data_2W08
# 
_entry.id   2W08 
# 
_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   2W08         
PDBE  EBI-37186    
WWPDB D_1290037186 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 2A3X unspecified 
;DECAMERIC CRYSTAL STRUCTURE OF HUMAN SERUM AMYLOID P-COMPONENT BOUND TO BIS-1,2-{[( Z)-2CARBOXY- 2-METHYL-1,3-DIOXANE]- 5- YLOXYCARBONYL}-PIPERAZINE
;
PDB 1SAC unspecified 'SERUM AMYLOID P COMPONENT (SAP)' 
PDB 1GYK unspecified 'SERUM AMYLOID P COMPONENT CO-CRYSTALLISED WITH MOBDG AT NEUTRAL PH' 
PDB 2A3Y unspecified 
;PENTAMERIC CRYSTAL STRUCTURE OF HUMAN SERUM AMYLOID P-COMPONENT BOUND TO BIS-1,2-{[( Z)-2CARBOXY-2-METHYL-1,3-DIOXANE]-5- YLOXYCARBAMOYL}-ETHANE.
;
PDB 2A3W unspecified 
;DECAMERIC STRUCTURE OF HUMAN SERUM AMYLOID P -COMPONENTBOUND TO BIS-1,2-{[(Z)-2- CARBOXY-2-METHYL-1,3-DIOXANE]-5- YLOXYCARBAMOYL}-ETHANE
;
PDB 1LGN unspecified 'DECAMERIC DAMP COMPLEX OF HUMAN SERUM AMYLOID P COMPONENT' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2W08 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2008-08-12 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kolstoe, S.E.' 1 
'Pepys, M.B.'   2 
'Wood, S.P.'    3 
# 
_citation.id                        primary 
_citation.title                     
;Molecular Dissection of Alzheimer'S Disease Neuropathology by Depletion of Serum Amyloid P Component.
;
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            106 
_citation.page_first                7619 
_citation.page_last                 ? 
_citation.year                      2009 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19372378 
_citation.pdbx_database_id_DOI      10.1073/PNAS.0902640106 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kolstoe, S.E.'       1  
primary 'Ridha, B.H.'         2  
primary 'Bellotti, V.'        3  
primary 'Wang, N.'            4  
primary 'Robinson, C.V.'      5  
primary 'Crutch, S.J.'        6  
primary 'Keir, G.'            7  
primary 'Kukkastenvehmas, R.' 8  
primary 'Gallimore, J.R.'     9  
primary 'Hutchinson, W.L.'    10 
primary 'Hawkins, P.N.'       11 
primary 'Wood, S.P.'          12 
primary 'Rossor, M.N.'        13 
primary 'Pepys, M.B.'         14 
# 
_cell.entry_id           2W08 
_cell.length_a           94.769 
_cell.length_b           69.435 
_cell.length_c           102.063 
_cell.angle_alpha        90.00 
_cell.angle_beta         97.05 
_cell.angle_gamma        90.00 
_cell.Z_PDB              10 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2W08 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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     nat 'SERUM AMYLOID P-COMPONENT' 23282.455 5    ? ? ? O-PHOSPHOTHREONINE 
2 non-polymer syn 'CALCIUM ION'               40.078    10   ? ? ? ?                  
3 non-polymer man N-ACETYL-D-GLUCOSAMINE      221.208   5    ? ? ? ?                  
4 non-polymer syn PHOSPHOTHREONINE            199.099   5    ? ? ? ?                  
5 water       nat water                       18.015    1354 ? ? ? ?                  
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'SERUM AMYLOID P COMPONENT, 9.5S ALPHA-1-GLYCOPROTEIN' 
# 
_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       
;HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKV
TSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMW
DSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKV
TSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMW
DSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E 
_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   HIS n 
1 2   THR n 
1 3   ASP n 
1 4   LEU n 
1 5   SER n 
1 6   GLY n 
1 7   LYS n 
1 8   VAL n 
1 9   PHE n 
1 10  VAL n 
1 11  PHE n 
1 12  PRO n 
1 13  ARG n 
1 14  GLU n 
1 15  SER n 
1 16  VAL n 
1 17  THR n 
1 18  ASP n 
1 19  HIS n 
1 20  VAL n 
1 21  ASN n 
1 22  LEU n 
1 23  ILE n 
1 24  THR n 
1 25  PRO n 
1 26  LEU n 
1 27  GLU n 
1 28  LYS n 
1 29  PRO n 
1 30  LEU n 
1 31  GLN n 
1 32  ASN n 
1 33  PHE n 
1 34  THR n 
1 35  LEU n 
1 36  CYS n 
1 37  PHE n 
1 38  ARG n 
1 39  ALA n 
1 40  TYR n 
1 41  SER n 
1 42  ASP n 
1 43  LEU n 
1 44  SER n 
1 45  ARG n 
1 46  ALA n 
1 47  TYR n 
1 48  SER n 
1 49  LEU n 
1 50  PHE n 
1 51  SER n 
1 52  TYR n 
1 53  ASN n 
1 54  THR n 
1 55  GLN n 
1 56  GLY n 
1 57  ARG n 
1 58  ASP n 
1 59  ASN n 
1 60  GLU n 
1 61  LEU n 
1 62  LEU n 
1 63  VAL n 
1 64  TYR n 
1 65  LYS n 
1 66  GLU n 
1 67  ARG n 
1 68  VAL n 
1 69  GLY n 
1 70  GLU n 
1 71  TYR n 
1 72  SER n 
1 73  LEU n 
1 74  TYR n 
1 75  ILE n 
1 76  GLY n 
1 77  ARG n 
1 78  HIS n 
1 79  LYS n 
1 80  VAL n 
1 81  THR n 
1 82  SER n 
1 83  LYS n 
1 84  VAL n 
1 85  ILE n 
1 86  GLU n 
1 87  LYS n 
1 88  PHE n 
1 89  PRO n 
1 90  ALA n 
1 91  PRO n 
1 92  VAL n 
1 93  HIS n 
1 94  ILE n 
1 95  CYS n 
1 96  VAL n 
1 97  SER n 
1 98  TRP n 
1 99  GLU n 
1 100 SER n 
1 101 SER n 
1 102 SER n 
1 103 GLY n 
1 104 ILE n 
1 105 ALA n 
1 106 GLU n 
1 107 PHE n 
1 108 TRP n 
1 109 ILE n 
1 110 ASN n 
1 111 GLY n 
1 112 THR n 
1 113 PRO n 
1 114 LEU n 
1 115 VAL n 
1 116 LYS n 
1 117 LYS n 
1 118 GLY n 
1 119 LEU n 
1 120 ARG n 
1 121 GLN n 
1 122 GLY n 
1 123 TYR n 
1 124 PHE n 
1 125 VAL n 
1 126 GLU n 
1 127 ALA n 
1 128 GLN n 
1 129 PRO n 
1 130 LYS n 
1 131 ILE n 
1 132 VAL n 
1 133 LEU n 
1 134 GLY n 
1 135 GLN n 
1 136 GLU n 
1 137 GLN n 
1 138 ASP n 
1 139 SER n 
1 140 TYR n 
1 141 GLY n 
1 142 GLY n 
1 143 LYS n 
1 144 PHE n 
1 145 ASP n 
1 146 ARG n 
1 147 SER n 
1 148 GLN n 
1 149 SER n 
1 150 PHE n 
1 151 VAL n 
1 152 GLY n 
1 153 GLU n 
1 154 ILE n 
1 155 GLY n 
1 156 ASP n 
1 157 LEU n 
1 158 TYR n 
1 159 MET n 
1 160 TRP n 
1 161 ASP n 
1 162 SER n 
1 163 VAL n 
1 164 LEU n 
1 165 PRO n 
1 166 PRO n 
1 167 GLU n 
1 168 ASN n 
1 169 ILE n 
1 170 LEU n 
1 171 SER n 
1 172 ALA n 
1 173 TYR n 
1 174 GLN n 
1 175 GLY n 
1 176 THR n 
1 177 PRO n 
1 178 LEU n 
1 179 PRO n 
1 180 ALA n 
1 181 ASN n 
1 182 ILE n 
1 183 LEU n 
1 184 ASP n 
1 185 TRP n 
1 186 GLN n 
1 187 ALA n 
1 188 LEU n 
1 189 ASN n 
1 190 TYR n 
1 191 GLU n 
1 192 ILE n 
1 193 ARG n 
1 194 GLY n 
1 195 TYR n 
1 196 VAL n 
1 197 ILE n 
1 198 ILE n 
1 199 LYS n 
1 200 PRO n 
1 201 LEU n 
1 202 VAL n 
1 203 TRP n 
1 204 VAL n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                HUMAN 
_entity_src_nat.pdbx_organism_scientific   'HOMO SAPIENS' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9606 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SAMP_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P02743 
_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 2W08 A 1 ? 204 ? P02743 20 ? 223 ? 1 204 
2 1 2W08 B 1 ? 204 ? P02743 20 ? 223 ? 1 204 
3 1 2W08 C 1 ? 204 ? P02743 20 ? 223 ? 1 204 
4 1 2W08 D 1 ? 204 ? P02743 20 ? 223 ? 1 204 
5 1 2W08 E 1 ? 204 ? P02743 20 ? 223 ? 1 204 
# 
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 
CA  non-polymer         . 'CALCIUM ION'          ?                  'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE               ?                  'C3 H7 N O2 S'   121.158 
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 
MET 'L-peptide linking' y METHIONINE             ?                  'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ?                  'C8 H15 N O6'    221.208 
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 
TPO 'L-peptide linking' n PHOSPHOTHREONINE       PHOSPHONOTHREONINE 'C4 H10 N O6 P'  199.099 
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 
# 
_exptl.entry_id          2W08 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_percent_sol   48.39 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'0.06M TRIS-HCL PH8, 16% PEG 550MME, 0.01M CACL2, 0.08M NACL, 0.1% NAN3, 14.2MG/ML PROTEIN, 50MM LIGAND' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2004-07-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID14-2' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID14-2 
_diffrn_source.pdbx_wavelength             0.98 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2W08 
_reflns.observed_criterion_sigma_I   2.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             47.67 
_reflns.d_resolution_high            1.70 
_reflns.number_obs                   140019 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         97.0 
_reflns.pdbx_Rmerge_I_obs            0.11 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.70 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.6 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.70 
_reflns_shell.d_res_low              1.78 
_reflns_shell.percent_possible_all   95.6 
_reflns_shell.Rmerge_I_obs           0.38 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    9.30 
_reflns_shell.pdbx_redundancy        4 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2W08 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     139007 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.040 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.48 
_refine.ls_d_res_high                            1.70 
_refine.ls_percent_reflns_obs                    96.1 
_refine.ls_R_factor_obs                          0.154 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.154 
_refine.ls_R_factor_R_free                       0.176 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 1.400 
_refine.ls_number_reflns_R_free                  1989 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.36 
_refine.solvent_model_param_bsol                 47.57 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1SAC' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.160 
_refine.pdbx_overall_phase_error                 15.790 
_refine.overall_SU_B                             ? 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8245 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         140 
_refine_hist.number_atoms_solvent             1354 
_refine_hist.number_atoms_total               9739 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        47.48 
# 
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 
f_bond_d           0.007  ? ? 8806  'X-RAY DIFFRACTION' ? 
f_angle_d          1.192  ? ? 12016 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 18.139 ? ? 3257  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.089  ? ? 1285  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.006  ? ? 1535  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 1.7000 1.7425  9414  0.1543 93.00 0.1938 . . 135 . . 
'X-RAY DIFFRACTION' . 1.7425 1.7896  9481  0.1466 93.00 0.1876 . . 147 . . 
'X-RAY DIFFRACTION' . 1.7896 1.8423  9498  0.1446 94.00 0.1843 . . 124 . . 
'X-RAY DIFFRACTION' . 1.8423 1.9018  9555  0.1485 94.00 0.1775 . . 157 . . 
'X-RAY DIFFRACTION' . 1.9018 1.9697  9687  0.1429 95.00 0.2128 . . 125 . . 
