ILE B CB  1 
ATOM   1547 C  CG1 . ILE B 1 88  ? -1.446  32.354 59.186 1.00 16.62 ? 88  ILE B CG1 1 
ATOM   1548 C  CG2 . ILE B 1 88  ? -2.622  34.230 60.436 1.00 17.18 ? 88  ILE B CG2 1 
ATOM   1549 C  CD1 . ILE B 1 88  ? -2.495  32.269 58.122 1.00 19.81 ? 88  ILE B CD1 1 
ATOM   1550 N  N   . LEU B 1 89  ? 1.280   33.367 61.465 1.00 11.99 ? 89  LEU B N   1 
ATOM   1551 C  CA  . LEU B 1 89  ? 2.423   34.289 61.418 1.00 13.02 ? 89  LEU B CA  1 
ATOM   1552 C  C   . LEU B 1 89  ? 2.800   34.516 59.947 1.00 13.13 ? 89  LEU B C   1 
ATOM   1553 O  O   . LEU B 1 89  ? 3.009   33.530 59.234 1.00 15.55 ? 89  LEU B O   1 
ATOM   1554 C  CB  . LEU B 1 89  ? 3.616   33.690 62.147 1.00 13.13 ? 89  LEU B CB  1 
ATOM   1555 C  CG  . LEU B 1 89  ? 3.657   33.807 63.656 1.00 16.09 ? 89  LEU B CG  1 
ATOM   1556 C  CD1 . LEU B 1 89  ? 3.902   35.268 64.053 1.00 20.97 ? 89  LEU B CD1 1 
ATOM   1557 C  CD2 . LEU B 1 89  ? 2.480   33.234 64.354 1.00 22.79 ? 89  LEU B CD2 1 
ATOM   1558 N  N   . TYR B 1 90  ? 2.863   35.771 59.535 1.00 14.58 ? 90  TYR B N   1 
ATOM   1559 C  CA  . TYR B 1 90  ? 3.157   36.065 58.125 1.00 14.70 ? 90  TYR B CA  1 
ATOM   1560 C  C   . TYR B 1 90  ? 4.276   37.081 58.014 1.00 16.91 ? 90  TYR B C   1 
ATOM   1561 O  O   . TYR B 1 90  ? 4.292   38.060 58.791 1.00 16.81 ? 90  TYR B O   1 
ATOM   1562 C  CB  . TYR B 1 90  ? 1.913   36.516 57.404 1.00 14.50 ? 90  TYR B CB  1 
ATOM   1563 C  CG  . TYR B 1 90  ? 1.168   37.704 57.919 1.00 14.62 ? 90  TYR B CG  1 
ATOM   1564 C  CD1 . TYR B 1 90  ? 0.262   37.596 58.969 1.00 14.42 ? 90  TYR B CD1 1 
ATOM   1565 C  CD2 . TYR B 1 90  ? 1.282   38.956 57.303 1.00 16.34 ? 90  TYR B CD2 1 
ATOM   1566 C  CE1 . TYR B 1 90  ? -0.454  38.685 59.442 1.00 15.36 ? 90  TYR B CE1 1 
ATOM   1567 C  CE2 . TYR B 1 90  ? 0.565   40.044 57.767 1.00 16.94 ? 90  TYR B CE2 1 
ATOM   1568 C  CZ  . TYR B 1 90  ? -0.288  39.913 58.828 1.00 16.18 ? 90  TYR B CZ  1 
ATOM   1569 O  OH  . TYR B 1 90  ? -1.034  40.985 59.298 1.00 17.40 ? 90  TYR B OH  1 
ATOM   1570 N  N   . SER B 1 91  ? 5.177   36.899 57.067 1.00 17.00 ? 91  SER B N   1 
ATOM   1571 C  CA  . SER B 1 91  ? 6.308   37.803 56.899 1.00 19.21 ? 91  SER B CA  1 
ATOM   1572 C  C   . SER B 1 91  ? 6.024   38.842 55.806 1.00 19.80 ? 91  SER B C   1 
ATOM   1573 O  O   . SER B 1 91  ? 5.089   38.693 55.015 1.00 19.89 ? 91  SER B O   1 
ATOM   1574 C  CB  . SER B 1 91  ? 7.594   37.040 56.555 1.00 18.32 ? 91  SER B CB  1 
ATOM   1575 O  OG  . SER B 1 91  ? 7.507   36.445 55.256 1.00 20.12 ? 91  SER B OG  1 
ATOM   1576 N  N   . SER B 1 92  ? 6.886   39.836 55.731 1.00 21.68 ? 92  SER B N   1 
ATOM   1577 C  CA  . SER B 1 92  ? 6.779   40.897 54.741 1.00 25.71 ? 92  SER B CA  1 
ATOM   1578 C  C   . SER B 1 92  ? 7.037   40.371 53.338 1.00 26.00 ? 92  SER B C   1 
ATOM   1579 O  O   . SER B 1 92  ? 6.619   40.979 52.352 1.00 25.36 ? 92  SER B O   1 
ATOM   1580 C  CB  . SER B 1 92  ? 7.672   42.069 55.102 1.00 27.97 ? 92  SER B CB  1 
ATOM   1581 O  OG  . SER B 1 92  ? 8.941   41.639 55.580 1.00 30.34 ? 92  SER B OG  1 
ATOM   1582 N  N   . ASP B 1 93  ? 7.630   39.179 53.253 1.00 25.64 ? 93  ASP B N   1 
ATOM   1583 C  CA  . ASP B 1 93  ? 7.865   38.477 52.020 1.00 25.36 ? 93  ASP B CA  1 
ATOM   1584 C  C   . ASP B 1 93  ? 6.991   37.264 51.812 1.00 25.38 ? 93  ASP B C   1 
ATOM   1585 O  O   . ASP B 1 93  ? 7.208   36.444 50.911 1.00 25.87 ? 93  ASP B O   1 
ATOM   1586 C  CB  . ASP B 1 93  ? 9.308   38.248 51.696 1.00 26.17 ? 93  ASP B CB  1 
ATOM   1587 C  CG  . ASP B 1 93  ? 10.080  37.492 52.758 1.00 26.12 ? 93  ASP B CG  1 
ATOM   1588 O  OD1 . ASP B 1 93  ? 9.579   37.367 53.897 1.00 27.47 ? 93  ASP B OD1 1 
ATOM   1589 O  OD2 . ASP B 1 93  ? 11.160  36.981 52.445 1.00 28.41 ? 93  ASP B OD2 1 
ATOM   1590 N  N   . TRP B 1 94  ? 5.923   37.152 52.606 1.00 24.54 ? 94  TRP B N   1 
ATOM   1591 C  CA  . TRP B 1 94  ? 4.860   36.233 52.418 1.00 24.28 ? 94  TRP B CA  1 
ATOM   1592 C  C   . TRP B 1 94  ? 5.130   34.798 52.657 1.00 22.39 ? 94  TRP B C   1 
ATOM   1593 O  O   . TRP B 1 94  ? 4.434   33.881 52.183 1.00 21.76 ? 94  TRP B O   1 
ATOM   1594 C  CB  . TRP B 1 94  ? 4.026   36.542 51.154 1.00 24.31 ? 94  TRP B CB  1 
ATOM   1595 C  CG  . TRP B 1 94  ? 3.759   38.023 51.054 1.00 25.60 ? 94  TRP B CG  1 
ATOM   1596 C  CD1 . TRP B 1 94  ? 4.357   38.909 50.209 1.00 26.13 ? 94  TRP B CD1 1 
ATOM   1597 C  CD2 . TRP B 1 94  ? 2.880   38.790 51.877 1.00 25.53 ? 94  TRP B CD2 1 
ATOM   1598 N  NE1 . TRP B 1 94  ? 3.866   40.178 50.438 1.00 27.24 ? 94  TRP B NE1 1 
ATOM   1599 C  CE2 . TRP B 1 94  ? 2.972   40.127 51.462 1.00 26.72 ? 94  TRP B CE2 1 
ATOM   1600 C  CE3 . TRP B 1 94  ? 2.000   38.476 52.918 1.00 25.42 ? 94  TRP B CE3 1 
ATOM   1601 C  CZ2 . TRP B 1 94  ? 2.233   41.141 52.064 1.00 26.95 ? 94  TRP B CZ2 1 
ATOM   1602 C  CZ3 . TRP B 1 94  ? 1.279   39.482 53.521 1.00 25.64 ? 94  TRP B CZ3 1 
ATOM   1603 C  CH2 . TRP B 1 94  ? 1.399   40.807 53.083 1.00 27.08 ? 94  TRP B CH2 1 
ATOM   1604 N  N   . LEU B 1 95  ? 6.067   34.545 53.584 1.00 22.60 ? 95  LEU B N   1 
ATOM   1605 C  CA  . LEU B 1 95  ? 6.195   33.242 54.222 1.00 20.51 ? 95  LEU B CA  1 
ATOM   1606 C  C   . LEU B 1 95  ? 5.035   33.136 55.259 1.00 18.17 ? 95  LEU B C   1 
ATOM   1607 O  O   . LEU B 1 95  ? 4.746   34.135 55.899 1.00 19.83 ? 95  LEU B O   1 
ATOM   1608 C  CB  . LEU B 1 95  ? 7.507   33.194 55.038 1.00 22.97 ? 95  LEU B CB  1 
ATOM   1609 C  CG  . LEU B 1 95  ? 8.803   32.993 54.278 1.00 23.77 ? 95  LEU B CG  1 
ATOM   1610 C  CD1 . LEU B 1 95  ? 9.913   32.593 55.269 1.00 24.40 ? 95  LEU B CD1 1 
ATOM   1611 C  CD2 . LEU B 1 95  ? 8.632   31.891 53.231 1.00 27.09 ? 95  LEU B CD2 1 
ATOM   1612 N  N   . ILE B 1 96  ? 4.406   31.999 55.354 1.00 15.72 ? 96  ILE B N   1 
ATOM   1613 C  CA  . ILE B 1 96  ? 3.277   31.740 56.231 1.00 13.89 ? 96  ILE B CA  1 
ATOM   1614 C  C   . ILE B 1 96  ? 3.515   30.537 57.147 1.00 14.18 ? 96  ILE B C   1 
ATOM   1615 O  O   . ILE B 1 96  ? 3.745   29.422 56.705 1.00 13.59 ? 96  ILE B O   1 
ATOM   1616 C  CB  A ILE B 1 96  ? 1.928   31.640 55.554 0.50 14.44 ? 96  ILE B CB  1 
ATOM   1617 C  CB  B ILE B 1 96  ? 2.006   31.476 55.377 0.50 14.47 ? 96  ILE B CB  1 
ATOM   1618 C  CG1 A ILE B 1 96  ? 1.610   32.623 54.449 0.50 13.64 ? 96  ILE B CG1 1 
ATOM   1619 C  CG1 B ILE B 1 96  ? 1.859   32.448 54.197 0.50 14.60 ? 96  ILE B CG1 1 
ATOM   1620 C  CG2 A ILE B 1 96  ? 0.803   31.589 56.586 0.50 17.08 ? 96  ILE B CG2 1 
ATOM   1621 C  CG2 B ILE B 1 96  ? 0.777   31.487 56.251 0.50 14.28 ? 96  ILE B CG2 1 
ATOM   1622 C  CD1 A ILE B 1 96  ? 1.543   34.065 54.861 0.50 13.36 ? 96  ILE B CD1 1 
ATOM   1623 C  CD1 B ILE B 1 96  ? 0.675   33.372 54.336 0.50 15.47 ? 96  ILE B CD1 1 
ATOM   1624 N  N   . TYR B 1 97  ? 3.406   30.795 58.446 1.00 12.40 ? 97  TYR B N   1 
ATOM   1625 C  CA  . TYR B 1 97  ? 3.571   29.772 59.463 1.00 13.02 ? 97  TYR B CA  1 
ATOM   1626 C  C   . TYR B 1 97  ? 2.277   29.762 60.317 1.00 13.11 ? 97  TYR B C   1 
ATOM   1627 O  O   . TYR B 1 97  ? 1.554   30.751 60.401 1.00 13.56 ? 97  TYR B O   1 
ATOM   1628 C  CB  . TYR B 1 97  ? 4.766   30.068 60.367 1.00 14.52 ? 97  TYR B CB  1 
ATOM   1629 C  CG  . TYR B 1 97  ? 6.110   29.626 59.849 1.00 15.42 ? 97  TYR B CG  1 
ATOM   1630 C  CD1 . TYR B 1 97  ? 6.740   30.294 58.806 1.00 15.82 ? 97  TYR B CD1 1 
ATOM   1631 C  CD2 . TYR B 1 97  ? 6.779   28.522 60.381 1.00 16.16 ? 97  TYR B CD2 1 
ATOM   1632 C  CE1 . TYR B 1 97  ? 7.966   29.908 58.308 1.00 16.02 ? 97  TYR B CE1 1 
ATOM   1633 C  CE2 . TYR B 1 97  ? 8.022   28.138 59.900 1.00 16.45 ? 97  TYR B CE2 1 
ATOM   1634 C  CZ  . TYR B 1 97  ? 8.615   28.830 58.886 1.00 16.41 ? 97  TYR B CZ  1 
ATOM   1635 O  OH  . TYR B 1 97  ? 9.833   28.423 58.397 1.00 18.78 ? 97  TYR B OH  1 
ATOM   1636 N  N   . LYS B 1 98  ? 2.100   28.652 61.006 1.00 12.67 ? 98  LYS B N   1 
ATOM   1637 C  CA  . LYS B 1 98  ? 1.048   28.517 61.983 1.00 13.79 ? 98  LYS B CA  1 
ATOM   1638 C  C   . LYS B 1 98  ? 1.622   28.067 63.330 1.00 13.98 ? 98  LYS B C   1 
ATOM   1639 O  O   . LYS B 1 98  ? 2.642   27.394 63.345 1.00 13.59 ? 98  LYS B O   1 
ATOM   1640 C  CB  . LYS B 1 98  ? -0.073  27.634 61.563 1.00 17.09 ? 98  LYS B CB  1 
ATOM   1641 C  CG  . LYS B 1 98  ? 0.103   26.175 61.568 1.00 18.85 ? 98  LYS B CG  1 
ATOM   1642 C  CD  . LYS B 1 98  ? -1.140  25.409 61.215 1.00 24.45 ? 98  LYS B CD  1 
ATOM   1643 C  CE  . LYS B 1 98  ? -0.878  23.917 61.078 1.00 27.96 ? 98  LYS B CE  1 
ATOM   1644 N  NZ  . LYS B 1 98  ? -2.183  23.198 60.823 1.00 33.71 ? 98  LYS B NZ  1 
ATOM   1645 N  N   . THR B 1 99  ? 0.867   28.405 64.357 1.00 13.79 ? 99  THR B N   1 
ATOM   1646 C  CA  . THR B 1 99  ? 1.036   27.876 65.701 1.00 13.92 ? 99  THR B CA  1 
ATOM   1647 C  C   . THR B 1 99  ? -0.364  27.525 66.249 1.00 14.10 ? 99  THR B C   1 
ATOM   1648 O  O   . THR B 1 99  ? -1.311  28.276 66.001 1.00 14.33 ? 99  THR B O   1 
ATOM   1649 C  CB  . THR B 1 99  ? 1.765   28.787 66.664 1.00 13.44 ? 99  THR B CB  1 
ATOM   1650 O  OG1 . THR B 1 99  ? 1.956   28.228 67.943 1.00 15.54 ? 99  THR B OG1 1 
ATOM   1651 C  CG2 . THR B 1 99  ? 1.129   30.152 66.851 1.00 15.44 ? 99  THR B CG2 1 
ATOM   1652 N  N   . THR B 1 100 ? -0.402  26.402 66.968 1.00 15.79 ? 100 THR B N   1 
ATOM   1653 C  CA  . THR B 1 100 ? -1.618  26.000 67.664 1.00 17.56 ? 100 THR B CA  1 
ATOM   1654 C  C   . THR B 1 100 ? -1.355  25.807 69.150 1.00 17.66 ? 100 THR B C   1 
ATOM   1655 O  O   . THR B 1 100 ? -2.177  25.291 69.900 1.00 20.52 ? 100 THR B O   1 
ATOM   1656 C  CB  . THR B 1 100 ? -2.227  24.734 67.069 1.00 19.34 ? 100 THR B CB  1 
ATOM   1657 O  OG1 . THR B 1 100 ? -1.251  23.675 67.102 1.00 23.11 ? 100 THR B OG1 1 
ATOM   1658 C  CG2 . THR B 1 100 ? -2.668  24.932 65.643 1.00 21.24 ? 100 THR B CG2 1 
ATOM   1659 N  N   . ASP B 1 101 ? -0.202  26.318 69.606 1.00 19.76 ? 101 ASP B N   1 
ATOM   1660 C  CA  . ASP B 1 101 ? 0.160   26.192 71.010 1.00 20.86 ? 101 ASP B CA  1 
ATOM   1661 C  C   . ASP B 1 101 ? 0.721   27.464 71.587 1.00 19.29 ? 101 ASP B C   1 
ATOM   1662 O  O   . ASP B 1 101 ? 1.698   27.445 72.357 1.00 19.89 ? 101 ASP B O   1 
ATOM   1663 C  CB  . ASP B 1 101 ? 1.119   25.020 71.210 1.00 21.04 ? 101 ASP B CB  1 
ATOM   1664 C  CG  . ASP B 1 101 ? 2.380   25.099 70.407 1.00 20.22 ? 101 ASP B CG  1 
ATOM   1665 O  OD1 . ASP B 1 101 ? 2.686   26.141 69.799 1.00 19.35 ? 101 ASP B OD1 1 
ATOM   1666 O  OD2 . ASP B 1 101 ? 3.129   24.078 70.390 1.00 23.78 ? 101 ASP B OD2 1 
ATOM   1667 N  N   . HIS B 1 102 ? 0.134   28.624 71.255 1.00 20.00 ? 102 HIS B N   1 
ATOM   1668 C  CA  . HIS B 1 102 ? 0.593   29.873 71.861 1.00 21.66 ? 102 HIS B CA  1 
ATOM   1669 C  C   . HIS B 1 102 ? 2.072   30.139 71.586 1.00 21.05 ? 102 HIS B C   1 
ATOM   1670 O  O   . HIS B 1 102 ? 2.804   30.525 72.502 1.00 20.42 ? 102 HIS B O   1 
ATOM   1671 C  CB  . HIS B 1 102 ? 0.386   29.884 73.376 1.00 25.05 ? 102 HIS B CB  1 
ATOM   1672 C  CG  . HIS B 1 102 ? -0.993  30.196 73.810 1.00 25.87 ? 102 HIS B CG  1 
ATOM   1673 N  ND1 . HIS B 1 102 ? -1.798  29.273 74.464 1.00 29.13 ? 102 HIS B ND1 1 
ATOM   1674 C  CD2 . HIS B 1 102 ? -1.700  31.365 73.721 1.00 26.02 ? 102 HIS B CD2 1 
ATOM   1675 C  CE1 . HIS B 1 102 ? -2.964  29.864 74.725 1.00 30.31 ? 102 HIS B CE1 1 
ATOM   1676 N  NE2 . HIS B 1 102 ? -2.914  31.107 74.288 1.00 29.12 ? 102 HIS B NE2 1 
ATOM   1677 N  N   . TYR B 1 103 ? 2.500   30.008 70.350 1.00 19.61 ? 103 TYR B N   1 
ATOM   1678 C  CA  . TYR B 1 103 ? 3.819   30.428 69.923 1.00 20.72 ? 103 TYR B CA  1 
ATOM   1679 C  C   . TYR B 1 103 ? 4.944   29.566 70.428 1.00 19.93 ? 103 TYR B C   1 
ATOM   1680 O  O   . TYR B 1 103 ? 6.108   29.982 70.422 1.00 22.88 ? 103 TYR B O   1 
ATOM   1681 C  CB  . TYR B 1 103 ? 4.076   31.893 70.204 1.00 19.04 ? 103 TYR B CB  1 
ATOM   1682 C  CG  . TYR B 1 103 ? 2.982   32.882 70.066 1.00 17.76 ? 103 TYR B CG  1 
ATOM   1683 C  CD1 . TYR B 1 103 ? 2.671   33.517 68.869 1.00 16.98 ? 103 TYR B CD1 1 
ATOM   1684 C  CD2 . TYR B 1 103 ? 2.312   33.356 71.214 1.00 18.34 ? 103 TYR B CD2 1 
ATOM   1685 C  CE1 . TYR B 1 103 ? 1.686   34.487 68.780 1.00 17.19 ? 103 TYR B CE1 1 
ATOM   1686 C  CE2 . TYR B 1 103 ? 1.323   34.306 71.117 1.00 18.58 ? 103 TYR B CE2 1 
ATOM   1687 C  CZ  . TYR B 1 103 ? 1.017   34.882 69.910 1.00 17.42 ? 103 TYR B CZ  1 
ATOM   1688 O  OH  . TYR B 1 103 ? 0.011   35.838 69.851 1.00 17.35 ? 103 TYR B OH  1 
ATOM   1689 N  N   . GLN B 1 104 ? 4.643   28.348 70.889 1.00 21.54 ? 104 GLN B N   1 
ATOM   1690 C  CA  . GLN B 1 104 ? 5.718   27.473 71.362 1.00 22.94 ? 104 GLN B CA  1 
ATOM   1691 C  C   . GLN B 1 104 ? 6.406   26.741 70.221 1.00 22.36 ? 104 GLN B C   1 
ATOM   1692 O  O   . GLN B 1 104 ? 7.620   26.597 70.213 1.00 24.14 ? 104 GLN B O   1 
ATOM   1693 C  CB  . GLN B 1 104 ? 5.210   26.507 72.410 1.00 23.47 ? 104 GLN B CB  1 
ATOM   1694 C  CG  . GLN B 1 104 ? 4.899   27.236 73.740 1.00 26.54 ? 104 GLN B CG  1 
ATOM   1695 C  CD  . GLN B 1 104 ? 4.243   26.291 74.732 1.00 31.63 ? 104 GLN B CD  1 
ATOM   1696 O  OE1 . GLN B 1 104 ? 4.843   25.922 75.727 1.00 31.53 ? 104 GLN B OE1 1 
ATOM   1697 N  NE2 . GLN B 1 104 ? 2.996   25.909 74.465 1.00 33.00 ? 104 GLN B NE2 1 
ATOM   1698 N  N   . THR B 1 105 ? 5.598   26.280 69.277 1.00 21.62 ? 105 THR B N   1 
ATOM   1699 C  CA  . THR B 1 105 ? 6.044   25.589 68.105 1.00 21.02 ? 105 THR B CA  1 
ATOM   1700 C  C   . THR B 1 105 ? 5.370   26.164 66.853 1.00 19.89 ? 105 THR B C   1 
ATOM   1701 O  O   . THR B 1 105 ? 4.256   26.646 66.901 1.00 19.90 ? 105 THR B O   1 
ATOM   1702 C  CB  . THR B 1 105 ? 5.857   24.087 68.150 1.00 25.17 ? 105 THR B CB  1 
ATOM   1703 O  OG1 . THR B 1 105 ? 4.499   23.708 68.167 1.00 26.51 ? 105 THR B OG1 1 
ATOM   1704 C  CG2 . THR B 1 105 ? 6.557   23.444 69.319 1.00 25.30 ? 105 THR B CG2 1 
ATOM   1705 N  N   . PHE B 1 106 ? 6.096   26.140 65.749 1.00 20.39 ? 106 PHE B N   1 
ATOM   1706 C  CA  . PHE B 1 106 ? 5.599   26.684 64.500 1.00 18.57 ? 106 PHE B CA  1 
ATOM   1707 C  C   . PHE B 1 106 ? 5.756   25.652 63.371 1.00 19.50 ? 106 PHE B C   1 
ATOM   1708 O  O   . PHE B 1 106 ? 6.711   24.888 63.380 1.00 20.21 ? 106 PHE B O   1 
ATOM   1709 C  CB  . PHE B 1 106 ? 6.377   27.950 64.128 1.00 21.82 ? 106 PHE B CB  1 
ATOM   1710 C  CG  . PHE B 1 106 ? 6.204   29.066 65.143 1.00 21.54 ? 106 PHE B CG  1 
ATOM   1711 C  CD1 . PHE B 1 106 ? 5.117   29.939 65.055 1.00 21.50 ? 106 PHE B CD1 1 
ATOM   1712 C  CD2 . PHE B 1 106 ? 7.088   29.237 66.184 1.00 22.15 ? 106 PHE B CD2 1 
ATOM   1713 C  CE1 . PHE B 1 106 ? 5.016   31.016 65.906 1.00 22.50 ? 106 PHE B CE1 1 
ATOM   1714 C  CE2 . PHE B 1 106 ? 6.975   30.307 67.063 1.00 22.79 ? 106 PHE B CE2 1 
ATOM   1715 C  CZ  . PHE B 1 106 ? 5.882   31.151 66.976 1.00 22.76 ? 106 PHE B CZ  1 
ATOM   1716 N  N   . THR B 1 107 ? 4.824   25.699 62.433 1.00 18.65 ? 107 THR B N   1 
ATOM   1717 C  CA  . THR B 1 107 ? 4.874   24.797 61.262 1.00 16.86 ? 107 THR B CA  1 
ATOM   1718 C  C   . THR B 1 107 ? 4.668   25.689 60.026 1.00 15.72 ? 107 THR B C   1 
ATOM   1719 O  O   . THR B 1 107 ? 3.737   26.521 60.006 1.00 15.69 ? 107 THR B O   1 
ATOM   1720 C  CB  . THR B 1 107 ? 3.680   23.805 61.329 1.00 22.09 ? 107 THR B CB  1 
ATOM   1721 O  OG1 . THR B 1 107 ? 3.822   22.974 62.497 1.00 23.34 ? 107 THR B OG1 1 
ATOM   1722 C  CG2 . THR B 1 107 ? 3.657   22.901 60.111 1.00 23.97 ? 107 THR B CG2 1 
ATOM   1723 N  N   . LYS B 1 108 ? 5.499   25.514 59.019 1.00 15.46 ? 108 LYS B N   1 
ATOM   1724 C  CA  . LYS B 1 108 ? 5.318   26.285 57.768 1.00 14.49 ? 108 LYS B CA  1 
ATOM   1725 C  C   . LYS B 1 108 ? 4.157   25.670 56.983 1.00 13.64 ? 108 LYS B C   1 
ATOM   1726 O  O   . LYS B 1 108 ? 4.099   24.461 56.792 1.00 17.57 ? 108 LYS B O   1 
ATOM   1727 C  CB  . LYS B 1 108 ? 6.598   26.124 56.918 1.00 15.44 ? 108 LYS B CB  1 
ATOM   1728 C  CG  . LYS B 1 108 ? 6.606   27.001 55.664 1.00 19.26 ? 108 LYS B CG  1 
ATOM   1729 C  CD  . LYS B 1 108 ? 8.058   27.218 55.216 1.00 19.87 ? 108 LYS B CD  1 
ATOM   1730 C  CE  . LYS B 1 108 ? 8.204   28.011 53.970 1.00 23.00 ? 108 LYS B CE  1 
ATOM   1731 N  NZ  . LYS B 1 108 ? 8.575   27.200 52.786 1.00 23.48 ? 108 LYS B NZ  1 
ATOM   1732 N  N   . ILE B 1 109 ? 3.263   26.543 56.506 1.00 12.32 ? 109 ILE B N   1 
ATOM   1733 C  CA  . ILE B 1 109 ? 2.111   26.094 55.765 1.00 12.45 ? 109 ILE B CA  1 
ATOM   1734 C  C   . ILE B 1 109 ? 1.997   26.679 54.369 1.00 12.37 ? 109 ILE B C   1 
ATOM   1735 O  O   . ILE B 1 109 ? 1.086   26.259 53.623 1.00 12.23 ? 109 ILE B O   1 
ATOM   1736 C  CB  . ILE B 1 109 ? 0.795   26.311 56.533 1.00 12.23 ? 109 ILE B CB  1 
ATOM   1737 C  CG1 . ILE B 1 109 ? 0.494   27.757 56.887 1.00 13.67 ? 109 ILE B CG1 1 
ATOM   1738 C  CG2 . ILE B 1 109 ? 0.761   25.443 57.805 1.00 14.11 ? 109 ILE B CG2 1 
ATOM   1739 C  CD1 . ILE B 1 109 ? -0.944  28.003 57.303 1.00 15.05 ? 109 ILE B CD1 1 
ATOM   1740 N  N   . ARG B 1 110 ? 2.838   27.617 53.959 1.00 14.00 ? 110 ARG B N   1 
ATOM   1741 C  CA  . ARG B 1 110 ? 2.881   28.028 52.549 1.00 15.36 ? 110 ARG B CA  1 
ATOM   1742 C  C   . ARG B 1 110 ? 4.381   28.341 52.201 1.00 20.64 ? 110 ARG B C   1 
ATOM   1743 O  O   . ARG B 1 110 ? 4.567   29.040 51.223 1.00 21.90 ? 110 ARG B O   1 
ATOM   1744 C  CB  . ARG B 1 110 ? 2.077   29.272 52.241 1.00 15.50 ? 110 ARG B CB  1 
ATOM   1745 C  CG  . ARG B 1 110 ? 0.565   29.150 52.408 1.00 14.19 ? 110 ARG B CG  1 
ATOM   1746 C  CD  . ARG B 1 110 ? -0.068  28.312 51.339 1.00 11.39 ? 110 ARG B CD  1 
ATOM   1747 N  NE  . ARG B 1 110 ? -1.524  28.215 51.435 1.00 11.93 ? 110 ARG B NE  1 
ATOM   1748 C  CZ  . ARG B 1 110 ? -2.221  27.417 52.223 1.00 12.63 ? 110 ARG B CZ  1 
ATOM   1749 N  NH1 . ARG B 1 110 ? -1.639  26.590 53.099 1.00 12.93 ? 110 ARG B NH1 1 
ATOM   1750 N  NH2 . ARG B 1 110 ? -3.544  27.456 52.232 1.00 14.70 ? 110 ARG B NH2 1 
ATOM   1751 O  OXT . ARG B 1 110 ? 5.209   27.880 52.949 1.00 32.87 ? 110 ARG B OXT 1 
ATOM   1752 N  N   . VAL C 1 3   ? 12.546  16.119 39.565 1.00 29.94 ? 3   VAL C N   1 
ATOM   1753 C  CA  . VAL C 1 3   ? 13.625  16.080 40.546 1.00 29.61 ? 3   VAL C CA  1 
ATOM   1754 C  C   . VAL C 1 3   ? 14.768  15.209 40.007 1.00 29.36 ? 3   VAL C C   1 
ATOM   1755 O  O   . VAL C 1 3   ? 14.537  14.086 39.567 1.00 35.00 ? 3   VAL C O   1 
ATOM   1756 C  CB  . VAL C 1 3   ? 13.148  15.541 41.898 1.00 31.21 ? 3   VAL C CB  1 
ATOM   1757 C  CG1 . VAL C 1 3   ? 14.304  15.320 42.869 1.00 31.29 ? 3   VAL C CG1 1 
ATOM   1758 C  CG2 . VAL C 1 3   ? 12.108  16.467 42.545 1.00 31.24 ? 3   VAL C CG2 1 
ATOM   1759 N  N   . ILE C 1 4   ? 15.986  15.730 40.008 1.00 21.89 ? 4   ILE C N   1 
ATOM   1760 C  CA  . ILE C 1 4   ? 17.143  14.869 39.592 1.00 19.90 ? 4   ILE C CA  1 
ATOM   1761 C  C   . ILE C 1 4   ? 18.137  14.923 40.758 1.00 19.68 ? 4   ILE C C   1 
ATOM   1762 O  O   . ILE C 1 4   ? 18.532  16.051 41.110 1.00 19.08 ? 4   ILE C O   1 
ATOM   1763 C  CB  . ILE C 1 4   ? 17.806  15.508 38.367 1.00 23.48 ? 4   ILE C CB  1 
ATOM   1764 C  CG1 . ILE C 1 4   ? 16.855  15.598 37.167 1.00 23.16 ? 4   ILE C CG1 1 
ATOM   1765 C  CG2 . ILE C 1 4   ? 19.113  14.896 38.003 1.00 24.16 ? 4   ILE C CG2 1 
ATOM   1766 C  CD1 . ILE C 1 4   ? 17.457  16.327 35.982 1.00 32.19 ? 4   ILE C CD1 1 
ATOM   1767 N  N   . ASN C 1 5   ? 18.389  13.837 41.430 1.00 17.49 ? 5   ASN C N   1 
ATOM   1768 C  CA  . ASN C 1 5   ? 19.236  13.876 42.626 1.00 17.47 ? 5   ASN C CA  1 
ATOM   1769 C  C   . ASN C 1 5   ? 20.110  12.644 42.776 1.00 16.67 ? 5   ASN C C   1 
ATOM   1770 O  O   . ASN C 1 5   ? 20.549  12.357 43.906 1.00 17.36 ? 5   ASN C O   1 
ATOM   1771 C  CB  . ASN C 1 5   ? 18.412  14.058 43.896 1.00 17.88 ? 5   ASN C CB  1 
ATOM   1772 C  CG  . ASN C 1 5   ? 17.592  12.836 44.239 1.00 18.14 ? 5   ASN C CG  1 
ATOM   1773 O  OD1 . ASN C 1 5   ? 17.358  11.980 43.375 1.00 23.60 ? 5   ASN C OD1 1 
ATOM   1774 N  ND2 . ASN C 1 5   ? 17.155  12.725 45.481 1.00 22.14 ? 5   ASN C ND2 1 
ATOM   1775 N  N   . THR C 1 6   ? 20.414  11.956 41.690 1.00 16.34 ? 6   THR C N   1 
ATOM   1776 C  CA  . THR C 1 6   ? 21.345  10.815 41.750 1.00 17.42 ? 6   THR C CA  1 
ATOM   1777 C  C   . THR C 1 6   ? 22.721  11.241 41.206 1.00 14.55 ? 6   THR C C   1 
ATOM   1778 O  O   . THR C 1 6   ? 22.858  12.262 40.540 1.00 14.00 ? 6   THR C O   1 
ATOM   1779 C  CB  . THR C 1 6   ? 20.832  9.691  40.828 1.00 17.26 ? 6   THR C CB  1 
ATOM   1780 O  OG1 . THR C 1 6   ? 20.734  10.225 39.500 1.00 18.36 ? 6   THR C OG1 1 
ATOM   1781 C  CG2 . THR C 1 6   ? 19.489  9.169  41.225 1.00 18.49 ? 6   THR C CG2 1 
ATOM   1782 N  N   . PHE C 1 7   ? 23.760  10.490 41.530 1.00 14.51 ? 7   PHE C N   1 
ATOM   1783 C  CA  . PHE C 1 7   ? 25.111  10.824 41.081 1.00 13.49 ? 7   PHE C CA  1 
ATOM   1784 C  C   . PHE C 1 7   ? 25.191  11.010 39.583 1.00 12.98 ? 7   PHE C C   1 
ATOM   1785 O  O   . PHE C 1 7   ? 25.701  12.013 39.051 1.00 13.67 ? 7   PHE C O   1 
ATOM   1786 C  CB  . PHE C 1 7   ? 26.133  9.805  41.545 1.00 14.48 ? 7   PHE C CB  1 
ATOM   1787 C  CG  . PHE C 1 7   ? 26.552  9.924  42.994 1.00 14.04 ? 7   PHE C CG  1 
ATOM   1788 C  CD1 . PHE C 1 7   ? 27.255  11.047 43.428 1.00 14.19 ? 7   PHE C CD1 1 
ATOM   1789 C  CD2 . PHE C 1 7   ? 26.255  8.931  43.916 1.00 15.38 ? 7   PHE C CD2 1 
ATOM   1790 C  CE1 . PHE C 1 7   ? 27.620  11.180 44.743 1.00 16.06 ? 7   PHE C CE1 1 
ATOM   1791 C  CE2 . PHE C 1 7   ? 26.647  9.059  45.252 1.00 16.19 ? 7   PHE C CE2 1 
ATOM   1792 C  CZ  . PHE C 1 7   ? 27.318  10.187 45.663 1.00 15.68 ? 7   PHE C CZ  1 
ATOM   1793 N  N   . ASP C 1 8   ? 24.692  9.987  38.861 1.00 14.62 ? 8   ASP C N   1 
ATOM   1794 C  CA  . ASP C 1 8   ? 24.801  10.050 37.400 1.00 16.15 ? 8   ASP C CA  1 
ATOM   1795 C  C   . ASP C 1 8   ? 23.921  11.140 36.823 1.00 15.14 ? 8   ASP C C   1 
ATOM   1796 O  O   . ASP C 1 8   ? 24.300  11.873 35.896 1.00 15.76 ? 8   ASP C O   1 
ATOM   1797 C  CB  . ASP C 1 8   ? 24.469  8.693  36.795 1.00 21.52 ? 8   ASP C CB  1 
ATOM   1798 C  CG  . ASP C 1 8   ? 25.585  7.681  36.963 1.00 25.54 ? 8   ASP C CG  1 
ATOM   1799 O  OD1 . ASP C 1 8   ? 26.729  7.994  36.581 1.00 26.53 ? 8   ASP C OD1 1 
ATOM   1800 O  OD2 . ASP C 1 8   ? 25.321  6.599  37.541 1.00 29.91 ? 8   ASP C OD2 1 
ATOM   1801 N  N   . GLY C 1 9   ? 22.704  11.275 37.382 1.00 16.19 ? 9   GLY C N   1 
ATOM   1802 C  CA  . GLY C 1 9   ? 21.786  12.267 36.815 1.00 15.86 ? 9   GLY C CA  1 
ATOM   1803 C  C   . GLY C 1 9   ? 22.302  13.664 37.001 1.00 12.99 ? 9   GLY C C   1 
ATOM   1804 O  O   . GLY C 1 9   ? 22.210  14.499 36.096 1.00 13.69 ? 9   GLY C O   1 
ATOM   1805 N  N   . VAL C 1 10  ? 22.812  13.967 38.188 1.00 12.78 ? 10  VAL C N   1 
ATOM   1806 C  CA  . VAL C 1 10  ? 23.303  15.318 38.420 1.00 11.66 ? 10  VAL C CA  1 
ATOM   1807 C  C   . VAL C 1 10  ? 24.591  15.580 37.679 1.00 10.98 ? 10  VAL C C   1 
ATOM   1808 O  O   . VAL C 1 10  ? 24.757  16.698 37.101 1.00 11.99 ? 10  VAL C O   1 
ATOM   1809 C  CB  . VAL C 1 10  ? 23.397  15.663 39.912 1.00 11.46 ? 10  VAL C CB  1 
ATOM   1810 C  CG1 . VAL C 1 10  ? 23.944  17.060 40.135 1.00 13.25 ? 10  VAL C CG1 1 
ATOM   1811 C  CG2 . VAL C 1 10  ? 22.023  15.484 40.577 1.00 12.23 ? 10  VAL C CG2 1 
ATOM   1812 N  N   . ALA C 1 11  ? 25.492  14.613 37.641 1.00 11.19 ? 11  ALA C N   1 
ATOM   1813 C  CA  . ALA C 1 11  ? 26.765  14.785 36.905 1.00 11.07 ? 11  ALA C CA  1 
ATOM   1814 C  C   . ALA C 1 11  ? 26.502  15.146 35.464 1.00 11.01 ? 11  ALA C C   1 
ATOM   1815 O  O   . ALA C 1 11  ? 27.162  16.038 34.875 1.00 12.04 ? 11  ALA C O   1 
ATOM   1816 C  CB  . ALA C 1 11  ? 27.645  13.559 37.047 1.00 11.74 ? 11  ALA C CB  1 
ATOM   1817 N  N   . ASP C 1 12  ? 25.605  14.389 34.828 1.00 11.94 ? 12  ASP C N   1 
ATOM   1818 C  CA  . ASP C 1 12  ? 25.339  14.603 33.418 1.00 12.81 ? 12  ASP C CA  1 
ATOM   1819 C  C   . ASP C 1 12  ? 24.666  15.944 33.156 1.00 12.93 ? 12  ASP C C   1 
ATOM   1820 O  O   . ASP C 1 12  ? 24.972  16.602 32.162 1.00 13.71 ? 12  ASP C O   1 
ATOM   1821 C  CB  . ASP C 1 12  ? 24.589  13.453 32.817 1.00 16.35 ? 12  ASP C CB  1 
ATOM   1822 C  CG  . ASP C 1 12  ? 25.392  12.176 32.661 1.00 21.02 ? 12  ASP C CG  1 
ATOM   1823 O  OD1 . ASP C 1 12  ? 26.617  12.263 32.521 1.00 22.82 ? 12  ASP C OD1 1 
ATOM   1824 O  OD2 . ASP C 1 12  ? 24.774  11.106 32.598 1.00 27.91 ? 12  ASP C OD2 1 
ATOM   1825 N  N   . TYR C 1 13  ? 23.770  16.346 34.051 1.00 13.21 ? 13  TYR C N   1 
ATOM   1826 C  CA  . TYR C 1 13  ? 23.066  17.636 33.892 1.00 13.01 ? 13  TYR C CA  1 
ATOM   1827 C  C   . TYR C 1 13  ? 24.054  18.783 34.003 1.00 12.45 ? 13  TYR C C   1 
ATOM   1828 O  O   . TYR C 1 13  ? 24.026  19.718 33.197 1.00 12.90 ? 13  TYR C O   1 
ATOM   1829 C  CB  . TYR C 1 13  ? 21.992  17.726 34.986 1.00 13.44 ? 13  TYR C CB  1 
ATOM   1830 C  CG  . TYR C 1 13  ? 20.967  18.795 34.741 1.00 13.36 ? 13  TYR C CG  1 
ATOM   1831 C  CD1 . TYR C 1 13  ? 21.197  20.098 35.154 1.00 15.67 ? 13  TYR C CD1 1 
ATOM   1832 C  CD2 . TYR C 1 13  ? 19.770  18.521 34.077 1.00 15.24 ? 13  TYR C CD2 1 
ATOM   1833 C  CE1 . TYR C 1 13  ? 20.284  21.102 34.941 1.00 16.80 ? 13  TYR C CE1 1 
ATOM   1834 C  CE2 . TYR C 1 13  ? 18.832  19.541 33.871 1.00 15.76 ? 13  TYR C CE2 1 
ATOM   1835 C  CZ  . TYR C 1 13  ? 19.092  20.810 34.284 1.00 17.22 ? 13  TYR C CZ  1 
ATOM   1836 O  OH  . TYR C 1 13  ? 18.173  21.833 34.124 1.00 21.48 ? 13  TYR C OH  1 
ATOM   1837 N  N   . LEU C 1 14  ? 24.960  18.699 34.986 1.00 12.04 ? 14  LEU C N   1 
ATOM   1838 C  CA  . LEU C 1 14  ? 25.987  19.714 35.143 1.00 11.62 ? 14  LEU C CA  1 
ATOM   1839 C  C   . LEU C 1 14  ? 26.845  19.889 33.906 1.00 11.78 ? 14  LEU C C   1 
ATOM   1840 O  O   . LEU C 1 14  ? 27.121  21.001 33.433 1.00 10.83 ? 14  LEU C O   1 
ATOM   1841 C  CB  . LEU C 1 14  ? 26.868  19.463 36.350 1.00 11.16 ? 14  LEU C CB  1 
ATOM   1842 C  CG  . LEU C 1 14  ? 26.274  19.735 37.727 1.00 11.97 ? 14  LEU C CG  1 
ATOM   1843 C  CD1 . LEU C 1 14  ? 27.095  19.016 38.780 1.00 11.94 ? 14  LEU C CD1 1 
ATOM   1844 C  CD2 . LEU C 1 14  ? 26.198  21.243 37.993 1.00 13.38 ? 14  LEU C CD2 1 
ATOM   1845 N  N   . GLN C 1 15  ? 27.386  18.782 33.391 1.00 12.36 ? 15  GLN C N   1 
ATOM   1846 C  CA  . GLN C 1 15  ? 28.332  18.912 32.283 1.00 11.92 ? 15  GLN C CA  1 
ATOM   1847 C  C   . GLN C 1 15  ? 27.648  19.358 31.000 1.00 12.15 ? 15  GLN C C   1 
ATOM   1848 O  O   . GLN C 1 15  ? 28.313  19.885 30.096 1.00 13.29 ? 15  GLN C O   1 
ATOM   1849 C  CB  . GLN C 1 15  ? 29.014  17.543 32.041 1.00 13.86 ? 15  GLN C CB  1 
ATOM   1850 C  CG  . GLN C 1 15  ? 29.965  17.123 33.120 1.00 14.39 ? 15  GLN C CG  1 
ATOM   1851 C  CD  . GLN C 1 15  ? 30.988  16.110 32.647 1.00 13.55 ? 15  GLN C CD  1 
ATOM   1852 O  OE1 . GLN C 1 15  ? 30.651  15.074 32.061 1.00 16.87 ? 15  GLN C OE1 1 
ATOM   1853 N  NE2 . GLN C 1 15  ? 32.262  16.362 32.971 1.00 15.85 ? 15  GLN C NE2 1 
ATOM   1854 N  N   . THR C 1 16  ? 26.358  19.088 30.876 1.00 12.22 ? 16  THR C N   1 
ATOM   1855 C  CA  . THR C 1 16  ? 25.586  19.411 29.689 1.00 12.54 ? 16  THR C CA  1 
ATOM   1856 C  C   . THR C 1 16  ? 25.019  20.811 29.720 1.00 12.08 ? 16  THR C C   1 
ATOM   1857 O  O   . THR C 1 16  ? 25.100  21.538 28.714 1.00 13.10 ? 16  THR C O   1 
ATOM   1858 C  CB  . THR C 1 16  ? 24.477  18.386 29.439 1.00 13.06 ? 16  THR C CB  1 
ATOM   1859 O  OG1 . THR C 1 16  ? 25.089  17.065 29.429 1.00 17.17 ? 16  THR C OG1 1 
ATOM   1860 C  CG2 . THR C 1 16  ? 23.758  18.556 28.148 1.00 15.62 ? 16  THR C CG2 1 
ATOM   1861 N  N   . TYR C 1 17  ? 24.388  21.214 30.825 1.00 11.73 ? 17  TYR C N   1 
ATOM   1862 C  CA  . TYR C 1 17  ? 23.647  22.448 30.925 1.00 12.70 ? 17  TYR C CA  1 
ATOM   1863 C  C   . TYR C 1 17  ? 24.272  23.508 31.798 1.00 12.30 ? 17  TYR C C   1 
ATOM   1864 O  O   . TYR C 1 17  ? 23.825  24.673 31.824 1.00 14.14 ? 17  TYR C O   1 
ATOM   1865 C  CB  . TYR C 1 17  ? 22.196  22.146 31.407 1.00 16.08 ? 17  TYR C CB  1 
ATOM   1866 C  CG  . TYR C 1 17  ? 21.489  21.166 30.479 1.00 16.15 ? 17  TYR C CG  1 
ATOM   1867 C  CD1 . TYR C 1 17  ? 21.249  21.509 29.144 1.00 20.78 ? 17  TYR C CD1 1 
ATOM   1868 C  CD2 . TYR C 1 17  ? 21.056  19.937 30.922 1.00 19.16 ? 17  TYR C CD2 1 
ATOM   1869 C  CE1 . TYR C 1 17  ? 20.621  20.614 28.309 1.00 23.62 ? 17  TYR C CE1 1 
ATOM   1870 C  CE2 . TYR C 1 17  ? 20.396  19.049 30.092 1.00 22.16 ? 17  TYR C CE2 1 
ATOM   1871 C  CZ  . TYR C 1 17  ? 20.170  19.401 28.786 1.00 23.99 ? 17  TYR C CZ  1 
ATOM   1872 O  OH  . TYR C 1 17  ? 19.512  18.518 27.941 1.00 31.42 ? 17  TYR C OH  1 
ATOM   1873 N  N   . HIS C 1 18  ? 25.317  23.173 32.546 1.00 12.28 ? 18  HIS C N   1 
ATOM   1874 C  CA  . HIS C 1 18  ? 26.160  24.110 33.214 1.00 12.30 ? 18  HIS C CA  1 
ATOM   1875 C  C   . HIS C 1 18  ? 25.558  24.813 34.388 1.00 12.62 ? 18  HIS C C   1 
ATOM   1876 O  O   . HIS C 1 18  ? 25.890  25.972 34.710 1.00 14.82 ? 18  HIS C O   1 
ATOM   1877 C  CB  . HIS C 1 18  ? 26.787  25.124 32.214 1.00 11.67 ? 18  HIS C CB  1 
ATOM   1878 C  CG  . HIS C 1 18  ? 27.328  24.434 31.002 1.00 11.72 ? 18  HIS C CG  1 
ATOM   1879 N  ND1 . HIS C 1 18  ? 26.924  24.722 29.739 1.00 10.77 ? 18  HIS C ND1 1 
ATOM   1880 C  CD2 . HIS C 1 18  ? 28.048  23.284 30.920 1.00 12.56 ? 18  HIS C CD2 1 
ATOM   1881 C  CE1 . HIS C 1 18  ? 27.454  23.843 28.898 1.00 12.10 ? 18  HIS C CE1 1 
ATOM   1882 N  NE2 . HIS C 1 18  ? 28.165  22.962 29.587 1.00 12.32 ? 18  HIS C NE2 1 
ATOM   1883 N  N   . LYS C 1 19  ? 24.642  24.130 35.040 1.00 14.73 ? 19  LYS C N   1 
ATOM   1884 C  CA  . LYS C 1 19  ? 23.929  24.589 36.215 1.00 15.83 ? 19  LYS C CA  1 
ATOM   1885 C  C   . LYS C 1 19  ? 23.349  23.359 36.925 1.00 13.17 ? 19  LYS C C   1 
ATOM   1886 O  O   . LYS C 1 19  ? 23.255  22.299 36.314 1.00 14.03 ? 19  LYS C O   1 
ATOM   1887 C  CB  . LYS C 1 19  ? 22.818  25.569 35.849 1.00 18.45 ? 19  LYS C CB  1 
ATOM   1888 C  CG  . LYS C 1 19  ? 21.668  24.995 35.043 1.00 22.21 ? 19  LYS C CG  1 
ATOM   1889 C  CD  . LYS C 1 19  ? 20.733  26.091 34.490 1.00 22.53 ? 19  LYS C CD  1 
ATOM   1890 C  CE  . LYS C 1 19  ? 19.632  25.445 33.668 1.00 25.38 ? 19  LYS C CE  1 
ATOM   1891 N  NZ  . LYS C 1 19  ? 18.403  26.238 33.502 1.00 32.91 ? 19  LYS C NZ  1 
ATOM   1892 N  N   . LEU C 1 20  ? 22.988  23.496 38.178 1.00 12.82 ? 20  LEU C N   1 
ATOM   1893 C  CA  . LEU C 1 20  ? 22.263  22.435 38.864 1.00 14.15 ? 20  LEU C CA  1 
ATOM   1894 C  C   . LEU C 1 20  ? 20.821  22.356 38.392 1.00 15.16 ? 20  LEU C C   1 
ATOM   1895 O  O   . LEU C 1 20  ? 20.221  23.381 37.998 1.00 16.80 ? 20  LEU C O   1 
ATOM   1896 C  CB  . LEU C 1 20  ? 22.298  22.664 40.379 1.00 14.27 ? 20  LEU C CB  1 
ATOM   1897 C  CG  . LEU C 1 20  ? 23.633  22.376 41.073 1.00 14.06 ? 20  LEU C CG  1 
ATOM   1898 C  CD1 . LEU C 1 20  ? 23.589  22.871 42.520 1.00 18.44 ? 20  LEU C CD1 1 
ATOM   1899 C  CD2 . LEU C 1 20  ? 23.908  20.864 41.088 1.00 15.14 ? 20  LEU C CD2 1 
ATOM   1900 N  N   . PRO C 1 21  ? 20.222  21.183 38.539 1.00 15.36 ? 21  PRO C N   1 
ATOM   1901 C  CA  . PRO C 1 21  ? 18.774  21.040 38.308 1.00 17.20 ? 21  PRO C CA  1 
ATOM   1902 C  C   . PRO C 1 21  ? 17.962  21.883 39.290 1.00 17.45 ? 21  PRO C C   1 
ATOM   1903 O  O   . PRO C 1 21  ? 18.445  22.296 40.336 1.00 17.49 ? 21  PRO C O   1 
ATOM   1904 C  CB  . PRO C 1 21  ? 18.517  19.575 38.541 1.00 19.86 ? 21  PRO C CB  1 
ATOM   1905 C  CG  . PRO C 1 21  ? 19.816  18.876 38.509 1.00 19.20 ? 21  PRO C CG  1 
ATOM   1906 C  CD  . PRO C 1 21  ? 20.839  19.887 38.881 1.00 17.03 ? 21  PRO C CD  1 
ATOM   1907 N  N   . ASP C 1 22  ? 16.679  22.025 38.976 1.00 20.28 ? 22  ASP C N   1 
ATOM   1908 C  CA  . ASP C 1 22  ? 15.750  22.910 39.567 1.00 20.54 ? 22  ASP C CA  1 
ATOM   1909 C  C   . ASP C 1 22  ? 15.373  22.605 41.007 1.00 23.28 ? 22  ASP C C   1 
ATOM   1910 O  O   . ASP C 1 22  ? 14.791  23.441 41.678 1.00 26.16 ? 22  ASP C O   1 
ATOM   1911 C  CB  . ASP C 1 22  ? 14.477  23.040 38.721 1.00 20.67 ? 22  ASP C CB  1 
ATOM   1912 C  CG  . ASP C 1 22  ? 14.745  23.493 37.311 1.00 26.40 ? 22  ASP C CG  1 
ATOM   1913 O  OD1 . ASP C 1 22  ? 15.667  24.349 37.108 1.00 34.24 ? 22  ASP C OD1 1 
ATOM   1914 O  OD2 . ASP C 1 22  ? 14.019  23.101 36.381 1.00 36.82 ? 22  ASP C OD2 1 
ATOM   1915 N  N   . ASN C 1 23  ? 15.730  21.421 41.462 1.00 21.49 ? 23  ASN C N   1 
ATOM   1916 C  CA  . ASN C 1 23  ? 15.420  20.971 42.790 1.00 20.93 ? 23  ASN C CA  1 
ATOM   1917 C  C   . ASN C 1 23  ? 16.477  21.347 43.820 1.00 20.78 ? 23  ASN C C   1 
ATOM   1918 O  O   . ASN C 1 23  ? 16.292  20.999 44.993 1.00 22.29 ? 23  ASN C O   1 
ATOM   1919 C  CB  . ASN C 1 23  ? 15.129  19.474 42.829 1.00 22.01 ? 23  ASN C CB  1 
ATOM   1920 C  CG  . ASN C 1 23  ? 16.221  18.631 42.220 1.00 22.09 ? 23  ASN C CG  1 
ATOM   1921 O  OD1 . ASN C 1 23  ? 16.334  18.580 40.975 1.00 24.39 ? 23  ASN C OD1 1 
ATOM   1922 N  ND2 . ASN C 1 23  ? 16.949  17.880 42.998 1.00 23.81 ? 23  ASN C ND2 1 
ATOM   1923 N  N   . TYR C 1 24  ? 17.481  22.117 43.488 1.00 19.11 ? 24  TYR C N   1 
ATOM   1924 C  CA  . TYR C 1 24  ? 18.539  22.487 44.414 1.00 15.87 ? 24  TYR C CA  1 
ATOM   1925 C  C   . TYR C 1 24  ? 18.433  23.925 44.895 1.00 17.49 ? 24  TYR C C   1 
ATOM   1926 O  O   . TYR C 1 24  ? 18.059  24.841 44.144 1.00 21.81 ? 24  TYR C O   1 
ATOM   1927 C  CB  . TYR C 1 24  ? 19.928  22.287 43.735 1.00 14.87 ? 24  TYR C CB  1 
ATOM   1928 C  CG  . TYR C 1 24  ? 20.354  20.835 43.755 1.00 13.51 ? 24  TYR C CG  1 
ATOM   1929 C  CD1 . TYR C 1 24  ? 20.901  20.240 44.879 1.00 14.39 ? 24  TYR C CD1 1 
ATOM   1930 C  CD2 . TYR C 1 24  ? 20.104  20.044 42.633 1.00 15.33 ? 24  TYR C CD2 1 
ATOM   1931 C  CE1 . TYR C 1 24  ? 21.224  18.886 44.889 1.00 13.93 ? 24  TYR C CE1 1 
ATOM   1932 C  CE2 . TYR C 1 24  ? 20.397  18.700 42.648 1.00 14.08 ? 24  TYR C CE2 1 
ATOM   1933 C  CZ  . TYR C 1 24  ? 21.006  18.137 43.757 1.00 14.02 ? 24  TYR C CZ  1 
ATOM   1934 O  OH  . TYR C 1 24  ? 21.315  16.802 43.732 1.00 14.49 ? 24  TYR C OH  1 
ATOM   1935 N  N   . ILE C 1 25  ? 18.702  24.127 46.177 1.00 18.54 ? 25  ILE C N   1 
ATOM   1936 C  CA  . ILE C 1 25  ? 18.739  25.462 46.790 1.00 17.61 ? 25  ILE C CA  1 
ATOM   1937 C  C   . ILE C 1 25  ? 20.011  25.565 47.636 1.00 17.17 ? 25  ILE C C   1 
ATOM   1938 O  O   . ILE C 1 25  ? 20.483  24.545 48.163 1.00 17.50 ? 25  ILE C O   1 
ATOM   1939 C  CB  . ILE C 1 25  ? 17.511  25.744 47.679 1.00 18.39 ? 25  ILE C CB  1 
ATOM   1940 C  CG1 . ILE C 1 25  ? 17.235  24.700 48.745 1.00 21.58 ? 25  ILE C CG1 1 
ATOM   1941 C  CG2 . ILE C 1 25  ? 16.301  26.001 46.804 1.00 19.92 ? 25  ILE C CG2 1 
ATOM   1942 C  CD1 . ILE C 1 25  ? 16.072  25.053 49.678 1.00 21.89 ? 25  ILE C CD1 1 
ATOM   1943 N  N   . THR C 1 26  ? 20.594  26.753 47.701 1.00 17.97 ? 26  THR C N   1 
ATOM   1944 C  CA  . THR C 1 26  ? 21.779  26.957 48.512 1.00 18.09 ? 26  THR C CA  1 
ATOM   1945 C  C   . THR C 1 26  ? 21.449  26.946 50.004 1.00 18.90 ? 26  THR C C   1 
ATOM   1946 O  O   . THR C 1 26  ? 20.328  27.120 50.410 1.00 18.98 ? 26  THR C O   1 
ATOM   1947 C  CB  . THR C 1 26  ? 22.493  28.268 48.193 1.00 21.25 ? 26  THR C CB  1 
ATOM   1948 O  OG1 . THR C 1 26  ? 21.668  29.373 48.547 1.00 22.79 ? 26  THR C OG1 1 
ATOM   1949 C  CG2 . THR C 1 26  ? 22.864  28.369 46.736 1.00 23.39 ? 26  THR C CG2 1 
ATOM   1950 N  N   . LYS C 1 27  ? 22.506  26.803 50.832 1.00 19.67 ? 27  LYS C N   1 
ATOM   1951 C  CA  . LYS C 1 27  ? 22.314  26.823 52.277 1.00 22.56 ? 27  LYS C CA  1 
ATOM   1952 C  C   . LYS C 1 27  ? 21.649  28.110 52.737 1.00 22.56 ? 27  LYS C C   1 
ATOM   1953 O  O   . LYS C 1 27  ? 20.763  28.107 53.587 1.00 22.72 ? 27  LYS C O   1 
ATOM   1954 C  CB  . LYS C 1 27  ? 23.639  26.636 53.022 1.00 22.24 ? 27  LYS C CB  1 
ATOM   1955 C  CG  . LYS C 1 27  ? 24.131  25.197 53.074 1.00 24.37 ? 27  LYS C CG  1 
ATOM   1956 C  CD  . LYS C 1 27  ? 25.520  25.079 53.715 1.00 25.64 ? 27  LYS C CD  1 
ATOM   1957 C  CE  . LYS C 1 27  ? 26.592  24.921 52.657 1.00 27.88 ? 27  LYS C CE  1 
ATOM   1958 N  NZ  . LYS C 1 27  ? 27.973  25.068 53.135 1.00 36.22 ? 27  LYS C NZ  1 
ATOM   1959 N  N   . SER C 1 28  ? 22.077  29.238 52.195 1.00 23.44 ? 28  SER C N   1 
ATOM   1960 C  CA  . SER C 1 28  ? 21.506  30.521 52.675 1.00 26.61 ? 28  SER C CA  1 
ATOM   1961 C  C   . SER C 1 28  ? 20.080  30.668 52.210 1.00 26.09 ? 28  SER C C   1 
ATOM   1962 O  O   . SER C 1 28  ? 19.219  31.175 52.950 1.00 26.24 ? 28  SER C O   1 
ATOM   1963 C  CB  . SER C 1 28  ? 22.409  31.649 52.152 1.00 27.96 ? 28  SER C CB  1 
ATOM   1964 O  OG  . SER C 1 28  ? 22.383  31.678 50.754 1.00 38.23 ? 28  SER C OG  1 
ATOM   1965 N  N   . GLU C 1 29  ? 19.746  30.158 51.017 1.00 25.51 ? 29  GLU C N   1 
ATOM   1966 C  CA  . GLU C 1 29  ? 18.344  30.228 50.571 1.00 26.59 ? 29  GLU C CA  1 
ATOM   1967 C  C   . GLU C 1 29  ? 17.467  29.318 51.448 1.00 26.43 ? 29  GLU C C   1 
ATOM   1968 O  O   . GLU C 1 29  ? 16.352  29.702 51.833 1.00 25.08 ? 29  GLU C O   1 
ATOM   1969 C  CB  . GLU C 1 29  ? 18.248  29.741 49.108 1.00 27.56 ? 29  GLU C CB  1 
ATOM   1970 C  CG  . GLU C 1 29  ? 18.805  30.722 48.119 1.00 32.53 ? 29  GLU C CG  1 
ATOM   1971 C  CD  . GLU C 1 29  ? 19.004  30.216 46.721 1.00 37.88 ? 29  GLU C CD  1 
ATOM   1972 O  OE1 . GLU C 1 29  ? 19.008  29.008 46.467 1.00 35.11 ? 29  GLU C OE1 1 
ATOM   1973 O  OE2 . GLU C 1 29  ? 19.198  31.085 45.821 1.00 40.65 ? 29  GLU C OE2 1 
ATOM   1974 N  N   . ALA C 1 30  ? 17.983  28.139 51.751 1.00 23.88 ? 30  ALA C N   1 
ATOM   1975 C  CA  . ALA C 1 30  ? 17.247  27.172 52.569 1.00 21.66 ? 30  ALA C CA  1 
ATOM   1976 C  C   . ALA C 1 30  ? 17.003  27.768 53.946 1.00 22.82 ? 30  ALA C C   1 
ATOM   1977 O  O   . ALA C 1 30  ? 15.899  27.701 54.465 1.00 22.79 ? 30  ALA C O   1 
ATOM   1978 C  CB  . ALA C 1 30  ? 18.006  25.858 52.650 1.00 18.81 ? 30  ALA C CB  1 
ATOM   1979 N  N   . GLN C 1 31  ? 18.035  28.390 54.517 1.00 25.41 ? 31  GLN C N   1 
ATOM   1980 C  CA  . GLN C 1 31  ? 17.851  29.009 55.845 1.00 27.81 ? 31  GLN C CA  1 
ATOM   1981 C  C   . GLN C 1 31  ? 16.779  30.080 55.813 1.00 29.71 ? 31  GLN C C   1 
ATOM   1982 O  O   . GLN C 1 31  ? 15.951  30.164 56.737 1.00 29.50 ? 31  GLN C O   1 
ATOM   1983 C  CB  . GLN C 1 31  ? 19.193  29.583 56.332 1.00 28.16 ? 31  GLN C CB  1 
ATOM   1984 C  CG  . GLN C 1 31  ? 20.139  28.526 56.880 1.00 30.79 ? 31  GLN C CG  1 
ATOM   1985 C  CD  . GLN C 1 31  ? 21.593  28.847 56.728 1.00 37.70 ? 31  GLN C CD  1 
ATOM   1986 O  OE1 . GLN C 1 31  ? 21.978  29.954 56.365 1.00 47.79 ? 31  GLN C OE1 1 
ATOM   1987 N  NE2 . GLN C 1 31  ? 22.462  27.835 56.905 1.00 41.42 ? 31  GLN C NE2 1 
ATOM   1988 N  N   . ALA C 1 32  ? 16.758  30.916 54.783 1.00 29.93 ? 32  ALA C N   1 
ATOM   1989 C  CA  . ALA C 1 32  ? 15.800  32.021 54.729 1.00 31.34 ? 32  ALA C CA  1 
ATOM   1990 C  C   . ALA C 1 32  ? 14.370  31.523 54.611 1.00 31.40 ? 32  ALA C C   1 
ATOM   1991 O  O   . ALA C 1 32  ? 13.413  32.221 54.993 1.00 33.08 ? 32  ALA C O   1 
ATOM   1992 C  CB  . ALA C 1 32  ? 16.140  32.973 53.618 1.00 30.86 ? 32  ALA C CB  1 
ATOM   1993 N  N   . LEU C 1 33  ? 14.212  30.283 54.132 1.00 28.93 ? 33  LEU C N   1 
ATOM   1994 C  CA  . LEU C 1 33  ? 12.908  29.710 53.963 1.00 30.40 ? 33  LEU C CA  1 
ATOM   1995 C  C   . LEU C 1 33  ? 12.455  28.798 55.049 1.00 28.48 ? 33  LEU C C   1 
ATOM   1996 O  O   . LEU C 1 33  ? 11.303  28.300 55.072 1.00 32.85 ? 33  LEU C O   1 
ATOM   1997 C  CB  . LEU C 1 33  ? 12.579  29.245 52.591 1.00 32.58 ? 33  LEU C CB  1 
ATOM   1998 C  CG  . LEU C 1 33  ? 13.258  27.995 52.047 1.00 32.04 ? 33  LEU C CG  1 
ATOM   1999 C  CD1 . LEU C 1 33  ? 12.992  26.795 52.930 1.00 35.19 ? 33  LEU C CD1 1 
ATOM   2000 C  CD2 . LEU C 1 33  ? 12.837  27.763 50.609 1.00 32.24 ? 33  LEU C CD2 1 
ATOM   2001 N  N   . GLY C 1 34  ? 13.284  28.641 56.091 1.00 27.43 ? 34  GLY C N   1 
ATOM   2002 C  CA  . GLY C 1 34  ? 12.859  27.976 57.301 1.00 25.20 ? 34  GLY C CA  1 
ATOM   2003 C  C   . GLY C 1 34  ? 13.684  26.778 57.684 1.00 21.90 ? 34  GLY C C   1 
ATOM   2004 O  O   . GLY C 1 34  ? 13.388  26.147 58.705 1.00 24.06 ? 34  GLY C O   1 
ATOM   2005 N  N   . TRP C 1 35  ? 14.677  26.374 56.882 1.00 21.28 ? 35  TRP C N   1 
ATOM   2006 C  CA  . TRP C 1 35  ? 15.463  25.160 57.202 1.00 19.94 ? 35  TRP C CA  1 
ATOM   2007 C  C   . TRP C 1 35  ? 16.291  25.451 58.481 1.00 20.51 ? 35  TRP C C   1 
ATOM   2008 O  O   . TRP C 1 35  ? 16.995  26.460 58.521 1.00 22.29 ? 35  TRP C O   1 
ATOM   2009 C  CB  . TRP C 1 35  ? 16.476  24.887 56.081 1.00 19.80 ? 35  TRP C CB  1 
ATOM   2010 C  CG  . TRP C 1 35  ? 17.431  23.763 56.352 1.00 18.07 ? 35  TRP C CG  1 
ATOM   2011 C  CD1 . TRP C 1 35  ? 17.109  22.517 56.789 1.00 18.16 ? 35  TRP C CD1 1 
ATOM   2012 C  CD2 . TRP C 1 35  ? 18.854  23.770 56.185 1.00 17.21 ? 35  TRP C CD2 1 
ATOM   2013 N  NE1 . TRP C 1 35  ? 18.223  21.747 56.932 1.00 17.24 ? 35  TRP C NE1 1 
ATOM   2014 C  CE2 . TRP C 1 35  ? 19.318  22.487 56.550 1.00 15.53 ? 35  TRP C CE2 1 
ATOM   2015 C  CE3 . TRP C 1 35  ? 19.786  24.719 55.764 1.00 17.94 ? 35  TRP C CE3 1 
ATOM   2016 C  CZ2 . TRP C 1 35  ? 20.667  22.137 56.519 1.00 17.52 ? 35  TRP C CZ2 1 
ATOM   2017 C  CZ3 . TRP C 1 35  ? 21.128  24.359 55.725 1.00 18.07 ? 35  TRP C CZ3 1 
ATOM   2018 C  CH2 . TRP C 1 35  ? 21.549  23.076 56.082 1.00 17.26 ? 35  TRP C CH2 1 
ATOM   2019 N  N   . VAL C 1 36  ? 16.212  24.542 59.403 1.00 20.59 ? 36  VAL C N   1 
ATOM   2020 C  CA  . VAL C 1 36  ? 16.988  24.586 60.658 1.00 21.01 ? 36  VAL C CA  1 
ATOM   2021 C  C   . VAL C 1 36  ? 17.755  23.253 60.744 1.00 19.97 ? 36  VAL C C   1 
ATOM   2022 O  O   . VAL C 1 36  ? 17.168  22.184 60.888 1.00 19.11 ? 36  VAL C O   1 
ATOM   2023 C  CB  . VAL C 1 36  ? 16.047  24.746 61.852 1.00 20.72 ? 36  VAL C CB  1 
ATOM   2024 C  CG1 . VAL C 1 36  ? 16.787  24.761 63.162 1.00 22.12 ? 36  VAL C CG1 1 
ATOM   2025 C  CG2 . VAL C 1 36  ? 15.128  25.931 61.688 1.00 22.35 ? 36  VAL C CG2 1 
ATOM   2026 N  N   . ALA C 1 37  ? 19.047  23.317 60.422 1.00 18.69 ? 37  ALA C N   1 
ATOM   2027 C  CA  . ALA C 1 37  ? 19.837  22.102 60.273 1.00 17.92 ? 37  ALA C CA  1 
ATOM   2028 C  C   . ALA C 1 37  ? 19.666  21.145 61.452 1.00 16.99 ? 37  ALA C C   1 
ATOM   2029 O  O   . ALA C 1 37  ? 19.593  19.926 61.268 1.00 15.94 ? 37  ALA C O   1 
ATOM   2030 C  CB  . ALA C 1 37  ? 21.335  22.472 60.173 1.00 19.79 ? 37  ALA C CB  1 
ATOM   2031 N  N   . SER C 1 38  ? 19.718  21.677 62.675 1.00 16.18 ? 38  SER C N   1 
ATOM   2032 C  CA  . SER C 1 38  ? 19.689  20.863 63.873 1.00 17.99 ? 38  SER C CA  1 
ATOM   2033 C  C   . SER C 1 38  ? 18.346  20.194 64.106 1.00 17.83 ? 38  SER C C   1 
ATOM   2034 O  O   . SER C 1 38  ? 18.240  19.263 64.913 1.00 17.64 ? 38  SER C O   1 
ATOM   2035 C  CB  . SER C 1 38  ? 20.118  21.655 65.097 1.00 18.41 ? 38  SER C CB  1 
ATOM   2036 O  OG  . SER C 1 38  ? 21.457  22.054 65.056 1.00 24.05 ? 38  SER C OG  1 
ATOM   2037 N  N   . LYS C 1 39  ? 17.327  20.573 63.357 1.00 18.20 ? 39  LYS C N   1 
ATOM   2038 C  CA  . LYS C 1 39  ? 16.020  19.943 63.434 1.00 18.19 ? 39  LYS C CA  1 
ATOM   2039 C  C   . LYS C 1 39  ? 15.779  18.939 62.313 1.00 17.71 ? 39  LYS C C   1 
ATOM   2040 O  O   . LYS C 1 39  ? 14.758  18.230 62.318 1.00 21.32 ? 39  LYS C O   1 
ATOM   2041 C  CB  . LYS C 1 39  ? 14.918  20.999 63.399 1.00 21.85 ? 39  LYS C CB  1 
ATOM   2042 C  CG  . LYS C 1 39  ? 14.794  21.900 64.598 1.00 24.69 ? 39  LYS C CG  1 
ATOM   2043 C  CD  . LYS C 1 39  ? 13.604  22.838 64.497 0.80 26.53 ? 39  LYS C CD  1 
ATOM   2044 C  CE  . LYS C 1 39  ? 12.458  22.197 63.734 0.00 26.21 ? 39  LYS C CE  1 
ATOM   2045 N  NZ  . LYS C 1 39  ? 11.303  23.125 63.587 0.00 26.33 ? 39  LYS C NZ  1 
ATOM   2046 N  N   . GLY C 1 40  ? 16.681  18.848 61.348 1.00 17.33 ? 40  GLY C N   1 
ATOM   2047 C  CA  . GLY C 1 40  ? 16.518  17.922 60.231 1.00 16.29 ? 40  GLY C CA  1 
ATOM   2048 C  C   . GLY C 1 40  ? 15.212  18.142 59.500 1.00 15.74 ? 40  GLY C C   1 
ATOM   2049 O  O   . GLY C 1 40  ? 14.576  17.180 59.075 1.00 16.89 ? 40  GLY C O   1 
ATOM   2050 N  N   . ASN C 1 41  ? 14.822  19.399 59.272 1.00 16.56 ? 41  ASN C N   1 
ATOM   2051 C  CA  . ASN C 1 41  ? 13.524  19.742 58.756 1.00 16.51 ? 41  ASN C CA  1 
ATOM   2052 C  C   . ASN C 1 41  ? 13.455  20.158 57.316 1.00 16.66 ? 41  ASN C C   1 
ATOM   2053 O  O   . ASN C 1 41  ? 12.440  20.722 56.855 1.00 16.76 ? 41  ASN C O   1 
ATOM   2054 C  CB  . ASN C 1 41  ? 12.856  20.810 59.633 1.00 17.11 ? 41  ASN C CB  1 
ATOM   2055 C  CG  . ASN C 1 41  ? 13.420  22.194 59.411 1.00 19.25 ? 41  ASN C CG  1 
ATOM   2056 O  OD1 . ASN C 1 41  ? 14.543  22.343 58.885 1.00 21.27 ? 41  ASN C OD1 1 
ATOM   2057 N  ND2 . ASN C 1 41  ? 12.648  23.208 59.784 1.00 21.49 ? 41  ASN C ND2 1 
ATOM   2058 N  N   . LEU C 1 42  ? 14.480  19.900 56.515 1.00 17.22 ? 42  LEU C N   1 
ATOM   2059 C  CA  . LEU C 1 42  ? 14.454  20.397 55.141 1.00 17.73 ? 42  LEU C CA  1 
ATOM   2060 C  C   . LEU C 1 42  ? 13.243  19.985 54.368 1.00 18.01 ? 42  LEU C C   1 
ATOM   2061 O  O   . LEU C 1 42  ? 12.620  20.839 53.671 1.00 18.48 ? 42  LEU C O   1 
ATOM   2062 C  CB  . LEU C 1 42  ? 15.768  20.088 54.432 1.00 17.05 ? 42  LEU C CB  1 
ATOM   2063 C  CG  . LEU C 1 42  ? 15.882  20.646 52.998 1.00 18.79 ? 42  LEU C CG  1 
ATOM   2064 C  CD1 . LEU C 1 42  ? 15.923  22.169 53.041 1.00 19.46 ? 42  LEU C CD1 1 
ATOM   2065 C  CD2 . LEU C 1 42  ? 17.187  20.114 52.379 1.00 18.75 ? 42  LEU C CD2 1 
ATOM   2066 N  N   . ALA C 1 43  ? 12.838  18.713 54.423 1.00 19.07 ? 43  ALA C N   1 
ATOM   2067 C  CA  . ALA C 1 43  ? 11.705  18.225 53.665 1.00 22.00 ? 43  ALA C CA  1 
ATOM   2068 C  C   . ALA C 1 43  ? 10.377  18.771 54.185 1.00 22.97 ? 43  ALA C C   1 
ATOM   2069 O  O   . ALA C 1 43  ? 9.358   18.703 53.484 1.00 24.86 ? 43  ALA C O   1 
ATOM   2070 C  CB  . ALA C 1 43  ? 11.644  16.704 53.632 1.00 21.61 ? 43  ALA C CB  1 
ATOM   2071 N  N   . ASP C 1 44  ? 10.370  19.277 55.406 1.00 22.18 ? 44  ASP C N   1 
ATOM   2072 C  CA  . ASP C 1 44  ? 9.168   19.867 55.964 1.00 22.65 ? 44  ASP C CA  1 
ATOM   2073 C  C   . ASP C 1 44  ? 8.940   21.278 55.420 1.00 22.96 ? 44  ASP C C   1 
ATOM   2074 O  O   . ASP C 1 44  ? 7.795   21.640 55.135 1.00 23.66 ? 44  ASP C O   1 
ATOM   2075 C  CB  . ASP C 1 44  ? 9.205   19.905 57.483 1.00 24.71 ? 44  ASP C CB  1 
ATOM   2076 C  CG  . ASP C 1 44  ? 9.318   18.544 58.121 1.00 28.89 ? 44  ASP C CG  1 
ATOM   2077 O  OD1 . ASP C 1 44  ? 8.533   17.640 57.755 1.00 31.85 ? 44  ASP C OD1 1 
ATOM   2078 O  OD2 . ASP C 1 44  ? 10.188  18.357 58.988 1.00 29.15 ? 44  ASP C OD2 1 
ATOM   2079 N  N   . VAL C 1 45  ? 10.014  22.046 55.268 1.00 20.32 ? 45  VAL C N   1 
ATOM   2080 C  CA  . VAL C 1 45  ? 9.926   23.408 54.800 1.00 21.11 ? 45  VAL C CA  1 
ATOM   2081 C  C   . VAL C 1 45  ? 10.112  23.566 53.294 1.00 20.64 ? 45  VAL C C   1 
ATOM   2082 O  O   . VAL C 1 45  ? 9.642   24.533 52.684 1.00 21.15 ? 45  VAL C O   1 
ATOM   2083 C  CB  . VAL C 1 45  ? 10.868  24.355 55.545 1.00 21.30 ? 45  VAL C CB  1 
ATOM   2084 C  CG1 . VAL C 1 45  ? 10.570  24.329 57.037 1.00 21.82 ? 45  VAL C CG1 1 
ATOM   2085 C  CG2 . VAL C 1 45  ? 12.341  23.954 55.317 1.00 22.21 ? 45  VAL C CG2 1 
ATOM   2086 N  N   . ALA C 1 46  ? 10.725  22.582 52.668 1.00 20.56 ? 46  ALA C N   1 
ATOM   2087 C  CA  . ALA C 1 46  ? 10.980  22.587 51.251 1.00 20.70 ? 46  ALA C CA  1 
ATOM   2088 C  C   . ALA C 1 46  ? 10.904  21.198 50.647 1.00 19.79 ? 46  ALA C C   1 
ATOM   2089 O  O   . ALA C 1 46  ? 11.927  20.682 50.167 1.00 20.12 ? 46  ALA C O   1 
ATOM   2090 C  CB  . ALA C 1 46  ? 12.240  23.322 50.877 1.00 22.39 ? 46  ALA C CB  1 
ATOM   2091 N  N   . PRO C 1 47  ? 9.691   20.612 50.678 1.00 21.72 ? 47  PRO C N   1 
ATOM   2092 C  CA  . PRO C 1 47  ? 9.530   19.272 50.112 1.00 22.12 ? 47  PRO C CA  1 
ATOM   2093 C  C   . PRO C 1 47  ? 10.101  19.214 48.691 1.00 23.57 ? 47  PRO C C   1 
ATOM   2094 O  O   . PRO C 1 47  ? 9.838   20.087 47.858 1.00 25.16 ? 47  PRO C O   1 
ATOM   2095 C  CB  . PRO C 1 47  ? 8.048   19.009 50.105 1.00 23.10 ? 47  PRO C CB  1 
ATOM   2096 C  CG  . PRO C 1 47  ? 7.438   20.006 51.006 1.00 22.13 ? 47  PRO C CG  1 
ATOM   2097 C  CD  . PRO C 1 47  ? 8.396   21.127 51.175 1.00 22.40 ? 47  PRO C CD  1 
ATOM   2098 N  N   . GLY C 1 48  ? 10.805  18.128 48.407 1.00 21.62 ? 48  GLY C N   1 
ATOM   2099 C  CA  . GLY C 1 48  ? 11.388  17.919 47.112 1.00 22.82 ? 48  GLY C CA  1 
ATOM   2100 C  C   . GLY C 1 48  ? 12.681  18.623 46.846 1.00 22.48 ? 48  GLY C C   1 
ATOM   2101 O  O   . GLY C 1 48  ? 13.283  18.361 45.773 1.00 27.01 ? 48  GLY C O   1 
ATOM   2102 N  N   . LYS C 1 49  ? 13.146  19.519 47.706 1.00 20.37 ? 49  LYS C N   1 
ATOM   2103 C  CA  . LYS C 1 49  ? 14.367  20.261 47.513 1.00 18.04 ? 49  LYS C CA  1 
ATOM   2104 C  C   . LYS C 1 49  ? 15.575  19.616 48.197 1.00 17.60 ? 49  LYS C C   1 
ATOM   2105 O  O   . LYS C 1 49  ? 15.416  18.889 49.178 1.00 17.97 ? 49  LYS C O   1 
ATOM   2106 C  CB  A LYS C 1 49  ? 14.236  21.726 47.882 0.50 21.89 ? 49  LYS C CB  1 
ATOM   2107 C  CB  B LYS C 1 49  ? 14.243  21.707 48.015 0.50 21.78 ? 49  LYS C CB  1 
ATOM   2108 C  CG  A LYS C 1 49  ? 13.097  22.462 47.197 0.50 21.81 ? 49  LYS C CG  1 
ATOM   2109 C  CG  B LYS C 1 49  ? 13.052  22.473 47.511 0.50 21.85 ? 49  LYS C CG  1 
ATOM   2110 C  CD  A LYS C 1 49  ? 13.290  22.553 45.698 0.50 23.90 ? 49  LYS C CD  1 
ATOM   2111 C  CD  B LYS C 1 49  ? 13.008  22.596 46.011 0.50 22.33 ? 49  LYS C CD  1 
ATOM   2112 C  CE  A LYS C 1 49  ? 12.269  23.508 45.073 0.50 24.06 ? 49  LYS C CE  1 
ATOM   2113 C  CE  B LYS C 1 49  ? 11.725  23.290 45.550 0.50 22.30 ? 49  LYS C CE  1 
ATOM   2114 N  NZ  A LYS C 1 49  ? 11.741  23.034 43.785 0.50 23.33 ? 49  LYS C NZ  1 
ATOM   2115 N  NZ  B LYS C 1 49  ? 10.570  22.370 45.584 0.50 23.83 ? 49  LYS C NZ  1 
ATOM   2116 N  N   . SER C 1 50  ? 16.757  19.845 47.653 1.00 15.12 ? 50  SER C N   1 
ATOM   2117 C  CA  . SER C 1 50  ? 18.024  19.417 48.241 1.00 14.17 ? 50  SER C CA  1 
ATOM   2118 C  C   . SER C 1 50  ? 18.991  20.617 48.312 1.00 14.32 ? 50  SER C C   1 
ATOM   2119 O  O   . SER C 1 50  ? 18.915  21.541 47.497 1.00 15.89 ? 50  SER C O   1 
ATOM   2120 C  CB  . SER C 1 50  ? 18.694  18.347 47.354 1.00 16.07 ? 50  SER C CB  1 
ATOM   2121 O  OG  . SER C 1 50  ? 17.965  17.137 47.354 1.00 15.66 ? 50  SER C OG  1 
ATOM   2122 N  N   . ILE C 1 51  ? 19.899  20.560 49.260 1.00 13.99 ? 51  ILE C N   1 
ATOM   2123 C  CA  . ILE C 1 51  ? 20.930  21.607 49.381 1.00 13.77 ? 51  ILE C CA  1 
ATOM   2124 C  C   . ILE C 1 51  ? 21.992  21.406 48.295 1.00 13.56 ? 51  ILE C C   1 
ATOM   2125 O  O   . ILE C 1 51  ? 22.483  20.276 48.098 1.00 13.21 ? 51  ILE C O   1 
ATOM   2126 C  CB  . ILE C 1 51  ? 21.619  21.533 50.757 1.00 15.35 ? 51  ILE C CB  1 
ATOM   2127 C  CG1 . ILE C 1 51  ? 20.696  21.736 51.956 1.00 15.71 ? 51  ILE C CG1 1 
ATOM   2128 C  CG2 . ILE C 1 51  ? 22.830  22.450 50.816 1.00 16.48 ? 51  ILE C CG2 1 
ATOM   2129 C  CD1 . ILE C 1 51  ? 20.002  23.043 51.999 1.00 17.76 ? 51  ILE C CD1 1 
ATOM   2130 N  N   . GLY C 1 52  ? 22.330  22.462 47.580 1.00 13.78 ? 52  GLY C N   1 
ATOM   2131 C  CA  . GLY C 1 52  ? 23.441  22.410 46.627 1.00 13.48 ? 52  GLY C CA  1 
ATOM   2132 C  C   . GLY C 1 52  ? 23.739  23.768 46.030 1.00 12.60 ? 52  GLY C C   1 
ATOM   2133 O  O   . GLY C 1 52  ? 22.881  24.638 46.012 1.00 14.20 ? 52  GLY C O   1 
ATOM   2134 N  N   . GLY C 1 53  ? 24.959  23.907 45.498 1.00 12.48 ? 53  GLY C N   1 
ATOM   2135 C  CA  . GLY C 1 53  ? 25.413  25.065 44.815 1.00 13.65 ? 53  GLY C CA  1 
ATOM   2136 C  C   . GLY C 1 53  ? 26.389  25.935 45.574 1.00 14.60 ? 53  GLY C C   1 
ATOM   2137 O  O   . GLY C 1 53  ? 26.873  26.931 44.989 1.00 17.19 ? 53  GLY C O   1 
ATOM   2138 N  N   . ASP C 1 54  ? 26.729  25.604 46.812 1.00 13.32 ? 54  ASP C N   1 
ATOM   2139 C  CA  . ASP C 1 54  ? 27.647  26.420 47.599 1.00 14.02 ? 54  ASP C CA  1 
ATOM   2140 C  C   . ASP C 1 54  ? 29.110  26.120 47.254 1.00 15.02 ? 54  ASP C C   1 
ATOM   2141 O  O   . ASP C 1 54  ? 29.471  25.026 46.865 1.00 14.05 ? 54  ASP C O   1 
ATOM   2142 C  CB  . ASP C 1 54  ? 27.432  26.187 49.098 1.00 16.31 ? 54  ASP C CB  1 
ATOM   2143 C  CG  . ASP C 1 54  ? 26.092  26.749 49.568 1.00 15.57 ? 54  ASP C CG  1 
ATOM   2144 O  OD1 . ASP C 1 54  ? 25.935  27.979 49.420 1.00 26.40 ? 54  ASP C OD1 1 
ATOM   2145 O  OD2 . ASP C 1 54  ? 25.253  25.998 50.033 1.00 18.76 ? 54  ASP C OD2 1 
ATOM   2146 N  N   . ILE C 1 55  ? 29.950  27.118 47.391 1.00 16.10 ? 55  ILE C N   1 