'X-RAY DIFFRACTION' . 1.9697 2.0486  9747  0.1434 96.00 0.1726 . . 149 . . 
'X-RAY DIFFRACTION' . 2.0486 2.1418  9806  0.1398 96.00 0.1596 . . 135 . . 
'X-RAY DIFFRACTION' . 2.1418 2.2548  9794  0.1437 97.00 0.1641 . . 159 . . 
'X-RAY DIFFRACTION' . 2.2548 2.3960  9887  0.1488 97.00 0.1614 . . 137 . . 
'X-RAY DIFFRACTION' . 2.3960 2.5810  9892  0.1586 97.00 0.2029 . . 143 . . 
'X-RAY DIFFRACTION' . 2.5810 2.8407  9932  0.1686 98.00 0.1802 . . 142 . . 
'X-RAY DIFFRACTION' . 2.8407 3.2517  10026 0.1647 98.00 0.1589 . . 145 . . 
'X-RAY DIFFRACTION' . 3.2517 4.0964  10106 0.1429 98.00 0.1699 . . 141 . . 
'X-RAY DIFFRACTION' . 4.0964 47.4933 10193 0.1559 98.00 0.1611 . . 150 . . 
# 
_struct.entry_id                  2W08 
_struct.title                     'The structure of serum amyloid P component bound to 0-phospho- threonine' 
_struct.pdbx_descriptor           'SERUM AMYLOID P-COMPONENT' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2W08 
_struct_keywords.pdbx_keywords   GLYCOPROTEIN 
_struct_keywords.text            'GLYCOPROTEIN, POLYMORPHISM, METAL-BINDING, TAU, LECTIN, CALCIUM, AMYLOID, SECRETED, ALZHEIMERS' 
# 
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 1 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 2 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 2 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 5 ? 
CA N N 5 ? 
DA N N 5 ? 
# 
_struct_biol.id   1 
# 
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  ASP A 145 ? SER A 149 ? ASP A 145 SER A 149 5 ? 5  
HELX_P HELX_P2  2  PRO A 165 ? GLY A 175 ? PRO A 165 GLY A 175 1 ? 11 
HELX_P HELX_P3  3  ASP B 145 ? SER B 149 ? ASP B 145 SER B 149 5 ? 5  
HELX_P HELX_P4  4  PRO B 165 ? GLY B 175 ? PRO B 165 GLY B 175 1 ? 11 
HELX_P HELX_P5  5  ASP C 145 ? SER C 149 ? ASP C 145 SER C 149 5 ? 5  
HELX_P HELX_P6  6  PRO C 165 ? GLN C 174 ? PRO C 165 GLN C 174 1 ? 10 
HELX_P HELX_P7  7  ASP D 145 ? SER D 149 ? ASP D 145 SER D 149 5 ? 5  
HELX_P HELX_P8  8  PRO D 165 ? GLY D 175 ? PRO D 165 GLY D 175 1 ? 11 
HELX_P HELX_P9  9  ASP E 145 ? SER E 149 ? ASP E 145 SER E 149 5 ? 5  
HELX_P HELX_P10 10 PRO E 165 ? GLN E 174 ? PRO E 165 GLN E 174 1 ? 10 
# 
_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 
disulf1  disulf ? ? A CYS 36 SG  ? ? ? 1_555 A  CYS 95  SG  ? ? A CYS 36  A CYS 95   1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf2  disulf ? ? B CYS 36 SG  ? ? ? 1_555 B  CYS 95  SG  ? ? B CYS 36  B CYS 95   1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf3  disulf ? ? C CYS 36 SG  ? ? ? 1_555 C  CYS 95  SG  ? ? C CYS 36  C CYS 95   1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf4  disulf ? ? D CYS 36 SG  ? ? ? 1_555 D  CYS 95  SG  ? ? D CYS 36  D CYS 95   1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf5  disulf ? ? E CYS 36 SG  ? ? ? 1_555 E  CYS 95  SG  ? ? E CYS 36  E CYS 95   1_555 ? ? ? ? ? ? ? 2.032 ? 
covale1  covale ? ? A ASN 32 ND2 ? ? ? 1_555 H  NAG .   C1  ? ? A ASN 32  A NAG 207  1_555 ? ? ? ? ? ? ? 1.443 ? 
metalc1  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  ASP 58  OD1 ? ? A CA  205 A ASP 58   1_555 ? ? ? ? ? ? ? 2.531 ? 
metalc2  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  ASN 59  OD1 ? ? A CA  205 A ASN 59   1_555 ? ? ? ? ? ? ? 2.421 ? 
metalc3  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  GLU 136 OE2 ? ? A CA  205 A GLU 136  1_555 ? ? ? ? ? ? ? 2.481 ? 
metalc4  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  GLN 137 O   ? ? A CA  205 A GLN 137  1_555 ? ? ? ? ? ? ? 2.451 ? 
metalc5  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  ASP 58  OD2 ? ? A CA  205 A ASP 58   1_555 ? ? ? ? ? ? ? 2.685 ? 
metalc6  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  ASP 138 OD1 ? ? A CA  205 A ASP 138  1_555 ? ? ? ? ? ? ? 2.461 ? 
metalc7  metalc ? ? F CA  .  CA  ? ? ? 1_555 I  TPO .   O1P ? ? A CA  205 A TPO 500  1_555 ? ? ? ? ? ? ? 2.360 ? 
metalc8  metalc ? ? F CA  .  CA  ? ? ? 1_555 A  GLU 136 OE1 ? ? A CA  205 A GLU 136  1_555 ? ? ? ? ? ? ? 2.664 ? 
metalc9  metalc ? ? G CA  .  CA  ? ? ? 1_555 Z  HOH .   O   ? ? A CA  206 A HOH 2184 1_555 ? ? ? ? ? ? ? 2.526 ? 
metalc10 metalc ? ? G CA  .  CA  ? ? ? 1_555 A  GLU 136 OE1 ? ? A CA  206 A GLU 136  1_555 ? ? ? ? ? ? ? 2.383 ? 
metalc11 metalc ? ? G CA  .  CA  ? ? ? 1_555 I  TPO .   O2P ? ? A CA  206 A TPO 500  1_555 ? ? ? ? ? ? ? 2.383 ? 
metalc12 metalc ? ? G CA  .  CA  ? ? ? 1_555 Z  HOH .   O   ? ? A CA  206 A HOH 2192 1_555 ? ? ? ? ? ? ? 2.457 ? 
metalc13 metalc ? ? G CA  .  CA  ? ? ? 1_555 A  ASP 138 OD1 ? ? A CA  206 A ASP 138  1_555 ? ? ? ? ? ? ? 2.615 ? 
metalc14 metalc ? ? G CA  .  CA  ? ? ? 1_555 A  ASP 138 OD2 ? ? A CA  206 A ASP 138  1_555 ? ? ? ? ? ? ? 2.602 ? 
metalc15 metalc ? ? G CA  .  CA  ? ? ? 1_555 A  GLN 148 OE1 ? ? A CA  206 A GLN 148  1_555 ? ? ? ? ? ? ? 2.413 ? 
covale2  covale ? ? B ASN 32 ND2 ? ? ? 1_555 L  NAG .   C1  ? ? B ASN 32  B NAG 207  1_555 ? ? ? ? ? ? ? 1.445 ? 
metalc16 metalc ? ? J CA  .  CA  ? ? ? 1_555 B  ASP 138 OD2 ? ? B CA  205 B ASP 138  1_555 ? ? ? ? ? ? ? 2.561 ? 
metalc17 metalc ? ? J CA  .  CA  ? ? ? 1_555 B  GLU 136 OE1 ? ? B CA  205 B GLU 136  1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc18 metalc ? ? J CA  .  CA  ? ? ? 1_555 B  GLN 148 OE1 ? ? B CA  205 B GLN 148  1_555 ? ? ? ? ? ? ? 2.442 ? 
metalc19 metalc ? ? J CA  .  CA  ? ? ? 1_555 M  TPO .   O2P ? ? B CA  205 B TPO 500  1_555 ? ? ? ? ? ? ? 2.320 ? 
metalc20 metalc ? ? J CA  .  CA  ? ? ? 1_555 AA HOH .   O   ? ? B CA  205 B HOH 2200 1_555 ? ? ? ? ? ? ? 2.450 ? 
metalc21 metalc ? ? J CA  .  CA  ? ? ? 1_555 AA HOH .   O   ? ? B CA  205 B HOH 2186 1_555 ? ? ? ? ? ? ? 2.500 ? 
metalc22 metalc ? ? J CA  .  CA  ? ? ? 1_555 B  ASP 138 OD1 ? ? B CA  205 B ASP 138  1_555 ? ? ? ? ? ? ? 2.560 ? 
metalc23 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  ASP 58  OD1 ? ? B CA  206 B ASP 58   1_555 ? ? ? ? ? ? ? 2.539 ? 
metalc24 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  ASP 58  OD2 ? ? B CA  206 B ASP 58   1_555 ? ? ? ? ? ? ? 2.720 ? 
metalc25 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  ASN 59  OD1 ? ? B CA  206 B ASN 59   1_555 ? ? ? ? ? ? ? 2.399 ? 
metalc26 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  GLU 136 OE1 ? ? B CA  206 B GLU 136  1_555 ? ? ? ? ? ? ? 2.650 ? 
metalc27 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  GLU 136 OE2 ? ? B CA  206 B GLU 136  1_555 ? ? ? ? ? ? ? 2.451 ? 
metalc28 metalc ? ? K CA  .  CA  ? ? ? 1_555 M  TPO .   O1P ? ? B CA  206 B TPO 500  1_555 ? ? ? ? ? ? ? 2.305 ? 
metalc29 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  ASP 138 OD1 ? ? B CA  206 B ASP 138  1_555 ? ? ? ? ? ? ? 2.359 ? 
metalc30 metalc ? ? K CA  .  CA  ? ? ? 1_555 B  GLN 137 O   ? ? B CA  206 B GLN 137  1_555 ? ? ? ? ? ? ? 2.432 ? 
covale3  covale ? ? C ASN 32 ND2 ? ? ? 1_555 P  NAG .   C1  ? ? C ASN 32  C NAG 207  1_555 ? ? ? ? ? ? ? 1.447 ? 
metalc31 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  GLU 136 OE1 ? ? C CA  205 C GLU 136  1_555 ? ? ? ? ? ? ? 2.668 ? 
metalc32 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  GLU 136 OE2 ? ? C CA  205 C GLU 136  1_555 ? ? ? ? ? ? ? 2.479 ? 
metalc33 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  GLN 137 O   ? ? C CA  205 C GLN 137  1_555 ? ? ? ? ? ? ? 2.449 ? 
metalc34 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  ASP 138 OD1 ? ? C CA  205 C ASP 138  1_555 ? ? ? ? ? ? ? 2.415 ? 
metalc35 metalc ? ? N CA  .  CA  ? ? ? 1_555 Q  TPO .   O1P ? ? C CA  205 C TPO 500  1_555 ? ? ? ? ? ? ? 2.313 ? 
metalc36 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  ASP 58  OD1 ? ? C CA  205 C ASP 58   1_555 ? ? ? ? ? ? ? 2.525 ? 
metalc37 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  ASP 58  OD2 ? ? C CA  205 C ASP 58   1_555 ? ? ? ? ? ? ? 2.834 ? 
metalc38 metalc ? ? N CA  .  CA  ? ? ? 1_555 C  ASN 59  OD1 ? ? C CA  205 C ASN 59   1_555 ? ? ? ? ? ? ? 2.395 ? 
metalc39 metalc ? ? O CA  .  CA  ? ? ? 1_555 C  GLN 148 OE1 ? ? C CA  206 C GLN 148  1_555 ? ? ? ? ? ? ? 2.370 ? 
metalc40 metalc ? ? O CA  .  CA  ? ? ? 1_555 BA HOH .   O   ? ? C CA  206 C HOH 2190 1_555 ? ? ? ? ? ? ? 2.382 ? 
metalc41 metalc ? ? O CA  .  CA  ? ? ? 1_555 BA HOH .   O   ? ? C CA  206 C HOH 2199 1_555 ? ? ? ? ? ? ? 2.434 ? 
metalc42 metalc ? ? O CA  .  CA  ? ? ? 1_555 Q  TPO .   O2P ? ? C CA  206 C TPO 500  1_555 ? ? ? ? ? ? ? 2.372 ? 
metalc43 metalc ? ? O CA  .  CA  ? ? ? 1_555 C  ASP 138 OD2 ? ? C CA  206 C ASP 138  1_555 ? ? ? ? ? ? ? 2.559 ? 
metalc44 metalc ? ? O CA  .  CA  ? ? ? 1_555 C  ASP 138 OD1 ? ? C CA  206 C ASP 138  1_555 ? ? ? ? ? ? ? 2.652 ? 
metalc45 metalc ? ? O CA  .  CA  ? ? ? 1_555 C  GLU 136 OE1 ? ? C CA  206 C GLU 136  1_555 ? ? ? ? ? ? ? 2.362 ? 
covale4  covale ? ? D ASN 32 ND2 ? ? ? 1_555 T  NAG .   C1  ? ? D ASN 32  D NAG 207  1_555 ? ? ? ? ? ? ? 1.452 ? 
metalc46 metalc ? ? R CA  .  CA  ? ? ? 1_555 CA HOH .   O   ? ? D CA  205 D HOH 2176 1_555 ? ? ? ? ? ? ? 2.448 ? 
metalc47 metalc ? ? R CA  .  CA  ? ? ? 1_555 CA HOH .   O   ? ? D CA  205 D HOH 2190 1_555 ? ? ? ? ? ? ? 2.498 ? 
metalc48 metalc ? ? R CA  .  CA  ? ? ? 1_555 D  ASP 138 OD2 ? ? D CA  205 D ASP 138  1_555 ? ? ? ? ? ? ? 2.600 ? 
metalc49 metalc ? ? R CA  .  CA  ? ? ? 1_555 D  ASP 138 OD1 ? ? D CA  205 D ASP 138  1_555 ? ? ? ? ? ? ? 2.634 ? 
metalc50 metalc ? ? R CA  .  CA  ? ? ? 1_555 U  TPO .   O2P ? ? D CA  205 D TPO 500  1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc51 metalc ? ? R CA  .  CA  ? ? ? 1_555 D  GLN 148 OE1 ? ? D CA  205 D GLN 148  1_555 ? ? ? ? ? ? ? 2.424 ? 
metalc52 metalc ? ? R CA  .  CA  ? ? ? 1_555 D  GLU 136 OE1 ? ? D CA  205 D GLU 136  1_555 ? ? ? ? ? ? ? 2.416 ? 
metalc53 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  ASP 58  OD1 ? ? D CA  206 D ASP 58   1_555 ? ? ? ? ? ? ? 2.494 ? 
metalc54 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  GLN 137 O   ? ? D CA  206 D GLN 137  1_555 ? ? ? ? ? ? ? 2.469 ? 
metalc55 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  ASP 138 OD1 ? ? D CA  206 D ASP 138  1_555 ? ? ? ? ? ? ? 2.404 ? 
metalc56 metalc ? ? S CA  .  CA  ? ? ? 1_555 U  TPO .   O1P ? ? D CA  206 D TPO 500  1_555 ? ? ? ? ? ? ? 2.359 ? 
metalc57 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  ASP 58  OD2 ? ? D CA  206 D ASP 58   1_555 ? ? ? ? ? ? ? 2.670 ? 
metalc58 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  GLU 136 OE1 ? ? D CA  206 D GLU 136  1_555 ? ? ? ? ? ? ? 2.654 ? 
metalc59 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  GLU 136 OE2 ? ? D CA  206 D GLU 136  1_555 ? ? ? ? ? ? ? 2.474 ? 
metalc60 metalc ? ? S CA  .  CA  ? ? ? 1_555 D  ASN 59  OD1 ? ? D CA  206 D ASN 59   1_555 ? ? ? ? ? ? ? 2.379 ? 
covale5  covale ? ? E ASN 32 ND2 ? ? ? 1_555 X  NAG .   C1  ? ? E ASN 32  E NAG 207  1_555 ? ? ? ? ? ? ? 1.446 ? 
metalc61 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  ASP 58  OD1 ? ? E CA  205 E ASP 58   1_555 ? ? ? ? ? ? ? 2.559 ? 
metalc62 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  ASP 58  OD2 ? ? E CA  205 E ASP 58   1_555 ? ? ? ? ? ? ? 2.667 ? 
metalc63 metalc ? ? V CA  .  CA  ? ? ? 1_555 Y  TPO .   O1P ? ? E CA  205 E TPO 500  1_555 ? ? ? ? ? ? ? 2.308 ? 
metalc64 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  ASP 138 OD1 ? ? E CA  205 E ASP 138  1_555 ? ? ? ? ? ? ? 2.370 ? 
metalc65 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  GLN 137 O   ? ? E CA  205 E GLN 137  1_555 ? ? ? ? ? ? ? 2.495 ? 
metalc66 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  GLU 136 OE2 ? ? E CA  205 E GLU 136  1_555 ? ? ? ? ? ? ? 2.481 ? 
metalc67 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  GLU 136 OE1 ? ? E CA  205 E GLU 136  1_555 ? ? ? ? ? ? ? 2.622 ? 
metalc68 metalc ? ? V CA  .  CA  ? ? ? 1_555 E  ASN 59  OD1 ? ? E CA  205 E ASN 59   1_555 ? ? ? ? ? ? ? 2.417 ? 
metalc69 metalc ? ? W CA  .  CA  ? ? ? 1_555 DA HOH .   O   ? ? E CA  206 E HOH 2188 1_555 ? ? ? ? ? ? ? 2.466 ? 
metalc70 metalc ? ? W CA  .  CA  ? ? ? 1_555 DA HOH .   O   ? ? E CA  206 E HOH 2201 1_555 ? ? ? ? ? ? ? 2.420 ? 
metalc71 metalc ? ? W CA  .  CA  ? ? ? 1_555 Y  TPO .   O2P ? ? E CA  206 E TPO 500  1_555 ? ? ? ? ? ? ? 2.330 ? 
metalc72 metalc ? ? W CA  .  CA  ? ? ? 1_555 E  ASP 138 OD2 ? ? E CA  206 E ASP 138  1_555 ? ? ? ? ? ? ? 2.564 ? 
metalc73 metalc ? ? W CA  .  CA  ? ? ? 1_555 E  ASP 138 OD1 ? ? E CA  206 E ASP 138  1_555 ? ? ? ? ? ? ? 2.608 ? 
metalc74 metalc ? ? W CA  .  CA  ? ? ? 1_555 E  GLU 136 OE1 ? ? E CA  206 E GLU 136  1_555 ? ? ? ? ? ? ? 2.399 ? 
metalc75 metalc ? ? W CA  .  CA  ? ? ? 1_555 E  GLN 148 OE1 ? ? E CA  206 E GLN 148  1_555 ? ? ? ? ? ? ? 2.443 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 88 A . ? PHE 88 A PRO 89 A ? PRO 89 A 1 -6.13 
2 PHE 88 B . ? PHE 88 B PRO 89 B ? PRO 89 B 1 -5.84 
3 PHE 88 C . ? PHE 88 C PRO 89 C ? PRO 89 C 1 -6.03 
4 PHE 88 D . ? PHE 88 D PRO 89 D ? PRO 89 D 1 -5.71 
5 PHE 88 E . ? PHE 88 E PRO 89 E ? PRO 89 E 1 -7.81 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 3 ? 
AC ? 7 ? 
BA ? 5 ? 
BB ? 3 ? 
BC ? 7 ? 
CA ? 5 ? 
CB ? 3 ? 
CC ? 7 ? 
DA ? 9 ? 
DB ? 7 ? 
EA ? 9 ? 
EB ? 7 ? 
# 
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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AC 3 4 ? anti-parallel 
AC 4 5 ? anti-parallel 
AC 5 6 ? anti-parallel 
AC 6 7 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BC 1 2 ? anti-parallel 
BC 2 3 ? anti-parallel 
BC 3 4 ? anti-parallel 
BC 4 5 ? anti-parallel 
BC 5 6 ? anti-parallel 
BC 6 7 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CA 4 5 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CC 1 2 ? anti-parallel 
CC 2 3 ? anti-parallel 
CC 3 4 ? anti-parallel 
CC 4 5 ? anti-parallel 
CC 5 6 ? anti-parallel 
CC 6 7 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DA 5 6 ? anti-parallel 
DA 7 8 ? anti-parallel 
DA 8 9 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? anti-parallel 
DB 3 4 ? anti-parallel 
DB 4 5 ? anti-parallel 
DB 5 6 ? anti-parallel 
DB 6 7 ? anti-parallel 
EA 1 2 ? anti-parallel 
EA 2 3 ? anti-parallel 
EA 3 4 ? anti-parallel 
EA 5 6 ? anti-parallel 
EA 7 8 ? anti-parallel 
EA 8 9 ? anti-parallel 
EB 1 2 ? anti-parallel 
EB 2 3 ? anti-parallel 
EB 3 4 ? anti-parallel 
EB 4 5 ? anti-parallel 
EB 5 6 ? anti-parallel 
EB 6 7 ? 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 
AA 1 THR A 112 ? PRO A 113 ? THR A 112 PRO A 113 
AA 2 ILE A 104 ? ILE A 109 ? ILE A 104 ILE A 109 
AA 3 VAL A 92  ? GLU A 99  ? VAL A 92  GLU A 99  
AA 4 ASN A 32  ? TYR A 40  ? ASN A 32  TYR A 40  
AA 5 GLY A 152 ? TRP A 160 ? GLY A 152 TRP A 160 
AB 1 THR A 112 ? PRO A 113 ? THR A 112 PRO A 113 
AB 2 ILE A 104 ? ILE A 109 ? ILE A 104 ILE A 109 
AB 3 LYS A 117 ? GLY A 118 ? LYS A 117 GLY A 118 
AC 1 HIS A 78  ? LYS A 83  ? HIS A 78  LYS A 83  
AC 2 GLU A 70  ? ILE A 75  ? GLU A 70  ILE A 75  
AC 3 ARG A 57  ? ARG A 67  ? ARG A 57  ARG A 67  
AC 4 TYR A 47  ? THR A 54  ? TYR A 47  THR A 54  
AC 5 LYS A 130 ? LEU A 133 ? LYS A 130 LEU A 133 
AC 6 HIS A 19  ? LEU A 22  ? HIS A 19  LEU A 22  
AC 7 TYR A 190 ? ARG A 193 ? TYR A 190 ARG A 193 
BA 1 THR B 112 ? PRO B 113 ? THR B 112 PRO B 113 
BA 2 ILE B 104 ? ILE B 109 ? ILE B 104 ILE B 109 
BA 3 VAL B 92  ? GLU B 99  ? VAL B 92  GLU B 99  
BA 4 ASN B 32  ? TYR B 40  ? ASN B 32  TYR B 40  
BA 5 GLY B 152 ? TRP B 160 ? GLY B 152 TRP B 160 
BB 1 THR B 112 ? PRO B 113 ? THR B 112 PRO B 113 
BB 2 ILE B 104 ? ILE B 109 ? ILE B 104 ILE B 109 
BB 3 LYS B 117 ? GLY B 118 ? LYS B 117 GLY B 118 
BC 1 HIS B 78  ? LYS B 83  ? HIS B 78  LYS B 83  
BC 2 GLU B 70  ? ILE B 75  ? GLU B 70  ILE B 75  
BC 3 ARG B 57  ? ARG B 67  ? ARG B 57  ARG B 67  
BC 4 TYR B 47  ? THR B 54  ? TYR B 47  THR B 54  
BC 5 LYS B 130 ? LEU B 133 ? LYS B 130 LEU B 133 
BC 6 HIS B 19  ? ILE B 23  ? HIS B 19  ILE B 23  
BC 7 ASN B 189 ? ARG B 193 ? ASN B 189 ARG B 193 