ATOM   2147 C  CA  . ILE C 1 55  ? 31.415  26.908 47.196 1.00 15.74 ? 55  ILE C CA  1 
ATOM   2148 C  C   . ILE C 1 55  ? 31.950  25.988 48.291 1.00 15.05 ? 55  ILE C C   1 
ATOM   2149 O  O   . ILE C 1 55  ? 31.495  26.106 49.424 1.00 16.69 ? 55  ILE C O   1 
ATOM   2150 C  CB  . ILE C 1 55  ? 32.088  28.313 47.341 1.00 21.69 ? 55  ILE C CB  1 
ATOM   2151 C  CG1 . ILE C 1 55  ? 31.659  29.188 46.146 1.00 23.67 ? 55  ILE C CG1 1 
ATOM   2152 C  CG2 . ILE C 1 55  ? 33.598  28.170 47.380 1.00 23.93 ? 55  ILE C CG2 1 
ATOM   2153 C  CD1 . ILE C 1 55  ? 32.284  30.535 46.169 1.00 30.05 ? 55  ILE C CD1 1 
ATOM   2154 N  N   . PHE C 1 56  ? 32.812  25.080 47.897 1.00 15.61 ? 56  PHE C N   1 
ATOM   2155 C  CA  . PHE C 1 56  ? 33.541  24.173 48.783 1.00 15.60 ? 56  PHE C CA  1 
ATOM   2156 C  C   . PHE C 1 56  ? 35.022  24.613 48.788 1.00 16.39 ? 56  PHE C C   1 
ATOM   2157 O  O   . PHE C 1 56  ? 35.632  24.712 47.735 1.00 19.92 ? 56  PHE C O   1 
ATOM   2158 C  CB  . PHE C 1 56  ? 33.481  22.749 48.226 1.00 14.54 ? 56  PHE C CB  1 
ATOM   2159 C  CG  . PHE C 1 56  ? 34.150  21.700 49.091 1.00 15.41 ? 56  PHE C CG  1 
ATOM   2160 C  CD1 . PHE C 1 56  ? 33.535  21.230 50.236 1.00 17.84 ? 56  PHE C CD1 1 
ATOM   2161 C  CD2 . PHE C 1 56  ? 35.374  21.162 48.737 1.00 17.11 ? 56  PHE C CD2 1 
ATOM   2162 C  CE1 . PHE C 1 56  ? 34.130  20.268 51.022 1.00 18.90 ? 56  PHE C CE1 1 
ATOM   2163 C  CE2 . PHE C 1 56  ? 36.003  20.239 49.541 1.00 18.06 ? 56  PHE C CE2 1 
ATOM   2164 C  CZ  . PHE C 1 56  ? 35.387  19.790 50.690 1.00 20.10 ? 56  PHE C CZ  1 
ATOM   2165 N  N   . SER C 1 57  ? 35.565  24.818 49.980 1.00 17.61 ? 57  SER C N   1 
ATOM   2166 C  CA  . SER C 1 57  ? 36.892  25.374 50.132 1.00 20.13 ? 57  SER C CA  1 
ATOM   2167 C  C   . SER C 1 57  ? 38.058  24.506 49.761 1.00 23.00 ? 57  SER C C   1 
ATOM   2168 O  O   . SER C 1 57  ? 39.156  25.022 49.448 1.00 26.82 ? 57  SER C O   1 
ATOM   2169 C  CB  . SER C 1 57  ? 37.061  26.030 51.497 1.00 25.31 ? 57  SER C CB  1 
ATOM   2170 O  OG  . SER C 1 57  ? 37.728  25.205 52.409 1.00 29.03 ? 57  SER C OG  1 
ATOM   2171 N  N   . ASN C 1 58  ? 37.980  23.190 49.867 1.00 22.49 ? 58  ASN C N   1 
ATOM   2172 C  CA  . ASN C 1 58  ? 39.116  22.338 49.544 1.00 20.42 ? 58  ASN C CA  1 
ATOM   2173 C  C   . ASN C 1 58  ? 40.356  22.658 50.362 1.00 19.84 ? 58  ASN C C   1 
ATOM   2174 O  O   . ASN C 1 58  ? 41.482  22.489 49.885 1.00 20.39 ? 58  ASN C O   1 
ATOM   2175 C  CB  . ASN C 1 58  ? 39.436  22.360 48.054 1.00 23.04 ? 58  ASN C CB  1 
ATOM   2176 C  CG  . ASN C 1 58  ? 40.258  21.168 47.604 1.00 21.43 ? 58  ASN C CG  1 
ATOM   2177 O  OD1 . ASN C 1 58  ? 40.151  20.074 48.157 1.00 20.13 ? 58  ASN C OD1 1 
ATOM   2178 N  ND2 . ASN C 1 58  ? 41.048  21.341 46.541 1.00 22.90 ? 58  ASN C ND2 1 
ATOM   2179 N  N   . ARG C 1 59  ? 40.174  23.033 51.615 1.00 20.51 ? 59  ARG C N   1 
ATOM   2180 C  CA  . ARG C 1 59  ? 41.288  23.373 52.500 1.00 20.85 ? 59  ARG C CA  1 
ATOM   2181 C  C   . ARG C 1 59  ? 42.212  22.222 52.798 1.00 20.47 ? 59  ARG C C   1 
ATOM   2182 O  O   . ARG C 1 59  ? 43.413  22.425 53.040 1.00 22.68 ? 59  ARG C O   1 
ATOM   2183 C  CB  . ARG C 1 59  ? 40.698  24.010 53.786 1.00 22.27 ? 59  ARG C CB  1 
ATOM   2184 C  CG  . ARG C 1 59  ? 40.040  25.357 53.539 0.30 27.21 ? 59  ARG C CG  1 
ATOM   2185 C  CD  . ARG C 1 59  ? 39.373  25.954 54.743 0.80 27.08 ? 59  ARG C CD  1 
ATOM   2186 N  NE  . ARG C 1 59  ? 38.326  26.932 54.406 0.80 30.53 ? 59  ARG C NE  1 
ATOM   2187 C  CZ  . ARG C 1 59  ? 37.667  27.682 55.274 0.80 30.96 ? 59  ARG C CZ  1 
ATOM   2188 N  NH1 . ARG C 1 59  ? 37.784  27.419 56.580 0.30 36.83 ? 59  ARG C NH1 1 
ATOM   2189 N  NH2 . ARG C 1 59  ? 36.876  28.677 54.887 0.30 34.53 ? 59  ARG C NH2 1 
ATOM   2190 N  N   . GLU C 1 60  ? 41.715  20.978 52.787 1.00 16.78 ? 60  GLU C N   1 
ATOM   2191 C  CA  . GLU C 1 60  ? 42.542  19.794 53.071 1.00 16.69 ? 60  GLU C CA  1 
ATOM   2192 C  C   . GLU C 1 60  ? 43.300  19.307 51.845 1.00 16.82 ? 60  GLU C C   1 
ATOM   2193 O  O   . GLU C 1 60  ? 44.053  18.336 51.908 1.00 17.28 ? 60  GLU C O   1 
ATOM   2194 C  CB  . GLU C 1 60  ? 41.678  18.652 53.629 1.00 16.33 ? 60  GLU C CB  1 
ATOM   2195 C  CG  . GLU C 1 60  ? 41.111  18.931 55.018 1.00 14.88 ? 60  GLU C CG  1 
ATOM   2196 C  CD  . GLU C 1 60  ? 40.309  17.737 55.525 1.00 15.96 ? 60  GLU C CD  1 
ATOM   2197 O  OE1 . GLU C 1 60  ? 39.134  17.600 55.170 1.00 17.24 ? 60  GLU C OE1 1 
ATOM   2198 O  OE2 . GLU C 1 60  ? 40.886  16.921 56.283 1.00 16.79 ? 60  GLU C OE2 1 
ATOM   2199 N  N   . GLY C 1 61  ? 43.029  19.880 50.671 1.00 17.13 ? 61  GLY C N   1 
ATOM   2200 C  CA  . GLY C 1 61  ? 43.754  19.530 49.464 1.00 18.49 ? 61  GLY C CA  1 
ATOM   2201 C  C   . GLY C 1 61  ? 43.382  18.224 48.834 1.00 17.85 ? 61  GLY C C   1 
ATOM   2202 O  O   . GLY C 1 61  ? 44.110  17.691 47.980 1.00 18.13 ? 61  GLY C O   1 
ATOM   2203 N  N   . LYS C 1 62  ? 42.277  17.599 49.235 1.00 16.63 ? 62  LYS C N   1 
ATOM   2204 C  CA  . LYS C 1 62  ? 41.926  16.277 48.706 1.00 16.85 ? 62  LYS C CA  1 
ATOM   2205 C  C   . LYS C 1 62  ? 41.472  16.308 47.267 1.00 18.43 ? 62  LYS C C   1 
ATOM   2206 O  O   . LYS C 1 62  ? 41.540  15.270 46.585 1.00 21.57 ? 62  LYS C O   1 
ATOM   2207 C  CB  . LYS C 1 62  ? 40.855  15.635 49.605 1.00 15.67 ? 62  LYS C CB  1 
ATOM   2208 C  CG  . LYS C 1 62  ? 41.301  15.522 51.064 1.00 15.69 ? 62  LYS C CG  1 
ATOM   2209 C  CD  . LYS C 1 62  ? 40.251  14.905 51.940 1.00 17.45 ? 62  LYS C CD  1 
ATOM   2210 C  CE  . LYS C 1 62  ? 40.525  15.053 53.416 1.00 16.00 ? 62  LYS C CE  1 
ATOM   2211 N  NZ  . LYS C 1 62  ? 39.423  14.531 54.278 1.00 12.98 ? 62  LYS C NZ  1 
ATOM   2212 N  N   . LEU C 1 63  ? 40.994  17.445 46.771 1.00 17.45 ? 63  LEU C N   1 
ATOM   2213 C  CA  . LEU C 1 63  ? 40.598  17.562 45.353 1.00 17.11 ? 63  LEU C CA  1 
ATOM   2214 C  C   . LEU C 1 63  ? 41.688  18.329 44.572 1.00 18.33 ? 63  LEU C C   1 
ATOM   2215 O  O   . LEU C 1 63  ? 42.376  19.186 45.113 1.00 21.14 ? 63  LEU C O   1 
ATOM   2216 C  CB  . LEU C 1 63  ? 39.288  18.343 45.263 1.00 17.24 ? 63  LEU C CB  1 
ATOM   2217 C  CG  . LEU C 1 63  ? 38.026  17.743 45.876 1.00 18.30 ? 63  LEU C CG  1 
ATOM   2218 C  CD1 . LEU C 1 63  ? 36.934  18.817 45.934 1.00 21.38 ? 63  LEU C CD1 1 
ATOM   2219 C  CD2 . LEU C 1 63  ? 37.515  16.571 45.031 1.00 23.27 ? 63  LEU C CD2 1 
ATOM   2220 N  N   . PRO C 1 64  ? 41.812  18.101 43.269 1.00 19.16 ? 64  PRO C N   1 
ATOM   2221 C  CA  . PRO C 1 64  ? 42.817  18.816 42.459 1.00 20.41 ? 64  PRO C CA  1 
ATOM   2222 C  C   . PRO C 1 64  ? 42.562  20.294 42.311 1.00 21.74 ? 64  PRO C C   1 
ATOM   2223 O  O   . PRO C 1 64  ? 41.482  20.758 41.924 1.00 22.50 ? 64  PRO C O   1 
ATOM   2224 C  CB  . PRO C 1 64  ? 42.799  18.094 41.131 1.00 22.39 ? 64  PRO C CB  1 
ATOM   2225 C  CG  . PRO C 1 64  ? 41.581  17.278 41.089 1.00 22.33 ? 64  PRO C CG  1 
ATOM   2226 C  CD  . PRO C 1 64  ? 41.072  17.104 42.468 1.00 20.16 ? 64  PRO C CD  1 
ATOM   2227 N  N   . GLY C 1 65  ? 43.625  21.114 42.457 1.00 21.12 ? 65  GLY C N   1 
ATOM   2228 C  CA  . GLY C 1 65  ? 43.459  22.561 42.333 1.00 22.13 ? 65  GLY C CA  1 
ATOM   2229 C  C   . GLY C 1 65  ? 44.088  23.166 41.109 1.00 21.09 ? 65  GLY C C   1 
ATOM   2230 O  O   . GLY C 1 65  ? 44.872  22.544 40.416 1.00 21.35 ? 65  GLY C O   1 
ATOM   2231 N  N   . LYS C 1 66  ? 43.677  24.420 40.786 1.00 21.94 ? 66  LYS C N   1 
ATOM   2232 C  CA  . LYS C 1 66  ? 44.269  25.116 39.645 1.00 21.88 ? 66  LYS C CA  1 
ATOM   2233 C  C   . LYS C 1 66  ? 43.973  26.604 39.725 1.00 24.96 ? 66  LYS C C   1 
ATOM   2234 O  O   . LYS C 1 66  ? 42.902  27.000 40.212 1.00 22.93 ? 66  LYS C O   1 
ATOM   2235 C  CB  . LYS C 1 66  ? 43.662  24.545 38.345 1.00 23.86 ? 66  LYS C CB  1 
ATOM   2236 C  CG  . LYS C 1 66  ? 44.080  25.290 37.103 1.00 27.40 ? 66  LYS C CG  1 
ATOM   2237 C  CD  . LYS C 1 66  ? 43.335  24.770 35.866 1.00 34.58 ? 66  LYS C CD  1 
ATOM   2238 C  CE  . LYS C 1 66  ? 43.948  25.349 34.596 0.80 35.38 ? 66  LYS C CE  1 
ATOM   2239 N  NZ  . LYS C 1 66  ? 43.702  24.479 33.411 0.80 37.38 ? 66  LYS C NZ  1 
ATOM   2240 N  N   . SER C 1 67  ? 44.860  27.430 39.181 1.00 28.13 ? 67  SER C N   1 
ATOM   2241 C  CA  . SER C 1 67  ? 44.604  28.896 39.216 1.00 31.50 ? 67  SER C CA  1 
ATOM   2242 C  C   . SER C 1 67  ? 43.216  29.119 38.568 1.00 31.23 ? 67  SER C C   1 
ATOM   2243 O  O   . SER C 1 67  ? 43.031  28.650 37.440 1.00 31.38 ? 67  SER C O   1 
ATOM   2244 C  CB  . SER C 1 67  ? 45.630  29.625 38.339 1.00 33.99 ? 67  SER C CB  1 
ATOM   2245 O  OG  . SER C 1 67  ? 46.949  29.590 38.888 1.00 33.75 ? 67  SER C OG  1 
ATOM   2246 N  N   . GLY C 1 68  ? 42.355  29.847 39.239 1.00 31.32 ? 68  GLY C N   1 
ATOM   2247 C  CA  . GLY C 1 68  ? 41.060  30.254 38.754 1.00 31.35 ? 68  GLY C CA  1 
ATOM   2248 C  C   . GLY C 1 68  ? 39.960  29.238 38.883 1.00 30.51 ? 68  GLY C C   1 
ATOM   2249 O  O   . GLY C 1 68  ? 38.785  29.551 38.574 1.00 33.82 ? 68  GLY C O   1 
ATOM   2250 N  N   . ARG C 1 69  ? 40.262  28.038 39.341 1.00 27.34 ? 69  ARG C N   1 
ATOM   2251 C  CA  . ARG C 1 69  ? 39.287  26.972 39.521 1.00 24.56 ? 69  ARG C CA  1 
ATOM   2252 C  C   . ARG C 1 69  ? 38.577  27.061 40.872 1.00 24.77 ? 69  ARG C C   1 
ATOM   2253 O  O   . ARG C 1 69  ? 39.245  27.147 41.914 1.00 29.17 ? 69  ARG C O   1 
ATOM   2254 C  CB  . ARG C 1 69  ? 39.985  25.586 39.431 1.00 23.70 ? 69  ARG C CB  1 
ATOM   2255 C  CG  . ARG C 1 69  ? 39.009  24.443 39.705 1.00 24.05 ? 69  ARG C CG  1 
ATOM   2256 C  CD  . ARG C 1 69  ? 39.746  23.101 39.644 1.00 24.29 ? 69  ARG C CD  1 
ATOM   2257 N  NE  . ARG C 1 69  ? 39.961  22.711 38.247 1.00 25.21 ? 69  ARG C NE  1 
ATOM   2258 C  CZ  . ARG C 1 69  ? 40.826  21.789 37.869 1.00 24.73 ? 69  ARG C CZ  1 
ATOM   2259 N  NH1 . ARG C 1 69  ? 41.528  21.159 38.786 1.00 26.27 ? 69  ARG C NH1 1 
ATOM   2260 N  NH2 . ARG C 1 69  ? 41.154  21.676 36.583 1.00 27.12 ? 69  ARG C NH2 1 
ATOM   2261 N  N   . THR C 1 70  ? 37.265  27.006 40.823 1.00 24.05 ? 70  THR C N   1 
ATOM   2262 C  CA  . THR C 1 70  ? 36.391  27.019 41.995 1.00 22.06 ? 70  THR C CA  1 
ATOM   2263 C  C   . THR C 1 70  ? 35.669  25.641 42.060 1.00 18.93 ? 70  THR C C   1 
ATOM   2264 O  O   . THR C 1 70  ? 35.300  25.104 41.024 1.00 23.72 ? 70  THR C O   1 
ATOM   2265 C  CB  . THR C 1 70  ? 35.287  28.097 41.806 1.00 25.75 ? 70  THR C CB  1 
ATOM   2266 O  OG1 . THR C 1 70  ? 35.909  29.394 41.767 1.00 30.30 ? 70  THR C OG1 1 
ATOM   2267 C  CG2 . THR C 1 70  ? 34.270  28.066 42.902 1.00 24.74 ? 70  THR C CG2 1 
ATOM   2268 N  N   . TRP C 1 71  ? 35.549  25.115 43.257 1.00 15.84 ? 71  TRP C N   1 
ATOM   2269 C  CA  . TRP C 1 71  ? 34.793  23.895 43.529 1.00 14.65 ? 71  TRP C CA  1 
ATOM   2270 C  C   . TRP C 1 71  ? 33.483  24.278 44.251 1.00 13.87 ? 71  TRP C C   1 
ATOM   2271 O  O   . TRP C 1 71  ? 33.512  25.145 45.128 1.00 15.01 ? 71  TRP C O   1 
ATOM   2272 C  CB  . TRP C 1 71  ? 35.598  22.967 44.446 1.00 14.65 ? 71  TRP C CB  1 
ATOM   2273 C  CG  . TRP C 1 71  ? 36.750  22.282 43.783 1.00 14.69 ? 71  TRP C CG  1 
ATOM   2274 C  CD1 . TRP C 1 71  ? 38.069  22.667 43.757 1.00 15.52 ? 71  TRP C CD1 1 
ATOM   2275 C  CD2 . TRP C 1 71  ? 36.676  21.104 42.961 1.00 15.70 ? 71  TRP C CD2 1 
ATOM   2276 N  NE1 . TRP C 1 71  ? 38.824  21.766 43.049 1.00 15.96 ? 71  TRP C NE1 1 
ATOM   2277 C  CE2 . TRP C 1 71  ? 37.985  20.811 42.527 1.00 16.07 ? 71  TRP C CE2 1 
ATOM   2278 C  CE3 . TRP C 1 71  ? 35.620  20.256 42.588 1.00 16.11 ? 71  TRP C CE3 1 
ATOM   2279 C  CZ2 . TRP C 1 71  ? 38.271  19.718 41.715 1.00 15.79 ? 71  TRP C CZ2 1 
ATOM   2280 C  CZ3 . TRP C 1 71  ? 35.920  19.175 41.790 1.00 15.88 ? 71  TRP C CZ3 1 
ATOM   2281 C  CH2 . TRP C 1 71  ? 37.232  18.918 41.354 1.00 16.71 ? 71  TRP C CH2 1 
ATOM   2282 N  N   . ARG C 1 72  ? 32.421  23.608 43.883 1.00 12.32 ? 72  ARG C N   1 
ATOM   2283 C  CA  . ARG C 1 72  ? 31.123  23.691 44.517 1.00 12.32 ? 72  ARG C CA  1 
ATOM   2284 C  C   . ARG C 1 72  ? 30.602  22.290 44.848 1.00 11.49 ? 72  ARG C C   1 
ATOM   2285 O  O   . ARG C 1 72  ? 31.107  21.299 44.297 1.00 11.55 ? 72  ARG C O   1 
ATOM   2286 C  CB  . ARG C 1 72  ? 30.110  24.438 43.627 1.00 12.82 ? 72  ARG C CB  1 
ATOM   2287 C  CG  . ARG C 1 72  ? 30.444  25.950 43.561 1.00 15.58 ? 72  ARG C CG  1 
ATOM   2288 C  CD  . ARG C 1 72  ? 29.565  26.653 42.556 1.00 16.72 ? 72  ARG C CD  1 
ATOM   2289 N  NE  . ARG C 1 72  ? 29.811  28.043 42.383 1.00 22.61 ? 72  ARG C NE  1 
ATOM   2290 C  CZ  . ARG C 1 72  ? 29.419  29.098 43.055 1.00 23.71 ? 72  ARG C CZ  1 
ATOM   2291 N  NH1 . ARG C 1 72  ? 28.606  29.000 44.105 1.00 25.11 ? 72  ARG C NH1 1 
ATOM   2292 N  NH2 . ARG C 1 72  ? 29.838  30.318 42.692 1.00 29.09 ? 72  ARG C NH2 1 
ATOM   2293 N  N   . GLU C 1 73  ? 29.632  22.191 45.720 1.00 11.28 ? 73  GLU C N   1 
ATOM   2294 C  CA  . GLU C 1 73  ? 29.091  20.905 46.169 1.00 11.45 ? 73  GLU C CA  1 
ATOM   2295 C  C   . GLU C 1 73  ? 27.562  20.862 46.018 1.00 11.42 ? 73  GLU C C   1 
ATOM   2296 O  O   . GLU C 1 73  ? 26.909  21.905 46.020 1.00 11.39 ? 73  GLU C O   1 
ATOM   2297 C  CB  . GLU C 1 73  ? 29.446  20.640 47.624 1.00 11.46 ? 73  GLU C CB  1 
ATOM   2298 C  CG  . GLU C 1 73  ? 29.095  21.732 48.600 1.00 11.90 ? 73  GLU C CG  1 
ATOM   2299 C  CD  . GLU C 1 73  ? 29.113  21.237 50.046 1.00 12.46 ? 73  GLU C CD  1 
ATOM   2300 O  OE1 . GLU C 1 73  ? 28.543  20.166 50.271 1.00 13.57 ? 73  GLU C OE1 1 
ATOM   2301 O  OE2 . GLU C 1 73  ? 29.695  21.905 50.916 1.00 20.13 ? 73  GLU C OE2 1 
ATOM   2302 N  N   . ALA C 1 74  ? 27.041  19.646 45.997 1.00 9.68  ? 74  ALA C N   1 
ATOM   2303 C  CA  . ALA C 1 74  ? 25.582  19.433 46.006 1.00 9.28  ? 74  ALA C CA  1 
ATOM   2304 C  C   . ALA C 1 74  ? 25.267  18.094 46.678 1.00 9.49  ? 74  ALA C C   1 
ATOM   2305 O  O   . ALA C 1 74  ? 26.033  17.133 46.552 1.00 10.10 ? 74  ALA C O   1 
ATOM   2306 C  CB  . ALA C 1 74  ? 24.994  19.496 44.627 1.00 11.04 ? 74  ALA C CB  1 
ATOM   2307 N  N   . ASP C 1 75  ? 24.184  18.061 47.453 1.00 9.60  ? 75  ASP C N   1 
ATOM   2308 C  CA  . ASP C 1 75  ? 23.736  16.850 48.113 1.00 9.27  ? 75  ASP C CA  1 
ATOM   2309 C  C   . ASP C 1 75  ? 23.103  15.853 47.095 1.00 10.98 ? 75  ASP C C   1 
ATOM   2310 O  O   . ASP C 1 75  ? 22.380  16.253 46.217 1.00 11.38 ? 75  ASP C O   1 
ATOM   2311 C  CB  . ASP C 1 75  ? 22.710  17.112 49.194 1.00 9.99  ? 75  ASP C CB  1 
ATOM   2312 C  CG  . ASP C 1 75  ? 23.226  17.821 50.427 1.00 11.22 ? 75  ASP C CG  1 
ATOM   2313 O  OD1 . ASP C 1 75  ? 24.339  18.393 50.381 1.00 11.31 ? 75  ASP C OD1 1 
ATOM   2314 O  OD2 . ASP C 1 75  ? 22.552  17.740 51.458 1.00 11.23 ? 75  ASP C OD2 1 
ATOM   2315 N  N   . ILE C 1 76  ? 23.451  14.583 47.308 1.00 10.30 ? 76  ILE C N   1 
ATOM   2316 C  CA  . ILE C 1 76  ? 22.969  13.488 46.444 1.00 9.98  ? 76  ILE C CA  1 
ATOM   2317 C  C   . ILE C 1 76  ? 22.163  12.504 47.291 1.00 11.54 ? 76  ILE C C   1 
ATOM   2318 O  O   . ILE C 1 76  ? 22.457  12.304 48.463 1.00 11.79 ? 76  ILE C O   1 
ATOM   2319 C  CB  . ILE C 1 76  ? 24.146  12.830 45.734 1.00 10.12 ? 76  ILE C CB  1 
ATOM   2320 C  CG1 . ILE C 1 76  ? 24.891  13.787 44.770 1.00 10.57 ? 76  ILE C CG1 1 
ATOM   2321 C  CG2 . ILE C 1 76  ? 23.776  11.568 44.982 1.00 12.42 ? 76  ILE C CG2 1 
ATOM   2322 C  CD1 . ILE C 1 76  ? 24.039  14.256 43.619 1.00 11.30 ? 76  ILE C CD1 1 
ATOM   2323 N  N   . ASN C 1 77  ? 21.126  11.903 46.707 1.00 12.40 ? 77  ASN C N   1 
ATOM   2324 C  CA  . ASN C 1 77  ? 20.313  10.902 47.341 1.00 14.27 ? 77  ASN C CA  1 
ATOM   2325 C  C   . ASN C 1 77  ? 19.439  11.387 48.469 1.00 14.07 ? 77  ASN C C   1 
ATOM   2326 O  O   . ASN C 1 77  ? 18.932  10.605 49.267 1.00 17.15 ? 77  ASN C O   1 
ATOM   2327 C  CB  . ASN C 1 77  ? 21.119  9.678  47.736 1.00 16.79 ? 77  ASN C CB  1 
ATOM   2328 C  CG  . ASN C 1 77  ? 21.751  8.936  46.585 1.00 16.67 ? 77  ASN C CG  1 
ATOM   2329 O  OD1 . ASN C 1 77  ? 21.173  8.785  45.496 1.00 18.15 ? 77  ASN C OD1 1 
ATOM   2330 N  ND2 . ASN C 1 77  ? 22.976  8.440  46.798 1.00 18.51 ? 77  ASN C ND2 1 
ATOM   2331 N  N   . TYR C 1 78  ? 19.260  12.701 48.613 1.00 13.18 ? 78  TYR C N   1 
ATOM   2332 C  CA  . TYR C 1 78  ? 18.477  13.173 49.766 1.00 13.69 ? 78  TYR C CA  1 
ATOM   2333 C  C   . TYR C 1 78  ? 16.979  13.120 49.453 1.00 14.79 ? 78  TYR C C   1 
ATOM   2334 O  O   . TYR C 1 78  ? 16.551  13.557 48.389 1.00 16.42 ? 78  TYR C O   1 
ATOM   2335 C  CB  . TYR C 1 78  ? 18.875  14.643 50.079 1.00 13.29 ? 78  TYR C CB  1 
ATOM   2336 C  CG  . TYR C 1 78  ? 18.031  15.213 51.196 1.00 12.90 ? 78  TYR C CG  1 
ATOM   2337 C  CD1 . TYR C 1 78  ? 18.306  14.870 52.520 1.00 13.70 ? 78  TYR C CD1 1 
ATOM   2338 C  CD2 . TYR C 1 78  ? 16.941  16.031 50.957 1.00 13.73 ? 78  TYR C CD2 1 
ATOM   2339 C  CE1 . TYR C 1 78  ? 17.521  15.351 53.552 1.00 14.12 ? 78  TYR C CE1 1 
ATOM   2340 C  CE2 . TYR C 1 78  ? 16.160  16.527 51.975 1.00 13.66 ? 78  TYR C CE2 1 
ATOM   2341 C  CZ  . TYR C 1 78  ? 16.477  16.200 53.284 1.00 14.40 ? 78  TYR C CZ  1 
ATOM   2342 O  OH  . TYR C 1 78  ? 15.686  16.637 54.298 1.00 14.85 ? 78  TYR C OH  1 
ATOM   2343 N  N   . THR C 1 79  ? 16.193  12.684 50.435 1.00 16.73 ? 79  THR C N   1 
ATOM   2344 C  CA  . THR C 1 79  ? 14.743  12.655 50.355 1.00 18.90 ? 79  THR C CA  1 
ATOM   2345 C  C   . THR C 1 79  ? 14.104  13.396 51.499 1.00 18.30 ? 79  THR C C   1 
ATOM   2346 O  O   . THR C 1 79  ? 13.294  14.310 51.285 1.00 19.20 ? 79  THR C O   1 
ATOM   2347 C  CB  . THR C 1 79  ? 14.178  11.265 50.152 1.00 22.80 ? 79  THR C CB  1 
ATOM   2348 O  OG1 . THR C 1 79  ? 14.618  10.347 51.140 1.00 28.32 ? 79  THR C OG1 1 
ATOM   2349 C  CG2 . THR C 1 79  ? 14.605  10.678 48.817 1.00 22.36 ? 79  THR C CG2 1 
ATOM   2350 N  N   . SER C 1 80  ? 14.453  13.023 52.741 1.00 18.52 ? 80  SER C N   1 
ATOM   2351 C  CA  . SER C 1 80  ? 13.924  13.692 53.924 1.00 17.50 ? 80  SER C CA  1 
ATOM   2352 C  C   . SER C 1 80  ? 14.844  13.456 55.132 1.00 17.36 ? 80  SER C C   1 
ATOM   2353 O  O   . SER C 1 80  ? 15.679  12.556 55.106 1.00 17.43 ? 80  SER C O   1 
ATOM   2354 C  CB  . SER C 1 80  ? 12.520  13.216 54.267 1.00 18.64 ? 80  SER C CB  1 
ATOM   2355 O  OG  . SER C 1 80  ? 12.458  11.871 54.584 1.00 24.96 ? 80  SER C OG  1 
ATOM   2356 N  N   . GLY C 1 81  ? 14.594  14.224 56.168 1.00 16.56 ? 81  GLY C N   1 
ATOM   2357 C  CA  . GLY C 1 81  ? 15.286  14.144 57.442 1.00 15.20 ? 81  GLY C CA  1 
ATOM   2358 C  C   . GLY C 1 81  ? 16.594  14.916 57.445 1.00 13.16 ? 81  GLY C C   1 
ATOM   2359 O  O   . GLY C 1 81  ? 16.742  15.873 56.717 1.00 13.60 ? 81  GLY C O   1 
ATOM   2360 N  N   . PHE C 1 82  ? 17.530  14.478 58.291 1.00 12.80 ? 82  PHE C N   1 
ATOM   2361 C  CA  . PHE C 1 82  ? 18.847  15.077 58.323 1.00 11.78 ? 82  PHE C CA  1 
ATOM   2362 C  C   . PHE C 1 82  ? 19.559  14.798 57.000 1.00 11.97 ? 82  PHE C C   1 
ATOM   2363 O  O   . PHE C 1 82  ? 19.295  13.810 56.339 1.00 13.23 ? 82  PHE C O   1 
ATOM   2364 C  CB  . PHE C 1 82  ? 19.695  14.546 59.476 1.00 12.17 ? 82  PHE C CB  1 
ATOM   2365 C  CG  . PHE C 1 82  ? 19.213  15.054 60.823 1.00 12.46 ? 82  PHE C CG  1 
ATOM   2366 C  CD1 . PHE C 1 82  ? 19.642  16.260 61.316 1.00 13.27 ? 82  PHE C CD1 1 
ATOM   2367 C  CD2 . PHE C 1 82  ? 18.257  14.325 61.533 1.00 16.27 ? 82  PHE C CD2 1 
ATOM   2368 C  CE1 . PHE C 1 82  ? 19.164  16.720 62.540 1.00 13.91 ? 82  PHE C CE1 1 
ATOM   2369 C  CE2 . PHE C 1 82  ? 17.829  14.752 62.782 1.00 16.74 ? 82  PHE C CE2 1 
ATOM   2370 C  CZ  . PHE C 1 82  ? 18.220  16.007 63.222 1.00 15.40 ? 82  PHE C CZ  1 
ATOM   2371 N  N   . ARG C 1 83  ? 20.468  15.694 56.643 1.00 11.99 ? 83  ARG C N   1 
ATOM   2372 C  CA  . ARG C 1 83  ? 21.278  15.468 55.461 1.00 12.11 ? 83  ARG C CA  1 
ATOM   2373 C  C   . ARG C 1 83  ? 22.101  14.187 55.615 1.00 12.26 ? 83  ARG C C   1 
ATOM   2374 O  O   . ARG C 1 83  ? 22.521  13.824 56.708 1.00 12.63 ? 83  ARG C O   1 
ATOM   2375 C  CB  . ARG C 1 83  ? 22.167  16.674 55.221 1.00 11.46 ? 83  ARG C CB  1 
ATOM   2376 C  CG  . ARG C 1 83  ? 21.424  17.900 54.730 1.00 12.92 ? 83  ARG C CG  1 
ATOM   2377 C  CD  . ARG C 1 83  ? 22.320  19.144 54.789 1.00 13.20 ? 83  ARG C CD  1 
ATOM   2378 N  NE  . ARG C 1 83  ? 23.379  19.110 53.771 1.00 12.59 ? 83  ARG C NE  1 
ATOM   2379 C  CZ  . ARG C 1 83  ? 24.428  19.896 53.713 1.00 12.89 ? 83  ARG C CZ  1 
ATOM   2380 N  NH1 . ARG C 1 83  ? 24.773  20.712 54.718 1.00 13.91 ? 83  ARG C NH1 1 
ATOM   2381 N  NH2 . ARG C 1 83  ? 25.198  19.887 52.620 1.00 14.05 ? 83  ARG C NH2 1 
ATOM   2382 N  N   . ASN C 1 84  ? 22.329  13.508 54.495 1.00 12.24 ? 84  ASN C N   1 
ATOM   2383 C  CA  . ASN C 1 84  ? 23.085  12.269 54.451 1.00 11.96 ? 84  ASN C CA  1 
ATOM   2384 C  C   . ASN C 1 84  ? 24.562  12.533 54.189 1.00 11.63 ? 84  ASN C C   1 
ATOM   2385 O  O   . ASN C 1 84  ? 25.000  13.689 54.361 1.00 12.52 ? 84  ASN C O   1 
ATOM   2386 C  CB  . ASN C 1 84  ? 22.483  11.338 53.402 1.00 12.43 ? 84  ASN C CB  1 
ATOM   2387 C  CG  . ASN C 1 84  ? 22.616  11.864 51.986 1.00 10.95 ? 84  ASN C CG  1 
ATOM   2388 O  OD1 . ASN C 1 84  ? 23.483  12.702 51.730 1.00 12.04 ? 84  ASN C OD1 1 
ATOM   2389 N  ND2 . ASN C 1 84  ? 21.777  11.357 51.080 1.00 15.39 ? 84  ASN C ND2 1 
ATOM   2390 N  N   . SER C 1 85  ? 25.351  11.516 53.877 1.00 11.40 ? 85  SER C N   1 
ATOM   2391 C  CA  . SER C 1 85  ? 26.793  11.611 53.742 1.00 12.12 ? 85  SER C CA  1 
ATOM   2392 C  C   . SER C 1 85  ? 27.261  11.780 52.289 1.00 12.05 ? 85  SER C C   1 
ATOM   2393 O  O   . SER C 1 85  ? 28.478  11.809 52.066 1.00 11.70 ? 85  SER C O   1 
ATOM   2394 C  CB  . SER C 1 85  ? 27.496  10.350 54.298 1.00 12.65 ? 85  SER C CB  1 
ATOM   2395 O  OG  . SER C 1 85  ? 27.048  9.192  53.644 1.00 22.34 ? 85  SER C OG  1 
ATOM   2396 N  N   . ASP C 1 86  ? 26.353  11.873 51.347 1.00 10.98 ? 86  ASP C N   1 
ATOM   2397 C  CA  . ASP C 1 86  ? 26.668  11.800 49.912 1.00 10.15 ? 86  ASP C CA  1 
ATOM   2398 C  C   . ASP C 1 86  ? 26.664  13.192 49.273 1.00 10.43 ? 86  ASP C C   1 
ATOM   2399 O  O   . ASP C 1 86  ? 25.714  13.965 49.411 1.00 9.93  ? 86  ASP C O   1 
ATOM   2400 C  CB  . ASP C 1 86  ? 25.589  10.949 49.207 1.00 11.39 ? 86  ASP C CB  1 
ATOM   2401 C  CG  . ASP C 1 86  ? 25.561  9.515  49.623 1.00 15.61 ? 86  ASP C CG  1 
ATOM   2402 O  OD1 . ASP C 1 86  ? 26.432  9.051  50.372 1.00 16.29 ? 86  ASP C OD1 1 
ATOM   2403 O  OD2 . ASP C 1 86  ? 24.639  8.786  49.194 1.00 18.79 ? 86  ASP C OD2 1 
ATOM   2404 N  N   . ARG C 1 87  ? 27.752  13.492 48.565 1.00 9.35  ? 87  ARG C N   1 
ATOM   2405 C  CA  . ARG C 1 87  ? 27.857  14.780 47.861 1.00 9.78  ? 87  ARG C CA  1 
ATOM   2406 C  C   . ARG C 1 87  ? 28.505  14.564 46.500 1.00 9.22  ? 87  ARG C C   1 
ATOM   2407 O  O   . ARG C 1 87  ? 29.420  13.751 46.346 1.00 10.56 ? 87  ARG C O   1 
ATOM   2408 C  CB  . ARG C 1 87  ? 28.717  15.759 48.659 1.00 8.98  ? 87  ARG C CB  1 
ATOM   2409 C  CG  . ARG C 1 87  ? 28.375  15.877 50.133 1.00 10.35 ? 87  ARG C CG  1 
ATOM   2410 C  CD  . ARG C 1 87  ? 27.204  16.820 50.379 1.00 10.19 ? 87  ARG C CD  1 
ATOM   2411 N  NE  . ARG C 1 87  ? 26.963  16.993 51.838 1.00 10.87 ? 87  ARG C NE  1 
ATOM   2412 C  CZ  . ARG C 1 87  ? 26.207  16.203 52.573 1.00 11.21 ? 87  ARG C CZ  1 
ATOM   2413 N  NH1 . ARG C 1 87  ? 25.462  15.269 51.993 1.00 11.94 ? 87  ARG C NH1 1 
ATOM   2414 N  NH2 . ARG C 1 87  ? 26.054  16.396 53.875 1.00 13.62 ? 87  ARG C NH2 1 
ATOM   2415 N  N   . ILE C 1 88  ? 28.114  15.431 45.578 1.00 9.64  ? 88  ILE C N   1 
ATOM   2416 C  CA  . ILE C 1 88  ? 28.849  15.600 44.331 1.00 11.43 ? 88  ILE C CA  1 
ATOM   2417 C  C   . ILE C 1 88  ? 29.662  16.893 44.415 1.00 9.14  ? 88  ILE C C   1 
ATOM   2418 O  O   . ILE C 1 88  ? 29.162  17.865 44.999 1.00 10.03 ? 88  ILE C O   1 
ATOM   2419 C  CB  . ILE C 1 88  ? 27.915  15.582 43.140 1.00 11.82 ? 88  ILE C CB  1 
ATOM   2420 C  CG1 . ILE C 1 88  ? 28.430  15.097 41.846 1.00 15.16 ? 88  ILE C CG1 1 
ATOM   2421 C  CG2 . ILE C 1 88  ? 26.919  16.707 43.100 1.00 14.70 ? 88  ILE C CG2 1 
ATOM   2422 C  CD1 . ILE C 1 88  ? 27.428  14.865 40.758 1.00 17.13 ? 88  ILE C CD1 1 
ATOM   2423 N  N   . LEU C 1 89  ? 30.910  16.845 43.997 1.00 10.68 ? 89  LEU C N   1 
ATOM   2424 C  CA  . LEU C 1 89  ? 31.802  18.008 43.997 1.00 10.92 ? 89  LEU C CA  1 
ATOM   2425 C  C   . LEU C 1 89  ? 32.103  18.344 42.533 1.00 10.58 ? 89  LEU C C   1 
ATOM   2426 O  O   . LEU C 1 89  ? 32.458  17.411 41.775 1.00 11.96 ? 89  LEU C O   1 
ATOM   2427 C  CB  . LEU C 1 89  ? 33.140  17.691 44.715 1.00 11.77 ? 89  LEU C CB  1 
ATOM   2428 C  CG  . LEU C 1 89  ? 33.142  17.924 46.222 1.00 13.96 ? 89  LEU C CG  1 
ATOM   2429 C  CD1 . LEU C 1 89  ? 33.153  19.380 46.568 1.00 16.44 ? 89  LEU C CD1 1 
ATOM   2430 C  CD2 . LEU C 1 89  ? 32.025  17.167 46.919 1.00 16.91 ? 89  LEU C CD2 1 
ATOM   2431 N  N   . TYR C 1 90  ? 31.830  19.563 42.127 1.00 12.16 ? 90  TYR C N   1 
ATOM   2432 C  CA  . TYR C 1 90  ? 32.017  19.932 40.730 1.00 11.31 ? 90  TYR C CA  1 
ATOM   2433 C  C   . TYR C 1 90  ? 32.858  21.179 40.590 1.00 12.17 ? 90  TYR C C   1 
ATOM   2434 O  O   . TYR C 1 90  ? 32.680  22.159 41.334 1.00 13.58 ? 90  TYR C O   1 
ATOM   2435 C  CB  . TYR C 1 90  ? 30.711  20.025 39.991 1.00 11.81 ? 90  TYR C CB  1 
ATOM   2436 C  CG  . TYR C 1 90  ? 29.715  21.026 40.496 1.00 12.37 ? 90  TYR C CG  1 
ATOM   2437 C  CD1 . TYR C 1 90  ? 28.907  20.756 41.581 1.00 12.61 ? 90  TYR C CD1 1 
ATOM   2438 C  CD2 . TYR C 1 90  ? 29.584  22.270 39.886 1.00 14.00 ? 90  TYR C CD2 1 
ATOM   2439 C  CE1 . TYR C 1 90  ? 27.993  21.651 42.064 1.00 13.28 ? 90  TYR C CE1 1 
ATOM   2440 C  CE2 . TYR C 1 90  ? 28.645  23.187 40.354 1.00 15.24 ? 90  TYR C CE2 1 
ATOM   2441 C  CZ  . TYR C 1 90  ? 27.839  22.863 41.424 1.00 14.62 ? 90  TYR C CZ  1 
ATOM   2442 O  OH  . TYR C 1 90  ? 26.928  23.751 41.914 1.00 16.50 ? 90  TYR C OH  1 
ATOM   2443 N  N   . SER C 1 91  ? 33.778  21.203 39.617 1.00 13.82 ? 91  SER C N   1 
ATOM   2444 C  CA  . SER C 1 91  ? 34.640  22.374 39.445 1.00 17.04 ? 91  SER C CA  1 
ATOM   2445 C  C   . SER C 1 91  ? 34.112  23.296 38.355 1.00 17.64 ? 91  SER C C   1 
ATOM   2446 O  O   . SER C 1 91  ? 33.222  22.915 37.586 1.00 16.38 ? 91  SER C O   1 
ATOM   2447 C  CB  . SER C 1 91  ? 36.061  21.921 39.114 1.00 16.60 ? 91  SER C CB  1 
ATOM   2448 O  OG  . SER C 1 91  ? 36.164  21.416 37.820 1.00 17.94 ? 91  SER C OG  1 
ATOM   2449 N  N   . SER C 1 92  ? 34.629  24.515 38.325 1.00 19.19 ? 92  SER C N   1 
ATOM   2450 C  CA  . SER C 1 92  ? 34.214  25.510 37.346 1.00 21.50 ? 92  SER C CA  1 
ATOM   2451 C  C   . SER C 1 92  ? 34.542  25.081 35.921 1.00 21.63 ? 92  SER C C   1 
ATOM   2452 O  O   . SER C 1 92  ? 33.920  25.557 34.965 1.00 22.06 ? 92  SER C O   1 
ATOM   2453 C  CB  . SER C 1 92  ? 34.789  26.866 37.683 1.00 24.88 ? 92  SER C CB  1 
ATOM   2454 O  OG  . SER C 1 92  ? 36.167  26.754 38.019 1.00 29.39 ? 92  SER C OG  1 
ATOM   2455 N  N   . ASP C 1 93  ? 35.472  24.132 35.814 1.00 21.20 ? 93  ASP C N   1 
ATOM   2456 C  CA  . ASP C 1 93  ? 35.869  23.504 34.592 1.00 21.37 ? 93  ASP C CA  1 
ATOM   2457 C  C   . ASP C 1 93  ? 35.327  22.106 34.408 1.00 20.15 ? 93  ASP C C   1 
ATOM   2458 O  O   . ASP C 1 93  ? 35.669  21.355 33.495 1.00 21.30 ? 93  ASP C O   1 
ATOM   2459 C  CB  . ASP C 1 93  ? 37.340  23.663 34.294 1.00 23.32 ? 93  ASP C CB  1 
ATOM   2460 C  CG  . ASP C 1 93  ? 38.268  23.038 35.300 1.00 23.09 ? 93  ASP C CG  1 
ATOM   2461 O  OD1 . ASP C 1 93  ? 37.848  22.781 36.452 1.00 26.25 ? 93  ASP C OD1 1 
ATOM   2462 O  OD2 . ASP C 1 93  ? 39.458  22.824 34.972 1.00 26.32 ? 93  ASP C OD2 1 
ATOM   2463 N  N   . TRP C 1 94  ? 34.308  21.747 35.198 1.00 18.33 ? 94  TRP C N   1 
ATOM   2464 C  CA  . TRP C 1 94  ? 33.507  20.584 35.029 1.00 17.35 ? 94  TRP C CA  1 
ATOM   2465 C  C   . TRP C 1 94  ? 34.159  19.256 35.260 1.00 17.31 ? 94  TRP C C   1 
ATOM   2466 O  O   . TRP C 1 94  ? 33.705  18.214 34.742 1.00 19.12 ? 94  TRP C O   1 
ATOM   2467 C  CB  . TRP C 1 94  ? 32.641  20.600 33.760 1.00 16.86 ? 94  TRP C CB  1 
ATOM   2468 C  CG  . TRP C 1 94  ? 31.953  21.922 33.581 1.00 17.44 ? 94  TRP C CG  1 
ATOM   2469 C  CD1 . TRP C 1 94  ? 32.227  22.877 32.641 1.00 17.54 ? 94  TRP C CD1 1 
ATOM   2470 C  CD2 . TRP C 1 94  ? 30.915  22.447 34.402 1.00 17.65 ? 94  TRP C CD2 1 
ATOM   2471 N  NE1 . TRP C 1 94  ? 31.394  23.958 32.822 1.00 18.08 ? 94  TRP C NE1 1 
ATOM   2472 C  CE2 . TRP C 1 94  ? 30.595  23.730 33.899 1.00 18.09 ? 94  TRP C CE2 1 
ATOM   2473 C  CE3 . TRP C 1 94  ? 30.224  21.971 35.523 1.00 18.26 ? 94  TRP C CE3 1 
ATOM   2474 C  CZ2 . TRP C 1 94  ? 29.609  24.532 34.477 1.00 18.51 ? 94  TRP C CZ2 1 
ATOM   2475 C  CZ3 . TRP C 1 94  ? 29.259  22.778 36.083 1.00 18.43 ? 94  TRP C CZ3 1 
ATOM   2476 C  CH2 . TRP C 1 94  ? 28.960  24.041 35.560 1.00 18.62 ? 94  TRP C CH2 1 
ATOM   2477 N  N   . LEU C 1 95  ? 35.101  19.198 36.191 1.00 18.09 ? 95  LEU C N   1 
ATOM   2478 C  CA  . LEU C 1 95  ? 35.535  17.872 36.720 1.00 16.39 ? 95  LEU C CA  1 
ATOM   2479 C  C   . LEU C 1 95  ? 34.466  17.498 37.794 1.00 14.20 ? 95  LEU C C   1 
ATOM   2480 O  O   . LEU C 1 95  ? 33.935  18.395 38.454 1.00 15.00 ? 95  LEU C O   1 
ATOM   2481 C  CB  . LEU C 1 95  ? 36.844  18.063 37.483 1.00 19.92 ? 95  LEU C CB  1 
ATOM   2482 C  CG  . LEU C 1 95  ? 38.113  18.312 36.696 1.00 20.72 ? 95  LEU C CG  1 
ATOM   2483 C  CD1 . LEU C 1 95  ? 39.306  18.395 37.633 1.00 25.52 ? 95  LEU C CD1 1 
ATOM   2484 C  CD2 . LEU C 1 95  ? 38.288  17.185 35.677 1.00 22.47 ? 95  LEU C CD2 1 
ATOM   2485 N  N   . ILE C 1 96  ? 34.143  16.234 37.900 1.00 14.17 ? 96  ILE C N   1 
ATOM   2486 C  CA  . ILE C 1 96  ? 33.087  15.803 38.834 1.00 12.22 ? 96  ILE C CA  1 
ATOM   2487 C  C   . ILE C 1 96  ? 33.634  14.652 39.687 1.00 12.38 ? 96  ILE C C   1 
ATOM   2488 O  O   . ILE C 1 96  ? 34.118  13.645 39.186 1.00 12.66 ? 96  ILE C O   1 
ATOM   2489 C  CB  A ILE C 1 96  ? 31.906  15.243 37.984 0.50 12.35 ? 96  ILE C CB  1 
ATOM   2490 C  CB  B ILE C 1 96  ? 31.805  15.381 38.142 0.50 12.85 ? 96  ILE C CB  1 
ATOM   2491 C  CG1 A ILE C 1 96  ? 31.593  16.180 36.780 0.50 12.84 ? 96  ILE C CG1 1 
ATOM   2492 C  CG1 B ILE C 1 96  ? 31.243  16.418 37.157 0.50 12.44 ? 96  ILE C CG1 1 
ATOM   2493 C  CG2 A ILE C 1 96  ? 30.678  15.073 38.848 0.50 14.29 ? 96  ILE C CG2 1 
ATOM   2494 C  CG2 B ILE C 1 96  ? 30.742  14.989 39.172 0.50 14.13 ? 96  ILE C CG2 1 
ATOM   2495 C  CD1 A ILE C 1 96  ? 30.738  17.367 37.214 0.70 15.12 ? 96  ILE C CD1 1 
ATOM   2496 C  CD1 B ILE C 1 96  ? 29.966  16.011 36.487 0.50 13.83 ? 96  ILE C CD1 1 
ATOM   2497 N  N   . TYR C 1 97  ? 33.523  14.807 40.996 1.00 10.66 ? 97  TYR C N   1 
ATOM   2498 C  CA  . TYR C 1 97  ? 33.958  13.811 41.964 1.00 11.20 ? 97  TYR C CA  1 
ATOM   2499 C  C   . TYR C 1 97  ? 32.773  13.505 42.900 1.00 11.27 ? 97  TYR C C   1 
ATOM   2500 O  O   . TYR C 1 97  ? 31.849  14.316 43.043 1.00 12.55 ? 97  TYR C O   1 
ATOM   2501 C  CB  . TYR C 1 97  ? 35.118  14.360 42.822 1.00 13.05 ? 97  TYR C CB  1 
ATOM   2502 C  CG  . TYR C 1 97  ? 36.461  14.312 42.122 1.00 14.17 ? 97  TYR C CG  1 
ATOM   2503 C  CD1 . TYR C 1 97  ? 36.752  15.168 41.057 1.00 15.94 ? 97  TYR C CD1 1 
ATOM   2504 C  CD2 . TYR C 1 97  ? 37.441  13.408 42.493 1.00 15.96 ? 97  TYR C CD2 1 
ATOM   2505 C  CE1 . TYR C 1 97  ? 37.947  15.093 40.387 1.00 17.04 ? 97  TYR C CE1 1 
ATOM   2506 C  CE2 . TYR C 1 97  ? 38.644  13.327 41.829 1.00 17.68 ? 97  TYR C CE2 1 
ATOM   2507 C  CZ  . TYR C 1 97  ? 38.912  14.181 40.784 1.00 18.39 ? 97  TYR C CZ  1 
ATOM   2508 O  OH  . TYR C 1 97  ? 40.128  14.146 40.135 1.00 20.52 ? 97  TYR C OH  1 
ATOM   2509 N  N   . LYS C 1 98  ? 32.838  12.362 43.536 1.00 11.35 ? 98  LYS C N   1 
ATOM   2510 C  CA  . LYS C 1 98  ? 31.821  11.958 44.500 1.00 11.79 ? 98  LYS C CA  1 
ATOM   2511 C  C   . LYS C 1 98  ? 32.499  11.618 45.837 1.00 11.26 ? 98  LYS C C   1 
ATOM   2512 O  O   . LYS C 1 98  ? 33.643  11.173 45.894 1.00 11.53 ? 98  LYS C O   1 
ATOM   2513 C  CB  . LYS C 1 98  ? 31.051  10.771 43.989 1.00 17.01 ? 98  LYS C CB  1 
ATOM   2514 C  CG  . LYS C 1 98  ? 31.377  9.416  44.446 1.00 24.40 ? 98  LYS C CG  1 
ATOM   2515 C  CD  . LYS C 1 98  ? 30.384  8.366  43.992 1.00 24.15 ? 98  LYS C CD  1 
ATOM   2516 C  CE  . LYS C 1 98  ? 31.019  7.087  43.574 1.00 29.00 ? 98  LYS C CE  1 
ATOM   2517 N  NZ  . LYS C 1 98  ? 29.984  6.000  43.421 1.00 39.72 ? 98  LYS C NZ  1 
ATOM   2518 N  N   . THR C 1 99  ? 31.738  11.899 46.893 1.00 10.59 ? 99  THR C N   1 
ATOM   2519 C  CA  . THR C 1 99  ? 32.020  11.438 48.224 1.00 10.12 ? 99  THR C CA  1 
ATOM   2520 C  C   . THR C 1 99  ? 30.756  10.791 48.809 1.00 10.43 ? 99  THR C C   1 
ATOM   2521 O  O   . THR C 1 99  ? 29.657  11.291 48.581 1.00 10.51 ? 99  THR C O   1 
ATOM   2522 C  CB  . THR C 1 99  ? 32.589  12.479 49.157 1.00 10.51 ? 99  THR C CB  1 
ATOM   2523 O  OG1 . THR C 1 99  ? 32.878  11.951 50.456 1.00 11.50 ? 99  THR C OG1 1 
ATOM   2524 C  CG2 . THR C 1 99  ? 31.663  13.650 49.367 1.00 11.67 ? 99  THR C CG2 1 
ATOM   2525 N  N   . THR C 1 100 ? 30.957  9.697  49.524 1.00 10.40 ? 100 THR C N   1 
ATOM   2526 C  CA  . THR C 1 100 ? 29.880  9.053  50.269 1.00 11.52 ? 100 THR C CA  1 
ATOM   2527 C  C   . THR C 1 100 ? 30.170  8.966  51.747 1.00 11.17 ? 100 THR C C   1 
ATOM   2528 O  O   . THR C 1 100 ? 29.525  8.199  52.480 1.00 13.86 ? 100 THR C O   1 
ATOM   2529 C  CB  . THR C 1 100 ? 29.552  7.669  49.707 1.00 14.30 ? 100 THR C CB  1 
ATOM   2530 O  OG1 . THR C 1 100 ? 30.702  6.798  49.792 1.00 19.45 ? 100 THR C OG1 1 
ATOM   2531 C  CG2 . THR C 1 100 ? 29.133  7.765  48.268 1.00 19.32 ? 100 THR C CG2 1 
ATOM   2532 N  N   . ASP C 1 101 ? 31.192  9.681  52.201 1.00 11.66 ? 101 ASP C N   1 
ATOM   2533 C  CA  . ASP C 1 101 ? 31.676  9.602  53.569 1.00 11.37 ? 101 ASP C CA  1 
ATOM   2534 C  C   . ASP C 1 101 ? 32.017  10.973 54.132 1.00 11.00 ? 101 ASP C C   1 
ATOM   2535 O  O   . ASP C 1 101 ? 32.941  11.147 54.894 1.00 11.79 ? 101 ASP C O   1 
ATOM   2536 C  CB  . ASP C 1 101 ? 32.845  8.634  53.665 1.00 11.63 ? 101 ASP C CB  1 
ATOM   2537 C  CG  . ASP C 1 101 ? 34.059  9.037  52.866 1.00 11.91 ? 101 ASP C CG  1 
ATOM   2538 O  OD1 . ASP C 1 101 ? 34.090  10.150 52.296 1.00 11.85 ? 101 ASP C OD1 1 
ATOM   2539 O  OD2 . ASP C 1 101 ? 35.028  8.260  52.822 1.00 13.41 ? 101 ASP C OD2 1 
ATOM   2540 N  N   . HIS C 1 102 ? 31.169  11.970 53.849 1.00 11.25 ? 102 HIS C N   1 
ATOM   2541 C  CA  . HIS C 1 102 ? 31.341  13.296 54.424 1.00 11.08 ? 102 HIS C CA  1 
ATOM   2542 C  C   . HIS C 1 102 ? 32.704  13.890 54.097 1.00 10.40 ? 102 HIS C C   1 
ATOM   2543 O  O   . HIS C 1 102 ? 33.371  14.462 54.954 1.00 11.68 ? 102 HIS C O   1 
ATOM   2544 C  CB  . HIS C 1 102 ? 31.071  13.358 55.908 1.00 13.85 ? 102 HIS C CB  1 
ATOM   2545 C  CG  . HIS C 1 102 ? 29.652  13.278 56.335 1.00 16.25 ? 102 HIS C CG  1 
ATOM   2546 N  ND1 . HIS C 1 102 ? 29.132  12.177 56.946 1.00 19.69 ? 102 HIS C ND1 1 
ATOM   2547 C  CD2 . HIS C 1 102 ? 28.629  14.165 56.276 1.00 18.45 ? 102 HIS C CD2 1 
ATOM   2548 C  CE1 . HIS C 1 102 ? 27.850  12.346 57.223 1.00 20.32 ? 102 HIS C CE1 1 
ATOM   2549 N  NE2 . HIS C 1 102 ? 27.540  13.596 56.825 1.00 20.31 ? 102 HIS C NE2 1 
ATOM   2550 N  N   . TYR C 1 103 ? 33.064  13.886 52.822 1.00 9.70  ? 103 TYR C N   1 
ATOM   2551 C  CA  . TYR C 1 103 ? 34.251  14.621 52.378 1.00 10.30 ? 103 TYR C CA  1 
ATOM   2552 C  C   . TYR C 1 103 ? 35.539  14.025 52.873 1.00 10.24 ? 103 TYR C C   1 
ATOM   2553 O  O   . TYR C 1 103 ? 36.591  14.694 52.800 1.00 11.80 ? 103 TYR C O   1 
ATOM   2554 C  CB  . TYR C 1 103 ? 34.170  16.100 52.685 1.00 10.89 ? 103 TYR C CB  1 
ATOM   2555 C  CG  . TYR C 1 103 ? 32.876  16.836 52.573 1.00 10.84 ? 103 TYR C CG  1 
ATOM   2556 C  CD1 . TYR C 1 103 ? 32.374  17.322 51.373 1.00 10.90 ? 103 TYR C CD1 1 
ATOM   2557 C  CD2 . TYR C 1 103 ? 32.084  17.067 53.708 1.00 11.22 ? 103 TYR C CD2 1 
ATOM   2558 C  CE1 . TYR C 1 103 ? 31.166  18.012 51.305 1.00 11.25 ? 103 TYR C CE1 1 
ATOM   2559 C  CE2 . TYR C 1 103 ? 30.911  17.770 53.652 1.00 11.36 ? 103 TYR C CE2 1 
ATOM   2560 C  CZ  . TYR C 1 103 ? 30.439  18.238 52.440 1.00 11.13 ? 103 TYR C CZ  1 
ATOM   2561 O  OH  . TYR C 1 103 ? 29.227  18.911 52.410 1.00 11.34 ? 103 TYR C OH  1 
ATOM   2562 N  N   . GLN C 1 104 ? 35.546  12.781 53.317 1.00 10.13 ? 104 GLN C N   1 
ATOM   2563 C  CA  . GLN C 1 104 ? 36.759  12.102 53.743 1.00 10.44 ? 104 GLN C CA  1 
ATOM   2564 C  C   . GLN C 1 104 ? 37.555  11.549 52.600 1.00 10.57 ? 104 GLN C C   1 
ATOM   2565 O  O   . GLN C 1 104 ? 38.780  11.721 52.533 1.00 11.21 ? 104 GLN C O   1 
ATOM   2566 C  CB  . GLN C 1 104 ? 36.479  11.042 54.816 1.00 10.85 ? 104 GLN C CB  1 
ATOM   2567 C  CG  . GLN C 1 104 ? 36.089  11.731 56.134 1.00 12.50 ? 104 GLN C CG  1 
ATOM   2568 C  CD  . GLN C 1 104 ? 35.750  10.700 57.207 1.00 14.75 ? 104 GLN C CD  1 
ATOM   2569 O  OE1 . GLN C 1 104 ? 36.451  10.585 58.210 1.00 14.99 ? 104 GLN C OE1 1 
ATOM   2570 N  NE2 . GLN C 1 104 ? 34.675  9.966  56.970 1.00 14.15 ? 104 GLN C NE2 1 
ATOM   2571 N  N   . THR C 1 105 ? 36.867  10.846 51.707 1.00 11.95 ? 105 THR C N   1 
ATOM   2572 C  CA  . THR C 1 105 ? 37.481  10.339 50.490 1.00 12.72 ? 105 THR C CA  1 
ATOM   2573 C  C   . THR C 1 105 ? 36.633  10.732 49.273 1.00 12.67 ? 105 THR C C   1 
ATOM   2574 O  O   . THR C 1 105 ? 35.418  10.958 49.380 1.00 12.82 ? 105 THR C O   1 
ATOM   2575 C  CB  . THR C 1 105 ? 37.651  8.820  50.509 1.00 14.86 ? 105 THR C CB  1 
ATOM   2576 O  OG1 . THR C 1 105 ? 36.376  8.172  50.582 1.00 16.98 ? 105 THR C OG1 1 
ATOM   2577 C  CG2 . THR C 1 105 ? 38.481  8.370  51.696 1.00 15.43 ? 105 THR C CG2 1 
ATOM   2578 N  N   . PHE C 1 106 ? 37.322  10.785 48.123 1.00 13.89 ? 106 PHE C N   1 
ATOM   2579 C  CA  . PHE C 1 106 ? 36.650  11.170 46.898 1.00 15.18 ? 106 PHE C CA  1 
ATOM   2580 C  C   . PHE C 1 106 ? 37.059  10.219 45.760 1.00 15.03 ? 106 PHE C C   1 
ATOM   2581 O  O   . PHE C 1 106 ? 38.209  9.786  45.708 1.00 16.83 ? 106 PHE C O   1 
ATOM   2582 C  CB  . PHE C 1 106 ? 37.034  12.581 46.478 1.00 15.64 ? 106 PHE C CB  1 
ATOM   2583 C  CG  . PHE C 1 106 ? 36.624  13.684 47.424 1.00 15.14 ? 106 PHE C CG  1 
ATOM   2584 C  CD1 . PHE C 1 106 ? 35.386  14.269 47.340 1.00 15.30 ? 106 PHE C CD1 1 
ATOM   2585 C  CD2 . PHE C 1 106 ? 37.505  14.143 48.400 1.00 16.70 ? 106 PHE C CD2 1 
ATOM   2586 C  CE1 . PHE C 1 106 ? 34.993  15.291 48.192 1.00 16.08 ? 106 PHE C CE1 1 
ATOM   2587 C  CE2 . PHE C 1 106 ? 37.141  15.182 49.227 1.00 17.73 ? 106 PHE C CE2 1 
ATOM   2588 C  CZ  . PHE C 1 106 ? 35.879  15.753 49.140 1.00 16.86 ? 106 PHE C CZ  1 
ATOM   2589 N  N   . THR C 1 107 ? 36.150  10.058 44.836 1.00 14.97 ? 107 THR C N   1 
ATOM   2590 C  CA  . THR C 1 107 ? 36.404  9.280  43.608 1.00 14.40 ? 107 THR C CA  1 
ATOM   2591 C  C   . THR C 1 107 ? 35.963  10.132 42.422 1.00 13.92 ? 107 THR C C   1 
ATOM   2592 O  O   . THR C 1 107 ? 34.886  10.721 42.407 1.00 13.70 ? 107 THR C O   1 
ATOM   2593 C  CB  . THR C 1 107 ? 35.474  8.013  43.637 1.00 21.31 ? 107 THR C CB  1 
ATOM   2594 O  OG1 . THR C 1 107 ? 35.742  7.313  44.858 1.00 22.18 ? 107 THR C OG1 1 
ATOM   2595 C  CG2 . THR C 1 107 ? 35.858  7.078  42.494 1.00 24.96 ? 107 THR C CG2 1 
ATOM   2596 N  N   . LYS C 1 108 ? 36.791  10.108 41.373 1.00 14.22 ? 108 LYS C N   1 
ATOM   2597 C  CA  . LYS C 1 108 ? 36.387  10.806 40.142 1.00 14.47 ? 108 LYS C CA  1 
ATOM   2598 C  C   . LYS C 1 108 ? 35.275  9.994  39.464 1.00 13.28 ? 108 LYS C C   1 
ATOM   2599 O  O   . LYS C 1 108 ? 35.395  8.778  39.323 1.00 15.44 ? 108 LYS C O   1 
ATOM   2600 C  CB  . LYS C 1 108 ? 37.615  10.835 39.214 1.00 16.80 ? 108 LYS C CB  1 
ATOM   2601 C  CG  . LYS C 1 108 ? 37.363  11.462 37.865 1.00 19.43 ? 108 LYS C CG  1 
ATOM   2602 C  CD  . LYS C 1 108 ? 38.632  11.389 36.986 1.00 20.84 ? 108 LYS C CD  1 
ATOM   2603 C  CE  . LYS C 1 108 ? 38.387  12.032 35.655 1.00 22.04 ? 108 LYS C CE  1 
ATOM   2604 N  NZ  . LYS C 1 108 ? 37.948  13.457 35.795 1.00 33.94 ? 108 LYS C NZ  1 
ATOM   2605 N  N   . ILE C 1 109 ? 34.247  10.696 39.001 1.00 13.09 ? 109 ILE C N   1 
ATOM   2606 C  CA  . ILE C 1 109 ? 33.143  10.119 38.302 1.00 13.22 ? 109 ILE C CA  1 
ATOM   2607 C  C   . ILE C 1 109 ? 32.874  10.612 36.906 1.00 12.55 ? 109 ILE C C   1 
ATOM   2608 O  O   . ILE C 1 109 ? 32.131  9.986  36.142 1.00 13.41 ? 109 ILE C O   1 
ATOM   2609 C  CB  . ILE C 1 109 ? 31.859  10.003 39.107 1.00 13.70 ? 109 ILE C CB  1 
ATOM   2610 C  CG1 . ILE C 1 109 ? 31.209  11.354 39.434 1.00 13.08 ? 109 ILE C CG1 1 
ATOM   2611 C  CG2 . ILE C 1 109 ? 32.027  9.133  40.331 1.00 14.47 ? 109 ILE C CG2 1 
ATOM   2612 C  CD1 . ILE C 1 109 ? 29.774  11.240 39.866 1.00 16.83 ? 109 ILE C CD1 1 
ATOM   2613 N  N   . ARG C 1 110 ? 33.481  11.720 36.509 1.00 13.75 ? 110 ARG C N   1 
ATOM   2614 C  CA  . ARG C 1 110 ? 33.465  12.268 35.202 1.00 14.11 ? 110 ARG C CA  1 
ATOM   2615 C  C   . ARG C 1 110 ? 34.789  13.062 34.976 1.00 19.46 ? 110 ARG C C   1 
ATOM   2616 O  O   . ARG C 1 110 ? 35.188  13.130 33.803 1.00 19.68 ? 110 ARG C O   1 
ATOM   2617 C  CB  . ARG C 1 110 ? 32.313  13.163 34.846 1.00 14.58 ? 110 ARG C CB  1 
ATOM   2618 C  CG  . ARG C 1 110 ? 30.911  12.700 34.907 1.00 14.60 ? 110 ARG C CG  1 
ATOM   2619 C  CD  . ARG C 1 110 ? 30.517  11.663 33.897 1.00 14.09 ? 110 ARG C CD  1 
ATOM   2620 N  NE  . ARG C 1 110 ? 29.089  11.336 33.982 1.00 16.48 ? 110 ARG C NE  1 
ATOM   2621 C  CZ  . ARG C 1 110 ? 28.586  10.407 34.783 1.00 16.20 ? 110 ARG C CZ  1 
ATOM   2622 N  NH1 . ARG C 1 110 ? 29.338  9.775  35.667 1.00 17.11 ? 110 ARG C NH1 1 
ATOM   2623 N  NH2 . ARG C 1 110 ? 27.269  10.154 34.725 1.00 19.89 ? 110 ARG C NH2 1 
ATOM   2624 O  OXT . ARG C 1 110 ? 35.186  13.726 35.951 1.00 20.92 ? 110 ARG C OXT 1 
HETATM 2625 ZN ZN  . ZN  D 2 .   ? 33.898  42.301 55.562 0.30 41.80 ? 112 ZN  A ZN  1 
HETATM 2626 ZN ZN  . ZN  E 2 .   ? 8.869   30.194 74.011 0.35 32.13 ? 112 ZN  B ZN  1 
HETATM 2627 ZN ZN  . ZN  F 2 .   ? 39.324  15.495 56.124 1.00 12.86 ? 112 ZN  C ZN  1 
HETATM 2628 O  O   . HOH G 3 .   ? 22.075  43.686 37.103 1.00 12.40 ? 113 HOH A O   1 
HETATM 2629 O  O   . HOH G 3 .   ? 30.344  45.360 35.202 1.00 15.19 ? 114 HOH A O   1 
HETATM 2630 O  O   . HOH G 3 .   ? 23.736  45.450 31.979 1.00 12.56 ? 115 HOH A O   1 
HETATM 2631 O  O   . HOH G 3 .   ? 20.156  37.244 27.180 1.00 13.73 ? 116 HOH A O   1 
HETATM 2632 O  O   . HOH G 3 .   ? 24.281  39.654 26.872 1.00 14.36 ? 117 HOH A O   1 
HETATM 2633 O  O   . HOH G 3 .   ? 25.796  41.292 25.354 1.00 15.66 ? 118 HOH A O   1 
HETATM 2634 O  O   . HOH G 3 .   ? 25.460  58.912 34.827 1.00 20.28 ? 119 HOH A O   1 
HETATM 2635 O  O   . HOH G 3 .   ? 21.259  39.055 38.119 1.00 17.67 ? 120 HOH A O   1 
HETATM 2636 O  O   . HOH G 3 .   ? 25.005  41.844 33.184 1.00 14.40 ? 121 HOH A O   1 
HETATM 2637 O  O   . HOH G 3 .   ? 27.190  57.065 52.614 1.00 18.76 ? 122 HOH A O   1 
HETATM 2638 O  O   . HOH G 3 .   ? 32.439  43.504 35.943 1.00 20.07 ? 123 HOH A O   1 
HETATM 2639 O  O   . HOH G 3 .   ? 26.854  43.786 25.914 1.00 21.27 ? 124 HOH A O   1 
HETATM 2640 O  O   . HOH G 3 .   ? 35.162  56.866 32.422 1.00 39.68 ? 125 HOH A O   1 
HETATM 2641 O  O   . HOH G 3 .   ? 29.599  44.007 26.684 1.00 20.40 ? 126 HOH A O   1 
HETATM 2642 O  O   . HOH G 3 .   ? 18.100  43.698 31.036 1.00 20.34 ? 127 HOH A O   1 
HETATM 2643 O  O   . HOH G 3 .   ? 18.047  50.209 40.385 1.00 20.68 ? 128 HOH A O   1 
HETATM 2644 O  O   . HOH G 3 .   ? 38.447  53.103 32.464 1.00 51.01 ? 129 HOH A O   1 
HETATM 2645 O  O   . HOH G 3 .   ? 17.662  51.541 43.534 1.00 24.43 ? 130 HOH A O   1 
HETATM 2646 O  O   . HOH G 3 .   ? 37.506  57.710 34.639 1.00 36.21 ? 131 HOH A O   1 
HETATM 2647 O  O   . HOH G 3 .   ? 36.818  48.003 44.653 1.00 23.60 ? 132 HOH A O   1 
HETATM 2648 O  O   . HOH G 3 .   ? 22.715  30.149 36.521 1.00 40.99 ? 133 HOH A O   1 
HETATM 2649 O  O   . HOH G 3 .   ? 41.094  50.670 39.858 1.00 26.69 ? 134 HOH A O   1 
HETATM 2650 O  O   . HOH G 3 .   ? 19.040  39.392 36.599 1.00 24.01 ? 135 HOH A O   1 
HETATM 2651 O  O   . HOH G 3 .   ? 20.562  44.898 49.885 1.00 38.33 ? 136 HOH A O   1 
HETATM 2652 O  O   . HOH G 3 .   ? 24.619  51.671 52.841 1.00 30.72 ? 137 HOH A O   1 
HETATM 2653 O  O   . HOH G 3 .   ? 28.376  29.874 23.509 1.00 18.34 ? 138 HOH A O   1 
HETATM 2654 O  O   . HOH G 3 .   ? 24.613  62.234 43.882 1.00 24.15 ? 139 HOH A O   1 
HETATM 2655 O  O   . HOH G 3 .   ? 31.464  62.552 36.153 1.00 32.37 ? 140 HOH A O   1 
HETATM 2656 O  O   . HOH G 3 .   ? 32.585  40.486 45.245 1.00 31.53 ? 141 HOH A O   1 
HETATM 2657 O  O   . HOH G 3 .   ? 25.989  53.979 54.203 1.00 37.48 ? 142 HOH A O   1 
HETATM 2658 O  O   . HOH G 3 .   ? 21.070  52.865 53.078 1.00 22.85 ? 143 HOH A O   1 
HETATM 2659 O  O   . HOH G 3 .   ? 21.725  36.320 33.066 1.00 23.83 ? 144 HOH A O   1 
HETATM 2660 O  O   . HOH G 3 .   ? 18.261  55.786 48.154 1.00 22.65 ? 145 HOH A O   1 
HETATM 2661 O  O   . HOH G 3 .   ? 29.962  48.125 28.939 1.00 28.64 ? 146 HOH A O   1 
HETATM 2662 O  O   . HOH G 3 .   ? 37.000  39.111 34.162 1.00 27.16 ? 147 HOH A O   1 
HETATM 2663 O  O   . HOH G 3 .   ? 32.181  32.817 25.159 1.00 20.90 ? 148 HOH A O   1 
HETATM 2664 O  O   . HOH G 3 .   ? 31.818  38.607 40.612 1.00 29.22 ? 149 HOH A O   1 
HETATM 2665 O  O   . HOH G 3 .   ? 34.237  42.610 44.563 1.00 30.72 ? 150 HOH A O   1 
HETATM 2666 O  O   . HOH G 3 .   ? 32.618  45.825 31.846 1.00 29.02 ? 151 HOH A O   1 
HETATM 2667 O  O   . HOH G 3 .   ? 19.676  37.424 34.344 1.00 30.58 ? 152 HOH A O   1 
HETATM 2668 O  O   . HOH G 3 .   ? 18.898  28.703 28.943 1.00 32.81 ? 153 HOH A O   1 
HETATM 2669 O  O   . HOH G 3 .   ? 31.726  37.622 24.942 1.00 24.36 ? 154 HOH A O   1 
HETATM 2670 O  O   . HOH G 3 .   ? 20.157  34.645 40.244 1.00 41.26 ? 155 HOH A O   1 
HETATM 2671 O  O   . HOH G 3 .   ? 19.528  45.059 29.308 1.00 30.55 ? 156 HOH A O   1 
HETATM 2672 O  O   . HOH G 3 .   ? 30.821  55.890 51.549 1.00 31.42 ? 157 HOH A O   1 
HETATM 2673 O  O   . HOH G 3 .   ? 32.951  30.105 34.126 1.00 24.58 ? 158 HOH A O   1 
HETATM 2674 O  O   . HOH G 3 .   ? 24.134  39.882 16.809 1.00 33.08 ? 159 HOH A O   1 
HETATM 2675 O  O   . HOH G 3 .   ? 33.118  40.259 25.697 1.00 39.62 ? 160 HOH A O   1 
HETATM 2676 O  O   . HOH G 3 .   ? 36.127  46.574 33.877 1.00 32.81 ? 161 HOH A O   1 
HETATM 2677 O  O   . HOH G 3 .   ? 42.622  55.192 43.224 1.00 39.26 ? 162 HOH A O   1 
HETATM 2678 O  O   . HOH G 3 .   ? 40.673  60.980 40.830 1.00 79.58 ? 163 HOH A O   1 
HETATM 2679 O  O   . HOH G 3 .   ? 42.102  53.362 38.915 1.00 55.21 ? 164 HOH A O   1 
HETATM 2680 O  O   . HOH G 3 .   ? 38.976  42.323 36.345 1.00 39.80 ? 165 HOH A O   1 
HETATM 2681 O  O   . HOH G 3 .   ? 38.133  49.733 32.675 1.00 41.02 ? 166 HOH A O   1 
HETATM 2682 O  O   . HOH G 3 .   ? 17.725  47.807 31.846 1.00 37.66 ? 167 HOH A O   1 
HETATM 2683 O  O   . HOH G 3 .   ? 24.861  59.568 37.511 1.00 29.62 ? 168 HOH A O   1 
HETATM 2684 O  O   . HOH G 3 .   ? 29.106  37.192 43.135 1.00 37.42 ? 169 HOH A O   1 
HETATM 2685 O  O   . HOH G 3 .   ? 32.509  45.662 28.427 1.00 58.76 ? 170 HOH A O   1 
HETATM 2686 O  O   . HOH G 3 .   ? 34.546  55.332 52.565 1.00 47.89 ? 171 HOH A O   1 
HETATM 2687 O  O   . HOH G 3 .   ? 19.765  54.198 32.252 1.00 38.56 ? 172 HOH A O   1 
HETATM 2688 O  O   . HOH G 3 .   ? 32.033  35.814 40.665 1.00 36.16 ? 173 HOH A O   1 
HETATM 2689 O  O   . HOH G 3 .   ? 35.135  41.851 48.091 1.00 52.99 ? 174 HOH A O   1 
HETATM 2690 O  O   . HOH G 3 .   ? 39.491  45.381 44.719 1.00 67.81 ? 175 HOH A O   1 
HETATM 2691 O  O   . HOH G 3 .   ? 31.414  59.290 51.754 1.00 46.05 ? 176 HOH A O   1 
HETATM 2692 O  O   . HOH G 3 .   ? 35.605  41.168 42.502 1.00 37.55 ? 177 HOH A O   1 
HETATM 2693 O  O   . HOH G 3 .   ? 26.194  30.752 20.668 1.00 43.82 ? 178 HOH A O   1 
HETATM 2694 O  O   . HOH G 3 .   ? 20.601  51.463 30.291 1.00 46.27 ? 179 HOH A O   1 
HETATM 2695 O  O   . HOH G 3 .   ? 41.651  51.114 49.854 1.00 42.99 ? 180 HOH A O   1 
HETATM 2696 O  O   . HOH G 3 .   ? 31.808  38.481 43.395 1.00 41.21 ? 181 HOH A O   1 
HETATM 2697 O  O   . HOH G 3 .   ? 33.517  30.379 39.027 1.00 42.61 ? 182 HOH A O   1 
HETATM 2698 O  O   . HOH G 3 .   ? 17.283  52.784 38.328 1.00 39.81 ? 183 HOH A O   1 
HETATM 2699 O  O   . HOH G 3 .   ? 35.240  43.908 46.517 1.00 41.41 ? 184 HOH A O   1 
HETATM 2700 O  O   . HOH G 3 .   ? 17.734  34.375 33.183 1.00 42.00 ? 185 HOH A O   1 
HETATM 2701 O  O   . HOH G 3 .   ? 17.625  44.856 44.377 1.00 49.50 ? 186 HOH A O   1 
HETATM 2702 O  O   . HOH G 3 .   ? 37.033  35.626 37.079 1.00 38.42 ? 187 HOH A O   1 
HETATM 2703 O  O   . HOH G 3 .   ? 28.552  37.160 16.948 1.00 49.96 ? 188 HOH A O   1 
HETATM 2704 O  O   . HOH G 3 .   ? 17.975  37.168 37.582 1.00 60.75 ? 189 HOH A O   1 
HETATM 2705 O  O   . HOH G 3 .   ? 37.684  39.820 38.331 1.00 46.19 ? 190 HOH A O   1 
HETATM 2706 O  O   . HOH G 3 .   ? 37.392  62.667 40.882 1.00 49.76 ? 191 HOH A O   1 
HETATM 2707 O  O   . HOH G 3 .   ? 30.300  38.584 54.042 1.00 55.74 ? 192 HOH A O   1 
HETATM 2708 O  O   . HOH G 3 .   ? 16.847  32.349 28.817 1.00 51.42 ? 193 HOH A O   1 
HETATM 2709 O  O   . HOH G 3 .   ? 21.411  35.109 21.283 1.00 26.17 ? 194 HOH A O   1 
HETATM 2710 O  O   . HOH G 3 .   ? 29.001  64.283 37.636 1.00 26.44 ? 195 HOH A O   1 
HETATM 2711 O  O   . HOH G 3 .   ? 18.005  35.794 26.129 1.00 28.97 ? 196 HOH A O   1 
HETATM 2712 O  O   . HOH G 3 .   ? 30.230  41.047 15.992 1.00 34.65 ? 197 HOH A O   1 
HETATM 2713 O  O   . HOH G 3 .   ? 37.321  33.010 30.226 1.00 31.57 ? 198 HOH A O   1 
HETATM 2714 O  O   . HOH G 3 .   ? 22.559  60.429 41.641 1.00 35.04 ? 199 HOH A O   1 
HETATM 2715 O  O   . HOH G 3 .   ? 33.040  60.087 47.731 1.00 30.29 ? 200 HOH A O   1 
HETATM 2716 O  O   . HOH G 3 .   ? 15.453  49.310 44.930 1.00 47.89 ? 201 HOH A O   1 
HETATM 2717 O  O   . HOH G 3 .   ? 16.124  46.332 38.572 1.00 33.34 ? 202 HOH A O   1 
HETATM 2718 O  O   . HOH G 3 .   ? 35.784  53.091 54.575 1.00 40.23 ? 203 HOH A O   1 
HETATM 2719 O  O   . HOH G 3 .   ? 36.054  30.123 26.540 1.00 42.98 ? 204 HOH A O   1 
HETATM 2720 O  O   . HOH G 3 .   ? 13.367  38.604 31.292 1.00 57.94 ? 205 HOH A O   1 
HETATM 2721 O  O   . HOH G 3 .   ? 43.320  49.326 39.344 1.00 39.18 ? 206 HOH A O   1 
HETATM 2722 O  O   . HOH G 3 .   ? 20.422  58.444 42.640 1.00 45.82 ? 207 HOH A O   1 
HETATM 2723 O  O   . HOH G 3 .   ? 23.879  36.866 47.601 1.00 45.77 ? 208 HOH A O   1 
HETATM 2724 O  O   . HOH G 3 .   ? 18.076  51.888 50.745 1.00 45.24 ? 209 HOH A O   1 
HETATM 2725 O  O   . HOH G 3 .   ? 38.863  60.310 48.377 1.00 57.58 ? 210 HOH A O   1 
HETATM 2726 O  O   . HOH G 3 .   ? 23.998  31.739 22.075 1.00 32.88 ? 211 HOH A O   1 
HETATM 2727 O  O   . HOH G 3 .   ? 28.245  33.605 41.319 1.00 50.53 ? 212 HOH A O   1 
HETATM 2728 O  O   . HOH G 3 .   ? 20.683  38.143 44.457 1.00 45.73 ? 213 HOH A O   1 
HETATM 2729 O  O   . HOH G 3 .   ? 20.237  35.822 43.644 1.00 55.03 ? 214 HOH A O   1 
HETATM 2730 O  O   . HOH G 3 .   ? 32.774  37.498 22.209 1.00 45.63 ? 215 HOH A O   1 
HETATM 2731 O  O   . HOH G 3 .   ? 15.409  44.088 37.608 1.00 57.61 ? 216 HOH A O   1 
HETATM 2732 O  O   . HOH G 3 .   ? 28.902  44.049 58.286 1.00 46.81 ? 217 HOH A O   1 
HETATM 2733 O  O   . HOH G 3 .   ? 26.664  47.857 27.300 1.00 38.07 ? 218 HOH A O   1 
HETATM 2734 O  O   . HOH G 3 .   ? 32.346  48.034 29.443 1.00 55.19 ? 219 HOH A O   1 
HETATM 2735 O  O   . HOH G 3 .   ? 20.790  50.642 55.199 1.00 48.68 ? 220 HOH A O   1 
HETATM 2736 O  O   . HOH G 3 .   ? 32.759  63.600 33.967 1.00 63.47 ? 221 HOH A O   1 
HETATM 2737 O  O   . HOH G 3 .   ? 20.394  46.818 26.416 1.00 38.14 ? 222 HOH A O   1 
HETATM 2738 O  O   . HOH G 3 .   ? 41.489  55.117 51.655 1.00 44.05 ? 223 HOH A O   1 
HETATM 2739 O  O   . HOH G 3 .   ? 50.992  57.054 49.113 1.00 50.60 ? 224 HOH A O   1 
HETATM 2740 O  O   . HOH G 3 .   ? 22.269  33.475 41.523 1.00 46.13 ? 225 HOH A O   1 
HETATM 2741 O  O   . HOH G 3 .   ? 35.674  34.966 41.283 1.00 60.45 ? 226 HOH A O   1 
HETATM 2742 O  O   . HOH G 3 .   ? 36.080  42.635 55.143 0.30 27.39 ? 227 HOH A O   1 
HETATM 2743 O  O   . HOH G 3 .   ? 38.778  46.413 50.965 1.00 46.29 ? 228 HOH A O   1 
HETATM 2744 O  O   . HOH G 3 .   ? 21.927  56.920 29.038 1.00 68.89 ? 229 HOH A O   1 
HETATM 2745 O  O   . HOH G 3 .   ? 41.527  45.114 46.600 1.00 58.26 ? 230 HOH A O   1 
HETATM 2746 O  O   . HOH G 3 .   ? 32.810  57.017 53.309 1.00 44.90 ? 231 HOH A O   1 
HETATM 2747 O  O   . HOH G 3 .   ? 40.269  40.837 40.239 1.00 55.46 ? 232 HOH A O   1 