CA 1 THR C 112 ? PRO C 113 ? THR C 112 PRO C 113 
CA 2 ILE C 104 ? ILE C 109 ? ILE C 104 ILE C 109 
CA 3 VAL C 92  ? GLU C 99  ? VAL C 92  GLU C 99  
CA 4 ASN C 32  ? TYR C 40  ? ASN C 32  TYR C 40  
CA 5 GLY C 152 ? TRP C 160 ? GLY C 152 TRP C 160 
CB 1 THR C 112 ? PRO C 113 ? THR C 112 PRO C 113 
CB 2 ILE C 104 ? ILE C 109 ? ILE C 104 ILE C 109 
CB 3 LYS C 117 ? GLY C 118 ? LYS C 117 GLY C 118 
CC 1 HIS C 78  ? LYS C 83  ? HIS C 78  LYS C 83  
CC 2 GLU C 70  ? ILE C 75  ? GLU C 70  ILE C 75  
CC 3 ARG C 57  ? ARG C 67  ? ARG C 57  ARG C 67  
CC 4 TYR C 47  ? THR C 54  ? TYR C 47  THR C 54  
CC 5 LYS C 130 ? LEU C 133 ? LYS C 130 LEU C 133 
CC 6 HIS C 19  ? LEU C 22  ? HIS C 19  LEU C 22  
CC 7 TYR C 190 ? ARG C 193 ? TYR C 190 ARG C 193 
DA 1 THR D 112 ? PRO D 113 ? THR D 112 PRO D 113 
DA 2 ILE D 104 ? ILE D 109 ? ILE D 104 ILE D 109 
DA 3 LYS D 117 ? GLY D 118 ? LYS D 117 GLY D 118 
DA 4 ILE D 104 ? ILE D 109 ? ILE D 104 ILE D 109 
DA 5 LEU D 183 ? ASP D 184 ? LEU D 183 ASP D 184 
DA 6 GLY D 152 ? TRP D 160 ? GLY D 152 TRP D 160 
DA 7 ILE D 197 ? PRO D 200 ? ILE D 197 PRO D 200 
DA 8 LYS D 7   ? PHE D 11  ? LYS D 7   PHE D 11  
DA 9 GLY D 152 ? TRP D 160 ? GLY D 152 TRP D 160 
DB 1 HIS D 78  ? LYS D 83  ? HIS D 78  LYS D 83  
DB 2 GLU D 70  ? ILE D 75  ? GLU D 70  ILE D 75  
DB 3 ARG D 57  ? ARG D 67  ? ARG D 57  ARG D 67  
DB 4 TYR D 47  ? THR D 54  ? TYR D 47  THR D 54  
DB 5 LYS D 130 ? LEU D 133 ? LYS D 130 LEU D 133 
DB 6 HIS D 19  ? LEU D 22  ? HIS D 19  LEU D 22  
DB 7 TYR D 190 ? ARG D 193 ? TYR D 190 ARG D 193 
EA 1 THR E 112 ? PRO E 113 ? THR E 112 PRO E 113 
EA 2 ILE E 104 ? ILE E 109 ? ILE E 104 ILE E 109 
EA 3 LYS E 117 ? GLY E 118 ? LYS E 117 GLY E 118 
EA 4 ILE E 104 ? ILE E 109 ? ILE E 104 ILE E 109 
EA 5 LEU E 183 ? ASP E 184 ? LEU E 183 ASP E 184 
EA 6 GLY E 152 ? TRP E 160 ? GLY E 152 TRP E 160 
EA 7 ILE E 197 ? PRO E 200 ? ILE E 197 PRO E 200 
EA 8 LYS E 7   ? PHE E 11  ? LYS E 7   PHE E 11  
EA 9 GLY E 152 ? TRP E 160 ? GLY E 152 TRP E 160 
EB 1 HIS E 78  ? LYS E 83  ? HIS E 78  LYS E 83  
EB 2 GLU E 70  ? ILE E 75  ? GLU E 70  ILE E 75  
EB 3 ARG E 57  ? ARG E 67  ? ARG E 57  ARG E 67  
EB 4 TYR E 47  ? THR E 54  ? TYR E 47  THR E 54  
EB 5 LYS E 130 ? LEU E 133 ? LYS E 130 LEU E 133 
EB 6 HIS E 19  ? LEU E 22  ? HIS E 19  LEU E 22  
EB 7 TYR E 190 ? ARG E 193 ? TYR E 190 ARG E 193 
# 
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 
AA 1 2 N THR A 112 ? N THR A 112 O ILE A 109 ? O ILE A 109 
AA 2 3 N TRP A 108 ? N TRP A 108 O CYS A 95  ? O CYS A 95  
AA 3 4 N TRP A 98  ? N TRP A 98  O PHE A 33  ? O PHE A 33  
AA 4 5 N TYR A 40  ? N TYR A 40  O GLU A 153 ? O GLU A 153 
AB 1 2 N THR A 112 ? N THR A 112 O ILE A 109 ? O ILE A 109 
AB 2 3 N ALA A 105 ? N ALA A 105 O LYS A 117 ? O LYS A 117 
AC 1 2 N SER A 82  ? N SER A 82  O TYR A 71  ? O TYR A 71  
AC 2 3 N TYR A 74  ? N TYR A 74  O LEU A 62  ? O LEU A 62  
AC 3 4 N LYS A 65  ? N LYS A 65  O TYR A 47  ? O TYR A 47  
AC 4 5 N ASN A 53  ? N ASN A 53  O LYS A 130 ? O LYS A 130 
AC 5 6 N LEU A 133 ? N LEU A 133 O VAL A 20  ? O VAL A 20  
AC 6 7 N ASN A 21  ? N ASN A 21  O GLU A 191 ? O GLU A 191 
BA 1 2 N THR B 112 ? N THR B 112 O ILE B 109 ? O ILE B 109 
BA 2 3 N TRP B 108 ? N TRP B 108 O CYS B 95  ? O CYS B 95  
BA 3 4 N TRP B 98  ? N TRP B 98  O PHE B 33  ? O PHE B 33  
BA 4 5 N TYR B 40  ? N TYR B 40  O GLU B 153 ? O GLU B 153 
BB 1 2 N THR B 112 ? N THR B 112 O ILE B 109 ? O ILE B 109 
BB 2 3 N ALA B 105 ? N ALA B 105 O LYS B 117 ? O LYS B 117 
BC 1 2 N SER B 82  ? N SER B 82  O TYR B 71  ? O TYR B 71  
BC 2 3 N TYR B 74  ? N TYR B 74  O LEU B 62  ? O LEU B 62  
BC 3 4 N LYS B 65  ? N LYS B 65  O TYR B 47  ? O TYR B 47  
BC 4 5 N ASN B 53  ? N ASN B 53  O LYS B 130 ? O LYS B 130 
BC 5 6 N LEU B 133 ? N LEU B 133 O VAL B 20  ? O VAL B 20  
BC 6 7 N ILE B 23  ? N ILE B 23  O ASN B 189 ? O ASN B 189 
CA 1 2 N THR C 112 ? N THR C 112 O ILE C 109 ? O ILE C 109 
CA 2 3 N TRP C 108 ? N TRP C 108 O CYS C 95  ? O CYS C 95  
CA 3 4 N TRP C 98  ? N TRP C 98  O PHE C 33  ? O PHE C 33  
CA 4 5 N TYR C 40  ? N TYR C 40  O GLU C 153 ? O GLU C 153 
CB 1 2 N THR C 112 ? N THR C 112 O ILE C 109 ? O ILE C 109 
CB 2 3 N ALA C 105 ? N ALA C 105 O LYS C 117 ? O LYS C 117 
CC 1 2 N SER C 82  ? N SER C 82  O TYR C 71  ? O TYR C 71  
CC 2 3 N TYR C 74  ? N TYR C 74  O LEU C 62  ? O LEU C 62  
CC 3 4 N LYS C 65  ? N LYS C 65  O TYR C 47  ? O TYR C 47  
CC 4 5 N ASN C 53  ? N ASN C 53  O LYS C 130 ? O LYS C 130 
CC 5 6 N LEU C 133 ? N LEU C 133 O VAL C 20  ? O VAL C 20  
CC 6 7 N ASN C 21  ? N ASN C 21  O GLU C 191 ? O GLU C 191 
DA 1 2 N THR D 112 ? N THR D 112 O ILE D 109 ? O ILE D 109 
DA 2 3 N ALA D 105 ? N ALA D 105 O LYS D 117 ? O LYS D 117 
DA 3 4 N LYS D 117 ? N LYS D 117 O ALA D 105 ? O ALA D 105 
DA 5 6 O LEU D 183 ? O LEU D 183 N MET D 159 ? N MET D 159 
DA 7 8 N LYS D 199 ? N LYS D 199 O VAL D 8   ? O VAL D 8   
DA 8 9 N PHE D 11  ? N PHE D 11  O GLY D 152 ? O GLY D 152 
DB 1 2 N SER D 82  ? N SER D 82  O TYR D 71  ? O TYR D 71  
DB 2 3 N TYR D 74  ? N TYR D 74  O LEU D 62  ? O LEU D 62  
DB 3 4 N LYS D 65  ? N LYS D 65  O TYR D 47  ? O TYR D 47  
DB 4 5 N ASN D 53  ? N ASN D 53  O LYS D 130 ? O LYS D 130 
DB 5 6 N LEU D 133 ? N LEU D 133 O VAL D 20  ? O VAL D 20  
DB 6 7 N ASN D 21  ? N ASN D 21  O GLU D 191 ? O GLU D 191 
EA 1 2 N THR E 112 ? N THR E 112 O ILE E 109 ? O ILE E 109 
EA 2 3 N ALA E 105 ? N ALA E 105 O LYS E 117 ? O LYS E 117 
EA 3 4 N LYS E 117 ? N LYS E 117 O ALA E 105 ? O ALA E 105 
EA 5 6 O LEU E 183 ? O LEU E 183 N MET E 159 ? N MET E 159 
EA 7 8 N LYS E 199 ? N LYS E 199 O VAL E 8   ? O VAL E 8   
EA 8 9 N PHE E 11  ? N PHE E 11  O GLY E 152 ? O GLY E 152 
EB 1 2 N SER E 82  ? N SER E 82  O TYR E 71  ? O TYR E 71  
EB 2 3 N TYR E 74  ? N TYR E 74  O LEU E 62  ? O LEU E 62  
EB 3 4 N LYS E 65  ? N LYS E 65  O TYR E 47  ? O TYR E 47  
EB 4 5 N ASN E 53  ? N ASN E 53  O LYS E 130 ? O LYS E 130 
EB 5 6 N LEU E 133 ? N LEU E 133 O VAL E 20  ? O VAL E 20  
EB 6 7 N ASN E 21  ? N ASN E 21  O GLU E 191 ? O GLU E 191 
# 
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 ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA A 205'  
AC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA A 206'  
AC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG A 207' 
AC4 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE TPO A 500' 
AC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA B 205'  
AC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA B 206'  
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 207' 
AC8 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE TPO B 500' 
AC9 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA C 205'  
BC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA C 206'  
BC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG C 207' 
BC3 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE TPO C 500' 
BC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA D 205'  
BC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA D 206'  
BC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG D 207' 
BC7 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE TPO D 500' 
BC8 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA E 205'  
BC9 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA E 206'  
CC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG E 207' 
CC2 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE TPO E 500' 
# 
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 6  ASP A  58  ? ASP A 58   . ? 1_555 ? 
2   AC1 6  ASN A  59  ? ASN A 59   . ? 1_555 ? 
3   AC1 6  GLU A  136 ? GLU A 136  . ? 1_555 ? 
4   AC1 6  GLN A  137 ? GLN A 137  . ? 1_555 ? 
5   AC1 6  ASP A  138 ? ASP A 138  . ? 1_555 ? 
6   AC1 6  TPO I  .   ? TPO A 500  . ? 1_555 ? 
7   AC2 6  GLU A  136 ? GLU A 136  . ? 1_555 ? 
8   AC2 6  ASP A  138 ? ASP A 138  . ? 1_555 ? 
9   AC2 6  GLN A  148 ? GLN A 148  . ? 1_555 ? 
10  AC2 6  TPO I  .   ? TPO A 500  . ? 1_555 ? 
11  AC2 6  HOH Z  .   ? HOH A 2184 . ? 1_555 ? 
12  AC2 6  HOH Z  .   ? HOH A 2192 . ? 1_555 ? 
13  AC3 7  GLN A  31  ? GLN A 31   . ? 1_555 ? 
14  AC3 7  ASN A  32  ? ASN A 32   . ? 1_555 ? 
15  AC3 7  GLU A  99  ? GLU A 99   . ? 1_555 ? 
16  AC3 7  SER A  101 ? SER A 101  . ? 1_555 ? 
17  AC3 7  HOH Z  .   ? HOH A 2058 . ? 1_555 ? 
18  AC3 7  HOH Z  .   ? HOH A 2150 . ? 1_555 ? 
19  AC3 7  HOH Z  .   ? HOH A 2258 . ? 1_555 ? 
20  AC4 15 ASP A  58  ? ASP A 58   . ? 1_555 ? 
21  AC4 15 ASN A  59  ? ASN A 59   . ? 1_555 ? 
22  AC4 15 LEU A  62  ? LEU A 62   . ? 1_555 ? 
23  AC4 15 TYR A  64  ? TYR A 64   . ? 1_555 ? 
24  AC4 15 TYR A  74  ? TYR A 74   . ? 1_555 ? 
25  AC4 15 GLU A  136 ? GLU A 136  . ? 1_555 ? 
26  AC4 15 ASP A  138 ? ASP A 138  . ? 1_555 ? 
27  AC4 15 GLN A  148 ? GLN A 148  . ? 1_555 ? 
28  AC4 15 CA  F  .   ? CA  A 205  . ? 1_555 ? 
29  AC4 15 CA  G  .   ? CA  A 206  . ? 1_555 ? 
30  AC4 15 HOH Z  .   ? HOH A 2101 . ? 1_555 ? 
31  AC4 15 HOH Z  .   ? HOH A 2106 . ? 1_555 ? 
32  AC4 15 HOH Z  .   ? HOH A 2259 . ? 1_555 ? 
33  AC4 15 HOH Z  .   ? HOH A 2260 . ? 1_555 ? 
34  AC4 15 HOH Z  .   ? HOH A 2261 . ? 1_555 ? 
35  AC5 6  GLU B  136 ? GLU B 136  . ? 1_555 ? 
36  AC5 6  ASP B  138 ? ASP B 138  . ? 1_555 ? 
37  AC5 6  GLN B  148 ? GLN B 148  . ? 1_555 ? 
38  AC5 6  TPO M  .   ? TPO B 500  . ? 1_555 ? 
39  AC5 6  HOH AA .   ? HOH B 2186 . ? 1_555 ? 
40  AC5 6  HOH AA .   ? HOH B 2200 . ? 1_555 ? 
41  AC6 6  ASP B  58  ? ASP B 58   . ? 1_555 ? 
42  AC6 6  ASN B  59  ? ASN B 59   . ? 1_555 ? 
43  AC6 6  GLU B  136 ? GLU B 136  . ? 1_555 ? 
44  AC6 6  GLN B  137 ? GLN B 137  . ? 1_555 ? 
45  AC6 6  ASP B  138 ? ASP B 138  . ? 1_555 ? 
46  AC6 6  TPO M  .   ? TPO B 500  . ? 1_555 ? 
47  AC7 4  GLN B  31  ? GLN B 31   . ? 1_555 ? 
48  AC7 4  ASN B  32  ? ASN B 32   . ? 1_555 ? 
49  AC7 4  GLU B  99  ? GLU B 99   . ? 1_555 ? 
50  AC7 4  HOH AA .   ? HOH B 2059 . ? 1_555 ? 
51  AC8 14 ASP B  58  ? ASP B 58   . ? 1_555 ? 
52  AC8 14 ASN B  59  ? ASN B 59   . ? 1_555 ? 
53  AC8 14 LEU B  62  ? LEU B 62   . ? 1_555 ? 
54  AC8 14 TYR B  74  ? TYR B 74   . ? 1_555 ? 
55  AC8 14 GLU B  136 ? GLU B 136  . ? 1_555 ? 
56  AC8 14 ASP B  138 ? ASP B 138  . ? 1_555 ? 
57  AC8 14 GLN B  148 ? GLN B 148  . ? 1_555 ? 
58  AC8 14 CA  J  .   ? CA  B 205  . ? 1_555 ? 
59  AC8 14 CA  K  .   ? CA  B 206  . ? 1_555 ? 
60  AC8 14 HOH AA .   ? HOH B 2101 . ? 1_555 ? 
61  AC8 14 HOH AA .   ? HOH B 2267 . ? 1_555 ? 
62  AC8 14 HOH AA .   ? HOH B 2268 . ? 1_555 ? 
63  AC8 14 HOH AA .   ? HOH B 2269 . ? 1_555 ? 
64  AC8 14 HOH AA .   ? HOH B 2270 . ? 1_555 ? 
65  AC9 6  ASP C  58  ? ASP C 58   . ? 1_555 ? 
66  AC9 6  ASN C  59  ? ASN C 59   . ? 1_555 ? 
67  AC9 6  GLU C  136 ? GLU C 136  . ? 1_555 ? 
68  AC9 6  GLN C  137 ? GLN C 137  . ? 1_555 ? 
69  AC9 6  ASP C  138 ? ASP C 138  . ? 1_555 ? 
70  AC9 6  TPO Q  .   ? TPO C 500  . ? 1_555 ? 
71  BC1 6  GLU C  136 ? GLU C 136  . ? 1_555 ? 
72  BC1 6  ASP C  138 ? ASP C 138  . ? 1_555 ? 
73  BC1 6  GLN C  148 ? GLN C 148  . ? 1_555 ? 
74  BC1 6  TPO Q  .   ? TPO C 500  . ? 1_555 ? 
75  BC1 6  HOH BA .   ? HOH C 2190 . ? 1_555 ? 
76  BC1 6  HOH BA .   ? HOH C 2199 . ? 1_555 ? 
77  BC2 5  GLN C  31  ? GLN C 31   . ? 1_555 ? 
78  BC2 5  ASN C  32  ? ASN C 32   . ? 1_555 ? 
79  BC2 5  GLU C  99  ? GLU C 99   . ? 1_555 ? 
80  BC2 5  HOH BA .   ? HOH C 2214 . ? 1_555 ? 
81  BC2 5  HOH BA .   ? HOH C 2269 . ? 1_555 ? 
82  BC3 14 ASP C  58  ? ASP C 58   . ? 1_555 ? 
83  BC3 14 ASN C  59  ? ASN C 59   . ? 1_555 ? 
84  BC3 14 LEU C  62  ? LEU C 62   . ? 1_555 ? 
85  BC3 14 TYR C  74  ? TYR C 74   . ? 1_555 ? 
86  BC3 14 GLU C  136 ? GLU C 136  . ? 1_555 ? 
87  BC3 14 ASP C  138 ? ASP C 138  . ? 1_555 ? 
88  BC3 14 GLN C  148 ? GLN C 148  . ? 1_555 ? 
89  BC3 14 CA  N  .   ? CA  C 205  . ? 1_555 ? 
90  BC3 14 CA  O  .   ? CA  C 206  . ? 1_555 ? 
91  BC3 14 HOH BA .   ? HOH C 2101 . ? 1_555 ? 
92  BC3 14 HOH BA .   ? HOH C 2117 . ? 1_555 ? 
93  BC3 14 HOH BA .   ? HOH C 2271 . ? 1_555 ? 
94  BC3 14 HOH BA .   ? HOH C 2272 . ? 1_555 ? 
95  BC3 14 HOH BA .   ? HOH C 2273 . ? 1_555 ? 
96  BC4 6  GLU D  136 ? GLU D 136  . ? 1_555 ? 
97  BC4 6  ASP D  138 ? ASP D 138  . ? 1_555 ? 
98  BC4 6  GLN D  148 ? GLN D 148  . ? 1_555 ? 
99  BC4 6  TPO U  .   ? TPO D 500  . ? 1_555 ? 
100 BC4 6  HOH CA .   ? HOH D 2176 . ? 1_555 ? 
101 BC4 6  HOH CA .   ? HOH D 2190 . ? 1_555 ? 
102 BC5 6  ASP D  58  ? ASP D 58   . ? 1_555 ? 
103 BC5 6  ASN D  59  ? ASN D 59   . ? 1_555 ? 
104 BC5 6  GLU D  136 ? GLU D 136  . ? 1_555 ? 
105 BC5 6  GLN D  137 ? GLN D 137  . ? 1_555 ? 
106 BC5 6  ASP D  138 ? ASP D 138  . ? 1_555 ? 
107 BC5 6  TPO U  .   ? TPO D 500  . ? 1_555 ? 
108 BC6 6  GLN D  31  ? GLN D 31   . ? 1_555 ? 
109 BC6 6  ASN D  32  ? ASN D 32   . ? 1_555 ? 
110 BC6 6  GLU D  99  ? GLU D 99   . ? 1_555 ? 
111 BC6 6  HOH CA .   ? HOH D 2055 . ? 1_555 ? 
112 BC6 6  HOH CA .   ? HOH D 2140 . ? 1_555 ? 
113 BC6 6  HOH CA .   ? HOH D 2265 . ? 1_555 ? 
114 BC7 11 ASP D  58  ? ASP D 58   . ? 1_555 ? 
115 BC7 11 ASN D  59  ? ASN D 59   . ? 1_555 ? 
116 BC7 11 LEU D  62  ? LEU D 62   . ? 1_555 ? 
117 BC7 11 TYR D  74  ? TYR D 74   . ? 1_555 ? 
118 BC7 11 GLU D  136 ? GLU D 136  . ? 1_555 ? 
119 BC7 11 ASP D  138 ? ASP D 138  . ? 1_555 ? 
120 BC7 11 GLN D  148 ? GLN D 148  . ? 1_555 ? 
121 BC7 11 CA  R  .   ? CA  D 205  . ? 1_555 ? 
122 BC7 11 CA  S  .   ? CA  D 206  . ? 1_555 ? 
123 BC7 11 HOH CA .   ? HOH D 2266 . ? 1_555 ? 
124 BC7 11 HOH CA .   ? HOH D 2267 . ? 1_555 ? 
125 BC8 6  ASP E  58  ? ASP E 58   . ? 1_555 ? 
126 BC8 6  ASN E  59  ? ASN E 59   . ? 1_555 ? 
127 BC8 6  GLU E  136 ? GLU E 136  . ? 1_555 ? 
128 BC8 6  GLN E  137 ? GLN E 137  . ? 1_555 ? 
129 BC8 6  ASP E  138 ? ASP E 138  . ? 1_555 ? 
130 BC8 6  TPO Y  .   ? TPO E 500  . ? 1_555 ? 
131 BC9 6  GLU E  136 ? GLU E 136  . ? 1_555 ? 
132 BC9 6  ASP E  138 ? ASP E 138  . ? 1_555 ? 
133 BC9 6  GLN E  148 ? GLN E 148  . ? 1_555 ? 
134 BC9 6  TPO Y  .   ? TPO E 500  . ? 1_555 ? 
135 BC9 6  HOH DA .   ? HOH E 2188 . ? 1_555 ? 
136 BC9 6  HOH DA .   ? HOH E 2201 . ? 1_555 ? 
137 CC1 7  GLN E  31  ? GLN E 31   . ? 1_555 ? 
138 CC1 7  ASN E  32  ? ASN E 32   . ? 1_555 ? 
139 CC1 7  GLU E  99  ? GLU E 99   . ? 1_555 ? 
140 CC1 7  HOH DA .   ? HOH E 2056 . ? 1_555 ? 
141 CC1 7  HOH DA .   ? HOH E 2277 . ? 1_555 ? 
142 CC1 7  HOH DA .   ? HOH E 2278 . ? 1_555 ? 
143 CC1 7  HOH DA .   ? HOH E 2279 . ? 1_555 ? 
144 CC2 15 ASP E  58  ? ASP E 58   . ? 1_555 ? 
145 CC2 15 ASN E  59  ? ASN E 59   . ? 1_555 ? 
146 CC2 15 LEU E  62  ? LEU E 62   . ? 1_555 ? 
147 CC2 15 TYR E  74  ? TYR E 74   . ? 1_555 ? 
148 CC2 15 GLU E  136 ? GLU E 136  . ? 1_555 ? 
149 CC2 15 ASP E  138 ? ASP E 138  . ? 1_555 ? 
150 CC2 15 GLN E  148 ? GLN E 148  . ? 1_555 ? 
151 CC2 15 CA  V  .   ? CA  E 205  . ? 1_555 ? 
152 CC2 15 CA  W  .   ? CA  E 206  . ? 1_555 ? 
153 CC2 15 HOH DA .   ? HOH E 2097 . ? 1_555 ? 
154 CC2 15 HOH DA .   ? HOH E 2109 . ? 1_555 ? 
155 CC2 15 HOH DA .   ? HOH E 2128 . ? 1_555 ? 