HETATM 2748 O  O   . HOH G 3 .   ? 18.606  53.644 35.436 1.00 46.84 ? 233 HOH A O   1 
HETATM 2749 O  O   . HOH G 3 .   ? 36.031  46.610 46.877 1.00 40.22 ? 234 HOH A O   1 
HETATM 2750 O  O   . HOH G 3 .   ? 42.034  55.770 40.707 1.00 40.44 ? 235 HOH A O   1 
HETATM 2751 O  O   . HOH G 3 .   ? 25.037  61.897 29.641 1.00 48.74 ? 236 HOH A O   1 
HETATM 2752 O  O   . HOH G 3 .   ? 24.036  60.482 33.006 1.00 53.36 ? 237 HOH A O   1 
HETATM 2753 O  O   . HOH G 3 .   ? 31.323  37.706 18.151 1.00 40.40 ? 238 HOH A O   1 
HETATM 2754 O  O   . HOH G 3 .   ? 34.990  38.861 41.649 1.00 52.49 ? 239 HOH A O   1 
HETATM 2755 O  O   . HOH G 3 .   ? 16.275  36.693 32.772 1.00 40.12 ? 240 HOH A O   1 
HETATM 2756 O  O   . HOH G 3 .   ? 17.296  54.323 40.415 1.00 63.60 ? 241 HOH A O   1 
HETATM 2757 O  O   . HOH G 3 .   ? 17.452  29.661 26.963 1.00 58.00 ? 242 HOH A O   1 
HETATM 2758 O  O   . HOH G 3 .   ? 34.461  49.201 31.835 1.00 46.31 ? 243 HOH A O   1 
HETATM 2759 O  O   . HOH G 3 .   ? 13.781  38.715 34.562 1.00 54.52 ? 244 HOH A O   1 
HETATM 2760 O  O   . HOH G 3 .   ? 35.523  30.077 35.036 1.00 39.47 ? 245 HOH A O   1 
HETATM 2761 O  O   . HOH G 3 .   ? 36.350  27.694 33.186 1.00 42.93 ? 246 HOH A O   1 
HETATM 2762 O  O   . HOH H 3 .   ? -10.066 34.208 63.981 1.00 13.30 ? 137 HOH B O   1 
HETATM 2763 O  O   . HOH H 3 .   ? -2.867  38.264 66.549 1.00 13.90 ? 138 HOH B O   1 
HETATM 2764 O  O   . HOH H 3 .   ? -8.050  33.793 69.257 1.00 12.64 ? 139 HOH B O   1 
HETATM 2765 O  O   . HOH H 3 .   ? -16.429 37.383 73.557 1.00 16.30 ? 140 HOH B O   1 
HETATM 2766 O  O   . HOH H 3 .   ? -11.489 38.370 74.186 1.00 15.52 ? 141 HOH B O   1 
HETATM 2767 O  O   . HOH H 3 .   ? -9.375  37.879 75.949 1.00 14.66 ? 142 HOH B O   1 
HETATM 2768 O  O   . HOH H 3 .   ? 1.973   24.589 66.897 1.00 20.00 ? 143 HOH B O   1 
HETATM 2769 O  O   . HOH H 3 .   ? -13.559 37.216 62.821 1.00 15.81 ? 144 HOH B O   1 
HETATM 2770 O  O   . HOH H 3 .   ? -9.351  37.277 68.204 1.00 12.56 ? 145 HOH B O   1 
HETATM 2771 O  O   . HOH H 3 .   ? 7.782   26.899 75.769 1.00 61.43 ? 146 HOH B O   1 
HETATM 2772 O  O   . HOH H 3 .   ? -2.373  41.046 66.168 1.00 20.69 ? 147 HOH B O   1 
HETATM 2773 O  O   . HOH H 3 .   ? -18.260 45.113 79.660 1.00 33.01 ? 148 HOH B O   1 
HETATM 2774 O  O   . HOH H 3 .   ? 8.158   31.976 69.855 1.00 40.69 ? 149 HOH B O   1 
HETATM 2775 O  O   . HOH H 3 .   ? -8.532  44.538 83.195 1.00 41.50 ? 150 HOH B O   1 
HETATM 2776 O  O   . HOH H 3 .   ? -4.753  38.556 74.998 1.00 19.36 ? 151 HOH B O   1 
HETATM 2777 O  O   . HOH H 3 .   ? -4.157  27.081 48.507 1.00 19.49 ? 152 HOH B O   1 
HETATM 2778 O  O   . HOH H 3 .   ? -8.547  26.754 60.594 1.00 22.39 ? 153 HOH B O   1 
HETATM 2779 O  O   . HOH H 3 .   ? -6.951  36.726 75.591 1.00 21.80 ? 154 HOH B O   1 
HETATM 2780 O  O   . HOH H 3 .   ? 10.206  33.213 68.009 1.00 32.19 ? 155 HOH B O   1 
HETATM 2781 O  O   . HOH H 3 .   ? 4.516   40.913 57.928 1.00 21.75 ? 156 HOH B O   1 
HETATM 2782 O  O   . HOH H 3 .   ? -7.684  44.690 76.868 1.00 25.72 ? 157 HOH B O   1 
HETATM 2783 O  O   . HOH H 3 .   ? 3.244   28.176 48.840 1.00 23.80 ? 158 HOH B O   1 
HETATM 2784 O  O   . HOH H 3 .   ? -15.123 35.288 64.156 1.00 27.58 ? 159 HOH B O   1 
HETATM 2785 O  O   . HOH H 3 .   ? -7.779  25.654 57.381 1.00 24.19 ? 160 HOH B O   1 
HETATM 2786 O  O   . HOH H 3 .   ? -1.936  35.676 72.815 1.00 30.28 ? 161 HOH B O   1 
HETATM 2787 O  O   . HOH H 3 .   ? -7.589  43.170 80.559 1.00 19.64 ? 162 HOH B O   1 
HETATM 2788 O  O   . HOH H 3 .   ? 9.076   41.300 63.233 1.00 24.82 ? 163 HOH B O   1 
HETATM 2789 O  O   . HOH H 3 .   ? -0.870  39.149 70.453 1.00 26.64 ? 164 HOH B O   1 
HETATM 2790 O  O   . HOH H 3 .   ? -10.931 51.249 67.193 1.00 24.53 ? 165 HOH B O   1 
HETATM 2791 O  O   . HOH H 3 .   ? 7.373   23.261 59.250 1.00 23.71 ? 166 HOH B O   1 
HETATM 2792 O  O   . HOH H 3 .   ? 5.760   22.224 57.168 1.00 28.36 ? 167 HOH B O   1 
HETATM 2793 O  O   . HOH H 3 .   ? -1.632  30.355 48.856 1.00 27.98 ? 168 HOH B O   1 
HETATM 2794 O  O   . HOH H 3 .   ? -15.714 39.361 67.886 1.00 26.87 ? 169 HOH B O   1 
HETATM 2795 O  O   . HOH H 3 .   ? 2.143   30.348 47.316 1.00 30.17 ? 170 HOH B O   1 
HETATM 2796 O  O   . HOH H 3 .   ? -12.221 31.260 72.372 1.00 27.50 ? 171 HOH B O   1 
HETATM 2797 O  O   . HOH H 3 .   ? -3.564  41.023 44.523 1.00 39.74 ? 172 HOH B O   1 
HETATM 2798 O  O   . HOH H 3 .   ? -10.107 48.468 76.740 1.00 33.74 ? 173 HOH B O   1 
HETATM 2799 O  O   . HOH H 3 .   ? -3.702  43.923 57.093 1.00 26.25 ? 174 HOH B O   1 
HETATM 2800 O  O   . HOH H 3 .   ? -5.872  44.497 61.312 1.00 28.20 ? 175 HOH B O   1 
HETATM 2801 O  O   . HOH H 3 .   ? 5.736   39.675 69.992 1.00 34.27 ? 176 HOH B O   1 
HETATM 2802 O  O   . HOH H 3 .   ? -16.189 37.235 66.460 1.00 27.53 ? 177 HOH B O   1 
HETATM 2803 O  O   . HOH H 3 .   ? -6.970  47.114 61.413 1.00 34.15 ? 178 HOH B O   1 
HETATM 2804 O  O   . HOH H 3 .   ? -9.285  33.015 51.106 1.00 29.92 ? 179 HOH B O   1 
HETATM 2805 O  O   . HOH H 3 .   ? 8.813   25.376 66.212 1.00 32.34 ? 180 HOH B O   1 
HETATM 2806 O  O   . HOH H 3 .   ? 1.734   23.875 64.152 1.00 33.85 ? 181 HOH B O   1 
HETATM 2807 O  O   . HOH H 3 .   ? 8.121   37.981 69.622 1.00 41.77 ? 182 HOH B O   1 
HETATM 2808 O  O   . HOH H 3 .   ? 2.082   41.161 68.622 1.00 33.44 ? 183 HOH B O   1 
HETATM 2809 O  O   . HOH H 3 .   ? -5.120  43.857 76.030 1.00 29.28 ? 184 HOH B O   1 
HETATM 2810 O  O   . HOH H 3 .   ? 5.518   31.071 50.376 1.00 33.62 ? 185 HOH B O   1 
HETATM 2811 O  O   . HOH H 3 .   ? -16.388 46.132 78.066 1.00 33.85 ? 186 HOH B O   1 
HETATM 2812 O  O   . HOH H 3 .   ? -14.320 29.001 67.726 1.00 30.82 ? 187 HOH B O   1 
HETATM 2813 O  O   . HOH H 3 .   ? -0.948  43.298 57.896 1.00 29.19 ? 188 HOH B O   1 
HETATM 2814 O  O   . HOH H 3 .   ? -17.367 38.136 79.076 1.00 31.66 ? 189 HOH B O   1 
HETATM 2815 O  O   . HOH H 3 .   ? -8.654  26.274 68.361 1.00 34.41 ? 190 HOH B O   1 
HETATM 2816 O  O   . HOH H 3 .   ? -19.020 36.901 74.191 1.00 35.98 ? 191 HOH B O   1 
HETATM 2817 O  O   . HOH H 3 .   ? -8.239  44.179 58.673 1.00 31.90 ? 192 HOH B O   1 
HETATM 2818 O  O   . HOH H 3 .   ? -12.517 40.924 53.807 1.00 38.30 ? 193 HOH B O   1 
HETATM 2819 O  O   . HOH H 3 .   ? -14.568 53.541 70.669 1.00 35.19 ? 194 HOH B O   1 
HETATM 2820 O  O   . HOH H 3 .   ? -11.246 28.541 72.027 1.00 47.13 ? 195 HOH B O   1 
HETATM 2821 O  O   . HOH H 3 .   ? -9.176  43.058 53.387 1.00 34.78 ? 196 HOH B O   1 
HETATM 2822 O  O   . HOH H 3 .   ? -5.435  24.803 69.168 1.00 40.15 ? 197 HOH B O   1 
HETATM 2823 O  O   . HOH H 3 .   ? -18.632 44.165 77.618 1.00 31.56 ? 198 HOH B O   1 
HETATM 2824 O  O   . HOH H 3 .   ? -0.975  45.197 59.894 1.00 35.11 ? 199 HOH B O   1 
HETATM 2825 O  O   . HOH H 3 .   ? -6.589  24.316 65.711 1.00 40.59 ? 200 HOH B O   1 
HETATM 2826 O  O   . HOH H 3 .   ? -19.619 37.594 66.790 1.00 47.75 ? 201 HOH B O   1 
HETATM 2827 O  O   . HOH H 3 .   ? -12.034 38.056 84.498 1.00 35.97 ? 202 HOH B O   1 
HETATM 2828 O  O   . HOH H 3 .   ? -12.669 28.838 61.765 1.00 37.98 ? 203 HOH B O   1 
HETATM 2829 O  O   . HOH H 3 .   ? 12.200  28.035 61.952 1.00 46.10 ? 204 HOH B O   1 
HETATM 2830 O  O   . HOH H 3 .   ? -6.875  41.347 85.201 1.00 35.12 ? 205 HOH B O   1 
HETATM 2831 O  O   . HOH H 3 .   ? 3.226   41.628 55.606 1.00 35.50 ? 206 HOH B O   1 
HETATM 2832 O  O   . HOH H 3 .   ? -19.274 41.864 83.167 1.00 63.80 ? 207 HOH B O   1 
HETATM 2833 O  O   . HOH H 3 .   ? -1.931  22.134 70.404 1.00 60.14 ? 208 HOH B O   1 
HETATM 2834 O  O   . HOH H 3 .   ? -6.073  30.420 75.054 1.00 37.71 ? 209 HOH B O   1 
HETATM 2835 O  O   . HOH H 3 .   ? -11.417 28.735 69.605 1.00 36.95 ? 210 HOH B O   1 
HETATM 2836 O  O   . HOH H 3 .   ? -7.164  26.930 70.957 1.00 39.88 ? 211 HOH B O   1 
HETATM 2837 O  O   . HOH H 3 .   ? -12.128 50.415 64.787 1.00 45.94 ? 212 HOH B O   1 
HETATM 2838 O  O   . HOH H 3 .   ? 3.815   22.491 72.388 1.00 50.77 ? 213 HOH B O   1 
HETATM 2839 O  O   . HOH H 3 .   ? -6.488  21.386 52.269 1.00 42.33 ? 214 HOH B O   1 
HETATM 2840 O  O   . HOH H 3 .   ? -7.183  27.275 73.460 1.00 47.90 ? 215 HOH B O   1 
HETATM 2841 O  O   . HOH H 3 .   ? -2.387  44.733 73.268 1.00 56.85 ? 216 HOH B O   1 
HETATM 2842 O  O   . HOH H 3 .   ? -21.337 42.873 81.995 1.00 54.10 ? 217 HOH B O   1 
HETATM 2843 O  O   . HOH H 3 .   ? -8.665  34.305 49.055 1.00 40.49 ? 218 HOH B O   1 
HETATM 2844 O  O   . HOH H 3 .   ? 9.578   35.581 70.046 1.00 33.31 ? 219 HOH B O   1 
HETATM 2845 O  O   . HOH H 3 .   ? 13.070  37.912 62.449 1.00 38.72 ? 220 HOH B O   1 
HETATM 2846 O  O   . HOH H 3 .   ? -8.395  53.171 67.409 1.00 42.96 ? 221 HOH B O   1 
HETATM 2847 O  O   . HOH H 3 .   ? -17.802 42.782 62.353 1.00 44.98 ? 222 HOH B O   1 
HETATM 2848 O  O   . HOH H 3 .   ? -10.696 26.555 55.309 1.00 46.19 ? 223 HOH B O   1 
HETATM 2849 O  O   . HOH H 3 .   ? -7.954  24.222 62.897 1.00 50.45 ? 224 HOH B O   1 
HETATM 2850 O  O   . HOH H 3 .   ? 17.024  32.727 60.687 1.00 47.40 ? 225 HOH B O   1 
HETATM 2851 O  O   . HOH H 3 .   ? 13.276  38.506 59.997 1.00 45.16 ? 226 HOH B O   1 
HETATM 2852 O  O   . HOH H 3 .   ? 6.859   36.597 47.861 1.00 53.78 ? 227 HOH B O   1 
HETATM 2853 O  O   . HOH H 3 .   ? 11.504  26.696 64.624 1.00 89.05 ? 228 HOH B O   1 
HETATM 2854 O  O   . HOH H 3 .   ? 21.483  39.249 57.878 1.00 54.95 ? 229 HOH B O   1 
HETATM 2855 O  O   . HOH H 3 .   ? -13.809 31.279 57.643 1.00 47.50 ? 230 HOH B O   1 
HETATM 2856 O  O   . HOH H 3 .   ? 9.935   43.794 63.676 1.00 43.77 ? 231 HOH B O   1 
HETATM 2857 O  O   . HOH H 3 .   ? -9.151  30.251 75.247 1.00 36.34 ? 232 HOH B O   1 
HETATM 2858 O  O   . HOH H 3 .   ? -17.189 40.221 60.522 1.00 31.49 ? 233 HOH B O   1 
HETATM 2859 O  O   . HOH H 3 .   ? 15.842  32.370 62.950 1.00 54.24 ? 234 HOH B O   1 
HETATM 2860 O  O   . HOH H 3 .   ? -5.405  44.932 58.695 1.00 46.84 ? 235 HOH B O   1 
HETATM 2861 O  O   . HOH H 3 .   ? -21.746 38.890 70.021 1.00 41.31 ? 236 HOH B O   1 
HETATM 2862 O  O   . HOH H 3 .   ? 10.740  41.720 53.249 1.00 47.65 ? 237 HOH B O   1 
HETATM 2863 O  O   . HOH H 3 .   ? -13.696 37.807 56.419 1.00 36.80 ? 238 HOH B O   1 
HETATM 2864 O  O   . HOH H 3 .   ? 5.787   30.475 53.275 1.00 31.47 ? 239 HOH B O   1 
HETATM 2865 O  O   . HOH H 3 .   ? 5.406   43.549 52.042 1.00 45.79 ? 240 HOH B O   1 
HETATM 2866 O  O   . HOH H 3 .   ? 10.106  44.051 66.209 1.00 51.50 ? 241 HOH B O   1 
HETATM 2867 O  O   . HOH H 3 .   ? 11.624  40.375 62.574 1.00 58.67 ? 242 HOH B O   1 
HETATM 2868 O  O   . HOH H 3 .   ? 2.488   23.872 76.602 1.00 63.73 ? 243 HOH B O   1 
HETATM 2869 O  O   . HOH H 3 .   ? -18.735 37.708 76.927 1.00 52.13 ? 244 HOH B O   1 
HETATM 2870 O  O   . HOH H 3 .   ? -13.480 31.504 76.049 1.00 24.93 ? 245 HOH B O   1 
HETATM 2871 O  O   . HOH H 3 .   ? -13.356 31.090 69.779 1.00 24.11 ? 246 HOH B O   1 
HETATM 2872 O  O   . HOH H 3 .   ? -15.063 36.497 81.826 1.00 34.15 ? 247 HOH B O   1 
HETATM 2873 O  O   . HOH H 3 .   ? -1.907  47.217 68.584 1.00 27.45 ? 248 HOH B O   1 
HETATM 2874 O  O   . HOH H 3 .   ? 7.590   28.298 50.593 1.00 29.55 ? 249 HOH B O   1 
HETATM 2875 O  O   . HOH H 3 .   ? -17.775 30.581 70.542 1.00 28.10 ? 250 HOH B O   1 
HETATM 2876 O  O   . HOH H 3 .   ? -3.274  49.704 65.639 1.00 30.27 ? 251 HOH B O   1 
HETATM 2877 O  O   . HOH H 3 .   ? -5.868  52.322 71.120 1.00 35.80 ? 252 HOH B O   1 
HETATM 2878 O  O   . HOH H 3 .   ? 0.392   46.904 63.198 1.00 52.19 ? 253 HOH B O   1 
HETATM 2879 O  O   . HOH H 3 .   ? 14.638  29.274 63.841 1.00 58.25 ? 254 HOH B O   1 
HETATM 2880 O  O   . HOH H 3 .   ? -15.624 47.064 64.512 1.00 53.06 ? 255 HOH B O   1 
HETATM 2881 O  O   . HOH H 3 .   ? 14.162  29.758 61.371 1.00 42.32 ? 256 HOH B O   1 
HETATM 2882 O  O   . HOH H 3 .   ? -19.437 35.386 68.022 1.00 42.06 ? 257 HOH B O   1 
HETATM 2883 O  O   . HOH H 3 .   ? -0.228  45.814 70.919 1.00 66.80 ? 259 HOH B O   1 
HETATM 2884 O  O   . HOH H 3 .   ? 9.758   28.015 74.593 0.30 26.47 ? 260 HOH B O   1 
HETATM 2885 O  O   . HOH H 3 .   ? -11.880 45.596 60.468 1.00 56.40 ? 261 HOH B O   1 
HETATM 2886 O  O   . HOH H 3 .   ? -20.591 35.002 72.356 1.00 45.68 ? 262 HOH B O   1 
HETATM 2887 O  O   . HOH H 3 .   ? -6.581  33.513 46.678 1.00 42.52 ? 263 HOH B O   1 
HETATM 2888 O  O   . HOH H 3 .   ? -10.302 27.473 52.900 1.00 67.67 ? 264 HOH B O   1 
HETATM 2889 O  O   . HOH H 3 .   ? -7.247  44.564 56.333 1.00 44.58 ? 265 HOH B O   1 
HETATM 2890 O  O   . HOH H 3 .   ? -19.172 41.847 77.920 1.00 58.50 ? 266 HOH B O   1 
HETATM 2891 O  O   . HOH H 3 .   ? 12.834  33.099 51.837 1.00 54.73 ? 267 HOH B O   1 
HETATM 2892 O  O   . HOH H 3 .   ? 18.027  33.018 57.931 1.00 49.58 ? 269 HOH B O   1 
HETATM 2893 O  O   . HOH H 3 .   ? 12.982  39.133 50.872 1.00 46.70 ? 270 HOH B O   1 
HETATM 2894 O  O   . HOH H 3 .   ? -9.405  29.700 50.533 1.00 59.00 ? 271 HOH B O   1 
HETATM 2895 O  O   . HOH H 3 .   ? 0.971   43.463 56.197 1.00 56.87 ? 272 HOH B O   1 
HETATM 2896 O  O   . HOH H 3 .   ? 4.406   43.796 55.158 1.00 61.06 ? 273 HOH B O   1 
HETATM 2897 O  O   . HOH H 3 .   ? 5.245   43.579 58.343 1.00 50.01 ? 274 HOH B O   1 
HETATM 2898 O  O   . HOH H 3 .   ? 2.380   38.304 70.634 1.00 48.48 ? 275 HOH B O   1 
HETATM 2899 O  O   . HOH H 3 .   ? -4.369  50.857 63.420 1.00 47.42 ? 276 HOH B O   1 
HETATM 2900 O  O   . HOH H 3 .   ? 1.808   22.055 67.735 1.00 52.14 ? 277 HOH B O   1 
HETATM 2901 O  O   . HOH H 3 .   ? 7.859   33.433 50.556 1.00 49.69 ? 278 HOH B O   1 
HETATM 2902 O  O   . HOH I 3 .   ? 22.308  29.498 40.311 1.00 56.61 ? 113 HOH C O   1 
HETATM 2903 O  O   . HOH I 3 .   ? 31.633  29.762 36.466 1.00 44.49 ? 114 HOH C O   1 
HETATM 2904 O  O   . HOH I 3 .   ? 16.117  9.240  43.374 1.00 59.34 ? 115 HOH C O   1 
HETATM 2905 O  O   . HOH I 3 .   ? 24.366  28.836 38.875 1.00 38.28 ? 116 HOH C O   1 
HETATM 2906 O  O   . HOH I 3 .   ? 27.673  30.396 37.219 1.00 43.10 ? 117 HOH C O   1 
HETATM 2907 O  O   . HOH I 3 .   ? 16.927  34.013 50.044 1.00 48.69 ? 118 HOH C O   1 
HETATM 2908 O  O   . HOH I 3 .   ? 19.772  15.055 46.846 1.00 14.31 ? 119 HOH C O   1 
HETATM 2909 O  O   . HOH I 3 .   ? 25.830  20.533 49.238 1.00 14.46 ? 120 HOH C O   1 
HETATM 2910 O  O   . HOH I 3 .   ? 21.885  15.059 51.981 1.00 12.98 ? 121 HOH C O   1 
HETATM 2911 O  O   . HOH I 3 .   ? 13.085  16.624 56.703 1.00 17.45 ? 122 HOH C O   1 
HETATM 2912 O  O   . HOH I 3 .   ? 17.349  18.654 57.084 1.00 16.71 ? 123 HOH C O   1 
HETATM 2913 O  O   . HOH I 3 .   ? 19.628  18.972 58.707 1.00 17.84 ? 124 HOH C O   1 
HETATM 2914 O  O   . HOH I 3 .   ? 33.656  8.414  49.371 1.00 15.20 ? 125 HOH C O   1 
HETATM 2915 O  O   . HOH I 3 .   ? 15.724  17.031 45.720 1.00 22.58 ? 126 HOH C O   1 
HETATM 2916 O  O   . HOH I 3 .   ? 19.839  18.181 50.943 1.00 14.64 ? 127 HOH C O   1 
HETATM 2917 O  O   . HOH I 3 .   ? 36.722  26.342 45.744 1.00 23.40 ? 128 HOH C O   1 
HETATM 2918 O  O   . HOH I 3 .   ? 25.660  23.390 48.705 1.00 18.76 ? 129 HOH C O   1 
HETATM 2919 O  O   . HOH I 3 .   ? 9.722   25.374 62.117 1.00 51.66 ? 130 HOH C O   1 
HETATM 2920 O  O   . HOH I 3 .   ? 37.705  17.278 51.827 1.00 21.59 ? 131 HOH C O   1 
HETATM 2921 O  O   . HOH I 3 .   ? 40.818  6.497  49.660 1.00 37.53 ? 132 HOH C O   1 
HETATM 2922 O  O   . HOH I 3 .   ? 45.251  15.983 50.851 1.00 24.40 ? 133 HOH C O   1 
HETATM 2923 O  O   . HOH I 3 .   ? 18.500  8.879  44.853 1.00 38.21 ? 134 HOH C O   1 
HETATM 2924 O  O   . HOH I 3 .   ? 24.947  28.564 33.833 1.00 26.21 ? 135 HOH C O   1 
HETATM 2925 O  O   . HOH I 3 .   ? 16.825  9.073  50.057 1.00 41.37 ? 136 HOH C O   1 
HETATM 2926 O  O   . HOH I 3 .   ? 39.853  18.980 50.579 1.00 17.87 ? 137 HOH C O   1 
HETATM 2927 O  O   . HOH I 3 .   ? 32.140  24.951 40.571 1.00 22.02 ? 138 HOH C O   1 
HETATM 2928 O  O   . HOH I 3 .   ? 40.382  14.218 57.232 1.00 11.96 ? 139 HOH C O   1 
HETATM 2929 O  O   . HOH I 3 .   ? 36.130  6.963  55.058 1.00 20.66 ? 140 HOH C O   1 
HETATM 2930 O  O   . HOH I 3 .   ? 14.521  15.079 47.195 1.00 29.59 ? 141 HOH C O   1 
HETATM 2931 O  O   . HOH I 3 .   ? 23.874  7.325  39.890 1.00 26.27 ? 142 HOH C O   1 
HETATM 2932 O  O   . HOH I 3 .   ? 20.646  13.988 33.738 1.00 24.55 ? 143 HOH C O   1 
HETATM 2933 O  O   . HOH I 3 .   ? 26.894  9.648  31.035 1.00 21.44 ? 144 HOH C O   1 
HETATM 2934 O  O   . HOH I 3 .   ? 28.602  13.552 31.158 1.00 24.72 ? 145 HOH C O   1 
HETATM 2935 O  O   . HOH I 3 .   ? 11.191  26.747 60.097 1.00 26.58 ? 146 HOH C O   1 
HETATM 2936 O  O   . HOH I 3 .   ? 37.501  6.935  39.315 1.00 30.87 ? 147 HOH C O   1 
HETATM 2937 O  O   . HOH I 3 .   ? 10.075  23.031 61.145 1.00 49.45 ? 148 HOH C O   1 
HETATM 2938 O  O   . HOH I 3 .   ? 40.401  10.666 48.401 1.00 25.51 ? 149 HOH C O   1 
HETATM 2939 O  O   . HOH I 3 .   ? 23.604  26.006 39.584 1.00 22.17 ? 150 HOH C O   1 
HETATM 2940 O  O   . HOH I 3 .   ? 13.530  18.544 51.009 1.00 28.54 ? 151 HOH C O   1 
HETATM 2941 O  O   . HOH I 3 .   ? 16.347  8.742  52.966 1.00 56.89 ? 152 HOH C O   1 
HETATM 2942 O  O   . HOH I 3 .   ? 37.305  18.971 53.787 1.00 19.59 ? 153 HOH C O   1 
HETATM 2943 O  O   . HOH I 3 .   ? 24.090  20.198 57.698 1.00 19.37 ? 154 HOH C O   1 
HETATM 2944 O  O   . HOH I 3 .   ? 17.219  11.255 52.709 1.00 24.76 ? 155 HOH C O   1 
HETATM 2945 O  O   . HOH I 3 .   ? 22.849  8.192  43.203 1.00 20.70 ? 156 HOH C O   1 
HETATM 2946 O  O   . HOH I 3 .   ? 38.683  20.582 52.362 1.00 31.58 ? 157 HOH C O   1 
HETATM 2947 O  O   . HOH I 3 .   ? 13.365  16.404 49.437 1.00 32.00 ? 158 HOH C O   1 
HETATM 2948 O  O   . HOH I 3 .   ? 32.359  14.124 29.923 1.00 23.75 ? 159 HOH C O   1 
HETATM 2949 O  O   . HOH I 3 .   ? 33.824  12.230 31.606 1.00 16.81 ? 160 HOH C O   1 
HETATM 2950 O  O   . HOH I 3 .   ? 28.724  32.885 43.683 1.00 49.11 ? 161 HOH C O   1 
HETATM 2951 O  O   . HOH I 3 .   ? 22.179  18.153 58.337 1.00 17.50 ? 162 HOH C O   1 
HETATM 2952 O  O   . HOH I 3 .   ? 27.529  5.259  36.220 1.00 31.39 ? 163 HOH C O   1 
HETATM 2953 O  O   . HOH I 3 .   ? 27.670  18.514 55.272 1.00 24.78 ? 164 HOH C O   1 
HETATM 2954 O  O   . HOH I 3 .   ? 24.691  29.742 50.927 1.00 28.66 ? 165 HOH C O   1 
HETATM 2955 O  O   . HOH I 3 .   ? 15.841  29.003 59.077 1.00 38.37 ? 166 HOH C O   1 
HETATM 2956 O  O   . HOH I 3 .   ? 21.599  26.183 44.018 1.00 27.13 ? 167 HOH C O   1 
HETATM 2957 O  O   . HOH I 3 .   ? 26.296  26.044 40.497 1.00 28.06 ? 168 HOH C O   1 
HETATM 2958 O  O   . HOH I 3 .   ? 27.443  21.895 52.893 1.00 29.91 ? 169 HOH C O   1 
HETATM 2959 O  O   . HOH I 3 .   ? 10.591  15.514 57.167 1.00 45.38 ? 170 HOH C O   1 
HETATM 2960 O  O   . HOH I 3 .   ? 17.094  11.694 59.244 1.00 30.67 ? 171 HOH C O   1 
HETATM 2961 O  O   . HOH I 3 .   ? 19.816  25.764 59.300 1.00 37.37 ? 172 HOH C O   1 
HETATM 2962 O  O   . HOH I 3 .   ? 18.890  11.509 54.906 1.00 35.15 ? 173 HOH C O   1 
HETATM 2963 O  O   . HOH I 3 .   ? 35.237  15.692 32.772 1.00 26.63 ? 174 HOH C O   1 
HETATM 2964 O  O   . HOH I 3 .   ? 14.989  31.744 50.602 1.00 34.05 ? 175 HOH C O   1 
HETATM 2965 O  O   . HOH I 3 .   ? 17.032  18.388 66.952 1.00 44.05 ? 176 HOH C O   1 
HETATM 2966 O  O   . HOH I 3 .   ? 25.161  7.483  31.810 1.00 50.95 ? 177 HOH C O   1 
HETATM 2967 O  O   . HOH I 3 .   ? 47.401  26.502 38.101 1.00 26.59 ? 178 HOH C O   1 
HETATM 2968 O  O   . HOH I 3 .   ? 30.038  24.495 51.175 1.00 29.07 ? 179 HOH C O   1 
HETATM 2969 O  O   . HOH I 3 .   ? 41.316  25.006 42.462 1.00 31.33 ? 180 HOH C O   1 
HETATM 2970 O  O   . HOH I 3 .   ? 41.264  24.088 45.114 1.00 33.54 ? 181 HOH C O   1 
HETATM 2971 O  O   . HOH I 3 .   ? 28.626  29.473 48.666 1.00 32.98 ? 182 HOH C O   1 
HETATM 2972 O  O   . HOH I 3 .   ? 33.512  6.066  51.167 1.00 44.46 ? 183 HOH C O   1 
HETATM 2973 O  O   . HOH I 3 .   ? 34.123  24.268 52.660 1.00 41.44 ? 184 HOH C O   1 
HETATM 2974 O  O   . HOH I 3 .   ? 19.942  9.112  51.935 1.00 33.67 ? 185 HOH C O   1 
HETATM 2975 O  O   . HOH I 3 .   ? 33.577  7.582  46.519 1.00 33.58 ? 186 HOH C O   1 
HETATM 2976 O  O   . HOH I 3 .   ? 19.186  25.125 41.496 1.00 38.13 ? 187 HOH C O   1 
HETATM 2977 O  O   . HOH I 3 .   ? 26.814  22.298 56.178 1.00 36.25 ? 188 HOH C O   1 
HETATM 2978 O  O   . HOH I 3 .   ? 36.366  18.267 32.688 1.00 48.52 ? 189 HOH C O   1 
HETATM 2979 O  O   . HOH I 3 .   ? 26.431  6.616  51.421 1.00 34.59 ? 190 HOH C O   1 
HETATM 2980 O  O   . HOH I 3 .   ? 19.892  28.233 44.350 1.00 44.62 ? 191 HOH C O   1 
HETATM 2981 O  O   . HOH I 3 .   ? 26.842  27.486 36.911 1.00 34.29 ? 192 HOH C O   1 
HETATM 2982 O  O   . HOH I 3 .   ? 31.756  27.530 40.221 1.00 49.58 ? 193 HOH C O   1 
HETATM 2983 O  O   . HOH I 3 .   ? 21.006  11.348 57.694 1.00 36.68 ? 194 HOH C O   1 
HETATM 2984 O  O   . HOH I 3 .   ? 25.435  28.015 42.725 1.00 34.79 ? 195 HOH C O   1 
HETATM 2985 O  O   . HOH I 3 .   ? 24.355  8.485  53.716 1.00 40.32 ? 196 HOH C O   1 
HETATM 2986 O  O   . HOH I 3 .   ? 21.777  26.446 41.494 1.00 36.16 ? 197 HOH C O   1 
HETATM 2987 O  O   . HOH I 3 .   ? 31.937  8.176  57.718 1.00 49.53 ? 198 HOH C O   1 
HETATM 2988 O  O   . HOH I 3 .   ? 16.607  11.700 40.368 1.00 41.25 ? 199 HOH C O   1 
HETATM 2989 O  O   . HOH I 3 .   ? 28.136  26.921 38.883 1.00 34.43 ? 200 HOH C O   1 
HETATM 2990 O  O   . HOH I 3 .   ? 8.653   15.465 50.938 1.00 46.24 ? 201 HOH C O   1 
HETATM 2991 O  O   . HOH I 3 .   ? 22.505  31.870 47.719 1.00 39.47 ? 202 HOH C O   1 
HETATM 2992 O  O   . HOH I 3 .   ? 26.477  30.186 47.379 1.00 44.20 ? 203 HOH C O   1 
HETATM 2993 O  O   . HOH I 3 .   ? 44.955  17.158 45.506 1.00 41.89 ? 204 HOH C O   1 
HETATM 2994 O  O   . HOH I 3 .   ? 20.120  27.002 30.975 1.00 51.32 ? 205 HOH C O   1 
HETATM 2995 O  O   . HOH I 3 .   ? 7.413   16.391 53.050 1.00 38.28 ? 206 HOH C O   1 
HETATM 2996 O  O   . HOH I 3 .   ? 36.569  28.237 59.289 1.00 53.23 ? 207 HOH C O   1 
HETATM 2997 O  O   . HOH I 3 .   ? 41.783  17.974 58.583 1.00 26.88 ? 208 HOH C O   1 
HETATM 2998 O  O   . HOH I 3 .   ? 47.119  18.449 47.925 1.00 29.01 ? 209 HOH C O   1 
HETATM 2999 O  O   . HOH I 3 .   ? 25.311  30.165 35.678 1.00 37.01 ? 210 HOH C O   1 
HETATM 3000 O  O   . HOH I 3 .   ? 39.375  8.720  41.612 1.00 31.63 ? 211 HOH C O   1 
HETATM 3001 O  O   . HOH I 3 .   ? 22.745  15.057 29.604 1.00 35.78 ? 212 HOH C O   1 
HETATM 3002 O  O   . HOH I 3 .   ? 25.401  6.175  48.560 1.00 38.86 ? 213 HOH C O   1 
HETATM 3003 O  O   . HOH I 3 .   ? 30.844  25.321 38.102 1.00 34.39 ? 214 HOH C O   1 
HETATM 3004 O  O   . HOH I 3 .   ? 30.836  21.581 53.233 1.00 48.09 ? 215 HOH C O   1 
HETATM 3005 O  O   . HOH I 3 .   ? 18.334  23.878 36.079 1.00 34.30 ? 216 HOH C O   1 
HETATM 3006 O  O   . HOH I 3 .   ? 30.265  9.943  57.696 1.00 34.80 ? 217 HOH C O   1 
HETATM 3007 O  O   . HOH I 3 .   ? 13.886  15.124 60.694 1.00 39.55 ? 218 HOH C O   1 
HETATM 3008 O  O   . HOH I 3 .   ? 28.641  7.144  40.791 1.00 29.74 ? 219 HOH C O   1 
HETATM 3009 O  O   . HOH I 3 .   ? 46.511  14.943 47.308 1.00 37.44 ? 220 HOH C O   1 
HETATM 3010 O  O   . HOH I 3 .   ? 38.005  13.564 32.749 1.00 41.04 ? 221 HOH C O   1 
HETATM 3011 O  O   . HOH I 3 .   ? 36.846  8.871  60.322 1.00 32.45 ? 222 HOH C O   1 
HETATM 3012 O  O   . HOH I 3 .   ? 24.561  11.900 57.627 1.00 33.64 ? 223 HOH C O   1 
HETATM 3013 O  O   . HOH I 3 .   ? 45.940  19.831 40.385 1.00 41.33 ? 224 HOH C O   1 
HETATM 3014 O  O   . HOH I 3 .   ? 44.248  28.727 35.252 1.00 44.22 ? 225 HOH C O   1 
HETATM 3015 O  O   . HOH I 3 .   ? 31.200  27.293 36.175 1.00 35.42 ? 226 HOH C O   1 
HETATM 3016 O  O   . HOH I 3 .   ? 31.237  5.251  52.189 1.00 52.70 ? 227 HOH C O   1 
HETATM 3017 O  O   . HOH I 3 .   ? 34.132  7.450  58.818 1.00 45.51 ? 228 HOH C O   1 
HETATM 3018 O  O   . HOH I 3 .   ? 39.448  26.132 45.824 1.00 49.35 ? 229 HOH C O   1 
HETATM 3019 O  O   . HOH I 3 .   ? 17.148  9.010  47.577 1.00 50.75 ? 230 HOH C O   1 
HETATM 3020 O  O   . HOH I 3 .   ? 35.470  3.830  41.591 1.00 44.60 ? 231 HOH C O   1 
HETATM 3021 O  O   . HOH I 3 .   ? 42.013  11.961 41.130 1.00 43.46 ? 232 HOH C O   1 
HETATM 3022 O  O   . HOH I 3 .   ? 23.592  8.924  56.281 1.00 45.93 ? 233 HOH C O   1 
HETATM 3023 O  O   . HOH I 3 .   ? 11.070  24.168 36.833 1.00 47.63 ? 234 HOH C O   1 
HETATM 3024 O  O   . HOH I 3 .   ? 11.667  14.207 59.596 1.00 53.87 ? 235 HOH C O   1 
HETATM 3025 O  O   . HOH I 3 .   ? 21.984  30.936 44.291 1.00 45.18 ? 236 HOH C O   1 
HETATM 3026 O  O   . HOH I 3 .   ? 37.213  22.366 52.155 1.00 35.45 ? 237 HOH C O   1 
HETATM 3027 O  O   . HOH I 3 .   ? 40.764  12.299 45.964 1.00 51.94 ? 238 HOH C O   1 
HETATM 3028 O  O   . HOH I 3 .   ? 21.035  15.500 31.569 1.00 37.89 ? 239 HOH C O   1 
HETATM 3029 O  O   . HOH I 3 .   ? 22.963  7.373  50.757 1.00 38.00 ? 240 HOH C O   1 
HETATM 3030 O  O   . HOH I 3 .   ? 15.968  20.939 36.452 1.00 42.82 ? 241 HOH C O   1 
HETATM 3031 O  O   . HOH I 3 .   ? 21.321  11.221 33.046 1.00 44.59 ? 242 HOH C O   1 
HETATM 3032 O  O   . HOH I 3 .   ? 18.862  28.385 60.476 1.00 68.52 ? 243 HOH C O   1 
HETATM 3033 O  O   . HOH I 3 .   ? 11.547  15.750 36.647 1.00 53.54 ? 244 HOH C O   1 
HETATM 3034 O  O   . HOH I 3 .   ? 44.537  21.127 45.828 1.00 37.65 ? 245 HOH C O   1 
HETATM 3035 O  O   . HOH I 3 .   ? 38.620  20.131 31.589 1.00 77.07 ? 246 HOH C O   1 
HETATM 3036 O  O   . HOH I 3 .   ? 10.006  14.403 47.823 1.00 55.92 ? 247 HOH C O   1 
HETATM 3037 O  O   . HOH I 3 .   ? 19.882  33.110 54.844 1.00 50.69 ? 248 HOH C O   1 
HETATM 3038 O  O   . HOH I 3 .   ? 19.266  15.941 29.153 1.00 50.15 ? 249 HOH C O   1 
HETATM 3039 O  O   . HOH I 3 .   ? 26.205  29.064 53.931 1.00 73.83 ? 250 HOH C O   1 
HETATM 3040 O  O   . HOH I 3 .   ? 26.434  15.156 27.840 1.00 39.83 ? 251 HOH C O   1 
HETATM 3041 O  O   . HOH I 3 .   ? 14.616  12.461 60.951 1.00 53.15 ? 252 HOH C O   1 
HETATM 3042 O  O   . HOH I 3 .   ? 37.200  28.915 46.426 1.00 42.29 ? 253 HOH C O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . VAL A 3   ? 0.9390 0.4614 0.4155 -0.4533 0.0401  -0.0753 3   VAL A N   
2    C  CA  . VAL A 3   ? 0.8639 0.3247 0.3879 -0.3472 0.0364  -0.0656 3   VAL A CA  
3    C  C   . VAL A 3   ? 0.6453 0.3086 0.3558 -0.1855 0.1056  -0.0986 3   VAL A C   
4    O  O   . VAL A 3   ? 0.4963 0.4293 0.3980 -0.0772 0.0665  -0.0408 3   VAL A O   
5    C  CB  . VAL A 3   ? 0.9192 0.2946 0.3865 -0.2868 0.0317  -0.0534 3   VAL A CB  
6    C  CG1 . VAL A 3   ? 0.7961 0.2821 0.3766 -0.1985 0.0505  -0.0958 3   VAL A CG1 
7    C  CG2 . VAL A 3   ? 1.0180 0.2879 0.4091 -0.2690 -0.0275 0.0338  3   VAL A CG2 
8    N  N   . ILE A 4   ? 0.6192 0.1979 0.2157 -0.1048 0.0963  -0.0541 4   ILE A N   
9    C  CA  . ILE A 4   ? 0.5555 0.1936 0.1657 -0.0496 0.1087  -0.0363 4   ILE A CA  
10   C  C   . ILE A 4   ? 0.4589 0.1708 0.1800 -0.0226 0.1563  -0.0508 4   ILE A C   
11   O  O   . ILE A 4   ? 0.4643 0.1345 0.2232 0.0326  0.1473  0.0056  4   ILE A O   
12   C  CB  . ILE A 4   ? 0.5759 0.1933 0.1741 -0.0527 0.1185  -0.0366 4   ILE A CB  
13   C  CG1 . ILE A 4   ? 0.6723 0.1861 0.1679 -0.0813 0.0674  -0.0041 4   ILE A CG1 
14   C  CG2 . ILE A 4   ? 0.5356 0.2036 0.2080 -0.0802 0.1479  -0.0345 4   ILE A CG2 
15   C  CD1 . ILE A 4   ? 0.7583 0.3635 0.1415 -0.1878 0.1016  0.0317  4   ILE A CD1 
16   N  N   . ASN A 5   ? 0.4182 0.1613 0.1849 -0.1126 0.1387  -0.0212 5   ASN A N   
17   C  CA  . ASN A 5   ? 0.4137 0.1513 0.1823 -0.0995 0.1153  -0.0334 5   ASN A CA  
18   C  C   . ASN A 5   ? 0.3246 0.1607 0.1696 -0.1042 0.0592  -0.0108 5   ASN A C   
19   O  O   . ASN A 5   ? 0.3261 0.1615 0.1620 -0.0264 0.0517  -0.0167 5   ASN A O   
20   C  CB  . ASN A 5   ? 0.4178 0.1616 0.1821 -0.0872 0.1271  -0.0872 5   ASN A CB  
21   C  CG  . ASN A 5   ? 0.4058 0.2019 0.1862 -0.0924 0.1060  -0.1096 5   ASN A CG  
22   O  OD1 . ASN A 5   ? 0.3406 0.2983 0.1881 -0.0849 0.0817  -0.0776 5   ASN A OD1 
23   N  ND2 . ASN A 5   ? 0.3783 0.3095 0.1835 -0.0754 0.0206  -0.1443 5   ASN A ND2 
24   N  N   . THR A 6   ? 0.2496 0.1777 0.1737 -0.0531 0.0611  -0.0363 6   THR A N   
25   C  CA  . THR A 6   ? 0.2268 0.1791 0.2328 -0.0275 0.0764  -0.0454 6   THR A CA  
26   C  C   . THR A 6   ? 0.2024 0.1573 0.1736 0.0095  0.0460  -0.0432 6   THR A C   
27   O  O   . THR A 6   ? 0.2588 0.1626 0.1248 -0.0301 0.0345  -0.0188 6   THR A O   
28   C  CB  . THR A 6   ? 0.1956 0.2162 0.2403 -0.0038 0.0679  -0.0018 6   THR A CB  
29   O  OG1 . THR A 6   ? 0.3490 0.3171 0.2148 -0.0902 0.0722  -0.0640 6   THR A OG1 
30   C  CG2 . THR A 6   ? 0.2141 0.3656 0.2770 -0.0682 0.0937  -0.0160 6   THR A CG2 
31   N  N   . PHE A 7   ? 0.2385 0.1641 0.1459 -0.0294 0.0525  -0.0714 7   PHE A N   
32   C  CA  . PHE A 7   ? 0.2609 0.1593 0.1474 -0.0315 0.0429  -0.0489 7   PHE A CA  
33   C  C   . PHE A 7   ? 0.3036 0.1545 0.1485 -0.0978 0.1007  -0.0325 7   PHE A C   
34   O  O   . PHE A 7   ? 0.2672 0.1756 0.1430 -0.0341 0.0860  -0.0354 7   PHE A O   
35   C  CB  . PHE A 7   ? 0.2846 0.1564 0.1537 -0.0268 0.0333  -0.0374 7   PHE A CB  
36   C  CG  . PHE A 7   ? 0.2806 0.1372 0.1526 -0.0061 0.0214  -0.0403 7   PHE A CG  
37   C  CD1 . PHE A 7   ? 0.2804 0.1477 0.1579 -0.0141 0.0176  -0.0426 7   PHE A CD1 
38   C  CD2 . PHE A 7   ? 0.2640 0.1793 0.1558 -0.0055 0.0709  -0.0426 7   PHE A CD2 
39   C  CE1 . PHE A 7   ? 0.2884 0.1957 0.1690 -0.0626 0.0795  -0.0539 7   PHE A CE1 
40   C  CE2 . PHE A 7   ? 0.2857 0.1836 0.1522 -0.0226 0.0596  -0.0462 7   PHE A CE2 
41   C  CZ  . PHE A 7   ? 0.3156 0.1536 0.1526 -0.0548 0.0650  -0.0378 7   PHE A CZ  
42   N  N   . ASP A 8   ? 0.2733 0.2055 0.1533 -0.0746 0.0972  -0.0683 8   ASP A N   
43   C  CA  . ASP A 8   ? 0.2335 0.2250 0.1490 -0.0044 0.0890  -0.0719 8   ASP A CA  
44   C  C   . ASP A 8   ? 0.2887 0.2173 0.1611 0.0101  0.0396  -0.0825 8   ASP A C   
45   O  O   . ASP A 8   ? 0.2712 0.1876 0.1790 0.0162  0.0343  -0.0239 8   ASP A O   
46   C  CB  . ASP A 8   ? 0.1862 0.2751 0.1857 0.0499  0.0760  -0.0784 8   ASP A CB  
47   C  CG  . ASP A 8   ? 0.1769 0.2758 0.3432 0.1170  0.0324  -0.0421 8   ASP A CG  
48   O  OD1 . ASP A 8   ? 0.2982 0.2594 0.2751 0.0387  -0.0462 -0.0581 8   ASP A OD1 
49   O  OD2 . ASP A 8   ? 0.2560 0.2374 0.3655 0.0306  -0.0081 -0.0550 8   ASP A OD2 
50   N  N   . GLY A 9   ? 0.3177 0.2261 0.1727 -0.0221 0.1112  -0.0709 9   GLY A N   
51   C  CA  . GLY A 9   ? 0.3732 0.2213 0.1726 -0.0787 0.1408  -0.0663 9   GLY A CA  
52   C  C   . GLY A 9   ? 0.3834 0.1857 0.1368 -0.0525 0.1144  -0.0669 9   GLY A C   
53   O  O   . GLY A 9   ? 0.4023 0.1971 0.1377 -0.0179 0.0891  -0.0112 9   GLY A O   
54   N  N   . VAL A 10  ? 0.3683 0.1399 0.1364 -0.0063 0.0930  -0.0292 10  VAL A N   
55   C  CA  . VAL A 10  ? 0.3723 0.1481 0.1076 -0.0077 0.1084  -0.0144 10  VAL A CA  
56   C  C   . VAL A 10  ? 0.3316 0.1474 0.0988 0.0331  -0.0103 0.0114  10  VAL A C   
57   O  O   . VAL A 10  ? 0.3417 0.1615 0.0885 0.0285  0.0132  -0.0147 10  VAL A O   
58   C  CB  . VAL A 10  ? 0.3774 0.1038 0.1064 0.0295  0.1211  -0.0445 10  VAL A CB  
59   C  CG1 . VAL A 10  ? 0.3330 0.1701 0.1266 0.0518  0.0372  -0.0035 10  VAL A CG1 
60   C  CG2 . VAL A 10  ? 0.4036 0.1267 0.1169 -0.0123 0.0338  -0.0483 10  VAL A CG2 
61   N  N   . ALA A 11  ? 0.2857 0.1478 0.1569 -0.0029 0.0299  -0.0165 11  ALA A N   
62   C  CA  . ALA A 11  ? 0.2345 0.1390 0.1519 0.0474  -0.0015 -0.0109 11  ALA A CA  
63   C  C   . ALA A 11  ? 0.4171 0.1528 0.1438 0.0170  -0.0604 -0.0146 11  ALA A C   
64   O  O   . ALA A 11  ? 0.3894 0.2080 0.1146 0.0569  0.0290  -0.0398 11  ALA A O   
65   C  CB  . ALA A 11  ? 0.2833 0.1290 0.1921 0.0071  0.0028  -0.0186 11  ALA A CB  
66   N  N   . ASP A 12  ? 0.4453 0.1759 0.1031 -0.0092 0.0351  -0.0271 12  ASP A N   
67   C  CA  . ASP A 12  ? 0.5526 0.1874 0.0970 -0.0039 0.0974  -0.0285 12  ASP A CA  
68   C  C   . ASP A 12  ? 0.6126 0.1807 0.1104 0.0131  0.0356  -0.0070 12  ASP A C   
69   O  O   . ASP A 12  ? 0.5304 0.2017 0.1393 0.0484  0.0543  -0.0400 12  ASP A O   
70   C  CB  . ASP A 12  ? 0.5410 0.2430 0.0624 -0.0134 0.1198  -0.0081 12  ASP A CB  
71   C  CG  . ASP A 12  ? 0.4670 0.2650 0.1296 0.0688  0.1558  -0.0303 12  ASP A CG  
72   O  OD1 . ASP A 12  ? 0.5353 0.2310 0.2319 0.0387  0.0837  0.0369  12  ASP A OD1 
73   O  OD2 . ASP A 12  ? 0.4028 0.3636 0.2078 0.1354  0.0654  -0.0406 12  ASP A OD2 
74   N  N   . TYR A 13  ? 0.5415 0.1826 0.1368 0.0484  0.0411  -0.0154 13  TYR A N   
75   C  CA  . TYR A 13  ? 0.5294 0.1921 0.1176 0.0758  0.1118  -0.0371 13  TYR A CA  
76   C  C   . TYR A 13  ? 0.5342 0.1864 0.1446 0.0796  0.0304  -0.0346 13  TYR A C   
77   O  O   . TYR A 13  ? 0.5385 0.1964 0.1587 0.0365  -0.0359 -0.0015 13  TYR A O   
78   C  CB  . TYR A 13  ? 0.5527 0.1922 0.1206 0.0740  0.1177  -0.0071 13  TYR A CB  
79   C  CG  . TYR A 13  ? 0.6268 0.1868 0.1571 0.0423  0.1012  0.0584  13  TYR A CG  
80   C  CD1 . TYR A 13  ? 0.6464 0.1573 0.1648 0.0629  0.0336  0.0511  13  TYR A CD1 
81   C  CD2 . TYR A 13  ? 0.6865 0.2055 0.2102 -0.0106 0.1256  0.0323  13  TYR A CD2 
82   C  CE1 . TYR A 13  ? 0.7080 0.1601 0.1670 0.0524  0.0810  0.0146  13  TYR A CE1 
83   C  CE2 . TYR A 13  ? 0.7545 0.2009 0.2361 -0.0272 0.1057  0.0194  13  TYR A CE2 
84   C  CZ  . TYR A 13  ? 0.7805 0.1660 0.2119 -0.0099 0.0569  0.0084  13  TYR A CZ  
85   O  OH  . TYR A 13  ? 0.8689 0.1648 0.2611 -0.0014 -0.0221 -0.0162 13  TYR A OH  
86   N  N   . LEU A 14  ? 0.5510 0.1719 0.1681 0.0460  0.0044  -0.0620 14  LEU A N   
87   C  CA  . LEU A 14  ? 0.5063 0.2061 0.1775 0.0913  -0.0434 -0.0449 14  LEU A CA  
88   C  C   . LEU A 14  ? 0.4630 0.2287 0.1758 0.1194  -0.0866 -0.0547 14  LEU A C   
89   O  O   . LEU A 14  ? 0.4928 0.2075 0.1762 0.0962  -0.1129 -0.0296 14  LEU A O   
90   C  CB  . LEU A 14  ? 0.4747 0.2015 0.1723 0.0878  -0.0052 -0.0684 14  LEU A CB  
91   C  CG  . LEU A 14  ? 0.5012 0.1819 0.1776 0.0503  -0.0011 -0.0520 14  LEU A CG  
92   C  CD1 . LEU A 14  ? 0.4411 0.1940 0.1711 -0.0107 -0.0513 -0.0121 14  LEU A CD1 
93   C  CD2 . LEU A 14  ? 0.4854 0.1929 0.1668 0.0435  0.0040  -0.0550 14  LEU A CD2 
94   N  N   . GLN A 15  ? 0.4947 0.2133 0.1983 0.1127  -0.0214 -0.0566 15  GLN A N   
95   C  CA  . GLN A 15  ? 0.5459 0.2339 0.1908 0.1377  -0.0261 -0.0769 15  GLN A CA  
96   C  C   . GLN A 15  ? 0.6398 0.2294 0.1929 0.1612  0.0143  -0.0707 15  GLN A C   
97   O  O   . GLN A 15  ? 0.7508 0.3319 0.1842 0.0730  0.0321  -0.0329 15  GLN A O   
98   C  CB  . GLN A 15  ? 0.5042 0.2393 0.1333 0.1241  -0.0543 -0.0735 15  GLN A CB  
99   C  CG  . GLN A 15  ? 0.4617 0.2414 0.1444 0.0927  -0.0795 -0.0798 15  GLN A CG  
100  C  CD  . GLN A 15  ? 0.3991 0.2399 0.1596 0.0775  -0.0664 -0.0453 15  GLN A CD  
101  O  OE1 . GLN A 15  ? 0.4052 0.2344 0.2053 0.0365  -0.0110 0.0398  15  GLN A OE1 
102  N  NE2 . GLN A 15  ? 0.3467 0.2566 0.1416 0.1066  -0.0261 -0.0278 15  GLN A NE2 
103  N  N   . THR A 16  ? 0.7806 0.2246 0.2038 0.0867  -0.0118 0.0029  16  THR A N   
104  C  CA  . THR A 16  ? 0.7922 0.2516 0.1977 0.0738  0.0526  0.0071  16  THR A CA  
105  C  C   . THR A 16  ? 0.8308 0.2393 0.1900 0.0829  0.0108  0.0407  16  THR A C   
106  O  O   . THR A 16  ? 0.7457 0.2928 0.1881 0.0912  0.0585  -0.0448 16  THR A O   
107  C  CB  . THR A 16  ? 0.7782 0.3400 0.2073 0.0546  0.1688  0.0358  16  THR A CB  
108  O  OG1 . THR A 16  ? 0.7035 0.3821 0.4085 0.1102  0.1540  0.0292  16  THR A OG1 
109  C  CG2 . THR A 16  ? 0.8487 0.4000 0.1977 -0.0130 0.1389  0.0511  16  THR A CG2 
110  N  N   . TYR A 17  ? 0.5735 0.2786 0.1933 0.1029  -0.0116 0.0141  17  TYR A N   
111  C  CA  . TYR A 17  ? 0.6005 0.2715 0.1636 0.1024  -0.0594 0.0451  17  TYR A CA  
112  C  C   . TYR A 17  ? 0.6292 0.2093 0.1783 0.0937  -0.0788 0.0173  17  TYR A C   
113  O  O   . TYR A 17  ? 0.6479 0.2064 0.2057 0.1405  -0.1087 -0.0123 17  TYR A O   
114  C  CB  . TYR A 17  ? 0.6672 0.2867 0.2265 0.0346  0.0520  0.0738  17  TYR A CB  
115  C  CG  . TYR A 17  ? 0.6713 0.3604 0.2783 0.0059  0.0475  0.1368  17  TYR A CG  
116  C  CD1 . TYR A 17  ? 0.6425 0.3846 0.3590 -0.0167 0.0746  0.1200  17  TYR A CD1 
117  C  CD2 . TYR A 17  ? 0.7081 0.3603 0.3226 -0.0616 0.0669  0.1286  17  TYR A CD2 
118  C  CE1 . TYR A 17  ? 0.6662 0.4314 0.3860 -0.0609 0.1149  0.1361  17  TYR A CE1 
119  C  CE2 . TYR A 17  ? 0.7122 0.4127 0.3853 -0.0921 0.0670  0.1228  17  TYR A CE2 
120  C  CZ  . TYR A 17  ? 0.6857 0.4328 0.3967 -0.0899 0.0865  0.1302  17  TYR A CZ  
121  O  OH  . TYR A 17  ? 0.6978 0.4796 0.4092 -0.1203 0.1061  0.0598  17  TYR A OH  
122  N  N   . HIS A 18  ? 0.5892 0.2071 0.1419 0.1291  -0.0635 -0.0560 18  HIS A N   
123  C  CA  . HIS A 18  ? 0.5925 0.2529 0.1143 0.1206  -0.1171 -0.0603 18  HIS A CA  
124  C  C   . HIS A 18  ? 0.5522 0.1951 0.1589 0.1099  -0.1177 -0.0771 18  HIS A C   
125  O  O   . HIS A 18  ? 0.5110 0.2432 0.2340 0.1416  -0.1020 -0.0884 18  HIS A O   
126  C  CB  . HIS A 18  ? 0.5534 0.3364 0.1303 0.1202  -0.1203 -0.0950 18  HIS A CB  
127  C  CG  . HIS A 18  ? 0.4909 0.3446 0.1314 0.1113  -0.0622 -0.0547 18  HIS A CG  
128  N  ND1 . HIS A 18  ? 0.3967 0.3561 0.1314 0.1033  -0.0803 -0.0683 18  HIS A ND1 
129  C  CD2 . HIS A 18  ? 0.5433 0.3348 0.1349 0.0774  -0.0248 -0.0516 18  HIS A CD2 
130  C  CE1 . HIS A 18  ? 0.4482 0.3483 0.1331 0.0786  -0.0383 -0.0863 18  HIS A CE1 
131  N  NE2 . HIS A 18  ? 0.4362 0.3476 0.1327 0.0819  -0.0257 -0.0968 18  HIS A NE2 
132  N  N   . LYS A 19  ? 0.5447 0.1887 0.1337 0.1237  -0.1292 -0.0807 19  LYS A N   
133  C  CA  . LYS A 19  ? 0.5506 0.1831 0.1473 0.1159  -0.0994 -0.0610 19  LYS A CA  
134  C  C   . LYS A 19  ? 0.5816 0.1776 0.1518 0.0388  -0.1094 -0.0388 19  LYS A C   
135  O  O   . LYS A 19  ? 0.5456 0.2215 0.0984 0.0643  0.0203  -0.0021 19  LYS A O   
136  C  CB  . LYS A 19  ? 0.5596 0.1715 0.2881 0.1088  -0.0677 -0.0651 19  LYS A CB  
137  C  CG  . LYS A 19  ? 0.6822 0.2078 0.3561 -0.0348 -0.0316 0.0054  19  LYS A CG  
138  C  CD  . LYS A 19  ? 0.7941 0.2044 0.4036 -0.0488 -0.0461 0.0053  19  LYS A CD  
139  C  CE  . LYS A 19  ? 0.9242 0.2054 0.4078 -0.1648 -0.0314 -0.0263 19  LYS A CE  
140  N  NZ  . LYS A 19  ? 1.1276 0.4437 0.4591 -0.4079 0.0458  -0.0270 19  LYS A NZ  
141  N  N   . LEU A 20  ? 0.5157 0.1266 0.1638 0.0305  -0.0560 -0.0655 20  LEU A N   
142  C  CA  . LEU A 20  ? 0.4966 0.1687 0.1710 0.0235  0.0012  -0.0512 20  LEU A CA  
143  C  C   . LEU A 20  ? 0.5200 0.1681 0.1312 0.0117  0.0214  -0.0590 20  LEU A C   
144  O  O   . LEU A 20  ? 0.5580 0.1690 0.1675 0.0471  -0.0322 -0.0361 20  LEU A O   
145  C  CB  . LEU A 20  ? 0.4842 0.1502 0.1706 -0.0096 0.0379  -0.0735 20  LEU A CB  
146  C  CG  . LEU A 20  ? 0.3877 0.1707 0.1872 -0.0007 0.0517  -0.0445 20  LEU A CG  
147  C  CD1 . LEU A 20  ? 0.3612 0.1964 0.1793 0.0501  -0.0112 -0.0553 20  LEU A CD1 
148  C  CD2 . LEU A 20  ? 0.4124 0.1576 0.1627 -0.0123 0.0194  -0.0145 20  LEU A CD2 
149  N  N   . PRO A 21  ? 0.5117 0.2069 0.1226 -0.0019 0.0220  -0.0253 21  PRO A N   
150  C  CA  . PRO A 21  ? 0.5338 0.2305 0.1434 -0.0281 0.0303  -0.0473 21  PRO A CA  
151  C  C   . PRO A 21  ? 0.5472 0.2180 0.1614 -0.0273 -0.0091 0.0338  21  PRO A C   
152  O  O   . PRO A 21  ? 0.4867 0.1667 0.1850 -0.0093 0.0172  -0.0324 21  PRO A O   
153  C  CB  . PRO A 21  ? 0.5120 0.2467 0.1589 -0.0142 0.0565  -0.0619 21  PRO A CB  
154  C  CG  . PRO A 21  ? 0.4826 0.2508 0.1396 -0.0093 0.0057  0.0252  21  PRO A CG  
155  C  CD  . PRO A 21  ? 0.4566 0.2280 0.1345 0.0243  0.0420  -0.0252 21  PRO A CD  
156  N  N   . ASP A 22  ? 0.5303 0.2313 0.1638 -0.0407 -0.0118 -0.0060 22  ASP A N   
157  C  CA  . ASP A 22  ? 0.5928 0.2216 0.1688 -0.0496 -0.0626 -0.0036 22  ASP A CA  
158  C  C   . ASP A 22  ? 0.5469 0.1904 0.1728 -0.0154 0.0014  -0.0499 22  ASP A C   
159  O  O   . ASP A 22  ? 0.7484 0.1630 0.1892 0.0105  -0.0734 -0.0311 22  ASP A O   
160  C  CB  . ASP A 22  ? 0.8175 0.2651 0.1711 -0.1982 -0.1151 0.0508  22  ASP A CB  
161  C  CG  . ASP A 22  ? 0.8469 0.4271 0.2258 -0.3289 -0.0885 0.0455  22  ASP A CG  
162  O  OD1 . ASP A 22  ? 0.7230 0.5241 0.2391 -0.2404 -0.0758 0.0870  22  ASP A OD1 
163  O  OD2 . ASP A 22  ? 0.8750 0.6535 0.2395 -0.4561 -0.0710 0.0144  22  ASP A OD2 
164  N  N   . ASN A 23  ? 0.5125 0.1982 0.1867 -0.0562 -0.0157 -0.0054 23  ASN A N   
165  C  CA  . ASN A 23  ? 0.4736 0.1915 0.1903 -0.0938 0.0124  -0.0553 23  ASN A CA  
166  C  C   . ASN A 23  ? 0.4568 0.2005 0.1866 -0.0832 0.0070  -0.0592 23  ASN A C   
167  O  O   . ASN A 23  ? 0.4182 0.2501 0.1854 -0.1073 -0.0182 -0.0142 23  ASN A O   
168  C  CB  . ASN A 23  ? 0.4560 0.2031 0.2571 -0.0818 -0.0272 -0.0626 23  ASN A CB  
169  C  CG  . ASN A 23  ? 0.4656 0.1963 0.2594 -0.0788 -0.0047 -0.0233 23  ASN A CG  
170  O  OD1 . ASN A 23  ? 0.5549 0.2109 0.2576 0.0000  0.0423  -0.0634 23  ASN A OD1 
171  N  ND2 . ASN A 23  ? 0.4290 0.2071 0.2642 -0.0513 0.1122  -0.0499 23  ASN A ND2 
172  N  N   . TYR A 24  ? 0.4007 0.1605 0.1651 -0.0157 0.0510  -0.0527 24  TYR A N   
173  C  CA  . TYR A 24  ? 0.3418 0.1626 0.1332 0.0420  -0.0198 -0.0428 24  TYR A CA  
174  C  C   . TYR A 24  ? 0.3492 0.1636 0.1722 0.0721  -0.0824 -0.0361 24  TYR A C   
175  O  O   . TYR A 24  ? 0.3931 0.1534 0.1823 0.0841  -0.0639 -0.0413 24  TYR A O   
176  C  CB  . TYR A 24  ? 0.2821 0.1647 0.1496 0.0474  -0.0018 -0.0661 24  TYR A CB  
177  C  CG  . TYR A 24  ? 0.2806 0.1633 0.1025 0.0268  0.0052  -0.0678 24  TYR A CG  
178  C  CD1 . TYR A 24  ? 0.2429 0.1669 0.0991 -0.0048 0.0125  -0.0078 24  TYR A CD1 
179  C  CD2 . TYR A 24  ? 0.3279 0.1404 0.0841 0.0254  0.0048  -0.0150 24  TYR A CD2 
180  C  CE1 . TYR A 24  ? 0.2602 0.1635 0.1021 0.0082  0.0126  -0.0277 24  TYR A CE1 
181  C  CE2 . TYR A 24  ? 0.3428 0.1376 0.0880 0.0398  -0.0315 -0.0046 24  TYR A CE2 
182  C  CZ  . TYR A 24  ? 0.2802 0.1481 0.0849 0.0487  -0.0062 0.0115  24  TYR A CZ  
183  O  OH  . TYR A 24  ? 0.3084 0.1407 0.1018 0.0304  0.0245  0.0219  24  TYR A OH  
184  N  N   . ILE A 25  ? 0.2495 0.1780 0.1825 0.0934  -0.0857 -0.0596 25  ILE A N   
185  C  CA  . ILE A 25  ? 0.2836 0.1483 0.2223 0.0477  -0.1075 -0.0734 25  ILE A CA  
186  C  C   . ILE A 25  ? 0.2522 0.1550 0.2085 0.0746  -0.0981 -0.0832 25  ILE A C   
187  O  O   . ILE A 25  ? 0.2508 0.1482 0.2374 0.0371  -0.0427 -0.0924 25  ILE A O   
188  C  CB  . ILE A 25  ? 0.3297 0.1421 0.2209 0.0449  -0.0557 -0.0615 25  ILE A CB  
189  C  CG1 . ILE A 25  ? 0.3319 0.1448 0.2257 -0.0047 0.0046  -0.1044 25  ILE A CG1 
190  C  CG2 . ILE A 25  ? 0.4680 0.1350 0.2283 -0.0171 -0.1049 -0.0157 25  ILE A CG2 
191  C  CD1 . ILE A 25  ? 0.3483 0.1283 0.2660 -0.0715 0.0252  -0.0645 25  ILE A CD1 
192  N  N   . THR A 26  ? 0.2518 0.1661 0.2492 0.0666  -0.0909 -0.1255 26  THR A N   
193  C  CA  . THR A 26  ? 0.2754 0.2230 0.2590 0.0197  -0.0828 -0.1267 26  THR A CA  
194  C  C   . THR A 26  ? 0.2152 0.1571 0.2602 0.0433  -0.0975 -0.0947 26  THR A C   
195  O  O   . THR A 26  ? 0.2045 0.1583 0.2751 0.0240  -0.0684 -0.1065 26  THR A O   
196  C  CB  . THR A 26  ? 0.2472 0.2555 0.2222 0.0485  -0.1098 -0.1961 26  THR A CB  
197  O  OG1 . THR A 26  ? 0.2484 0.2553 0.3048 0.0697  -0.1462 -0.1395 26  THR A OG1 
198  C  CG2 . THR A 26  ? 0.2965 0.3567 0.2246 -0.0087 -0.0938 -0.1713 26  THR A CG2 
199  N  N   . LYS A 27  ? 0.2207 0.1512 0.2730 0.0298  -0.0743 -0.1046 27  LYS A N   
200  C  CA  . LYS A 27  ? 0.1538 0.1888 0.2687 -0.0039 -0.0378 -0.0712 27  LYS A CA  
201  C  C   . LYS A 27  ? 0.1735 0.1929 0.2429 -0.0039 -0.0368 -0.0799 27  LYS A C   
202  O  O   . LYS A 27  ? 0.2291 0.2126 0.2049 0.0061  -0.0489 -0.0940 27  LYS A O   
203  C  CB  . LYS A 27  ? 0.2155 0.1958 0.2930 -0.0446 0.0187  -0.1105 27  LYS A CB  
204  C  CG  . LYS A 27  ? 0.3543 0.1774 0.3904 0.0511  -0.0324 -0.0857 27  LYS A CG  
205  C  CD  . LYS A 27  ? 0.4868 0.1775 0.4449 -0.0265 0.0106  -0.1032 27  LYS A CD  
206  C  CE  . LYS A 27  ? 0.5460 0.2908 0.4600 -0.1136 0.0112  -0.1251 27  LYS A CE  
207  N  NZ  . LYS A 27  ? 0.7357 0.3978 0.3576 -0.1922 0.0341  -0.1361 27  LYS A NZ  
208  N  N   . SER A 28  ? 0.1722 0.1812 0.2761 0.0250  -0.0483 -0.1056 28  SER A N   
209  C  CA  . SER A 28  ? 0.1841 0.1893 0.3441 0.0403  -0.0011 -0.1316 28  SER A CA  
210  C  C   . SER A 28  ? 0.1579 0.1746 0.2818 0.0708  -0.0610 -0.0991 28  SER A C   
211  O  O   . SER A 28  ? 0.2227 0.1765 0.2637 0.0738  -0.0613 -0.1400 28  SER A O   
212  C  CB  A SER A 28  ? 0.1234 0.2258 0.4372 0.0743  -0.0108 -0.0937 28  SER A CB  
213  C  CB  B SER A 28  ? 0.1283 0.2090 0.4347 0.0770  -0.0126 -0.0909 28  SER A CB  
214  O  OG  A SER A 28  ? 0.1731 0.2012 0.4916 0.0133  0.0174  -0.1421 28  SER A OG  
215  O  OG  B SER A 28  ? 0.2485 0.3380 0.5005 -0.0842 -0.0129 -0.0368 28  SER A OG  
216  N  N   . GLU A 29  ? 0.2015 0.1651 0.2629 0.0662  -0.0870 -0.0340 29  GLU A N   
217  C  CA  . GLU A 29  ? 0.2136 0.1485 0.2083 0.0708  -0.0897 -0.0557 29  GLU A CA  
218  C  C   . GLU A 29  ? 0.2300 0.1176 0.1917 0.0590  -0.0590 -0.0287 29  GLU A C   
219  O  O   . GLU A 29  ? 0.2546 0.1089 0.1596 0.0628  -0.0371 -0.0019 29  GLU A O   
220  C  CB  . GLU A 29  ? 0.3279 0.2706 0.1871 0.0589  -0.1262 -0.0580 29  GLU A CB  
221  C  CG  . GLU A 29  ? 0.3046 0.3493 0.2021 0.0905  -0.0746 -0.0639 29  GLU A CG  
222  C  CD  . GLU A 29  ? 0.4157 0.3543 0.1824 0.1388  -0.0674 -0.0357 29  GLU A CD  
223  O  OE1 . GLU A 29  ? 0.4147 0.3480 0.1789 0.1318  -0.0810 -0.0139 29  GLU A OE1 
224  O  OE2 . GLU A 29  ? 0.5840 0.3084 0.2107 0.1795  -0.0346 -0.0005 29  GLU A OE2 
225  N  N   . ALA A 30  ? 0.2572 0.1116 0.1476 0.0385  -0.0546 -0.0481 30  ALA A N   
226  C  CA  . ALA A 30  ? 0.2512 0.1153 0.1308 0.0446  -0.0655 -0.0309 30  ALA A CA  
227  C  C   . ALA A 30  ? 0.1882 0.1214 0.1439 0.0407  -0.0448 -0.0265 30  ALA A C   
228  O  O   . ALA A 30  ? 0.2185 0.1351 0.1196 0.0127  -0.0326 -0.0251 30  ALA A O   
229  C  CB  . ALA A 30  ? 0.2462 0.1147 0.1213 0.0307  -0.0231 -0.0283 30  ALA A CB  
230  N  N   . GLN A 31  ? 0.2144 0.1407 0.1606 0.0121  -0.0371 -0.0346 31  GLN A N   
231  C  CA  . GLN A 31  ? 0.1796 0.1359 0.1720 0.0125  0.0071  -0.0248 31  GLN A CA  
232  C  C   . GLN A 31  ? 0.2106 0.1395 0.1601 0.0181  -0.0032 -0.0322 31  GLN A C   
233  O  O   . GLN A 31  ? 0.2114 0.1339 0.1604 0.0161  -0.0002 -0.0865 31  GLN A O   
234  C  CB  A GLN A 31  ? 0.1909 0.1620 0.2145 -0.0088 0.0497  -0.0078 31  GLN A CB  
235  C  CB  B GLN A 31  ? 0.1882 0.1655 0.2147 -0.0082 0.0454  -0.0055 31  GLN A CB  
236  C  CG  A GLN A 31  ? 0.2796 0.1558 0.2569 -0.0412 0.0366  0.0184  31  GLN A CG  
237  C  CG  B GLN A 31  ? 0.3092 0.1561 0.2609 -0.0588 0.0456  0.0145  31  GLN A CG  
238  C  CD  A GLN A 31  ? 0.3565 0.1894 0.2703 -0.1128 0.0836  0.0069  31  GLN A CD  
239  C  CD  B GLN A 31  ? 0.3740 0.2001 0.2774 -0.1266 0.0983  0.0026  31  GLN A CD  
240  O  OE1 A GLN A 31  ? 0.3286 0.2444 0.2864 -0.1369 -0.0139 0.0067  31  GLN A OE1 
241  O  OE1 B GLN A 31  ? 0.2923 0.2758 0.2820 -0.0829 0.0886  -0.0181 31  GLN A OE1 
242  N  NE2 A GLN A 31  ? 0.4955 0.2396 0.2426 -0.1939 0.0968  0.0079  31  GLN A NE2 
243  N  NE2 B GLN A 31  ? 0.5679 0.2435 0.2460 -0.2617 0.0373  -0.0057 31  GLN A NE2 
244  N  N   . ALA A 32  ? 0.2103 0.1382 0.1604 0.0214  -0.0127 -0.0378 32  ALA A N   
245  C  CA  . ALA A 32  ? 0.2464 0.1358 0.1635 0.0197  -0.0515 -0.0130 32  ALA A CA  
246  C  C   . ALA A 32  ? 0.2213 0.1229 0.1559 0.0461  -0.0474 -0.0764 32  ALA A C   
247  O  O   . ALA A 32  ? 0.2460 0.1227 0.1383 0.0431  -0.0035 -0.0590 32  ALA A O   
248  C  CB  . ALA A 32  ? 0.2250 0.1375 0.1926 0.0303  -0.0457 -0.0147 32  ALA A CB  
249  N  N   . LEU A 33  ? 0.2149 0.1485 0.1094 0.0503  -0.0164 -0.0301 33  LEU A N   
250  C  CA  . LEU A 33  ? 0.2191 0.1334 0.1151 0.0450  -0.0095 -0.0170 33  LEU A CA  
251  C  C   . LEU A 33  ? 0.2283 0.1092 0.1176 0.0214  -0.0272 -0.0329 33  LEU A C   
252  O  O   . LEU A 33  ? 0.2747 0.1286 0.1313 -0.0302 -0.0127 -0.0198 33  LEU A O   
253  C  CB  . LEU A 33  ? 0.2109 0.1581 0.1143 0.0525  -0.0108 -0.0259 33  LEU A CB  
254  C  CG  . LEU A 33  ? 0.3011 0.1611 0.1131 0.0349  -0.0160 -0.0589 33  LEU A CG  
255  C  CD1 . LEU A 33  ? 0.3764 0.1562 0.1118 0.0255  0.0442  -0.0283 33  LEU A CD1 
256  C  CD2 . LEU A 33  ? 0.5195 0.1464 0.1373 -0.0009 -0.0314 -0.0259 33  LEU A CD2 
257  N  N   . GLY A 34  ? 0.1762 0.1233 0.1127 0.0272  -0.0216 -0.0238 34  GLY A N   
258  C  CA  . GLY A 34  ? 0.1947 0.1134 0.1136 0.0186  -0.0185 -0.0208 34  GLY A CA  
259  C  C   . GLY A 34  ? 0.1560 0.1111 0.1025 -0.0197 -0.0287 -0.0382 34  GLY A C   
260  O  O   . GLY A 34  ? 0.1571 0.1359 0.0862 -0.0123 0.0000  -0.0288 34  GLY A O   
261  N  N   . TRP A 35  ? 0.1779 0.1069 0.0944 -0.0052 -0.0259 0.0080  35  TRP A N   
262  C  CA  . TRP A 35  ? 0.1564 0.1113 0.1134 0.0080  -0.0255 -0.0059 35  TRP A CA  
263  C  C   . TRP A 35  ? 0.1578 0.0896 0.1237 -0.0028 -0.0335 0.0010  35  TRP A C   
264  O  O   . TRP A 35  ? 0.1502 0.1352 0.1693 -0.0131 -0.0220 -0.0351 35  TRP A O   
265  C  CB  . TRP A 35  ? 0.1764 0.1039 0.1155 0.0206  -0.0017 -0.0312 35  TRP A CB  
266  C  CG  . TRP A 35  ? 0.1571 0.1070 0.1465 0.0178  -0.0157 -0.0214 35  TRP A CG  
267  C  CD1 . TRP A 35  ? 0.1595 0.1028 0.1768 0.0085  -0.0263 -0.0181 35  TRP A CD1 
268  C  CD2 . TRP A 35  ? 0.1827 0.1144 0.0921 -0.0052 -0.0155 -0.0116 35  TRP A CD2 
269  N  NE1 . TRP A 35  ? 0.1679 0.1084 0.1567 0.0130  -0.0311 -0.0187 35  TRP A NE1 
270  C  CE2 . TRP A 35  ? 0.1961 0.1093 0.1186 -0.0157 -0.0027 -0.0167 35  TRP A CE2 
271  C  CE3 . TRP A 35  ? 0.1637 0.1347 0.1338 0.0069  -0.0102 -0.0091 35  TRP A CE3 
272  C  CZ2 . TRP A 35  ? 0.2225 0.1100 0.1729 -0.0199 0.0018  -0.0084 35  TRP A CZ2 
273  C  CZ3 . TRP A 35  ? 0.1811 0.1588 0.2173 -0.0356 -0.0679 0.0064  35  TRP A CZ3 
274  C  CH2 . TRP A 35  ? 0.2530 0.1265 0.1830 -0.0703 0.0406  0.0151  35  TRP A CH2 
275  N  N   . VAL A 36  ? 0.1572 0.1226 0.1117 -0.0038 0.0291  -0.0027 36  VAL A N   
276  C  CA  . VAL A 36  ? 0.1852 0.1461 0.1033 -0.0094 0.0099  0.0258  36  VAL A CA  
277  C  C   . VAL A 36  ? 0.1589 0.1475 0.0782 -0.0013 -0.0382 0.0315  36  VAL A C   
278  O  O   . VAL A 36  ? 0.1625 0.1614 0.1322 -0.0120 -0.0332 0.0269  36  VAL A O   
279  C  CB  . VAL A 36  ? 0.2451 0.1421 0.1128 0.0121  0.0078  0.0655  36  VAL A CB  
280  C  CG1 . VAL A 36  ? 0.3094 0.1813 0.0924 0.0642  -0.0004 0.0236  36  VAL A CG1 
281  C  CG2 . VAL A 36  ? 0.2969 0.1422 0.1573 0.0316  0.0947  0.0371  36  VAL A CG2 
282  N  N   . ALA A 37  ? 0.1518 0.1494 0.1344 -0.0028 -0.0083 -0.0021 37  ALA A N   
283  C  CA  . ALA A 37  ? 0.1796 0.1419 0.1301 -0.0150 -0.0029 0.0254  37  ALA A CA  
284  C  C   . ALA A 37  ? 0.1902 0.1412 0.1205 0.0120  0.0269  -0.0263 37  ALA A C   
285  O  O   . ALA A 37  ? 0.1960 0.1370 0.0923 -0.0091 0.0178  0.0134  37  ALA A O   
286  C  CB  . ALA A 37  ? 0.1918 0.1561 0.1997 -0.0327 -0.0259 0.0283  37  ALA A CB  
287  N  N   . SER A 38  ? 0.1582 0.1543 0.1259 0.0313  -0.0225 -0.0148 38  SER A N   
288  C  CA  . SER A 38  ? 0.1815 0.1682 0.1210 0.0204  -0.0111 0.0127  38  SER A CA  
289  C  C   . SER A 38  ? 0.1608 0.1884 0.1228 0.0297  -0.0296 0.0014  38  SER A C   
290  O  O   . SER A 38  ? 0.2007 0.2016 0.1085 -0.0060 -0.0283 0.0251  38  SER A O   
291  C  CB  A SER A 38  ? 0.1801 0.1851 0.1254 0.0075  -0.0012 -0.0081 38  SER A CB  
292  C  CB  B SER A 38  ? 0.1740 0.1553 0.1272 0.0242  -0.0016 -0.0080 38  SER A CB  
293  O  OG  A SER A 38  ? 0.1967 0.1529 0.1235 0.0104  0.0435  -0.0206 38  SER A OG  
294  O  OG  B SER A 38  ? 0.2115 0.1444 0.1822 -0.0057 0.0296  -0.0097 38  SER A OG  
295  N  N   . LYS A 39  ? 0.1917 0.1983 0.1156 -0.0092 -0.0199 -0.0182 39  LYS A N   
296  C  CA  . LYS A 39  ? 0.1898 0.2195 0.1331 -0.0144 -0.0392 -0.0012 39  LYS A CA  
297  C  C   . LYS A 39  ? 0.2192 0.2135 0.1291 -0.0552 -0.0564 0.0408  39  LYS A C   
298  O  O   . LYS A 39  ? 0.1798 0.1558 0.1751 -0.0015 -0.0273 -0.0158 39  LYS A O   
299  C  CB  . LYS A 39  ? 0.2198 0.2151 0.2500 -0.0132 0.0284  -0.0637 39  LYS A CB  
300  C  CG  . LYS A 39  ? 0.2632 0.2017 0.2486 0.0071  0.0503  -0.0991 39  LYS A CG  
301  C  CD  . LYS A 39  ? 0.3744 0.1958 0.3547 0.0251  0.0756  -0.1305 39  LYS A CD  
302  C  CE  . LYS A 39  ? 0.5426 0.1818 0.3603 0.0433  -0.0209 -0.0747 39  LYS A CE  
303  N  NZ  . LYS A 39  ? 0.9188 0.1879 0.4410 -0.0299 -0.0931 -0.1441 39  LYS A NZ  
304  N  N   . GLY A 40  ? 0.1458 0.1475 0.1589 0.0167  0.0172  0.0134  40  GLY A N   
305  C  CA  . GLY A 40  ? 0.1481 0.1329 0.1704 0.0135  0.0029  0.0433  40  GLY A CA  
306  C  C   . GLY A 40  ? 0.1976 0.1299 0.1430 -0.0174 -0.0127 0.0218  40  GLY A C   
307  O  O   . GLY A 40  ? 0.1853 0.1302 0.1395 0.0107  -0.0066 0.0328  40  GLY A O   
308  N  N   . ASN A 41  ? 0.1528 0.1449 0.0960 -0.0145 -0.0032 0.0320  41  ASN A N   