156 CC2 15 HOH DA .   ? HOH E 2280 . ? 1_555 ? 
157 CC2 15 HOH DA .   ? HOH E 2281 . ? 1_555 ? 
158 CC2 15 HOH DA .   ? HOH E 2282 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2W08 
_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                    2W08 
_atom_sites.fract_transf_matrix[1][1]   0.010552 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001305 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014402 
_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]   0.009873 
_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  
CA 
N  
O  
P  
S  
# 
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   . HIS A  1 1   ? 1.222   -7.219  66.612  1.00 41.42 ? 1    HIS A N   1 
ATOM   2    C  CA  . HIS A  1 1   ? -0.117  -7.587  67.040  1.00 40.98 ? 1    HIS A CA  1 
ATOM   3    C  C   . HIS A  1 1   ? -1.044  -7.746  65.844  1.00 41.59 ? 1    HIS A C   1 
ATOM   4    O  O   . HIS A  1 1   ? -2.178  -8.201  65.985  1.00 29.62 ? 1    HIS A O   1 
ATOM   5    C  CB  . HIS A  1 1   ? -0.649  -6.542  68.010  1.00 41.31 ? 1    HIS A CB  1 
ATOM   6    C  CG  . HIS A  1 1   ? 0.410   -5.978  68.903  1.00 53.51 ? 1    HIS A CG  1 
ATOM   7    N  ND1 . HIS A  1 1   ? 1.419   -6.753  69.434  1.00 51.76 ? 1    HIS A ND1 1 
ATOM   8    C  CD2 . HIS A  1 1   ? 0.624   -4.720  69.352  1.00 49.16 ? 1    HIS A CD2 1 
ATOM   9    C  CE1 . HIS A  1 1   ? 2.208   -5.996  70.174  1.00 53.07 ? 1    HIS A CE1 1 
ATOM   10   N  NE2 . HIS A  1 1   ? 1.747   -4.759  70.142  1.00 61.36 ? 1    HIS A NE2 1 
ATOM   11   N  N   . THR A  1 2   ? -0.554  -7.363  64.669  1.00 22.84 ? 2    THR A N   1 
ATOM   12   C  CA  . THR A  1 2   ? -1.240  -7.659  63.417  1.00 16.02 ? 2    THR A CA  1 
ATOM   13   C  C   . THR A  1 2   ? -0.278  -8.390  62.483  1.00 19.02 ? 2    THR A C   1 
ATOM   14   O  O   . THR A  1 2   ? 0.873   -7.980  62.329  1.00 18.30 ? 2    THR A O   1 
ATOM   15   C  CB  . THR A  1 2   ? -1.736  -6.380  62.720  1.00 21.61 ? 2    THR A CB  1 
ATOM   16   O  OG1 . THR A  1 2   ? -2.604  -5.653  63.597  1.00 32.22 ? 2    THR A OG1 1 
ATOM   17   C  CG2 . THR A  1 2   ? -2.484  -6.726  61.441  1.00 19.37 ? 2    THR A CG2 1 
ATOM   18   N  N   . ASP A  1 3   ? -0.738  -9.481  61.877  1.00 15.14 ? 3    ASP A N   1 
ATOM   19   C  CA  . ASP A  1 3   ? 0.053   -10.185 60.875  1.00 16.84 ? 3    ASP A CA  1 
ATOM   20   C  C   . ASP A  1 3   ? -0.247  -9.558  59.520  1.00 18.20 ? 3    ASP A C   1 
ATOM   21   O  O   . ASP A  1 3   ? -1.325  -9.759  58.961  1.00 16.70 ? 3    ASP A O   1 
ATOM   22   C  CB  . ASP A  1 3   ? -0.285  -11.683 60.869  1.00 18.06 ? 3    ASP A CB  1 
ATOM   23   C  CG  . ASP A  1 3   ? 0.526   -12.477 59.850  1.00 22.91 ? 3    ASP A CG  1 
ATOM   24   O  OD1 . ASP A  1 3   ? 1.296   -11.886 59.057  1.00 16.18 ? 3    ASP A OD1 1 
ATOM   25   O  OD2 . ASP A  1 3   ? 0.388   -13.718 59.831  1.00 22.65 ? 3    ASP A OD2 1 
ATOM   26   N  N   . LEU A  1 4   ? 0.699   -8.779  59.001  1.00 13.29 ? 4    LEU A N   1 
ATOM   27   C  CA  . LEU A  1 4   ? 0.489   -8.122  57.711  1.00 13.75 ? 4    LEU A CA  1 
ATOM   28   C  C   . LEU A  1 4   ? 1.028   -8.911  56.528  1.00 12.55 ? 4    LEU A C   1 
ATOM   29   O  O   . LEU A  1 4   ? 1.213   -8.353  55.446  1.00 12.51 ? 4    LEU A O   1 
ATOM   30   C  CB  . LEU A  1 4   ? 1.073   -6.700  57.722  1.00 9.04  ? 4    LEU A CB  1 
ATOM   31   C  CG  . LEU A  1 4   ? 0.374   -5.698  58.637  1.00 13.61 ? 4    LEU A CG  1 
ATOM   32   C  CD1 . LEU A  1 4   ? 1.133   -4.376  58.686  1.00 18.13 ? 4    LEU A CD1 1 
ATOM   33   C  CD2 . LEU A  1 4   ? -1.063  -5.463  58.191  1.00 17.66 ? 4    LEU A CD2 1 
ATOM   34   N  N   . SER A  1 5   ? 1.273   -10.209 56.714  1.00 11.91 ? 5    SER A N   1 
ATOM   35   C  CA  . SER A  1 5   ? 1.733   -11.048 55.609  1.00 11.79 ? 5    SER A CA  1 
ATOM   36   C  C   . SER A  1 5   ? 0.873   -10.828 54.373  1.00 12.08 ? 5    SER A C   1 
ATOM   37   O  O   . SER A  1 5   ? -0.353  -10.899 54.443  1.00 14.96 ? 5    SER A O   1 
ATOM   38   C  CB  . SER A  1 5   ? 1.650   -12.532 55.982  1.00 15.55 ? 5    SER A CB  1 
ATOM   39   O  OG  . SER A  1 5   ? 2.640   -12.888 56.924  1.00 16.93 ? 5    SER A OG  1 
ATOM   40   N  N   . GLY A  1 6   ? 1.516   -10.578 53.242  1.00 10.52 ? 6    GLY A N   1 
ATOM   41   C  CA  . GLY A  1 6   ? 0.808   -10.464 51.987  1.00 13.89 ? 6    GLY A CA  1 
ATOM   42   C  C   . GLY A  1 6   ? 0.136   -9.123  51.781  1.00 15.10 ? 6    GLY A C   1 
ATOM   43   O  O   . GLY A  1 6   ? -0.620  -8.959  50.823  1.00 13.50 ? 6    GLY A O   1 
ATOM   44   N  N   . LYS A  1 7   ? 0.399   -8.178  52.682  1.00 10.89 ? 7    LYS A N   1 
ATOM   45   C  CA  . LYS A  1 7   ? -0.198  -6.843  52.603  1.00 9.53  ? 7    LYS A CA  1 
ATOM   46   C  C   . LYS A  1 7   ? 0.881   -5.758  52.607  1.00 9.94  ? 7    LYS A C   1 
ATOM   47   O  O   . LYS A  1 7   ? 2.022   -6.004  53.011  1.00 11.47 ? 7    LYS A O   1 
ATOM   48   C  CB  . LYS A  1 7   ? -1.167  -6.614  53.764  1.00 13.84 ? 7    LYS A CB  1 
ATOM   49   C  CG  . LYS A  1 7   ? -2.283  -7.654  53.833  1.00 14.00 ? 7    LYS A CG  1 
ATOM   50   C  CD  . LYS A  1 7   ? -3.192  -7.423  55.026  1.00 17.65 ? 7    LYS A CD  1 
ATOM   51   C  CE  . LYS A  1 7   ? -4.286  -8.478  55.078  1.00 29.84 ? 7    LYS A CE  1 
ATOM   52   N  NZ  . LYS A  1 7   ? -5.135  -8.417  53.859  1.00 41.94 ? 7    LYS A NZ  1 
ATOM   53   N  N   . VAL A  1 8   ? 0.510   -4.565  52.152  1.00 11.12 ? 8    VAL A N   1 
ATOM   54   C  CA  . VAL A  1 8   ? 1.403   -3.407  52.170  1.00 7.58  ? 8    VAL A CA  1 
ATOM   55   C  C   . VAL A  1 8   ? 0.691   -2.214  52.780  1.00 11.42 ? 8    VAL A C   1 
ATOM   56   O  O   . VAL A  1 8   ? -0.540  -2.159  52.806  1.00 11.06 ? 8    VAL A O   1 
ATOM   57   C  CB  . VAL A  1 8   ? 1.840   -2.981  50.743  1.00 10.76 ? 8    VAL A CB  1 
ATOM   58   C  CG1 . VAL A  1 8   ? 2.770   -4.007  50.128  1.00 15.56 ? 8    VAL A CG1 1 
ATOM   59   C  CG2 . VAL A  1 8   ? 0.629   -2.725  49.846  1.00 11.52 ? 8    VAL A CG2 1 
ATOM   60   N  N   . PHE A  1 9   ? 1.464   -1.255  53.281  1.00 8.56  ? 9    PHE A N   1 
ATOM   61   C  CA  . PHE A  1 9   ? 0.927   0.080   53.510  1.00 8.36  ? 9    PHE A CA  1 
ATOM   62   C  C   . PHE A  1 9   ? 1.004   0.854   52.206  1.00 10.75 ? 9    PHE A C   1 
ATOM   63   O  O   . PHE A  1 9   ? 2.064   0.896   51.565  1.00 10.30 ? 9    PHE A O   1 
ATOM   64   C  CB  . PHE A  1 9   ? 1.743   0.846   54.547  1.00 8.21  ? 9    PHE A CB  1 
ATOM   65   C  CG  . PHE A  1 9   ? 1.572   0.352   55.955  1.00 11.66 ? 9    PHE A CG  1 
ATOM   66   C  CD1 . PHE A  1 9   ? 0.313   0.282   56.541  1.00 14.87 ? 9    PHE A CD1 1 
ATOM   67   C  CD2 . PHE A  1 9   ? 2.677   -0.014  56.705  1.00 14.10 ? 9    PHE A CD2 1 
ATOM   68   C  CE1 . PHE A  1 9   ? 0.164   -0.167  57.856  1.00 15.78 ? 9    PHE A CE1 1 
ATOM   69   C  CE2 . PHE A  1 9   ? 2.537   -0.461  58.016  1.00 11.84 ? 9    PHE A CE2 1 
ATOM   70   C  CZ  . PHE A  1 9   ? 1.278   -0.544  58.586  1.00 14.11 ? 9    PHE A CZ  1 
ATOM   71   N  N   . VAL A  1 10  ? -0.106  1.476   51.817  1.00 8.18  ? 10   VAL A N   1 
ATOM   72   C  CA  . VAL A  1 10  ? -0.103  2.349   50.646  1.00 10.84 ? 10   VAL A CA  1 
ATOM   73   C  C   . VAL A  1 10  ? -0.207  3.780   51.129  1.00 9.49  ? 10   VAL A C   1 
ATOM   74   O  O   . VAL A  1 10  ? -1.164  4.140   51.828  1.00 8.82  ? 10   VAL A O   1 
ATOM   75   C  CB  . VAL A  1 10  ? -1.281  2.065   49.697  1.00 9.77  ? 10   VAL A CB  1 