309  C  CA  . ASN A 41  ? 0.1478 0.1313 0.0916 -0.0203 -0.0016 0.0166  41  ASN A CA  
310  C  C   . ASN A 41  ? 0.1407 0.1106 0.0973 -0.0035 0.0262  -0.0140 41  ASN A C   
311  O  O   . ASN A 41  ? 0.2029 0.1076 0.1112 -0.0119 0.0182  0.0000  41  ASN A O   
312  C  CB  . ASN A 41  ? 0.1658 0.1439 0.0865 -0.0289 -0.0293 -0.0123 41  ASN A CB  
313  C  CG  . ASN A 41  ? 0.1769 0.1031 0.1388 -0.0259 -0.0238 0.0047  41  ASN A CG  
314  O  OD1 . ASN A 41  ? 0.1565 0.1257 0.1399 -0.0195 0.0275  -0.0219 41  ASN A OD1 
315  N  ND2 . ASN A 41  ? 0.2260 0.1108 0.1880 0.0437  0.0167  -0.0354 41  ASN A ND2 
316  N  N   . LEU A 42  ? 0.2124 0.1067 0.0899 0.0056  0.0029  -0.0196 42  LEU A N   
317  C  CA  . LEU A 42  ? 0.2021 0.1145 0.0872 0.0314  -0.0239 -0.0098 42  LEU A CA  
318  C  C   . LEU A 42  ? 0.2325 0.1014 0.0966 0.0047  0.0184  -0.0006 42  LEU A C   
319  O  O   . LEU A 42  ? 0.2565 0.0993 0.1162 0.0071  0.0066  0.0023  42  LEU A O   
320  C  CB  . LEU A 42  ? 0.1916 0.1456 0.1034 -0.0086 -0.0057 -0.0676 42  LEU A CB  
321  C  CG  . LEU A 42  ? 0.1607 0.1670 0.1035 -0.0190 0.0082  -0.0615 42  LEU A CG  
322  C  CD1 . LEU A 42  ? 0.1750 0.1650 0.1312 0.0382  -0.0160 -0.0229 42  LEU A CD1 
323  C  CD2 . LEU A 42  ? 0.2216 0.1528 0.1004 0.0301  -0.0159 -0.0542 42  LEU A CD2 
324  N  N   . ALA A 43  ? 0.2323 0.1095 0.1259 0.0034  0.0537  0.0071  43  ALA A N   
325  C  CA  . ALA A 43  ? 0.2192 0.1248 0.1775 -0.0062 0.0509  -0.0013 43  ALA A CA  
326  C  C   . ALA A 43  ? 0.2043 0.1225 0.2020 0.0028  0.0180  0.0184  43  ALA A C   
327  O  O   . ALA A 43  ? 0.2917 0.1594 0.2096 -0.0762 0.0461  -0.0016 43  ALA A O   
328  C  CB  . ALA A 43  ? 0.2103 0.1296 0.2689 0.0284  0.0904  0.0139  43  ALA A CB  
329  N  N   . ASP A 44  ? 0.2001 0.1217 0.2046 0.0315  0.0569  0.0126  44  ASP A N   
330  C  CA  . ASP A 44  ? 0.1911 0.1236 0.2006 0.0146  0.0046  0.0117  44  ASP A CA  
331  C  C   . ASP A 44  ? 0.1860 0.1212 0.2418 0.0216  0.0126  0.0000  44  ASP A C   
332  O  O   . ASP A 44  ? 0.2268 0.1229 0.1932 0.0068  -0.0088 0.0174  44  ASP A O   
333  C  CB  . ASP A 44  ? 0.3512 0.2338 0.1838 -0.0384 -0.0190 0.0563  44  ASP A CB  
334  C  CG  . ASP A 44  ? 0.3727 0.2337 0.1541 0.0033  0.0441  0.0716  44  ASP A CG  
335  O  OD1 . ASP A 44  ? 0.2610 0.3437 0.4115 0.0593  -0.0432 0.0062  44  ASP A OD1 
336  O  OD2 . ASP A 44  ? 0.5978 0.3216 0.1344 0.0711  -0.0510 0.0517  44  ASP A OD2 
337  N  N   . VAL A 45  ? 0.1906 0.1091 0.1325 0.0263  0.0091  -0.0238 45  VAL A N   
338  C  CA  . VAL A 45  ? 0.2035 0.1103 0.1295 -0.0058 0.0471  -0.0360 45  VAL A CA  
339  C  C   . VAL A 45  ? 0.1886 0.1149 0.1234 0.0024  0.0207  -0.0504 45  VAL A C   
340  O  O   . VAL A 45  ? 0.2021 0.1336 0.1308 0.0522  -0.0151 -0.0092 45  VAL A O   
341  C  CB  . VAL A 45  ? 0.1811 0.1211 0.1167 0.0335  0.0009  0.0161  45  VAL A CB  
342  C  CG1 . VAL A 45  ? 0.3342 0.1760 0.1035 0.0834  0.0224  0.0464  45  VAL A CG1 
343  C  CG2 . VAL A 45  ? 0.2764 0.1655 0.1810 -0.0796 0.0616  -0.0315 45  VAL A CG2 
344  N  N   . ALA A 46  ? 0.2363 0.1124 0.1257 0.0036  0.0201  -0.0448 46  ALA A N   
345  C  CA  . ALA A 46  ? 0.2686 0.1163 0.1205 -0.0211 -0.0053 -0.0075 46  ALA A CA  
346  C  C   . ALA A 46  ? 0.2361 0.1327 0.1205 0.0008  0.0019  -0.0102 46  ALA A C   
347  O  O   . ALA A 46  ? 0.2315 0.1294 0.1311 -0.0013 0.0389  -0.0031 46  ALA A O   
348  C  CB  . ALA A 46  ? 0.2314 0.1583 0.1275 -0.0059 0.0056  -0.0529 46  ALA A CB  
349  N  N   . PRO A 47  ? 0.2665 0.1556 0.1903 -0.0399 0.0524  -0.0468 47  PRO A N   
350  C  CA  . PRO A 47  ? 0.2486 0.1794 0.1966 -0.0412 0.0376  -0.0066 47  PRO A CA  
351  C  C   . PRO A 47  ? 0.2347 0.1953 0.1921 -0.0349 0.0444  -0.0105 47  PRO A C   
352  O  O   . PRO A 47  ? 0.3282 0.1678 0.1922 -0.0378 0.0653  -0.0234 47  PRO A O   
353  C  CB  . PRO A 47  ? 0.2849 0.2084 0.2235 -0.0815 0.0472  -0.0594 47  PRO A CB  
354  C  CG  . PRO A 47  ? 0.3148 0.1766 0.2953 -0.0823 0.0594  -0.0386 47  PRO A CG  
355  C  CD  . PRO A 47  ? 0.2985 0.1493 0.2640 -0.0606 0.0501  -0.0776 47  PRO A CD  
356  N  N   . GLY A 48  ? 0.2343 0.1944 0.1782 -0.0441 0.0726  -0.0541 48  GLY A N   
357  C  CA  . GLY A 48  ? 0.2558 0.2013 0.1846 -0.0391 0.0749  -0.0910 48  GLY A CA  
358  C  C   . GLY A 48  ? 0.2979 0.1674 0.1766 -0.0716 0.0473  -0.0915 48  GLY A C   
359  O  O   . GLY A 48  ? 0.3618 0.2093 0.1561 -0.0829 0.1096  -0.0652 48  GLY A O   
360  N  N   . LYS A 49  ? 0.2851 0.1461 0.1848 -0.0469 0.1055  -0.0300 49  LYS A N   
361  C  CA  . LYS A 49  ? 0.2894 0.1548 0.1429 -0.0560 0.0117  -0.0178 49  LYS A CA  
362  C  C   . LYS A 49  ? 0.2802 0.1480 0.1610 -0.0356 -0.0099 -0.0117 49  LYS A C   
363  O  O   . LYS A 49  ? 0.2646 0.1283 0.1825 -0.0440 0.0268  -0.0360 49  LYS A O   
364  C  CB  . LYS A 49  ? 0.2931 0.1435 0.2258 -0.0525 0.0230  -0.0465 49  LYS A CB  
365  C  CG  . LYS A 49  ? 0.3967 0.1446 0.2193 -0.0215 -0.0344 -0.0150 49  LYS A CG  
366  C  CD  . LYS A 49  ? 0.5723 0.2146 0.2147 -0.0143 0.0479  0.0023  49  LYS A CD  
367  C  CE  . LYS A 49  ? 0.6596 0.2205 0.1825 0.0175  -0.0216 0.0438  49  LYS A CE  
368  N  NZ  . LYS A 49  ? 0.8450 0.3004 0.1772 -0.0868 0.0187  0.0193  49  LYS A NZ  
369  N  N   . SER A 50  ? 0.2821 0.1247 0.1227 -0.0090 0.0274  -0.0386 50  SER A N   
370  C  CA  . SER A 50  ? 0.2373 0.1328 0.1267 -0.0006 -0.0074 -0.0398 50  SER A CA  
371  C  C   . SER A 50  ? 0.2097 0.1453 0.1087 0.0315  -0.0484 -0.0196 50  SER A C   
372  O  O   . SER A 50  ? 0.2295 0.1666 0.1079 0.0160  -0.0067 -0.0078 50  SER A O   
373  C  CB  . SER A 50  ? 0.2212 0.1213 0.1877 0.0144  -0.0073 -0.0461 50  SER A CB  
374  O  OG  . SER A 50  ? 0.2052 0.1506 0.1911 0.0226  0.0064  0.0023  50  SER A OG  
375  N  N   . ILE A 51  ? 0.2276 0.1634 0.1121 -0.0078 0.0257  -0.0379 51  ILE A N   
376  C  CA  . ILE A 51  ? 0.2145 0.1421 0.1527 0.0129  0.0055  -0.0587 51  ILE A CA  
377  C  C   . ILE A 51  ? 0.2203 0.1302 0.1571 0.0100  -0.0007 -0.0351 51  ILE A C   
378  O  O   . ILE A 51  ? 0.2394 0.1316 0.1600 0.0237  0.0032  -0.0292 51  ILE A O   
379  C  CB  . ILE A 51  ? 0.1998 0.2074 0.1516 -0.0203 0.0523  -0.1030 51  ILE A CB  
380  C  CG1 . ILE A 51  ? 0.2719 0.1890 0.1652 -0.0612 0.0411  -0.0403 51  ILE A CG1 
381  C  CG2 . ILE A 51  ? 0.2033 0.2392 0.1899 -0.0306 -0.0132 -0.0747 51  ILE A CG2 
382  C  CD1 . ILE A 51  ? 0.2675 0.1811 0.2901 -0.0536 -0.0124 -0.0869 51  ILE A CD1 
383  N  N   . GLY A 52  ? 0.2472 0.1289 0.1252 0.0282  -0.0027 -0.0503 52  GLY A N   
384  C  CA  . GLY A 52  ? 0.2640 0.1506 0.1108 0.0396  0.0079  -0.0386 52  GLY A CA  
385  C  C   . GLY A 52  ? 0.2526 0.1483 0.1384 0.0479  -0.0536 -0.0233 52  GLY A C   
386  O  O   . GLY A 52  ? 0.2739 0.1398 0.2316 0.0117  -0.0779 -0.0490 52  GLY A O   
387  N  N   . GLY A 53  ? 0.2282 0.1315 0.2073 0.0576  -0.0694 -0.0711 53  GLY A N   
388  C  CA  . GLY A 53  ? 0.2127 0.1642 0.2387 0.0497  -0.1095 -0.0500 53  GLY A CA  
389  C  C   . GLY A 53  ? 0.2235 0.1994 0.2705 0.0228  -0.0747 -0.1143 53  GLY A C   
390  O  O   . GLY A 53  ? 0.2049 0.2724 0.2689 0.0133  -0.0695 -0.0767 53  GLY A O   
391  N  N   . ASP A 54  ? 0.2137 0.2644 0.2629 0.0309  0.0000  -0.1487 54  ASP A N   
392  C  CA  . ASP A 54  ? 0.2445 0.3085 0.2572 -0.0041 -0.0427 -0.1271 54  ASP A CA  
393  C  C   . ASP A 54  ? 0.2030 0.2955 0.2528 0.0243  -0.0200 -0.1599 54  ASP A C   
394  O  O   . ASP A 54  ? 0.1746 0.3184 0.2557 0.0813  -0.0376 -0.1448 54  ASP A O   
395  C  CB  . ASP A 54  ? 0.2666 0.2715 0.2550 0.0246  -0.0317 -0.1552 54  ASP A CB  
396  C  CG  . ASP A 54  ? 0.3326 0.2579 0.2803 0.0116  -0.0265 -0.1851 54  ASP A CG  
397  O  OD1 . ASP A 54  ? 0.2773 0.2730 0.5110 0.0158  -0.0982 -0.1926 54  ASP A OD1 
398  O  OD2 . ASP A 54  ? 0.3388 0.2334 0.3468 -0.0123 -0.0446 -0.1990 54  ASP A OD2 
399  N  N   . ILE A 55  ? 0.1996 0.2990 0.3340 0.0341  -0.0339 -0.1657 55  ILE A N   
400  C  CA  . ILE A 55  ? 0.2114 0.3136 0.3968 0.0081  0.0136  -0.1692 55  ILE A CA  
401  C  C   . ILE A 55  ? 0.2033 0.3082 0.3951 0.0120  0.1214  -0.2419 55  ILE A C   
402  O  O   . ILE A 55  ? 0.2939 0.2523 0.3997 -0.0338 0.1070  -0.1531 55  ILE A O   
403  C  CB  . ILE A 55  ? 0.2000 0.2984 0.4935 0.0360  -0.0055 -0.0698 55  ILE A CB  
404  C  CG1 . ILE A 55  ? 0.1840 0.3086 0.5306 0.0952  0.0194  -0.0210 55  ILE A CG1 
405  C  CG2 . ILE A 55  ? 0.2460 0.3230 0.5762 -0.0265 -0.0081 -0.1924 55  ILE A CG2 
406  C  CD1 . ILE A 55  ? 0.3057 0.4161 0.4751 0.0472  0.1111  -0.0281 55  ILE A CD1 
407  N  N   . PHE A 56  ? 0.1992 0.3221 0.3461 0.0328  0.0201  -0.1963 56  PHE A N   
408  C  CA  . PHE A 56  ? 0.2578 0.3055 0.3744 0.0206  0.0500  -0.1818 56  PHE A CA  
409  C  C   . PHE A 56  ? 0.2598 0.3117 0.4448 0.0168  0.1216  -0.1717 56  PHE A C   
410  O  O   . PHE A 56  ? 0.2106 0.3928 0.4513 -0.0212 0.0278  -0.2331 56  PHE A O   
411  C  CB  . PHE A 56  ? 0.2764 0.2914 0.3631 0.0039  -0.0305 -0.1039 56  PHE A CB  
412  C  CG  . PHE A 56  ? 0.2700 0.3000 0.3521 0.0212  -0.0209 -0.0332 56  PHE A CG  
413  C  CD1 . PHE A 56  ? 0.3018 0.3291 0.3440 0.0017  0.0061  -0.0087 56  PHE A CD1 
414  C  CD2 . PHE A 56  ? 0.2786 0.2930 0.3508 0.0434  -0.0327 0.0019  56  PHE A CD2 
415  C  CE1 . PHE A 56  ? 0.3755 0.3328 0.3130 -0.0102 0.0865  -0.0530 56  PHE A CE1 
416  C  CE2 . PHE A 56  ? 0.3433 0.3005 0.3296 0.0073  0.0202  -0.0202 56  PHE A CE2 
417  C  CZ  . PHE A 56  ? 0.3546 0.3281 0.3228 0.0039  0.0493  -0.0083 56  PHE A CZ  
418  N  N   . SER A 57  ? 0.2446 0.3397 0.4520 0.0185  0.1180  -0.0927 57  SER A N   
419  C  CA  . SER A 57  ? 0.2605 0.3571 0.4685 0.0017  0.1712  -0.0796 57  SER A CA  
420  C  C   . SER A 57  ? 0.3120 0.3447 0.5412 -0.0189 0.1789  -0.0308 57  SER A C   
421  O  O   . SER A 57  ? 0.3199 0.3228 0.6010 -0.0278 0.0990  0.0090  57  SER A O   
422  C  CB  . SER A 57  ? 0.3431 0.4435 0.4483 -0.0915 0.1913  -0.0800 57  SER A CB  
423  O  OG  . SER A 57  ? 0.5356 0.6505 0.4358 -0.2920 0.1694  -0.0891 57  SER A OG  
424  N  N   . ASN A 58  ? 0.2991 0.3478 0.5805 0.0064  0.1824  0.0052  58  ASN A N   
425  C  CA  . ASN A 58  ? 0.3812 0.3365 0.6168 -0.0086 0.1862  -0.0200 58  ASN A CA  
426  C  C   . ASN A 58  ? 0.3663 0.3308 0.6135 0.0108  0.1042  0.0499  58  ASN A C   
427  O  O   . ASN A 58  ? 0.3599 0.4291 0.5874 -0.0434 0.1651  0.0252  58  ASN A O   
428  C  CB  . ASN A 58  ? 0.3946 0.3054 0.6173 -0.0167 0.1861  -0.0599 58  ASN A CB  
429  C  CG  . ASN A 58  ? 0.3526 0.3075 0.6346 -0.0150 0.1213  -0.0762 58  ASN A CG  
430  O  OD1 . ASN A 58  ? 0.3373 0.3170 0.6308 -0.0459 0.1428  -0.0304 58  ASN A OD1 
431  N  ND2 . ASN A 58  ? 0.3100 0.2891 0.6502 -0.0194 -0.0041 -0.1538 58  ASN A ND2 
432  N  N   . ARG A 59  ? 0.3881 0.3572 0.6057 0.0216  0.1347  0.0275  59  ARG A N   
433  C  CA  . ARG A 59  ? 0.5219 0.3917 0.5827 -0.0781 0.1802  0.0034  59  ARG A CA  
434  C  C   . ARG A 59  ? 0.5787 0.3881 0.5897 -0.0720 0.2121  -0.0195 59  ARG A C   
435  O  O   . ARG A 59  ? 0.6041 0.3833 0.6481 -0.0883 0.3011  -0.1407 59  ARG A O   
436  C  CB  . ARG A 59  ? 0.5361 0.3893 0.5850 -0.0806 0.1802  0.0034  59  ARG A CB  
437  C  CG  . ARG A 59  ? 0.5341 0.3882 0.5844 -0.0789 0.1801  0.0034  59  ARG A CG  
438  C  CD  . ARG A 59  ? 0.5349 0.3869 0.5840 -0.0786 0.1801  0.0034  59  ARG A CD  
439  N  NE  . ARG A 59  ? 0.5345 0.3861 0.5844 -0.0784 0.1800  0.0034  59  ARG A NE  
440  C  CZ  . ARG A 59  ? 0.5348 0.3849 0.5842 -0.0781 0.1800  0.0034  59  ARG A CZ  
441  N  NH1 . ARG A 59  ? 0.5365 0.3843 0.5844 -0.0790 0.1800  0.0034  59  ARG A NH1 
442  N  NH2 . ARG A 59  ? 0.5338 0.3845 0.5843 -0.0770 0.1800  0.0034  59  ARG A NH2 
443  N  N   . GLU A 60  ? 0.5661 0.3917 0.6010 -0.0348 0.1967  -0.0026 60  GLU A N   
444  C  CA  . GLU A 60  ? 0.5778 0.3910 0.6146 -0.0499 0.1602  0.0220  60  GLU A CA  
445  C  C   . GLU A 60  ? 0.5505 0.3833 0.6176 -0.0516 0.1124  0.0541  60  GLU A C   
446  O  O   . GLU A 60  ? 0.5409 0.3828 0.6541 -0.0295 0.1693  -0.0130 60  GLU A O   
447  C  CB  . GLU A 60  ? 0.5633 0.4033 0.5880 -0.0231 0.1299  0.0094  60  GLU A CB  
448  C  CG  . GLU A 60  ? 0.6300 0.4678 0.5779 -0.0580 0.1573  -0.0253 60  GLU A CG  
449  C  CD  . GLU A 60  ? 0.6220 0.4832 0.5496 -0.0517 0.2103  -0.0732 60  GLU A CD  
450  O  OE1 . GLU A 60  ? 0.5674 0.4259 0.5617 0.0935  0.3723  -0.0661 60  GLU A OE1 
451  O  OE2 . GLU A 60  ? 0.6873 0.4265 0.5498 -0.0788 0.3761  -0.3048 60  GLU A OE2 
452  N  N   . GLY A 61  ? 0.3775 0.4015 0.6178 -0.0216 0.0832  0.0407  61  GLY A N   
453  C  CA  . GLY A 61  ? 0.3386 0.4297 0.6179 -0.0734 0.1027  0.0025  61  GLY A CA  
454  C  C   . GLY A 61  ? 0.3776 0.3921 0.5960 -0.0990 0.0447  0.0026  61  GLY A C   
455  O  O   . GLY A 61  ? 0.4088 0.3902 0.6011 -0.1723 0.0510  0.0517  61  GLY A O   
456  N  N   . LYS A 62  ? 0.3640 0.3213 0.4691 -0.0455 0.0740  -0.0218 62  LYS A N   
457  C  CA  . LYS A 62  ? 0.3733 0.3069 0.4528 -0.0331 0.0563  -0.0439 62  LYS A CA  
458  C  C   . LYS A 62  ? 0.3841 0.2895 0.4564 -0.0684 0.0861  -0.0753 62  LYS A C   
459  O  O   . LYS A 62  ? 0.3815 0.3083 0.4517 -0.0120 0.0221  -0.0074 62  LYS A O   
460  C  CB  . LYS A 62  ? 0.3337 0.3827 0.4560 -0.0218 0.0474  -0.0341 62  LYS A CB  
461  C  CG  . LYS A 62  ? 0.5506 0.4905 0.4470 -0.1584 0.0397  -0.0217 62  LYS A CG  
462  C  CD  . LYS A 62  ? 0.5458 0.5326 0.4092 -0.1564 0.0349  -0.0286 62  LYS A CD  
463  C  CE  . LYS A 62  ? 0.6851 0.5710 0.4032 -0.2224 0.0933  -0.0262 62  LYS A CE  
464  N  NZ  . LYS A 62  ? 0.7973 0.5893 0.3930 -0.2143 0.2369  0.0405  62  LYS A NZ  
465  N  N   . LEU A 63  ? 0.2526 0.3019 0.4458 -0.0675 0.0319  -0.0610 63  LEU A N   
466  C  CA  . LEU A 63  ? 0.2581 0.2859 0.4453 -0.0592 0.0268  -0.0959 63  LEU A CA  
467  C  C   . LEU A 63  ? 0.2413 0.2693 0.4489 -0.0365 -0.0192 -0.0786 63  LEU A C   
468  O  O   . LEU A 63  ? 0.2508 0.2302 0.5042 -0.0319 0.0346  -0.0661 63  LEU A O   
469  C  CB  . LEU A 63  ? 0.1813 0.2805 0.4165 -0.0104 -0.0420 -0.0820 63  LEU A CB  
470  C  CG  . LEU A 63  ? 0.1826 0.2689 0.4145 -0.0090 0.0100  -0.0811 63  LEU A CG  
471  C  CD1 . LEU A 63  ? 0.4286 0.2579 0.4646 -0.1065 -0.1357 -0.1115 63  LEU A CD1 
472  C  CD2 . LEU A 63  ? 0.1849 0.3669 0.2928 -0.0555 -0.0635 0.0128  63  LEU A CD2 
473  N  N   . PRO A 64  ? 0.2933 0.3123 0.4376 -0.0670 -0.0591 -0.1102 64  PRO A N   
474  C  CA  . PRO A 64  ? 0.3162 0.3229 0.4452 -0.0913 -0.0397 -0.1322 64  PRO A CA  
475  C  C   . PRO A 64  ? 0.2593 0.3542 0.5084 -0.0790 -0.0570 -0.1125 64  PRO A C   
476  O  O   . PRO A 64  ? 0.2318 0.3458 0.3896 -0.0294 -0.0229 -0.0411 64  PRO A O   
477  C  CB  . PRO A 64  ? 0.3274 0.3286 0.4367 -0.0862 -0.0522 -0.1180 64  PRO A CB  
478  C  CG  . PRO A 64  ? 0.3110 0.3379 0.4286 -0.0723 -0.0309 -0.1079 64  PRO A CG  
479  C  CD  . PRO A 64  ? 0.2792 0.2911 0.4233 -0.0246 -0.0247 -0.1188 64  PRO A CD  
480  N  N   . GLY A 65  ? 0.2451 0.4373 0.5801 -0.0858 -0.0739 -0.1094 65  GLY A N   
481  C  CA  . GLY A 65  ? 0.1962 0.4752 0.5909 -0.0520 -0.0776 -0.1045 65  GLY A CA  
482  C  C   . GLY A 65  ? 0.2207 0.4785 0.5819 -0.0660 -0.0767 -0.0815 65  GLY A C   
483  O  O   . GLY A 65  ? 0.4075 0.4703 0.5707 -0.0565 -0.1256 -0.1543 65  GLY A O   
484  N  N   . LYS A 66  ? 0.2824 0.4742 0.5482 -0.0633 -0.1242 -0.0076 66  LYS A N   
485  C  CA  . LYS A 66  ? 0.3074 0.4506 0.5491 -0.0677 -0.0910 -0.0337 66  LYS A CA  
486  C  C   . LYS A 66  ? 0.2803 0.4646 0.6083 -0.0471 -0.1480 -0.0295 66  LYS A C   
487  O  O   . LYS A 66  ? 0.2803 0.4636 0.5667 -0.0116 -0.1236 -0.0840 66  LYS A O   
488  C  CB  . LYS A 66  ? 0.3155 0.4529 0.5453 -0.0643 -0.0557 -0.0671 66  LYS A CB  
489  C  CG  . LYS A 66  ? 0.2416 0.4782 0.5506 -0.0456 -0.0745 -0.0693 66  LYS A CG  
490  C  CD  . LYS A 66  ? 0.2390 0.5081 0.5474 -0.0595 -0.0024 -0.0958 66  LYS A CD  
491  C  CE  . LYS A 66  ? 0.2400 0.5205 0.5511 -0.0849 0.0273  -0.1458 66  LYS A CE  
492  N  NZ  . LYS A 66  ? 0.2812 0.5398 0.5467 -0.1379 0.1840  -0.2614 66  LYS A NZ  
493  N  N   . SER A 67  ? 0.2865 0.4668 0.6911 -0.0734 -0.1354 -0.0323 67  SER A N   
494  C  CA  . SER A 67  ? 0.2615 0.4779 0.7482 -0.0576 -0.1624 -0.0511 67  SER A CA  
495  C  C   . SER A 67  ? 0.2758 0.4667 0.6940 -0.0545 -0.1762 -0.0581 67  SER A C   
496  O  O   . SER A 67  ? 0.2663 0.4252 0.6867 0.0422  -0.1574 -0.1281 67  SER A O   
497  C  CB  . SER A 67  ? 0.2459 0.5122 0.7814 -0.0595 -0.1201 -0.0614 67  SER A CB  
498  O  OG  . SER A 67  ? 0.4778 0.5122 0.8885 -0.2409 -0.1144 -0.1020 67  SER A OG  
499  N  N   . GLY A 68  ? 0.2725 0.4812 0.6238 -0.0680 -0.1530 -0.0735 68  GLY A N   
500  C  CA  . GLY A 68  ? 0.1940 0.4515 0.5267 0.0177  -0.1567 -0.0900 68  GLY A CA  
501  C  C   . GLY A 68  ? 0.2143 0.4054 0.4779 0.0004  -0.1603 -0.0616 68  GLY A C   
502  O  O   . GLY A 68  ? 0.2939 0.3887 0.5245 -0.0420 -0.1700 -0.0442 68  GLY A O   
503  N  N   . ARG A 69  ? 0.2330 0.4249 0.4074 -0.0299 -0.2120 -0.0879 69  ARG A N   
504  C  CA  . ARG A 69  ? 0.2674 0.3555 0.3636 -0.0392 -0.1261 -0.1038 69  ARG A CA  
505  C  C   . ARG A 69  ? 0.2485 0.3293 0.3637 0.0094  -0.1324 -0.0822 69  ARG A C   
506  O  O   . ARG A 69  ? 0.3185 0.3550 0.3636 -0.0586 -0.0462 -0.0443 69  ARG A O   
507  C  CB  . ARG A 69  ? 0.2926 0.3525 0.2927 -0.0322 -0.1197 -0.1287 69  ARG A CB  
508  C  CG  . ARG A 69  ? 0.2982 0.3160 0.2305 -0.0143 -0.1015 -0.1181 69  ARG A CG  
509  C  CD  . ARG A 69  ? 0.3373 0.3112 0.2507 -0.0242 -0.0738 -0.0643 69  ARG A CD  
510  N  NE  . ARG A 69  ? 0.2847 0.2980 0.2567 -0.0138 -0.0797 -0.0496 69  ARG A NE  
511  C  CZ  . ARG A 69  ? 0.2546 0.2943 0.2814 -0.0055 -0.1049 -0.0230 69  ARG A CZ  
512  N  NH1 . ARG A 69  ? 0.4083 0.2933 0.2849 -0.0721 -0.0531 0.0328  69  ARG A NH1 
513  N  NH2 . ARG A 69  ? 0.4363 0.2693 0.2821 -0.0399 -0.0888 -0.0647 69  ARG A NH2 
514  N  N   . THR A 70  ? 0.2012 0.3280 0.3444 0.0313  -0.0640 -0.0933 70  THR A N   
515  C  CA  . THR A 70  ? 0.1714 0.3226 0.3364 0.0677  -0.0222 -0.1205 70  THR A CA  
516  C  C   . THR A 70  ? 0.1898 0.3000 0.3387 0.0504  0.0241  -0.1667 70  THR A C   
517  O  O   . THR A 70  ? 0.1855 0.3206 0.3424 0.0441  -0.0662 -0.0942 70  THR A O   
518  C  CB  . THR A 70  ? 0.2056 0.3170 0.3850 0.1278  -0.0345 -0.1627 70  THR A CB  
519  O  OG1 . THR A 70  ? 0.2621 0.2818 0.5766 0.0649  -0.0085 -0.0736 70  THR A OG1 
520  C  CG2 . THR A 70  ? 0.3095 0.3168 0.3799 0.1047  0.0096  -0.0663 70  THR A CG2 
521  N  N   . TRP A 71  ? 0.2001 0.2329 0.3445 0.0183  -0.0421 -0.1680 71  TRP A N   
522  C  CA  . TRP A 71  ? 0.2150 0.2139 0.3577 0.0005  -0.0080 -0.1611 71  TRP A CA  
523  C  C   . TRP A 71  ? 0.1522 0.2191 0.3316 0.0485  -0.0587 -0.1274 71  TRP A C   
524  O  O   . TRP A 71  ? 0.1648 0.2515 0.2985 -0.0108 0.0156  -0.1512 71  TRP A O   
525  C  CB  . TRP A 71  ? 0.2278 0.2165 0.3275 0.0188  0.0347  -0.1592 71  TRP A CB  
526  C  CG  . TRP A 71  ? 0.1998 0.2195 0.3103 -0.0018 -0.0537 -0.0810 71  TRP A CG  
527  C  CD1 . TRP A 71  ? 0.1880 0.2354 0.3036 0.0072  -0.0421 -0.0885 71  TRP A CD1 
528  C  CD2 . TRP A 71  ? 0.2068 0.2342 0.2542 -0.0096 -0.0353 -0.1236 71  TRP A CD2 
529  N  NE1 . TRP A 71  ? 0.1959 0.2390 0.3001 -0.0079 0.0060  -0.1196 71  TRP A NE1 
530  C  CE2 . TRP A 71  ? 0.1785 0.2275 0.3003 0.0126  -0.0175 -0.1238 71  TRP A CE2 
531  C  CE3 . TRP A 71  ? 0.2147 0.2090 0.2222 -0.0018 -0.0355 -0.0495 71  TRP A CE3 
532  C  CZ2 . TRP A 71  ? 0.2266 0.2287 0.2619 -0.0142 -0.0839 -0.0480 71  TRP A CZ2 
533  C  CZ3 . TRP A 71  ? 0.2196 0.2060 0.2334 0.0048  -0.0532 -0.0342 71  TRP A CZ3 
534  C  CH2 . TRP A 71  ? 0.1962 0.2059 0.2388 0.0308  -0.0391 -0.0707 71  TRP A CH2 
535  N  N   . ARG A 72  ? 0.1882 0.2458 0.1928 -0.0047 -0.0757 -0.1112 72  ARG A N   
536  C  CA  . ARG A 72  ? 0.1712 0.2347 0.1743 0.0269  -0.0886 -0.0945 72  ARG A CA  
537  C  C   . ARG A 72  ? 0.2186 0.1812 0.1851 -0.0271 -0.0549 -0.1322 72  ARG A C   
538  O  O   . ARG A 72  ? 0.2272 0.1811 0.1646 0.0007  -0.0316 -0.1084 72  ARG A O   
539  C  CB  . ARG A 72  ? 0.2024 0.2295 0.1853 0.0557  -0.0883 -0.0931 72  ARG A CB  
540  C  CG  . ARG A 72  ? 0.2036 0.2230 0.2888 0.0869  -0.0660 -0.0461 72  ARG A CG  
541  C  CD  . ARG A 72  ? 0.3207 0.2007 0.3103 0.1219  -0.1029 -0.0713 72  ARG A CD  
542  N  NE  . ARG A 72  ? 0.3349 0.1917 0.4445 0.1732  -0.1265 -0.0610 72  ARG A NE  
543  C  CZ  . ARG A 72  ? 0.2124 0.2879 0.3811 0.1564  -0.0716 -0.0958 72  ARG A CZ  
544  N  NH1 . ARG A 72  ? 0.4225 0.3228 0.3733 0.0014  -0.1673 -0.0807 72  ARG A NH1 
545  N  NH2 . ARG A 72  ? 0.1718 0.3852 0.6505 0.0780  -0.0819 -0.0721 72  ARG A NH2 
546  N  N   . GLU A 73  ? 0.1634 0.1493 0.1965 0.0380  -0.0314 -0.0762 73  GLU A N   
547  C  CA  . GLU A 73  ? 0.1619 0.1523 0.2032 0.0172  -0.0240 -0.0628 73  GLU A CA  
548  C  C   . GLU A 73  ? 0.1746 0.1442 0.1848 0.0190  0.0040  -0.0747 73  GLU A C   
549  O  O   . GLU A 73  ? 0.1900 0.1437 0.1965 0.0231  -0.0303 -0.0720 73  GLU A O   
550  C  CB  . GLU A 73  ? 0.1821 0.1582 0.1998 0.0167  0.0184  -0.0628 73  GLU A CB  
551  C  CG  . GLU A 73  ? 0.2292 0.1520 0.2074 0.0259  -0.0168 -0.0291 73  GLU A CG  
552  C  CD  . GLU A 73  ? 0.2604 0.2061 0.1950 -0.0008 0.0229  0.0177  73  GLU A CD  
553  O  OE1 . GLU A 73  ? 0.2456 0.3181 0.1603 -0.0342 -0.0039 0.0151  73  GLU A OE1 
554  O  OE2 . GLU A 73  ? 0.2444 0.4438 0.2204 -0.0795 0.0275  0.0351  73  GLU A OE2 
555  N  N   . ALA A 74  ? 0.1933 0.1324 0.1319 -0.0125 -0.0123 -0.0690 74  ALA A N   
556  C  CA  . ALA A 74  ? 0.1917 0.1205 0.0923 -0.0038 -0.0112 -0.0236 74  ALA A CA  
557  C  C   . ALA A 74  ? 0.1857 0.1204 0.0982 -0.0076 0.0125  -0.0731 74  ALA A C   
558  O  O   . ALA A 74  ? 0.1903 0.1178 0.1194 -0.0082 -0.0158 -0.0559 74  ALA A O   
559  C  CB  . ALA A 74  ? 0.2290 0.1853 0.0741 -0.0160 -0.0427 0.0231  74  ALA A CB  
560  N  N   . ASP A 75  ? 0.1675 0.1176 0.0932 0.0009  0.0010  -0.0299 75  ASP A N   
561  C  CA  . ASP A 75  ? 0.1640 0.1143 0.0861 0.0247  -0.0120 -0.0301 75  ASP A CA  
562  C  C   . ASP A 75  ? 0.1776 0.1220 0.0833 -0.0320 0.0293  -0.0081 75  ASP A C   
563  O  O   . ASP A 75  ? 0.2048 0.1275 0.0870 -0.0044 0.0260  0.0050  75  ASP A O   
564  C  CB  . ASP A 75  ? 0.1537 0.1206 0.0906 -0.0176 0.0111  -0.0236 75  ASP A CB  
565  C  CG  . ASP A 75  ? 0.1725 0.1450 0.0846 -0.0369 0.0019  -0.0347 75  ASP A CG  
566  O  OD1 . ASP A 75  ? 0.1573 0.1898 0.0814 -0.0373 0.0222  -0.0409 75  ASP A OD1 
567  O  OD2 . ASP A 75  ? 0.1923 0.1596 0.0824 -0.0504 0.0092  -0.0342 75  ASP A OD2 
568  N  N   . ILE A 76  ? 0.1781 0.1195 0.0793 -0.0232 0.0281  -0.0015 76  ILE A N   
569  C  CA  . ILE A 76  ? 0.1816 0.1149 0.1173 -0.0239 0.0372  -0.0258 76  ILE A CA  
570  C  C   . ILE A 76  ? 0.1701 0.1363 0.1319 -0.0192 0.0344  -0.0533 76  ILE A C   
571  O  O   . ILE A 76  ? 0.1838 0.1440 0.1238 -0.0246 0.0035  -0.0149 76  ILE A O   
572  C  CB  . ILE A 76  ? 0.1670 0.1184 0.1185 0.0150  0.0508  -0.0334 76  ILE A CB  
573  C  CG1 . ILE A 76  ? 0.1675 0.1474 0.1094 -0.0121 -0.0230 0.0150  76  ILE A CG1 
574  C  CG2 . ILE A 76  ? 0.1543 0.1362 0.1554 0.0269  0.0226  -0.0401 76  ILE A CG2 
575  C  CD1 . ILE A 76  ? 0.2584 0.1899 0.0907 -0.0205 0.0188  0.0019  76  ILE A CD1 
576  N  N   . ASN A 77  ? 0.1576 0.1917 0.1342 -0.0164 0.0168  -0.0532 77  ASN A N   
577  C  CA  . ASN A 77  ? 0.1803 0.1566 0.1631 -0.0408 0.0035  -0.0511 77  ASN A CA  
578  C  C   . ASN A 77  ? 0.2112 0.1640 0.1433 -0.0468 -0.0092 -0.0383 77  ASN A C   
579  O  O   . ASN A 77  ? 0.1818 0.2115 0.1591 -0.0102 -0.0033 -0.0711 77  ASN A O   
580  C  CB  . ASN A 77  ? 0.1788 0.1679 0.2142 0.0050  -0.0118 -0.0697 77  ASN A CB  
581  C  CG  . ASN A 77  ? 0.2092 0.1681 0.2032 0.0212  -0.0028 -0.0176 77  ASN A CG  
582  O  OD1 . ASN A 77  ? 0.2584 0.2519 0.1936 -0.0225 0.0738  -0.0509 77  ASN A OD1 
583  N  ND2 . ASN A 77  ? 0.2756 0.1791 0.2493 -0.0376 0.0262  -0.0386 77  ASN A ND2 
584  N  N   . TYR A 78  ? 0.2217 0.1635 0.0941 -0.0370 0.0284  -0.0391 78  TYR A N   
585  C  CA  . TYR A 78  ? 0.1868 0.1689 0.1017 -0.0146 0.0534  -0.0167 78  TYR A CA  
586  C  C   . TYR A 78  ? 0.2008 0.1713 0.1213 -0.0308 0.0641  -0.0130 78  TYR A C   
587  O  O   . TYR A 78  ? 0.2399 0.1751 0.1213 -0.0307 0.0479  -0.0334 78  TYR A O   
588  C  CB  . TYR A 78  ? 0.1852 0.1728 0.1032 -0.0123 -0.0169 -0.0301 78  TYR A CB  
589  C  CG  . TYR A 78  ? 0.1828 0.1619 0.1004 -0.0039 0.0035  -0.0290 78  TYR A CG  
590  C  CD1 . TYR A 78  ? 0.2010 0.1460 0.1021 -0.0078 -0.0084 -0.0223 78  TYR A CD1 
591  C  CD2 . TYR A 78  ? 0.2106 0.1673 0.0913 -0.0009 -0.0429 -0.0219 78  TYR A CD2 
592  C  CE1 . TYR A 78  ? 0.1904 0.1421 0.0978 -0.0309 0.0140  -0.0403 78  TYR A CE1 
593  C  CE2 . TYR A 78  ? 0.2081 0.1566 0.0891 -0.0138 -0.0469 -0.0040 78  TYR A CE2 
594  C  CZ  . TYR A 78  ? 0.1854 0.1410 0.0918 -0.0183 -0.0440 -0.0695 78  TYR A CZ  
595  O  OH  . TYR A 78  ? 0.1649 0.1494 0.0938 -0.0155 0.0131  -0.0085 78  TYR A OH  
596  N  N   . THR A 79  ? 0.1998 0.1556 0.1300 -0.0146 -0.0039 -0.0183 79  THR A N   
597  C  CA  . THR A 79  ? 0.2626 0.2037 0.1550 -0.0957 -0.0053 -0.0219 79  THR A CA  
598  C  C   . THR A 79  ? 0.2360 0.1947 0.1471 -0.1139 0.0082  -0.0004 79  THR A C   
599  O  O   . THR A 79  ? 0.2641 0.1916 0.1397 -0.0826 0.0336  -0.0068 79  THR A O   
600  C  CB  . THR A 79  ? 0.2128 0.2077 0.2568 -0.0313 0.0282  -0.0400 79  THR A CB  
601  O  OG1 . THR A 79  ? 0.2420 0.2339 0.2709 0.0142  0.0503  -0.0220 79  THR A OG1 
602  C  CG2 . THR A 79  ? 0.2146 0.2234 0.2639 -0.0387 0.0353  -0.0992 79  THR A CG2 
603  N  N   . SER A 80  ? 0.1299 0.1696 0.1546 -0.0193 0.0126  -0.0334 80  SER A N   
604  C  CA  . SER A 80  ? 0.1586 0.1526 0.1463 -0.0436 -0.0032 -0.0279 80  SER A CA  
605  C  C   . SER A 80  ? 0.1260 0.1396 0.1484 -0.0187 -0.0269 -0.0416 80  SER A C   
606  O  O   . SER A 80  ? 0.2376 0.1375 0.1542 -0.0183 0.0138  -0.0433 80  SER A O   
607  C  CB  . SER A 80  ? 0.1965 0.2372 0.1447 -0.1003 -0.0096 -0.0486 80  SER A CB  
608  O  OG  . SER A 80  ? 0.1282 0.2972 0.2566 -0.0693 -0.0403 -0.0182 80  SER A OG  
609  N  N   . GLY A 81  ? 0.1345 0.1428 0.1503 -0.0305 -0.0043 -0.0233 81  GLY A N   
610  C  CA  . GLY A 81  ? 0.1373 0.1321 0.1470 -0.0287 0.0070  -0.0460 81  GLY A CA  
611  C  C   . GLY A 81  ? 0.1056 0.1147 0.1187 0.0091  -0.0058 -0.0003 81  GLY A C   
612  O  O   . GLY A 81  ? 0.1159 0.1461 0.1004 0.0118  -0.0096 0.0034  81  GLY A O   
613  N  N   . PHE A 82  ? 0.1808 0.1311 0.1099 -0.0402 -0.0261 0.0172  82  PHE A N   
614  C  CA  . PHE A 82  ? 0.2022 0.1433 0.1138 -0.0662 -0.0059 -0.0115 82  PHE A CA  
615  C  C   . PHE A 82  ? 0.1339 0.1406 0.1130 -0.0086 0.0300  0.0011  82  PHE A C   
616  O  O   . PHE A 82  ? 0.1321 0.1387 0.1522 -0.0073 0.0290  -0.0224 82  PHE A O   
617  C  CB  . PHE A 82  ? 0.1655 0.1183 0.1191 -0.0300 -0.0038 -0.0111 82  PHE A CB  
618  C  CG  . PHE A 82  ? 0.1716 0.1359 0.1151 -0.0012 -0.0394 0.0013  82  PHE A CG  
619  C  CD1 . PHE A 82  ? 0.1671 0.1682 0.0908 -0.0186 -0.0434 -0.0016 82  PHE A CD1 
620  C  CD2 . PHE A 82  ? 0.1404 0.1961 0.1084 0.0229  -0.0002 0.0016  82  PHE A CD2 
621  C  CE1 . PHE A 82  ? 0.1919 0.1622 0.0967 -0.0197 0.0431  0.0033  82  PHE A CE1 
622  C  CE2 . PHE A 82  ? 0.1722 0.2120 0.1108 -0.0047 -0.0249 0.0132  82  PHE A CE2 
623  C  CZ  . PHE A 82  ? 0.2099 0.1642 0.0900 -0.0218 -0.0183 0.0255  82  PHE A CZ  
624  N  N   . ARG A 83  ? 0.1383 0.1683 0.1121 -0.0257 0.0070  -0.0291 83  ARG A N   
625  C  CA  . ARG A 83  ? 0.1788 0.1703 0.0892 -0.0198 0.0014  -0.0048 83  ARG A CA  
626  C  C   . ARG A 83  ? 0.1753 0.1723 0.0747 -0.0344 0.0023  0.0000  83  ARG A C   
627  O  O   . ARG A 83  ? 0.2464 0.1747 0.0803 0.0032  0.0220  -0.0129 83  ARG A O   
628  C  CB  . ARG A 83  ? 0.1997 0.1555 0.0955 -0.0524 -0.0015 -0.0425 83  ARG A CB  
629  C  CG  . ARG A 83  ? 0.1965 0.1596 0.1200 -0.0198 -0.0032 -0.0521 83  ARG A CG  
630  C  CD  . ARG A 83  ? 0.1617 0.2010 0.1253 0.0159  -0.0082 -0.0461 83  ARG A CD  
631  N  NE  . ARG A 83  ? 0.1459 0.2473 0.1132 0.0230  0.0004  -0.0354 83  ARG A NE  
632  C  CZ  . ARG A 83  ? 0.1614 0.2837 0.1318 -0.0093 -0.0079 -0.0299 83  ARG A CZ  
633  N  NH1 . ARG A 83  ? 0.1736 0.3634 0.1167 -0.0437 0.0319  -0.0505 83  ARG A NH1 
634  N  NH2 . ARG A 83  ? 0.1711 0.3467 0.1214 -0.0110 0.0335  -0.0855 83  ARG A NH2 
635  N  N   . ASN A 84  ? 0.1586 0.1729 0.0784 -0.0203 0.0219  -0.0468 84  ASN A N   
636  C  CA  . ASN A 84  ? 0.1843 0.1709 0.1188 -0.0086 0.0206  -0.0276 84  ASN A CA  
637  C  C   . ASN A 84  ? 0.2013 0.1686 0.1233 -0.0182 0.0212  -0.0608 84  ASN A C   
638  O  O   . ASN A 84  ? 0.2214 0.1515 0.1617 -0.0402 0.0162  -0.0259 84  ASN A O   
639  C  CB  . ASN A 84  ? 0.1855 0.1563 0.1238 0.0042  -0.0173 -0.0131 84  ASN A CB  
640  C  CG  . ASN A 84  ? 0.1971 0.1346 0.1195 -0.0050 0.0917  -0.0214 84  ASN A CG  
641  O  OD1 . ASN A 84  ? 0.1924 0.1946 0.1258 -0.0173 0.0174  -0.0332 84  ASN A OD1 
642  N  ND2 . ASN A 84  ? 0.2187 0.2617 0.1249 -0.0572 0.0449  -0.0468 84  ASN A ND2 
643  N  N   . SER A 85  ? 0.2141 0.1683 0.0887 -0.0036 -0.0059 -0.0355 85  SER A N   
644  C  CA  . SER A 85  ? 0.3050 0.1762 0.0863 -0.0561 -0.0384 -0.0514 85  SER A CA  
645  C  C   . SER A 85  ? 0.2594 0.1836 0.0870 -0.0476 -0.0072 -0.0556 85  SER A C   
646  O  O   . SER A 85  ? 0.3583 0.1809 0.0917 -0.0941 -0.0137 0.0051  85  SER A O   
647  C  CB  A SER A 85  ? 0.3866 0.1748 0.0827 -0.0603 -0.0357 -0.0135 85  SER A CB  
648  C  CB  B SER A 85  ? 0.3459 0.1760 0.0829 -0.0508 -0.0343 -0.0137 85  SER A CB  
649  O  OG  A SER A 85  ? 0.4002 0.1330 0.1962 -0.0372 -0.0159 -0.0217 85  SER A OG  
650  O  OG  B SER A 85  ? 0.5331 0.2357 0.0738 -0.1213 -0.0864 0.0284  85  SER A OG  
651  N  N   . ASP A 86  ? 0.2092 0.1607 0.0845 -0.0091 -0.0261 -0.0134 86  ASP A N   
652  C  CA  . ASP A 86  ? 0.1997 0.1175 0.0839 -0.0007 0.0031  0.0067  86  ASP A CA  
653  C  C   . ASP A 86  ? 0.2024 0.1148 0.0911 -0.0153 0.0467  -0.0260 86  ASP A C   
654  O  O   . ASP A 86  ? 0.1725 0.1203 0.1249 -0.0072 -0.0044 -0.0182 86  ASP A O   
655  C  CB  . ASP A 86  ? 0.1495 0.2249 0.1104 0.0168  -0.0281 -0.0170 86  ASP A CB  
656  C  CG  . ASP A 86  ? 0.1528 0.2057 0.2087 0.0186  -0.0206 -0.0379 86  ASP A CG  
657  O  OD1 . ASP A 86  ? 0.2590 0.1727 0.2976 0.0233  -0.0227 0.0128  86  ASP A OD1 
658  O  OD2 . ASP A 86  ? 0.1468 0.2720 0.3088 0.0013  -0.0235 -0.0186 86  ASP A OD2 
659  N  N   . ARG A 87  ? 0.1869 0.0906 0.1038 -0.0017 0.0344  -0.0186 87  ARG A N   
660  C  CA  . ARG A 87  ? 0.1653 0.1004 0.1103 0.0182  0.0536  -0.0083 87  ARG A CA  
661  C  C   . ARG A 87  ? 0.1345 0.1012 0.1132 0.0573  0.0136  -0.0117 87  ARG A C   
662  O  O   . ARG A 87  ? 0.2143 0.0992 0.1119 0.0199  -0.0210 -0.0094 87  ARG A O   
663  C  CB  . ARG A 87  ? 0.1782 0.1236 0.1012 -0.0063 0.0029  -0.0242 87  ARG A CB  
664  C  CG  . ARG A 87  ? 0.2078 0.1472 0.0938 -0.0184 0.0277  -0.0797 87  ARG A CG  
665  C  CD  . ARG A 87  ? 0.1804 0.1466 0.0965 -0.0104 0.0189  -0.0539 87  ARG A CD  
666  N  NE  . ARG A 87  ? 0.1837 0.1636 0.1003 -0.0111 0.0285  -0.0615 87  ARG A NE  
667  C  CZ  . ARG A 87  ? 0.1834 0.1734 0.0929 -0.0036 -0.0031 -0.0693 87  ARG A CZ  
668  N  NH1 . ARG A 87  ? 0.1734 0.1683 0.1540 0.0042  -0.0308 -0.0797 87  ARG A NH1 
669  N  NH2 . ARG A 87  ? 0.2546 0.2362 0.0895 -0.0211 -0.0011 -0.1166 87  ARG A NH2 
670  N  N   . ILE A 88  ? 0.1888 0.1020 0.1108 0.0083  -0.0391 -0.0306 88  ILE A N   
671  C  CA  . ILE A 88  ? 0.1848 0.1323 0.1081 0.0301  -0.0214 -0.0250 88  ILE A CA  
672  C  C   . ILE A 88  ? 0.1819 0.1424 0.0625 0.0383  -0.0243 -0.0718 88  ILE A C   
673  O  O   . ILE A 88  ? 0.1779 0.1286 0.1374 0.0066  0.0133  -0.0754 88  ILE A O   
674  C  CB  . ILE A 88  ? 0.2213 0.1578 0.1094 -0.0122 0.0166  0.0026  88  ILE A CB  
675  C  CG1 . ILE A 88  ? 0.3286 0.1714 0.1051 -0.0082 0.0612  -0.0279 88  ILE A CG1 
676  C  CG2 . ILE A 88  ? 0.3907 0.1398 0.1697 -0.0415 -0.0151 -0.0370 88  ILE A CG2 
677  C  CD1 . ILE A 88  ? 0.3474 0.1868 0.0969 -0.0222 0.0876  -0.0349 88  ILE A CD1 
678  N  N   . LEU A 89  ? 0.1649 0.1293 0.1162 0.0500  -0.0497 -0.0929 89  LEU A N   
679  C  CA  . LEU A 89  ? 0.1777 0.1053 0.1786 0.0420  -0.0785 -0.0665 89  LEU A CA  
680  C  C   . LEU A 89  ? 0.1584 0.1429 0.1800 0.0077  -0.0553 -0.1049 89  LEU A C   
681  O  O   . LEU A 89  ? 0.2005 0.1600 0.1596 0.0665  -0.0316 -0.0782 89  LEU A O   
682  C  CB  . LEU A 89  ? 0.2254 0.1710 0.1784 -0.0221 -0.0178 -0.0589 89  LEU A CB  
683  C  CG  . LEU A 89  ? 0.2565 0.2059 0.1753 -0.0269 -0.0214 -0.0334 89  LEU A CG  
684  C  CD1 . LEU A 89  ? 0.3334 0.1597 0.1657 0.0035  0.0804  -0.0488 89  LEU A CD1 
685  C  CD2 . LEU A 89  ? 0.3051 0.3227 0.1811 -0.1221 -0.0603 0.0279  89  LEU A CD2 
686  N  N   . TYR A 90  ? 0.2092 0.1338 0.1547 0.0116  -0.0293 -0.0676 90  TYR A N   
687  C  CA  . TYR A 90  ? 0.1967 0.1630 0.1587 0.0018  -0.0341 -0.0447 90  TYR A CA  
688  C  C   . TYR A 90  ? 0.1662 0.1990 0.1776 0.0298  -0.0647 -0.0555 90  TYR A C   
689  O  O   . TYR A 90  ? 0.1797 0.1635 0.2483 0.0318  -0.0378 -0.0672 90  TYR A O   
690  C  CB  . TYR A 90  ? 0.1991 0.1609 0.1518 0.0090  -0.0181 -0.0244 90  TYR A CB  
691  C  CG  . TYR A 90  ? 0.2734 0.1537 0.1756 0.0035  -0.0416 -0.0669 90  TYR A CG  
692  C  CD1 . TYR A 90  ? 0.3035 0.1576 0.1690 0.0036  -0.0453 -0.0277 90  TYR A CD1 
693  C  CD2 . TYR A 90  ? 0.2751 0.1532 0.1817 0.0305  -0.0543 -0.0556 90  TYR A CD2 
694  C  CE1 . TYR A 90  ? 0.3396 0.1535 0.1924 -0.0278 -0.0359 -0.0402 90  TYR A CE1 
695  C  CE2 . TYR A 90  ? 0.3157 0.1561 0.1913 0.0421  -0.0516 -0.0620 90  TYR A CE2 
696  C  CZ  . TYR A 90  ? 0.3443 0.1556 0.1913 0.0126  -0.0013 -0.1064 90  TYR A CZ  
697  O  OH  . TYR A 90  ? 0.3615 0.1642 0.2013 0.0215  -0.0476 -0.0472 90  TYR A OH  
698  N  N   . SER A 91  ? 0.2076 0.2271 0.1933 -0.0354 -0.0410 -0.0804 91  SER A N   
699  C  CA  . SER A 91  ? 0.1946 0.2464 0.2027 -0.0194 -0.0504 -0.0780 91  SER A CA  
700  C  C   . SER A 91  ? 0.2006 0.2460 0.2059 0.0327  0.0024  -0.0618 91  SER A C   
701  O  O   . SER A 91  ? 0.2158 0.2072 0.2156 0.0393  -0.0459 -0.0509 91  SER A O   
702  C  CB  . SER A 91  ? 0.1480 0.2436 0.2268 -0.0010 -0.0926 -0.0688 91  SER A CB  
703  O  OG  . SER A 91  ? 0.2399 0.2203 0.2155 0.0001  -0.0244 -0.0347 91  SER A OG  
704  N  N   . SER A 92  ? 0.1782 0.2662 0.2437 0.0658  -0.0750 -0.0802 92  SER A N   
705  C  CA  . SER A 92  ? 0.1881 0.2479 0.2614 0.0369  -0.0890 -0.0604 92  SER A CA  
706  C  C   . SER A 92  ? 0.2528 0.2528 0.2507 0.0575  -0.1340 -0.0518 92  SER A C   
707  O  O   . SER A 92  ? 0.3720 0.2514 0.2610 0.0635  -0.0799 0.0083  92  SER A O   
708  C  CB  . SER A 92  ? 0.1716 0.2721 0.3349 0.0517  -0.0747 -0.0398 92  SER A CB  
709  O  OG  . SER A 92  ? 0.2447 0.3732 0.4271 -0.0733 -0.1008 0.0439  92  SER A OG  
710  N  N   . ASP A 93  ? 0.2205 0.2523 0.2739 0.0567  -0.1181 -0.0630 93  ASP A N   
711  C  CA  . ASP A 93  ? 0.2214 0.2573 0.2610 0.0545  -0.1047 -0.0831 93  ASP A CA  
712  C  C   . ASP A 93  ? 0.2248 0.2610 0.2234 0.0470  -0.0481 -0.0310 93  ASP A C   
713  O  O   . ASP A 93  ? 0.2128 0.2850 0.1815 0.0186  -0.0048 -0.0198 93  ASP A O   
714  C  CB  . ASP A 93  ? 0.2323 0.3017 0.2480 0.0219  -0.0924 -0.0710 93  ASP A CB  
715  C  CG  . ASP A 93  ? 0.2560 0.3110 0.2587 -0.0325 -0.1447 -0.0567 93  ASP A CG  
716  O  OD1 . ASP A 93  ? 0.2667 0.2261 0.2608 0.0073  -0.1026 -0.0353 93  ASP A OD1 
717  O  OD2 . ASP A 93  ? 0.3230 0.3451 0.2536 -0.0957 -0.0858 -0.0430 93  ASP A OD2 
718  N  N   . TRP A 94  ? 0.2211 0.2139 0.2067 0.0800  -0.0200 -0.0411 94  TRP A N   
719  C  CA  . TRP A 94  ? 0.1904 0.2638 0.1966 0.0956  -0.0234 -0.0234 94  TRP A CA  
720  C  C   . TRP A 94  ? 0.1632 0.2732 0.1807 0.0842  -0.0244 -0.0557 94  TRP A C   
721  O  O   . TRP A 94  ? 0.1993 0.2454 0.2271 0.0400  0.0135  0.0302  94  TRP A O   
722  C  CB  . TRP A 94  ? 0.2883 0.2573 0.2196 0.0042  -0.0393 0.0154  94  TRP A CB  
723  C  CG  . TRP A 94  ? 0.3254 0.2553 0.2563 0.0320  -0.0890 0.0408  94  TRP A CG  
724  C  CD1 . TRP A 94  ? 0.3171 0.2465 0.2811 0.0376  -0.0495 0.0047  94  TRP A CD1 
725  C  CD2 . TRP A 94  ? 0.4095 0.2566 0.2537 0.0269  -0.0773 0.0034  94  TRP A CD2 
726  N  NE1 . TRP A 94  ? 0.3576 0.2425 0.3179 0.0367  -0.0451 0.0230  94  TRP A NE1 
727  C  CE2 . TRP A 94  ? 0.4326 0.2454 0.2959 0.0197  -0.0056 -0.0130 94  TRP A CE2 
728  C  CE3 . TRP A 94  ? 0.4786 0.2645 0.2342 -0.0038 -0.0404 -0.0402 94  TRP A CE3 
729  C  CZ2 . TRP A 94  ? 0.4848 0.2505 0.3002 0.0388  -0.0831 0.0141  94  TRP A CZ2 
730  C  CZ3 . TRP A 94  ? 0.5308 0.2613 0.2487 0.0034  -0.0724 0.0029  94  TRP A CZ3 
731  C  CH2 . TRP A 94  ? 0.5387 0.2652 0.2741 0.0256  -0.0567 0.0234  94  TRP A CH2 
732  N  N   . LEU A 95  ? 0.1871 0.2565 0.1882 0.0680  -0.0710 -0.1253 95  LEU A N   
733  C  CA  . LEU A 95  ? 0.1573 0.2542 0.1881 0.0518  -0.0609 -0.1007 95  LEU A CA  
734  C  C   . LEU A 95  ? 0.2015 0.2148 0.1923 0.0244  -0.0563 -0.0902 95  LEU A C   
735  O  O   . LEU A 95  ? 0.2050 0.2192 0.2086 0.0574  -0.0791 -0.0965 95  LEU A O   
736  C  CB  . LEU A 95  ? 0.1506 0.2350 0.2709 0.0499  -0.0765 -0.0698 95  LEU A CB  
737  C  CG  . LEU A 95  ? 0.2193 0.2691 0.2802 0.0035  -0.0673 -0.1214 95  LEU A CG  
738  C  CD1 . LEU A 95  ? 0.3190 0.2761 0.3542 -0.0921 -0.0743 -0.0579 95  LEU A CD1 
739  C  CD2 . LEU A 95  ? 0.3550 0.2349 0.2747 0.0381  -0.1285 -0.0867 95  LEU A CD2 
740  N  N   . ILE A 96  ? 0.2239 0.1946 0.0929 0.0251  -0.0337 -0.0753 96  ILE A N   
741  C  CA  . ILE A 96  ? 0.2331 0.1389 0.1147 0.0270  -0.0103 -0.0634 96  ILE A CA  
742  C  C   . ILE A 96  ? 0.1651 0.1344 0.1323 0.0135  0.0409  -0.1099 96  ILE A C   
743  O  O   . ILE A 96  ? 0.2165 0.1323 0.0972 0.0117  0.0450  -0.0443 96  ILE A O   
744  C  CB  A ILE A 96  ? 0.2515 0.1423 0.1110 0.0121  -0.0525 -0.0230 96  ILE A CB  
745  C  CB  B ILE A 96  ? 0.2453 0.1446 0.1110 0.0193  -0.0506 -0.0248 96  ILE A CB  
746  C  CG1 A ILE A 96  ? 0.2836 0.1484 0.1069 0.0120  -0.0344 -0.0264 96  ILE A CG1 
747  C  CG1 B ILE A 96  ? 0.2767 0.1470 0.1043 0.0130  -0.0575 -0.0182 96  ILE A CG1 
748  C  CG2 A ILE A 96  ? 0.2937 0.1597 0.1129 -0.0283 -0.0192 -0.0198 96  ILE A CG2 
749  C  CG2 B ILE A 96  ? 0.2378 0.1667 0.1191 0.0065  -0.0312 -0.0155 96  ILE A CG2 
750  C  CD1 A ILE A 96  ? 0.3934 0.1228 0.0335 -0.0313 -0.0234 -0.0365 96  ILE A CD1 
751  C  CD1 B ILE A 96  ? 0.3798 0.1986 0.0972 -0.0819 0.0368  -0.0078 96  ILE A CD1 
752  N  N   . TYR A 97  ? 0.1605 0.0942 0.1337 0.0107  0.0132  -0.0826 97  TYR A N   
753  C  CA  . TYR A 97  ? 0.1792 0.1056 0.1285 0.0211  -0.0045 -0.0240 97  TYR A CA  
754  C  C   . TYR A 97  ? 0.2358 0.0938 0.1156 -0.0023 -0.0253 -0.0109 97  TYR A C   
755  O  O   . TYR A 97  ? 0.2110 0.1027 0.1503 0.0197  -0.0326 -0.0297 97  TYR A O   
756  C  CB  . TYR A 97  ? 0.2197 0.1320 0.1199 -0.0076 0.0485  -0.0658 97  TYR A CB  
757  C  CG  . TYR A 97  ? 0.1883 0.0948 0.1619 0.0241  0.0233  -0.0481 97  TYR A CG  
758  C  CD1 . TYR A 97  ? 0.1703 0.1086 0.1768 -0.0060 -0.0663 -0.0454 97  TYR A CD1 
759  C  CD2 . TYR A 97  ? 0.2085 0.1010 0.1736 0.0265  0.0415  -0.0274 97  TYR A CD2 
760  C  CE1 . TYR A 97  ? 0.2153 0.1142 0.1808 -0.0193 -0.0618 -0.0325 97  TYR A CE1 
761  C  CE2 . TYR A 97  ? 0.2341 0.1037 0.1974 -0.0131 0.0432  -0.0569 97  TYR A CE2 
762  C  CZ  . TYR A 97  ? 0.2080 0.1089 0.2148 -0.0216 0.0100  -0.0416 97  TYR A CZ  
763  O  OH  . TYR A 97  ? 0.2359 0.1140 0.2170 -0.0095 -0.0484 -0.0502 97  TYR A OH  
764  N  N   . LYS A 98  ? 0.2682 0.0946 0.0670 -0.0045 -0.0133 -0.0261 98  LYS A N   
765  C  CA  . LYS A 98  ? 0.3370 0.1811 0.0489 -0.0498 0.0206  0.0200  98  LYS A CA  
766  C  C   . LYS A 98  ? 0.2258 0.1327 0.0601 0.0144  0.0404  -0.0088 98  LYS A C   
767  O  O   . LYS A 98  ? 0.2921 0.1594 0.0879 -0.0853 0.0088  -0.0116 98  LYS A O   
768  C  CB  . LYS A 98  ? 0.2991 0.3566 0.0938 -0.1443 0.0228  0.0646  98  LYS A CB  
769  C  CG  . LYS A 98  ? 0.2804 0.2917 0.2653 -0.0268 0.1044  0.0714  98  LYS A CG  
770  C  CD  . LYS A 98  ? 0.2899 0.3126 0.3039 -0.0420 0.0860  -0.0118 98  LYS A CD  
771  C  CE  . LYS A 98  ? 0.2666 0.3109 0.3840 -0.0295 0.0223  0.0254  98  LYS A CE  
772  N  NZ  . LYS A 98  ? 0.2340 0.3771 0.6104 -0.0122 0.1263  0.0239  98  LYS A NZ  
773  N  N   . THR A 99  ? 0.2332 0.1282 0.0643 0.0168  0.0579  -0.0063 99  THR A N   
774  C  CA  . THR A 99  ? 0.3166 0.1289 0.0590 -0.0077 0.0693  -0.0084 99  THR A CA  
775  C  C   . THR A 99  ? 0.3208 0.1356 0.0548 -0.0135 -0.0288 -0.0273 99  THR A C   
776  O  O   . THR A 99  ? 0.2633 0.1421 0.1065 -0.0004 -0.0194 0.0001  99  THR A O   
777  C  CB  . THR A 99  ? 0.3073 0.1547 0.0553 -0.0102 0.0355  -0.0166 99  THR A CB  
778  O  OG1 . THR A 99  ? 0.3136 0.1811 0.0583 -0.0120 0.0385  0.0049  99  THR A OG1 
779  C  CG2 . THR A 99  ? 0.2473 0.1693 0.1133 0.0353  0.0771  -0.0064 99  THR A CG2 
780  N  N   . THR A 100 ? 0.2991 0.1328 0.1080 -0.0031 -0.0417 -0.0020 100 THR A N   
781  C  CA  . THR A 100 ? 0.2987 0.1531 0.1182 -0.0070 -0.0480 0.0305  100 THR A CA  
782  C  C   . THR A 100 ? 0.3365 0.1452 0.1117 0.0154  -0.0492 0.0129  100 THR A C   
783  O  O   . THR A 100 ? 0.3477 0.2353 0.1136 -0.0207 -0.0466 0.0116  100 THR A O   
784  C  CB  . THR A 100 ? 0.2828 0.1741 0.1320 0.0091  -0.0412 0.0359  100 THR A CB  
785  O  OG1 . THR A 100 ? 0.3140 0.1686 0.2634 0.0666  -0.0384 -0.0010 100 THR A OG1 
786  C  CG2 . THR A 100 ? 0.2892 0.2895 0.1242 -0.0298 -0.0002 0.0091  100 THR A CG2 
787  N  N   . ASP A 101 ? 0.4099 0.1642 0.1013 -0.0714 0.0087  -0.0287 101 ASP A N   
788  C  CA  . ASP A 101 ? 0.4368 0.1710 0.0953 -0.0556 -0.0204 0.0051  101 ASP A CA  
789  C  C   . ASP A 101 ? 0.4228 0.1909 0.0919 -0.0863 0.0798  0.0060  101 ASP A C   
790  O  O   . ASP A 101 ? 0.4588 0.2523 0.0892 -0.1240 0.0666  -0.0045 101 ASP A O   
791  C  CB  . ASP A 101 ? 0.4766 0.1801 0.0640 -0.0572 -0.0046 0.0028  101 ASP A CB  
792  C  CG  . ASP A 101 ? 0.4631 0.1476 0.0880 -0.0470 0.0260  -0.0346 101 ASP A CG  
793  O  OD1 . ASP A 101 ? 0.4124 0.1643 0.1312 -0.0391 0.0066  -0.0046 101 ASP A OD1 
794  O  OD2 . ASP A 101 ? 0.4882 0.1488 0.2077 -0.0331 -0.0380 0.0161  101 ASP A OD2 
795  N  N   . HIS A 102 ? 0.3804 0.1943 0.1607 -0.0558 0.0003  0.0147  102 HIS A N   
796  C  CA  . HIS A 102 ? 0.3420 0.2444 0.1102 0.0029  0.0371  -0.0210 102 HIS A CA  
797  C  C   . HIS A 102 ? 0.3248 0.2224 0.1255 0.0216  0.1446  -0.0671 102 HIS A C   
798  O  O   . HIS A 102 ? 0.4049 0.2917 0.0942 -0.0695 0.1103  -0.0933 102 HIS A O   
799  C  CB  . HIS A 102 ? 0.4484 0.3313 0.1009 -0.0420 0.0822  -0.0652 102 HIS A CB  
800  C  CG  . HIS A 102 ? 0.5461 0.3480 0.0973 -0.0970 0.0216  -0.0555 102 HIS A CG  
801  N  ND1 . HIS A 102 ? 0.5498 0.3868 0.2115 -0.1459 0.0968  -0.0685 102 HIS A ND1 
802  C  CD2 . HIS A 102 ? 0.6170 0.3353 0.1373 -0.1104 -0.0453 -0.0070 102 HIS A CD2 
803  C  CE1 . HIS A 102 ? 0.6389 0.3936 0.2284 -0.1966 0.1463  -0.0753 102 HIS A CE1 
804  N  NE2 . HIS A 102 ? 0.6792 0.3614 0.2065 -0.1690 0.0787  -0.0164 102 HIS A NE2 
805  N  N   . TYR A 103 ? 0.3409 0.2043 0.1179 -0.0132 0.0960  -0.0021 103 TYR A N   
806  C  CA  . TYR A 103 ? 0.3692 0.2181 0.1510 -0.0490 0.0646  -0.0072 103 TYR A CA  
807  C  C   . TYR A 103 ? 0.4194 0.2220 0.1452 -0.0716 0.1015  -0.0620 103 TYR A C   
808  O  O   . TYR A 103 ? 0.4208 0.2129 0.2304 -0.0694 0.0966  -0.0566 103 TYR A O   
809  C  CB  . TYR A 103 ? 0.3535 0.2269 0.1932 -0.0794 0.0421  0.0027  103 TYR A CB  
810  C  CG  . TYR A 103 ? 0.3452 0.2216 0.1610 -0.0396 0.0558  -0.0317 103 TYR A CG  
811  C  CD1 . TYR A 103 ? 0.2777 0.2309 0.1574 0.0009  0.0343  -0.0049 103 TYR A CD1 
812  C  CD2 . TYR A 103 ? 0.4370 0.2287 0.1562 -0.0601 0.0392  -0.0510 103 TYR A CD2 
813  C  CE1 . TYR A 103 ? 0.2400 0.2361 0.1270 -0.0063 0.0512  -0.0208 103 TYR A CE1 
814  C  CE2 . TYR A 103 ? 0.3664 0.2308 0.1245 -0.0326 -0.0418 0.0149  103 TYR A CE2 
815  C  CZ  . TYR A 103 ? 0.2311 0.2265 0.1280 0.0128  0.0356  -0.0120 103 TYR A CZ  
816  O  OH  . TYR A 103 ? 0.2907 0.2255 0.1729 -0.0165 0.0325  -0.0216 103 TYR A OH  
817  N  N   . GLN A 104 ? 0.4417 0.2215 0.0920 -0.0839 0.0882  -0.0373 104 GLN A N   
818  C  CA  . GLN A 104 ? 0.4565 0.2207 0.1339 -0.0700 0.0770  -0.0062 104 GLN A CA  
819  C  C   . GLN A 104 ? 0.4571 0.2091 0.1458 -0.0760 0.1017  0.0012  104 GLN A C   
820  O  O   . GLN A 104 ? 0.4993 0.2366 0.1809 -0.1203 0.1258  -0.0033 104 GLN A O   
821  C  CB  . GLN A 104 ? 0.4652 0.2102 0.1495 -0.0393 0.0738  -0.0158 104 GLN A CB  
822  C  CG  . GLN A 104 ? 0.7785 0.3324 0.1068 -0.1655 0.1133  -0.0582 104 GLN A CG  
823  C  CD  . GLN A 104 ? 0.7349 0.3549 0.1269 -0.1142 0.1063  -0.0122 104 GLN A CD  
824  O  OE1 . GLN A 104 ? 0.8024 0.2670 0.1824 -0.0919 0.0243  0.0241  104 GLN A OE1 
825  N  NE2 . GLN A 104 ? 0.6690 0.4389 0.2241 -0.0662 0.0640  0.0151  104 GLN A NE2 
826  N  N   . THR A 105 ? 0.5122 0.1987 0.1001 -0.1059 0.0897  -0.0057 105 THR A N   
827  C  CA  . THR A 105 ? 0.5962 0.1793 0.0980 -0.1464 0.1126  -0.0456 105 THR A CA  
828  C  C   . THR A 105 ? 0.4253 0.1838 0.0936 -0.1048 0.0810  -0.0641 105 THR A C   
829  O  O   . THR A 105 ? 0.3609 0.1608 0.0815 -0.0583 -0.0062 -0.0094 105 THR A O   
830  C  CB  . THR A 105 ? 0.6708 0.1513 0.1331 -0.1100 0.1283  -0.0362 105 THR A CB  
831  O  OG1 . THR A 105 ? 0.5446 0.1778 0.1786 0.0111  0.0186  0.0024  105 THR A OG1 
832  C  CG2 . THR A 105 ? 0.6453 0.2084 0.0942 -0.0319 0.0850  0.0088  105 THR A CG2 
833  N  N   . PHE A 106 ? 0.3893 0.1594 0.0919 -0.0667 0.0912  -0.0209 106 PHE A N   
834  C  CA  . PHE A 106 ? 0.2891 0.1727 0.0867 -0.0590 0.0277  -0.0208 106 PHE A CA  
835  C  C   . PHE A 106 ? 0.2781 0.1506 0.1024 -0.0458 0.0422  -0.0312 106 PHE A C   
836  O  O   . PHE A 106 ? 0.3805 0.1556 0.1415 -0.1030 0.0360  -0.0052 106 PHE A O   
837  C  CB  . PHE A 106 ? 0.2758 0.1605 0.1641 -0.0221 0.0548  -0.0399 106 PHE A CB  
838  C  CG  . PHE A 106 ? 0.3078 0.1686 0.1443 -0.0265 0.0860  -0.0811 106 PHE A CG  
839  C  CD1 . PHE A 106 ? 0.2973 0.1616 0.1791 0.0045  0.0558  -0.0711 106 PHE A CD1 
840  C  CD2 . PHE A 106 ? 0.3136 0.1912 0.1370 -0.0348 0.0658  -0.0638 106 PHE A CD2 
841  C  CE1 . PHE A 106 ? 0.2744 0.1646 0.1997 0.0119  0.0424  -0.0336 106 PHE A CE1 
842  C  CE2 . PHE A 106 ? 0.3170 0.1883 0.1493 -0.0146 0.0536  -0.0668 106 PHE A CE2 
843  C  CZ  . PHE A 106 ? 0.2847 0.1862 0.1904 0.0025  0.0174  -0.0495 106 PHE A CZ  
844  N  N   . THR A 107 ? 0.2623 0.1440 0.0877 -0.0242 0.0476  -0.0030 107 THR A N   
845  C  CA  . THR A 107 ? 0.3071 0.1353 0.0884 -0.0453 0.0608  0.0152  107 THR A CA  
846  C  C   . THR A 107 ? 0.2904 0.1347 0.0852 -0.0618 0.0831  -0.0293 107 THR A C   
847  O  O   . THR A 107 ? 0.2425 0.1206 0.0839 -0.0173 -0.0141 -0.0030 107 THR A O   
848  C  CB  . THR A 107 ? 0.2704 0.1519 0.1320 0.0109  0.0793  0.0360  107 THR A CB  
849  O  OG1 . THR A 107 ? 0.2905 0.2167 0.2396 -0.0440 -0.0352 0.0203  107 THR A OG1 
850  C  CG2 . THR A 107 ? 0.2900 0.1795 0.1406 0.0455  0.0687  0.0724  107 THR A CG2 
851  N  N   . LYS A 108 ? 0.2351 0.0913 0.0956 -0.0182 0.0171  -0.0372 108 LYS A N   
852  C  CA  . LYS A 108 ? 0.2226 0.0994 0.0827 0.0133  0.0036  -0.0185 108 LYS A CA  
853  C  C   . LYS A 108 ? 0.2123 0.0903 0.0776 0.0240  0.0341  -0.0210 108 LYS A C   
854  O  O   . LYS A 108 ? 0.2242 0.0907 0.1408 0.0187  0.0055  0.0063  108 LYS A O   
855  C  CB  . LYS A 108 ? 0.2500 0.1255 0.0949 -0.0255 -0.0103 -0.0173 108 LYS A CB  
856  C  CG  . LYS A 108 ? 0.2031 0.1715 0.0914 -0.0204 0.0112  -0.0053 108 LYS A CG  
857  C  CD  . LYS A 108 ? 0.2555 0.2386 0.0944 -0.0750 -0.0207 -0.0094 108 LYS A CD  
858  C  CE  . LYS A 108 ? 0.2107 0.2595 0.0907 -0.0085 0.0018  -0.0197 108 LYS A CE  
859  N  NZ  . LYS A 108 ? 0.3050 0.2317 0.1684 0.0498  -0.0398 -0.0232 108 LYS A NZ  
860  N  N   . ILE A 109 ? 0.2001 0.0929 0.0963 0.0254  0.0353  -0.0035 109 ILE A N   
861  C  CA  . ILE A 109 ? 0.1991 0.1145 0.1028 0.0194  0.0326  0.0011  109 ILE A CA  
862  C  C   . ILE A 109 ? 0.2415 0.1017 0.0977 -0.0112 0.0098  -0.0005 109 ILE A C   
863  O  O   . ILE A 109 ? 0.2093 0.1700 0.0999 -0.0001 0.0309  0.0257  109 ILE A O   
864  C  CB  . ILE A 109 ? 0.1978 0.1411 0.0953 0.0028  0.0143  -0.0193 109 ILE A CB  
865  C  CG1 . ILE A 109 ? 0.2541 0.1308 0.0943 -0.0036 0.0294  -0.0429 109 ILE A CG1 
866  C  CG2 . ILE A 109 ? 0.2369 0.1565 0.0837 0.0227  -0.0122 -0.0212 109 ILE A CG2 
867  C  CD1 . ILE A 109 ? 0.2435 0.1326 0.1556 0.0025  -0.0165 -0.0318 109 ILE A CD1 
868  N  N   . ARG A 110 ? 0.2234 0.1272 0.1092 -0.0057 -0.0295 -0.0101 110 ARG A N   
869  C  CA  . ARG A 110 ? 0.2187 0.1535 0.1115 0.0059  -0.0258 0.0040  110 ARG A CA  
870  C  C   . ARG A 110 ? 0.2236 0.2305 0.0849 -0.0203 -0.0040 0.0068  110 ARG A C   
871  O  O   . ARG A 110 ? 0.3472 0.3489 0.0854 -0.1153 -0.0452 -0.0204 110 ARG A O   
872  C  CB  . ARG A 110 ? 0.2386 0.1461 0.1212 0.0217  0.0130  0.0076  110 ARG A CB  
873  C  CG  . ARG A 110 ? 0.2412 0.1332 0.1336 0.0174  0.0267  -0.0397 110 ARG A CG  
874  C  CD  . ARG A 110 ? 0.2655 0.1435 0.1255 -0.0119 0.0218  0.0417  110 ARG A CD  
875  N  NE  . ARG A 110 ? 0.2424 0.1569 0.1589 0.0064  0.0532  0.0287  110 ARG A NE  
876  C  CZ  . ARG A 110 ? 0.2135 0.1286 0.1895 0.0258  0.0815  0.0106  110 ARG A CZ  
877  N  NH1 . ARG A 110 ? 0.2360 0.1352 0.1810 -0.0076 0.0550  0.0154  110 ARG A NH1 
878  N  NH2 . ARG A 110 ? 0.2892 0.1416 0.1980 -0.0366 0.0731  -0.0043 110 ARG A NH2 
879  O  OXT . ARG A 110 ? 0.2272 0.2261 0.1036 -0.0298 0.0372  -0.0276 110 ARG A OXT 
880  N  N   . VAL B 3   ? 0.3188 0.5019 0.5170 -0.0525 0.0121  -0.0961 3   VAL B N   
881  C  CA  . VAL B 3   ? 0.2709 0.4727 0.3958 0.0000  0.0120  -0.0961 3   VAL B CA  
882  C  C   . VAL B 3   ? 0.3261 0.4269 0.3887 0.0027  0.0347  -0.0985 3   VAL B C   
883  O  O   . VAL B 3   ? 0.4050 0.4322 0.5239 -0.0804 0.0703  -0.1297 3   VAL B O   
884  C  CB  . VAL B 3   ? 0.3268 0.4740 0.3845 0.0859  0.1129  -0.1240 3   VAL B CB  
885  C  CG1 . VAL B 3   ? 0.3109 0.5564 0.3694 -0.0066 0.0004  0.0343  3   VAL B CG1 
886  C  CG2 . VAL B 3   ? 0.4965 0.4530 0.3709 0.1215  -0.1617 0.0237  3   VAL B CG2 
887  N  N   . ILE B 4   ? 0.3087 0.3174 0.2173 0.0658  0.0198  -0.0639 4   ILE B N   
888  C  CA  . ILE B 4   ? 0.3417 0.3087 0.1291 0.1080  -0.0189 -0.0545 4   ILE B CA  
889  C  C   . ILE B 4   ? 0.3248 0.2793 0.1428 0.1012  -0.0098 -0.0870 4   ILE B C   
890  O  O   . ILE B 4   ? 0.2895 0.2614 0.1966 0.1113  -0.0572 -0.0864 4   ILE B O   
891  C  CB  . ILE B 4   ? 0.3055 0.3927 0.1346 0.1068  -0.0907 -0.0544 4   ILE B CB  
892  C  CG1 . ILE B 4   ? 0.3376 0.3731 0.1260 0.1002  -0.0284 -0.0474 4   ILE B CG1 
893  C  CG2 . ILE B 4   ? 0.2656 0.4248 0.1792 0.1039  -0.0455 -0.0986 4   ILE B CG2 
894  C  CD1 . ILE B 4   ? 0.5066 0.4962 0.1161 -0.0345 -0.0670 0.0658  4   ILE B CD1 
895  N  N   . ASN B 5   ? 0.1931 0.2780 0.1640 0.0536  -0.0312 -0.0756 5   ASN B N   
896  C  CA  . ASN B 5   ? 0.1798 0.2451 0.1755 0.0764  -0.0159 -0.0804 5   ASN B CA  
897  C  C   . ASN B 5   ? 0.2292 0.2400 0.1618 0.0523  -0.0167 -0.0539 5   ASN B C   
898  O  O   . ASN B 5   ? 0.2313 0.2349 0.1564 0.0671  0.0210  -0.0465 5   ASN B O   
899  C  CB  . ASN B 5   ? 0.1761 0.2770 0.1682 0.0777  -0.0063 -0.0594 5   ASN B CB  
900  C  CG  . ASN B 5   ? 0.1785 0.3539 0.1937 0.0339  0.0968  -0.1026 5   ASN B CG  
901  O  OD1 . ASN B 5   ? 0.2572 0.3953 0.1963 -0.0619 0.0057  -0.0920 5   ASN B OD1 
902  N  ND2 . ASN B 5   ? 0.2446 0.4037 0.1895 -0.0123 0.0740  -0.0923 5   ASN B ND2 
903  N  N   . THR B 6   ? 0.1635 0.2339 0.1612 0.0462  -0.0534 -0.0663 6   THR B N   
904  C  CA  . THR B 6   ? 0.1582 0.2355 0.1763 0.0384  -0.0233 -0.0306 6   THR B CA  
905  C  C   . THR B 6   ? 0.1953 0.1790 0.1586 0.0225  -0.0186 -0.0838 6   THR B C   
906  O  O   . THR B 6   ? 0.1962 0.1792 0.1351 0.0340  -0.0137 -0.0608 6   THR B O   
907  C  CB  . THR B 6   ? 0.1892 0.2384 0.1971 0.0104  -0.0095 -0.0440 6   THR B CB  
908  O  OG1 . THR B 6   ? 0.2006 0.3131 0.1829 0.0197  -0.0261 -0.0692 6   THR B OG1 
909  C  CG2 . THR B 6   ? 0.2016 0.3194 0.2232 -0.0352 0.0362  -0.0970 6   THR B CG2 
910  N  N   . PHE B 7   ? 0.2105 0.1654 0.1605 0.0293  0.0226  -0.0438 7   PHE B N   
911  C  CA  . PHE B 7   ? 0.2058 0.1505 0.1766 0.0419  -0.0096 -0.0341 7   PHE B CA  
912  C  C   . PHE B 7   ? 0.1755 0.1422 0.1793 0.0397  -0.0145 -0.0242 7   PHE B C   
913  O  O   . PHE B 7   ? 0.1913 0.1564 0.1971 0.0087  0.0356  -0.0577 7   PHE B O   
914  C  CB  . PHE B 7   ? 0.2250 0.1449 0.1803 0.0421  0.0245  0.0062  7   PHE B CB  
915  C  CG  . PHE B 7   ? 0.2142 0.1609 0.1816 0.0556  0.0255  0.0009  7   PHE B CG  
916  C  CD1 . PHE B 7   ? 0.1694 0.1940 0.1736 0.0723  -0.0298 -0.0157 7   PHE B CD1 
917  C  CD2 . PHE B 7   ? 0.2433 0.1779 0.1767 0.0457  -0.0122 0.0147  7   PHE B CD2 
918  C  CE1 . PHE B 7   ? 0.2037 0.1971 0.1764 0.0652  -0.0021 -0.0665 7   PHE B CE1 
919  C  CE2 . PHE B 7   ? 0.2532 0.2037 0.1769 0.0385  0.0409  -0.0008 7   PHE B CE2 
920  C  CZ  . PHE B 7   ? 0.2303 0.1958 0.1712 0.0616  0.0305  -0.0438 7   PHE B CZ  
921  N  N   . ASP B 8   ? 0.1634 0.1946 0.1689 0.0183  0.0334  -0.0274 8   ASP B N   
922  C  CA  . ASP B 8   ? 0.1754 0.2339 0.1649 0.0528  0.0033  -0.0846 8   ASP B CA  
923  C  C   . ASP B 8   ? 0.1887 0.2368 0.1445 0.0382  -0.0122 -0.0580 8   ASP B C   
924  O  O   . ASP B 8   ? 0.2373 0.2660 0.1292 0.0199  0.0061  -0.0187 8   ASP B O   
925  C  CB  . ASP B 8   ? 0.3296 0.2480 0.1484 -0.0138 0.0065  -0.0561 8   ASP B CB  
926  C  CG  . ASP B 8   ? 0.4274 0.2247 0.2543 0.0084  0.0385  -0.0038 8   ASP B CG  
927  O  OD1 . ASP B 8   ? 0.3910 0.1956 0.2338 0.0915  0.0281  -0.0498 8   ASP B OD1 
928  O  OD2 . ASP B 8   ? 0.4626 0.2297 0.3429 -0.0032 0.0369  0.0238  8   ASP B OD2 
929  N  N   . GLY B 9   ? 0.2253 0.1925 0.1651 0.0154  -0.0046 -0.0365 9   GLY B N   
930  C  CA  . GLY B 9   ? 0.2472 0.1918 0.1698 0.0109  0.0135  -0.0184 9   GLY B CA  
931  C  C   . GLY B 9   ? 0.2086 0.1864 0.1322 0.0393  0.0384  -0.0226 9   GLY B C   
932  O  O   . GLY B 9   ? 0.2398 0.1939 0.1344 0.0374  -0.0115 -0.0406 9   GLY B O   
933  N  N   . VAL B 10  ? 0.1860 0.1853 0.1330 0.0603  -0.0138 -0.0442 10  VAL B N   
934  C  CA  . VAL B 10  ? 0.2180 0.1577 0.1130 0.0673  -0.0294 0.0010  10  VAL B CA  
935  C  C   . VAL B 10  ? 0.2347 0.1534 0.1183 0.0281  -0.0047 0.0114  10  VAL B C   
936  O  O   . VAL B 10  ? 0.2533 0.1552 0.1144 0.0394  -0.0064 0.0208  10  VAL B O   
937  C  CB  . VAL B 10  ? 0.2361 0.1766 0.1110 0.0545  0.0121  -0.0072 10  VAL B CB  
938  C  CG1 . VAL B 10  ? 0.2713 0.1797 0.1074 0.0329  0.0148  -0.0375 10  VAL B CG1 
939  C  CG2 . VAL B 10  ? 0.2637 0.1591 0.1085 0.0384  -0.0100 -0.0189 10  VAL B CG2 
940  N  N   . ALA B 11  ? 0.2139 0.1603 0.1211 0.0466  0.0245  -0.0133 11  ALA B N   
941  C  CA  . ALA B 11  ? 0.2071 0.1686 0.1306 0.0339  -0.0125 -0.0586 11  ALA B CA  
942  C  C   . ALA B 11  ? 0.2123 0.1966 0.1271 0.0564  -0.0161 -0.0228 11  ALA B C   
943  O  O   . ALA B 11  ? 0.2553 0.1881 0.1325 0.0329  0.0095  -0.0391 11  ALA B O   
944  C  CB  . ALA B 11  ? 0.1875 0.1770 0.1597 0.0631  0.0043  -0.0695 11  ALA B CB  
945  N  N   . ASP B 12  ? 0.2094 0.1988 0.1168 0.0664  -0.0514 -0.0422 12  ASP B N   
946  C  CA  . ASP B 12  ? 0.2369 0.2342 0.1112 0.0903  -0.0635 -0.0372 12  ASP B CA  
947  C  C   . ASP B 12  ? 0.2344 0.2354 0.0891 0.0877  -0.0058 -0.0036 12  ASP B C   
948  O  O   . ASP B 12  ? 0.3229 0.2515 0.0682 0.0691  0.0151  0.0176  12  ASP B O   
949  C  CB  . ASP B 12  ? 0.3425 0.2470 0.0789 0.0338  -0.1184 -0.0793 12  ASP B CB  
950  C  CG  . ASP B 12  ? 0.5006 0.2340 0.1164 0.0497  -0.0914 -0.0959 12  ASP B CG  
951  O  OD1 . ASP B 12  ? 0.4605 0.2179 0.2396 0.1783  -0.1313 -0.0705 12  ASP B OD1 
952  O  OD2 . ASP B 12  ? 0.6663 0.2622 0.1878 -0.0664 0.0447  -0.0617 12  ASP B OD2 
953  N  N   . TYR B 13  ? 0.2542 0.2291 0.0932 0.0847  0.0229  0.0138  13  TYR B N   
954  C  CA  . TYR B 13  ? 0.2693 0.2268 0.0931 0.0785  0.0237  0.0162  13  TYR B CA  
955  C  C   . TYR B 13  ? 0.2947 0.2269 0.0916 0.0567  0.0325  0.0215  13  TYR B C   
956  O  O   . TYR B 13  ? 0.3038 0.2157 0.1107 0.0623  0.0418  0.0075  13  TYR B O   
957  C  CB  . TYR B 13  ? 0.2632 0.2379 0.0898 0.0973  0.0444  0.0301  13  TYR B CB  
958  C  CG  . TYR B 13  ? 0.2924 0.2411 0.0873 0.1389  -0.0005 0.0072  13  TYR B CG  
959  C  CD1 . TYR B 13  ? 0.3780 0.2424 0.1078 0.0903  0.0725  -0.0060 13  TYR B CD1 
960  C  CD2 . TYR B 13  ? 0.2703 0.2422 0.1409 0.1619  -0.0655 -0.0132 13  TYR B CD2 
961  C  CE1 . TYR B 13  ? 0.4064 0.2394 0.1332 0.0822  0.0427  -0.0046 13  TYR B CE1 
962  C  CE2 . TYR B 13  ? 0.3129 0.2324 0.1867 0.1392  -0.0738 -0.0115 13  TYR B CE2 
963  C  CZ  . TYR B 13  ? 0.3877 0.2333 0.1837 0.1013  0.0038  -0.0158 13  TYR B CZ  
964  O  OH  . TYR B 13  ? 0.4032 0.2407 0.2630 0.1278  -0.0222 -0.0043 13  TYR B OH  
965  N  N   . LEU B 14  ? 0.2693 0.2037 0.1097 0.0719  0.0468  0.0208  14  LEU B N   
966  C  CA  . LEU B 14  ? 0.2596 0.1934 0.1306 0.0858  0.0149  0.0010  14  LEU B CA  
967  C  C   . LEU B 14  ? 0.2479 0.2232 0.1335 0.0779  0.0733  0.0192  14  LEU B C   
968  O  O   . LEU B 14  ? 0.3121 0.2250 0.1154 0.0493  0.0326  0.0098  14  LEU B O   
969  C  CB  . LEU B 14  ? 0.2654 0.2027 0.1297 0.0508  -0.0025 -0.0570 14  LEU B CB  
970  C  CG  . LEU B 14  ? 0.2497 0.2351 0.1278 0.0316  0.0614  -0.0910 14  LEU B CG  
971  C  CD1 . LEU B 14  ? 0.2755 0.2247 0.1257 0.0120  0.0192  0.0339  14  LEU B CD1 
972  C  CD2 . LEU B 14  ? 0.3533 0.2274 0.1211 0.0938  -0.0018 -0.0550 14  LEU B CD2 
973  N  N   . GLN B 15  ? 0.2682 0.2274 0.1086 0.0938  0.0397  -0.0172 15  GLN B N   
974  C  CA  . GLN B 15  ? 0.3203 0.2250 0.1034 0.0804  0.0504  -0.0292 15  GLN B CA  
975  C  C   . GLN B 15  ? 0.3069 0.2331 0.1016 0.0996  0.0173  0.0109  15  GLN B C   
976  O  O   . GLN B 15  ? 0.3566 0.2690 0.1141 0.0234  0.0189  0.0091  15  GLN B O   
977  C  CB  . GLN B 15  ? 0.2842 0.2289 0.1429 0.0980  0.0684  -0.0248 15  GLN B CB  
978  C  CG  . GLN B 15  ? 0.3394 0.2239 0.1337 0.1007  0.0117  0.0175  15  GLN B CG  
979  C  CD  . GLN B 15  ? 0.3182 0.2214 0.1717 0.1136  0.0697  -0.0070 15  GLN B CD  
980  O  OE1 . GLN B 15  ? 0.3699 0.1906 0.3102 0.0488  0.0869  -0.0234 15  GLN B OE1 
981  N  NE2 . GLN B 15  ? 0.3302 0.2387 0.2316 0.0801  0.1151  0.0448  15  GLN B NE2 
982  N  N   . THR B 16  ? 0.3246 0.2268 0.1421 0.0701  0.0456  0.0161  16  THR B N   
983  C  CA  . THR B 16  ? 0.3064 0.2262 0.1556 0.0660  -0.0096 0.0261  16  THR B CA  
984  C  C   . THR B 16  ? 0.3825 0.2209 0.1410 0.0687  0.0108  0.0420  16  THR B C   
985  O  O   . THR B 16  ? 0.4611 0.2388 0.1355 0.0467  0.0117  0.0348  16  THR B O   
986  C  CB  . THR B 16  ? 0.3589 0.3050 0.1610 -0.0116 -0.0622 -0.0169 16  THR B CB  
987  O  OG1 . THR B 16  ? 0.4800 0.2983 0.2928 -0.0775 0.0344  -0.0689 16  THR B OG1 
988  C  CG2 . THR B 16  ? 0.3007 0.3910 0.1511 0.0191  -0.0487 0.0214  16  THR B CG2 
989  N  N   . TYR B 17  ? 0.3670 0.2270 0.1436 0.1040  0.0077  0.0229  17  TYR B N   
990  C  CA  . TYR B 17  ? 0.3714 0.2216 0.1548 0.0945  0.0129  0.0476  17  TYR B CA  
991  C  C   . TYR B 17  ? 0.3773 0.2135 0.1503 0.0929  0.0341  0.0514  17  TYR B C   
992  O  O   . TYR B 17  ? 0.4240 0.2030 0.2171 0.0682  0.0060  0.0246  17  TYR B O   
993  C  CB  . TYR B 17  ? 0.3483 0.2459 0.2366 0.1120  0.0062  0.0382  17  TYR B CB  
994  C  CG  . TYR B 17  ? 0.3763 0.3286 0.2475 0.0539  -0.0453 0.0248  17  TYR B CG  
995  C  CD1 . TYR B 17  ? 0.5221 0.4117 0.2288 -0.0570 -0.0676 0.0248  17  TYR B CD1 
996  C  CD2 . TYR B 17  ? 0.3567 0.3250 0.2598 0.0669  -0.0419 0.0497  17  TYR B CD2 
997  C  CE1 . TYR B 17  ? 0.5306 0.4863 0.2342 -0.0856 -0.1048 0.0676  17  TYR B CE1 
998  C  CE2 . TYR B 17  ? 0.4273 0.4216 0.2686 -0.0277 -0.0304 0.0405  17  TYR B CE2 
999  C  CZ  . TYR B 17  ? 0.5025 0.5131 0.2541 -0.1023 -0.1099 0.0600  17  TYR B CZ  
1000 O  OH  . TYR B 17  ? 0.6472 0.6923 0.2539 -0.2686 -0.0696 0.0073  17  TYR B OH  
1001 N  N   . HIS B 18  ? 0.3748 0.2172 0.1384 0.0885  0.0553  0.0454  18  HIS B N   
1002 C  CA  . HIS B 18  ? 0.4070 0.2331 0.1270 0.0534  0.0845  -0.0081 18  HIS B CA  
1003 C  C   . HIS B 18  ? 0.3975 0.2037 0.1550 0.0559  0.0923  -0.0108 18  HIS B C   
1004 O  O   . HIS B 18  ? 0.4941 0.2189 0.1710 -0.0113 0.0941  -0.0292 18  HIS B O   
1005 C  CB  . HIS B 18  ? 0.5010 0.2874 0.1243 -0.0329 0.0978  -0.0355 18  HIS B CB  
1006 C  CG  . HIS B 18  ? 0.5068 0.2832 0.1220 -0.0837 0.1184  -0.0472 18  HIS B CG  
1007 N  ND1 . HIS B 18  ? 0.5696 0.2726 0.1227 -0.0993 0.1008  -0.0334 18  HIS B ND1 
1008 C  CD2 . HIS B 18  ? 0.5307 0.2785 0.1325 -0.0687 0.0854  -0.0265 18  HIS B CD2 
1009 C  CE1 . HIS B 18  ? 0.5513 0.2830 0.1254 -0.0643 0.1164  -0.0276 18  HIS B CE1 
1010 N  NE2 . HIS B 18  ? 0.5658 0.2787 0.1327 -0.0764 0.1035  0.0090  18  HIS B NE2 
1011 N  N   . LYS B 19  ? 0.4303 0.2591 0.0887 0.0215  0.0853  0.0367  19  LYS B N   
1012 C  CA  . LYS B 19  ? 0.4999 0.2462 0.0648 0.0108  0.0370  0.0472  19  LYS B CA  
1013 C  C   . LYS B 19  ? 0.3282 0.2383 0.0991 0.1086  0.0582  -0.0403 19  LYS B C   
1014 O  O   . LYS B 19  ? 0.4241 0.2409 0.0977 0.0597  0.0224  -0.0262 19  LYS B O   
1015 C  CB  . LYS B 19  ? 0.5019 0.2398 0.1690 0.0268  0.0301  0.0681  19  LYS B CB  
1016 C  CG  . LYS B 19  ? 0.4169 0.2682 0.2566 0.0613  0.0694  0.0521  19  LYS B CG  
1017 C  CD  . LYS B 19  ? 0.4090 0.2739 0.3048 0.0880  -0.0518 0.0764  19  LYS B CD  
1018 C  CE  . LYS B 19  ? 0.4329 0.2515 0.3096 0.0564  -0.0559 0.0155  19  LYS B CE  
1019 N  NZ  . LYS B 19  ? 0.6005 0.3071 0.2714 -0.0238 0.0293  -0.0931 19  LYS B NZ  
1020 N  N   . LEU B 20  ? 0.3092 0.2512 0.1027 0.0865  0.0328  -0.0481 20  LEU B N   
1021 C  CA  . LEU B 20  ? 0.2997 0.2848 0.1156 0.0727  -0.0038 -0.0262 20  LEU B CA  
1022 C  C   . LEU B 20  ? 0.3175 0.2595 0.0868 0.0700  0.0391  -0.0532 20  LEU B C   
1023 O  O   . LEU B 20  ? 0.3567 0.2522 0.1908 0.0855  -0.0220 0.0000  20  LEU B O   
1024 C  CB  . LEU B 20  ? 0.2573 0.2293 0.1197 0.0601  -0.0382 -0.0774 20  LEU B CB  
1025 C  CG  . LEU B 20  ? 0.2518 0.2316 0.1400 0.0044  -0.0308 -0.0794 20  LEU B CG  
1026 C  CD1 . LEU B 20  ? 0.2590 0.2487 0.1317 0.0362  -0.0078 -0.0267 20  LEU B CD1 
1027 C  CD2 . LEU B 20  ? 0.2001 0.2331 0.1654 0.0232  -0.0215 -0.0252 20  LEU B CD2 
1028 N  N   . PRO B 21  ? 0.3157 0.2737 0.1264 0.0565  -0.0104 -0.0261 21  PRO B N   
1029 C  CA  . PRO B 21  ? 0.2838 0.2925 0.1608 0.0987  0.0217  -0.0387 21  PRO B CA  
1030 C  C   . PRO B 21  ? 0.2880 0.3004 0.1674 0.1133  -0.0091 -0.0111 21  PRO B C   
1031 O  O   . PRO B 21  ? 0.3037 0.2505 0.1671 0.1339  -0.0318 -0.0232 21  PRO B O   
1032 C  CB  . PRO B 21  ? 0.2734 0.2996 0.2321 0.0831  -0.0020 -0.0523 21  PRO B CB  
1033 C  CG  . PRO B 21  ? 0.3019 0.2824 0.2317 0.0455  -0.0351 0.0158  21  PRO B CG  
1034 C  CD  . PRO B 21  ? 0.3044 0.2682 0.1445 0.0517  0.0087  -0.0376 21  PRO B CD  
1035 N  N   . ASP B 22  ? 0.2783 0.3063 0.1887 0.1421  -0.0025 -0.0209 22  ASP B N   
1036 C  CA  . ASP B 22  ? 0.3177 0.2898 0.2013 0.1350  -0.0559 0.0011  22  ASP B CA  
1037 C  C   . ASP B 22  ? 0.3436 0.2889 0.1850 0.1278  -0.0257 -0.0530 22  ASP B C   
1038 O  O   . ASP B 22  ? 0.4598 0.2897 0.1915 0.1549  0.0274  -0.0150 22  ASP B O   
1039 C  CB  . ASP B 22  ? 0.3572 0.2801 0.1826 0.1522  -0.0653 0.0411  22  ASP B CB  
1040 C  CG  . ASP B 22  ? 0.4753 0.3385 0.1864 0.0214  -0.1010 0.0393  22  ASP B CG  
1041 O  OD1 . ASP B 22  ? 0.5702 0.5243 0.3722 -0.1446 -0.0940 -0.0257 22  ASP B OD1 
1042 O  OD2 . ASP B 22  ? 0.7769 0.4513 0.1761 -0.1221 -0.0429 -0.0514 22  ASP B OD2 
1043 N  N   . ASN B 23  ? 0.3031 0.2906 0.1854 0.1028  -0.0483 -0.0182 23  ASN B N   
1044 C  CA  . ASN B 23  ? 0.2154 0.2956 0.1939 0.0982  0.0067  -0.0246 23  ASN B CA  
1045 C  C   . ASN B 23  ? 0.2211 0.2709 0.1901 0.0959  -0.0093 -0.0265 23  ASN B C   
1046 O  O   . ASN B 23  ? 0.2052 0.3826 0.1915 0.0390  0.0107  0.0106  23  ASN B O   
1047 C  CB  . ASN B 23  ? 0.2348 0.3197 0.2486 0.0561  0.0674  -0.0563 23  ASN B CB  
1048 C  CG  . ASN B 23  ? 0.3151 0.2889 0.1966 0.0211  0.1059  -0.0512 23  ASN B CG  
1049 O  OD1 . ASN B 23  ? 0.3708 0.3310 0.1784 0.0933  0.1232  -0.0312 23  ASN B OD1 
1050 N  ND2 . ASN B 23  ? 0.3273 0.2900 0.2052 0.0326  -0.0248 -0.0735 23  ASN B ND2 
1051 N  N   . TYR B 24  ? 0.2482 0.2364 0.1351 0.0808  -0.0209 -0.0340 24  TYR B N   
1052 C  CA  . TYR B 24  ? 0.2563 0.1699 0.1357 0.0899  0.0257  -0.0440 24  TYR B CA  
1053 C  C   . TYR B 24  ? 0.2586 0.1678 0.1491 0.0837  0.0173  -0.0239 24  TYR B C   
1054 O  O   . TYR B 24  ? 0.3753 0.1815 0.1386 0.0624  0.0577  0.0133  24  TYR B O   
1055 C  CB  . TYR B 24  ? 0.2720 0.1654 0.1555 0.0753  0.0088  -0.0165 24  TYR B CB  
1056 C  CG  . TYR B 24  ? 0.2027 0.1710 0.1215 0.0653  -0.0355 -0.0072 24  TYR B CG  
1057 C  CD1 . TYR B 24  ? 0.1924 0.1774 0.1071 0.0494  -0.0278 -0.0325 24  TYR B CD1 
1058 C  CD2 . TYR B 24  ? 0.2373 0.1801 0.0988 0.0839  -0.0071 -0.0042 24  TYR B CD2 
1059 C  CE1 . TYR B 24  ? 0.1730 0.1812 0.0984 0.0730  -0.0030 -0.0604 24  TYR B CE1 
1060 C  CE2 . TYR B 24  ? 0.2068 0.1823 0.0919 0.0660  -0.0451 -0.0305 24  TYR B CE2 
1061 C  CZ  . TYR B 24  ? 0.1804 0.1712 0.0993 0.0623  -0.0255 -0.0500 24  TYR B CZ  
1062 O  OH  . TYR B 24  ? 0.2723 0.1668 0.1558 0.0621  -0.0244 -0.0735 24  TYR B OH  
1063 N  N   . ILE B 25  ? 0.2370 0.1679 0.1500 0.0499  0.0330  -0.0489 25  ILE B N   
1064 C  CA  . ILE B 25  ? 0.2066 0.1595 0.1539 0.0684  0.0514  -0.0354 25  ILE B CA  
1065 C  C   . ILE B 25  ? 0.2054 0.1167 0.2022 0.0519  0.0569  0.0013  25  ILE B C   
1066 O  O   . ILE B 25  ? 0.2027 0.1253 0.1701 0.0301  0.0294  -0.0059 25  ILE B O   
1067 C  CB  . ILE B 25  ? 0.1710 0.1749 0.2094 0.0657  0.0216  0.0040  25  ILE B CB  
1068 C  CG1 . ILE B 25  ? 0.1858 0.2637 0.1877 0.0193  0.0662  -0.0424 25  ILE B CG1 
1069 C  CG2 . ILE B 25  ? 0.1946 0.1816 0.2419 0.0576  0.0087  0.0262  25  ILE B CG2 
1070 C  CD1 . ILE B 25  ? 0.2278 0.2707 0.1379 0.0924  0.0027  -0.0607 25  ILE B CD1 
1071 N  N   . THR B 26  ? 0.2474 0.1270 0.2059 0.0172  0.0752  0.0257  26  THR B N   
1072 C  CA  . THR B 26  ? 0.2101 0.1430 0.2187 0.0274  0.0790  0.0054  26  THR B CA  
1073 C  C   . THR B 26  ? 0.2204 0.1110 0.2178 0.0261  0.0521  0.0334  26  THR B C   
1074 O  O   . THR B 26  ? 0.1973 0.1488 0.2085 0.0436  0.0311  -0.0049 26  THR B O   
1075 C  CB  . THR B 26  ? 0.2996 0.1575 0.2121 -0.0414 0.1773  -0.0180 26  THR B CB  
1076 O  OG1 . THR B 26  ? 0.2750 0.1656 0.2459 -0.0084 0.0669  -0.0538 26  THR B OG1 
1077 C  CG2 . THR B 26  ? 0.2685 0.2335 0.2134 -0.0611 0.0583  -0.0155 26  THR B CG2 
1078 N  N   . LYS B 27  ? 0.2392 0.0865 0.2312 0.0289  0.0249  0.0144  27  LYS B N   
1079 C  CA  . LYS B 27  ? 0.1865 0.1628 0.2216 0.0068  0.0203  0.0018  27  LYS B CA  
1080 C  C   . LYS B 27  ? 0.1706 0.1575 0.1971 -0.0089 0.0257  0.0150  27  LYS B C   
1081 O  O   . LYS B 27  ? 0.2041 0.1539 0.1657 -0.0132 0.0309  -0.0324 27  LYS B O   
1082 C  CB  . LYS B 27  ? 0.1612 0.1794 0.2487 0.0385  0.0035  -0.0351 27  LYS B CB  
1083 C  CG  . LYS B 27  ? 0.2808 0.1695 0.3903 0.0846  -0.0283 0.0089  27  LYS B CG  
1084 C  CD  . LYS B 27  ? 0.2447 0.1631 0.4766 0.0717  -0.0580 0.0217  27  LYS B CD  
1085 C  CE  . LYS B 27  ? 0.2602 0.3155 0.4071 0.0066  -0.0871 -0.0083 27  LYS B CE  
1086 N  NZ  . LYS B 27  ? 0.3908 0.4344 0.3793 -0.1068 -0.0297 -0.0986 27  LYS B NZ  
1087 N  N   . SER B 28  ? 0.1796 0.1678 0.2323 -0.0254 0.0698  -0.0102 28  SER B N   
1088 C  CA  . SER B 28  ? 0.2251 0.1581 0.2760 -0.0288 0.0699  -0.0230 28  SER B CA  
1089 C  C   . SER B 28  ? 0.2403 0.1412 0.2409 -0.0156 0.0569  -0.0391 28  SER B C   
1090 O  O   . SER B 28  ? 0.2875 0.1041 0.2479 -0.0002 0.0233  -0.0475 28  SER B O   
1091 C  CB  A SER B 28  ? 0.2715 0.1824 0.2928 -0.0716 0.0994  -0.0483 28  SER B CB  
1092 C  CB  B SER B 28  ? 0.2706 0.1808 0.2635 -0.0690 0.1004  -0.0500 28  SER B CB  
1093 O  OG  A SER B 28  ? 0.2404 0.1651 0.3820 -0.0481 -0.0014 -0.0648 28  SER B OG  
1094 O  OG  B SER B 28  ? 0.4042 0.2571 0.2594 -0.1211 0.0291  -0.0046 28  SER B OG  
1095 N  N   . GLU B 29  ? 0.2528 0.1097 0.2436 -0.0044 0.0409  -0.0057 29  GLU B N   
1096 C  CA  . GLU B 29  ? 0.2713 0.0861 0.2227 -0.0139 0.0784  -0.0283 29  GLU B CA  
1097 C  C   . GLU B 29  ? 0.2579 0.1004 0.2160 -0.0099 0.0095  0.0109  29  GLU B C   
1098 O  O   . GLU B 29  ? 0.2193 0.1313 0.2094 0.0646  0.0303  0.0050  29  GLU B O   
1099 C  CB  . GLU B 29  ? 0.2693 0.1453 0.2191 0.0331  0.0719  -0.0077 29  GLU B CB  
1100 C  CG  . GLU B 29  ? 0.4705 0.2102 0.2162 -0.0746 0.0812  0.0204  29  GLU B CG  
1101 C  CD  . GLU B 29  ? 0.6480 0.2534 0.2000 -0.1345 0.1071  0.0364  29  GLU B CD  
1102 O  OE1 . GLU B 29  ? 0.4379 0.2245 0.2254 -0.0002 0.0080  0.0103  29  GLU B OE1 
1103 O  OE2 . GLU B 29  ? 0.7057 0.2479 0.2010 -0.0949 0.0744  0.0290  29  GLU B OE2 
1104 N  N   . ALA B 30  ? 0.2017 0.1150 0.1317 0.0081  0.0341  0.0053  30  ALA B N   
1105 C  CA  . ALA B 30  ? 0.1526 0.1084 0.1417 0.0417  0.0012  -0.0247 30  ALA B CA  
1106 C  C   . ALA B 30  ? 0.1331 0.1118 0.1347 0.0698  0.0300  -0.0246 30  ALA B C   
1107 O  O   . ALA B 30  ? 0.1501 0.1166 0.1417 0.0457  -0.0041 -0.0041 30  ALA B O   
1108 C  CB  . ALA B 30  ? 0.2418 0.0969 0.1179 0.0043  0.0030  -0.0173 30  ALA B CB  
1109 N  N   . GLN B 31  ? 0.1465 0.1740 0.1378 0.0282  -0.0293 -0.0075 31  GLN B N   
1110 C  CA  . GLN B 31  ? 0.2346 0.1647 0.1250 0.0039  -0.0364 -0.0563 31  GLN B CA  
1111 C  C   . GLN B 31  ? 0.2524 0.1617 0.1652 0.0120  -0.0393 -0.0438 31  GLN B C   
1112 O  O   . GLN B 31  ? 0.2167 0.1611 0.1915 0.0324  -0.0149 -0.0147 31  GLN B O   
1113 C  CB  . GLN B 31  ? 0.2392 0.1985 0.1592 -0.0225 -0.0569 -0.0414 31  GLN B CB  
1114 C  CG  . GLN B 31  ? 0.2063 0.2061 0.3131 0.0182  -0.0768 0.0075  31  GLN B CG  
1115 C  CD  . GLN B 31  ? 0.1751 0.2440 0.4807 0.0319  -0.1212 0.0962  31  GLN B CD  
1116 O  OE1 . GLN B 31  ? 0.3355 0.2784 0.6182 -0.1141 -0.1547 -0.0102 31  GLN B OE1 
1117 N  NE2 . GLN B 31  ? 0.1442 0.2793 0.5144 0.0517  -0.0527 0.0558  31  GLN B NE2 
1118 N  N   . ALA B 32  ? 0.2517 0.1522 0.1817 0.0040  -0.0292 -0.0362 32  ALA B N   
1119 C  CA  . ALA B 32  ? 0.2867 0.1433 0.2217 -0.0043 -0.0075 -0.0606 32  ALA B CA  
1120 C  C   . ALA B 32  ? 0.2525 0.1562 0.1834 0.0348  0.0281  -0.0757 32  ALA B C   
1121 O  O   . ALA B 32  ? 0.2823 0.1483 0.2271 0.0203  0.0666  -0.0262 32  ALA B O   
1122 C  CB  . ALA B 32  ? 0.2625 0.1354 0.2352 0.0138  0.0601  0.0108  32  ALA B CB  
1123 N  N   . LEU B 33  ? 0.2105 0.1546 0.1879 0.0497  -0.0250 -0.0693 33  LEU B N   
1124 C  CA  . LEU B 33  ? 0.1943 0.1998 0.1892 0.0561  -0.0302 -0.0452 33  LEU B CA  
1125 C  C   . LEU B 33  ? 0.1741 0.1982 0.1933 0.0646  0.0005  -0.0298 33  LEU B C   
1126 O  O   . LEU B 33  ? 0.1409 0.4255 0.1869 0.0353  -0.0076 -0.0402 33  LEU B O   
1127 C  CB  . LEU B 33  ? 0.1898 0.2333 0.1912 0.0352  -0.0369 -0.0007 33  LEU B CB  
1128 C  CG  . LEU B 33  ? 0.2401 0.2467 0.1892 0.0319  -0.0314 -0.0101 33  LEU B CG  
1129 C  CD1 . LEU B 33  ? 0.2702 0.2456 0.1892 0.0593  0.0023  -0.0408 33  LEU B CD1 
1130 C  CD2 . LEU B 33  ? 0.2867 0.2363 0.2026 0.0420  -0.0737 0.0289  33  LEU B CD2 
1131 N  N   . GLY B 34  ? 0.2181 0.1146 0.1978 0.0699  -0.0165 0.0180  34  GLY B N   
1132 C  CA  . GLY B 34  ? 0.1856 0.1242 0.2087 0.0377  -0.0345 0.0203  34  GLY B CA  
1133 C  C   . GLY B 34  ? 0.1393 0.1274 0.1698 0.0305  -0.0290 0.0006  34  GLY B C   
1134 O  O   . GLY B 34  ? 0.2056 0.1647 0.1295 0.0354  -0.0034 -0.0154 34  GLY B O   
1135 N  N   . TRP B 35  ? 0.1784 0.1229 0.1424 0.0578  -0.0206 -0.0328 35  TRP B N   
1136 C  CA  . TRP B 35  ? 0.1761 0.1210 0.1212 0.0418  0.0090  -0.0571 35  TRP B CA  
1137 C  C   . TRP B 35  ? 0.1693 0.1239 0.1259 0.0145  -0.0399 -0.0250 35  TRP B C   
1138 O  O   . TRP B 35  ? 0.1659 0.1464 0.1819 0.0004  -0.0482 -0.0209 35  TRP B O   
1139 C  CB  . TRP B 35  ? 0.1769 0.1263 0.1274 0.0646  -0.0388 -0.0307 35  TRP B CB  
1140 C  CG  . TRP B 35  ? 0.1799 0.1194 0.1028 0.0572  -0.0141 -0.0130 35  TRP B CG  
1141 C  CD1 . TRP B 35  ? 0.1819 0.1334 0.1435 0.0380  -0.0129 -0.0208 35  TRP B CD1 
1142 C  CD2 . TRP B 35  ? 0.1849 0.1192 0.1117 0.0416  -0.0165 -0.0323 35  TRP B CD2 
1143 N  NE1 . TRP B 35  ? 0.2245 0.1115 0.1323 0.0177  0.0425  -0.0065 35  TRP B NE1 
1144 C  CE2 . TRP B 35  ? 0.1787 0.1222 0.0971 0.0680  0.0084  -0.0188 35  TRP B CE2 
1145 C  CE3 . TRP B 35  ? 0.1909 0.1436 0.1601 0.0309  0.0116  -0.0210 35  TRP B CE3 
1146 C  CZ2 . TRP B 35  ? 0.2055 0.1147 0.1456 0.0438  0.0350  -0.0070 35  TRP B CZ2 
1147 C  CZ3 . TRP B 35  ? 0.1922 0.1508 0.1760 0.0068  -0.0038 -0.0123 35  TRP B CZ3 
1148 C  CH2 . TRP B 35  ? 0.1782 0.1539 0.1644 0.0494  -0.0039 0.0143  35  TRP B CH2 
1149 N  N   . VAL B 36  ? 0.1381 0.1296 0.1197 0.0270  -0.0320 0.0027  36  VAL B N   
1150 C  CA  . VAL B 36  ? 0.1648 0.1512 0.1076 0.0309  -0.0354 0.0088  36  VAL B CA  
1151 C  C   . VAL B 36  ? 0.1568 0.1407 0.1136 0.0143  -0.0105 -0.0006 36  VAL B C   
1152 O  O   . VAL B 36  ? 0.1307 0.1608 0.1157 0.0200  -0.0069 -0.0054 36  VAL B O   
1153 C  CB  . VAL B 36  ? 0.1514 0.1579 0.1159 0.0480  -0.0147 -0.0129 36  VAL B CB  
1154 C  CG1 . VAL B 36  ? 0.2116 0.1902 0.0983 0.0441  -0.0375 -0.0813 36  VAL B CG1 
1155 C  CG2 . VAL B 36  ? 0.2197 0.1527 0.1496 0.0519  -0.0562 -0.0250 36  VAL B CG2 
1156 N  N   . ALA B 37  ? 0.1567 0.1416 0.1321 0.0088  -0.0314 0.0037  37  ALA B N   
1157 C  CA  . ALA B 37  ? 0.1407 0.1509 0.0973 0.0214  -0.0020 -0.0038 37  ALA B CA  
1158 C  C   . ALA B 37  ? 0.1238 0.1447 0.0960 0.0435  -0.0049 -0.0081 37  ALA B C   
1159 O  O   . ALA B 37  ? 0.1911 0.1477 0.1086 0.0089  0.0033  0.0207  37  ALA B O   
1160 C  CB  . ALA B 37  ? 0.1284 0.1674 0.1572 0.0256  0.0315  -0.0184 37  ALA B CB  
1161 N  N   . SER B 38  ? 0.1336 0.1662 0.0958 0.0397  -0.0099 0.0044  38  SER B N   
1162 C  CA  . SER B 38  ? 0.1458 0.1818 0.0974 0.0250  -0.0208 -0.0004 38  SER B CA  
1163 C  C   . SER B 38  ? 0.1666 0.1580 0.1343 0.0047  0.0082  0.0137  38  SER B C   
1164 O  O   . SER B 38  ? 0.2094 0.1669 0.1438 0.0016  -0.0049 0.0586  38  SER B O   
1165 C  CB  A SER B 38  ? 0.1471 0.1964 0.0963 0.0223  -0.0346 -0.0016 38  SER B CB  
1166 C  CB  B SER B 38  ? 0.1471 0.1908 0.0962 0.0255  -0.0332 -0.0022 38  SER B CB  
1167 O  OG  A SER B 38  ? 0.1528 0.2388 0.0630 -0.0025 -0.0632 -0.0329 38  SER B OG  
1168 O  OG  B SER B 38  ? 0.2638 0.1655 0.1545 0.0679  0.0235  -0.0039 38  SER B OG  
1169 N  N   . LYS B 39  ? 0.1444 0.1698 0.1495 0.0148  -0.0278 0.0063  39  LYS B N   
1170 C  CA  . LYS B 39  ? 0.1453 0.2312 0.1294 -0.0064 0.0058  -0.0141 39  LYS B CA  
1171 C  C   . LYS B 39  ? 0.1545 0.2348 0.1288 -0.0176 -0.0218 0.0317  39  LYS B C   
1172 O  O   . LYS B 39  ? 0.1814 0.2675 0.1485 -0.0495 0.0221  -0.0380 39  LYS B O   
1173 C  CB  . LYS B 39  ? 0.1181 0.2256 0.2415 -0.0152 0.0086  -0.1008 39  LYS B CB  
1174 C  CG  . LYS B 39  ? 0.4721 0.1504 0.2829 -0.0418 -0.0273 -0.0978 39  LYS B CG  
1175 C  CD  . LYS B 39  ? 0.3922 0.1753 0.3923 -0.0160 0.0061  -0.0984 39  LYS B CD  
1176 C  CE  . LYS B 39  ? 0.4006 0.2323 0.4828 -0.0688 -0.0665 -0.0443 39  LYS B CE  
1177 N  NZ  . LYS B 39  ? 0.2649 0.3096 0.7105 0.0839  -0.0296 -0.1990 39  LYS B NZ  
1178 N  N   . GLY B 40  ? 0.1586 0.1197 0.1488 0.0032  0.0248  0.0240  40  GLY B N   
1179 C  CA  . GLY B 40  ? 0.1604 0.1538 0.1509 -0.0012 0.0227  -0.0036 40  GLY B CA  
1180 C  C   . GLY B 40  ? 0.1501 0.1645 0.1458 0.0035  0.0359  -0.0071 40  GLY B C   
1181 O  O   . GLY B 40  ? 0.1900 0.1700 0.1498 -0.0297 -0.0139 -0.0172 40  GLY B O   
1182 N  N   . ASN B 41  ? 0.1421 0.1624 0.1247 -0.0047 0.0060  0.0221  41  ASN B N   
1183 C  CA  . ASN B 41  ? 0.1255 0.1791 0.1224 0.0292  -0.0196 0.0010  41  ASN B CA  
1184 C  C   . ASN B 41  ? 0.1244 0.1682 0.1245 0.0580  -0.0373 0.0021  41  ASN B C   
1185 O  O   . ASN B 41  ? 0.1355 0.1669 0.1164 0.0463  -0.0311 -0.0231 41  ASN B O   
1186 C  CB  . ASN B 41  ? 0.1393 0.1903 0.1206 0.0517  -0.0058 -0.0443 41  ASN B CB  
1187 C  CG  . ASN B 41  ? 0.1719 0.1824 0.1144 0.0395  -0.0434 -0.0487 41  ASN B CG  
1188 O  OD1 . ASN B 41  ? 0.1569 0.1957 0.1719 0.0314  -0.0180 -0.0300 41  ASN B OD1 
1189 N  ND2 . ASN B 41  ? 0.1832 0.1784 0.2252 0.0506  -0.0294 -0.0809 41  ASN B ND2 
1190 N  N   . LEU B 42  ? 0.1228 0.1724 0.1229 0.0536  -0.0407 -0.0587 42  LEU B N   
1191 C  CA  . LEU B 42  ? 0.1546 0.1748 0.1129 0.0790  -0.0111 -0.0409 42  LEU B CA  
1192 C  C   . LEU B 42  ? 0.1511 0.1894 0.1237 0.0611  -0.0042 -0.0187 42  LEU B C   
1193 O  O   . LEU B 42  ? 0.1737 0.1912 0.1034 0.0546  0.0089  0.0047  42  LEU B O   
1194 C  CB  . LEU B 42  ? 0.1506 0.1765 0.1166 0.0684  0.0001  -0.0241 42  LEU B CB  
1195 C  CG  . LEU B 42  ? 0.1735 0.1506 0.1285 0.0131  0.0058  -0.0190 42  LEU B CG  
1196 C  CD1 . LEU B 42  ? 0.2699 0.1474 0.2330 -0.0010 0.0659  -0.0215 42  LEU B CD1 
1197 C  CD2 . LEU B 42  ? 0.1640 0.1696 0.1381 -0.0148 0.0843  -0.0351 42  LEU B CD2 
1198 N  N   . ALA B 43  ? 0.1863 0.1813 0.1391 0.0526  -0.0267 -0.0456 43  ALA B N   
1199 C  CA  . ALA B 43  ? 0.1829 0.2245 0.1620 0.0242  -0.1066 -0.0414 43  ALA B CA  
1200 C  C   . ALA B 43  ? 0.1680 0.2264 0.1883 0.0324  -0.1005 -0.0200 43  ALA B C   
1201 O  O   . ALA B 43  ? 0.1599 0.2727 0.1732 0.0593  -0.0541 -0.0086 43  ALA B O   
1202 C  CB  . ALA B 43  ? 0.1473 0.2224 0.3027 0.0366  -0.0976 -0.0686 43  ALA B CB  
1203 N  N   . ASP B 44  ? 0.1127 0.2220 0.1927 0.0133  -0.0863 -0.0205 44  ASP B N   
1204 C  CA  . ASP B 44  ? 0.1059 0.2419 0.1798 0.0546  -0.0018 -0.0241 44  ASP B CA  
1205 C  C   . ASP B 44  ? 0.1286 0.2338 0.1815 0.0725  0.0227  -0.0559 44  ASP B C   
1206 O  O   . ASP B 44  ? 0.1241 0.2314 0.2461 0.0478  0.0005  -0.0454 44  ASP B O   
1207 C  CB  . ASP B 44  ? 0.1834 0.2785 0.1716 0.0576  0.0184  0.0011  44  ASP B CB  
1208 C  CG  . ASP B 44  ? 0.5069 0.2861 0.1830 -0.0696 -0.0199 0.0640  44  ASP B CG  
1209 O  OD1 . ASP B 44  ? 0.4256 0.3528 0.3287 -0.1011 0.0349  0.0017  44  ASP B OD1 
1210 O  OD2 . ASP B 44  ? 0.9737 0.3661 0.1405 -0.2106 -0.0763 0.0639  44  ASP B OD2 
1211 N  N   . VAL B 45  ? 0.1265 0.1812 0.1489 0.0951  -0.0539 -0.0145 45  VAL B N   
1212 C  CA  . VAL B 45  ? 0.1495 0.1798 0.1701 0.0853  -0.1098 -0.0384 45  VAL B CA  
1213 C  C   . VAL B 45  ? 0.1540 0.1645 0.1704 0.0938  -0.1187 -0.0017 45  VAL B C   
1214 O  O   . VAL B 45  ? 0.1505 0.1720 0.1702 0.0901  0.0025  -0.0033 45  VAL B O   
1215 C  CB  . VAL B 45  ? 0.1853 0.2719 0.1721 0.0216  -0.0543 0.0013  45  VAL B CB  
1216 C  CG1 . VAL B 45  ? 0.2957 0.2532 0.1702 0.0070  -0.0035 0.0146  45  VAL B CG1 
1217 C  CG2 . VAL B 45  ? 0.1590 0.3162 0.2461 -0.0019 -0.0602 0.0312  45  VAL B CG2 
1218 N  N   . ALA B 46  ? 0.2165 0.1474 0.1635 0.0511  -0.0306 -0.0673 46  ALA B N   
1219 C  CA  . ALA B 46  ? 0.1675 0.1658 0.1678 0.0537  -0.0247 -0.0573 46  ALA B CA  
1220 C  C   . ALA B 46  ? 0.1278 0.1773 0.1548 0.0561  -0.0362 -0.0534 46  ALA B C   
1221 O  O   . ALA B 46  ? 0.1377 0.1664 0.1540 0.0444  -0.0054 -0.0300 46  ALA B O   
1222 C  CB  . ALA B 46  ? 0.2292 0.1800 0.2117 -0.0241 -0.0259 -0.0298 46  ALA B CB  
1223 N  N   . PRO B 47  ? 0.1022 0.2407 0.1544 0.0593  -0.0415 -0.0315 47  PRO B N   
1224 C  CA  . PRO B 47  ? 0.1562 0.2626 0.1599 0.0112  -0.0377 -0.0462 47  PRO B CA  
1225 C  C   . PRO B 47  ? 0.1710 0.2470 0.1571 0.0239  -0.0063 -0.0748 47  PRO B C   
1226 O  O   . PRO B 47  ? 0.2436 0.2564 0.1382 0.0815  -0.0354 -0.0574 47  PRO B O   
1227 C  CB  . PRO B 47  ? 0.1581 0.2883 0.1851 -0.0092 -0.0014 -0.1025 47  PRO B CB  
1228 C  CG  . PRO B 47  ? 0.1111 0.3011 0.1848 0.0151  -0.0056 -0.0933 47  PRO B CG  
1229 C  CD  . PRO B 47  ? 0.0872 0.2680 0.1566 0.0444  0.0080  -0.0325 47  PRO B CD  
1230 N  N   . GLY B 48  ? 0.1362 0.2501 0.1925 0.0350  0.0308  -0.1025 48  GLY B N   
1231 C  CA  . GLY B 48  ? 0.1678 0.2315 0.1992 0.0159  0.0448  -0.1004 48  GLY B CA  
1232 C  C   . GLY B 48  ? 0.1860 0.2600 0.1421 -0.0165 0.0619  -0.0749 48  GLY B C   
1233 O  O   . GLY B 48  ? 0.1724 0.2873 0.1399 0.0524  -0.0099 -0.0919 48  GLY B O   
1234 N  N   . LYS B 49  ? 0.1391 0.2066 0.1553 0.0423  -0.0183 -0.0602 49  LYS B N   
1235 C  CA  . LYS B 49  ? 0.1291 0.1887 0.1531 0.0517  0.0096  0.0050  49  LYS B CA  
1236 C  C   . LYS B 49  ? 0.1481 0.1735 0.1402 0.0283  0.0291  -0.0514 49  LYS B C   
1237 O  O   . LYS B 49  ? 0.1495 0.2109 0.1384 0.0326  0.0034  -0.0147 49  LYS B O   
1238 C  CB  . LYS B 49  ? 0.1265 0.1810 0.2468 0.0656  0.0140  -0.0352 49  LYS B CB  
1239 C  CG  . LYS B 49  ? 0.2112 0.1902 0.2308 0.1204  -0.0116 -0.0512 49  LYS B CG  
1240 C  CD  . LYS B 49  ? 0.4484 0.2928 0.2114 0.0399  0.0251  0.0443  49  LYS B CD  
1241 C  CE  . LYS B 49  ? 0.4260 0.3066 0.2015 0.0714  0.0376  0.0142  49  LYS B CE  
1242 N  NZ  . LYS B 49  ? 0.3933 0.3411 0.4348 0.0770  -0.0942 -0.0398 49  LYS B NZ  
1243 N  N   . SER B 50  ? 0.1443 0.1640 0.1181 0.0587  -0.0059 -0.0332 50  SER B N   
1244 C  CA  . SER B 50  ? 0.1268 0.1762 0.1244 0.0392  0.0244  -0.0304 50  SER B CA  
1245 C  C   . SER B 50  ? 0.1629 0.1550 0.1399 0.0180  0.0726  -0.0239 50  SER B C   
1246 O  O   . SER B 50  ? 0.1782 0.1762 0.1282 0.0074  0.0267  -0.0192 50  SER B O   
1247 C  CB  . SER B 50  ? 0.1528 0.1515 0.1665 0.0332  -0.0084 -0.0154 50  SER B CB  
1248 O  OG  . SER B 50  ? 0.1551 0.1729 0.1667 0.0209  -0.0113 -0.0261 50  SER B OG  
1249 N  N   . ILE B 51  ? 0.1409 0.1217 0.1708 0.0191  0.0342  0.0158  51  ILE B N   
1250 C  CA  . ILE B 51  ? 0.1450 0.1325 0.1502 0.0212  0.0374  -0.0071 51  ILE B CA  
1251 C  C   . ILE B 51  ? 0.1305 0.1297 0.1332 0.0334  0.0017  0.0230  51  ILE B C   
1252 O  O   . ILE B 51  ? 0.1634 0.1332 0.1275 0.0317  0.0276  0.0002  51  ILE B O   
1253 C  CB  . ILE B 51  ? 0.1989 0.1977 0.1299 -0.0414 0.0749  -0.0354 51  ILE B CB  
1254 C  CG1 . ILE B 51  ? 0.1775 0.1903 0.1602 -0.0376 0.0017  -0.0131 51  ILE B CG1 
1255 C  CG2 . ILE B 51  ? 0.1636 0.1832 0.1283 -0.0041 0.0382  -0.0215 51  ILE B CG2 
1256 C  CD1 . ILE B 51  ? 0.1315 0.1929 0.2985 0.0198  0.0173  -0.0421 51  ILE B CD1 
1257 N  N   . GLY B 52  ? 0.1855 0.1467 0.1293 -0.0111 0.0779  0.0174  52  GLY B N   
1258 C  CA  . GLY B 52  ? 0.1951 0.1460 0.1202 -0.0221 0.0791  -0.0057 52  GLY B CA  
1259 C  C   . GLY B 52  ? 0.1971 0.1376 0.1212 -0.0100 0.0546  0.0157  52  GLY B C   
1260 O  O   . GLY B 52  ? 0.2221 0.1471 0.1781 0.0310  0.0786  0.0074  52  GLY B O   
1261 N  N   . GLY B 53  ? 0.1727 0.1783 0.1441 -0.0180 0.0657  -0.0208 53  GLY B N   
1262 C  CA  . GLY B 53  ? 0.1575 0.1276 0.2163 0.0135  0.0808  -0.0002 53  GLY B CA  
1263 C  C   . GLY B 53  ? 0.1892 0.1714 0.2237 -0.0305 0.0678  -0.0152 53  GLY B C   
1264 O  O   . GLY B 53  ? 0.2607 0.1875 0.2253 -0.0743 0.0853  -0.0405 53  GLY B O   
1265 N  N   . ASP B 54  ? 0.1552 0.1624 0.2270 0.0053  0.0141  -0.0289 54  ASP B N   
1266 C  CA  . ASP B 54  ? 0.1463 0.2197 0.2291 0.0050  0.0400  -0.0440 54  ASP B CA  
1267 C  C   . ASP B 54  ? 0.1704 0.2047 0.2359 -0.0397 0.0467  -0.0535 54  ASP B C   
1268 O  O   . ASP B 54  ? 0.1793 0.2066 0.2082 -0.0051 0.0775  -0.0726 54  ASP B O   
1269 C  CB  . ASP B 54  ? 0.1376 0.2500 0.2263 0.0332  0.0578  -0.0571 54  ASP B CB  
1270 C  CG  . ASP B 54  ? 0.1996 0.1860 0.2316 -0.0098 0.1286  -0.0633 54  ASP B CG  
1271 O  OD1 . ASP B 54  ? 0.3713 0.1914 0.3895 -0.0260 0.1342  -0.0795 54  ASP B OD1 
1272 O  OD2 . ASP B 54  ? 0.1543 0.2657 0.2681 0.0033  0.0783  -0.0152 54  ASP B OD2 
1273 N  N   . ILE B 55  ? 0.1883 0.2434 0.3018 -0.0723 0.1272  -0.1219 55  ILE B N   
1274 C  CA  . ILE B 55  ? 0.1402 0.2875 0.3243 -0.0264 0.1041  -0.1018 55  ILE B CA  
1275 C  C   . ILE B 55  ? 0.1462 0.2864 0.3258 -0.0222 0.0541  -0.0801 55  ILE B C   
1276 O  O   . ILE B 55  ? 0.1800 0.3028 0.3223 0.0135  0.0224  -0.0985 55  ILE B O   
1277 C  CB  . ILE B 55  ? 0.1563 0.2903 0.3752 -0.0364 0.1226  -0.1134 55  ILE B CB  
1278 C  CG1 . ILE B 55  ? 0.2621 0.2979 0.3749 -0.0935 0.1219  -0.0199 55  ILE B CG1 
1279 C  CG2 . ILE B 55  ? 0.1399 0.3247 0.4728 -0.0438 0.1344  -0.1078 55  ILE B CG2 
1280 C  CD1 . ILE B 55  ? 0.4297 0.1893 0.5496 -0.0291 -0.0083 0.0315  55  ILE B CD1 
1281 N  N   . PHE B 56  ? 0.1813 0.2836 0.3236 -0.0044 0.0433  -0.0957 56  PHE B N   
1282 C  CA  . PHE B 56  ? 0.1939 0.2842 0.3346 0.0211  0.0281  -0.1401 56  PHE B CA  
1283 C  C   . PHE B 56  ? 0.1508 0.3229 0.3289 0.0616  -0.0153 -0.1627 56  PHE B C   
1284 O  O   . PHE B 56  ? 0.1658 0.3392 0.3296 0.0201  0.0398  -0.1030 56  PHE B O   
1285 C  CB  . PHE B 56  ? 0.2447 0.2795 0.3497 -0.0057 0.0086  -0.1067 56  PHE B CB  
1286 C  CG  . PHE B 56  ? 0.2024 0.2858 0.3568 0.0007  0.0037  -0.0898 56  PHE B CG  
1287 C  CD1 . PHE B 56  ? 0.2368 0.2869 0.3536 -0.0259 -0.0747 -0.0126 56  PHE B CD1 
1288 C  CD2 . PHE B 56  ? 0.2076 0.2855 0.3837 0.0034  -0.0482 -0.0719 56  PHE B CD2 
1289 C  CE1 . PHE B 56  ? 0.2406 0.2967 0.3521 -0.0128 -0.0474 0.0069  56  PHE B CE1 
1290 C  CE2 . PHE B 56  ? 0.2200 0.2801 0.3880 0.0003  -0.0258 -0.0580 56  PHE B CE2 
1291 C  CZ  . PHE B 56  ? 0.2363 0.2974 0.3783 0.0089  -0.0310 -0.0125 56  PHE B CZ  
1292 N  N   . SER B 57  ? 0.2110 0.4398 0.3281 -0.0259 0.0123  -0.1708 57  SER B N   
1293 C  CA  . SER B 57  ? 0.1974 0.4800 0.3239 -0.0214 -0.0510 -0.1564 57  SER B CA  
1294 C  C   . SER B 57  ? 0.1862 0.4786 0.3594 0.0040  -0.0120 -0.1610 57  SER B C   
1295 O  O   . SER B 57  ? 0.1709 0.4653 0.5751 -0.0024 0.0295  -0.1589 57  SER B O   
1296 C  CB  . SER B 57  ? 0.2414 0.5025 0.3167 -0.0406 -0.0659 -0.1093 57  SER B CB  
1297 O  OG  . SER B 57  ? 0.6209 0.4942 0.2841 0.0151  0.0149  -0.0550 57  SER B OG  
1298 N  N   . ASN B 58  ? 0.2919 0.4727 0.3316 -0.0355 -0.0338 -0.1056 58  ASN B N   
1299 C  CA  . ASN B 58  ? 0.2898 0.4777 0.3475 0.0167  -0.0356 -0.1181 58  ASN B CA  
1300 C  C   . ASN B 58  ? 0.2779 0.4989 0.3527 0.0239  -0.0201 -0.1353 58  ASN B C   
1301 O  O   . ASN B 58  ? 0.2354 0.5408 0.4102 0.0585  0.0054  -0.1371 58  ASN B O   
1302 C  CB  . ASN B 58  ? 0.2821 0.4642 0.3512 0.0228  -0.0033 -0.1625 58  ASN B CB  
1303 C  CG  . ASN B 58  ? 0.2427 0.4678 0.3532 0.0067  0.0127  -0.1224 58  ASN B CG  
1304 O  OD1 . ASN B 58  ? 0.2937 0.4669 0.2914 0.0305  0.0472  -0.1050 58  ASN B OD1 
1305 N  ND2 . ASN B 58  ? 0.2187 0.4907 0.3650 -0.0041 -0.0059 -0.0005 58  ASN B ND2 
1306 N  N   . ARG B 59  ? 0.3339 0.5621 0.3417 -0.0106 -0.1041 -0.1434 59  ARG B N   
1307 C  CA  . ARG B 59  ? 0.3162 0.5692 0.3461 0.0153  -0.1418 -0.1122 59  ARG B CA  
1308 C  C   . ARG B 59  ? 0.2940 0.5791 0.4058 0.0730  -0.1284 -0.0798 59  ARG B C   
1309 O  O   . ARG B 59  ? 0.2677 0.6119 0.4161 0.1028  -0.0452 -0.0266 59  ARG B O   
1310 C  CB  . ARG B 59  ? 0.2876 0.5728 0.3454 -0.0036 -0.1556 -0.1132 59  ARG B CB  
1311 C  CG  . ARG B 59  ? 0.2827 0.5739 0.3509 -0.0022 -0.1558 -0.1131 59  ARG B CG  
1312 C  CD  . ARG B 59  ? 0.2840 0.5727 0.3510 -0.0047 -0.1559 -0.1129 59  ARG B CD  
1313 N  NE  . ARG B 59  ? 0.2853 0.5720 0.3511 -0.0064 -0.1560 -0.1129 59  ARG B NE  
1314 C  CZ  . ARG B 59  ? 0.2854 0.5718 0.3512 -0.0075 -0.1561 -0.1128 59  ARG B CZ  
1315 N  NH1 . ARG B 59  ? 0.2848 0.5718 0.3514 -0.0077 -0.1561 -0.1128 59  ARG B NH1 
1316 N  NH2 . ARG B 59  ? 0.2860 0.5712 0.3518 -0.0088 -0.1561 -0.1128 59  ARG B NH2 
1317 N  N   . GLU B 60  ? 0.3083 0.5599 0.4167 0.0740  -0.1086 -0.0793 60  GLU B N   
1318 C  CA  . GLU B 60  ? 0.2866 0.5708 0.4065 0.0952  -0.0785 -0.1018 60  GLU B CA  
1319 C  C   . GLU B 60  ? 0.2974 0.5727 0.4032 0.1184  -0.0713 -0.0496 60  GLU B C   
1320 O  O   . GLU B 60  ? 0.3567 0.5528 0.4099 0.1056  -0.0709 -0.1379 60  GLU B O   
1321 C  CB  . GLU B 60  ? 0.3252 0.5663 0.4259 0.0633  -0.0505 -0.1415 60  GLU B CB  
1322 C  CG  . GLU B 60  ? 0.3335 0.5889 0.4256 0.0331  -0.0450 -0.1858 60  GLU B CG  
1323 C  CD  . GLU B 60  ? 0.4056 0.6171 0.4429 -0.0283 -0.0283 -0.2163 60  GLU B CD  
1324 O  OE1 . GLU B 60  ? 0.5999 0.6251 0.4503 -0.1661 -0.1543 -0.0685 60  GLU B OE1 
1325 O  OE2 . GLU B 60  ? 0.3460 0.6193 0.4489 0.0033  -0.0021 -0.2638 60  GLU B OE2 
1326 N  N   . GLY B 61  ? 0.3295 0.5609 0.4024 0.0958  -0.0082 -0.0559 61  GLY B N   
1327 C  CA  . GLY B 61  ? 0.3120 0.5781 0.4029 0.0812  0.0004  -0.0713 61  GLY B CA  
1328 C  C   . GLY B 61  ? 0.3267 0.5977 0.3565 0.0653  0.0158  -0.0773 61  GLY B C   
1329 O  O   . GLY B 61  ? 0.2841 0.5905 0.3780 -0.0011 -0.0187 -0.0692 61  GLY B O   
1330 N  N   . LYS B 62  ? 0.2970 0.5066 0.2666 0.1242  -0.0160 -0.0251 62  LYS B N   
1331 C  CA  . LYS B 62  ? 0.2967 0.4813 0.2570 0.1396  0.0386  -0.0286 62  LYS B CA  
1332 C  C   . LYS B 62  ? 0.3557 0.4151 0.2657 0.1102  0.0176  -0.0600 62  LYS B C   
1333 O  O   . LYS B 62  ? 0.4694 0.4052 0.2533 0.1223  -0.0356 -0.0395 62  LYS B O   
1334 C  CB  . LYS B 62  ? 0.3516 0.5929 0.2701 0.0479  0.0475  0.0109  62  LYS B CB  
1335 C  CG  . LYS B 62  ? 0.4825 0.6664 0.2508 -0.0462 0.0217  0.0589  62  LYS B CG  
1336 C  CD  . LYS B 62  ? 0.6025 0.7729 0.2577 -0.1726 -0.0324 0.0962  62  LYS B CD  
1337 C  CE  . LYS B 62  ? 0.6439 0.8266 0.2552 -0.2317 -0.0221 0.0671  62  LYS B CE  
1338 N  NZ  . LYS B 62  ? 0.8288 0.8283 0.2515 -0.3710 0.0799  0.0506  62  LYS B NZ  
1339 N  N   . LEU B 63  ? 0.2218 0.4066 0.2872 0.1244  0.0666  -0.0714 63  LEU B N   
1340 C  CA  . LEU B 63  ? 0.2204 0.3987 0.2896 0.1048  0.0312  -0.0578 63  LEU B CA  
1341 C  C   . LEU B 63  ? 0.2114 0.4076 0.2906 0.1173  0.0442  -0.0821 63  LEU B C   
1342 O  O   . LEU B 63  ? 0.2180 0.5225 0.3001 0.0664  0.0618  -0.0873 63  LEU B O   
1343 C  CB  . LEU B 63  ? 0.2328 0.3934 0.2606 0.0780  0.0525  -0.0368 63  LEU B CB  
1344 C  CG  . LEU B 63  ? 0.2483 0.3677 0.2142 0.0762  0.0935  -0.0014 63  LEU B CG  
1345 C  CD1 . LEU B 63  ? 0.2159 0.3918 0.3415 0.1108  0.1030  0.0320  63  LEU B CD1 
1346 C  CD2 . LEU B 63  ? 0.3420 0.3916 0.2309 0.0029  0.0177  0.0015  63  LEU B CD2 
1347 N  N   . PRO B 64  ? 0.2479 0.4254 0.2857 0.1147  0.0635  -0.0330 64  PRO B N   
1348 C  CA  . PRO B 64  ? 0.2423 0.4197 0.2829 0.1274  0.0536  -0.0376 64  PRO B CA  
1349 C  C   . PRO B 64  ? 0.2471 0.4217 0.3893 0.0926  0.0930  -0.0265 64  PRO B C   
1350 O  O   . PRO B 64  ? 0.2670 0.4087 0.3756 0.1149  0.0836  0.0689  64  PRO B O   
1351 C  CB  . PRO B 64  ? 0.2708 0.4477 0.2803 0.0951  0.0539  -0.0522 64  PRO B CB  
1352 C  CG  . PRO B 64  ? 0.2682 0.4517 0.2811 0.0956  0.0758  -0.0580 64  PRO B CG  
1353 C  CD  . PRO B 64  ? 0.2492 0.4038 0.2796 0.1299  0.0754  -0.0182 64  PRO B CD  
1354 N  N   . GLY B 65  ? 0.2572 0.4947 0.5475 0.0556  0.0980  -0.0431 65  GLY B N   
1355 C  CA  . GLY B 65  ? 0.2791 0.4990 0.5822 0.0279  0.1294  -0.0649 65  GLY B CA  
1356 C  C   . GLY B 65  ? 0.3786 0.5080 0.5633 -0.0024 0.1437  -0.0409 65  GLY B C   
1357 O  O   . GLY B 65  ? 0.4311 0.5195 0.5293 0.0583  0.1481  -0.0221 65  GLY B O   
1358 N  N   . LYS B 66  ? 0.3348 0.5098 0.5778 0.0039  0.1695  -0.0183 66  LYS B N   
1359 C  CA  . LYS B 66  ? 0.3083 0.4897 0.5835 0.0265  0.1982  -0.0423 66  LYS B CA  
1360 C  C   . LYS B 66  ? 0.3244 0.4901 0.6331 -0.0024 0.2362  -0.0350 66  LYS B C   
1361 O  O   . LYS B 66  ? 0.2899 0.4810 0.7363 0.0123  0.1877  0.0037  66  LYS B O   
1362 C  CB  . LYS B 66  ? 0.4095 0.5282 0.5760 -0.0482 0.2436  -0.0609 66  LYS B CB  
1363 C  CG  . LYS B 66  ? 0.5045 0.5933 0.5770 -0.1334 0.2038  -0.0399 66  LYS B CG  
1364 C  CD  . LYS B 66  ? 0.5309 0.6166 0.5750 -0.1563 0.2027  -0.0517 66  LYS B CD  
1365 C  CE  . LYS B 66  ? 0.5199 0.6094 0.5751 -0.1377 0.2042  -0.0622 66  LYS B CE  
1366 N  NZ  . LYS B 66  ? 0.5198 0.5642 0.5770 -0.0797 0.1986  -0.0879 66  LYS B NZ  
1367 N  N   . SER B 67  ? 0.3185 0.5083 0.6664 -0.0154 0.3083  -0.0527 67  SER B N   
1368 C  CA  . SER B 67  ? 0.3478 0.5081 0.6601 -0.0334 0.3201  -0.0629 67  SER B CA  
1369 C  C   . SER B 67  ? 0.3731 0.4931 0.5850 -0.0671 0.3064  -0.0693 67  SER B C   
1370 O  O   . SER B 67  ? 0.5037 0.5360 0.5810 -0.1825 0.2141  -0.0371 67  SER B O   
1371 C  CB  . SER B 67  ? 0.3481 0.5125 0.6589 -0.0332 0.3200  -0.0629 67  SER B CB  
1372 O  OG  . SER B 67  ? 0.3478 0.5133 0.6595 -0.0360 0.3202  -0.0631 67  SER B OG  
1373 N  N   . GLY B 68  ? 0.3805 0.4740 0.6174 -0.1072 0.2019  -0.0080 68  GLY B N   
1374 C  CA  . GLY B 68  ? 0.4270 0.4454 0.5618 -0.1299 0.1699  0.0621  68  GLY B CA  
1375 C  C   . GLY B 68  ? 0.3736 0.4138 0.5139 -0.0704 0.2037  0.0822  68  GLY B C   
1376 O  O   . GLY B 68  ? 0.3615 0.3951 0.6481 0.0021  0.1674  0.1426  68  GLY B O   
1377 N  N   . ARG B 69  ? 0.3114 0.4340 0.4391 -0.0493 0.2169  0.0497  69  ARG B N   
1378 C  CA  . ARG B 69  ? 0.2505 0.3834 0.4237 0.0234  0.2024  0.0198  69  ARG B CA  
1379 C  C   . ARG B 69  ? 0.2971 0.3637 0.4194 -0.0197 0.1584  0.0032  69  ARG B C   
1380 O  O   . ARG B 69  ? 0.2634 0.4043 0.4247 -0.0263 0.0007  -0.0120 69  ARG B O   
1381 C  CB  . ARG B 69  ? 0.2238 0.3876 0.4377 0.0555  0.2025  0.0179  69  ARG B CB  
1382 C  CG  . ARG B 69  ? 0.2620 0.3844 0.3931 0.0256  0.1955  0.0332  69  ARG B CG  
1383 C  CD  . ARG B 69  ? 0.2857 0.3874 0.3999 0.0420  0.1981  0.0064  69  ARG B CD  
1384 N  NE  . ARG B 69  ? 0.3219 0.3898 0.3998 0.0715  0.1959  -0.0045 69  ARG B NE  
1385 C  CZ  . ARG B 69  ? 0.3086 0.3997 0.3898 0.0843  0.2167  -0.0019 69  ARG B CZ  
1386 N  NH1 . ARG B 69  ? 0.3357 0.3952 0.3907 0.1144  0.1193  0.0793  69  ARG B NH1 
1387 N  NH2 . ARG B 69  ? 0.3522 0.4157 0.3890 0.1391  0.1859  0.0516  69  ARG B NH2 
1388 N  N   . THR B 70  ? 0.3194 0.3683 0.3430 -0.0900 0.2057  -0.0540 70  THR B N   
1389 C  CA  . THR B 70  ? 0.3748 0.3118 0.3359 -0.1192 0.1558  -0.0265 70  THR B CA  
1390 C  C   . THR B 70  ? 0.2614 0.2828 0.3078 -0.0253 0.1212  -0.0430 70  THR B C   
1391 O  O   . THR B 70  ? 0.3226 0.3605 0.3061 -0.0923 0.1730  -0.0371 70  THR B O   
1392 C  CB  . THR B 70  ? 0.4230 0.3041 0.3983 -0.0910 0.0839  0.0451  70  THR B CB  
1393 O  OG1 . THR B 70  ? 0.4400 0.3117 0.3961 0.0008  0.1004  -0.0065 70  THR B OG1 
1394 C  CG2 . THR B 70  ? 0.4822 0.3068 0.5329 -0.1239 0.1967  0.0791  70  THR B CG2 
1395 N  N   . TRP B 71  ? 0.1631 0.2381 0.3117 0.0203  0.0892  -0.0154 71  TRP B N   
1396 C  CA  . TRP B 71  ? 0.1434 0.2667 0.2883 0.0289  0.0777  -0.0062 71  TRP B CA  
1397 C  C   . TRP B 71  ? 0.1599 0.2598 0.2618 0.0060  0.0626  0.0095  71  TRP B C   
1398 O  O   . TRP B 71  ? 0.1740 0.2759 0.2471 -0.0159 0.0423  -0.0266 71  TRP B O   
1399 C  CB  . TRP B 71  ? 0.2094 0.2446 0.2668 0.0121  0.0752  -0.0088 71  TRP B CB  
1400 C  CG  . TRP B 71  ? 0.1822 0.2648 0.2372 0.0456  0.0634  -0.0088 71  TRP B CG  
1401 C  CD1 . TRP B 71  ? 0.2014 0.2638 0.2514 0.0239  0.0341  -0.0418 71  TRP B CD1 
1402 C  CD2 . TRP B 71  ? 0.1750 0.2714 0.2187 0.0509  0.0942  -0.0153 71  TRP B CD2 
1403 N  NE1 . TRP B 71  ? 0.1794 0.2765 0.2505 0.0373  0.0223  -0.0372 71  TRP B NE1 
1404 C  CE2 . TRP B 71  ? 0.1989 0.2574 0.2420 0.0300  0.0766  -0.0126 71  TRP B CE2 
1405 C  CE3 . TRP B 71  ? 0.2032 0.2292 0.2231 0.0465  0.0844  0.0147  71  TRP B CE3 
1406 C  CZ2 . TRP B 71  ? 0.1890 0.2599 0.2452 0.0471  0.0682  -0.0346 71  TRP B CZ2 
1407 C  CZ3 . TRP B 71  ? 0.1767 0.2341 0.2116 0.0807  0.0755  -0.0095 71  TRP B CZ3 
1408 C  CH2 . TRP B 71  ? 0.1855 0.2305 0.2466 0.0606  0.0432  0.0120  71  TRP B CH2 
1409 N  N   . ARG B 72  ? 0.1573 0.2221 0.2146 0.0204  0.1287  -0.0212 72  ARG B N   
1410 C  CA  . ARG B 72  ? 0.1797 0.2170 0.1897 -0.0154 0.0708  -0.0016 72  ARG B CA  
1411 C  C   . ARG B 72  ? 0.1539 0.1968 0.1805 0.0253  0.0717  -0.0249 72  ARG B C   
1412 O  O   . ARG B 72  ? 0.1719 0.1945 0.1647 0.0115  0.0603  -0.0525 72  ARG B O   
1413 C  CB  . ARG B 72  ? 0.1844 0.1915 0.2521 0.0059  0.0706  -0.0389 72  ARG B CB  
1414 C  CG  . ARG B 72  ? 0.2200 0.2055 0.3305 -0.0196 0.0984  -0.0397 72  ARG B CG  
1415 C  CD  . ARG B 72  ? 0.2689 0.1630 0.3786 0.0341  0.1053  -0.0386 72  ARG B CD  
1416 N  NE  . ARG B 72  ? 0.3949 0.1756 0.4692 -0.0193 0.1079  -0.0452 72  ARG B NE  
1417 C  CZ  . ARG B 72  ? 0.4758 0.1915 0.4450 -0.1105 0.1123  0.0014  72  ARG B CZ  
1418 N  NH1 . ARG B 72  ? 0.4405 0.2976 0.3797 -0.0047 0.1701  0.0253  72  ARG B NH1 
1419 N  NH2 . ARG B 72  ? 0.6720 0.3101 0.5713 -0.3041 -0.0723 0.0774  72  ARG B NH2 
1420 N  N   . GLU B 73  ? 0.1752 0.1523 0.1994 -0.0039 0.0594  -0.0384 73  GLU B N   
1421 C  CA  . GLU B 73  ? 0.1618 0.1360 0.1957 0.0132  0.0175  -0.0131 73  GLU B CA  
1422 C  C   . GLU B 73  ? 0.1697 0.1253 0.1642 0.0095  0.0265  0.0311  73  GLU B C   
1423 O  O   . GLU B 73  ? 0.1621 0.1285 0.1589 0.0102  0.0539  0.0096  73  GLU B O   
1424 C  CB  . GLU B 73  ? 0.1312 0.1561 0.1990 0.0236  0.0011  0.0019  73  GLU B CB  
1425 C  CG  . GLU B 73  ? 0.1525 0.1647 0.1957 0.0130  0.0338  -0.0411 73  GLU B CG  
1426 C  CD  . GLU B 73  ? 0.2654 0.2278 0.1884 0.0023  0.0110  -0.0535 73  GLU B CD  
1427 O  OE1 . GLU B 73  ? 0.2423 0.2943 0.1375 -0.0119 0.0023  0.0176  73  GLU B OE1 
1428 O  OE2 . GLU B 73  ? 0.3925 0.3660 0.1839 -0.1462 -0.0565 -0.0244 73  GLU B OE2 
1429 N  N   . ALA B 74  ? 0.1576 0.1130 0.1112 0.0256  0.0115  -0.0010 74  ALA B N   
1430 C  CA  . ALA B 74  ? 0.1428 0.1363 0.1168 0.0317  0.0164  0.0295  74  ALA B CA  
1431 C  C   . ALA B 74  ? 0.1365 0.1365 0.1188 0.0344  0.0298  -0.0294 74  ALA B C   
1432 O  O   . ALA B 74  ? 0.1568 0.1399 0.1520 0.0361  0.0604  -0.0177 74  ALA B O   
1433 C  CB  . ALA B 74  ? 0.1765 0.1708 0.1165 -0.0381 -0.0139 0.0166  74  ALA B CB  
1434 N  N   . ASP B 75  ? 0.1387 0.1453 0.1153 0.0310  0.0154  0.0012  75  ASP B N   
1435 C  CA  . ASP B 75  ? 0.1372 0.1295 0.1032 0.0495  0.0268  -0.0135 75  ASP B CA  
1436 C  C   . ASP B 75  ? 0.1899 0.1444 0.1004 0.0076  -0.0046 -0.0226 75  ASP B C   
1437 O  O   . ASP B 75  ? 0.1753 0.1418 0.1157 0.0097  -0.0119 -0.0223 75  ASP B O   
1438 C  CB  . ASP B 75  ? 0.1210 0.1342 0.1035 0.0307  0.0223  -0.0245 75  ASP B CB  
1439 C  CG  . ASP B 75  ? 0.1480 0.1379 0.1007 -0.0148 0.0440  -0.0255 75  ASP B CG  
1440 O  OD1 . ASP B 75  ? 0.1317 0.1683 0.1035 -0.0109 0.0267  -0.0115 75  ASP B OD1 
1441 O  OD2 . ASP B 75  ? 0.1255 0.1637 0.1046 0.0063  0.0042  -0.0111 75  ASP B OD2 
1442 N  N   . ILE B 76  ? 0.1468 0.1429 0.1158 0.0267  -0.0098 -0.0125 76  ILE B N   
1443 C  CA  . ILE B 76  ? 0.1423 0.1483 0.1412 0.0170  0.0240  -0.0433 76  ILE B CA  
1444 C  C   . ILE B 76  ? 0.1512 0.1419 0.1387 0.0198  -0.0412 -0.0068 76  ILE B C   
1445 O  O   . ILE B 76  ? 0.1904 0.1503 0.1406 -0.0041 0.0192  -0.0104 76  ILE B O   
1446 C  CB  . ILE B 76  ? 0.1667 0.1457 0.1233 0.0267  0.0004  -0.0253 76  ILE B CB  
1447 C  CG1 . ILE B 76  ? 0.1629 0.1849 0.1190 0.0104  0.0384  -0.0264 76  ILE B CG1 
1448 C  CG2 . ILE B 76  ? 0.2073 0.1397 0.1441 0.0137  -0.0362 -0.0637 76  ILE B CG2 
1449 C  CD1 . ILE B 76  ? 0.2563 0.1653 0.1040 0.0305  -0.0164 -0.0355 76  ILE B CD1 
1450 N  N   . ASN B 77  ? 0.1545 0.1732 0.1632 -0.0098 0.0054  -0.0561 77  ASN B N   
1451 C  CA  . ASN B 77  ? 0.1631 0.1809 0.1841 -0.0112 0.0936  -0.0783 77  ASN B CA  
1452 C  C   . ASN B 77  ? 0.2001 0.1845 0.1521 -0.0451 0.0873  -0.0261 77  ASN B C   
1453 O  O   . ASN B 77  ? 0.2227 0.2089 0.1791 -0.0840 0.0948  -0.0495 77  ASN B O   
1454 C  CB  . ASN B 77  ? 0.3039 0.1570 0.2467 -0.0390 0.0485  -0.0718 77  ASN B CB  
1455 C  CG  . ASN B 77  ? 0.3203 0.1579 0.2428 -0.0189 0.0611  -0.0220 77  ASN B CG  
1456 O  OD1 . ASN B 77  ? 0.3055 0.2207 0.2446 -0.0427 0.0471  -0.1087 77  ASN B OD1 
1457 N  ND2 . ASN B 77  ? 0.3256 0.1664 0.2733 0.0212  0.0469  -0.0361 77  ASN B ND2 
1458 N  N   . TYR B 78  ? 0.1528 0.1847 0.1578 -0.0167 0.0260  -0.0317 78  TYR B N   
1459 C  CA  . TYR B 78  ? 0.1450 0.1769 0.1812 -0.0051 0.0538  -0.0725 78  TYR B CA  
1460 C  C   . TYR B 78  ? 0.1534 0.1814 0.1332 -0.0167 0.0074  -0.0566 78  TYR B C   
1461 O  O   . TYR B 78  ? 0.1758 0.2326 0.1187 -0.0073 0.0354  -0.0070 78  TYR B O   
1462 C  CB  . TYR B 78  ? 0.1565 0.1786 0.1561 -0.0203 0.0469  -0.0394 78  TYR B CB  
1463 C  CG  . TYR B 78  ? 0.1312 0.1807 0.1605 -0.0148 0.0295  -0.0534 78  TYR B CG  
1464 C  CD1 . TYR B 78  ? 0.1159 0.1696 0.1644 -0.0163 0.0291  -0.0372 78  TYR B CD1 
1465 C  CD2 . TYR B 78  ? 0.1410 0.1756 0.1400 -0.0361 -0.0011 -0.0123 78  TYR B CD2 
1466 C  CE1 . TYR B 78  ? 0.1459 0.1624 0.1574 -0.0437 0.0626  -0.0617 78  TYR B CE1 
1467 C  CE2 . TYR B 78  ? 0.1601 0.1713 0.1415 -0.0103 0.0040  -0.0045 78  TYR B CE2 
1468 C  CZ  . TYR B 78  ? 0.1371 0.1639 0.1424 -0.0297 0.0538  -0.0570 78  TYR B CZ  
1469 O  OH  . TYR B 78  ? 0.2167 0.1444 0.1423 -0.0094 0.0661  -0.0222 78  TYR B OH  
1470 N  N   . THR B 79  ? 0.1503 0.1679 0.1283 -0.0074 0.0317  -0.0485 79  THR B N   
1471 C  CA  . THR B 79  ? 0.1079 0.2483 0.1708 0.0063  0.0410  -0.0256 79  THR B CA  
1472 C  C   . THR B 79  ? 0.0604 0.2588 0.1727 0.0374  0.0346  -0.0200 79  THR B C   
1473 O  O   . THR B 79  ? 0.2105 0.2392 0.1683 0.0510  -0.0133 -0.0825 79  THR B O   
1474 C  CB  . THR B 79  ? 0.1382 0.2664 0.2289 -0.0282 0.0040  -0.0569 79  THR B CB  
1475 O  OG1 . THR B 79  ? 0.3904 0.2458 0.2406 -0.0919 0.0294  -0.0021 79  THR B OG1 
1476 C  CG2 . THR B 79  ? 0.2019 0.2557 0.2311 -0.0424 0.0624  -0.1210 79  THR B CG2 
1477 N  N   . SER B 80  ? 0.1314 0.2339 0.1685 -0.0186 -0.0198 -0.0148 80  SER B N   
1478 C  CA  . SER B 80  ? 0.1457 0.2351 0.1720 -0.0349 0.0198  -0.0818 80  SER B CA  
1479 C  C   . SER B 80  ? 0.1943 0.1924 0.1663 -0.0857 0.0612  -0.0701 80  SER B C   
1480 O  O   . SER B 80  ? 0.2635 0.1878 0.1507 -0.0503 0.0264  -0.0468 80  SER B O   
1481 C  CB  . SER B 80  ? 0.1301 0.2996 0.1572 -0.0404 0.0032  -0.0605 80  SER B CB  
1482 O  OG  . SER B 80  ? 0.3079 0.3171 0.2945 -0.1976 0.1474  -0.1404 80  SER B OG  
1483 N  N   . GLY B 81  ? 0.1490 0.1956 0.1711 -0.0413 0.0388  -0.0895 81  GLY B N   
1484 C  CA  . GLY B 81  ? 0.2174 0.2098 0.1572 -0.0858 0.0314  -0.0650 81  GLY B CA  
1485 C  C   . GLY B 81  ? 0.1995 0.2031 0.0815 -0.0636 0.0658  -0.0264 81  GLY B C   
1486 O  O   . GLY B 81  ? 0.1554 0.1852 0.1030 -0.0256 0.0479  -0.0208 81  GLY B O   
1487 N  N   . PHE B 82  ? 0.1994 0.1691 0.1218 -0.0124 0.0603  0.0211  82  PHE B N   
1488 C  CA  . PHE B 82  ? 0.1829 0.1737 0.1224 -0.0007 0.0807  0.0188  82  PHE B CA  
1489 C  C   . PHE B 82  ? 0.1925 0.1972 0.1192 -0.0298 0.0813  -0.0240 82  PHE B C   
1490 O  O   . PHE B 82  ? 0.2420 0.1979 0.1399 -0.0681 0.0586  -0.0192 82  PHE B O   
1491 C  CB  . PHE B 82  ? 0.1908 0.1778 0.1172 0.0410  0.0601  0.0323  82  PHE B CB  
1492 C  CG  . PHE B 82  ? 0.1158 0.1843 0.1215 0.0153  0.0088  0.0286  82  PHE B CG  
1493 C  CD1 . PHE B 82  ? 0.1650 0.1633 0.1315 0.0034  -0.0029 0.0130  82  PHE B CD1 
1494 C  CD2 . PHE B 82  ? 0.1285 0.2496 0.1387 -0.0304 0.0127  0.0379  82  PHE B CD2 
1495 C  CE1 . PHE B 82  ? 0.1646 0.1782 0.1251 -0.0061 -0.0029 0.0488  82  PHE B CE1 
1496 C  CE2 . PHE B 82  ? 0.2704 0.3175 0.0979 -0.1545 -0.0134 0.0308  82  PHE B CE2 
1497 C  CZ  . PHE B 82  ? 0.1710 0.2430 0.1317 -0.0280 -0.0484 0.0648  82  PHE B CZ  
1498 N  N   . ARG B 83  ? 0.1750 0.1894 0.1226 -0.0243 0.0845  -0.0277 83  ARG B N   
1499 C  CA  . ARG B 83  ? 0.1811 0.1763 0.1275 -0.0212 0.0589  -0.0177 83  ARG B CA  
1500 C  C   . ARG B 83  ? 0.2046 0.1732 0.1262 -0.0399 0.0663  0.0054  83  ARG B C   
1501 O  O   . ARG B 83  ? 0.3058 0.1655 0.1272 -0.0258 0.0856  -0.0011 83  ARG B O   
1502 C  CB  . ARG B 83  ? 0.1475 0.1534 0.1401 0.0084  0.0377  -0.0371 83  ARG B CB  
1503 C  CG  . ARG B 83  ? 0.1624 0.1525 0.1171 0.0069  0.0159  -0.0332 83  ARG B CG  
1504 C  CD  . ARG B 83  ? 0.1937 0.1644 0.0921 -0.0168 0.0419  -0.0278 83  ARG B CD  
1505 N  NE  . ARG B 83  ? 0.1760 0.1367 0.1212 -0.0102 -0.0087 -0.0218 83  ARG B NE  
1506 C  CZ  . ARG B 83  ? 0.2008 0.1687 0.1251 -0.0445 -0.0644 -0.0063 83  ARG B CZ  
1507 N  NH1 . ARG B 83  ? 0.2062 0.1825 0.1269 -0.0461 -0.0154 -0.0248 83  ARG B NH1 
1508 N  NH2 . ARG B 83  ? 0.1706 0.2764 0.0987 -0.0534 0.0323  -0.0157 83  ARG B NH2 
1509 N  N   . ASN B 84  ? 0.2011 0.1775 0.1289 0.0055  0.0282  -0.0138 84  ASN B N   
1510 C  CA  . ASN B 84  ? 0.2345 0.1750 0.1406 -0.0080 0.0928  0.0183  84  ASN B CA  
1511 C  C   . ASN B 84  ? 0.2150 0.1794 0.1363 0.0227  0.0552  -0.0109 84  ASN B C   
1512 O  O   . ASN B 84  ? 0.2317 0.1982 0.1590 -0.0094 0.0309  -0.0146 84  ASN B O   
1513 C  CB  . ASN B 84  ? 0.2275 0.1692 0.1437 0.0043  0.0857  -0.0001 84  ASN B CB  
1514 C  CG  . ASN B 84  ? 0.2281 0.1581 0.1435 -0.0192 0.0573  -0.0170 84  ASN B CG  
1515 O  OD1 . ASN B 84  ? 0.2208 0.1716 0.1512 -0.0235 0.0397  -0.0272 84  ASN B OD1 
1516 N  ND2 . ASN B 84  ? 0.2512 0.2331 0.1429 -0.0613 0.0358  -0.0250 84  ASN B ND2 
1517 N  N   . SER B 85  ? 0.2460 0.1829 0.1595 0.0562  0.0352  -0.0021 85  SER B N   
1518 C  CA  . SER B 85  ? 0.2347 0.1835 0.1515 0.0722  0.0527  -0.0125 85  SER B CA  
1519 C  C   . SER B 85  ? 0.2140 0.2199 0.1577 0.0731  0.1139  -0.0247 85  SER B C   
1520 O  O   . SER B 85  ? 0.2401 0.1978 0.1336 0.0501  0.0283  0.0002  85  SER B O   
1521 C  CB  . SER B 85  ? 0.2975 0.1777 0.2087 0.1079  -0.0033 0.0145  85  SER B CB  
1522 O  OG  . SER B 85  ? 0.5400 0.1964 0.2769 -0.0100 0.0808  -0.0320 85  SER B OG  
1523 N  N   . ASP B 86  ? 0.2520 0.1711 0.1440 0.0234  0.0066  0.0270  86  ASP B N   