ATOM   76   C  CG1 . VAL A  1 10  ? -1.180  2.954   48.449  1.00 11.84 ? 10   VAL A CG1 1 
ATOM   77   C  CG2 . VAL A  1 10  ? -1.330  0.588   49.321  1.00 10.88 ? 10   VAL A CG2 1 
ATOM   78   N  N   . PHE A  1 11  ? 0.799   4.581   50.785  1.00 7.87  ? 11   PHE A N   1 
ATOM   79   C  CA  . PHE A  1 11  ? 0.791   6.016   51.020  1.00 9.84  ? 11   PHE A CA  1 
ATOM   80   C  C   . PHE A  1 11  ? 0.402   6.620   49.676  1.00 8.45  ? 11   PHE A C   1 
ATOM   81   O  O   . PHE A  1 11  ? 1.244   6.776   48.794  1.00 9.77  ? 11   PHE A O   1 
ATOM   82   C  CB  . PHE A  1 11  ? 2.189   6.476   51.466  1.00 7.52  ? 11   PHE A CB  1 
ATOM   83   C  CG  . PHE A  1 11  ? 2.663   5.799   52.737  1.00 8.52  ? 11   PHE A CG  1 
ATOM   84   C  CD1 . PHE A  1 11  ? 3.293   4.565   52.686  1.00 10.03 ? 11   PHE A CD1 1 
ATOM   85   C  CD2 . PHE A  1 11  ? 2.438   6.386   53.970  1.00 11.62 ? 11   PHE A CD2 1 
ATOM   86   C  CE1 . PHE A  1 11  ? 3.700   3.921   53.853  1.00 10.67 ? 11   PHE A CE1 1 
ATOM   87   C  CE2 . PHE A  1 11  ? 2.841   5.757   55.148  1.00 9.21  ? 11   PHE A CE2 1 
ATOM   88   C  CZ  . PHE A  1 11  ? 3.472   4.525   55.091  1.00 8.74  ? 11   PHE A CZ  1 
ATOM   89   N  N   . PRO A  1 12  ? -0.891  6.921   49.491  1.00 10.24 ? 12   PRO A N   1 
ATOM   90   C  CA  . PRO A  1 12  ? -1.374  7.084   48.114  1.00 8.43  ? 12   PRO A CA  1 
ATOM   91   C  C   . PRO A  1 12  ? -1.172  8.475   47.539  1.00 10.79 ? 12   PRO A C   1 
ATOM   92   O  O   . PRO A  1 12  ? -1.508  8.688   46.371  1.00 10.48 ? 12   PRO A O   1 
ATOM   93   C  CB  . PRO A  1 12  ? -2.883  6.780   48.239  1.00 10.32 ? 12   PRO A CB  1 
ATOM   94   C  CG  . PRO A  1 12  ? -3.049  6.157   49.636  1.00 9.97  ? 12   PRO A CG  1 
ATOM   95   C  CD  . PRO A  1 12  ? -2.010  6.863   50.445  1.00 10.52 ? 12   PRO A CD  1 
ATOM   96   N  N   . ARG A  1 13  ? -0.629  9.396   48.329  1.00 9.36  ? 13   ARG A N   1 
ATOM   97   C  CA  . ARG A  1 13  ? -0.489  10.767  47.875  1.00 11.18 ? 13   ARG A CA  1 
ATOM   98   C  C   . ARG A  1 13  ? 0.660   11.470  48.578  1.00 13.84 ? 13   ARG A C   1 
ATOM   99   O  O   . ARG A  1 13  ? 1.095   11.067  49.660  1.00 11.98 ? 13   ARG A O   1 
ATOM   100  C  CB  . ARG A  1 13  ? -1.778  11.547  48.150  1.00 12.42 ? 13   ARG A CB  1 
ATOM   101  C  CG  . ARG A  1 13  ? -1.951  11.805  49.622  1.00 12.65 ? 13   ARG A CG  1 
ATOM   102  C  CD  . ARG A  1 13  ? -3.178  12.632  49.951  1.00 15.01 ? 13   ARG A CD  1 
ATOM   103  N  NE  . ARG A  1 13  ? -3.301  12.730  51.402  1.00 15.44 ? 13   ARG A NE  1 
ATOM   104  C  CZ  . ARG A  1 13  ? -4.296  13.342  52.031  1.00 19.89 ? 13   ARG A CZ  1 
ATOM   105  N  NH1 . ARG A  1 13  ? -5.270  13.912  51.332  1.00 22.21 ? 13   ARG A NH1 1 
ATOM   106  N  NH2 . ARG A  1 13  ? -4.323  13.371  53.358  1.00 16.45 ? 13   ARG A NH2 1 
ATOM   107  N  N   . GLU A  1 14  ? 1.144   12.537  47.955  1.00 11.83 ? 14   GLU A N   1 
ATOM   108  C  CA  . GLU A  1 14  ? 2.088   13.417  48.616  1.00 10.68 ? 14   GLU A CA  1 
ATOM   109  C  C   . GLU A  1 14  ? 1.375   14.256  49.670  1.00 13.20 ? 14   GLU A C   1 
ATOM   110  O  O   . GLU A  1 14  ? 0.294   14.786  49.423  1.00 14.53 ? 14   GLU A O   1 
ATOM   111  C  CB  . GLU A  1 14  ? 2.743   14.333  47.588  1.00 14.68 ? 14   GLU A CB  1 
ATOM   112  C  CG  . GLU A  1 14  ? 3.830   15.192  48.163  1.00 14.68 ? 14   GLU A CG  1 
ATOM   113  C  CD  . GLU A  1 14  ? 4.593   15.919  47.080  1.00 20.71 ? 14   GLU A CD  1 
ATOM   114  O  OE1 . GLU A  1 14  ? 4.379   17.140  46.929  1.00 29.65 ? 14   GLU A OE1 1 
ATOM   115  O  OE2 . GLU A  1 14  ? 5.367   15.260  46.359  1.00 18.20 ? 14   GLU A OE2 1 
ATOM   116  N  N   . SER A  1 15  ? 1.992   14.385  50.840  1.00 12.93 ? 15   SER A N   1 
ATOM   117  C  CA  . SER A  1 15  ? 1.385   15.098  51.951  1.00 15.82 ? 15   SER A CA  1 
ATOM   118  C  C   . SER A  1 15  ? 2.425   15.376  53.012  1.00 16.22 ? 15   SER A C   1 
ATOM   119  O  O   . SER A  1 15  ? 3.542   14.874  52.943  1.00 14.53 ? 15   SER A O   1 
ATOM   120  C  CB  . SER A  1 15  ? 0.297   14.240  52.586  1.00 16.35 ? 15   SER A CB  1 
ATOM   121  O  OG  . SER A  1 15  ? 0.890   13.301  53.474  1.00 14.25 ? 15   SER A OG  1 
ATOM   122  N  N   . VAL A  1 16  ? 2.036   16.156  54.012  1.00 17.86 ? 16   VAL A N   1 
ATOM   123  C  CA  . VAL A  1 16  ? 2.845   16.327  55.210  1.00 15.38 ? 16   VAL A CA  1 
ATOM   124  C  C   . VAL A  1 16  ? 2.134   15.671  56.391  1.00 15.33 ? 16   VAL A C   1 
ATOM   125  O  O   . VAL A  1 16  ? 2.587   15.759  57.531  1.00 24.88 ? 16   VAL A O   1 
ATOM   126  C  CB  . VAL A  1 16  ? 3.104   17.822  55.496  1.00 22.75 ? 16   VAL A CB  1 
ATOM   127  C  CG1 . VAL A  1 16  ? 1.857   18.474  56.067  1.00 22.02 ? 16   VAL A CG1 1 
ATOM   128  C  CG2 . VAL A  1 16  ? 4.288   17.997  56.434  1.00 26.11 ? 16   VAL A CG2 1 
ATOM   129  N  N   . THR A  1 17  ? 1.029   14.985  56.110  1.00 17.27 ? 17   THR A N   1 
ATOM   130  C  CA  . THR A  1 17  ? 0.172   14.434  57.156  1.00 20.55 ? 17   THR A CA  1 
ATOM   131  C  C   . THR A  1 17  ? 0.192   12.915  57.270  1.00 17.33 ? 17   THR A C   1 
ATOM   132  O  O   . THR A  1 17  ? 0.068   12.372  58.368  1.00 20.86 ? 17   THR A O   1 
ATOM   133  C  CB  . THR A  1 17  ? -1.300  14.826  56.917  1.00 20.14 ? 17   THR A CB  1 
ATOM   134  O  OG1 . THR A  1 17  ? -1.672  14.483  55.569  1.00 23.86 ? 17   THR A OG1 1 
ATOM   135  C  CG2 . THR A  1 17  ? -1.491  16.317  57.124  1.00 23.39 ? 17   THR A CG2 1 
ATOM   136  N  N   . ASP A  1 18  ? 0.295   12.237  56.129  1.00 15.47 ? 18   ASP A N   1 
ATOM   137  C  CA  . ASP A  1 18  ? 0.067   10.800  56.073  1.00 15.37 ? 18   ASP A CA  1 
ATOM   138  C  C   . ASP A  1 18  ? 1.297   10.055  56.559  1.00 14.09 ? 18   ASP A C   1 
ATOM   139  O  O   . ASP A  1 18  ? 2.391   10.251  56.030  1.00 14.25 ? 18   ASP A O   1 
ATOM   140  C  CB  . ASP A  1 18  ? -0.270  10.369  54.641  1.00 12.57 ? 18   ASP A CB  1 
ATOM   141  C  CG  . ASP A  1 18  ? -1.351  11.235  54.005  1.00 15.90 ? 18   ASP A CG  1 
ATOM   142  O  OD1 . ASP A  1 18  ? -2.167  11.810  54.763  1.00 14.06 ? 18   ASP A OD1 1 
ATOM   143  O  OD2 . ASP A  1 18  ? -1.384  11.334  52.751  1.00 13.58 ? 18   ASP A OD2 1 
ATOM   144  N  N   . HIS A  1 19  ? 1.124   9.204   57.566  1.00 10.10 ? 19   HIS A N   1 
ATOM   145  C  CA  . HIS A  1 19  ? 2.248   8.445   58.106  1.00 13.05 ? 19   HIS A CA  1 
ATOM   146  C  C   . HIS A  1 19  ? 1.806   7.262   58.943  1.00 15.08 ? 19   HIS A C   1 
ATOM   147  O  O   . HIS A  1 19  ? 0.644   7.166   59.338  1.00 14.45 ? 19   HIS A O   1 
ATOM   148  C  CB  . HIS A  1 19  ? 3.210   9.340   58.913  1.00 11.43 ? 19   HIS A CB  1 
ATOM   149  C  CG  . HIS A  1 19  ? 2.623   9.921   60.169  1.00 11.29 ? 19   HIS A CG  1 
ATOM   150  N  ND1 . HIS A  1 19  ? 1.694   10.940  60.159  1.00 14.89 ? 19   HIS A ND1 1 
ATOM   151  C  CD2 . HIS A  1 19  ? 2.885   9.665   61.474  1.00 16.83 ? 19   HIS A CD2 1 
ATOM   152  C  CE1 . HIS A  1 19  ? 1.387   11.267  61.404  1.00 16.33 ? 19   HIS A CE1 1 
ATOM   153  N  NE2 . HIS A  1 19  ? 2.097   10.511  62.220  1.00 15.27 ? 19   HIS A NE2 1 
ATOM   154  N  N   . VAL A  1 20  ? 2.738   6.346   59.185  1.00 10.79 ? 20   VAL A N   1 
ATOM   155  C  CA  . VAL A  1 20  ? 2.499   5.238   60.093  1.00 10.26 ? 20   VAL A CA  1 
ATOM   156  C  C   . VAL A  1 20  ? 3.537   5.274   61.210  1.00 14.95 ? 20   VAL A C   1 