1524 C  CA  . ASP B 86  ? 0.2019 0.1354 0.1544 0.0306  -0.0223 0.0241  86  ASP B CA  
1525 C  C   . ASP B 86  ? 0.1472 0.1390 0.1305 0.0563  0.0252  -0.0014 86  ASP B C   
1526 O  O   . ASP B 86  ? 0.1464 0.1341 0.1782 0.0238  0.0177  -0.0115 86  ASP B O   
1527 C  CB  . ASP B 86  ? 0.2515 0.1769 0.1620 -0.0272 0.0465  -0.0250 86  ASP B CB  
1528 C  CG  . ASP B 86  ? 0.2842 0.1654 0.2797 -0.0274 0.0851  -0.0209 86  ASP B CG  
1529 O  OD1 . ASP B 86  ? 0.3234 0.1587 0.2836 -0.0061 0.0121  -0.0111 86  ASP B OD1 
1530 O  OD2 . ASP B 86  ? 0.3118 0.1901 0.3638 -0.0691 0.0570  -0.0443 86  ASP B OD2 
1531 N  N   . ARG B 87  ? 0.1488 0.1456 0.1065 0.0599  0.0204  -0.0146 87  ARG B N   
1532 C  CA  . ARG B 87  ? 0.1928 0.1456 0.1055 0.0372  -0.0109 -0.0062 87  ARG B CA  
1533 C  C   . ARG B 87  ? 0.1296 0.1695 0.1104 0.0509  0.0118  0.0016  87  ARG B C   
1534 O  O   . ARG B 87  ? 0.1724 0.1712 0.1210 0.0921  0.0432  0.0287  87  ARG B O   
1535 C  CB  . ARG B 87  ? 0.1734 0.1450 0.1054 0.0383  0.0084  -0.0285 87  ARG B CB  
1536 C  CG  . ARG B 87  ? 0.1683 0.1696 0.1019 0.0437  0.0095  -0.0474 87  ARG B CG  
1537 C  CD  . ARG B 87  ? 0.1751 0.1613 0.1035 0.0298  0.0275  -0.0520 87  ARG B CD  
1538 N  NE  . ARG B 87  ? 0.1922 0.1691 0.1036 0.0378  0.0378  -0.0349 87  ARG B NE  
1539 C  CZ  . ARG B 87  ? 0.1941 0.1578 0.0945 0.0465  0.0535  -0.0639 87  ARG B CZ  
1540 N  NH1 . ARG B 87  ? 0.2362 0.1485 0.1228 0.0123  0.0470  -0.0160 87  ARG B NH1 
1541 N  NH2 . ARG B 87  ? 0.2789 0.2014 0.0852 0.0535  0.0274  -0.0494 87  ARG B NH2 
1542 N  N   . ILE B 88  ? 0.1692 0.1584 0.1154 0.0371  0.0228  -0.0092 88  ILE B N   
1543 C  CA  . ILE B 88  ? 0.1572 0.2045 0.1104 0.0240  -0.0076 -0.0159 88  ILE B CA  
1544 C  C   . ILE B 88  ? 0.1288 0.1695 0.1166 0.0735  0.0131  -0.0342 88  ILE B C   
1545 O  O   . ILE B 88  ? 0.1426 0.1677 0.1351 0.0264  0.0443  -0.0321 88  ILE B O   
1546 C  CB  . ILE B 88  ? 0.1674 0.1737 0.1164 0.0510  0.0096  -0.0213 88  ILE B CB  
1547 C  CG1 . ILE B 88  ? 0.2973 0.2271 0.1073 0.0822  -0.0301 -0.0331 88  ILE B CG1 
1548 C  CG2 . ILE B 88  ? 0.1728 0.1800 0.2999 0.0709  0.0809  -0.0112 88  ILE B CG2 
1549 C  CD1 . ILE B 88  ? 0.3075 0.3459 0.0994 0.0478  -0.0889 -0.0596 88  ILE B CD1 
1550 N  N   . LEU B 89  ? 0.1283 0.1696 0.1576 0.0618  0.0307  -0.0349 89  LEU B N   
1551 C  CA  . LEU B 89  ? 0.1485 0.1750 0.1714 0.0480  0.0762  -0.0388 89  LEU B CA  
1552 C  C   . LEU B 89  ? 0.1618 0.1654 0.1717 0.0425  0.0523  -0.0255 89  LEU B C   
1553 O  O   . LEU B 89  ? 0.2670 0.1594 0.1646 0.0569  0.0694  -0.0168 89  LEU B O   
1554 C  CB  . LEU B 89  ? 0.1314 0.1928 0.1747 0.0496  0.0185  -0.0430 89  LEU B CB  
1555 C  CG  . LEU B 89  ? 0.2070 0.2379 0.1664 0.0273  -0.0223 0.0026  89  LEU B CG  
1556 C  CD1 . LEU B 89  ? 0.3994 0.2299 0.1673 0.0443  -0.0145 -0.1318 89  LEU B CD1 
1557 C  CD2 . LEU B 89  ? 0.2446 0.4665 0.1547 -0.0564 -0.0683 0.1017  89  LEU B CD2 
1558 N  N   . TYR B 90  ? 0.2423 0.1653 0.1465 0.0390  0.0882  -0.0132 90  TYR B N   
1559 C  CA  . TYR B 90  ? 0.2021 0.2145 0.1418 0.0629  0.0726  0.0158  90  TYR B CA  
1560 C  C   . TYR B 90  ? 0.2329 0.2681 0.1415 0.0220  0.0882  0.0062  90  TYR B C   
1561 O  O   . TYR B 90  ? 0.2130 0.2626 0.1633 0.0016  0.0996  -0.0166 90  TYR B O   
1562 C  CB  . TYR B 90  ? 0.1877 0.2293 0.1339 0.0963  0.0580  -0.0091 90  TYR B CB  
1563 C  CG  . TYR B 90  ? 0.2040 0.2198 0.1315 0.1006  0.0632  0.0051  90  TYR B CG  
1564 C  CD1 . TYR B 90  ? 0.2035 0.2051 0.1394 0.0684  0.0525  0.0083  90  TYR B CD1 
1565 C  CD2 . TYR B 90  ? 0.2731 0.2162 0.1314 0.0323  0.0673  0.0259  90  TYR B CD2 
1566 C  CE1 . TYR B 90  ? 0.2233 0.1977 0.1626 0.0740  0.0384  0.0386  90  TYR B CE1 
1567 C  CE2 . TYR B 90  ? 0.2754 0.2121 0.1560 0.0554  0.0616  -0.0201 90  TYR B CE2 
1568 C  CZ  . TYR B 90  ? 0.2457 0.2014 0.1678 0.0596  0.1053  -0.0616 90  TYR B CZ  
1569 O  OH  . TYR B 90  ? 0.2806 0.1905 0.1901 0.0394  0.0928  -0.0420 90  TYR B OH  
1570 N  N   . SER B 91  ? 0.1791 0.3008 0.1660 0.0647  0.0897  0.0155  91  SER B N   
1571 C  CA  . SER B 91  ? 0.1845 0.3222 0.2234 0.0438  0.1228  0.0234  91  SER B CA  
1572 C  C   . SER B 91  ? 0.2107 0.3008 0.2409 0.0731  0.1031  0.0668  91  SER B C   
1573 O  O   . SER B 91  ? 0.2408 0.2906 0.2244 0.0751  0.0756  0.0785  91  SER B O   
1574 C  CB  . SER B 91  ? 0.2139 0.2947 0.1877 0.0203  0.1129  0.0216  91  SER B CB  
1575 O  OG  . SER B 91  ? 0.2408 0.3495 0.1741 0.0572  0.0698  -0.0066 91  SER B OG  
1576 N  N   . SER B 92  ? 0.2433 0.2850 0.2953 0.0679  0.1512  0.0860  92  SER B N   
1577 C  CA  . SER B 92  ? 0.3834 0.2944 0.2993 0.0292  0.1256  0.0856  92  SER B CA  
1578 C  C   . SER B 92  ? 0.3578 0.3375 0.2927 0.0740  0.1071  0.0821  92  SER B C   
1579 O  O   . SER B 92  ? 0.3192 0.3428 0.3016 0.0675  0.0769  0.0899  92  SER B O   
1580 C  CB  . SER B 92  ? 0.4246 0.2894 0.3486 0.0077  0.1306  0.0948  92  SER B CB  
1581 O  OG  . SER B 92  ? 0.3633 0.3607 0.4287 0.0166  0.1484  0.0763  92  SER B OG  
1582 N  N   . ASP B 93  ? 0.3569 0.3461 0.2711 0.0999  0.1794  0.0398  93  ASP B N   
1583 C  CA  . ASP B 93  ? 0.3320 0.3670 0.2645 0.1406  0.1663  0.0561  93  ASP B CA  
1584 C  C   . ASP B 93  ? 0.3738 0.3753 0.2152 0.1081  0.1306  0.0550  93  ASP B C   
1585 O  O   . ASP B 93  ? 0.3889 0.3846 0.2096 0.1262  0.1636  0.0351  93  ASP B O   
1586 C  CB  . ASP B 93  ? 0.3050 0.4083 0.2811 0.1632  0.1541  0.0967  93  ASP B CB  
1587 C  CG  . ASP B 93  ? 0.3018 0.4019 0.2887 0.1711  0.2191  0.0737  93  ASP B CG  
1588 O  OD1 . ASP B 93  ? 0.3469 0.4165 0.2803 0.1711  0.1430  0.0601  93  ASP B OD1 
1589 O  OD2 . ASP B 93  ? 0.2914 0.4118 0.3761 0.1216  0.1652  0.0426  93  ASP B OD2 
1590 N  N   . TRP B 94  ? 0.3574 0.3549 0.2200 0.1287  0.1124  0.0819  94  TRP B N   
1591 C  CA  . TRP B 94  ? 0.3816 0.3908 0.1503 0.1006  0.0815  0.1011  94  TRP B CA  
1592 C  C   . TRP B 94  ? 0.3467 0.3881 0.1158 0.0643  0.0906  0.0540  94  TRP B C   
1593 O  O   . TRP B 94  ? 0.2761 0.3970 0.1537 0.0935  -0.0052 0.0385  94  TRP B O   
1594 C  CB  . TRP B 94  ? 0.3882 0.3800 0.1555 0.1209  0.0832  0.1106  94  TRP B CB  
1595 C  CG  . TRP B 94  ? 0.4019 0.3753 0.1955 0.1063  0.0713  0.1336  94  TRP B CG  
1596 C  CD1 . TRP B 94  ? 0.3945 0.3759 0.2226 0.0885  0.0551  0.1235  94  TRP B CD1 
1597 C  CD2 . TRP B 94  ? 0.3443 0.3850 0.2410 0.1246  0.0836  0.1270  94  TRP B CD2 
1598 N  NE1 . TRP B 94  ? 0.3949 0.3718 0.2683 0.0786  0.0764  0.0822  94  TRP B NE1 
1599 C  CE2 . TRP B 94  ? 0.3552 0.3802 0.2799 0.1137  0.0725  0.0857  94  TRP B CE2 
1600 C  CE3 . TRP B 94  ? 0.3280 0.3998 0.2379 0.1447  0.0761  0.1273  94  TRP B CE3 
1601 C  CZ2 . TRP B 94  ? 0.3506 0.3838 0.2895 0.1133  0.0426  0.0912  94  TRP B CZ2 
1602 C  CZ3 . TRP B 94  ? 0.3293 0.3924 0.2527 0.1354  0.0887  0.1026  94  TRP B CZ3 
1603 C  CH2 . TRP B 94  ? 0.3621 0.3926 0.2741 0.1190  0.0109  0.1094  94  TRP B CH2 
1604 N  N   . LEU B 95  ? 0.3771 0.3849 0.0969 0.0285  0.1384  0.0334  95  LEU B N   
1605 C  CA  . LEU B 95  ? 0.2449 0.3687 0.1657 0.0273  0.1028  0.0030  95  LEU B CA  
1606 C  C   . LEU B 95  ? 0.2342 0.2883 0.1680 0.0506  0.0565  0.0638  95  LEU B C   
1607 O  O   . LEU B 95  ? 0.2788 0.2701 0.2045 0.0131  0.1187  -0.0239 95  LEU B O   
1608 C  CB  . LEU B 95  ? 0.1921 0.4054 0.2752 0.0596  0.0688  0.0536  95  LEU B CB  
1609 C  CG  . LEU B 95  ? 0.2273 0.3989 0.2771 0.0391  0.0595  0.0235  95  LEU B CG  
1610 C  CD1 . LEU B 95  ? 0.1579 0.4606 0.3084 0.0903  -0.0375 0.0380  95  LEU B CD1 
1611 C  CD2 . LEU B 95  ? 0.3759 0.4225 0.2309 0.0741  0.0837  -0.0026 95  LEU B CD2 
1612 N  N   . ILE B 96  ? 0.2039 0.2649 0.1287 0.0854  0.0787  -0.0081 96  ILE B N   
1613 C  CA  . ILE B 96  ? 0.2123 0.1874 0.1280 0.0967  0.0285  -0.0276 96  ILE B CA  
1614 C  C   . ILE B 96  ? 0.2159 0.1919 0.1309 0.0822  0.0061  -0.0481 96  ILE B C   
1615 O  O   . ILE B 96  ? 0.2108 0.1886 0.1170 0.0616  0.0033  -0.0540 96  ILE B O   
1616 C  CB  A ILE B 96  ? 0.2207 0.1857 0.1423 0.0887  0.0021  -0.0132 96  ILE B CB  
1617 C  CB  B ILE B 96  ? 0.2225 0.1987 0.1286 0.0811  -0.0170 0.0044  96  ILE B CB  
1618 C  CG1 A ILE B 96  ? 0.1780 0.1813 0.1588 0.1140  -0.0264 -0.0005 96  ILE B CG1 
1619 C  CG1 B ILE B 96  ? 0.2302 0.1923 0.1324 0.0831  -0.0126 -0.0066 96  ILE B CG1 
1620 C  CG2 A ILE B 96  ? 0.2630 0.2190 0.1672 -0.0098 -0.1141 0.0084  96  ILE B CG2 
1621 C  CG2 B ILE B 96  ? 0.2248 0.1774 0.1405 0.0775  0.0116  -0.0817 96  ILE B CG2 
1622 C  CD1 A ILE B 96  ? 0.1780 0.1769 0.1528 0.0224  -0.0543 -0.0116 96  ILE B CD1 
1623 C  CD1 B ILE B 96  ? 0.2189 0.2045 0.1644 0.1049  -0.0664 0.0201  96  ILE B CD1 
1624 N  N   . TYR B 97  ? 0.1436 0.1964 0.1313 0.0771  0.0219  -0.0510 97  TYR B N   
1625 C  CA  . TYR B 97  ? 0.1749 0.1986 0.1212 0.0956  -0.0523 -0.0395 97  TYR B CA  
1626 C  C   . TYR B 97  ? 0.2001 0.1848 0.1131 0.0855  -0.0158 0.0038  97  TYR B C   
1627 O  O   . TYR B 97  ? 0.1907 0.1761 0.1486 0.0382  0.0227  -0.0114 97  TYR B O   
1628 C  CB  . TYR B 97  ? 0.1985 0.2502 0.1030 0.0624  0.0406  -0.0312 97  TYR B CB  
1629 C  CG  . TYR B 97  ? 0.1709 0.2609 0.1541 0.0689  0.0042  -0.0373 97  TYR B CG  
1630 C  CD1 . TYR B 97  ? 0.1829 0.2646 0.1537 0.0666  0.0255  -0.0185 97  TYR B CD1 
1631 C  CD2 . TYR B 97  ? 0.1952 0.2638 0.1549 0.0898  0.0223  -0.0187 97  TYR B CD2 
1632 C  CE1 . TYR B 97  ? 0.1922 0.2644 0.1522 0.0650  0.0251  -0.0006 97  TYR B CE1 
1633 C  CE2 . TYR B 97  ? 0.2133 0.2380 0.1738 0.1025  0.0133  -0.0046 97  TYR B CE2 
1634 C  CZ  . TYR B 97  ? 0.1818 0.2715 0.1700 0.1062  -0.0037 0.0053  97  TYR B CZ  
1635 O  OH  . TYR B 97  ? 0.1584 0.2981 0.2572 0.1094  0.0490  -0.0115 97  TYR B OH  
1636 N  N   . LYS B 98  ? 0.1941 0.1953 0.0922 0.1150  -0.0026 -0.0194 98  LYS B N   
1637 C  CA  . LYS B 98  ? 0.1920 0.2472 0.0850 0.0899  0.0091  -0.0353 98  LYS B CA  
1638 C  C   . LYS B 98  ? 0.2430 0.1978 0.0905 0.1141  -0.0102 -0.0356 98  LYS B C   
1639 O  O   . LYS B 98  ? 0.2199 0.2210 0.0757 0.1047  0.0110  -0.0121 98  LYS B O   
1640 C  CB  . LYS B 98  ? 0.2463 0.2587 0.1444 0.0450  0.0031  -0.0151 98  LYS B CB  
1641 C  CG  . LYS B 98  ? 0.2953 0.2567 0.1642 0.0477  -0.0164 0.0010  98  LYS B CG  
1642 C  CD  . LYS B 98  ? 0.4123 0.2944 0.2221 -0.0623 0.0344  -0.0288 98  LYS B CD  
1643 C  CE  . LYS B 98  ? 0.4908 0.2883 0.2831 -0.0740 0.0425  -0.0141 98  LYS B CE  
1644 N  NZ  . LYS B 98  ? 0.5566 0.3018 0.4225 -0.1384 -0.1019 -0.0403 98  LYS B NZ  
1645 N  N   . THR B 99  ? 0.2408 0.1960 0.0872 0.1289  -0.0203 0.0022  99  THR B N   
1646 C  CA  . THR B 99  ? 0.2267 0.2108 0.0916 0.1101  0.0060  -0.0376 99  THR B CA  
1647 C  C   . THR B 99  ? 0.2422 0.1738 0.1196 0.1035  0.0261  -0.0325 99  THR B C   
1648 O  O   . THR B 99  ? 0.2331 0.1814 0.1298 0.1108  0.0104  0.0096  99  THR B O   
1649 C  CB  . THR B 99  ? 0.2101 0.2206 0.0801 0.1205  -0.0410 -0.0298 99  THR B CB  
1650 O  OG1 . THR B 99  ? 0.2821 0.2224 0.0861 0.1131  -0.0290 -0.0069 99  THR B OG1 
1651 C  CG2 . THR B 99  ? 0.2782 0.2150 0.0934 0.1150  -0.0268 -0.0187 99  THR B CG2 
1652 N  N   . THR B 100 ? 0.2883 0.1607 0.1510 0.0851  -0.0003 0.0178  100 THR B N   
1653 C  CA  . THR B 100 ? 0.3251 0.1770 0.1652 0.0372  -0.0009 0.0637  100 THR B CA  
1654 C  C   . THR B 100 ? 0.3458 0.1666 0.1588 0.0879  0.0465  0.0707  100 THR B C   
1655 O  O   . THR B 100 ? 0.4058 0.2015 0.1725 0.0225  0.0367  0.0127  100 THR B O   
1656 C  CB  . THR B 100 ? 0.3950 0.1599 0.1800 0.0224  0.0032  0.0470  100 THR B CB  
1657 O  OG1 . THR B 100 ? 0.4013 0.1823 0.2946 0.1152  0.0381  0.0469  100 THR B OG1 
1658 C  CG2 . THR B 100 ? 0.4054 0.2210 0.1804 -0.0868 0.0293  -0.0575 100 THR B CG2 
1659 N  N   . ASP B 101 ? 0.3434 0.2639 0.1436 0.0637  0.0502  0.0530  101 ASP B N   
1660 C  CA  . ASP B 101 ? 0.3601 0.2913 0.1413 0.0880  0.0163  0.0197  101 ASP B CA  
1661 C  C   . ASP B 101 ? 0.3109 0.2913 0.1307 0.1150  -0.0080 0.0245  101 ASP B C   
1662 O  O   . ASP B 101 ? 0.3079 0.2907 0.1572 0.1137  -0.0079 0.0105  101 ASP B O   
1663 C  CB  . ASP B 101 ? 0.3872 0.2864 0.1258 0.1133  0.0213  0.0282  101 ASP B CB  
1664 C  CG  . ASP B 101 ? 0.3730 0.2741 0.1211 0.1517  0.0119  0.0723  101 ASP B CG  
1665 O  OD1 . ASP B 101 ? 0.3406 0.2878 0.1070 0.1482  -0.0274 0.0359  101 ASP B OD1 
1666 O  OD2 . ASP B 101 ? 0.3787 0.2771 0.2475 0.1651  0.0248  0.0120  101 ASP B OD2 
1667 N  N   . HIS B 102 ? 0.2811 0.2926 0.1861 0.1298  0.0100  0.0121  102 HIS B N   
1668 C  CA  . HIS B 102 ? 0.3551 0.2975 0.1704 0.0895  -0.0140 0.0184  102 HIS B CA  
1669 C  C   . HIS B 102 ? 0.3788 0.2729 0.1481 0.0677  -0.0574 0.0038  102 HIS B C   
1670 O  O   . HIS B 102 ? 0.3409 0.3007 0.1343 0.1098  -0.0089 -0.0567 102 HIS B O   
1671 C  CB  . HIS B 102 ? 0.3681 0.4227 0.1611 0.0360  0.0268  -0.0185 102 HIS B CB  
1672 C  CG  . HIS B 102 ? 0.3489 0.4765 0.1577 0.0249  0.0111  0.0037  102 HIS B CG  
1673 N  ND1 . HIS B 102 ? 0.3970 0.5069 0.2029 -0.0341 -0.0499 0.0248  102 HIS B ND1 
1674 C  CD2 . HIS B 102 ? 0.2847 0.4987 0.2054 0.0509  0.0050  0.0184  102 HIS B CD2 
1675 C  CE1 . HIS B 102 ? 0.3615 0.5459 0.2443 -0.0344 0.0011  0.0281  102 HIS B CE1 
1676 N  NE2 . HIS B 102 ? 0.2924 0.5422 0.2720 0.0111  0.0103  -0.0116 102 HIS B NE2 
1677 N  N   . TYR B 103 ? 0.3514 0.2536 0.1402 0.1093  -0.0356 -0.0212 103 TYR B N   
1678 C  CA  . TYR B 103 ? 0.3325 0.3184 0.1365 0.1129  -0.0342 -0.0021 103 TYR B CA  
1679 C  C   . TYR B 103 ? 0.3019 0.3366 0.1187 0.1361  -0.0301 -0.0504 103 TYR B C   
1680 O  O   . TYR B 103 ? 0.2664 0.4359 0.1672 0.1443  -0.0586 -0.0410 103 TYR B O   
1681 C  CB  . TYR B 103 ? 0.2623 0.3230 0.1383 0.1028  -0.0182 0.0014  103 TYR B CB  
1682 C  CG  . TYR B 103 ? 0.2535 0.3109 0.1105 0.0403  0.0020  -0.0314 103 TYR B CG  
1683 C  CD1 . TYR B 103 ? 0.2245 0.3138 0.1068 -0.0016 0.0202  -0.0119 103 TYR B CD1 
1684 C  CD2 . TYR B 103 ? 0.3153 0.2789 0.1027 0.0582  -0.0172 -0.0221 103 TYR B CD2 
1685 C  CE1 . TYR B 103 ? 0.2597 0.2836 0.1096 -0.0283 0.0280  -0.0267 103 TYR B CE1 
1686 C  CE2 . TYR B 103 ? 0.3311 0.2666 0.1081 0.0532  0.0007  -0.0295 103 TYR B CE2 
1687 C  CZ  . TYR B 103 ? 0.2868 0.2657 0.1096 0.0079  -0.0522 0.0059  103 TYR B CZ  
1688 O  OH  . TYR B 103 ? 0.2110 0.3130 0.1352 0.0580  -0.0284 0.0204  103 TYR B OH  
1689 N  N   . GLN B 104 ? 0.3771 0.3341 0.1072 0.1455  -0.0847 -0.0387 104 GLN B N   
1690 C  CA  . GLN B 104 ? 0.3907 0.3359 0.1450 0.1846  -0.0646 -0.0276 104 GLN B CA  
1691 C  C   . GLN B 104 ? 0.3501 0.3532 0.1463 0.1752  -0.0903 -0.0126 104 GLN B C   
1692 O  O   . GLN B 104 ? 0.3372 0.4174 0.1626 0.1462  -0.0323 -0.0345 104 GLN B O   
1693 C  CB  . GLN B 104 ? 0.4149 0.3366 0.1401 0.1941  -0.0353 -0.0228 104 GLN B CB  
1694 C  CG  . GLN B 104 ? 0.4777 0.3948 0.1359 0.2044  -0.0229 -0.0451 104 GLN B CG  
1695 C  CD  . GLN B 104 ? 0.6125 0.4751 0.1143 0.0969  -0.0212 -0.0147 104 GLN B CD  
1696 O  OE1 . GLN B 104 ? 0.5988 0.4659 0.1332 0.1588  -0.0712 0.0447  104 GLN B OE1 
1697 N  NE2 . GLN B 104 ? 0.6643 0.4217 0.1677 0.0489  -0.0474 -0.0007 104 GLN B NE2 
1698 N  N   . THR B 105 ? 0.3212 0.3715 0.1286 0.1967  -0.0705 -0.0407 105 THR B N   
1699 C  CA  . THR B 105 ? 0.3111 0.3553 0.1322 0.1901  -0.0386 -0.0351 105 THR B CA  
1700 C  C   . THR B 105 ? 0.2274 0.3997 0.1287 0.2097  -0.0492 -0.0662 105 THR B C   
1701 O  O   . THR B 105 ? 0.2652 0.3723 0.1188 0.1622  -0.0065 -0.0298 105 THR B O   
1702 C  CB  . THR B 105 ? 0.4326 0.3609 0.1630 0.1285  -0.0382 -0.0136 105 THR B CB  
1703 O  OG1 . THR B 105 ? 0.4201 0.3481 0.2392 0.1458  -0.0311 -0.0780 105 THR B OG1 
1704 C  CG2 . THR B 105 ? 0.4466 0.3327 0.1819 0.1504  -0.0169 0.0676  105 THR B CG2 
1705 N  N   . PHE B 106 ? 0.2581 0.3897 0.1270 0.1584  -0.0554 -0.0599 106 PHE B N   
1706 C  CA  . PHE B 106 ? 0.2153 0.3592 0.1310 0.1453  -0.0467 -0.1246 106 PHE B CA  
1707 C  C   . PHE B 106 ? 0.2647 0.3433 0.1329 0.1408  -0.0310 -0.0980 106 PHE B C   
1708 O  O   . PHE B 106 ? 0.2335 0.3636 0.1707 0.1639  -0.0156 -0.0613 106 PHE B O   
1709 C  CB  . PHE B 106 ? 0.2873 0.3602 0.1815 0.0944  -0.0581 -0.1055 106 PHE B CB  
1710 C  CG  . PHE B 106 ? 0.2717 0.3682 0.1785 0.0990  -0.0243 -0.1269 106 PHE B CG  
1711 C  CD1 . PHE B 106 ? 0.2636 0.3745 0.1789 0.1284  -0.0194 -0.1062 106 PHE B CD1 
1712 C  CD2 . PHE B 106 ? 0.2735 0.3833 0.1846 0.0824  -0.0466 -0.1080 106 PHE B CD2 
1713 C  CE1 . PHE B 106 ? 0.2980 0.3660 0.1909 0.0968  0.0355  -0.1009 106 PHE B CE1 
1714 C  CE2 . PHE B 106 ? 0.2968 0.3819 0.1870 0.0635  -0.0250 -0.1418 106 PHE B CE2 
1715 C  CZ  . PHE B 106 ? 0.2968 0.3790 0.1889 0.0830  0.0373  -0.1438 106 PHE B CZ  
1716 N  N   . THR B 107 ? 0.2982 0.2863 0.1243 0.1298  -0.0508 -0.0599 107 THR B N   
1717 C  CA  . THR B 107 ? 0.2624 0.2402 0.1380 0.1800  -0.0413 -0.0457 107 THR B CA  
1718 C  C   . THR B 107 ? 0.2276 0.2398 0.1299 0.1677  -0.0361 -0.0400 107 THR B C   
1719 O  O   . THR B 107 ? 0.2384 0.2283 0.1294 0.1437  -0.0013 -0.0135 107 THR B O   
1720 C  CB  . THR B 107 ? 0.4266 0.2306 0.1822 0.0744  -0.0433 0.0356  107 THR B CB  
1721 O  OG1 . THR B 107 ? 0.4468 0.2616 0.1784 0.0672  -0.0428 -0.0069 107 THR B OG1 
1722 C  CG2 . THR B 107 ? 0.4919 0.2423 0.1768 0.0539  0.0423  -0.0541 107 THR B CG2 
1723 N  N   . LYS B 108 ? 0.1935 0.2482 0.1457 0.1445  -0.0497 -0.0525 108 LYS B N   
1724 C  CA  . LYS B 108 ? 0.1603 0.2411 0.1491 0.0997  -0.0634 -0.0347 108 LYS B CA  
1725 C  C   . LYS B 108 ? 0.1895 0.1612 0.1675 0.0914  -0.0502 -0.0549 108 LYS B C   
1726 O  O   . LYS B 108 ? 0.3420 0.1544 0.1713 0.0851  -0.0396 -0.0488 108 LYS B O   
1727 C  CB  . LYS B 108 ? 0.1436 0.2839 0.1590 0.1209  0.0302  -0.0121 108 LYS B CB  
1728 C  CG  . LYS B 108 ? 0.2429 0.3999 0.0891 0.1308  0.0399  0.0005  108 LYS B CG  
1729 C  CD  . LYS B 108 ? 0.2431 0.4423 0.0698 0.1186  0.0934  0.0298  108 LYS B CD  
1730 C  CE  . LYS B 108 ? 0.3448 0.4378 0.0913 0.0642  0.0227  0.0580  108 LYS B CE  
1731 N  NZ  . LYS B 108 ? 0.4043 0.4195 0.0684 -0.1141 0.0408  -0.0054 108 LYS B NZ  
1732 N  N   . ILE B 109 ? 0.1755 0.1749 0.1177 0.1024  -0.0296 -0.0212 109 ILE B N   
1733 C  CA  . ILE B 109 ? 0.2096 0.1534 0.1100 0.0682  -0.0255 0.0231  109 ILE B CA  
1734 C  C   . ILE B 109 ? 0.1961 0.1597 0.1143 0.0544  -0.0082 -0.0127 109 ILE B C   
1735 O  O   . ILE B 109 ? 0.2035 0.1527 0.1084 0.0396  0.0098  -0.0147 109 ILE B O   
1736 C  CB  . ILE B 109 ? 0.2252 0.1368 0.1027 0.0452  0.0147  0.0224  109 ILE B CB  
1737 C  CG1 . ILE B 109 ? 0.2020 0.1408 0.1764 0.0680  0.0384  -0.0385 109 ILE B CG1 
1738 C  CG2 . ILE B 109 ? 0.2835 0.1518 0.1010 0.0189  0.0390  0.0097  109 ILE B CG2 
1739 C  CD1 . ILE B 109 ? 0.2053 0.1429 0.2235 0.0537  0.0510  -0.0065 109 ILE B CD1 
1740 N  N   . ARG B 110 ? 0.2166 0.1660 0.1493 0.0259  -0.0298 0.0365  110 ARG B N   
1741 C  CA  . ARG B 110 ? 0.2126 0.2166 0.1543 -0.0050 -0.0667 0.0633  110 ARG B CA  
1742 C  C   . ARG B 110 ? 0.2367 0.3042 0.2432 -0.0905 -0.1270 0.1368  110 ARG B C   
1743 O  O   . ARG B 110 ? 0.1672 0.4066 0.2583 -0.0458 0.0211  0.1653  110 ARG B O   
1744 C  CB  . ARG B 110 ? 0.3030 0.1761 0.1098 -0.0608 -0.0661 0.0238  110 ARG B CB  
1745 C  CG  . ARG B 110 ? 0.2831 0.1482 0.1080 -0.0340 -0.0137 -0.0101 110 ARG B CG  
1746 C  CD  . ARG B 110 ? 0.1840 0.1761 0.0729 0.0494  0.0485  -0.0305 110 ARG B CD  
1747 N  NE  . ARG B 110 ? 0.1517 0.2259 0.0758 0.0756  0.0141  -0.0241 110 ARG B NE  
1748 C  CZ  . ARG B 110 ? 0.1620 0.2115 0.1064 0.0578  -0.0155 -0.0433 110 ARG B CZ  
1749 N  NH1 . ARG B 110 ? 0.2035 0.1867 0.1009 0.0155  0.0180  -0.0372 110 ARG B NH1 
1750 N  NH2 . ARG B 110 ? 0.1748 0.1714 0.2125 0.0519  -0.0161 -0.0128 110 ARG B NH2 
1751 O  OXT . ARG B 110 ? 0.2585 0.7218 0.2686 -0.2403 -0.1205 0.2246  110 ARG B OXT 
1752 N  N   . VAL C 3   ? 0.1725 0.4705 0.4946 0.0341  -0.0637 -0.0636 3   VAL C N   
1753 C  CA  . VAL C 3   ? 0.1603 0.4679 0.4968 0.0196  -0.0122 -0.1243 3   VAL C CA  
1754 C  C   . VAL C 3   ? 0.1934 0.4458 0.4765 0.0259  0.0036  -0.1346 3   VAL C C   
1755 O  O   . VAL C 3   ? 0.2432 0.4178 0.6688 -0.0099 -0.0763 -0.2038 3   VAL C O   
1756 C  CB  . VAL C 3   ? 0.1636 0.5340 0.4885 0.0053  0.0934  -0.1532 3   VAL C CB  
1757 C  CG1 . VAL C 3   ? 0.2307 0.4757 0.4823 -0.0419 0.0527  -0.1163 3   VAL C CG1 
1758 C  CG2 . VAL C 3   ? 0.2133 0.4987 0.4751 -0.0616 0.0325  -0.0570 3   VAL C CG2 
1759 N  N   . ILE C 4   ? 0.1813 0.4014 0.2489 0.0520  -0.0946 0.0156  4   ILE C N   
1760 C  CA  . ILE C 4   ? 0.2237 0.3811 0.1513 0.0329  -0.0367 0.0232  4   ILE C CA  
1761 C  C   . ILE C 4   ? 0.2162 0.3649 0.1668 -0.0046 0.0161  -0.0046 4   ILE C C   
1762 O  O   . ILE C 4   ? 0.1973 0.3450 0.1824 0.0299  0.0140  0.0526  4   ILE C O   
1763 C  CB  . ILE C 4   ? 0.2438 0.4916 0.1566 -0.0221 -0.0634 0.0428  4   ILE C CB  
1764 C  CG1 . ILE C 4   ? 0.2409 0.4975 0.1415 -0.0056 -0.0212 0.0185  4   ILE C CG1 
1765 C  CG2 . ILE C 4   ? 0.1816 0.5644 0.1720 0.0121  -0.0030 0.0453  4   ILE C CG2 
1766 C  CD1 . ILE C 4   ? 0.5271 0.5587 0.1374 -0.1833 0.1063  0.0079  4   ILE C CD1 
1767 N  N   . ASN C 5   ? 0.1147 0.3471 0.2028 -0.0438 -0.0250 0.0212  5   ASN C N   
1768 C  CA  . ASN C 5   ? 0.0981 0.3596 0.2061 0.0019  -0.0621 0.0677  5   ASN C CA  
1769 C  C   . ASN C 5   ? 0.1707 0.3280 0.1347 -0.0444 -0.0471 0.0648  5   ASN C C   
1770 O  O   . ASN C 5   ? 0.1615 0.3755 0.1225 -0.0031 -0.0103 0.0766  5   ASN C O   
1771 C  CB  . ASN C 5   ? 0.1314 0.3470 0.2012 0.0153  -0.0173 0.0368  5   ASN C CB  
1772 C  CG  . ASN C 5   ? 0.0770 0.3931 0.2192 -0.0049 0.0742  0.0119  5   ASN C CG  
1773 O  OD1 . ASN C 5   ? 0.2430 0.4466 0.2070 -0.1397 0.0394  -0.0229 5   ASN C OD1 
1774 N  ND2 . ASN C 5   ? 0.2413 0.3906 0.2094 -0.0727 0.0315  0.0398  5   ASN C ND2 
1775 N  N   . THR C 6   ? 0.1626 0.3294 0.1288 -0.0532 -0.0548 0.0602  6   THR C N   
1776 C  CA  . THR C 6   ? 0.1906 0.3146 0.1567 -0.0489 -0.0629 0.0187  6   THR C CA  
1777 C  C   . THR C 6   ? 0.2133 0.2292 0.1103 -0.0441 -0.0742 0.0273  6   THR C C   
1778 O  O   . THR C 6   ? 0.1761 0.2391 0.1167 0.0080  -0.0363 -0.0046 6   THR C O   
1779 C  CB  . THR C 6   ? 0.1751 0.3203 0.1605 -0.0521 -0.0493 0.0551  6   THR C CB  
1780 O  OG1 . THR C 6   ? 0.2657 0.2668 0.1651 -0.0675 -0.0494 0.0080  6   THR C OG1 
1781 C  CG2 . THR C 6   ? 0.1770 0.3159 0.2095 -0.0499 -0.0505 0.0398  6   THR C CG2 
1782 N  N   . PHE C 7   ? 0.2010 0.2377 0.1125 0.0077  -0.0703 0.0236  7   PHE C N   
1783 C  CA  . PHE C 7   ? 0.1965 0.1816 0.1345 0.0346  -0.0587 0.0165  7   PHE C CA  
1784 C  C   . PHE C 7   ? 0.1884 0.1679 0.1368 0.0168  -0.0671 0.0352  7   PHE C C   
1785 O  O   . PHE C 7   ? 0.2125 0.1689 0.1379 0.0007  0.0094  0.0275  7   PHE C O   
1786 C  CB  . PHE C 7   ? 0.2379 0.1622 0.1502 0.0354  -0.0488 0.0328  7   PHE C CB  
1787 C  CG  . PHE C 7   ? 0.1746 0.2059 0.1529 0.0562  -0.0396 -0.0156 7   PHE C CG  
1788 C  CD1 . PHE C 7   ? 0.1685 0.2144 0.1562 0.0620  0.0006  -0.0373 7   PHE C CD1 
1789 C  CD2 . PHE C 7   ? 0.2158 0.2305 0.1380 0.0321  -0.0175 0.0201  7   PHE C CD2 
1790 C  CE1 . PHE C 7   ? 0.1634 0.2899 0.1569 0.0336  -0.0335 -0.0455 7   PHE C CE1 
1791 C  CE2 . PHE C 7   ? 0.1940 0.2787 0.1425 0.0419  -0.0038 0.0094  7   PHE C CE2 
1792 C  CZ  . PHE C 7   ? 0.1365 0.3169 0.1423 0.0323  -0.0255 -0.0175 7   PHE C CZ  
1793 N  N   . ASP C 8   ? 0.2296 0.1919 0.1340 -0.0111 -0.0037 -0.0122 8   ASP C N   
1794 C  CA  . ASP C 8   ? 0.2556 0.2267 0.1313 0.0009  -0.0227 -0.0199 8   ASP C CA  
1795 C  C   . ASP C 8   ? 0.2177 0.2340 0.1237 -0.0013 -0.0095 0.0003  8   ASP C C   
1796 O  O   . ASP C 8   ? 0.2355 0.2230 0.1403 -0.0290 -0.0325 -0.0002 8   ASP C O   
1797 C  CB  . ASP C 8   ? 0.4606 0.2216 0.1354 -0.0367 0.0138  -0.0798 8   ASP C CB  
1798 C  CG  . ASP C 8   ? 0.4932 0.2040 0.2732 -0.0075 -0.0463 -0.0264 8   ASP C CG  
1799 O  OD1 . ASP C 8   ? 0.3753 0.3192 0.3137 0.0934  -0.0968 0.0182  8   ASP C OD1 
1800 O  OD2 . ASP C 8   ? 0.6415 0.1994 0.2955 -0.0049 -0.0455 0.0538  8   ASP C OD2 
1801 N  N   . GLY C 9   ? 0.2509 0.2204 0.1438 -0.0471 -0.0344 0.0030  9   GLY C N   
1802 C  CA  . GLY C 9   ? 0.2067 0.2406 0.1555 -0.0690 -0.0158 0.0438  9   GLY C CA  
1803 C  C   . GLY C 9   ? 0.1554 0.2244 0.1138 -0.0213 -0.0184 0.1118  9   GLY C C   
1804 O  O   . GLY C 9   ? 0.1746 0.2392 0.1064 -0.0238 -0.0563 0.0628  9   GLY C O   
1805 N  N   . VAL C 10  ? 0.1653 0.2109 0.1094 0.0008  -0.0393 0.0190  10  VAL C N   
1806 C  CA  . VAL C 10  ? 0.1489 0.1964 0.0976 0.0274  -0.0086 0.0281  10  VAL C CA  
1807 C  C   . VAL C 10  ? 0.1578 0.1649 0.0946 0.0258  -0.0156 0.0449  10  VAL C C   
1808 O  O   . VAL C 10  ? 0.1874 0.1619 0.1062 0.0276  0.0012  0.0272  10  VAL C O   
1809 C  CB  . VAL C 10  ? 0.1004 0.2414 0.0938 0.0035  -0.0394 0.0084  10  VAL C CB  
1810 C  CG1 . VAL C 10  ? 0.1464 0.2462 0.1107 -0.0281 -0.0119 0.0040  10  VAL C CG1 
1811 C  CG2 . VAL C 10  ? 0.0902 0.2612 0.1132 -0.0003 0.0016  0.0416  10  VAL C CG2 
1812 N  N   . ALA C 11  ? 0.1678 0.1569 0.1006 0.0079  -0.0053 0.0326  11  ALA C N   
1813 C  CA  . ALA C 11  ? 0.1792 0.1375 0.1039 -0.0060 0.0034  0.0139  11  ALA C CA  
1814 C  C   . ALA C 11  ? 0.1486 0.1627 0.1070 0.0080  -0.0021 0.0373  11  ALA C C   
1815 O  O   . ALA C 11  ? 0.1689 0.1800 0.1087 -0.0051 0.0281  0.0205  11  ALA C O   
1816 C  CB  . ALA C 11  ? 0.1776 0.1522 0.1161 0.0193  -0.0245 0.0024  11  ALA C CB  
1817 N  N   . ASP C 12  ? 0.1390 0.2161 0.0985 -0.0005 -0.0110 0.0007  12  ASP C N   
1818 C  CA  . ASP C 12  ? 0.1597 0.2341 0.0927 0.0495  0.0026  -0.0083 12  ASP C CA  
1819 C  C   . ASP C 12  ? 0.1773 0.2292 0.0847 0.0310  -0.0328 0.0132  12  ASP C C   
1820 O  O   . ASP C 12  ? 0.2026 0.2367 0.0815 0.0414  -0.0119 0.0467  12  ASP C O   
1821 C  CB  . ASP C 12  ? 0.3237 0.2395 0.0581 -0.0097 -0.0538 -0.0118 12  ASP C CB  
1822 C  CG  . ASP C 12  ? 0.4246 0.2234 0.1508 0.0081  -0.0150 -0.0110 12  ASP C CG  
1823 O  OD1 . ASP C 12  ? 0.3668 0.2088 0.2913 0.1146  -0.0749 -0.0130 12  ASP C OD1 
1824 O  OD2 . ASP C 12  ? 0.5980 0.2291 0.2333 -0.0730 0.0596  -0.0225 12  ASP C OD2 
1825 N  N   . TYR C 13  ? 0.1730 0.2236 0.1051 0.0094  0.0011  0.0244  13  TYR C N   
1826 C  CA  . TYR C 13  ? 0.1425 0.2381 0.1137 0.0191  0.0287  0.0384  13  TYR C CA  
1827 C  C   . TYR C 13  ? 0.1548 0.2229 0.0953 0.0228  0.0108  0.0497  13  TYR C C   
1828 O  O   . TYR C 13  ? 0.1607 0.2228 0.1066 0.0217  0.0083  0.0575  13  TYR C O   
1829 C  CB  . TYR C 13  ? 0.1457 0.2526 0.1122 0.0144  -0.0227 0.0840  13  TYR C CB  
1830 C  CG  . TYR C 13  ? 0.1279 0.2611 0.1186 0.0476  -0.0352 0.0813  13  TYR C CG  
1831 C  CD1 . TYR C 13  ? 0.2434 0.2544 0.0975 0.0128  0.0517  0.0068  13  TYR C CD1 
1832 C  CD2 . TYR C 13  ? 0.1116 0.2816 0.1861 0.0384  -0.0168 0.0602  13  TYR C CD2 
1833 C  CE1 . TYR C 13  ? 0.2762 0.2468 0.1152 0.0182  0.0321  -0.0119 13  TYR C CE1 
1834 C  CE2 . TYR C 13  ? 0.1204 0.2800 0.1986 0.0517  -0.0513 0.0617  13  TYR C CE2 
1835 C  CZ  . TYR C 13  ? 0.2118 0.2768 0.1655 0.0626  -0.0302 0.0280  13  TYR C CZ  
1836 O  OH  . TYR C 13  ? 0.2293 0.2798 0.3072 0.1003  -0.0009 0.0614  13  TYR C OH  
1837 N  N   . LEU C 14  ? 0.1322 0.2176 0.1077 0.0421  -0.0137 0.0383  14  LEU C N   
1838 C  CA  . LEU C 14  ? 0.1495 0.2041 0.0880 0.0342  -0.0015 0.0370  14  LEU C CA  
1839 C  C   . LEU C 14  ? 0.1976 0.1686 0.0813 0.0189  0.0000  0.0780  14  LEU C C   
1840 O  O   . LEU C 14  ? 0.1770 0.1628 0.0717 0.0498  0.0277  0.0475  14  LEU C O   
1841 C  CB  . LEU C 14  ? 0.1475 0.1902 0.0862 0.0489  -0.0189 0.0101  14  LEU C CB  
1842 C  CG  . LEU C 14  ? 0.1791 0.1896 0.0863 0.0440  -0.0036 0.0025  14  LEU C CG  
1843 C  CD1 . LEU C 14  ? 0.1665 0.2002 0.0869 -0.0041 0.0165  -0.0071 14  LEU C CD1 
1844 C  CD2 . LEU C 14  ? 0.2316 0.1924 0.0845 0.0216  0.0286  -0.0045 14  LEU C CD2 
1845 N  N   . GLN C 15  ? 0.2187 0.1619 0.0890 0.0318  0.0152  0.0117  15  GLN C N   
1846 C  CA  . GLN C 15  ? 0.1746 0.1686 0.1098 0.0432  0.0423  0.0515  15  GLN C CA  
1847 C  C   . GLN C 15  ? 0.1967 0.1664 0.0988 0.0424  0.0708  0.0309  15  GLN C C   
1848 O  O   . GLN C 15  ? 0.1866 0.2166 0.1019 0.0313  0.0560  0.0618  15  GLN C O   
1849 C  CB  . GLN C 15  ? 0.1971 0.1717 0.1580 0.0854  0.0289  0.0439  15  GLN C CB  
1850 C  CG  . GLN C 15  ? 0.2085 0.1748 0.1634 0.0928  0.0132  0.0396  15  GLN C CG  
1851 C  CD  . GLN C 15  ? 0.1719 0.1845 0.1583 0.0668  -0.0121 0.0699  15  GLN C CD  
1852 O  OE1 . GLN C 15  ? 0.2192 0.1488 0.2730 0.0452  0.0271  -0.0077 15  GLN C OE1 
1853 N  NE2 . GLN C 15  ? 0.1486 0.3085 0.1451 0.0520  -0.0375 0.0211  15  GLN C NE2 
1854 N  N   . THR C 16  ? 0.1722 0.1774 0.1148 0.0664  0.0505  0.0448  16  THR C N   
1855 C  CA  . THR C 16  ? 0.1800 0.1757 0.1207 0.0665  -0.0187 0.0651  16  THR C CA  
1856 C  C   . THR C 16  ? 0.1960 0.1767 0.0865 0.0765  -0.0096 0.0703  16  THR C C   
1857 O  O   . THR C 16  ? 0.2349 0.1833 0.0795 0.0263  -0.0309 0.0321  16  THR C O   
1858 C  CB  . THR C 16  ? 0.1800 0.1916 0.1247 0.0559  -0.0428 -0.0214 16  THR C CB  
1859 O  OG1 . THR C 16  ? 0.3341 0.1711 0.1471 0.0407  -0.0101 0.0024  16  THR C OG1 
1860 C  CG2 . THR C 16  ? 0.2789 0.2045 0.1101 -0.0088 -0.0306 0.0181  16  THR C CG2 
1861 N  N   . TYR C 17  ? 0.2007 0.1649 0.0802 0.0556  0.0251  0.0172  17  TYR C N   
1862 C  CA  . TYR C 17  ? 0.1927 0.1615 0.1283 0.0290  -0.0168 0.0036  17  TYR C CA  
1863 C  C   . TYR C 17  ? 0.1890 0.1492 0.1293 0.0297  0.0076  -0.0224 17  TYR C C   
1864 O  O   . TYR C 17  ? 0.2207 0.1557 0.1608 0.0459  0.0260  0.0150  17  TYR C O   
1865 C  CB  . TYR C 17  ? 0.1812 0.1862 0.2437 0.0185  -0.0402 -0.0067 17  TYR C CB  
1866 C  CG  . TYR C 17  ? 0.1878 0.1820 0.2437 0.0321  -0.0674 0.0183  17  TYR C CG  
1867 C  CD1 . TYR C 17  ? 0.3008 0.2587 0.2301 -0.0041 -0.1116 0.0477  17  TYR C CD1 
1868 C  CD2 . TYR C 17  ? 0.2441 0.1936 0.2903 -0.0190 -0.0581 0.0147  17  TYR C CD2 
1869 C  CE1 . TYR C 17  ? 0.3624 0.3082 0.2267 -0.0540 -0.1105 0.0488  17  TYR C CE1 
1870 C  CE2 . TYR C 17  ? 0.3373 0.2130 0.2918 -0.0642 -0.0069 -0.0010 17  TYR C CE2 
1871 C  CZ  . TYR C 17  ? 0.3362 0.2934 0.2820 -0.0573 -0.0872 0.0111  17  TYR C CZ  
1872 O  OH  . TYR C 17  ? 0.4681 0.4292 0.2966 -0.2283 -0.0638 0.0002  17  TYR C OH  
1873 N  N   . HIS C 18  ? 0.1894 0.1626 0.1148 0.0385  0.0112  0.0169  18  HIS C N   
1874 C  CA  . HIS C 18  ? 0.2026 0.1647 0.1002 0.0339  0.0618  0.0195  18  HIS C CA  
1875 C  C   . HIS C 18  ? 0.2159 0.1526 0.1109 0.0928  0.0299  0.0177  18  HIS C C   
1876 O  O   . HIS C 18  ? 0.2752 0.1594 0.1285 0.0601  0.0571  0.0006  18  HIS C O   
1877 C  CB  . HIS C 18  ? 0.1928 0.1405 0.1103 0.0497  0.0193  -0.0079 18  HIS C CB  
1878 C  CG  . HIS C 18  ? 0.2170 0.1273 0.1012 0.0376  -0.0361 -0.0009 18  HIS C CG  
1879 N  ND1 . HIS C 18  ? 0.1579 0.1474 0.1038 0.0540  -0.0251 -0.0091 18  HIS C ND1 
1880 C  CD2 . HIS C 18  ? 0.2579 0.1255 0.0938 0.0647  0.0123  -0.0260 18  HIS C CD2 
1881 C  CE1 . HIS C 18  ? 0.2386 0.1200 0.1012 0.0566  0.0379  0.0119  18  HIS C CE1 
1882 N  NE2 . HIS C 18  ? 0.2549 0.1232 0.0902 0.0413  0.0515  -0.0092 18  HIS C NE2 
1883 N  N   . LYS C 19  ? 0.2738 0.2160 0.0698 0.0298  0.0606  0.0366  19  LYS C N   
1884 C  CA  . LYS C 19  ? 0.3280 0.2006 0.0727 0.0433  0.0567  0.0492  19  LYS C CA  
1885 C  C   . LYS C 19  ? 0.2167 0.2111 0.0725 0.0840  0.0620  0.0424  19  LYS C C   
1886 O  O   . LYS C 19  ? 0.2390 0.2082 0.0860 0.0479  0.0117  0.0110  19  LYS C O   
1887 C  CB  . LYS C 19  ? 0.3319 0.1850 0.1843 0.0613  0.0845  0.0685  19  LYS C CB  
1888 C  CG  . LYS C 19  ? 0.2584 0.2864 0.2990 0.0460  0.0674  0.0291  19  LYS C CG  
1889 C  CD  . LYS C 19  ? 0.2308 0.3091 0.3160 0.0600  0.0046  0.0550  19  LYS C CD  
1890 C  CE  . LYS C 19  ? 0.2142 0.4000 0.3501 0.0269  -0.0032 0.0518  19  LYS C CE  
1891 N  NZ  . LYS C 19  ? 0.2282 0.3839 0.6384 -0.0685 -0.0429 -0.0576 19  LYS C NZ  
1892 N  N   . LEU C 20  ? 0.1481 0.2599 0.0792 0.0949  0.0476  0.0541  20  LEU C N   
1893 C  CA  . LEU C 20  ? 0.1920 0.2579 0.0879 0.0570  0.0536  0.0897  20  LEU C CA  
1894 C  C   . LEU C 20  ? 0.1606 0.3125 0.1029 0.0733  0.0355  0.0585  20  LEU C C   
1895 O  O   . LEU C 20  ? 0.1581 0.3036 0.1769 0.0775  0.0375  0.0496  20  LEU C O   
1896 C  CB  . LEU C 20  ? 0.2179 0.2300 0.0945 0.0340  0.0298  0.0429  20  LEU C CB  
1897 C  CG  . LEU C 20  ? 0.1817 0.2669 0.0857 0.0563  -0.0100 0.0446  20  LEU C CG  
1898 C  CD1 . LEU C 20  ? 0.2990 0.3295 0.0723 0.0370  0.0133  0.0097  20  LEU C CD1 
1899 C  CD2 . LEU C 20  ? 0.1148 0.2700 0.1905 0.0418  -0.0072 0.1167  20  LEU C CD2 
1900 N  N   . PRO C 21  ? 0.1539 0.3202 0.1095 0.0675  0.0289  0.0959  21  PRO C N   
1901 C  CA  . PRO C 21  ? 0.1327 0.3669 0.1539 0.0769  0.0567  0.0791  21  PRO C CA  
1902 C  C   . PRO C 21  ? 0.1063 0.3952 0.1615 0.1122  0.0298  0.1249  21  PRO C C   
1903 O  O   . PRO C 21  ? 0.1555 0.3502 0.1590 0.1309  0.0329  0.0683  21  PRO C O   
1904 C  CB  . PRO C 21  ? 0.1532 0.3728 0.2287 0.0415  -0.0011 0.0437  21  PRO C CB  
1905 C  CG  . PRO C 21  ? 0.1915 0.3378 0.2003 0.0184  -0.0846 0.0900  21  PRO C CG  
1906 C  CD  . PRO C 21  ? 0.1676 0.3132 0.1662 0.0431  -0.0351 0.0796  21  PRO C CD  
1907 N  N   . ASP C 22  ? 0.0845 0.4238 0.2622 0.1307  0.0156  0.1095  22  ASP C N   
1908 C  CA  . ASP C 22  ? 0.1205 0.3925 0.2674 0.1625  0.0220  0.1592  22  ASP C CA  
1909 C  C   . ASP C 22  ? 0.1852 0.4522 0.2471 0.1281  0.0879  0.0882  22  ASP C C   
1910 O  O   . ASP C 22  ? 0.3160 0.4502 0.2279 0.1972  0.0998  0.0931  22  ASP C O   
1911 C  CB  . ASP C 22  ? 0.1626 0.3529 0.2699 0.1257  -0.0372 0.1417  22  ASP C CB  
1912 C  CG  . ASP C 22  ? 0.3055 0.4074 0.2536 0.0483  -0.0838 0.1236  22  ASP C CG  
1913 O  OD1 . ASP C 22  ? 0.4571 0.5162 0.2800 -0.1053 0.0575  0.1062  22  ASP C OD1 
1914 O  OD2 . ASP C 22  ? 0.4446 0.6405 0.2627 -0.1337 -0.0213 0.0037  22  ASP C OD2 
1915 N  N   . ASN C 23  ? 0.1540 0.4598 0.2027 0.1156  0.0493  0.0851  23  ASN C N   
1916 C  CA  . ASN C 23  ? 0.0956 0.4991 0.2005 0.0750  0.0466  0.0774  23  ASN C CA  
1917 C  C   . ASN C 23  ? 0.1346 0.4525 0.2025 0.0452  0.0256  0.0866  23  ASN C C   
1918 O  O   . ASN C 23  ? 0.1523 0.5006 0.1940 0.0243  -0.0088 0.1092  23  ASN C O   
1919 C  CB  . ASN C 23  ? 0.1477 0.5179 0.1707 -0.0023 0.0181  0.0661  23  ASN C CB  
1920 C  CG  . ASN C 23  ? 0.2149 0.4698 0.1547 -0.0182 0.0061  0.0896  23  ASN C CG  
1921 O  OD1 . ASN C 23  ? 0.3214 0.4178 0.1537 -0.0652 0.0135  0.0390  23  ASN C OD1 
1922 N  ND2 . ASN C 23  ? 0.2571 0.4529 0.1613 0.0140  0.0026  0.0218  23  ASN C ND2 
1923 N  N   . TYR C 24  ? 0.1393 0.3901 0.1967 0.0631  0.0652  0.0917  24  TYR C N   
1924 C  CA  . TYR C 24  ? 0.1066 0.2858 0.2105 0.1207  0.0884  0.0576  24  TYR C CA  
1925 C  C   . TYR C 24  ? 0.1682 0.2810 0.2152 0.1351  0.0699  0.0861  24  TYR C C   
1926 O  O   . TYR C 24  ? 0.3343 0.2811 0.2132 0.1740  0.0158  0.1047  24  TYR C O   
1927 C  CB  . TYR C 24  ? 0.1429 0.2769 0.1451 0.1033  -0.0102 0.1083  24  TYR C CB  
1928 C  CG  . TYR C 24  ? 0.1189 0.2752 0.1194 0.0868  0.0582  0.1097  24  TYR C CG  
1929 C  CD1 . TYR C 24  ? 0.1582 0.2684 0.1203 0.0740  -0.0096 0.0877  24  TYR C CD1 
1930 C  CD2 . TYR C 24  ? 0.1930 0.2718 0.1177 0.0719  -0.0006 0.1281  24  TYR C CD2 
1931 C  CE1 . TYR C 24  ? 0.1499 0.2680 0.1114 0.0763  0.0232  0.0776  24  TYR C CE1 
1932 C  CE2 . TYR C 24  ? 0.1424 0.2796 0.1130 0.0898  0.0271  0.0544  24  TYR C CE2 
1933 C  CZ  . TYR C 24  ? 0.1486 0.2741 0.1099 0.0618  0.0348  0.0799  24  TYR C CZ  
1934 O  OH  . TYR C 24  ? 0.1851 0.2647 0.1009 0.0264  -0.0459 0.0501  24  TYR C OH  
1935 N  N   . ILE C 25  ? 0.1830 0.3093 0.2120 0.1006  0.0799  0.0533  25  ILE C N   
1936 C  CA  . ILE C 25  ? 0.1509 0.3040 0.2143 0.1213  0.1068  0.0990  25  ILE C CA  
1937 C  C   . ILE C 25  ? 0.1608 0.2622 0.2294 0.1094  0.0765  0.0982  25  ILE C C   
1938 O  O   . ILE C 25  ? 0.1908 0.2564 0.2178 0.0945  0.0613  0.0744  25  ILE C O   
1939 C  CB  . ILE C 25  ? 0.1391 0.3306 0.2291 0.1095  0.1069  0.1032  25  ILE C CB  
1940 C  CG1 . ILE C 25  ? 0.2289 0.3738 0.2173 0.0348  0.1733  0.0748  25  ILE C CG1 
1941 C  CG2 . ILE C 25  ? 0.1292 0.3774 0.2504 0.0793  0.0660  0.0670  25  ILE C CG2 
1942 C  CD1 . ILE C 25  ? 0.2291 0.3859 0.2167 0.0473  0.0929  0.0905  25  ILE C CD1 
1943 N  N   . THR C 26  ? 0.1650 0.2468 0.2711 0.1229  0.0833  0.1131  26  THR C N   
1944 C  CA  . THR C 26  ? 0.1901 0.2164 0.2809 0.0870  0.0949  0.0643  26  THR C CA  
1945 C  C   . THR C 26  ? 0.2173 0.2221 0.2788 0.0744  0.1108  0.0511  26  THR C C   
1946 O  O   . THR C 26  ? 0.1898 0.2748 0.2564 0.0930  0.0899  0.0956  26  THR C O   
1947 C  CB  . THR C 26  ? 0.3090 0.2148 0.2836 0.0275  0.1530  0.0567  26  THR C CB  
1948 O  OG1 . THR C 26  ? 0.3109 0.2212 0.3337 0.0790  0.1674  0.0266  26  THR C OG1 
1949 C  CG2 . THR C 26  ? 0.4058 0.2052 0.2777 -0.0054 0.1388  0.0819  26  THR C CG2 
1950 N  N   . LYS C 27  ? 0.2013 0.2656 0.2803 0.0713  0.1030  0.0249  27  LYS C N   
1951 C  CA  . LYS C 27  ? 0.3142 0.2728 0.2702 0.0917  0.1489  -0.0036 27  LYS C CA  
1952 C  C   . LYS C 27  ? 0.3136 0.2708 0.2728 0.0932  0.1290  0.0504  27  LYS C C   
1953 O  O   . LYS C 27  ? 0.2826 0.2929 0.2878 0.1165  0.1502  0.0244  27  LYS C O   
1954 C  CB  . LYS C 27  ? 0.3328 0.2609 0.2512 0.0898  0.0766  -0.0068 27  LYS C CB  
1955 C  CG  . LYS C 27  ? 0.3494 0.2644 0.3120 0.1388  0.0645  -0.0197 27  LYS C CG  
1956 C  CD  . LYS C 27  ? 0.3384 0.2722 0.3634 0.1495  0.0422  -0.0087 27  LYS C CD  
1957 C  CE  . LYS C 27  ? 0.3165 0.3695 0.3732 0.1123  0.0053  -0.0097 27  LYS C CE  
1958 N  NZ  . LYS C 27  ? 0.3667 0.4878 0.5215 -0.0318 0.0017  -0.0390 27  LYS C NZ  
1959 N  N   . SER C 28  ? 0.2834 0.2720 0.3354 0.0972  0.1811  0.0221  28  SER C N   
1960 C  CA  . SER C 28  ? 0.3185 0.2663 0.4261 0.1020  0.2308  0.0202  28  SER C CA  
1961 C  C   . SER C 28  ? 0.3093 0.2556 0.4264 0.1291  0.2319  0.0489  28  SER C C   
1962 O  O   . SER C 28  ? 0.3046 0.2763 0.4163 0.1291  0.1971  0.0180  28  SER C O   
1963 C  CB  . SER C 28  ? 0.3731 0.2750 0.4141 0.0656  0.1582  0.0021  28  SER C CB  
1964 O  OG  . SER C 28  ? 0.5961 0.4447 0.4118 -0.0968 0.2353  -0.0281 28  SER C OG  
1965 N  N   . GLU C 29  ? 0.2919 0.2450 0.4323 0.1358  0.2016  0.1076  29  GLU C N   
1966 C  CA  . GLU C 29  ? 0.3061 0.2714 0.4329 0.1023  0.2004  0.1686  29  GLU C CA  
1967 C  C   . GLU C 29  ? 0.3015 0.2732 0.4295 0.1101  0.1271  0.1855  29  GLU C C   
1968 O  O   . GLU C 29  ? 0.2755 0.2933 0.3840 0.1556  0.1613  0.1444  29  GLU C O   
1969 C  CB  . GLU C 29  ? 0.2994 0.3175 0.4304 0.1291  0.2157  0.1698  29  GLU C CB  
1970 C  CG  . GLU C 29  ? 0.4688 0.3460 0.4212 0.0828  0.1678  0.1653  29  GLU C CG  
1971 C  CD  . GLU C 29  ? 0.6447 0.3839 0.4106 0.0366  0.1113  0.1889  29  GLU C CD  
1972 O  OE1 . GLU C 29  ? 0.5558 0.3819 0.3962 0.1921  0.0455  0.1602  29  GLU C OE1 
1973 O  OE2 . GLU C 29  ? 0.7368 0.3949 0.4130 0.0446  0.0888  0.1515  29  GLU C OE2 
1974 N  N   . ALA C 30  ? 0.2671 0.2883 0.3520 0.1288  0.1759  0.1682  30  ALA C N   
1975 C  CA  . ALA C 30  ? 0.1916 0.2979 0.3336 0.1679  0.1714  0.1904  30  ALA C CA  
1976 C  C   . ALA C 30  ? 0.2478 0.2780 0.3414 0.2100  0.2402  0.1058  30  ALA C C   
1977 O  O   . ALA C 30  ? 0.2648 0.3200 0.2811 0.1974  0.1823  0.1027  30  ALA C O   
1978 C  CB  . ALA C 30  ? 0.1459 0.2930 0.2756 0.0979  0.0922  0.1390  30  ALA C CB  
1979 N  N   . GLN C 31  ? 0.3141 0.3391 0.3122 0.1475  0.2126  0.0729  31  GLN C N   
1980 C  CA  . GLN C 31  ? 0.4481 0.2902 0.3186 0.1704  0.2546  0.0629  31  GLN C CA  
1981 C  C   . GLN C 31  ? 0.4626 0.2909 0.3755 0.2024  0.3304  0.0821  31  GLN C C   
1982 O  O   . GLN C 31  ? 0.4139 0.3110 0.3958 0.2405  0.2256  0.1123  31  GLN C O   
1983 C  CB  . GLN C 31  ? 0.5174 0.2632 0.2893 0.1145  0.2029  0.0184  31  GLN C CB  
1984 C  CG  . GLN C 31  ? 0.4393 0.2863 0.4443 0.1336  0.1318  0.0381  31  GLN C CG  
1985 C  CD  . GLN C 31  ? 0.4738 0.3557 0.6031 0.0637  0.0014  0.0784  31  GLN C CD  
1986 O  OE1 . GLN C 31  ? 0.6414 0.3700 0.8046 -0.0611 -0.1958 0.0915  31  GLN C OE1 
1987 N  NE2 . GLN C 31  ? 0.3813 0.4051 0.7875 0.0920  0.0105  -0.0186 31  GLN C NE2 
1988 N  N   . ALA C 32  ? 0.4685 0.2728 0.3960 0.1924  0.3110  0.1168  32  ALA C N   
1989 C  CA  . ALA C 32  ? 0.4783 0.2707 0.4418 0.1763  0.2830  0.1245  32  ALA C CA  
1990 C  C   . ALA C 32  ? 0.4274 0.3403 0.4255 0.2087  0.2311  0.1193  32  ALA C C   
1991 O  O   . ALA C 32  ? 0.4301 0.3294 0.4976 0.2349  0.2228  0.0872  32  ALA C O   
1992 C  CB  . ALA C 32  ? 0.4668 0.2579 0.4479 0.2077  0.2290  0.1604  32  ALA C CB  
1993 N  N   . LEU C 33  ? 0.3591 0.3457 0.3943 0.2086  0.2232  0.1291  33  LEU C N   
1994 C  CA  . LEU C 33  ? 0.3387 0.4140 0.4022 0.2126  0.1684  0.1657  33  LEU C CA  
1995 C  C   . LEU C 33  ? 0.2567 0.4102 0.4153 0.2391  0.1893  0.2138  33  LEU C C   
1996 O  O   . LEU C 33  ? 0.2546 0.5263 0.4674 0.2065  0.1993  0.3065  33  LEU C O   
1997 C  CB  . LEU C 33  ? 0.3842 0.4430 0.4106 0.1540  0.1521  0.1238  33  LEU C CB  
1998 C  CG  . LEU C 33  ? 0.4060 0.4350 0.3764 0.1402  0.1195  0.1542  33  LEU C CG  
1999 C  CD1 . LEU C 33  ? 0.5107 0.4350 0.3914 0.1030  0.1703  0.0715  33  LEU C CD1 
2000 C  CD2 . LEU C 33  ? 0.3498 0.4929 0.3822 0.1050  -0.0159 0.1593  33  LEU C CD2 
2001 N  N   . GLY C 34  ? 0.3180 0.3020 0.4223 0.2115  0.2009  0.1985  34  GLY C N   
2002 C  CA  . GLY C 34  ? 0.2290 0.2901 0.4385 0.1879  0.2149  0.1909  34  GLY C CA  
2003 C  C   . GLY C 34  ? 0.1722 0.3085 0.3515 0.1742  0.2058  0.1437  34  GLY C C   
2004 O  O   . GLY C 34  ? 0.2492 0.3501 0.3148 0.1300  0.1933  0.1575  34  GLY C O   
2005 N  N   . TRP C 35  ? 0.1964 0.2972 0.3148 0.1836  0.1435  0.1583  35  TRP C N   
2006 C  CA  . TRP C 35  ? 0.1990 0.2871 0.2716 0.1579  0.1548  0.0821  35  TRP C CA  
2007 C  C   . TRP C 35  ? 0.2268 0.2814 0.2710 0.1475  0.0716  0.1050  35  TRP C C   
2008 O  O   . TRP C 35  ? 0.2752 0.2970 0.2749 0.1113  0.1071  0.0469  35  TRP C O   
2009 C  CB  . TRP C 35  ? 0.2033 0.2765 0.2725 0.1498  0.0894  0.0668  35  TRP C CB  
2010 C  CG  . TRP C 35  ? 0.2047 0.2680 0.2139 0.1017  0.0888  0.0585  35  TRP C CG  
2011 C  CD1 . TRP C 35  ? 0.1793 0.2681 0.2427 0.1041  0.0671  0.0851  35  TRP C CD1 
2012 C  CD2 . TRP C 35  ? 0.2051 0.2747 0.1741 0.0915  0.0903  0.0447  35  TRP C CD2 
2013 N  NE1 . TRP C 35  ? 0.1756 0.2705 0.2088 0.1021  0.0528  0.0648  35  TRP C NE1 
2014 C  CE2 . TRP C 35  ? 0.1762 0.2853 0.1284 0.1002  0.0542  0.0214  35  TRP C CE2 
2015 C  CE3 . TRP C 35  ? 0.2125 0.2757 0.1936 0.0907  0.0859  0.0494  35  TRP C CE3 
2016 C  CZ2 . TRP C 35  ? 0.1847 0.2841 0.1968 0.0915  0.0667  0.0332  35  TRP C CZ2 
2017 C  CZ3 . TRP C 35  ? 0.2075 0.2869 0.1923 0.0817  0.0410  0.0756  35  TRP C CZ3 
2018 C  CH2 . TRP C 35  ? 0.1736 0.2956 0.1866 0.0946  0.0803  0.0467  35  TRP C CH2 
2019 N  N   . VAL C 36  ? 0.2400 0.2789 0.2636 0.1484  0.0690  0.1137  36  VAL C N   
2020 C  CA  . VAL C 36  ? 0.2420 0.2885 0.2678 0.1395  0.0863  0.0595  36  VAL C CA  
2021 C  C   . VAL C 36  ? 0.2539 0.2665 0.2382 0.0897  0.0868  0.0111  36  VAL C C   
2022 O  O   . VAL C 36  ? 0.2473 0.2826 0.1962 0.0772  0.0114  0.0344  36  VAL C O   
2023 C  CB  . VAL C 36  ? 0.2479 0.2762 0.2630 0.1639  0.0082  0.0643  36  VAL C CB  
2024 C  CG1 . VAL C 36  ? 0.2808 0.2929 0.2667 0.0732  -0.0560 -0.0101 36  VAL C CG1 
2025 C  CG2 . VAL C 36  ? 0.3225 0.2303 0.2963 0.0891  0.0207  0.0453  36  VAL C CG2 
2026 N  N   . ALA C 37  ? 0.2750 0.2622 0.1728 0.0627  0.0508  0.0516  37  ALA C N   
2027 C  CA  . ALA C 37  ? 0.2618 0.2563 0.1627 0.0120  0.0017  0.0514  37  ALA C CA  
2028 C  C   . ALA C 37  ? 0.2312 0.2618 0.1524 0.0231  0.0458  0.0207  37  ALA C C   
2029 O  O   . ALA C 37  ? 0.2083 0.2577 0.1396 0.0628  0.0285  0.0458  37  ALA C O   
2030 C  CB  . ALA C 37  ? 0.2818 0.2883 0.1820 -0.0318 -0.0526 0.0754  37  ALA C CB  
2031 N  N   . SER C 38  ? 0.2082 0.2455 0.1611 0.0488  0.0331  -0.0114 38  SER C N   
2032 C  CA  . SER C 38  ? 0.2573 0.2774 0.1490 0.0196  0.0476  0.0020  38  SER C CA  
2033 C  C   . SER C 38  ? 0.2307 0.3564 0.0904 0.0186  0.0576  -0.0047 38  SER C C   
2034 O  O   . SER C 38  ? 0.2046 0.3142 0.1513 0.0220  0.0219  0.0095  38  SER C O   
2035 C  CB  . SER C 38  ? 0.2423 0.2964 0.1609 0.0121  0.0567  0.0124  38  SER C CB  
2036 O  OG  . SER C 38  ? 0.2626 0.3835 0.2676 -0.0422 0.0022  0.0168  38  SER C OG  
2037 N  N   . LYS C 39  ? 0.2269 0.3589 0.1060 0.0392  0.0404  0.0522  39  LYS C N   
2038 C  CA  . LYS C 39  ? 0.1812 0.3879 0.1219 0.0709  0.0880  0.0021  39  LYS C CA  
2039 C  C   . LYS C 39  ? 0.1512 0.3929 0.1289 0.0559  0.0537  0.0443  39  LYS C C   
2040 O  O   . LYS C 39  ? 0.1957 0.4371 0.1775 0.0075  0.0480  0.0549  39  LYS C O   
2041 C  CB  . LYS C 39  ? 0.2080 0.3739 0.2483 0.0881  0.0913  -0.0803 39  LYS C CB  
2042 C  CG  . LYS C 39  ? 0.3275 0.3180 0.2926 0.0895  0.0715  -0.0925 39  LYS C CG  
2043 C  CD  . LYS C 39  ? 0.3312 0.3163 0.3604 0.0809  0.0705  -0.0716 39  LYS C CD  
2044 C  CE  . LYS C 39  ? 0.3204 0.3127 0.3628 0.0900  0.0706  -0.0715 39  LYS C CE  
2045 N  NZ  . LYS C 39  ? 0.3282 0.3076 0.3645 0.0936  0.0704  -0.0715 39  LYS C NZ  
2046 N  N   . GLY C 40  ? 0.1890 0.3503 0.1190 0.0533  0.0372  0.0503  40  GLY C N   
2047 C  CA  . GLY C 40  ? 0.1575 0.3002 0.1612 0.0576  0.0022  0.1193  40  GLY C CA  
2048 C  C   . GLY C 40  ? 0.1329 0.3065 0.1585 0.0708  0.0362  0.1157  40  GLY C C   
2049 O  O   . GLY C 40  ? 0.1954 0.3007 0.1457 0.0422  0.0119  0.0514  40  GLY C O   
2050 N  N   . ASN C 41  ? 0.1600 0.3021 0.1670 0.0740  0.0164  0.0892  41  ASN C N   
2051 C  CA  . ASN C 41  ? 0.1615 0.2963 0.1695 0.0910  0.0099  0.0540  41  ASN C CA  
2052 C  C   . ASN C 41  ? 0.1616 0.3006 0.1710 0.1146  -0.0045 0.1132  41  ASN C C   
2053 O  O   . ASN C 41  ? 0.1582 0.3150 0.1635 0.1024  0.0202  0.1005  41  ASN C O   
2054 C  CB  . ASN C 41  ? 0.1858 0.2952 0.1690 0.0993  0.0054  0.0373  41  ASN C CB  
2055 C  CG  . ASN C 41  ? 0.2430 0.2933 0.1950 0.0790  0.0117  0.0383  41  ASN C CG  
2056 O  OD1 . ASN C 41  ? 0.2076 0.2992 0.3014 0.0832  0.1039  0.0566  41  ASN C OD1 
2057 N  ND2 . ASN C 41  ? 0.2321 0.2925 0.2920 0.0892  0.0772  0.0053  41  ASN C ND2 
2058 N  N   . LEU C 42  ? 0.1496 0.3320 0.1728 0.0753  0.0419  0.1272  42  LEU C N   
2059 C  CA  . LEU C 42  ? 0.1630 0.3382 0.1725 0.1052  0.0733  0.1015  42  LEU C CA  
2060 C  C   . LEU C 42  ? 0.1582 0.3618 0.1642 0.1025  0.0401  0.1326  42  LEU C C   
2061 O  O   . LEU C 42  ? 0.1604 0.3667 0.1749 0.1255  0.0519  0.1148  42  LEU C O   
2062 C  CB  . LEU C 42  ? 0.1622 0.3246 0.1612 0.1078  0.1100  0.0680  42  LEU C CB  
2063 C  CG  . LEU C 42  ? 0.2299 0.3211 0.1628 0.0728  0.1276  0.0453  42  LEU C CG  
2064 C  CD1 . LEU C 42  ? 0.2519 0.3214 0.1661 0.0803  0.1005  0.0648  42  LEU C CD1 
2065 C  CD2 . LEU C 42  ? 0.2506 0.3131 0.1487 0.0274  0.1105  0.0457  42  LEU C CD2 
2066 N  N   . ALA C 43  ? 0.1697 0.3693 0.1854 0.0853  0.0574  0.1164  43  ALA C N   
2067 C  CA  . ALA C 43  ? 0.1704 0.4234 0.2420 0.0540  -0.0169 0.1211  43  ALA C CA  
2068 C  C   . ALA C 43  ? 0.1478 0.4337 0.2912 0.0716  0.0536  0.1340  43  ALA C C   
2069 O  O   . ALA C 43  ? 0.1244 0.5209 0.2991 0.0609  0.0392  0.1847  43  ALA C O   
2070 C  CB  . ALA C 43  ? 0.1553 0.4231 0.2428 0.0423  -0.0135 0.1044  43  ALA C CB  
2071 N  N   . ASP C 44  ? 0.1054 0.4433 0.2940 0.1224  0.0614  0.1895  44  ASP C N   
2072 C  CA  . ASP C 44  ? 0.1455 0.4225 0.2928 0.0791  0.0512  0.1887  44  ASP C CA  
2073 C  C   . ASP C 44  ? 0.1612 0.4246 0.2864 0.1066  0.0810  0.1630  44  ASP C C   
2074 O  O   . ASP C 44  ? 0.1819 0.4086 0.3085 0.0733  0.0270  0.1813  44  ASP C O   
2075 C  CB  . ASP C 44  ? 0.2329 0.4217 0.2843 0.0873  0.0477  0.1429  44  ASP C CB  
2076 C  CG  . ASP C 44  ? 0.3775 0.4112 0.3090 0.0587  0.0121  0.1598  44  ASP C CG  
2077 O  OD1 . ASP C 44  ? 0.3590 0.4276 0.4237 0.0416  0.0631  0.2023  44  ASP C OD1 
2078 O  OD2 . ASP C 44  ? 0.4465 0.3441 0.3168 0.0216  -0.0675 0.0732  44  ASP C OD2 
2079 N  N   . VAL C 45  ? 0.1363 0.3931 0.2427 0.1352  0.0301  0.1646  45  VAL C N   
2080 C  CA  . VAL C 45  ? 0.1741 0.3887 0.2393 0.1632  0.0771  0.1663  45  VAL C CA  
2081 C  C   . VAL C 45  ? 0.1556 0.3841 0.2446 0.1190  0.0747  0.2091  45  VAL C C   
2082 O  O   . VAL C 45  ? 0.1778 0.3846 0.2411 0.1432  0.0495  0.1511  45  VAL C O   
2083 C  CB  . VAL C 45  ? 0.1988 0.3722 0.2384 0.1563  0.0867  0.1269  45  VAL C CB  
2084 C  CG1 . VAL C 45  ? 0.2507 0.3401 0.2382 0.1540  0.0694  0.0992  45  VAL C CG1 
2085 C  CG2 . VAL C 45  ? 0.2027 0.3768 0.2643 0.1342  0.0637  0.0356  45  VAL C CG2 
2086 N  N   . ALA C 46  ? 0.1520 0.3912 0.2380 0.1304  0.0896  0.1684  46  ALA C N   
2087 C  CA  . ALA C 46  ? 0.1142 0.4352 0.2372 0.1237  0.0897  0.1939  46  ALA C CA  
2088 C  C   . ALA C 46  ? 0.0909 0.4341 0.2269 0.1296  0.0888  0.1932  46  ALA C C   
2089 O  O   . ALA C 46  ? 0.0984 0.4372 0.2289 0.1014  0.0613  0.1628  46  ALA C O   
2090 C  CB  . ALA C 46  ? 0.1451 0.4453 0.2605 0.0945  0.0844  0.1115  46  ALA C CB  
2091 N  N   . PRO C 47  ? 0.0967 0.4497 0.2787 0.1140  0.1096  0.2052  47  PRO C N   
2092 C  CA  . PRO C 47  ? 0.1343 0.4661 0.2402 0.0870  0.0602  0.1752  47  PRO C CA  
2093 C  C   . PRO C 47  ? 0.1113 0.5580 0.2265 0.1011  0.0715  0.2167  47  PRO C C   
2094 O  O   . PRO C 47  ? 0.1579 0.5581 0.2400 0.1128  0.0420  0.2560  47  PRO C O   
2095 C  CB  . PRO C 47  ? 0.1527 0.4693 0.2555 0.0666  0.0669  0.1614  47  PRO C CB  
2096 C  CG  . PRO C 47  ? 0.1269 0.4863 0.2275 0.0666  0.0525  0.1086  47  PRO C CG  
2097 C  CD  . PRO C 47  ? 0.1052 0.4591 0.2868 0.0848  0.1100  0.1774  47  PRO C CD  
2098 N  N   . GLY C 48  ? 0.0957 0.5560 0.1699 0.0529  0.0109  0.1321  48  GLY C N   
2099 C  CA  . GLY C 48  ? 0.1210 0.5810 0.1649 0.0173  0.0314  0.0911  48  GLY C CA  
2100 C  C   . GLY C 48  ? 0.1328 0.5702 0.1511 0.0075  0.0599  0.0610  48  GLY C C   
2101 O  O   . GLY C 48  ? 0.1547 0.7765 0.0952 -0.0103 -0.0004 -0.0116 48  GLY C O   
2102 N  N   . LYS C 49  ? 0.0759 0.5035 0.1946 0.0584  0.0000  0.1035  49  LYS C N   
2103 C  CA  . LYS C 49  ? 0.0588 0.4432 0.1836 0.0958  0.0143  0.0951  49  LYS C CA  
2104 C  C   . LYS C 49  ? 0.0857 0.4387 0.1442 0.0576  0.0236  0.0843  49  LYS C C   
2105 O  O   . LYS C 49  ? 0.1043 0.4324 0.1459 0.0703  0.0053  0.0856  49  LYS C O   
2106 C  CB  A LYS C 49  ? 0.1447 0.4372 0.2499 0.1076  0.0288  0.1347  49  LYS C CB  
2107 C  CB  B LYS C 49  ? 0.1504 0.4353 0.2420 0.1066  0.0233  0.1364  49  LYS C CB  
2108 C  CG  A LYS C 49  ? 0.1656 0.4214 0.2417 0.1029  0.0230  0.1358  49  LYS C CG  
2109 C  CG  B LYS C 49  ? 0.1686 0.4200 0.2416 0.1045  0.0155  0.1409  49  LYS C CG  
2110 C  CD  A LYS C 49  ? 0.2469 0.4223 0.2391 0.0669  -0.0329 0.1346  49  LYS C CD  
2111 C  CD  B LYS C 49  ? 0.1985 0.4105 0.2396 0.0847  -0.0347 0.1411  49  LYS C CD  
2112 C  CE  A LYS C 49  ? 0.2705 0.4084 0.2351 0.0578  -0.0249 0.1107  49  LYS C CE  
2113 C  CE  B LYS C 49  ? 0.2029 0.4018 0.2425 0.0823  0.0450  0.0830  49  LYS C CE  
2114 N  NZ  A LYS C 49  ? 0.2905 0.3567 0.2392 0.0636  -0.0268 0.1291  49  LYS C NZ  
2115 N  NZ  B LYS C 49  ? 0.1962 0.3651 0.3441 0.1026  -0.0572 0.0656  49  LYS C NZ  
2116 N  N   . SER C 50  ? 0.1009 0.3409 0.1327 0.0785  0.0060  0.0975  50  SER C N   
2117 C  CA  . SER C 50  ? 0.1351 0.3039 0.0995 0.0367  -0.0083 0.0439  50  SER C CA  
2118 C  C   . SER C 50  ? 0.1273 0.2823 0.1344 0.0600  0.0391  0.0700  50  SER C C   
2119 O  O   . SER C 50  ? 0.1787 0.2732 0.1519 0.0445  0.0488  0.0700  50  SER C O   
2120 C  CB  . SER C 50  ? 0.1548 0.2806 0.1754 0.0326  -0.0331 -0.0037 50  SER C CB  
2121 O  OG  . SER C 50  ? 0.1434 0.2871 0.1643 0.0280  -0.0378 0.0112  50  SER C OG  
2122 N  N   . ILE C 51  ? 0.0938 0.2684 0.1695 0.0614  0.0043  0.0549  51  ILE C N   
2123 C  CA  . ILE C 51  ? 0.1273 0.2135 0.1825 0.0617  0.0373  0.0601  51  ILE C CA  
2124 C  C   . ILE C 51  ? 0.1121 0.2173 0.1858 0.0529  0.0235  0.0889  51  ILE C C   
2125 O  O   . ILE C 51  ? 0.1303 0.2183 0.1531 0.0484  0.0293  0.0450  51  ILE C O   
2126 C  CB  . ILE C 51  ? 0.1417 0.2596 0.1817 0.0333  0.0755  0.0087  51  ILE C CB  
2127 C  CG1 . ILE C 51  ? 0.1844 0.2231 0.1895 0.0037  0.0437  0.0014  51  ILE C CG1 
2128 C  CG2 . ILE C 51  ? 0.1447 0.2957 0.1859 0.0177  0.0585  0.0297  51  ILE C CG2 
2129 C  CD1 . ILE C 51  ? 0.1927 0.2278 0.2544 0.0468  0.0494  0.0058  51  ILE C CD1 
2130 N  N   . GLY C 52  ? 0.1333 0.2190 0.1713 0.0522  0.0426  0.0479  52  GLY C N   
2131 C  CA  . GLY C 52  ? 0.1206 0.2082 0.1835 0.0629  0.0602  0.0572  52  GLY C CA  
2132 C  C   . GLY C 52  ? 0.1341 0.2137 0.1309 0.0879  0.0731  0.0612  52  GLY C C   
2133 O  O   . GLY C 52  ? 0.1437 0.2168 0.1790 0.0959  0.0483  0.0443  52  GLY C O   
2134 N  N   . GLY C 53  ? 0.1534 0.1964 0.1245 0.0658  0.0350  0.0114  53  GLY C N   
2135 C  CA  . GLY C 53  ? 0.1772 0.1952 0.1461 0.0519  0.0289  0.0479  53  GLY C CA  
2136 C  C   . GLY C 53  ? 0.2135 0.1826 0.1585 0.0382  0.0082  0.0456  53  GLY C C   
2137 O  O   . GLY C 53  ? 0.2876 0.1786 0.1870 0.0062  0.0205  0.0407  53  GLY C O   
2138 N  N   . ASP C 54  ? 0.1493 0.1913 0.1655 0.0593  -0.0009 0.0103  54  ASP C N   
2139 C  CA  . ASP C 54  ? 0.1806 0.1833 0.1686 0.0502  -0.0024 -0.0092 54  ASP C CA  
2140 C  C   . ASP C 54  ? 0.1795 0.1994 0.1916 0.0226  0.0267  -0.0179 54  ASP C C   
2141 O  O   . ASP C 54  ? 0.1497 0.1927 0.1915 -0.0202 0.0574  0.0098  54  ASP C O   
2142 C  CB  . ASP C 54  ? 0.2347 0.2241 0.1608 0.0177  0.0531  -0.0475 54  ASP C CB  
2143 C  CG  . ASP C 54  ? 0.2305 0.2196 0.1416 0.0676  0.0791  0.0191  54  ASP C CG  
2144 O  OD1 . ASP C 54  ? 0.3098 0.2232 0.4701 0.1208  0.0934  0.0035  54  ASP C OD1 
2145 O  OD2 . ASP C 54  ? 0.1710 0.2974 0.2444 0.0624  0.1215  0.0271  54  ASP C OD2 
2146 N  N   . ILE C 55  ? 0.2141 0.1782 0.2195 0.0110  0.0472  -0.0032 55  ILE C N   
2147 C  CA  . ILE C 55  ? 0.2290 0.1867 0.1823 -0.0228 0.0484  0.0334  55  ILE C CA  
2148 C  C   . ILE C 55  ? 0.1853 0.2179 0.1686 -0.0212 0.0765  -0.0300 55  ILE C C   
2149 O  O   . ILE C 55  ? 0.1963 0.2711 0.1666 0.0073  0.0331  0.0167  55  ILE C O   
2150 C  CB  . ILE C 55  ? 0.3280 0.2152 0.2808 -0.1026 0.0331  0.0493  55  ILE C CB  
2151 C  CG1 . ILE C 55  ? 0.4117 0.1671 0.3205 -0.0714 0.0965  0.0412  55  ILE C CG1 
2152 C  CG2 . ILE C 55  ? 0.2907 0.3070 0.3114 -0.1069 0.0535  0.0253  55  ILE C CG2 
2153 C  CD1 . ILE C 55  ? 0.6469 0.2176 0.2773 -0.1093 0.0173  0.0307  55  ILE C CD1 
2154 N  N   . PHE C 56  ? 0.1923 0.2168 0.1842 0.0080  0.0578  -0.0125 56  PHE C N   
2155 C  CA  . PHE C 56  ? 0.1840 0.2207 0.1879 0.0126  -0.0098 -0.0138 56  PHE C CA  
2156 C  C   . PHE C 56  ? 0.1892 0.2342 0.1995 0.0011  -0.0666 0.0638  56  PHE C C   
2157 O  O   . PHE C 56  ? 0.2090 0.3483 0.1997 -0.0648 -0.0042 0.0592  56  PHE C O   
2158 C  CB  . PHE C 56  ? 0.1436 0.2249 0.1840 0.0244  0.0075  -0.0078 56  PHE C CB  
2159 C  CG  . PHE C 56  ? 0.1755 0.2109 0.1991 -0.0285 0.0115  0.0008  56  PHE C CG  
2160 C  CD1 . PHE C 56  ? 0.2771 0.2175 0.1833 -0.0635 -0.0394 0.0412  56  PHE C CD1 
2161 C  CD2 . PHE C 56  ? 0.1998 0.1774 0.2728 -0.0102 -0.0240 -0.0116 56  PHE C CD2 
2162 C  CE1 . PHE C 56  ? 0.3098 0.2004 0.2080 -0.0507 -0.0729 0.0334  56  PHE C CE1 
2163 C  CE2 . PHE C 56  ? 0.2299 0.1711 0.2851 0.0089  -0.1077 0.0475  56  PHE C CE2 
2164 C  CZ  . PHE C 56  ? 0.2945 0.2040 0.2652 -0.0182 -0.0842 0.0211  56  PHE C CZ  
2165 N  N   . SER C 57  ? 0.1729 0.2973 0.1989 0.0087  -0.0425 0.0097  57  SER C N   
2166 C  CA  . SER C 57  ? 0.1809 0.3593 0.2248 -0.0155 -0.0816 -0.0367 57  SER C CA  
2167 C  C   . SER C 57  ? 0.1567 0.3715 0.3458 -0.0161 -0.0848 -0.0479 57  SER C C   
2168 O  O   . SER C 57  ? 0.1640 0.4284 0.4265 -0.0401 -0.0039 -0.0467 57  SER C O   
2169 C  CB  . SER C 57  ? 0.3178 0.4348 0.2089 -0.1230 -0.0874 -0.0172 57  SER C CB  
2170 O  OG  . SER C 57  ? 0.4728 0.4492 0.1810 0.0138  -0.0155 -0.0065 57  SER C OG  
2171 N  N   . ASN C 58  ? 0.1954 0.3630 0.2960 0.0241  -0.0940 -0.0097 58  ASN C N   
2172 C  CA  . ASN C 58  ? 0.1718 0.3869 0.2170 0.0475  -0.0249 -0.0115 58  ASN C CA  
2173 C  C   . ASN C 58  ? 0.2020 0.3389 0.2130 0.0387  -0.0160 0.0064  58  ASN C C   
2174 O  O   . ASN C 58  ? 0.2293 0.3246 0.2209 -0.0062 0.0754  0.0119  58  ASN C O   
2175 C  CB  . ASN C 58  ? 0.2407 0.4227 0.2122 -0.0133 0.0044  0.0175  58  ASN C CB  
2176 C  CG  . ASN C 58  ? 0.2156 0.4343 0.1643 -0.0188 -0.0151 0.0220  58  ASN C CG  
2177 O  OD1 . ASN C 58  ? 0.1889 0.4318 0.1443 0.0096  0.0405  -0.0512 58  ASN C OD1 
2178 N  ND2 . ASN C 58  ? 0.2339 0.4595 0.1766 -0.0750 0.0186  -0.0371 58  ASN C ND2 
2179 N  N   . ARG C 59  ? 0.2415 0.3222 0.2157 0.0204  -0.0247 -0.0412 59  ARG C N   
2180 C  CA  . ARG C 59  ? 0.2611 0.3221 0.2090 0.0111  -0.0182 -0.0147 59  ARG C CA  
2181 C  C   . ARG C 59  ? 0.2440 0.3190 0.2149 -0.0327 0.0218  -0.0349 59  ARG C C   
2182 O  O   . ARG C 59  ? 0.2998 0.2833 0.2787 -0.0990 0.0462  -0.0309 59  ARG C O   
2183 C  CB  . ARG C 59  ? 0.3193 0.3117 0.2152 0.0599  -0.0614 -0.0090 59  ARG C CB  
2184 C  CG  . ARG C 59  ? 0.4212 0.2620 0.3508 0.0488  -0.0376 -0.0195 59  ARG C CG  
2185 C  CD  . ARG C 59  ? 0.3757 0.2689 0.3843 0.0765  -0.0162 -0.0246 59  ARG C CD  
2186 N  NE  . ARG C 59  ? 0.4059 0.2632 0.4910 0.1038  0.0387  -0.0864 59  ARG C NE  
2187 C  CZ  . ARG C 59  ? 0.4626 0.2327 0.4812 0.0909  0.0388  -0.0901 59  ARG C CZ  
2188 N  NH1 . ARG C 59  ? 0.6428 0.2860 0.4705 -0.0661 0.0831  -0.1031 59  ARG C NH1 
2189 N  NH2 . ARG C 59  ? 0.4585 0.2307 0.6228 0.0990  0.0224  -0.1125 59  ARG C NH2 
2190 N  N   . GLU C 60  ? 0.1551 0.3178 0.1646 -0.0141 -0.0517 0.0188  60  GLU C N   
2191 C  CA  . GLU C 60  ? 0.1366 0.3232 0.1742 -0.0226 -0.0229 0.0248  60  GLU C CA  
2192 C  C   . GLU C 60  ? 0.1332 0.3346 0.1713 0.0158  -0.0094 -0.0006 60  GLU C C   
2193 O  O   . GLU C 60  ? 0.1200 0.3470 0.1897 0.0469  0.0000  0.0212  60  GLU C O   
2194 C  CB  . GLU C 60  ? 0.1376 0.3074 0.1754 0.0058  0.0563  -0.0142 60  GLU C CB  
2195 C  CG  . GLU C 60  ? 0.1301 0.2574 0.1780 0.0000  0.0347  -0.0028 60  GLU C CG  
2196 C  CD  . GLU C 60  ? 0.1451 0.2560 0.2054 -0.0149 0.0205  -0.0058 60  GLU C CD  
2197 O  OE1 . GLU C 60  ? 0.1380 0.2658 0.2511 -0.0067 0.0034  -0.0022 60  GLU C OE1 
2198 O  OE2 . GLU C 60  ? 0.1756 0.2249 0.2375 -0.0240 0.0056  -0.0198 60  GLU C OE2 
2199 N  N   . GLY C 61  ? 0.1359 0.3387 0.1762 0.0085  0.0122  -0.0333 61  GLY C N   
2200 C  CA  . GLY C 61  ? 0.1418 0.3939 0.1667 -0.0610 0.0310  -0.0428 61  GLY C CA  
2201 C  C   . GLY C 61  ? 0.1438 0.3829 0.1515 -0.0274 0.0193  -0.0419 61  GLY C C   
2202 O  O   . GLY C 61  ? 0.1235 0.4155 0.1500 -0.0213 0.0276  -0.0004 61  GLY C O   
2203 N  N   . LYS C 62  ? 0.1183 0.3595 0.1540 -0.0139 -0.0307 -0.0217 62  LYS C N   
2204 C  CA  . LYS C 62  ? 0.1259 0.3656 0.1486 -0.0021 -0.0041 -0.0201 62  LYS C CA  
2205 C  C   . LYS C 62  ? 0.1613 0.4002 0.1387 -0.0121 0.0444  -0.0701 62  LYS C C   
2206 O  O   . LYS C 62  ? 0.2691 0.4062 0.1442 0.0388  -0.0115 -0.0478 62  LYS C O   
2207 C  CB  . LYS C 62  ? 0.1381 0.3184 0.1390 0.0012  0.0201  -0.0073 62  LYS C CB  
2208 C  CG  . LYS C 62  ? 0.1268 0.3309 0.1385 0.0182  0.0319  0.0030  62  LYS C CG  
2209 C  CD  . LYS C 62  ? 0.1560 0.3768 0.1301 -0.0210 0.0214  -0.0240 62  LYS C CD  
2210 C  CE  . LYS C 62  ? 0.1088 0.3678 0.1316 0.0078  -0.0215 -0.0099 62  LYS C CE  
2211 N  NZ  . LYS C 62  ? 0.1367 0.2371 0.1195 0.0276  -0.0290 -0.0634 62  LYS C NZ  
2212 N  N   . LEU C 63  ? 0.1145 0.4105 0.1381 0.0109  -0.0168 -0.0193 63  LEU C N   
2213 C  CA  . LEU C 63  ? 0.0544 0.4563 0.1394 0.0281  -0.0290 -0.0082 63  LEU C CA  
2214 C  C   . LEU C 63  ? 0.0706 0.4844 0.1416 0.0003  0.0444  -0.0446 63  LEU C C   
2215 O  O   . LEU C 63  ? 0.1627 0.4919 0.1487 -0.0603 0.0222  -0.0777 63  LEU C O   
2216 C  CB  . LEU C 63  ? 0.1075 0.4152 0.1324 -0.0258 -0.0034 0.0298  63  LEU C CB  
2217 C  CG  . LEU C 63  ? 0.1065 0.3996 0.1891 -0.0297 0.0157  0.0485  63  LEU C CG  
2218 C  CD1 . LEU C 63  ? 0.0893 0.4158 0.3073 0.0155  0.0194  0.0923  63  LEU C CD1 
2219 C  CD2 . LEU C 63  ? 0.2505 0.3915 0.2422 -0.1127 -0.0846 0.0303  63  LEU C CD2 
2220 N  N   . PRO C 64  ? 0.1117 0.4765 0.1399 0.0092  0.0457  -0.0136 64  PRO C N   
2221 C  CA  . PRO C 64  ? 0.1832 0.4695 0.1228 -0.0343 0.0710  0.0236  64  PRO C CA  
2222 C  C   . PRO C 64  ? 0.1613 0.4712 0.1934 -0.0251 0.0810  0.0170  64  PRO C C   
2223 O  O   . PRO C 64  ? 0.1386 0.4883 0.2280 -0.0147 0.0120  0.0148  64  PRO C O   
2224 C  CB  . PRO C 64  ? 0.2418 0.4806 0.1281 -0.0704 0.0415  0.0394  64  PRO C CB  
2225 C  CG  . PRO C 64  ? 0.2423 0.4636 0.1425 -0.0639 0.0464  0.0071  64  PRO C CG  
2226 C  CD  . PRO C 64  ? 0.1521 0.4670 0.1467 -0.0081 0.0414  -0.0317 64  PRO C CD  
2227 N  N   . GLY C 65  ? 0.1366 0.4476 0.2181 0.0033  0.0375  0.0050  65  GLY C N   
2228 C  CA  . GLY C 65  ? 0.1522 0.4473 0.2414 0.0127  0.0278  -0.0054 65  GLY C CA  
2229 C  C   . GLY C 65  ? 0.1340 0.4160 0.2513 0.0297  0.0209  0.0237  65  GLY C C   
2230 O  O   . GLY C 65  ? 0.1900 0.4085 0.2126 0.0567  0.0005  0.0210  65  GLY C O   
2231 N  N   . LYS C 66  ? 0.1513 0.4080 0.2741 0.0157  0.0212  0.0734  66  LYS C N   
2232 C  CA  . LYS C 66  ? 0.1531 0.3969 0.2814 -0.0047 -0.0319 0.1017  66  LYS C CA  
2233 C  C   . LYS C 66  ? 0.2037 0.3967 0.3480 -0.0206 0.0606  0.0652  66  LYS C C   
2234 O  O   . LYS C 66  ? 0.2412 0.3705 0.2596 -0.0026 -0.0433 0.0410  66  LYS C O   
2235 C  CB  . LYS C 66  ? 0.2035 0.4248 0.2783 -0.0182 0.0244  0.0759  66  LYS C CB  
2236 C  CG  . LYS C 66  ? 0.3011 0.4641 0.2759 -0.0535 0.0466  0.0463  66  LYS C CG  
2237 C  CD  . LYS C 66  ? 0.4757 0.5661 0.2720 -0.1729 0.0268  0.0188  66  LYS C CD  
2238 C  CE  . LYS C 66  ? 0.4615 0.6092 0.2735 -0.1817 -0.0169 -0.0084 66  LYS C CE  
2239 N  NZ  . LYS C 66  ? 0.5608 0.5880 0.2715 -0.1112 0.0836  -0.1009 66  LYS C NZ  
2240 N  N   . SER C 67  ? 0.2483 0.3964 0.4243 -0.0717 0.1366  0.1285  67  SER C N   
2241 C  CA  . SER C 67  ? 0.2820 0.3930 0.5218 -0.0267 0.1038  0.1083  67  SER C CA  
2242 C  C   . SER C 67  ? 0.2887 0.3821 0.5158 -0.0238 0.1364  0.0618  67  SER C C   
2243 O  O   . SER C 67  ? 0.2914 0.3917 0.5092 0.0090  0.0980  0.0881  67  SER C O   
2244 C  CB  . SER C 67  ? 0.3543 0.3815 0.5558 -0.1044 0.1082  0.1153  67  SER C CB  
2245 O  OG  . SER C 67  ? 0.3299 0.4330 0.5193 -0.0864 0.1306  0.1917  67  SER C OG  
2246 N  N   . GLY C 68  ? 0.3129 0.3611 0.5161 -0.0619 0.1189  0.1229  68  GLY C N   
2247 C  CA  . GLY C 68  ? 0.3044 0.3653 0.5213 -0.0345 0.1026  0.1457  68  GLY C CA  
2248 C  C   . GLY C 68  ? 0.2754 0.3968 0.4870 -0.0341 0.0289  0.1574  68  GLY C C   
2249 O  O   . GLY C 68  ? 0.2589 0.3741 0.6520 0.0205  0.0396  0.2085  68  GLY C O   
2250 N  N   . ARG C 69  ? 0.2137 0.4057 0.4195 -0.0632 0.0414  0.1000  69  ARG C N   
2251 C  CA  . ARG C 69  ? 0.1753 0.4127 0.3451 -0.0389 0.0238  0.1235  69  ARG C CA  
2252 C  C   . ARG C 69  ? 0.2125 0.3945 0.3343 -0.0218 0.0007  0.1090  69  ARG C C   
2253 O  O   . ARG C 69  ? 0.2829 0.4825 0.3428 -0.1900 0.0409  0.0934  69  ARG C O   
2254 C  CB  . ARG C 69  ? 0.1473 0.4110 0.3422 -0.0672 0.0346  0.1118  69  ARG C CB  
2255 C  CG  . ARG C 69  ? 0.1496 0.4121 0.3519 -0.0579 0.0114  0.1501  69  ARG C CG  
2256 C  CD  . ARG C 69  ? 0.1870 0.4107 0.3252 -0.0162 0.0063  0.1315  69  ARG C CD  
2257 N  NE  . ARG C 69  ? 0.1786 0.4534 0.3257 0.0293  -0.0054 0.1217  69  ARG C NE  
2258 C  CZ  . ARG C 69  ? 0.1914 0.4611 0.2871 0.0646  -0.0824 0.1480  69  ARG C CZ  
2259 N  NH1 . ARG C 69  ? 0.3228 0.3847 0.2905 0.0397  0.0742  0.1051  69  ARG C NH1 
2260 N  NH2 . ARG C 69  ? 0.2987 0.4505 0.2812 -0.0038 0.0909  0.0438  69  ARG C NH2 
2261 N  N   . THR C 70  ? 0.3002 0.3675 0.2461 -0.1452 0.0005  0.1156  70  THR C N   
2262 C  CA  . THR C 70  ? 0.3195 0.2840 0.2347 -0.1015 0.1405  0.0226  70  THR C CA  
2263 C  C   . THR C 70  ? 0.2559 0.2715 0.1917 -0.0665 0.0679  0.0288  70  THR C C   
2264 O  O   . THR C 70  ? 0.4153 0.2993 0.1867 -0.1556 0.1144  0.0205  70  THR C O   
2265 C  CB  . THR C 70  ? 0.3705 0.2713 0.3367 -0.0294 0.2391  -0.0129 70  THR C CB  
2266 O  OG1 . THR C 70  ? 0.4241 0.2883 0.4389 -0.0518 0.0507  0.0469  70  THR C OG1 
2267 C  CG2 . THR C 70  ? 0.2975 0.2784 0.3642 0.0597  -0.0082 0.0463  70  THR C CG2 
2268 N  N   . TRP C 71  ? 0.1154 0.2977 0.1886 -0.0427 0.0194  0.0483  71  TRP C N   
2269 C  CA  . TRP C 71  ? 0.1001 0.3100 0.1463 -0.0335 -0.0180 0.0492  71  TRP C CA  
2270 C  C   . TRP C 71  ? 0.1435 0.2700 0.1135 -0.0501 0.0030  0.0270  71  TRP C C   
2271 O  O   . TRP C 71  ? 0.1829 0.2528 0.1345 -0.0625 -0.0066 0.0054  71  TRP C O   
2272 C  CB  . TRP C 71  ? 0.1044 0.3149 0.1375 -0.0087 0.0117  0.0070  71  TRP C CB  
2273 C  CG  . TRP C 71  ? 0.0936 0.3229 0.1418 -0.0042 0.0462  0.0012  71  TRP C CG  
2274 C  CD1 . TRP C 71  ? 0.1021 0.3274 0.1600 -0.0164 0.0581  -0.0074 71  TRP C CD1 
2275 C  CD2 . TRP C 71  ? 0.1094 0.2975 0.1896 -0.0183 -0.0147 0.0509  71  TRP C CD2 
2276 N  NE1 . TRP C 71  ? 0.0987 0.3257 0.1821 -0.0161 0.0475  0.0239  71  TRP C NE1 
2277 C  CE2 . TRP C 71  ? 0.1097 0.2979 0.2028 -0.0037 0.0254  0.0501  71  TRP C CE2 
2278 C  CE3 . TRP C 71  ? 0.1260 0.3324 0.1535 -0.0369 0.0250  0.0403  71  TRP C CE3 
2279 C  CZ2 . TRP C 71  ? 0.0918 0.3087 0.1994 0.0075  0.0600  -0.0103 71  TRP C CZ2 
2280 C  CZ3 . TRP C 71  ? 0.1228 0.3287 0.1517 -0.0319 -0.0180 0.0351  71  TRP C CZ3 
2281 C  CH2 . TRP C 71  ? 0.1211 0.3348 0.1792 -0.0327 0.0055  0.0128  71  TRP C CH2 
2282 N  N   . ARG C 72  ? 0.0984 0.2375 0.1324 0.0030  0.0358  -0.0084 72  ARG C N   
2283 C  CA  . ARG C 72  ? 0.1048 0.1929 0.1705 0.0125  0.0256  0.0035  72  ARG C CA  
2284 C  C   . ARG C 72  ? 0.1052 0.1880 0.1435 0.0125  0.0264  -0.0014 72  ARG C C   
2285 O  O   . ARG C 72  ? 0.1442 0.1923 0.1025 0.0067  0.0489  -0.0139 72  ARG C O   
2286 C  CB  . ARG C 72  ? 0.1309 0.1823 0.1738 0.0251  -0.0036 0.0243  72  ARG C CB  
2287 C  CG  . ARG C 72  ? 0.1699 0.1856 0.2365 0.0181  -0.0222 0.0275  72  ARG C CG  
2288 C  CD  . ARG C 72  ? 0.2437 0.1607 0.2307 0.0009  0.0194  0.0363  72  ARG C CD  
2289 N  NE  . ARG C 72  ? 0.3874 0.1533 0.3184 -0.0148 -0.0288 0.0495  72  ARG C NE  
2290 C  CZ  . ARG C 72  ? 0.4377 0.1571 0.3061 -0.0240 0.0316  0.0650  72  ARG C CZ  
2291 N  NH1 . ARG C 72  ? 0.4776 0.2262 0.2501 0.0274  0.1110  0.0308  72  ARG C NH1 
2292 N  NH2 . ARG C 72  ? 0.5367 0.1594 0.4094 -0.0824 -0.0643 0.1001  72  ARG C NH2 
2293 N  N   . GLU C 73  ? 0.1199 0.1531 0.1557 0.0202  0.0432  0.0299  73  GLU C N   
2294 C  CA  . GLU C 73  ? 0.1273 0.1520 0.1556 0.0073  0.0492  -0.0044 73  GLU C CA  
2295 C  C   . GLU C 73  ? 0.1255 0.1519 0.1564 0.0152  0.0680  -0.0055 73  GLU C C   
2296 O  O   . GLU C 73  ? 0.1367 0.1493 0.1465 0.0281  0.0277  0.0146  73  GLU C O   
2297 C  CB  . GLU C 73  ? 0.1281 0.1483 0.1590 0.0267  0.0204  -0.0222 73  GLU C CB  
2298 C  CG  . GLU C 73  ? 0.1507 0.1463 0.1552 0.0030  -0.0267 0.0121  73  GLU C CG  
2299 C  CD  . GLU C 73  ? 0.1364 0.1835 0.1535 0.0367  -0.0290 -0.0053 73  GLU C CD  
2300 O  OE1 . GLU C 73  ? 0.2141 0.1786 0.1228 0.0145  -0.0136 0.0515  73  GLU C OE1 
2301 O  OE2 . GLU C 73  ? 0.2865 0.3249 0.1535 -0.1173 -0.0408 0.0117  73  GLU C OE2 
2302 N  N   . ALA C 74  ? 0.1013 0.1473 0.1192 0.0250  0.0275  -0.0080 74  ALA C N   
2303 C  CA  . ALA C 74  ? 0.1023 0.1541 0.0960 0.0268  0.0241  0.0136  74  ALA C CA  
2304 C  C   . ALA C 74  ? 0.0949 0.1476 0.1182 0.0280  0.0070  0.0379  74  ALA C C   
2305 O  O   . ALA C 74  ? 0.1147 0.1482 0.1210 0.0428  0.0379  0.0137  74  ALA C O   
2306 C  CB  . ALA C 74  ? 0.1118 0.2220 0.0856 -0.0035 0.0216  0.0384  74  ALA C CB  
2307 N  N   . ASP C 75  ? 0.0906 0.1590 0.1154 0.0303  0.0193  0.0290  75  ASP C N   
2308 C  CA  . ASP C 75  ? 0.0790 0.1660 0.1073 0.0328  0.0067  0.0376  75  ASP C CA  
2309 C  C   . ASP C 75  ? 0.1429 0.1821 0.0921 0.0013  0.0142  0.0167  75  ASP C C   
2310 O  O   . ASP C 75  ? 0.1734 0.1832 0.0758 0.0114  -0.0354 0.0255  75  ASP C O   
2311 C  CB  . ASP C 75  ? 0.0729 0.2092 0.0975 0.0283  0.0278  0.0149  75  ASP C CB  
2312 C  CG  . ASP C 75  ? 0.1455 0.1804 0.1006 -0.0017 -0.0035 -0.0015 75  ASP C CG  
2313 O  OD1 . ASP C 75  ? 0.1224 0.2020 0.1051 0.0060  0.0167  0.0199  75  ASP C OD1 
2314 O  OD2 . ASP C 75  ? 0.1200 0.2051 0.1014 0.0153  0.0024  0.0474  75  ASP C OD2 
2315 N  N   . ILE C 76  ? 0.1197 0.1802 0.0915 -0.0073 -0.0045 0.0055  76  ILE C N   
2316 C  CA  . ILE C 76  ? 0.0880 0.1875 0.1036 0.0066  0.0189  0.0150  76  ILE C CA  
2317 C  C   . ILE C 76  ? 0.1132 0.2106 0.1147 -0.0247 0.0010  0.0305  76  ILE C C   
2318 O  O   . ILE C 76  ? 0.1135 0.2215 0.1131 -0.0241 -0.0334 0.0485  76  ILE C O   
2319 C  CB  . ILE C 76  ? 0.1088 0.1876 0.0881 0.0164  0.0121  0.0136  76  ILE C CB  
2320 C  CG1 . ILE C 76  ? 0.1085 0.2176 0.0754 -0.0093 0.0097  0.0515  76  ILE C CG1 
2321 C  CG2 . ILE C 76  ? 0.1661 0.1775 0.1285 0.0041  -0.0163 -0.0322 76  ILE C CG2 
2322 C  CD1 . ILE C 76  ? 0.1434 0.2098 0.0760 -0.0231 0.0034  0.0257  76  ILE C CD1 
2323 N  N   . ASN C 77  ? 0.1240 0.2210 0.1261 -0.0353 -0.0121 0.0308  77  ASN C N   
2324 C  CA  . ASN C 77  ? 0.1480 0.2278 0.1664 -0.0519 0.0063  -0.0071 77  ASN C CA  
2325 C  C   . ASN C 77  ? 0.1170 0.2678 0.1498 -0.0472 -0.0030 0.0429  77  ASN C C   
2326 O  O   . ASN C 77  ? 0.2221 0.2725 0.1571 -0.0863 0.0475  0.0329  77  ASN C O   
2327 C  CB  . ASN C 77  ? 0.2427 0.2077 0.1874 -0.0291 0.0109  -0.0143 77  ASN C CB  
2328 C  CG  . ASN C 77  ? 0.2295 0.2080 0.1959 -0.0025 -0.0575 -0.0022 77  ASN C CG  
2329 O  OD1 . ASN C 77  ? 0.2797 0.2253 0.1845 -0.0381 -0.0179 -0.0300 77  ASN C OD1 
2330 N  ND2 . ASN C 77  ? 0.1966 0.2459 0.2609 0.0323  -0.0152 -0.0215 77  ASN C ND2 
2331 N  N   . TYR C 78  ? 0.1249 0.2673 0.1087 -0.0186 0.0085  0.0212  78  TYR C N   
2332 C  CA  . TYR C 78  ? 0.1222 0.2762 0.1219 -0.0177 -0.0176 -0.0074 78  TYR C CA  
2333 C  C   . TYR C 78  ? 0.1072 0.2971 0.1578 -0.0144 -0.0426 0.0183  78  TYR C C   
2334 O  O   . TYR C 78  ? 0.1106 0.3688 0.1446 -0.0332 -0.0271 0.0366  78  TYR C O   
2335 C  CB  . TYR C 78  ? 0.1286 0.2772 0.0992 -0.0252 -0.0129 -0.0019 78  TYR C CB  
2336 C  CG  . TYR C 78  ? 0.0895 0.2959 0.1049 0.0082  0.0236  0.0083  78  TYR C CG  
2337 C  CD1 . TYR C 78  ? 0.1370 0.2826 0.1009 0.0267  -0.0145 0.0232  78  TYR C CD1 
2338 C  CD2 . TYR C 78  ? 0.1096 0.2877 0.1244 0.0105  0.0549  -0.0152 78  TYR C CD2 
2339 C  CE1 . TYR C 78  ? 0.1808 0.2531 0.1027 0.0259  0.0243  0.0119  78  TYR C CE1 
2340 C  CE2 . TYR C 78  ? 0.1366 0.2566 0.1258 0.0324  0.0049  -0.0105 78  TYR C CE2 
2341 C  CZ  . TYR C 78  ? 0.1529 0.2719 0.1223 0.0391  0.0103  0.0041  78  TYR C CZ  
2342 O  OH  . TYR C 78  ? 0.1474 0.2918 0.1253 0.0469  0.0079  0.0520  78  TYR C OH  
2343 N  N   . THR C 79  ? 0.1222 0.3553 0.1582 -0.0485 0.0155  0.0131  79  THR C N   
2344 C  CA  . THR C 79  ? 0.1144 0.4269 0.1770 -0.0698 -0.0200 0.0560  79  THR C CA  
2345 C  C   . THR C 79  ? 0.0652 0.4558 0.1743 -0.0358 -0.0020 0.0508  79  THR C C   
2346 O  O   . THR C 79  ? 0.1367 0.4470 0.1457 0.0416  -0.0078 0.0058  79  THR C O   
2347 C  CB  . THR C 79  ? 0.1827 0.4495 0.2342 -0.1319 -0.0100 0.0399  79  THR C CB  
2348 O  OG1 . THR C 79  ? 0.4041 0.4183 0.2536 -0.1389 0.0548  0.0461  79  THR C OG1 
2349 C  CG2 . THR C 79  ? 0.1942 0.4048 0.2505 -0.1342 0.0494  -0.0499 79  THR C CG2 
2350 N  N   . SER C 80  ? 0.1509 0.3763 0.1768 -0.0483 -0.0187 0.0366  80  SER C N   
2351 C  CA  . SER C 80  ? 0.1164 0.3753 0.1733 -0.0083 -0.0150 0.0485  80  SER C CA  
2352 C  C   . SER C 80  ? 0.1413 0.3454 0.1728 -0.0194 -0.0012 0.0618  80  SER C C   
2353 O  O   . SER C 80  ? 0.1683 0.3398 0.1543 -0.0065 0.0316  -0.0204 80  SER C O   
2354 C  CB  . SER C 80  ? 0.1307 0.3647 0.2129 -0.0198 -0.0615 0.0514  80  SER C CB  
2355 O  OG  . SER C 80  ? 0.2934 0.3712 0.2839 -0.1066 0.0244  -0.0175 80  SER C OG  
2356 N  N   . GLY C 81  ? 0.1158 0.3395 0.1737 -0.0297 0.0032  0.0344  81  GLY C N   
2357 C  CA  . GLY C 81  ? 0.1015 0.3003 0.1760 0.0027  0.0106  0.0163  81  GLY C CA  
2358 C  C   . GLY C 81  ? 0.1188 0.2491 0.1322 0.0048  0.0395  0.0217  81  GLY C C   
2359 O  O   . GLY C 81  ? 0.1409 0.2643 0.1115 0.0099  0.0172  0.0480  81  GLY C O   
2360 N  N   . PHE C 82  ? 0.1200 0.2544 0.1117 0.0130  0.0350  0.0423  82  PHE C N   
2361 C  CA  . PHE C 82  ? 0.1019 0.2352 0.1107 0.0372  0.0328  0.0524  82  PHE C CA  
2362 C  C   . PHE C 82  ? 0.1214 0.2192 0.1142 0.0214  0.0179  -0.0018 82  PHE C C   
2363 O  O   . PHE C 82  ? 0.1554 0.2427 0.1045 -0.0049 0.0426  -0.0038 82  PHE C O   
2364 C  CB  . PHE C 82  ? 0.1089 0.2330 0.1204 0.0470  0.0012  0.0583  82  PHE C CB  
2365 C  CG  . PHE C 82  ? 0.1157 0.2457 0.1121 0.0216  0.0013  0.0459  82  PHE C CG  
2366 C  CD1 . PHE C 82  ? 0.1488 0.2467 0.1088 0.0155  -0.0219 0.0617  82  PHE C CD1 
2367 C  CD2 . PHE C 82  ? 0.2079 0.3005 0.1097 -0.0646 -0.0046 0.0216  82  PHE C CD2 
2368 C  CE1 . PHE C 82  ? 0.1578 0.2703 0.1005 0.0228  -0.0268 0.0262  82  PHE C CE1 
2369 C  CE2 . PHE C 82  ? 0.1818 0.3438 0.1103 -0.0562 0.0068  0.0535  82  PHE C CE2 
2370 C  CZ  . PHE C 82  ? 0.1742 0.3141 0.0967 -0.0012 -0.0149 0.0404  82  PHE C CZ  
2371 N  N   . ARG C 83  ? 0.1375 0.2219 0.0960 0.0156  0.0165  -0.0168 83  ARG C N   
2372 C  CA  . ARG C 83  ? 0.1559 0.2138 0.0904 0.0049  -0.0305 0.0024  83  ARG C CA  
2373 C  C   . ARG C 83  ? 0.1457 0.2074 0.1128 -0.0155 -0.0338 0.0236  83  ARG C C   
2374 O  O   . ARG C 83  ? 0.1341 0.2323 0.1135 0.0111  -0.0008 -0.0108 83  ARG C O   
2375 C  CB  . ARG C 83  ? 0.1544 0.2099 0.0711 0.0119  -0.0045 0.0103  83  ARG C CB  
2376 C  CG  . ARG C 83  ? 0.1523 0.2089 0.1297 0.0408  0.0218  0.0397  83  ARG C CG  
2377 C  CD  . ARG C 83  ? 0.1732 0.2155 0.1128 0.0207  0.0477  0.0023  83  ARG C CD  
2378 N  NE  . ARG C 83  ? 0.1702 0.1920 0.1163 0.0264  -0.0180 -0.0011 83  ARG C NE  
2379 C  CZ  . ARG C 83  ? 0.1811 0.1922 0.1166 0.0191  0.0104  -0.0277 83  ARG C CZ  
2380 N  NH1 . ARG C 83  ? 0.2186 0.1894 0.1205 -0.0002 0.0229  -0.0550 83  ARG C NH1 
2381 N  NH2 . ARG C 83  ? 0.1638 0.2580 0.1119 0.0167  -0.0199 -0.0369 83  ARG C NH2 
2382 N  N   . ASN C 84  ? 0.1490 0.2040 0.1120 -0.0016 -0.0261 0.0011  84  ASN C N   
2383 C  CA  . ASN C 84  ? 0.1432 0.2046 0.1065 -0.0038 0.0584  0.0064  84  ASN C CA  
2384 C  C   . ASN C 84  ? 0.1470 0.2007 0.0944 -0.0084 0.0386  0.0063  84  ASN C C   
2385 O  O   . ASN C 84  ? 0.1552 0.1988 0.1217 -0.0048 -0.0132 0.0252  84  ASN C O   
2386 C  CB  . ASN C 84  ? 0.1572 0.1982 0.1168 -0.0146 0.0165  0.0293  84  ASN C CB  
2387 C  CG  . ASN C 84  ? 0.1314 0.1721 0.1124 -0.0008 0.0071  0.0016  84  ASN C CG  
2388 O  OD1 . ASN C 84  ? 0.1298 0.1910 0.1368 -0.0173 -0.0097 -0.0098 84  ASN C OD1 
2389 N  ND2 . ASN C 84  ? 0.1925 0.2724 0.1198 -0.0860 -0.0140 -0.0026 84  ASN C ND2 
2390 N  N   . SER C 85  ? 0.1373 0.2058 0.0902 0.0029  0.0163  0.0121  85  SER C N   
2391 C  CA  . SER C 85  ? 0.0926 0.2572 0.1107 0.0378  -0.0206 0.0427  85  SER C CA  
2392 C  C   . SER C 85  ? 0.1142 0.2270 0.1165 0.0087  0.0017  0.0068  85  SER C C   
2393 O  O   . SER C 85  ? 0.1242 0.2009 0.1194 0.0123  -0.0309 0.0107  85  SER C O   
2394 C  CB  . SER C 85  ? 0.0852 0.2644 0.1309 0.0498  -0.0131 0.0342  85  SER C CB  
2395 O  OG  . SER C 85  ? 0.2894 0.2526 0.3069 -0.0304 -0.0333 0.0597  85  SER C OG  
2396 N  N   . ASP C 86  ? 0.1188 0.1853 0.1132 0.0319  0.0303  -0.0118 86  ASP C N   
2397 C  CA  . ASP C 86  ? 0.0978 0.1748 0.1133 0.0267  0.0243  -0.0144 86  ASP C CA  
2398 C  C   . ASP C 86  ? 0.1113 0.1832 0.1018 0.0151  0.0172  0.0029  86  ASP C C   
2399 O  O   . ASP C 86  ? 0.1190 0.1691 0.0891 0.0150  -0.0175 -0.0022 86  ASP C O   
2400 C  CB  . ASP C 86  ? 0.1251 0.1853 0.1223 0.0085  -0.0241 0.0349  86  ASP C CB  
2401 C  CG  . ASP C 86  ? 0.2686 0.1816 0.1429 -0.0331 -0.0433 0.0283  86  ASP C CG  
2402 O  OD1 . ASP C 86  ? 0.2681 0.1411 0.2098 -0.0145 -0.0476 0.0162  86  ASP C OD1 
2403 O  OD2 . ASP C 86  ? 0.2399 0.2004 0.2735 -0.0363 -0.0520 0.0173  86  ASP C OD2 
2404 N  N   . ARG C 87  ? 0.1055 0.1771 0.0727 0.0338  -0.0068 0.0218  87  ARG C N   
2405 C  CA  . ARG C 87  ? 0.1144 0.1835 0.0738 0.0261  -0.0243 -0.0005 87  ARG C CA  
2406 C  C   . ARG C 87  ? 0.1001 0.1666 0.0834 0.0046  0.0242  0.0186  87  ARG C C   
2407 O  O   . ARG C 87  ? 0.1138 0.1729 0.1146 0.0420  0.0050  0.0045  87  ARG C O   
2408 C  CB  . ARG C 87  ? 0.0791 0.1811 0.0810 0.0492  -0.0012 -0.0210 87  ARG C CB  
2409 C  CG  . ARG C 87  ? 0.1296 0.1872 0.0765 0.0410  0.0202  -0.0127 87  ARG C CG  
2410 C  CD  . ARG C 87  ? 0.1488 0.1638 0.0744 0.0247  0.0014  0.0020  87  ARG C CD  
2411 N  NE  . ARG C 87  ? 0.1348 0.1997 0.0786 0.0067  0.0091  -0.0114 87  ARG C NE  
2412 C  CZ  . ARG C 87  ? 0.1473 0.2071 0.0715 0.0095  0.0098  0.0257  87  ARG C CZ  
2413 N  NH1 . ARG C 87  ? 0.1606 0.2112 0.0820 -0.0061 0.0039  0.0070  87  ARG C NH1 
2414 N  NH2 . ARG C 87  ? 0.2107 0.2351 0.0718 0.0161  0.0356  0.0210  87  ARG C NH2 
2415 N  N   . ILE C 88  ? 0.1258 0.1694 0.0711 0.0311  0.0270  0.0314  88  ILE C N   
2416 C  CA  . ILE C 88  ? 0.1575 0.2063 0.0705 -0.0067 -0.0224 0.0248  88  ILE C CA  
2417 C  C   . ILE C 88  ? 0.0880 0.1806 0.0787 0.0630  0.0671  -0.0154 88  ILE C C   
2418 O  O   . ILE C 88  ? 0.0871 0.1774 0.1167 0.0482  0.0395  -0.0243 88  ILE C O   
2419 C  CB  . ILE C 88  ? 0.1292 0.2484 0.0716 0.0280  0.0115  0.0055  88  ILE C CB  
2420 C  CG1 . ILE C 88  ? 0.2438 0.2647 0.0675 0.0621  0.0024  -0.0087 88  ILE C CG1 
2421 C  CG2 . ILE C 88  ? 0.1155 0.2578 0.1853 0.0276  0.0225  0.0431  88  ILE C CG2 
2422 C  CD1 . ILE C 88  ? 0.2245 0.3639 0.0623 0.0772  -0.0882 -0.0659 88  ILE C CD1 
2423 N  N   . LEU C 89  ? 0.1102 0.1671 0.1284 0.0369  0.0605  0.0000  89  LEU C N   
2424 C  CA  . LEU C 89  ? 0.1201 0.1697 0.1251 0.0336  0.0604  -0.0024 89  LEU C CA  
2425 C  C   . LEU C 89  ? 0.0837 0.1938 0.1245 0.0374  0.0417  -0.0455 89  LEU C C   
2426 O  O   . LEU C 89  ? 0.1399 0.1851 0.1293 0.0216  0.0518  0.0033  89  LEU C O   
2427 C  CB  . LEU C 89  ? 0.1001 0.2290 0.1181 0.0288  0.0060  0.0367  89  LEU C CB  
2428 C  CG  . LEU C 89  ? 0.1377 0.2741 0.1187 0.0054  0.0059  -0.0052 89  LEU C CG  
2429 C  CD1 . LEU C 89  ? 0.2537 0.2704 0.1006 0.0845  0.0021  -0.0416 89  LEU C CD1 
2430 C  CD2 . LEU C 89  ? 0.1203 0.4027 0.1194 -0.0147 0.0362  0.0575  89  LEU C CD2 
2431 N  N   . TYR C 90  ? 0.1795 0.1839 0.0986 0.0069  0.0490  0.0037  90  TYR C N   
2432 C  CA  . TYR C 90  ? 0.1140 0.2160 0.0997 0.0170  0.0416  0.0428  90  TYR C CA  
2433 C  C   . TYR C 90  ? 0.1217 0.2243 0.1163 0.0034  0.0282  0.0742  90  TYR C C   
2434 O  O   . TYR C 90  ? 0.1764 0.2132 0.1264 -0.0047 0.0328  0.0124  90  TYR C O   
2435 C  CB  . TYR C 90  ? 0.1138 0.2257 0.1092 0.0083  0.0196  0.0478  90  TYR C CB  
2436 C  CG  . TYR C 90  ? 0.1139 0.2176 0.1386 -0.0054 0.0131  0.0381  90  TYR C CG  
2437 C  CD1 . TYR C 90  ? 0.1140 0.2315 0.1338 0.0053  0.0000  0.0198  90  TYR C CD1 
2438 C  CD2 . TYR C 90  ? 0.1809 0.2173 0.1337 0.0110  0.0206  0.0125  90  TYR C CD2 
2439 C  CE1 . TYR C 90  ? 0.1154 0.2346 0.1544 0.0018  0.0206  0.0073  90  TYR C CE1 
2440 C  CE2 . TYR C 90  ? 0.2013 0.2039 0.1740 0.0104  0.0430  0.0194  90  TYR C CE2 
2441 C  CZ  . TYR C 90  ? 0.1400 0.2380 0.1776 0.0496  0.0529  0.0013  90  TYR C CZ  
2442 O  OH  . TYR C 90  ? 0.1623 0.2327 0.2320 0.0276  0.0148  -0.0035 90  TYR C OH  
2443 N  N   . SER C 91  ? 0.1212 0.2960 0.1080 -0.0198 0.0140  0.0403  91  SER C N   
2444 C  CA  . SER C 91  ? 0.1658 0.3260 0.1555 -0.0684 0.0262  0.0519  91  SER C CA  
2445 C  C   . SER C 91  ? 0.2045 0.3028 0.1630 -0.0624 0.0538  0.0604  91  SER C C   
2446 O  O   . SER C 91  ? 0.1546 0.2781 0.1896 -0.0138 0.0157  0.0900  91  SER C O   
2447 C  CB  . SER C 91  ? 0.1497 0.3514 0.1297 -0.0706 0.0122  0.0636  91  SER C CB  
2448 O  OG  . SER C 91  ? 0.1608 0.3879 0.1328 0.0100  0.0033  0.0181  91  SER C OG  
2449 N  N   . SER C 92  ? 0.2086 0.3056 0.2150 -0.0604 0.0234  0.0826  92  SER C N   
2450 C  CA  . SER C 92  ? 0.2998 0.3005 0.2167 -0.0888 -0.0062 0.1294  92  SER C CA  
2451 C  C   . SER C 92  ? 0.2549 0.3528 0.2142 -0.0807 -0.0369 0.1712  92  SER C C   
2452 O  O   . SER C 92  ? 0.2740 0.3484 0.2157 -0.0051 -0.0550 0.1031  92  SER C O   
2453 C  CB  . SER C 92  ? 0.3733 0.2948 0.2773 -0.0912 -0.0124 0.1056  92  SER C CB  
2454 O  OG  . SER C 92  ? 0.3913 0.3725 0.3530 -0.2006 -0.0298 0.1326  92  SER C OG  
2455 N  N   . ASP C 93  ? 0.2223 0.3694 0.2138 -0.0486 0.0533  0.1031  93  ASP C N   
2456 C  CA  . ASP C 93  ? 0.2124 0.3946 0.2050 -0.0816 0.0393  0.0569  93  ASP C CA  
2457 C  C   . ASP C 93  ? 0.2103 0.3766 0.1787 -0.0500 -0.0085 0.0128  93  ASP C C   
2458 O  O   . ASP C 93  ? 0.2555 0.4229 0.1309 -0.0675 0.0387  0.0516  93  ASP C O   
2459 C  CB  . ASP C 93  ? 0.2040 0.4684 0.2137 -0.0881 -0.0125 0.0814  93  ASP C CB  
2460 C  CG  . ASP C 93  ? 0.1321 0.5339 0.2115 -0.0368 -0.0606 0.0866  93  ASP C CG  
2461 O  OD1 . ASP C 93  ? 0.2257 0.5758 0.1959 -0.0434 0.0186  0.0673  93  ASP C OD1 
2462 O  OD2 . ASP C 93  ? 0.1340 0.5404 0.3255 -0.0416 0.0493  0.0624  93  ASP C OD2 
2463 N  N   . TRP C 94  ? 0.2289 0.3041 0.1636 -0.0478 -0.0468 0.0745  94  TRP C N   
2464 C  CA  . TRP C 94  ? 0.2611 0.2862 0.1121 -0.0429 -0.0113 0.0391  94  TRP C CA  
2465 C  C   . TRP C 94  ? 0.2318 0.2983 0.1277 0.0061  0.0073  0.0387  94  TRP C C   
2466 O  O   . TRP C 94  ? 0.2860 0.2973 0.1432 -0.0042 -0.0437 0.0376  94  TRP C O   
2467 C  CB  . TRP C 94  ? 0.1987 0.3028 0.1391 -0.0127 -0.0284 0.0417  94  TRP C CB  
2468 C  CG  . TRP C 94  ? 0.2128 0.2981 0.1516 -0.0051 -0.0427 0.0668  94  TRP C CG  
2469 C  CD1 . TRP C 94  ? 0.2162 0.2994 0.1507 0.0041  -0.0108 0.0832  94  TRP C CD1 
2470 C  CD2 . TRP C 94  ? 0.2155 0.2988 0.1563 -0.0249 -0.0321 0.1038  94  TRP C CD2 
2471 N  NE1 . TRP C 94  ? 0.2288 0.2916 0.1666 -0.0100 -0.0230 0.0800  94  TRP C NE1 
2472 C  CE2 . TRP C 94  ? 0.2080 0.2959 0.1834 -0.0148 -0.0339 0.0790  94  TRP C CE2 
2473 C  CE3 . TRP C 94  ? 0.2104 0.3370 0.1465 -0.0200 -0.0043 0.0812  94  TRP C CE3 
2474 C  CZ2 . TRP C 94  ? 0.1938 0.3059 0.2035 -0.0268 -0.0278 0.0936  94  TRP C CZ2 
2475 C  CZ3 . TRP C 94  ? 0.1834 0.3482 0.1686 -0.0178 -0.0080 0.0832  94  TRP C CZ3 
2476 C  CH2 . TRP C 94  ? 0.1804 0.3537 0.1735 0.0202  -0.0014 0.1139  94  TRP C CH2 
2477 N  N   . LEU C 95  ? 0.2075 0.3109 0.1689 -0.0070 0.0490  0.0433  95  LEU C N   
2478 C  CA  . LEU C 95  ? 0.1455 0.3216 0.1558 0.0375  0.0619  0.0133  95  LEU C CA  
2479 C  C   . LEU C 95  ? 0.1171 0.2580 0.1645 0.0770  0.0635  0.0150  95  LEU C C   
2480 O  O   . LEU C 95  ? 0.2081 0.2438 0.1181 0.0497  0.0523  0.0451  95  LEU C O   
2481 C  CB  . LEU C 95  ? 0.1428 0.3576 0.2566 0.0138  -0.0052 0.0415  95  LEU C CB  
2482 C  CG  . LEU C 95  ? 0.1484 0.3820 0.2569 0.0126  -0.0219 -0.0198 95  LEU C CG  
2483 C  CD1 . LEU C 95  ? 0.1741 0.5317 0.2638 -0.0907 -0.0424 0.0089  95  LEU C CD1 
2484 C  CD2 . LEU C 95  ? 0.2261 0.4004 0.2274 0.0203  0.0210  0.0073  95  LEU C CD2 
2485 N  N   . ILE C 96  ? 0.2091 0.2505 0.0790 0.0594  0.0235  0.0147  96  ILE C N   
2486 C  CA  . ILE C 96  ? 0.1739 0.2056 0.0847 0.0967  -0.0046 -0.0200 96  ILE C CA  
2487 C  C   . ILE C 96  ? 0.1787 0.1997 0.0921 0.0806  0.0557  -0.0541 96  ILE C C   
2488 O  O   . ILE C 96  ? 0.2001 0.2001 0.0808 0.0825  0.0164  -0.0171 96  ILE C O   
2489 C  CB  A ILE C 96  ? 0.1920 0.1974 0.0800 0.0896  0.0104  0.0016  96  ILE C CB  
2490 C  CB  B ILE C 96  ? 0.2063 0.2027 0.0793 0.0739  0.0285  -0.0047 96  ILE C CB  
2491 C  CG1 A ILE C 96  ? 0.2174 0.1900 0.0803 0.0681  0.0518  -0.0361 96  ILE C CG1 
2492 C  CG1 B ILE C 96  ? 0.1645 0.1889 0.1194 0.1023  0.0145  -0.0187 96  ILE C CG1 
2493 C  CG2 A ILE C 96  ? 0.2478 0.1970 0.0982 0.0105  -0.0114 0.0522  96  ILE C CG2 
2494 C  CG2 B ILE C 96  ? 0.2020 0.2231 0.1119 0.0532  0.0464  -0.0231 96  ILE C CG2 
2495 C  CD1 A ILE C 96  ? 0.2823 0.1694 0.1230 0.0823  0.0151  0.0247  96  ILE C CD1 
2496 C  CD1 B ILE C 96  ? 0.2061 0.2093 0.1100 0.0567  0.0071  -0.0479 96  ILE C CD1 
2497 N  N   . TYR C 97  ? 0.1141 0.1996 0.0913 0.0503  0.0232  -0.0524 97  TYR C N   
2498 C  CA  . TYR C 97  ? 0.1401 0.2056 0.0799 0.0655  -0.0091 0.0116  97  TYR C CA  
2499 C  C   . TYR C 97  ? 0.1338 0.2145 0.0801 0.0818  0.0018  0.0119  97  TYR C C   
2500 O  O   . TYR C 97  ? 0.1306 0.2135 0.1327 0.0472  0.0038  -0.0013 97  TYR C O   
2501 C  CB  . TYR C 97  ? 0.1527 0.2881 0.0549 0.0487  0.0225  0.0197  97  TYR C CB  
2502 C  CG  . TYR C 97  ? 0.1190 0.3300 0.0896 0.0598  0.0485  0.0082  97  TYR C CG  
2503 C  CD1 . TYR C 97  ? 0.1597 0.3556 0.0906 0.0089  0.0516  -0.0215 97  TYR C CD1 
2504 C  CD2 . TYR C 97  ? 0.1120 0.3363 0.1582 0.0935  -0.0189 -0.0026 97  TYR C CD2 
2505 C  CE1 . TYR C 97  ? 0.1365 0.3851 0.1258 0.0077  0.0583  0.0303  97  TYR C CE1 
2506 C  CE2 . TYR C 97  ? 0.1107 0.3498 0.2112 0.0635  -0.0160 -0.0072 97  TYR C CE2 
2507 C  CZ  . TYR C 97  ? 0.1288 0.3893 0.1806 0.0493  0.0549  0.0141  97  TYR C CZ  
2508 O  OH  . TYR C 97  ? 0.1212 0.4081 0.2502 0.0283  0.0243  -0.0335 97  TYR C OH  
2509 N  N   . LYS C 98  ? 0.1461 0.2190 0.0663 0.0625  0.0077  0.0270  98  LYS C N   
2510 C  CA  . LYS C 98  ? 0.1186 0.2673 0.0621 0.0708  -0.0201 -0.0140 98  LYS C CA  
2511 C  C   . LYS C 98  ? 0.1367 0.2241 0.0669 0.0710  -0.0150 -0.0127 98  LYS C C   
2512 O  O   . LYS C 98  ? 0.1160 0.2479 0.0742 0.0702  -0.0106 -0.0115 98  LYS C O   
2513 C  CB  . LYS C 98  ? 0.2237 0.3241 0.0986 -0.0326 -0.0639 0.0129  98  LYS C CB  
2514 C  CG  . LYS C 98  ? 0.3862 0.2945 0.2466 -0.0465 -0.1562 -0.0325 98  LYS C CG  
2515 C  CD  . LYS C 98  ? 0.3229 0.3062 0.2883 -0.0125 -0.1264 0.0051  98  LYS C CD  
2516 C  CE  . LYS C 98  ? 0.4545 0.2761 0.3713 -0.0123 -0.1876 0.0070  98  LYS C CE  
2517 N  NZ  . LYS C 98  ? 0.6599 0.3086 0.5405 -0.1526 -0.2912 -0.0195 98  LYS C NZ  
2518 N  N   . THR C 99  ? 0.1336 0.2034 0.0654 0.0598  -0.0257 0.0171  99  THR C N   
2519 C  CA  . THR C 99  ? 0.1067 0.2120 0.0660 0.0636  -0.0237 -0.0161 99  THR C CA  
2520 C  C   . THR C 99  ? 0.1452 0.1775 0.0735 0.0387  -0.0574 0.0104  99  THR C C   
2521 O  O   . THR C 99  ? 0.1354 0.1770 0.0868 0.0417  -0.0324 0.0220  99  THR C O   
2522 C  CB  . THR C 99  ? 0.1125 0.2196 0.0671 0.0427  -0.0199 -0.0066 99  THR C CB  
2523 O  OG1 . THR C 99  ? 0.1587 0.2120 0.0664 0.0418  -0.0417 -0.0087 99  THR C OG1 
2524 C  CG2 . THR C 99  ? 0.1547 0.2104 0.0783 0.0506  -0.0341 0.0034  99  THR C CG2 
2525 N  N   . THR C 100 ? 0.1300 0.1697 0.0956 0.0568  -0.0278 0.0394  100 THR C N   
2526 C  CA  . THR C 100 ? 0.1516 0.1705 0.1158 0.0177  -0.0477 0.0129  100 THR C CA  
2527 C  C   . THR C 100 ? 0.1268 0.1853 0.1122 0.0211  -0.0611 0.0321  100 THR C C   
2528 O  O   . THR C 100 ? 0.2224 0.1813 0.1228 -0.0223 -0.0379 0.0124  100 THR C O   
2529 C  CB  . THR C 100 ? 0.2518 0.1743 0.1173 -0.0084 -0.0484 -0.0125 100 THR C CB  
2530 O  OG1 . THR C 100 ? 0.2960 0.1534 0.2896 0.0438  0.0227  -0.0074 100 THR C OG1 
2531 C  CG2 . THR C 100 ? 0.4282 0.2010 0.1048 -0.0873 -0.0423 0.0068  100 THR C CG2 
2532 N  N   . ASP C 101 ? 0.1284 0.2039 0.1106 0.0212  -0.0188 0.0132  101 ASP C N   
2533 C  CA  . ASP C 101 ? 0.1288 0.1956 0.1074 0.0349  -0.0507 0.0046  101 ASP C CA  
2534 C  C   . ASP C 101 ? 0.1070 0.1973 0.1139 0.0180  0.0002  -0.0273 101 ASP C C   
2535 O  O   . ASP C 101 ? 0.1305 0.2131 0.1045 0.0196  -0.0186 -0.0220 101 ASP C O   
2536 C  CB  . ASP C 101 ? 0.1484 0.1966 0.0968 0.0432  -0.0429 -0.0217 101 ASP C CB  
2537 C  CG  . ASP C 101 ? 0.1290 0.1933 0.1303 0.0427  -0.0191 -0.0099 101 ASP C CG  
2538 O  OD1 . ASP C 101 ? 0.1360 0.1899 0.1242 0.0265  -0.0356 0.0031  101 ASP C OD1 
2539 O  OD2 . ASP C 101 ? 0.1409 0.1983 0.1702 0.0646  -0.0196 0.0004  101 ASP C OD2 
2540 N  N   . HIS C 102 ? 0.1235 0.1972 0.1067 0.0207  -0.0159 -0.0235 102 HIS C N   
2541 C  CA  . HIS C 102 ? 0.1238 0.1978 0.0996 0.0275  0.0184  -0.0229 102 HIS C CA  
2542 C  C   . HIS C 102 ? 0.1289 0.1772 0.0892 0.0297  -0.0267 0.0121  102 HIS C C   
2543 O  O   . HIS C 102 ? 0.1386 0.2304 0.0747 0.0120  -0.0326 -0.0416 102 HIS C O   
2544 C  CB  . HIS C 102 ? 0.1741 0.2679 0.0842 0.0042  0.0704  -0.0758 102 HIS C CB  
2545 C  CG  . HIS C 102 ? 0.1787 0.3437 0.0950 -0.0375 0.0359  -0.0574 102 HIS C CG  
2546 N  ND1 . HIS C 102 ? 0.2544 0.3561 0.1376 -0.0925 0.0475  -0.0220 102 HIS C ND1 
2547 C  CD2 . HIS C 102 ? 0.1519 0.3587 0.1905 -0.0627 0.0076  -0.0204 102 HIS C CD2 
2548 C  CE1 . HIS C 102 ? 0.2444 0.4009 0.1266 -0.1116 0.0608  -0.0372 102 HIS C CE1 
2549 N  NE2 . HIS C 102 ? 0.1744 0.4036 0.1935 -0.0869 0.0326  -0.0485 102 HIS C NE2 
2550 N  N   . TYR C 103 ? 0.1169 0.1694 0.0821 0.0371  -0.0559 -0.0351 103 TYR C N   
2551 C  CA  . TYR C 103 ? 0.1414 0.1700 0.0799 0.0137  -0.0325 -0.0312 103 TYR C CA  
2552 C  C   . TYR C 103 ? 0.1181 0.1841 0.0870 0.0277  -0.0296 -0.0190 103 TYR C C   
2553 O  O   . TYR C 103 ? 0.1207 0.1995 0.1282 0.0312  -0.0263 -0.0124 103 TYR C O   
2554 C  CB  . TYR C 103 ? 0.1476 0.1707 0.0956 0.0256  0.0205  -0.0065 103 TYR C CB  
2555 C  CG  . TYR C 103 ? 0.1263 0.1837 0.1019 0.0501  0.0256  -0.0169 103 TYR C CG  
2556 C  CD1 . TYR C 103 ? 0.1163 0.1942 0.1037 0.0235  0.0161  -0.0357 103 TYR C CD1 
2557 C  CD2 . TYR C 103 ? 0.1247 0.1960 0.1055 0.0356  -0.0380 -0.0114 103 TYR C CD2 
2558 C  CE1 . TYR C 103 ? 0.1144 0.1945 0.1185 0.0199  -0.0176 -0.0208 103 TYR C CE1 
2559 C  CE2 . TYR C 103 ? 0.1026 0.2111 0.1180 0.0504  -0.0297 0.0043  103 TYR C CE2 
2560 C  CZ  . TYR C 103 ? 0.1025 0.1997 0.1207 0.0297  -0.0117 -0.0422 103 TYR C CZ  
2561 O  OH  . TYR C 103 ? 0.1277 0.1784 0.1246 0.0342  0.0103  0.0306  103 TYR C OH  
2562 N  N   . GLN C 104 ? 0.0906 0.1927 0.1017 0.0419  -0.0116 -0.0012 104 GLN C N   
2563 C  CA  . GLN C 104 ? 0.0961 0.1943 0.1062 0.0502  -0.0037 0.0032  104 GLN C CA  
2564 C  C   . GLN C 104 ? 0.0794 0.2170 0.1053 0.0624  -0.0440 0.0024  104 GLN C C   
2565 O  O   . GLN C 104 ? 0.0931 0.2318 0.1012 0.0415  -0.0220 0.0033  104 GLN C O   
2566 C  CB  . GLN C 104 ? 0.1038 0.2009 0.1074 0.0433  -0.0251 -0.0226 104 GLN C CB  
2567 C  CG  . GLN C 104 ? 0.1261 0.2472 0.1018 0.0651  -0.0152 -0.0487 104 GLN C CG  
2568 C  CD  . GLN C 104 ? 0.1961 0.2731 0.0912 0.0300  -0.0625 0.0153  104 GLN C CD  
2569 O  OE1 . GLN C 104 ? 0.1648 0.3148 0.0901 0.0668  -0.0120 0.0008  104 GLN C OE1 
2570 N  NE2 . GLN C 104 ? 0.2092 0.2380 0.0904 0.0340  -0.0115 -0.0216 104 GLN C NE2 
2571 N  N   . THR C 105 ? 0.0916 0.2839 0.0786 0.0442  -0.0105 -0.0224 105 THR C N   
2572 C  CA  . THR C 105 ? 0.1120 0.2892 0.0819 0.0810  -0.0334 0.0097  105 THR C CA  
2573 C  C   . THR C 105 ? 0.0920 0.3106 0.0789 0.0852  0.0167  -0.0220 105 THR C C   
2574 O  O   . THR C 105 ? 0.1027 0.2897 0.0947 0.0849  -0.0028 -0.0283 105 THR C O   
2575 C  CB  . THR C 105 ? 0.1444 0.2828 0.1375 0.0966  -0.0257 -0.0248 105 THR C CB  
2576 O  OG1 . THR C 105 ? 0.1641 0.2804 0.2005 0.0782  -0.0477 -0.0541 105 THR C OG1 
2577 C  CG2 . THR C 105 ? 0.1660 0.2666 0.1538 0.1067  -0.0465 0.0125  105 THR C CG2 
2578 N  N   . PHE C 106 ? 0.0890 0.3543 0.0844 0.0779  0.0025  -0.0139 106 PHE C N   
2579 C  CA  . PHE C 106 ? 0.1595 0.3415 0.0756 0.0547  -0.0382 -0.0088 106 PHE C CA  
2580 C  C   . PHE C 106 ? 0.1487 0.3382 0.0840 0.1275  -0.0537 -0.0411 106 PHE C C   
2581 O  O   . PHE C 106 ? 0.1386 0.3632 0.1377 0.1293  -0.0457 -0.0403 106 PHE C O   
2582 C  CB  . PHE C 106 ? 0.1367 0.3363 0.1212 0.0355  -0.0116 -0.0059 106 PHE C CB  
2583 C  CG  . PHE C 106 ? 0.1260 0.3410 0.1083 0.0078  0.0075  -0.0477 106 PHE C CG  
2584 C  CD1 . PHE C 106 ? 0.1560 0.3139 0.1114 -0.0014 0.0069  0.0393  106 PHE C CD1 
2585 C  CD2 . PHE C 106 ? 0.1591 0.3355 0.1401 -0.0453 -0.0057 -0.0742 106 PHE C CD2 
2586 C  CE1 . PHE C 106 ? 0.1909 0.3025 0.1176 -0.0149 0.0257  0.0140  106 PHE C CE1 
2587 C  CE2 . PHE C 106 ? 0.2014 0.3201 0.1520 -0.0555 -0.0130 -0.0687 106 PHE C CE2 
2588 C  CZ  . PHE C 106 ? 0.2063 0.3091 0.1253 -0.0395 0.0309  -0.0286 106 PHE C CZ  
2589 N  N   . THR C 107 ? 0.1861 0.2994 0.0834 0.1030  -0.0344 -0.0176 107 THR C N   
2590 C  CA  . THR C 107 ? 0.1579 0.3011 0.0883 0.1347  -0.0309 -0.0149 107 THR C CA  
2591 C  C   . THR C 107 ? 0.1476 0.2934 0.0879 0.1398  -0.0188 -0.0306 107 THR C C   
2592 O  O   . THR C 107 ? 0.1678 0.2863 0.0664 0.1240  0.0082  -0.0092 107 THR C O   
2593 C  CB  . THR C 107 ? 0.3710 0.2739 0.1647 0.0547  -0.0417 0.0319  107 THR C CB  
2594 O  OG1 . THR C 107 ? 0.3903 0.2832 0.1693 0.0857  -0.0052 0.0095  107 THR C OG1 
2595 C  CG2 . THR C 107 ? 0.5138 0.2672 0.1672 0.0931  -0.0360 -0.0164 107 THR C CG2 
2596 N  N   . LYS C 108 ? 0.1777 0.2703 0.0923 0.0853  0.0012  -0.0190 108 LYS C N   
2597 C  CA  . LYS C 108 ? 0.1921 0.2598 0.0979 0.1007  -0.0210 0.0033  108 LYS C CA  
2598 C  C   . LYS C 108 ? 0.2089 0.2169 0.0789 0.1062  0.0250  -0.0201 108 LYS C C   
2599 O  O   . LYS C 108 ? 0.2582 0.2168 0.1116 0.1190  -0.0338 -0.0226 108 LYS C O   
2600 C  CB  . LYS C 108 ? 0.2102 0.3398 0.0883 0.0695  0.0364  -0.0120 108 LYS C CB  
2601 C  CG  . LYS C 108 ? 0.2920 0.3585 0.0878 0.0517  0.0793  -0.0088 108 LYS C CG  
2602 C  CD  . LYS C 108 ? 0.3252 0.3840 0.0824 -0.0139 0.0819  -0.0148 108 LYS C CD  
2603 C  CE  . LYS C 108 ? 0.4290 0.3099 0.0987 -0.0002 -0.0030 -0.0367 108 LYS C CE  
2604 N  NZ  . LYS C 108 ? 0.6758 0.2788 0.3351 -0.0441 -0.0829 -0.0587 108 LYS C NZ  
2605 N  N   . ILE C 109 ? 0.2146 0.2109 0.0718 0.0860  -0.0240 -0.0115 109 ILE C N   
2606 C  CA  . ILE C 109 ? 0.2316 0.1834 0.0873 0.0765  -0.0266 -0.0335 109 ILE C CA  
2607 C  C   . ILE C 109 ? 0.2157 0.1746 0.0864 0.0547  -0.0301 -0.0103 109 ILE C C   
2608 O  O   . ILE C 109 ? 0.2410 0.1724 0.0962 0.0352  -0.0488 -0.0055 109 ILE C O   
2609 C  CB  . ILE C 109 ? 0.2453 0.2000 0.0754 0.0528  -0.0073 0.0218  109 ILE C CB  
2610 C  CG1 . ILE C 109 ? 0.1884 0.2149 0.0936 0.0712  0.0077  -0.0494 109 ILE C CG1 
2611 C  CG2 . ILE C 109 ? 0.2625 0.2087 0.0786 0.0676  0.0135  0.0273  109 ILE C CG2 
2612 C  CD1 . ILE C 109 ? 0.1736 0.2642 0.2017 0.0464  0.0196  -0.0171 109 ILE C CD1 
2613 N  N   . ARG C 110 ? 0.2480 0.1770 0.0975 0.0401  -0.0707 0.0086  110 ARG C N   
2614 C  CA  . ARG C 110 ? 0.2633 0.1850 0.0878 0.0278  -0.1019 0.0560  110 ARG C CA  
2615 C  C   . ARG C 110 ? 0.3211 0.2737 0.1447 -0.0630 -0.0035 0.0245  110 ARG C C   
2616 O  O   . ARG C 110 ? 0.2435 0.3593 0.1451 -0.0176 0.0141  0.0259  110 ARG C O   
2617 C  CB  . ARG C 110 ? 0.2955 0.1607 0.0977 0.0333  -0.0967 0.0229  110 ARG C CB  
2618 C  CG  . ARG C 110 ? 0.2676 0.1686 0.1188 0.0521  -0.0390 -0.0115 110 ARG C CG  
2619 C  CD  . ARG C 110 ? 0.2350 0.2293 0.0709 0.0524  -0.0086 -0.0130 110 ARG C CD  
2620 N  NE  . ARG C 110 ? 0.2399 0.2761 0.1101 0.0306  -0.0477 0.0180  110 ARG C NE  
2621 C  CZ  . ARG C 110 ? 0.2218 0.2802 0.1135 0.0417  -0.0768 0.0326  110 ARG C CZ  
2622 N  NH1 . ARG C 110 ? 0.2567 0.2594 0.1340 0.0508  -0.0351 0.0234  110 ARG C NH1 
2623 N  NH2 . ARG C 110 ? 0.2557 0.2703 0.2296 -0.0006 -0.0469 -0.0875 110 ARG C NH2 
2624 O  OXT . ARG C 110 ? 0.2769 0.3762 0.1418 -0.0678 0.0247  -0.0118 110 ARG C OXT 
2625 ZN ZN  . ZN  D .   ? 0.6550 0.5943 0.3390 0.1326  -0.1310 0.2128  112 ZN  A ZN  
2626 ZN ZN  . ZN  E .   ? 0.3821 0.4909 0.3479 0.1260  0.0990  0.0201  112 ZN  B ZN  
2627 ZN ZN  . ZN  F .   ? 0.1419 0.2253 0.1215 0.0328  -0.0127 -0.0077 112 ZN  C ZN  
2628 O  O   . HOH G .   ? 0.2039 0.1599 0.1075 -0.0086 0.0114  -0.0133 113 HOH A O   
2629 O  O   . HOH G .   ? 0.1678 0.2182 0.1910 0.0106  -0.0341 -0.0630 114 HOH A O   
2630 O  O   . HOH G .   ? 0.1995 0.1491 0.1288 -0.0381 -0.0032 -0.0038 115 HOH A O   
2631 O  O   . HOH G .   ? 0.2169 0.1598 0.1449 0.0059  0.0598  -0.0293 116 HOH A O   
2632 O  O   . HOH G .   ? 0.2127 0.1719 0.1610 0.0427  -0.0227 -0.0073 117 HOH A O   
2633 O  O   . HOH G .   ? 0.1646 0.3034 0.1270 0.0108  0.0123  0.0049  118 HOH A O   
2634 O  O   . HOH G .   ? 0.4111 0.1295 0.2300 -0.0033 0.0259  0.0297  119 HOH A O   
2635 O  O   . HOH G .   ? 0.3124 0.1851 0.1739 -0.0289 0.0838  0.0044  120 HOH A O   
2636 O  O   . HOH G .   ? 0.1891 0.1672 0.1910 -0.0374 -0.0048 -0.0196 121 HOH A O   
2637 O  O   . HOH G .   ? 0.2970 0.2228 0.1928 -0.0002 -0.0266 -0.0916 122 HOH A O   
2638 O  O   . HOH G .   ? 0.2802 0.2208 0.2616 0.0370  -0.0337 -0.0994 123 HOH A O   
2639 O  O   . HOH G .   ? 0.4403 0.2512 0.1165 -0.0126 0.0539  -0.0207 124 HOH A O   
2640 O  O   . HOH G .   ? 0.4541 0.5263 0.5272 -0.0196 0.1859  -0.0164 125 HOH A O   
2641 O  O   . HOH G .   ? 0.4257 0.2533 0.0960 0.0111  0.0078  -0.0346 126 HOH A O   
2642 O  O   . HOH G .   ? 0.3332 0.2108 0.2290 -0.0344 -0.0544 -0.0140 127 HOH A O   
2643 O  O   . HOH G .   ? 0.2566 0.2673 0.2620 -0.0312 -0.0277 -0.0435 128 HOH A O   
2644 O  O   . HOH G .   ? 0.4974 0.7480 0.6928 0.0056  0.2737  0.0121  129 HOH A O   
2645 O  O   . HOH G .   ? 0.2501 0.3964 0.2818 -0.0269 0.0056  -0.0888 130 HOH A O   
2646 O  O   . HOH G .   ? 0.5760 0.3280 0.4719 0.0433  0.1313  0.1277  131 HOH A O   
2647 O  O   . HOH G .   ? 0.3687 0.2507 0.2775 0.0858  -0.0949 -0.0438 132 HOH A O   
2648 O  O   . HOH G .   ? 0.7768 0.4255 0.3553 0.0615  -0.1373 0.0467  133 HOH A O   
2649 O  O   . HOH G .   ? 0.2110 0.3975 0.4056 -0.0258 -0.0263 -0.1226 134 HOH A O   
2650 O  O   . HOH G .   ? 0.3646 0.2653 0.2823 -0.0743 -0.0225 0.0564  135 HOH A O   
2651 O  O   . HOH G .   ? 0.7068 0.4943 0.2552 -0.1217 0.2061  0.0049  136 HOH A O   
2652 O  O   . HOH G .   ? 0.4067 0.3117 0.4487 0.0036  0.1945  -0.0229 137 HOH A O   
2653 O  O   . HOH G .   ? 0.3325 0.1948 0.1695 0.0366  -0.0178 -0.0821 138 HOH A O   
2654 O  O   . HOH G .   ? 0.4339 0.2746 0.2092 0.0367  -0.0328 0.0140  139 HOH A O   
2655 O  O   . HOH G .   ? 0.6171 0.3478 0.2652 -0.2873 0.1319  -0.0577 140 HOH A O   
2656 O  O   . HOH G .   ? 0.5549 0.3476 0.2954 0.0477  -0.0479 -0.0205 141 HOH A O   
2657 O  O   . HOH G .   ? 0.5970 0.4283 0.3990 0.1431  -0.0735 -0.0780 142 HOH A O   
2658 O  O   . HOH G .   ? 0.4405 0.2265 0.2014 -0.0614 -0.0124 -0.0078 143 HOH A O   
2659 O  O   . HOH G .   ? 0.3253 0.3030 0.2770 0.0330  -0.0250 0.0479  144 HOH A O   
2660 O  O   . HOH G .   ? 0.2642 0.2505 0.3461 -0.0380 0.0905  -0.0936 145 HOH A O   
2661 O  O   . HOH G .   ? 0.3883 0.3494 0.3502 0.0418  0.1443  -0.0220 146 HOH A O   
2662 O  O   . HOH G .   ? 0.2338 0.3375 0.4609 0.0510  -0.0609 -0.2265 147 HOH A O   
2663 O  O   . HOH G .   ? 0.2665 0.2582 0.2695 0.0487  0.0407  -0.0078 148 HOH A O   
2664 O  O   . HOH G .   ? 0.6561 0.2368 0.2174 0.0714  -0.0643 -0.0599 149 HOH A O   
2665 O  O   . HOH G .   ? 0.5492 0.2081 0.4097 0.1245  -0.1523 -0.0166 150 HOH A O   
2666 O  O   . HOH G .   ? 0.3001 0.4129 0.3896 0.0018  0.0219  -0.1611 151 HOH A O   
2667 O  O   . HOH G .   ? 0.5339 0.3656 0.2623 -0.0452 0.0861  0.1263  152 HOH A O   
2668 O  O   . HOH G .   ? 0.2675 0.3955 0.5837 -0.1292 0.1454  -0.0873 153 HOH A O   
2669 O  O   . HOH G .   ? 0.3294 0.3569 0.2394 0.0335  -0.0209 0.0433  154 HOH A O   
2670 O  O   . HOH G .   ? 0.7759 0.4808 0.3110 -0.2601 -0.0106 0.1016  155 HOH A O   
2671 O  O   . HOH G .   ? 0.3379 0.4023 0.4207 0.0505  0.1753  -0.0991 156 HOH A O   
2672 O  O   . HOH G .   ? 0.4224 0.3639 0.4076 0.1315  -0.0682 -0.0512 157 HOH A O   
2673 O  O   . HOH G .   ? 0.4136 0.2166 0.3036 0.1039  -0.1184 0.0206  158 HOH A O   
2674 O  O   . HOH G .   ? 0.4223 0.5482 0.2862 -0.2445 -0.1905 0.0715  159 HOH A O   
2675 O  O   . HOH G .   ? 0.5271 0.5890 0.3891 -0.1355 0.0226  -0.0407 160 HOH A O   
2676 O  O   . HOH G .   ? 0.4315 0.4654 0.3496 0.1327  0.0554  0.0445  161 HOH A O   
2677 O  O   . HOH G .   ? 0.5282 0.5156 0.4480 -0.1373 0.0017  -0.1481 162 HOH A O   
2678 O  O   . HOH G .   ? 1.0404 1.0231 0.9601 -0.0554 0.0591  -0.0013 163 HOH A O   
2679 O  O   . HOH G .   ? 0.6697 0.6554 0.7726 0.0922  0.0503  -0.0610 164 HOH A O   
2680 O  O   . HOH G .   ? 0.4694 0.3951 0.6479 0.1101  -0.0700 -0.0457 165 HOH A O   
2681 O  O   . HOH G .   ? 0.5148 0.5725 0.4714 -0.0224 0.1129  -0.2129 166 HOH A O   
2682 O  O   . HOH G .   ? 0.4658 0.6062 0.3590 -0.1347 -0.0915 0.0160  167 HOH A O   
2683 O  O   . HOH G .   ? 0.5882 0.3331 0.2042 -0.0166 -0.0230 -0.0966 168 HOH A O   
2684 O  O   . HOH G .   ? 0.6176 0.5196 0.2845 0.0319  -0.0931 -0.0428 169 HOH A O   
2685 O  O   . HOH G .   ? 0.6875 0.8226 0.7225 -0.0261 0.0858  -0.0014 170 HOH A O   
2686 O  O   . HOH G .   ? 0.7102 0.4493 0.6602 0.2200  0.1283  -0.1322 171 HOH A O   
2687 O  O   . HOH G .   ? 0.5400 0.4279 0.4971 0.0136  -0.2230 0.1073  172 HOH A O   
2688 O  O   . HOH G .   ? 0.7190 0.3584 0.2966 0.0558  -0.1314 -0.0720 173 HOH A O   
2689 O  O   . HOH G .   ? 0.7643 0.6539 0.5953 0.0034  -0.0358 -0.1566 174 HOH A O   
2690 O  O   . HOH G .   ? 0.9311 0.7856 0.8599 -0.0524 -0.0750 -0.0164 175 HOH A O   
2691 O  O   . HOH G .   ? 0.9293 0.4751 0.3454 0.1881  -0.2110 -0.1352 176 HOH A O   
2692 O  O   . HOH G .   ? 0.4933 0.4563 0.4772 0.0819  -0.0412 -0.0178 177 HOH A O   
2693 O  O   . HOH G .   ? 0.6045 0.4928 0.5677 0.0209  0.0472  -0.0074 178 HOH A O   
2694 O  O   . HOH G .   ? 0.4742 0.4814 0.8024 0.1703  -0.0354 -0.0361 179 HOH A O   
2695 O  O   . HOH G .   ? 0.3844 0.7344 0.5148 -0.0548 -0.2207 -0.0964 180 HOH A O   
2696 O  O   . HOH G .   ? 0.5269 0.4391 0.5999 0.0956  0.0228  -0.1495 181 HOH A O   
2697 O  O   . HOH G .   ? 0.6341 0.4588 0.5260 0.0784  0.0029  0.0493  182 HOH A O   
2698 O  O   . HOH G .   ? 0.5731 0.4561 0.4834 0.0184  -0.0657 0.0415  183 HOH A O   
2699 O  O   . HOH G .   ? 0.5764 0.5222 0.4749 0.0119  -0.1013 0.0428  184 HOH A O   
2700 O  O   . HOH G .   ? 0.5046 0.4615 0.6295 0.1098  0.0381  0.1759  185 HOH A O   
2701 O  O   . HOH G .   ? 0.6874 0.6540 0.5393 -0.1109 0.1715  0.0828  186 HOH A O   
2702 O  O   . HOH G .   ? 0.4672 0.4801 0.5124 0.1521  -0.0763 -0.0211 187 HOH A O   
2703 O  O   . HOH G .   ? 0.9195 0.5084 0.4702 -0.1634 0.1198  -0.1320 188 HOH A O   
2704 O  O   . HOH G .   ? 0.8130 0.7337 0.7614 -0.0129 -0.0931 0.0308  189 HOH A O   
2705 O  O   . HOH G .   ? 0.4732 0.4897 0.7922 0.0748  -0.0667 -0.0205 190 HOH A O   
2706 O  O   . HOH G .   ? 0.5612 0.6158 0.7134 -0.0127 -0.1595 -0.0368 191 HOH A O   
2707 O  O   . HOH G .   ? 0.7138 0.6459 0.7580 0.1267  -0.2468 0.0766  192 HOH A O   
2708 O  O   . HOH G .   ? 0.4277 0.7992 0.7269 -0.1508 -0.1142 0.0012  193 HOH A O   
2709 O  O   . HOH G .   ? 0.2878 0.2922 0.4142 -0.0652 -0.1667 0.0933  194 HOH A O   
2710 O  O   . HOH G .   ? 0.4804 0.2901 0.2341 -0.0857 -0.0350 0.0467  195 HOH A O   
2711 O  O   . HOH G .   ? 0.3880 0.2630 0.4498 -0.0830 -0.1388 -0.0116 196 HOH A O   
2712 O  O   . HOH G .   ? 0.5516 0.3892 0.3758 0.0136  0.0504  0.0678  197 HOH A O   
2713 O  O   . HOH G .   ? 0.3786 0.4555 0.3655 0.0496  -0.0019 -0.1267 198 HOH A O   
2714 O  O   . HOH G .   ? 0.4561 0.4970 0.3784 -0.0411 0.0517  0.0030  199 HOH A O   
2715 O  O   . HOH G .   ? 0.2958 0.4937 0.3614 0.0079  -0.0406 -0.0172 200 HOH A O   
2716 O  O   . HOH G .   ? 0.6212 0.6567 0.5418 -0.1497 0.2602  -0.3043 201 HOH A O   
2717 O  O   . HOH G .   ? 0.4370 0.4439 0.3860 -0.1476 0.1072  -0.1457 202 HOH A O   
2718 O  O   . HOH G .   ? 0.5462 0.5497 0.4328 0.0628  0.0793  -0.0820 203 HOH A O   
2719 O  O   . HOH G .   ? 0.6811 0.5588 0.3931 -0.2485 0.1054  -0.1933 204 HOH A O   
2720 O  O   . HOH G .   ? 0.4914 0.8207 0.8894 -0.0990 -0.0397 -0.0167 205 HOH A O   
2721 O  O   . HOH G .   ? 0.5017 0.5056 0.4814 0.0017  0.0821  -0.0962 206 HOH A O   
2722 O  O   . HOH G .   ? 0.6147 0.5575 0.5690 0.0723  -0.0041 -0.0265 207 HOH A O   
2723 O  O   . HOH G .   ? 0.9803 0.5067 0.2521 -0.1480 0.1336  -0.1020 208 HOH A O   
2724 O  O   . HOH G .   ? 0.5008 0.6883 0.5299 0.1018  0.0487  -0.0854 209 HOH A O   
2725 O  O   . HOH G .   ? 0.9325 0.5143 0.7412 -0.0051 -0.0856 -0.1753 210 HOH A O   
2726 O  O   . HOH G .   ? 0.4438 0.3353 0.4702 -0.0725 -0.0579 -0.1318 211 HOH A O   
2727 O  O   . HOH G .   ? 0.8591 0.5675 0.4932 -0.0914 0.2734  -0.1157 212 HOH A O   
2728 O  O   . HOH G .   ? 0.5445 0.6284 0.5647 -0.0572 0.1436  -0.1486 213 HOH A O   
2729 O  O   . HOH G .   ? 0.8210 0.6240 0.6461 -0.0646 0.2065  0.0419  214 HOH A O   
2730 O  O   . HOH G .   ? 0.4498 0.7718 0.5121 0.0675  -0.1599 0.0754  215 HOH A O   
2731 O  O   . HOH G .   ? 0.5868 0.8882 0.7140 0.0079  0.1059  -0.1291 216 HOH A O   
2732 O  O   . HOH G .   ? 0.6560 0.6804 0.4422 -0.1966 0.0061  0.0201  217 HOH A O   
2733 O  O   . HOH G .   ? 0.6337 0.5610 0.2517 -0.1084 0.0604  -0.0779 218 HOH A O   
2734 O  O   . HOH G .   ? 0.6858 0.6292 0.7820 0.1204  0.0269  -0.0845 219 HOH A O   
2735 O  O   . HOH G .   ? 0.7464 0.6153 0.4879 0.0073  -0.0591 0.0797  220 HOH A O   
2736 O  O   . HOH G .   ? 0.8711 0.7929 0.7477 -0.0097 0.3067  -0.2615 221 HOH A O   
2737 O  O   . HOH G .   ? 0.5029 0.4559 0.4904 0.0055  -0.1841 0.0360  222 HOH A O   
2738 O  O   . HOH G .   ? 0.4881 0.5739 0.6119 -0.0399 -0.1088 -0.1192 223 HOH A O   
2739 O  O   . HOH G .   ? 0.6303 0.7134 0.5789 -0.1630 -0.1520 0.1413  224 HOH A O   
2740 O  O   . HOH G .   ? 0.4888 0.5718 0.6919 0.0315  -0.0721 0.0800  225 HOH A O   
2741 O  O   . HOH G .   ? 0.7516 0.7706 0.7748 0.0972  -0.0605 0.1155  226 HOH A O   
2742 O  O   . HOH G .   ? 0.3273 0.4568 0.2564 -0.0572 -0.1435 -0.0348 227 HOH A O   
2743 O  O   . HOH G .   ? 0.4515 0.5582 0.7491 0.0852  0.0087  -0.0234 228 HOH A O   
2744 O  O   . HOH G .   ? 0.8536 0.8699 0.8940 0.0357  -0.2457 0.1018  229 HOH A O   
2745 O  O   . HOH G .   ? 0.7406 0.7717 0.7015 0.0383  -0.1581 0.0134  230 HOH A O   
2746 O  O   . HOH G .   ? 0.6521 0.6210 0.4329 0.0009  -0.1866 -0.0207 231 HOH A O   
2747 O  O   . HOH G .   ? 0.7806 0.6217 0.7049 0.0542  0.2344  -0.1233 232 HOH A O   
2748 O  O   . HOH G .   ? 0.5818 0.5375 0.6605 0.1071  -0.0421 -0.0146 233 HOH A O   
2749 O  O   . HOH G .   ? 0.3293 0.6760 0.5229 0.0056  -0.1356 -0.0045 234 HOH A O   
2750 O  O   . HOH G .   ? 0.4414 0.5904 0.5050 -0.0483 0.1197  -0.0889 235 HOH A O   
2751 O  O   . HOH G .   ? 0.7898 0.4989 0.5632 -0.0195 -0.2130 0.1768  236 HOH A O   
2752 O  O   . HOH G .   ? 0.7601 0.5366 0.7307 0.0232  -0.2992 0.2554  237 HOH A O   
2753 O  O   . HOH G .   ? 0.4169 0.5704 0.5477 0.0368  -0.0737 -0.0809 238 HOH A O   
2754 O  O   . HOH G .   ? 0.6233 0.7641 0.6071 -0.1425 -0.2027 0.1211  239 HOH A O   
2755 O  O   . HOH G .   ? 0.3742 0.4821 0.6680 0.0408  0.0153  0.1278  240 HOH A O   
2756 O  O   . HOH G .   ? 0.6567 0.8176 0.9422 0.1458  0.2749  -0.0840 241 HOH A O   
2757 O  O   . HOH G .   ? 0.6345 0.7221 0.8471 -0.0630 -0.1943 0.0655  242 HOH A O   
2758 O  O   . HOH G .   ? 0.6619 0.4928 0.6049 -0.0406 0.1291  -0.0257 243 HOH A O   
2759 O  O   . HOH G .   ? 0.8383 0.5647 0.6687 -0.2250 0.0085  0.1746  244 HOH A O   
2760 O  O   . HOH G .   ? 0.5117 0.4602 0.5280 0.1423  -0.2496 0.0081  245 HOH A O   
2761 O  O   . HOH G .   ? 0.4895 0.6098 0.5317 0.1126  -0.0557 0.1809  246 HOH A O   
2762 O  O   . HOH H .   ? 0.1783 0.1730 0.1542 0.0217  -0.0153 -0.0264 137 HOH B O   
2763 O  O   . HOH H .   ? 0.1738 0.1918 0.1624 -0.0352 0.0286  0.0133  138 HOH B O   
2764 O  O   . HOH H .   ? 0.1881 0.1731 0.1192 -0.0389 0.0384  -0.0120 139 HOH B O   
2765 O  O   . HOH H .   ? 0.2109 0.2625 0.1460 -0.0130 0.0008  -0.0739 140 HOH B O   
2766 O  O   . HOH H .   ? 0.2472 0.1526 0.1898 -0.0218 0.0094  -0.0092 141 HOH B O   
2767 O  O   . HOH H .   ? 0.2376 0.1713 0.1481 -0.0499 0.0012  0.0003  142 HOH B O   
2768 O  O   . HOH H .   ? 0.3209 0.2528 0.1864 0.1161  -0.0058 0.0420  143 HOH B O   
2769 O  O   . HOH H .   ? 0.1781 0.2714 0.1513 0.0383  -0.0183 -0.0149 144 HOH B O   
2770 O  O   . HOH H .   ? 0.1341 0.1533 0.1900 0.0013  0.0195  -0.0155 145 HOH B O   
2771 O  O   . HOH H .   ? 0.7945 0.7442 0.7953 0.1300  -0.2777 0.1427  146 HOH B O   
2772 O  O   . HOH H .   ? 0.2275 0.3075 0.2513 -0.0453 0.0853  -0.0169 147 HOH B O   
2773 O  O   . HOH H .   ? 0.3931 0.2656 0.5955 0.0356  -0.0421 0.0127  148 HOH B O   
2774 O  O   . HOH H .   ? 0.5037 0.5748 0.4675 -0.0812 -0.0509 0.0510  149 HOH B O   
2775 O  O   . HOH H .   ? 0.7107 0.5008 0.3653 -0.1802 -0.0515 -0.0033 150 HOH B O   
2776 O  O   . HOH H .   ? 0.2530 0.3125 0.1702 0.0447  -0.0302 -0.0170 151 HOH B O   
2777 O  O   . HOH H .   ? 0.2642 0.2765 0.2000 0.0058  0.0219  -0.0619 152 HOH B O   
2778 O  O   . HOH H .   ? 0.3553 0.2701 0.2256 -0.0081 0.0217  0.0142  153 HOH B O   
2779 O  O   . HOH H .   ? 0.2498 0.3635 0.2148 -0.0065 -0.0053 -0.0572 154 HOH B O   
2780 O  O   . HOH H .   ? 0.3633 0.4794 0.3805 0.1502  0.0120  0.0371  155 HOH B O   
2781 O  O   . HOH H .   ? 0.2838 0.2542 0.2885 -0.0211 0.1034  -0.0209 156 HOH B O   
2782 O  O   . HOH H .   ? 0.3308 0.2970 0.3495 -0.0390 -0.0188 0.0445  157 HOH B O   
2783 O  O   . HOH H .   ? 0.2520 0.3862 0.2661 0.0860  0.0557  0.0892  158 HOH B O   
2784 O  O   . HOH H .   ? 0.2142 0.4741 0.3596 -0.0315 -0.0323 0.1461  159 HOH B O   
2785 O  O   . HOH H .   ? 0.4169 0.2268 0.2755 -0.0320 0.0443  -0.0587 160 HOH B O   
2786 O  O   . HOH H .   ? 0.4532 0.3561 0.3414 0.0748  -0.0205 -0.0990 161 HOH B O   
2787 O  O   . HOH H .   ? 0.2013 0.2629 0.2821 0.0029  -0.0720 -0.0441 162 HOH B O   
2788 O  O   . HOH H .   ? 0.2718 0.3404 0.3310 -0.0485 0.0757  -0.0299 163 HOH B O   
2789 O  O   . HOH H .   ? 0.2463 0.4027 0.3632 -0.0723 0.0371  -0.1275 164 HOH B O   
2790 O  O   . HOH H .   ? 0.3951 0.2292 0.3078 0.0969  0.0093  0.0498  165 HOH B O   
2791 O  O   . HOH H .   ? 0.2756 0.3242 0.3010 0.1531  0.0297  0.0097  166 HOH B O   
2792 O  O   . HOH H .   ? 0.3672 0.3576 0.3530 0.0703  0.0244  -0.0171 167 HOH B O   
2793 O  O   . HOH H .   ? 0.3763 0.3480 0.3388 0.0633  -0.0961 -0.0557 168 HOH B O   
2794 O  O   . HOH H .   ? 0.3811 0.3378 0.3022 -0.0405 0.0351  -0.0200 169 HOH B O   
2795 O  O   . HOH H .   ? 0.4507 0.3206 0.3752 0.1429  -0.1173 -0.0578 170 HOH B O   
2796 O  O   . HOH H .   ? 0.3722 0.2245 0.4484 -0.0097 -0.0611 -0.0727 171 HOH B O   
2797 O  O   . HOH H .   ? 0.6811 0.4328 0.3963 0.0637  -0.0312 0.1496  172 HOH B O   
2798 O  O   . HOH H .   ? 0.6382 0.2820 0.3618 -0.0905 0.0196  -0.0835 173 HOH B O   
2799 O  O   . HOH H .   ? 0.4762 0.2732 0.2482 0.0237  0.0334  0.0294  174 HOH B O   
2800 O  O   . HOH H .   ? 0.5249 0.2368 0.3097 0.1358  -0.0220 0.0372  175 HOH B O   
2801 O  O   . HOH H .   ? 0.3540 0.5653 0.3827 -0.0065 -0.0188 0.0548  176 HOH B O   
2802 O  O   . HOH H .   ? 0.3709 0.3814 0.2936 0.0220  -0.1105 -0.0006 177 HOH B O   
2803 O  O   . HOH H .   ? 0.5945 0.3526 0.3503 0.0969  0.1034  -0.0840 178 HOH B O   
2804 O  O   . HOH H .   ? 0.4112 0.4554 0.2701 -0.0346 -0.1442 -0.0439 179 HOH B O   
2805 O  O   . HOH H .   ? 0.3545 0.4491 0.4253 0.1693  -0.0672 -0.0779 180 HOH B O   
2806 O  O   . HOH H .   ? 0.5655 0.3896 0.3309 0.1653  0.0540  -0.0450 181 HOH B O   
2807 O  O   . HOH H .   ? 0.6671 0.5145 0.4055 0.0325  -0.0468 -0.0983 182 HOH B O   
2808 O  O   . HOH H .   ? 0.4946 0.4667 0.3094 -0.1459 0.1072  -0.0201 183 HOH B O   
2809 O  O   . HOH H .   ? 0.3045 0.4355 0.3727 -0.0654 -0.0727 0.0619  184 HOH B O   
2810 O  O   . HOH H .   ? 0.3990 0.4344 0.4441 0.0041  0.1266  0.0960  185 HOH B O   
2811 O  O   . HOH H .   ? 0.4252 0.4322 0.4288 0.1033  -0.0389 -0.0097 186 HOH B O   
2812 O  O   . HOH H .   ? 0.3582 0.3239 0.4891 -0.0143 0.0599  -0.0683 187 HOH B O   
2813 O  O   . HOH H .   ? 0.4741 0.2097 0.4253 0.0255  0.0734  0.0176  188 HOH B O   
2814 O  O   . HOH H .   ? 0.2576 0.3614 0.5839 0.0139  0.0181  0.0607  189 HOH B O   
2815 O  O   . HOH H .   ? 0.4189 0.3637 0.5250 -0.0502 0.1761  0.0395  190 HOH B O   
2816 O  O   . HOH H .   ? 0.3668 0.5121 0.4881 0.1193  0.1314  -0.0330 191 HOH B O   
2817 O  O   . HOH H .   ? 0.5244 0.3695 0.3183 0.1027  0.0055  0.0936  192 HOH B O   
2818 O  O   . HOH H .   ? 0.4522 0.6116 0.3914 0.1181  -0.1442 -0.0983 193 HOH B O   
2819 O  O   . HOH H .   ? 0.5345 0.3061 0.4966 0.1225  -0.0043 -0.0394 194 HOH B O   
2820 O  O   . HOH H .   ? 0.4831 0.6480 0.6598 -0.0940 0.2052  0.0804  195 HOH B O   
2821 O  O   . HOH H .   ? 0.5745 0.3966 0.3504 0.0627  -0.0291 0.0188  196 HOH B O   
2822 O  O   . HOH H .   ? 0.5989 0.4696 0.4568 -0.1280 0.0356  0.1068  197 HOH B O   
2823 O  O   . HOH H .   ? 0.2116 0.4778 0.5099 -0.0871 0.0102  0.0053  198 HOH B O   
2824 O  O   . HOH H .   ? 0.5444 0.3345 0.4553 -0.0137 0.0182  0.0106  199 HOH B O   
2825 O  O   . HOH H .   ? 0.5527 0.3826 0.6070 0.0020  -0.1328 0.0066  200 HOH B O   
2826 O  O   . HOH H .   ? 0.7274 0.4705 0.6163 -0.0836 -0.0823 -0.0410 201 HOH B O   
2827 O  O   . HOH H .   ? 0.4268 0.5798 0.3602 0.0565  0.1086  0.0722  202 HOH B O   
2828 O  O   . HOH H .   ? 0.4894 0.5682 0.3856 -0.1295 0.1262  -0.1073 203 HOH B O   
2829 O  O   . HOH H .   ? 0.5111 0.7573 0.4831 -0.0528 0.0560  -0.0903 204 HOH B O   
2830 O  O   . HOH H .   ? 0.4756 0.4120 0.4467 -0.0189 -0.0543 0.1703  205 HOH B O   
2831 O  O   . HOH H .   ? 0.3387 0.5760 0.4341 0.0054  -0.0150 0.0818  206 HOH B O   
2832 O  O   . HOH H .   ? 0.8389 0.7824 0.8028 -0.0092 0.0172  0.0323  207 HOH B O   
2833 O  O   . HOH H .   ? 0.8300 0.6885 0.7665 -0.0240 -0.0679 0.0985  208 HOH B O   
2834 O  O   . HOH H .   ? 0.5274 0.4447 0.4605 0.1292  -0.0166 0.0047  209 HOH B O   
2835 O  O   . HOH H .   ? 0.2241 0.5797 0.6001 -0.1074 -0.0557 0.0844  210 HOH B O   
2836 O  O   . HOH H .   ? 0.5136 0.2944 0.7071 0.1438  0.0514  -0.0509 211 HOH B O   
2837 O  O   . HOH H .   ? 0.6377 0.6296 0.4783 -0.0205 0.0218  0.1018  212 HOH B O   
2838 O  O   . HOH H .   ? 0.7357 0.4574 0.7360 0.2323  -0.0661 0.1606  213 HOH B O   
2839 O  O   . HOH H .   ? 0.3993 0.5585 0.6504 -0.0868 0.0681  -0.0961 214 HOH B O   
2840 O  O   . HOH H .   ? 0.6148 0.5375 0.6679 0.0183  0.0720  0.1160  215 HOH B O   
2841 O  O   . HOH H .   ? 0.7304 0.6650 0.7647 0.0429  0.1726  0.1417  216 HOH B O   
2842 O  O   . HOH H .   ? 0.7115 0.7518 0.5922 -0.0735 0.1348  -0.1072 217 HOH B O   
2843 O  O   . HOH H .   ? 0.6806 0.5155 0.3424 -0.0349 -0.1923 0.0066  218 HOH B O   
2844 O  O   . HOH H .   ? 0.3025 0.5536 0.4096 -0.0395 -0.0390 0.0338  219 HOH B O   
2845 O  O   . HOH H .   ? 0.5015 0.5889 0.3808 -0.1617 0.0825  0.0020  220 HOH B O   
2846 O  O   . HOH H .   ? 0.7570 0.3412 0.5339 -0.0809 0.1396  -0.0155 221 HOH B O   
2847 O  O   . HOH H .   ? 0.4239 0.6938 0.5914 -0.0108 -0.1274 -0.0113 222 HOH B O   
2848 O  O   . HOH H .   ? 0.4701 0.7343 0.5505 -0.0297 0.0386  -0.1574 223 HOH B O   
2849 O  O   . HOH H .   ? 0.8483 0.5167 0.5519 0.0003  0.2382  -0.2588 224 HOH B O   
2850 O  O   . HOH H .   ? 0.3977 0.6117 0.7914 0.1321  -0.0347 -0.0045 225 HOH B O   
2851 O  O   . HOH H .   ? 0.4309 0.5705 0.7146 0.1971  -0.0253 0.0414  226 HOH B O   
2852 O  O   . HOH H .   ? 0.8429 0.5859 0.6147 -0.0131 0.0172  0.0927  227 HOH B O   
2853 O  O   . HOH H .   ? 1.2159 1.0954 1.0721 -0.0736 0.0335  0.0282  228 HOH B O   
2854 O  O   . HOH H .   ? 0.7127 0.7276 0.6475 -0.0137 0.0229  0.1313  229 HOH B O   
2855 O  O   . HOH H .   ? 0.6917 0.6163 0.4966 -0.1318 -0.2353 0.0196  230 HOH B O   
2856 O  O   . HOH H .   ? 0.4771 0.4771 0.7089 -0.0442 -0.0834 0.0216  231 HOH B O   
2857 O  O   . HOH H .   ? 0.5723 0.3867 0.4217 -0.0638 0.1787  0.0327  232 HOH B O   
2858 O  O   . HOH H .   ? 0.3616 0.5018 0.3330 0.1380  0.0074  0.0144  233 HOH B O   
2859 O  O   . HOH H .   ? 0.5441 0.8503 0.6664 -0.1202 0.0964  -0.0216 234 HOH B O   
2860 O  O   . HOH H .   ? 0.7524 0.4633 0.5642 0.0942  0.0163  -0.0527 235 HOH B O   
2861 O  O   . HOH H .   ? 0.3765 0.6033 0.5898 -0.1921 -0.1233 0.1310  236 HOH B O   
2862 O  O   . HOH H .   ? 0.7522 0.5251 0.5331 0.0963  0.3099  -0.0257 237 HOH B O   
2863 O  O   . HOH H .   ? 0.5563 0.5546 0.2873 -0.0668 -0.0626 -0.0705 238 HOH B O   
2864 O  O   . HOH H .   ? 0.4411 0.4283 0.3263 0.1711  0.1128  -0.1521 239 HOH B O   
2865 O  O   . HOH H .   ? 0.5013 0.5013 0.7372 0.1596  0.1190  -0.0427 240 HOH B O   
2866 O  O   . HOH H .   ? 0.6164 0.6577 0.6826 -0.0780 -0.0504 0.1350  241 HOH B O   
2867 O  O   . HOH H .   ? 0.5943 0.7506 0.8845 0.0797  0.0102  -0.0387 242 HOH B O   
2868 O  O   . HOH H .   ? 0.8036 0.8396 0.7783 0.0486  0.1820  -0.0286 243 HOH B O   
2869 O  O   . HOH H .   ? 0.5008 0.7479 0.7322 -0.0060 -0.2093 0.0359  244 HOH B O   
2870 O  O   . HOH H .   ? 0.4508 0.2501 0.2464 -0.1249 0.1355  -0.0300 245 HOH B O   
2871 O  O   . HOH H .   ? 0.3331 0.3335 0.2493 -0.0225 0.0647  0.0321  246 HOH B O   
2872 O  O   . HOH H .   ? 0.5439 0.3995 0.3540 -0.1219 0.1630  0.0193  247 HOH B O   
2873 O  O   . HOH H .   ? 0.3315 0.2655 0.4460 -0.0312 0.1364  -0.1317 248 HOH B O   
2874 O  O   . HOH H .   ? 0.3103 0.3981 0.4143 0.0302  -0.0729 0.0048  249 HOH B O   
2875 O  O   . HOH H .   ? 0.4154 0.3571 0.2950 -0.1429 0.0908  -0.0485 250 HOH B O   
2876 O  O   . HOH H .   ? 0.4738 0.2745 0.4019 -0.1867 0.0606  -0.0361 251 HOH B O   
2877 O  O   . HOH H .   ? 0.4234 0.2647 0.6723 -0.1400 0.1230  -0.0814 252 HOH B O   
2878 O  O   . HOH H .   ? 0.7151 0.7458 0.5222 -0.1947 0.1077  -0.0134 253 HOH B O   
2879 O  O   . HOH H .   ? 0.5623 0.8561 0.7946 0.1445  0.3760  -0.2639 254 HOH B O   
2880 O  O   . HOH H .   ? 0.7565 0.7015 0.5579 0.0005  -0.1554 0.1551  255 HOH B O   
2881 O  O   . HOH H .   ? 0.6184 0.4199 0.5697 0.0637  0.0868  -0.1570 256 HOH B O   
2882 O  O   . HOH H .   ? 0.3603 0.5871 0.6507 0.0246  -0.1651 -0.1351 257 HOH B O   
2883 O  O   . HOH H .   ? 0.7386 0.9578 0.8418 -0.1339 -0.1162 0.0351  259 HOH B O   
2884 O  O   . HOH H .   ? 0.2799 0.4542 0.2717 0.0126  0.0768  -0.0195 260 HOH B O   
2885 O  O   . HOH H .   ? 0.6893 0.6116 0.8422 0.1887  -0.0176 -0.0785 261 HOH B O   
2886 O  O   . HOH H .   ? 0.2454 0.7428 0.7477 -0.0080 -0.0168 0.0843  262 HOH B O   
2887 O  O   . HOH H .   ? 0.4630 0.6040 0.5487 0.0214  -0.2010 0.1795  263 HOH B O   
2888 O  O   . HOH H .   ? 0.7402 0.9213 0.9096 0.0300  -0.0530 -0.0093 264 HOH B O   
2889 O  O   . HOH H .   ? 0.5403 0.4678 0.6857 0.2048  0.0693  -0.1025 265 HOH B O   
2890 O  O   . HOH H .   ? 0.6826 0.8241 0.7162 -0.0522 0.3968  -0.1826 266 HOH B O   
2891 O  O   . HOH H .   ? 0.6101 0.6298 0.8396 0.2032  0.2045  -0.0206 267 HOH B O   
2892 O  O   . HOH H .   ? 0.5859 0.6273 0.6707 0.0896  -0.1167 -0.1331 269 HOH B O   
2893 O  O   . HOH H .   ? 0.3825 0.7662 0.6255 -0.1209 0.1464  -0.0394 270 HOH B O   
2894 O  O   . HOH H .   ? 0.8428 0.7712 0.6277 -0.1547 0.0218  -0.1564 271 HOH B O   
2895 O  O   . HOH H .   ? 0.7686 0.6988 0.6936 -0.0458 0.1259  0.0201  272 HOH B O   
2896 O  O   . HOH H .   ? 0.7627 0.7595 0.7977 0.1296  -0.1414 0.0552  273 HOH B O   
2897 O  O   . HOH H .   ? 0.7672 0.5596 0.5733 -0.1812 0.0970  0.0172  274 HOH B O   
2898 O  O   . HOH H .   ? 0.5568 0.5580 0.7274 -0.0187 -0.2882 0.0061  275 HOH B O   
2899 O  O   . HOH H .   ? 0.6919 0.5816 0.5283 -0.2183 -0.0085 0.0020  276 HOH B O   
2900 O  O   . HOH H .   ? 0.5696 0.5628 0.8485 0.1374  -0.0909 0.1405  277 HOH B O   
2901 O  O   . HOH H .   ? 0.5988 0.6336 0.6555 0.0930  0.0654  0.0213  278 HOH B O   
2902 O  O   . HOH I .   ? 0.8625 0.5710 0.7174 -0.0016 0.0608  0.0729  113 HOH C O   
2903 O  O   . HOH I .   ? 0.6021 0.6140 0.4743 -0.0429 0.0610  0.0278  114 HOH C O   
2904 O  O   . HOH I .   ? 0.7014 0.8665 0.6866 -0.1729 0.1487  -0.0980 115 HOH C O   
2905 O  O   . HOH I .   ? 0.6462 0.3317 0.4767 -0.0759 0.0674  0.1489  116 HOH C O   
2906 O  O   . HOH I .   ? 0.6970 0.4770 0.4637 -0.0842 0.1481  0.0359  117 HOH C O   
2907 O  O   . HOH I .   ? 0.6519 0.5376 0.6606 0.0228  0.0863  -0.0561 118 HOH C O   
2908 O  O   . HOH I .   ? 0.1469 0.2845 0.1122 -0.0239 -0.0446 0.0460  119 HOH C O   
2909 O  O   . HOH I .   ? 0.2117 0.1852 0.1526 -0.0035 0.0181  0.0033  120 HOH C O   
2910 O  O   . HOH I .   ? 0.1614 0.2160 0.1159 -0.0083 0.0099  0.0480  121 HOH C O   
2911 O  O   . HOH I .   ? 0.1759 0.3253 0.1617 -0.0080 -0.0128 0.0399  122 HOH C O   
2912 O  O   . HOH I .   ? 0.1629 0.2477 0.2242 0.0262  -0.0146 0.0545  123 HOH C O   
2913 O  O   . HOH I .   ? 0.1574 0.3017 0.2189 -0.0003 -0.0149 0.0204  124 HOH C O   
2914 O  O   . HOH I .   ? 0.1560 0.2555 0.1660 0.0456  -0.0389 -0.0260 125 HOH C O   
2915 O  O   . HOH I .   ? 0.1843 0.5466 0.1271 -0.0717 -0.0219 0.0279  126 HOH C O   
2916 O  O   . HOH I .   ? 0.1086 0.2139 0.2340 0.0109  -0.0169 0.0140  127 HOH C O   
2917 O  O   . HOH I .   ? 0.3031 0.3939 0.1920 -0.1013 0.0473  -0.0045 128 HOH C O   
2918 O  O   . HOH I .   ? 0.2683 0.2370 0.2073 0.0310  0.0982  -0.0047 129 HOH C O   
2919 O  O   . HOH I .   ? 0.4089 0.7297 0.8242 0.1022  0.0526  0.0136  130 HOH C O   
2920 O  O   . HOH I .   ? 0.2057 0.3608 0.2536 0.0040  0.0009  -0.0374 131 HOH C O   
2921 O  O   . HOH I .   ? 0.3820 0.5915 0.4523 -0.1184 0.0208  -0.1270 132 HOH C O   
2922 O  O   . HOH I .   ? 0.2689 0.4185 0.2397 0.1219  -0.0589 -0.0322 133 HOH C O   
2923 O  O   . HOH I .   ? 0.3317 0.6748 0.4455 -0.0485 0.0048  -0.1172 134 HOH C O   
2924 O  O   . HOH I .   ? 0.5270 0.2480 0.2209 0.0640  0.0638  0.0816  135 HOH C O   
2925 O  O   . HOH I .   ? 0.4680 0.5026 0.6013 -0.1636 -0.0318 0.1458  136 HOH C O   
2926 O  O   . HOH I .   ? 0.1306 0.3256 0.2229 0.0333  -0.0012 -0.0112 137 HOH C O   
2927 O  O   . HOH I .   ? 0.2506 0.3289 0.2570 -0.0352 0.0210  0.0454  138 HOH C O   
2928 O  O   . HOH I .   ? 0.1174 0.2209 0.1163 0.0116  -0.0292 -0.0274 139 HOH C O   
2929 O  O   . HOH I .   ? 0.2536 0.2002 0.3311 0.0056  -0.1380 0.0494  140 HOH C O   
2930 O  O   . HOH I .   ? 0.2255 0.5733 0.3256 -0.0053 -0.0483 0.1314  141 HOH C O   
2931 O  O   . HOH I .   ? 0.4727 0.2682 0.2571 -0.0645 0.0100  -0.0191 142 HOH C O   
2932 O  O   . HOH I .   ? 0.2631 0.3742 0.2955 -0.0144 -0.0956 0.0404  143 HOH C O   
2933 O  O   . HOH I .   ? 0.3404 0.2590 0.2154 0.0372  -0.0149 -0.0391 144 HOH C O   
2934 O  O   . HOH I .   ? 0.2839 0.2959 0.3596 0.0052  -0.0131 -0.0615 145 HOH C O   
2935 O  O   . HOH I .   ? 0.2520 0.3909 0.3670 0.0771  0.1180  0.0132  146 HOH C O   
2936 O  O   . HOH I .   ? 0.4065 0.3670 0.3995 0.1159  -0.1090 -0.0242 147 HOH C O   
2937 O  O   . HOH I .   ? 0.4388 0.8213 0.6188 0.0005  0.3508  -0.1891 148 HOH C O   
2938 O  O   . HOH I .   ? 0.1708 0.5569 0.2417 0.0723  0.0058  -0.0666 149 HOH C O   
2939 O  O   . HOH I .   ? 0.3831 0.2605 0.1988 0.0611  -0.0268 -0.0133 150 HOH C O   
2940 O  O   . HOH I .   ? 0.3981 0.4489 0.2373 0.0874  0.0456  0.0987  151 HOH C O   
2941 O  O   . HOH I .   ? 0.6614 0.7978 0.7023 -0.1224 -0.1629 0.0739  152 HOH C O   
2942 O  O   . HOH I .   ? 0.2138 0.3984 0.1321 0.0099  0.0511  0.0051  153 HOH C O   
2943 O  O   . HOH I .   ? 0.2333 0.3743 0.1284 0.0368  -0.0097 0.0458  154 HOH C O   
2944 O  O   . HOH I .   ? 0.3243 0.4461 0.1702 -0.0402 0.0020  0.0320  155 HOH C O   
2945 O  O   . HOH I .   ? 0.3214 0.2655 0.1995 -0.0352 -0.0262 0.0548  156 HOH C O   
2946 O  O   . HOH I .   ? 0.2686 0.4470 0.4841 0.0242  0.0180  0.0272  157 HOH C O   
2947 O  O   . HOH I .   ? 0.4305 0.4548 0.3306 0.0358  -0.2102 0.0574  158 HOH C O   
2948 O  O   . HOH I .   ? 0.3812 0.2654 0.2556 0.0945  -0.0167 -0.0239 159 HOH C O   
2949 O  O   . HOH I .   ? 0.2628 0.2216 0.1542 0.0393  0.0217  -0.0036 160 HOH C O   
2950 O  O   . HOH I .   ? 0.6905 0.5028 0.6729 0.0434  -0.0344 -0.0882 161 HOH C O   
2951 O  O   . HOH I .   ? 0.2182 0.2904 0.1565 0.0612  0.0397  -0.0288 162 HOH C O   
2952 O  O   . HOH I .   ? 0.3183 0.4196 0.4550 -0.0476 0.0138  -0.1122 163 HOH C O   
2953 O  O   . HOH I .   ? 0.2351 0.3513 0.3550 -0.0021 0.0504  -0.0880 164 HOH C O   
2954 O  O   . HOH I .   ? 0.3226 0.3535 0.4130 -0.0208 0.2134  -0.0537 165 HOH C O   
2955 O  O   . HOH I .   ? 0.4771 0.3732 0.6078 0.1175  0.1886  -0.1244 166 HOH C O   
2956 O  O   . HOH I .   ? 0.3464 0.3738 0.3107 0.0749  -0.0016 0.1111  167 HOH C O   
2957 O  O   . HOH I .   ? 0.3583 0.3115 0.3963 0.1300  -0.0597 0.0787  168 HOH C O   
2958 O  O   . HOH I .   ? 0.3902 0.3303 0.4160 -0.1106 0.2161  -0.1476 169 HOH C O   
2959 O  O   . HOH I .   ? 0.2830 0.7075 0.7338 -0.0538 0.2597  0.0097  170 HOH C O   
2960 O  O   . HOH I .   ? 0.4897 0.3495 0.3263 -0.0277 -0.1101 0.0017  171 HOH C O   
2961 O  O   . HOH I .   ? 0.5389 0.3576 0.5233 -0.0047 0.1009  0.1537  172 HOH C O   
2962 O  O   . HOH I .   ? 0.4558 0.4025 0.4772 -0.0271 -0.1178 -0.1070 173 HOH C O   
2963 O  O   . HOH I .   ? 0.3003 0.3967 0.3147 0.1033  0.1025  0.1340  174 HOH C O   
2964 O  O   . HOH I .   ? 0.4284 0.3668 0.4986 0.0904  0.0254  0.1581  175 HOH C O   
2965 O  O   . HOH I .   ? 0.6409 0.6065 0.4261 0.0300  0.0048  0.1622  176 HOH C O   
2966 O  O   . HOH I .   ? 0.6267 0.6485 0.6609 -0.0847 -0.1941 0.1764  177 HOH C O   
2967 O  O   . HOH I .   ? 0.2834 0.4780 0.2488 -0.1031 0.0977  -0.0063 178 HOH C O   
2968 O  O   . HOH I .   ? 0.5108 0.3493 0.2445 -0.0991 0.0275  0.0109  179 HOH C O   
2969 O  O   . HOH I .   ? 0.4785 0.4676 0.2442 0.0284  0.0447  0.0704  180 HOH C O   
2970 O  O   . HOH I .   ? 0.4039 0.4824 0.3881 -0.0500 0.0497  0.1562  181 HOH C O   
2971 O  O   . HOH I .   ? 0.6024 0.2960 0.3546 0.0362  -0.0662 -0.0771 182 HOH C O   
2972 O  O   . HOH I .   ? 0.5542 0.5262 0.6087 -0.0719 0.0497  -0.0957 183 HOH C O   
2973 O  O   . HOH I .   ? 0.7046 0.5502 0.3198 -0.1131 0.1682  0.0353  184 HOH C O   
2974 O  O   . HOH I .   ? 0.3807 0.5004 0.3984 -0.2150 -0.0551 0.1531  185 HOH C O   
2975 O  O   . HOH I .   ? 0.4558 0.4915 0.3285 0.1125  -0.0570 0.0667  186 HOH C O   
2976 O  O   . HOH I .   ? 0.6239 0.3865 0.4384 0.1073  0.0068  0.0839  187 HOH C O   
2977 O  O   . HOH I .   ? 0.5212 0.4796 0.3766 -0.1625 -0.1347 -0.0326 188 HOH C O   
2978 O  O   . HOH I .   ? 0.5878 0.6278 0.6280 -0.0613 -0.1571 -0.0535 189 HOH C O   
2979 O  O   . HOH I .   ? 0.4965 0.3086 0.5093 -0.0018 0.0070  0.1572  190 HOH C O   
2980 O  O   . HOH I .   ? 0.7065 0.4778 0.5111 0.0636  0.1510  0.0225  191 HOH C O   
2981 O  O   . HOH I .   ? 0.6933 0.3771 0.2325 0.0062  -0.1028 -0.0463 192 HOH C O   
2982 O  O   . HOH I .   ? 0.4957 0.7765 0.6117 -0.1305 -0.0505 0.1373  193 HOH C O   
2983 O  O   . HOH I .   ? 0.6195 0.4236 0.3507 -0.0202 -0.0009 0.0650  194 HOH C O   
2984 O  O   . HOH I .   ? 0.6545 0.2653 0.4021 -0.0484 -0.1401 0.1153  195 HOH C O   
2985 O  O   . HOH I .   ? 0.4219 0.3564 0.7537 0.0769  -0.0191 -0.0124 196 HOH C O   
2986 O  O   . HOH I .   ? 0.5682 0.4240 0.3817 0.1278  0.2125  0.0246  197 HOH C O   
2987 O  O   . HOH I .   ? 0.6705 0.6595 0.5518 -0.0477 0.1739  0.0777  198 HOH C O   
2988 O  O   . HOH I .   ? 0.6107 0.4538 0.5029 -0.0938 -0.2456 -0.0082 199 HOH C O   
2989 O  O   . HOH I .   ? 0.3448 0.5515 0.4118 -0.0233 -0.0175 0.0445  200 HOH C O   
2990 O  O   . HOH I .   ? 0.3927 0.5476 0.8165 0.0394  0.1427  0.0281  201 HOH C O   
2991 O  O   . HOH I .   ? 0.4651 0.4347 0.5997 -0.0575 0.0983  0.0523  202 HOH C O   
2992 O  O   . HOH I .   ? 0.4784 0.5163 0.6846 0.0758  -0.0114 -0.0362 203 HOH C O   
2993 O  O   . HOH I .   ? 0.4031 0.6909 0.4976 0.0459  0.2130  -0.0567 204 HOH C O   
2994 O  O   . HOH I .   ? 0.5757 0.6761 0.6981 0.1059  0.0399  -0.1007 205 HOH C O   
2995 O  O   . HOH I .   ? 0.4779 0.4032 0.5734 0.0538  -0.0907 0.0690  206 HOH C O   
2996 O  O   . HOH I .   ? 0.7428 0.4544 0.8255 0.0958  -0.0078 0.1151  207 HOH C O   
2997 O  O   . HOH I .   ? 0.3336 0.3000 0.3878 0.0529  -0.1342 -0.0319 208 HOH C O   
2998 O  O   . HOH I .   ? 0.2433 0.3884 0.4708 0.0247  0.0920  0.1074  209 HOH C O   
2999 O  O   . HOH I .   ? 0.7444 0.2705 0.3912 0.0263  0.0123  -0.0045 210 HOH C O   
3000 O  O   . HOH I .   ? 0.4033 0.5058 0.2926 0.1751  -0.0893 -0.0183 211 HOH C O   
3001 O  O   . HOH I .   ? 0.5349 0.3919 0.4326 -0.0604 -0.0128 0.0501  212 HOH C O   
3002 O  O   . HOH I .   ? 0.5152 0.2839 0.6775 -0.0069 0.0128  -0.0297 213 HOH C O   
3003 O  O   . HOH I .   ? 0.4514 0.4854 0.3698 -0.0548 -0.0654 0.1852  214 HOH C O   
3004 O  O   . HOH I .   ? 0.6360 0.5609 0.6304 -0.0281 -0.2366 0.0831  215 HOH C O   
3005 O  O   . HOH I .   ? 0.3758 0.5287 0.3986 0.0640  0.0364  0.1183  216 HOH C O   
3006 O  O   . HOH I .   ? 0.4164 0.4177 0.4880 0.0563  -0.0235 0.0725  217 HOH C O   
3007 O  O   . HOH I .   ? 0.5829 0.4966 0.4233 -0.1167 0.1523  -0.0493 218 HOH C O   
3008 O  O   . HOH I .   ? 0.3596 0.4004 0.3699 -0.0378 -0.0899 -0.0186 219 HOH C O   
3009 O  O   . HOH I .   ? 0.3628 0.4907 0.5689 -0.1102 -0.0445 0.1062  220 HOH C O   
3010 O  O   . HOH I .   ? 0.6044 0.4873 0.4677 0.0898  0.0256  -0.0603 221 HOH C O   
3011 O  O   . HOH I .   ? 0.3438 0.5018 0.3874 0.1219  0.1004  0.2154  222 HOH C O   
3012 O  O   . HOH I .   ? 0.4407 0.4795 0.3578 0.1239  -0.0890 0.0227  223 HOH C O   
3013 O  O   . HOH I .   ? 0.4045 0.5248 0.6411 -0.0601 0.1246  -0.0496 224 HOH C O   
3014 O  O   . HOH I .   ? 0.6903 0.5336 0.4564 -0.0570 0.0757  0.1199  225 HOH C O   
3015 O  O   . HOH I .   ? 0.4976 0.4515 0.3967 0.1082  -0.1607 -0.0571 226 HOH C O   
3016 O  O   . HOH I .   ? 0.6849 0.5858 0.7316 -0.0230 -0.1687 0.0797  227 HOH C O   
3017 O  O   . HOH I .   ? 0.6695 0.5224 0.5374 0.0409  0.2491  0.0317  228 HOH C O   
3018 O  O   . HOH I .   ? 0.5465 0.5846 0.7442 -0.0299 0.0669  -0.0115 229 HOH C O   
3019 O  O   . HOH I .   ? 0.4035 0.7974 0.7275 -0.2637 -0.0315 0.0948  230 HOH C O   
3020 O  O   . HOH I .   ? 0.5515 0.5280 0.6149 -0.0577 -0.0134 -0.0735 231 HOH C O   
3021 O  O   . HOH I .   ? 0.3198 0.7632 0.5685 0.1752  0.1893  -0.0096 232 HOH C O   
3022 O  O   . HOH I .   ? 0.6633 0.5169 0.5650 0.0662  -0.0389 0.2120  233 HOH C O   
3023 O  O   . HOH I .   ? 0.5281 0.6288 0.6528 0.2284  0.0180  0.0935  234 HOH C O   
3024 O  O   . HOH I .   ? 0.5960 0.6488 0.8020 0.1347  0.0800  -0.0487 235 HOH C O   
3025 O  O   . HOH I .   ? 0.6168 0.5404 0.5594 -0.0379 -0.0277 0.0322  236 HOH C O   
3026 O  O   . HOH I .   ? 0.3322 0.6036 0.4112 0.0522  -0.0081 -0.2540 237 HOH C O   
3027 O  O   . HOH I .   ? 0.4738 0.7388 0.7608 0.0365  -0.1673 0.0755  238 HOH C O   
3028 O  O   . HOH I .   ? 0.6496 0.4244 0.3657 0.0344  -0.1893 0.0727  239 HOH C O   
3029 O  O   . HOH I .   ? 0.4548 0.4946 0.4943 -0.0970 0.0082  0.1110  240 HOH C O   
3030 O  O   . HOH I .   ? 0.3543 0.7959 0.4766 0.0218  -0.1505 -0.0249 241 HOH C O   
3031 O  O   . HOH I .   ? 0.7510 0.4641 0.4791 -0.2231 -0.0419 -0.1466 242 HOH C O   
3032 O  O   . HOH I .   ? 0.8802 0.8356 0.8877 -0.0069 0.0000  -0.0287 243 HOH C O   
3033 O  O   . HOH I .   ? 0.5318 0.8126 0.6898 -0.0878 -0.2467 0.0263  244 HOH C O   
3034 O  O   . HOH I .   ? 0.4083 0.5415 0.4808 -0.1244 -0.0384 0.1195  245 HOH C O   
3035 O  O   . HOH I .   ? 0.9612 0.9821 0.9849 0.0625  0.2046  -0.1330 246 HOH C O   
3036 O  O   . HOH I .   ? 0.7159 0.7330 0.6759 -0.1157 0.0427  -0.0209 247 HOH C O   
3037 O  O   . HOH I .   ? 0.6615 0.5603 0.7041 -0.0553 0.2291  -0.2148 248 HOH C O   
3038 O  O   . HOH I .   ? 0.8455 0.4209 0.6391 -0.1165 -0.0394 0.0282  249 HOH C O   
3039 O  O   . HOH I .   ? 0.9818 0.8998 0.9234 -0.0195 -0.0435 0.0164  250 HOH C O   
3040 O  O   . HOH I .   ? 0.6194 0.4068 0.4869 -0.0374 0.1090  0.0394  251 HOH C O   
3041 O  O   . HOH I .   ? 0.7330 0.6979 0.5884 -0.1144 -0.0660 0.0694  252 HOH C O   
3042 O  O   . HOH I .   ? 0.5717 0.4352 0.5999 -0.1258 0.0486  -0.0212 253 HOH C O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   ?   ?   ?   A . n 
A 1 2   GLN 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ASN 5   5   5   ASN ASN A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  TYR 13  13  13  TYR TYR A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  TRP 35  35  35  TRP TRP A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  ASN 41  41  41  ASN ASN A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  TRP 71  71  71  TRP TRP A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 HIS 102 102 102 HIS HIS A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
B 1 1   ALA 1   1   ?   ?   ?   B . n 
B 1 2   GLN 2   2   ?   ?   ?   B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   ASN 5   5   5   ASN ASN B . n 
B 1 6   THR 6   6   6   THR THR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   ASP 8   8   8   ASP ASP B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  TYR 13  13  13  TYR TYR B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  THR 16  16  16  THR THR B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  HIS 18  18  18  HIS HIS B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  GLU 29  29  29  GLU GLU B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  GLN 31  31  31  GLN GLN B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  TRP 35  35  35  TRP TRP B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  GLY 40  40  40  GLY GLY B . n 
B 1 41  ASN 41  41  41  ASN ASN B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  PRO 47  47  47  PRO PRO B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  LYS 49  49  49  LYS LYS B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  PHE 56  56  56  PHE PHE B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ARG 59  59  59  ARG ARG B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  LYS 62  62  62  LYS LYS B . n 
B 1 63  LEU 63  63  63  LEU LEU B . n 
B 1 64  PRO 64  64  64  PRO PRO B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  LYS 66  66  66  LYS LYS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  TRP 71  71  71  TRP TRP B . n 
B 1 72  ARG 72  72  72  ARG ARG B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  PHE 82  82  82  PHE PHE B . n 
B 1 83  ARG 83  83  83  ARG ARG B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  ILE 88  88  88  ILE ILE B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  TYR 90  90  90  TYR TYR B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  SER 92  92  92  SER SER B . n 
B 1 93  ASP 93  93  93  ASP ASP B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  TYR 97  97  97  TYR TYR B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 HIS 102 102 102 HIS HIS B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLN 104 104 104 GLN GLN B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 PHE 106 106 106 PHE PHE B . n 
B 1 107 THR 107 107 107 THR THR B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 ARG 110 110 110 ARG ARG B . n 
C 1 1   ALA 1   1   ?   ?   ?   C . n 
C 1 2   GLN 2   2   ?   ?   ?   C . n 
C 1 3   VAL 3   3   3   VAL VAL C . n 
C 1 4   ILE 4   4   4   ILE ILE C . n 
C 1 5   ASN 5   5   5   ASN ASN C . n 
C 1 6   THR 6   6   6   THR THR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   ASP 8   8   8   ASP ASP C . n 
C 1 9   GLY 9   9   9   GLY GLY C . n 
C 1 10  VAL 10  10  10  VAL VAL C . n 
C 1 11  ALA 11  11  11  ALA ALA C . n 
C 1 12  ASP 12  12  12  ASP ASP C . n 
C 1 13  TYR 13  13  13  TYR TYR C . n 
C 1 14  LEU 14  14  14  LEU LEU C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  THR 16  16  16  THR THR C . n 
C 1 17  TYR 17  17  17  TYR TYR C . n 
C 1 18  HIS 18  18  18  HIS HIS C . n 
C 1 19  LYS 19  19  19  LYS LYS C . n 
C 1 20  LEU 20  20  20  LEU LEU C . n 
C 1 21  PRO 21  21  21  PRO PRO C . n 
C 1 22  ASP 22  22  22  ASP ASP C . n 
C 1 23  ASN 23  23  23  ASN ASN C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  ILE 25  25  25  ILE ILE C . n 
C 1 26  THR 26  26  26  THR THR C . n 
C 1 27  LYS 27  27  27  LYS LYS C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  GLU 29  29  29  GLU GLU C . n 
C 1 30  ALA 30  30  30  ALA ALA C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  ALA 32  32  32  ALA ALA C . n 
C 1 33  LEU 33  33  33  LEU LEU C . n 
C 1 34  GLY 34  34  34  GLY GLY C . n 
C 1 35  TRP 35  35  35  TRP TRP C . n 
C 1 36  VAL 36  36  36  VAL VAL C . n 
C 1 37  ALA 37  37  37  ALA ALA C . n 
C 1 38  SER 38  38  38  SER SER C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  GLY 40  40  40  GLY GLY C . n 
C 1 41  ASN 41  41  41  ASN ASN C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  ASP 44  44  44  ASP ASP C . n 
C 1 45  VAL 45  45  45  VAL VAL C . n 
C 1 46  ALA 46  46  46  ALA ALA C . n 
C 1 47  PRO 47  47  47  PRO PRO C . n 
C 1 48  GLY 48  48  48  GLY GLY C . n 
C 1 49  LYS 49  49  49  LYS LYS C . n 
C 1 50  SER 50  50  50  SER SER C . n 
C 1 51  ILE 51  51  51  ILE ILE C . n 
C 1 52  GLY 52  52  52  GLY GLY C . n 
C 1 53  GLY 53  53  53  GLY GLY C . n 
C 1 54  ASP 54  54  54  ASP ASP C . n 
C 1 55  ILE 55  55  55  ILE ILE C . n 
C 1 56  PHE 56  56  56  PHE PHE C . n 
C 1 57  SER 57  57  57  SER SER C . n 
C 1 58  ASN 58  58  58  ASN ASN C . n 
C 1 59  ARG 59  59  59  ARG ARG C . n 
C 1 60  GLU 60  60  60  GLU GLU C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  LYS 62  62  62  LYS LYS C . n 
C 1 63  LEU 63  63  63  LEU LEU C . n 
C 1 64  PRO 64  64  64  PRO PRO C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  LYS 66  66  66  LYS LYS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  THR 70  70  70  THR THR C . n 
C 1 71  TRP 71  71  71  TRP TRP C . n 
C 1 72  ARG 72  72  72  ARG ARG C . n 
C 1 73  GLU 73  73  73  GLU GLU C . n 
C 1 74  ALA 74  74  74  ALA ALA C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  ILE 76  76  76  ILE ILE C . n 
C 1 77  ASN 77  77  77  ASN ASN C . n 
C 1 78  TYR 78  78  78  TYR TYR C . n 
C 1 79  THR 79  79  79  THR THR C . n 
C 1 80  SER 80  80  80  SER SER C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  PHE 82  82  82  PHE PHE C . n 
C 1 83  ARG 83  83  83  ARG ARG C . n 
C 1 84  ASN 84  84  84  ASN ASN C . n 
C 1 85  SER 85  85  85  SER SER C . n 
C 1 86  ASP 86  86  86  ASP ASP C . n 
C 1 87  ARG 87  87  87  ARG ARG C . n 
C 1 88  ILE 88  88  88  ILE ILE C . n 
C 1 89  LEU 89  89  89  LEU LEU C . n 
C 1 90  TYR 90  90  90  TYR TYR C . n 
C 1 91  SER 91  91  91  SER SER C . n 
C 1 92  SER 92  92  92  SER SER C . n 
C 1 93  ASP 93  93  93  ASP ASP C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  ILE 96  96  96  ILE ILE C . n 
C 1 97  TYR 97  97  97  TYR TYR C . n 
C 1 98  LYS 98  98  98  LYS LYS C . n 
C 1 99  THR 99  99  99  THR THR C . n 
C 1 100 THR 100 100 100 THR THR C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 HIS 102 102 102 HIS HIS C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 GLN 104 104 104 GLN GLN C . n 
C 1 105 THR 105 105 105 THR THR C . n 
C 1 106 PHE 106 106 106 PHE PHE C . n 
C 1 107 THR 107 107 107 THR THR C . n 
C 1 108 LYS 108 108 108 LYS LYS C . n 
C 1 109 ILE 109 109 109 ILE ILE C . n 
C 1 110 ARG 110 110 110 ARG ARG C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 ZN  1   112 112 ZN  ZN  A . 
E 2 ZN  1   112 112 ZN  ZN  B . 
F 2 ZN  1   112 112 ZN  ZN  C . 
G 3 HOH 1   113 1   HOH HOH A . 
G 3 HOH 2   114 2   HOH HOH A . 
G 3 HOH 3   115 3   HOH HOH A . 
G 3 HOH 4   116 4   HOH HOH A . 
G 3 HOH 5   117 5   HOH HOH A . 
G 3 HOH 6   118 6   HOH HOH A . 
G 3 HOH 7   119 7   HOH HOH A . 
G 3 HOH 8   120 8   HOH HOH A . 
G 3 HOH 9   121 9   HOH HOH A . 
G 3 HOH 10  122 10  HOH HOH A . 
G 3 HOH 11  123 11  HOH HOH A . 
G 3 HOH 12  124 12  HOH HOH A . 
G 3 HOH 13  125 13  HOH HOH A . 
G 3 HOH 14  126 14  HOH HOH A . 
G 3 HOH 15  127 15  HOH HOH A . 
G 3 HOH 16  128 16  HOH HOH A . 
G 3 HOH 17  129 17  HOH HOH A . 
G 3 HOH 18  130 18  HOH HOH A . 
G 3 HOH 19  131 19  HOH HOH A . 
G 3 HOH 20  132 20  HOH HOH A . 
G 3 HOH 21  133 21  HOH HOH A . 
G 3 HOH 22  134 22  HOH HOH A . 
G 3 HOH 23  135 23  HOH HOH A . 
G 3 HOH 24  136 24  HOH HOH A . 
G 3 HOH 25  137 25  HOH HOH A . 
G 3 HOH 26  138 26  HOH HOH A . 
G 3 HOH 27  139 27  HOH HOH A . 
G 3 HOH 28  140 29  HOH HOH A . 
G 3 HOH 29  141 30  HOH HOH A . 
G 3 HOH 30  142 31  HOH HOH A . 
G 3 HOH 31  143 32  HOH HOH A . 
G 3 HOH 32  144 33  HOH HOH A . 
G 3 HOH 33  145 34  HOH HOH A . 
G 3 HOH 34  146 35  HOH HOH A . 
G 3 HOH 35  147 36  HOH HOH A . 
G 3 HOH 36  148 37  HOH HOH A . 
G 3 HOH 37  149 38  HOH HOH A . 
G 3 HOH 38  150 39  HOH HOH A . 
G 3 HOH 39  151 40  HOH HOH A . 
G 3 HOH 40  152 41  HOH HOH A . 
G 3 HOH 41  153 42  HOH HOH A . 
G 3 HOH 42  154 43  HOH HOH A . 
G 3 HOH 43  155 44  HOH HOH A . 
G 3 HOH 44  156 45  HOH HOH A . 
G 3 HOH 45  157 46  HOH HOH A . 
G 3 HOH 46  158 47  HOH HOH A . 
G 3 HOH 47  159 48  HOH HOH A . 
G 3 HOH 48  160 49  HOH HOH A . 
G 3 HOH 49  161 50  HOH HOH A . 
G 3 HOH 50  162 51  HOH HOH A . 
G 3 HOH 51  163 52  HOH HOH A . 
G 3 HOH 52  164 53  HOH HOH A . 
G 3 HOH 53  165 54  HOH HOH A . 
G 3 HOH 54  166 55  HOH HOH A . 
G 3 HOH 55  167 56  HOH HOH A . 
G 3 HOH 56  168 57  HOH HOH A . 
G 3 HOH 57  169 58  HOH HOH A . 
G 3 HOH 58  170 59  HOH HOH A . 
G 3 HOH 59  171 60  HOH HOH A . 
G 3 HOH 60  172 61  HOH HOH A . 
G 3 HOH 61  173 62  HOH HOH A . 
G 3 HOH 62  174 63  HOH HOH A . 
G 3 HOH 63  175 64  HOH HOH A . 
G 3 HOH 64  176 65  HOH HOH A . 
G 3 HOH 65  177 66  HOH HOH A . 
G 3 HOH 66  178 67  HOH HOH A . 
G 3 HOH 67  179 68  HOH HOH A . 
G 3 HOH 68  180 69  HOH HOH A . 
G 3 HOH 69  181 70  HOH HOH A . 
G 3 HOH 70  182 71  HOH HOH A . 
G 3 HOH 71  183 72  HOH HOH A . 
G 3 HOH 72  184 73  HOH HOH A . 
G 3 HOH 73  185 74  HOH HOH A . 
G 3 HOH 74  186 75  HOH HOH A . 
G 3 HOH 75  187 76  HOH HOH A . 
G 3 HOH 76  188 77  HOH HOH A . 
G 3 HOH 77  189 78  HOH HOH A . 
G 3 HOH 78  190 79  HOH HOH A . 
G 3 HOH 79  191 80  HOH HOH A . 
G 3 HOH 80  192 81  HOH HOH A . 
G 3 HOH 81  193 82  HOH HOH A . 
G 3 HOH 82  194 83  HOH HOH A . 
G 3 HOH 83  195 84  HOH HOH A . 
G 3 HOH 84  196 85  HOH HOH A . 
G 3 HOH 85  197 86  HOH HOH A . 
G 3 HOH 86  198 87  HOH HOH A . 
G 3 HOH 87  199 88  HOH HOH A . 
G 3 HOH 88  200 89  HOH HOH A . 
G 3 HOH 89  201 90  HOH HOH A . 
G 3 HOH 90  202 91  HOH HOH A . 
G 3 HOH 91  203 92  HOH HOH A . 
G 3 HOH 92  204 93  HOH HOH A . 
G 3 HOH 93  205 94  HOH HOH A . 
G 3 HOH 94  206 95  HOH HOH A . 
G 3 HOH 95  207 96  HOH HOH A . 
G 3 HOH 96  208 97  HOH HOH A . 
G 3 HOH 97  209 98  HOH HOH A . 
G 3 HOH 98  210 99  HOH HOH A . 
G 3 HOH 99  211 100 HOH HOH A . 
G 3 HOH 100 212 101 HOH HOH A . 
G 3 HOH 101 213 102 HOH HOH A . 
G 3 HOH 102 214 104 HOH HOH A . 
G 3 HOH 103 215 105 HOH HOH A . 
G 3 HOH 104 216 106 HOH HOH A . 
G 3 HOH 105 217 107 HOH HOH A . 
G 3 HOH 106 218 108 HOH HOH A . 
G 3 HOH 107 219 109 HOH HOH A . 
G 3 HOH 108 220 110 HOH HOH A . 
G 3 HOH 109 221 111 HOH HOH A . 
G 3 HOH 110 222 112 HOH HOH A . 
G 3 HOH 111 223 113 HOH HOH A . 
G 3 HOH 112 224 114 HOH HOH A . 
G 3 HOH 113 225 115 HOH HOH A . 
G 3 HOH 114 226 118 HOH HOH A . 
G 3 HOH 115 227 120 HOH HOH A . 
G 3 HOH 116 228 121 HOH HOH A . 
G 3 HOH 117 229 122 HOH HOH A . 
G 3 HOH 118 230 123 HOH HOH A . 
G 3 HOH 119 231 124 HOH HOH A . 
G 3 HOH 120 232 125 HOH HOH A . 
G 3 HOH 121 233 126 HOH HOH A . 
G 3 HOH 122 234 127 HOH HOH A . 
G 3 HOH 123 235 128 HOH HOH A . 
G 3 HOH 124 236 129 HOH HOH A . 
G 3 HOH 125 237 130 HOH HOH A . 
G 3 HOH 126 238 131 HOH HOH A . 
G 3 HOH 127 239 132 HOH HOH A . 
G 3 HOH 128 240 133 HOH HOH A . 
G 3 HOH 129 241 134 HOH HOH A . 
G 3 HOH 130 242 135 HOH HOH A . 
G 3 HOH 131 243 136 HOH HOH A . 
G 3 HOH 132 244 132 HOH HOH A . 
G 3 HOH 133 245 34  HOH HOH A . 
G 3 HOH 134 246 132 HOH HOH A . 
H 3 HOH 1   137 1   HOH HOH B . 
H 3 HOH 2   138 2   HOH HOH B . 
H 3 HOH 3   139 3   HOH HOH B . 
H 3 HOH 4   140 4   HOH HOH B . 
H 3 HOH 5   141 5   HOH HOH B . 
H 3 HOH 6   142 6   HOH HOH B . 
H 3 HOH 7   143 7   HOH HOH B . 
H 3 HOH 8   144 8   HOH HOH B . 
H 3 HOH 9   145 9   HOH HOH B . 
H 3 HOH 10  146 10  HOH HOH B . 
H 3 HOH 11  147 11  HOH HOH B . 
H 3 HOH 12  148 12  HOH HOH B . 
H 3 HOH 13  149 13  HOH HOH B . 
H 3 HOH 14  150 14  HOH HOH B . 
H 3 HOH 15  151 15  HOH HOH B . 
H 3 HOH 16  152 16  HOH HOH B . 
H 3 HOH 17  153 17  HOH HOH B . 
H 3 HOH 18  154 18  HOH HOH B . 
H 3 HOH 19  155 19  HOH HOH B . 
H 3 HOH 20  156 20  HOH HOH B . 
H 3 HOH 21  157 21  HOH HOH B . 
H 3 HOH 22  158 22  HOH HOH B . 
H 3 HOH 23  159 23  HOH HOH B . 
H 3 HOH 24  160 24  HOH HOH B . 
H 3 HOH 25  161 25  HOH HOH B . 
H 3 HOH 26  162 26  HOH HOH B . 
H 3 HOH 27  163 27  HOH HOH B . 
H 3 HOH 28  164 28  HOH HOH B . 
H 3 HOH 29  165 29  HOH HOH B . 
H 3 HOH 30  166 30  HOH HOH B . 
H 3 HOH 31  167 31  HOH HOH B . 
H 3 HOH 32  168 32  HOH HOH B . 
H 3 HOH 33  169 33  HOH HOH B . 
H 3 HOH 34  170 34  HOH HOH B . 
H 3 HOH 35  171 35  HOH HOH B . 
H 3 HOH 36  172 36  HOH HOH B . 
H 3 HOH 37  173 37  HOH HOH B . 
H 3 HOH 38  174 38  HOH HOH B . 
H 3 HOH 39  175 39  HOH HOH B . 
H 3 HOH 40  176 40  HOH HOH B . 
H 3 HOH 41  177 41  HOH HOH B . 
H 3 HOH 42  178 42  HOH HOH B . 
H 3 HOH 43  179 43  HOH HOH B . 
H 3 HOH 44  180 44  HOH HOH B . 
H 3 HOH 45  181 45  HOH HOH B . 
H 3 HOH 46  182 46  HOH HOH B . 
H 3 HOH 47  183 47  HOH HOH B . 
H 3 HOH 48  184 48  HOH HOH B . 
H 3 HOH 49  185 49  HOH HOH B . 
H 3 HOH 50  186 50  HOH HOH B . 
H 3 HOH 51  187 51  HOH HOH B . 
H 3 HOH 52  188 52  HOH HOH B . 
H 3 HOH 53  189 53  HOH HOH B . 
H 3 HOH 54  190 54  HOH HOH B . 
H 3 HOH 55  191 55  HOH HOH B . 
H 3 HOH 56  192 56  HOH HOH B . 
H 3 HOH 57  193 57  HOH HOH B . 
H 3 HOH 58  194 58  HOH HOH B . 
H 3 HOH 59  195 59  HOH HOH B . 
H 3 HOH 60  196 60  HOH HOH B . 
H 3 HOH 61  197 61  HOH HOH B . 
H 3 HOH 62  198 62  HOH HOH B . 
H 3 HOH 63  199 63  HOH HOH B . 
H 3 HOH 64  200 64  HOH HOH B . 
H 3 HOH 65  201 65  HOH HOH B . 
H 3 HOH 66  202 66  HOH HOH B . 
H 3 HOH 67  203 67  HOH HOH B . 
H 3 HOH 68  204 68  HOH HOH B . 
H 3 HOH 69  205 69  HOH HOH B . 
H 3 HOH 70  206 70  HOH HOH B . 
H 3 HOH 71  207 71  HOH HOH B . 
H 3 HOH 72  208 72  HOH HOH B . 
H 3 HOH 73  209 73  HOH HOH B . 
H 3 HOH 74  210 74  HOH HOH B . 
H 3 HOH 75  211 75  HOH HOH B . 
H 3 HOH 76  212 76  HOH HOH B . 
H 3 HOH 77  213 77  HOH HOH B . 
H 3 HOH 78  214 78  HOH HOH B . 
H 3 HOH 79  215 79  HOH HOH B . 
H 3 HOH 80  216 80  HOH HOH B . 
H 3 HOH 81  217 81  HOH HOH B . 
H 3 HOH 82  218 82  HOH HOH B . 
H 3 HOH 83  219 83  HOH HOH B . 
H 3 HOH 84  220 84  HOH HOH B . 
H 3 HOH 85  221 85  HOH HOH B . 
H 3 HOH 86  222 86  HOH HOH B . 
H 3 HOH 87  223 87  HOH HOH B . 
H 3 HOH 88  224 88  HOH HOH B . 
H 3 HOH 89  225 89  HOH HOH B . 
H 3 HOH 90  226 90  HOH HOH B . 
H 3 HOH 91  227 91  HOH HOH B . 
H 3 HOH 92  228 92  HOH HOH B . 
H 3 HOH 93  229 93  HOH HOH B . 
H 3 HOH 94  230 94  HOH HOH B . 
H 3 HOH 95  231 95  HOH HOH B . 
H 3 HOH 96  232 96  HOH HOH B . 
H 3 HOH 97  233 97  HOH HOH B . 
H 3 HOH 98  234 98  HOH HOH B . 
H 3 HOH 99  235 99  HOH HOH B . 
H 3 HOH 100 236 100 HOH HOH B . 
H 3 HOH 101 237 101 HOH HOH B . 
H 3 HOH 102 238 102 HOH HOH B . 
H 3 HOH 103 239 103 HOH HOH B . 
H 3 HOH 104 240 104 HOH HOH B . 
H 3 HOH 105 241 105 HOH HOH B . 
H 3 HOH 106 242 106 HOH HOH B . 
H 3 HOH 107 243 107 HOH HOH B . 
H 3 HOH 108 244 108 HOH HOH B . 
H 3 HOH 109 245 109 HOH HOH B . 
H 3 HOH 110 246 110 HOH HOH B . 
H 3 HOH 111 247 111 HOH HOH B . 
H 3 HOH 112 248 112 HOH HOH B . 
H 3 HOH 113 249 113 HOH HOH B . 
H 3 HOH 114 250 114 HOH HOH B . 
H 3 HOH 115 251 115 HOH HOH B . 
H 3 HOH 116 252 116 HOH HOH B . 
H 3 HOH 117 253 117 HOH HOH B . 
H 3 HOH 118 254 118 HOH HOH B . 
H 3 HOH 119 255 119 HOH HOH B . 
H 3 HOH 120 256 120 HOH HOH B . 
H 3 HOH 121 257 121 HOH HOH B . 
H 3 HOH 122 259 123 HOH HOH B . 
H 3 HOH 123 260 124 HOH HOH B . 
H 3 HOH 124 261 125 HOH HOH B . 
H 3 HOH 125 262 126 HOH HOH B . 
H 3 HOH 126 263 127 HOH HOH B . 
H 3 HOH 127 264 128 HOH HOH B . 
H 3 HOH 128 265 129 HOH HOH B . 
H 3 HOH 129 266 130 HOH HOH B . 
H 3 HOH 130 267 131 HOH HOH B . 
H 3 HOH 131 269 133 HOH HOH B . 
H 3 HOH 132 270 134 HOH HOH B . 
H 3 HOH 133 271 135 HOH HOH B . 
H 3 HOH 134 272 136 HOH HOH B . 
H 3 HOH 135 273 137 HOH HOH B . 
H 3 HOH 136 274 138 HOH HOH B . 
H 3 HOH 137 275 139 HOH HOH B . 
H 3 HOH 138 276 140 HOH HOH B . 
H 3 HOH 139 277 141 HOH HOH B . 
H 3 HOH 140 278 142 HOH HOH B . 
I 3 HOH 1   113 28  HOH HOH C . 
I 3 HOH 2   114 103 HOH HOH C . 
I 3 HOH 3   115 116 HOH HOH C . 
I 3 HOH 4   116 117 HOH HOH C . 
I 3 HOH 5   117 119 HOH HOH C . 
I 3 HOH 6   118 122 HOH HOH C . 
I 3 HOH 7   119 1   HOH HOH C . 
I 3 HOH 8   120 2   HOH HOH C . 
I 3 HOH 9   121 3   HOH HOH C . 
I 3 HOH 10  122 4   HOH HOH C . 
I 3 HOH 11  123 5   HOH HOH C . 
I 3 HOH 12  124 6   HOH HOH C . 
I 3 HOH 13  125 7   HOH HOH C . 
I 3 HOH 14  126 8   HOH HOH C . 
I 3 HOH 15  127 9   HOH HOH C . 
I 3 HOH 16  128 10  HOH HOH C . 
I 3 HOH 17  129 11  HOH HOH C . 
I 3 HOH 18  130 12  HOH HOH C . 
I 3 HOH 19  131 13  HOH HOH C . 
I 3 HOH 20  132 14  HOH HOH C . 
I 3 HOH 21  133 15  HOH HOH C . 
I 3 HOH 22  134 16  HOH HOH C . 
I 3 HOH 23  135 17  HOH HOH C . 
I 3 HOH 24  136 18  HOH HOH C . 
I 3 HOH 25  137 19  HOH HOH C . 
I 3 HOH 26  138 20  HOH HOH C . 
I 3 HOH 27  139 21  HOH HOH C . 
I 3 HOH 28  140 22  HOH HOH C . 
I 3 HOH 29  141 23  HOH HOH C . 
I 3 HOH 30  142 24  HOH HOH C . 
I 3 HOH 31  143 25  HOH HOH C . 
I 3 HOH 32  144 26  HOH HOH C . 
I 3 HOH 33  145 27  HOH HOH C . 
I 3 HOH 34  146 28  HOH HOH C . 
I 3 HOH 35  147 29  HOH HOH C . 
I 3 HOH 36  148 30  HOH HOH C . 
I 3 HOH 37  149 31  HOH HOH C . 
I 3 HOH 38  150 32  HOH HOH C . 
I 3 HOH 39  151 33  HOH HOH C . 
I 3 HOH 40  152 35  HOH HOH C . 
I 3 HOH 41  153 36  HOH HOH C . 
I 3 HOH 42  154 37  HOH HOH C . 
I 3 HOH 43  155 38  HOH HOH C . 
I 3 HOH 44  156 39  HOH HOH C . 
I 3 HOH 45  157 40  HOH HOH C . 
I 3 HOH 46  158 41  HOH HOH C . 
I 3 HOH 47  159 42  HOH HOH C . 
I 3 HOH 48  160 43  HOH HOH C . 
I 3 HOH 49  161 44  HOH HOH C . 
I 3 HOH 50  162 45  HOH HOH C . 
I 3 HOH 51  163 46  HOH HOH C . 
I 3 HOH 52  164 47  HOH HOH C . 
I 3 HOH 53  165 48  HOH HOH C . 
I 3 HOH 54  166 49  HOH HOH C . 
I 3 HOH 55  167 50  HOH HOH C . 
I 3 HOH 56  168 51  HOH HOH C . 
I 3 HOH 57  169 52  HOH HOH C . 
I 3 HOH 58  170 53  HOH HOH C . 
I 3 HOH 59  171 54  HOH HOH C . 
I 3 HOH 60  172 55  HOH HOH C . 
I 3 HOH 61  173 56  HOH HOH C . 
I 3 HOH 62  174 57  HOH HOH C . 
I 3 HOH 63  175 58  HOH HOH C . 
I 3 HOH 64  176 59  HOH HOH C . 
I 3 HOH 65  177 60  HOH HOH C . 
I 3 HOH 66  178 61  HOH HOH C . 
I 3 HOH 67  179 62  HOH HOH C . 
I 3 HOH 68  180 63  HOH HOH C . 
I 3 HOH 69  181 64  HOH HOH C . 
I 3 HOH 70  182 65  HOH HOH C . 
I 3 HOH 71  183 66  HOH HOH C . 
I 3 HOH 72  184 67  HOH HOH C . 
I 3 HOH 73  185 68  HOH HOH C . 
I 3 HOH 74  186 69  HOH HOH C . 
I 3 HOH 75  187 70  HOH HOH C . 
I 3 HOH 76  188 71  HOH HOH C . 
I 3 HOH 77  189 72  HOH HOH C . 
I 3 HOH 78  190 73  HOH HOH C . 
I 3 HOH 79  191 74  HOH HOH C . 
I 3 HOH 80  192 75  HOH HOH C . 
I 3 HOH 81  193 76  HOH HOH C . 
I 3 HOH 82  194 77  HOH HOH C . 
I 3 HOH 83  195 78  HOH HOH C . 
I 3 HOH 84  196 79  HOH HOH C . 
I 3 HOH 85  197 80  HOH HOH C . 
I 3 HOH 86  198 81  HOH HOH C . 
I 3 HOH 87  199 82  HOH HOH C . 
I 3 HOH 88  200 83  HOH HOH C . 
I 3 HOH 89  201 84  HOH HOH C . 
I 3 HOH 90  202 85  HOH HOH C . 
I 3 HOH 91  203 86  HOH HOH C . 
I 3 HOH 92  204 87  HOH HOH C . 
I 3 HOH 93  205 88  HOH HOH C . 
I 3 HOH 94  206 89  HOH HOH C . 
I 3 HOH 95  207 90  HOH HOH C . 
I 3 HOH 96  208 91  HOH HOH C . 
I 3 HOH 97  209 92  HOH HOH C . 
I 3 HOH 98  210 93  HOH HOH C . 
I 3 HOH 99  211 94  HOH HOH C . 
I 3 HOH 100 212 95  HOH HOH C . 
I 3 HOH 101 213 96  HOH HOH C . 
I 3 HOH 102 214 97  HOH HOH C . 
I 3 HOH 103 215 98  HOH HOH C . 
I 3 HOH 104 216 99  HOH HOH C . 
I 3 HOH 105 217 100 HOH HOH C . 
I 3 HOH 106 218 101 HOH HOH C . 
I 3 HOH 107 219 102 HOH HOH C . 
I 3 HOH 108 220 103 HOH HOH C . 
I 3 HOH 109 221 104 HOH HOH C . 
I 3 HOH 110 222 105 HOH HOH C . 
I 3 HOH 111 223 106 HOH HOH C . 
I 3 HOH 112 224 107 HOH HOH C . 
I 3 HOH 113 225 108 HOH HOH C . 
I 3 HOH 114 226 109 HOH HOH C . 
I 3 HOH 115 227 110 HOH HOH C . 
I 3 HOH 116 228 111 HOH HOH C . 
I 3 HOH 117 229 112 HOH HOH C . 
I 3 HOH 118 230 113 HOH HOH C . 
I 3 HOH 119 231 114 HOH HOH C . 
I 3 HOH 120 232 115 HOH HOH C . 
I 3 HOH 121 233 116 HOH HOH C . 
I 3 HOH 122 234 117 HOH HOH C . 
I 3 HOH 123 235 118 HOH HOH C . 
I 3 HOH 124 236 119 HOH HOH C . 
I 3 HOH 125 237 120 HOH HOH C . 
I 3 HOH 126 238 121 HOH HOH C . 
I 3 HOH 127 239 122 HOH HOH C . 
I 3 HOH 128 240 123 HOH HOH C . 
I 3 HOH 129 241 124 HOH HOH C . 
I 3 HOH 130 242 125 HOH HOH C . 
I 3 HOH 131 243 126 HOH HOH C . 
I 3 HOH 132 244 127 HOH HOH C . 
I 3 HOH 133 245 128 HOH HOH C . 
I 3 HOH 134 246 129 HOH HOH C . 
I 3 HOH 135 247 130 HOH HOH C . 
I 3 HOH 136 248 131 HOH HOH C . 
I 3 HOH 137 249 133 HOH HOH C . 
I 3 HOH 138 250 134 HOH HOH C . 
I 3 HOH 139 251 135 HOH HOH C . 
I 3 HOH 140 252 136 HOH HOH C . 
I 3 HOH 141 253 137 HOH HOH C . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly              ?    monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_defined_assembly              ?    monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,G 
2 1 B,E,H 
3 1 C,F,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 18 ? A HIS 18  ? 1_555 ZN ? D ZN . ? A ZN 112 ? 1_555 O   ? G HOH .  ? A HOH 227 ? 1_555 100.2 ? 
2  ND1 ? A HIS 18 ? A HIS 18  ? 1_555 ZN ? D ZN . ? A ZN 112 ? 1_555 OE2 ? A GLU 60 ? A GLU 60  ? 3_675 112.2 ? 
3  O   ? G HOH .  ? A HOH 227 ? 1_555 ZN ? D ZN . ? A ZN 112 ? 1_555 OE2 ? A GLU 60 ? A GLU 60  ? 3_675 147.3 ? 
4  OE1 ? B GLU 60 ? B GLU 60  ? 1_555 ZN ? E ZN . ? B ZN 112 ? 1_555 OE2 ? B GLU 60 ? B GLU 60  ? 1_555 58.5  ? 
5  OE1 ? B GLU 60 ? B GLU 60  ? 1_555 ZN ? E ZN . ? B ZN 112 ? 1_555 O   ? H HOH .  ? B HOH 260 ? 1_555 135.8 ? 
6  OE2 ? B GLU 60 ? B GLU 60  ? 1_555 ZN ? E ZN . ? B ZN 112 ? 1_555 O   ? H HOH .  ? B HOH 260 ? 1_555 87.3  ? 
7  OE1 ? B GLU 60 ? B GLU 60  ? 1_555 ZN ? E ZN . ? B ZN 112 ? 1_555 ND1 ? B HIS 18 ? B HIS 18  ? 3_565 110.3 ? 
8  OE2 ? B GLU 60 ? B GLU 60  ? 1_555 ZN ? E ZN . ? B ZN 112 ? 1_555 ND1 ? B HIS 18 ? B HIS 18  ? 3_565 153.5 ? 
9  O   ? H HOH .  ? B HOH 260 ? 1_555 ZN ? E ZN . ? B ZN 112 ? 1_555 ND1 ? B HIS 18 ? B HIS 18  ? 3_565 111.9 ? 
10 OE1 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 OE2 ? C GLU 60 ? C GLU 60  ? 1_555 58.7  ? 
11 OE1 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 NZ  ? C LYS 62 ? C LYS 62  ? 1_555 93.4  ? 
12 OE2 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 NZ  ? C LYS 62 ? C LYS 62  ? 1_555 110.0 ? 
13 OE1 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 O   ? I HOH .  ? C HOH 139 ? 1_555 148.6 ? 
14 OE2 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 O   ? I HOH .  ? C HOH 139 ? 1_555 89.9  ? 
15 NZ  ? C LYS 62 ? C LYS 62  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 O   ? I HOH .  ? C HOH 139 ? 1_555 99.8  ? 
16 OE1 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 ND1 ? C HIS 18 ? C HIS 18  ? 3_665 97.6  ? 
17 OE2 ? C GLU 60 ? C GLU 60  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 ND1 ? C HIS 18 ? C HIS 18  ? 3_665 132.9 ? 
18 NZ  ? C LYS 62 ? C LYS 62  ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 ND1 ? C HIS 18 ? C HIS 18  ? 3_665 111.6 ? 
19 O   ? I HOH .  ? C HOH 139 ? 1_555 ZN ? F ZN . ? C ZN 112 ? 1_555 ND1 ? C HIS 18 ? C HIS 18  ? 3_665 103.7 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 1998-04-29 
2 'Structure model' 1 1 2008-03-04 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
SHELXL-93 'model building' . ? 1 
X-PLOR    'model building' . ? 2 
SHELXL-93 refinement       . ? 3 
X-PLOR    refinement       . ? 4 
MOSFLM    'data reduction' . ? 5 
CCP4      'data scaling'   . ? 6 
SHELXL-93 phasing          . ? 7 
X-PLOR    phasing          . ? 8 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    CG2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    THR 
_pdbx_validate_symm_contact.auth_seq_id_1     16 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NH2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     59 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_675 
_pdbx_validate_symm_contact.dist              2.01 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              72 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              72 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              72 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.26 
_pdbx_validate_rmsd_angle.angle_target_value         123.60 
_pdbx_validate_rmsd_angle.angle_deviation            8.66 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.40 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 5  ? ? -141.90 23.54  
2 1 THR A 79 ? ? -124.87 -50.02 
3 1 ASN B 5  ? ? -145.06 22.77  
4 1 TRP B 94 ? ? 70.65   30.23  
5 1 ASN C 5  ? ? -143.95 24.51  
6 1 THR C 79 ? ? -125.06 -54.96 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 59 ? ? 0.207 'SIDE CHAIN' 
2 1 ARG B 59 ? ? 0.076 'SIDE CHAIN' 
3 1 ARG B 72 ? ? 0.085 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A ARG 59 ? CB  ? A ARG 59 CB  
2  1 Y 0 A ARG 59 ? CG  ? A ARG 59 CG  
3  1 Y 0 A ARG 59 ? CD  ? A ARG 59 CD  
4  1 Y 0 A ARG 59 ? NE  ? A ARG 59 NE  
5  1 Y 0 A ARG 59 ? CZ  ? A ARG 59 CZ  
6  1 Y 0 A ARG 59 ? NH1 ? A ARG 59 NH1 
7  1 Y 0 A ARG 59 ? NH2 ? A ARG 59 NH2 
8  1 Y 0 B VAL 3  ? N   ? B VAL 3  N   
9  1 Y 0 B ARG 59 ? CG  ? B ARG 59 CG  
10 1 Y 0 B ARG 59 ? CD  ? B ARG 59 CD  
11 1 Y 0 B ARG 59 ? NE  ? B ARG 59 NE  
12 1 Y 0 B ARG 59 ? CZ  ? B ARG 59 CZ  
13 1 Y 0 B ARG 59 ? NH1 ? B ARG 59 NH1 
14 1 Y 0 B ARG 59 ? NH2 ? B ARG 59 NH2 
15 1 Y 0 B SER 67 ? CB  ? B SER 67 CB  
16 1 Y 0 B SER 67 ? OG  ? B SER 67 OG  
17 1 Y 0 C LYS 39 ? CE  ? C LYS 39 CE  
18 1 Y 0 C LYS 39 ? NZ  ? C LYS 39 NZ  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 1 ? A ALA 1 
2 1 Y 1 A GLN 2 ? A GLN 2 
3 1 Y 1 B ALA 1 ? B ALA 1 
4 1 Y 1 B GLN 2 ? B GLN 2 
5 1 Y 1 C ALA 1 ? C ALA 1 
6 1 Y 1 C GLN 2 ? C GLN 2 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.