ATOM   157  O  O   . VAL A  1 20  ? 4.734   5.358   60.951  1.00 13.20 ? 20   VAL A O   1 
ATOM   158  C  CB  . VAL A  1 20  ? 2.613   3.867   59.394  1.00 13.87 ? 20   VAL A CB  1 
ATOM   159  C  CG1 . VAL A  1 20  ? 2.434   2.750   60.420  1.00 12.44 ? 20   VAL A CG1 1 
ATOM   160  C  CG2 . VAL A  1 20  ? 1.588   3.729   58.271  1.00 11.26 ? 20   VAL A CG2 1 
ATOM   161  N  N   . ASN A  1 21  ? 3.082   5.220   62.457  1.00 12.31 ? 21   ASN A N   1 
ATOM   162  C  CA  . ASN A  1 21  ? 4.000   5.067   63.577  1.00 11.37 ? 21   ASN A CA  1 
ATOM   163  C  C   . ASN A  1 21  ? 4.182   3.590   63.867  1.00 13.49 ? 21   ASN A C   1 
ATOM   164  O  O   . ASN A  1 21  ? 3.209   2.849   63.982  1.00 15.13 ? 21   ASN A O   1 
ATOM   165  C  CB  . ASN A  1 21  ? 3.468   5.768   64.828  1.00 15.56 ? 21   ASN A CB  1 
ATOM   166  C  CG  . ASN A  1 21  ? 3.231   7.249   64.618  1.00 19.82 ? 21   ASN A CG  1 
ATOM   167  O  OD1 . ASN A  1 21  ? 4.047   7.946   64.019  1.00 18.10 ? 21   ASN A OD1 1 
ATOM   168  N  ND2 . ASN A  1 21  ? 2.107   7.740   65.126  1.00 19.15 ? 21   ASN A ND2 1 
ATOM   169  N  N   . LEU A  1 22  ? 5.431   3.154   63.975  1.00 12.51 ? 22   LEU A N   1 
ATOM   170  C  CA  . LEU A  1 22  ? 5.715   1.761   64.300  1.00 12.05 ? 22   LEU A CA  1 
ATOM   171  C  C   . LEU A  1 22  ? 6.130   1.676   65.755  1.00 18.29 ? 22   LEU A C   1 
ATOM   172  O  O   . LEU A  1 22  ? 6.964   2.453   66.207  1.00 16.27 ? 22   LEU A O   1 
ATOM   173  C  CB  . LEU A  1 22  ? 6.829   1.217   63.398  1.00 14.24 ? 22   LEU A CB  1 
ATOM   174  C  CG  . LEU A  1 22  ? 6.519   1.253   61.900  1.00 12.55 ? 22   LEU A CG  1 
ATOM   175  C  CD1 . LEU A  1 22  ? 7.692   0.711   61.089  1.00 11.90 ? 22   LEU A CD1 1 
ATOM   176  C  CD2 . LEU A  1 22  ? 5.254   0.458   61.606  1.00 14.37 ? 22   LEU A CD2 1 
ATOM   177  N  N   . ILE A  1 23  ? 5.531   0.738   66.486  1.00 16.62 ? 23   ILE A N   1 
ATOM   178  C  CA  . ILE A  1 23  ? 5.723   0.644   67.926  1.00 18.04 ? 23   ILE A CA  1 
ATOM   179  C  C   . ILE A  1 23  ? 6.571   -0.560  68.293  1.00 17.70 ? 23   ILE A C   1 
ATOM   180  O  O   . ILE A  1 23  ? 6.239   -1.694  67.954  1.00 22.53 ? 23   ILE A O   1 
ATOM   181  C  CB  . ILE A  1 23  ? 4.363   0.520   68.649  1.00 19.78 ? 23   ILE A CB  1 
ATOM   182  C  CG1 . ILE A  1 23  ? 3.390   1.591   68.153  1.00 24.80 ? 23   ILE A CG1 1 
ATOM   183  C  CG2 . ILE A  1 23  ? 4.555   0.581   70.159  1.00 23.71 ? 23   ILE A CG2 1 
ATOM   184  C  CD1 . ILE A  1 23  ? 3.891   3.008   68.331  1.00 28.61 ? 23   ILE A CD1 1 
ATOM   185  N  N   . THR A  1 24  ? 7.675   -0.315  68.988  1.00 21.58 ? 24   THR A N   1 
ATOM   186  C  CA  . THR A  1 24  ? 8.531   -1.409  69.420  1.00 18.74 ? 24   THR A CA  1 
ATOM   187  C  C   . THR A  1 24  ? 8.874   -1.304  70.903  1.00 27.51 ? 24   THR A C   1 
ATOM   188  O  O   . THR A  1 24  ? 8.993   -0.206  71.438  1.00 31.38 ? 24   THR A O   1 
ATOM   189  C  CB  . THR A  1 24  ? 9.827   -1.486  68.583  1.00 27.38 ? 24   THR A CB  1 
ATOM   190  O  OG1 . THR A  1 24  ? 10.681  -2.507  69.113  1.00 25.77 ? 24   THR A OG1 1 
ATOM   191  C  CG2 . THR A  1 24  ? 10.562  -0.163  68.609  1.00 24.52 ? 24   THR A CG2 1 
ATOM   192  N  N   . PRO A  1 25  ? 9.033   -2.460  71.567  1.00 39.09 ? 25   PRO A N   1 
ATOM   193  C  CA  . PRO A  1 25  ? 9.492   -2.540  72.957  1.00 49.79 ? 25   PRO A CA  1 
ATOM   194  C  C   . PRO A  1 25  ? 11.011  -2.414  73.022  1.00 51.51 ? 25   PRO A C   1 
ATOM   195  O  O   . PRO A  1 25  ? 11.697  -3.426  73.168  1.00 64.46 ? 25   PRO A O   1 
ATOM   196  C  CB  . PRO A  1 25  ? 9.087   -3.960  73.382  1.00 43.30 ? 25   PRO A CB  1 
ATOM   197  C  CG  . PRO A  1 25  ? 8.303   -4.540  72.228  1.00 51.21 ? 25   PRO A CG  1 
ATOM   198  C  CD  . PRO A  1 25  ? 8.736   -3.791  71.018  1.00 40.53 ? 25   PRO A CD  1 
ATOM   199  N  N   . LEU A  1 26  ? 11.533  -1.197  72.906  1.00 50.79 ? 26   LEU A N   1 
ATOM   200  C  CA  . LEU A  1 26  ? 12.979  -1.011  72.875  1.00 38.89 ? 26   LEU A CA  1 
ATOM   201  C  C   . LEU A  1 26  ? 13.433  0.072   73.846  1.00 46.13 ? 26   LEU A C   1 
ATOM   202  O  O   . LEU A  1 26  ? 13.293  1.267   73.572  1.00 47.35 ? 26   LEU A O   1 
ATOM   203  C  CB  . LEU A  1 26  ? 13.449  -0.685  71.452  1.00 48.25 ? 26   LEU A CB  1 
ATOM   204  C  CG  . LEU A  1 26  ? 14.941  -0.856  71.149  1.00 40.98 ? 26   LEU A CG  1 
ATOM   205  C  CD1 . LEU A  1 26  ? 15.384  -2.290  71.408  1.00 36.63 ? 26   LEU A CD1 1 
ATOM   206  C  CD2 . LEU A  1 26  ? 15.243  -0.456  69.713  1.00 36.48 ? 26   LEU A CD2 1 
ATOM   207  N  N   . GLU A  1 27  ? 13.983  -0.353  74.979  1.00 34.16 ? 27   GLU A N   1 
ATOM   208  C  CA  . GLU A  1 27  ? 14.463  0.584   75.989  1.00 39.38 ? 27   GLU A CA  1 
ATOM   209  C  C   . GLU A  1 27  ? 15.984  0.605   76.042  1.00 36.24 ? 27   GLU A C   1 
ATOM   210  O  O   . GLU A  1 27  ? 16.580  1.500   76.641  1.00 40.28 ? 27   GLU A O   1 
ATOM   211  C  CB  . GLU A  1 27  ? 13.906  0.238   77.374  1.00 51.63 ? 27   GLU A CB  1 
ATOM   212  C  CG  . GLU A  1 27  ? 12.388  0.248   77.478  1.00 67.89 ? 27   GLU A CG  1 
ATOM   213  C  CD  . GLU A  1 27  ? 11.789  -1.147  77.443  1.00 82.59 ? 27   GLU A CD  1 
ATOM   214  O  OE1 . GLU A  1 27  ? 12.561  -2.129  77.486  1.00 87.44 ? 27   GLU A OE1 1 
ATOM   215  O  OE2 . GLU A  1 27  ? 10.545  -1.260  77.382  1.00 82.11 ? 27   GLU A OE2 1 
ATOM   216  N  N   . LYS A  1 28  ? 16.609  -0.388  75.416  1.00 30.96 ? 28   LYS A N   1 
ATOM   217  C  CA  . LYS A  1 28  ? 18.062  -0.495  75.416  1.00 23.17 ? 28   LYS A CA  1 
ATOM   218  C  C   . LYS A  1 28  ? 18.654  0.096   74.142  1.00 26.99 ? 28   LYS A C   1 
ATOM   219  O  O   . LYS A  1 28  ? 18.137  -0.139  73.052  1.00 22.09 ? 28   LYS A O   1 
ATOM   220  C  CB  . LYS A  1 28  ? 18.499  -1.956  75.558  1.00 27.28 ? 28   LYS A CB  1 
ATOM   221  C  CG  . LYS A  1 28  ? 17.761  -2.939  74.644  1.00 45.88 ? 28   LYS A CG  1 
ATOM   222  C  CD  . LYS A  1 28  ? 18.302  -2.959  73.209  1.00 38.99 ? 28   LYS A CD  1 
ATOM   223  C  CE  . LYS A  1 28  ? 19.590  -3.763  73.087  1.00 41.48 ? 28   LYS A CE  1 
ATOM   224  N  NZ  . LYS A  1 28  ? 19.929  -4.054  71.661  1.00 35.15 ? 28   LYS A NZ  1 
ATOM   225  N  N   . PRO A  1 29  ? 19.732  0.879   74.278  1.00 24.11 ? 29   PRO A N   1 
ATOM   226  C  CA  . PRO A  1 29  ? 20.439  1.392   73.098  1.00 21.15 ? 29   PRO A CA  1 
ATOM   227  C  C   . PRO A  1 29  ? 20.895  0.259   72.176  1.00 20.82 ? 29   PRO A C   1 
ATOM   228  O  O   . PRO A  1 29  ? 21.260  -0.821  72.651  1.00 21.80 ? 29   PRO A O   1 
ATOM   229  C  CB  . PRO A  1 29  ? 21.643  2.114   73.704  1.00 24.38 ? 29   PRO A CB  1 
ATOM   230  C  CG  . PRO A  1 29  ? 21.166  2.539   75.068  1.00 30.06 ? 29   PRO A CG  1 
ATOM   231  C  CD  . PRO A  1 29  ? 20.287  1.412   75.536  1.00 25.32 ? 29   PRO A CD  1 
ATOM   232  N  N   A LEU A  1 30  ? 20.862  0.506   70.868  0.38 17.64 ? 30   LEU A N   1 
ATOM   233  N  N   B LEU A  1 30  ? 20.884  0.525   70.870  0.62 17.55 ? 30   LEU A N   1 
ATOM   234  C  CA  A LEU A  1 30  ? 21.224  -0.506  69.879  0.38 19.93 ? 30   LEU A CA  1 
ATOM   235  C  CA  B LEU A  1 30  ? 21.229  -0.466  69.857  0.62 20.00 ? 30   LEU A CA  1 
ATOM   236  C  C   A LEU A  1 30  ? 22.692  -0.445  69.481  0.38 13.96 ? 30   LEU A C   1 
ATOM   237  C  C   B LEU A  1 30  ? 22.709  -0.433  69.496  0.62 13.83 ? 30   LEU A C   1 
ATOM   238  O  O   A LEU A  1 30  ? 23.191  0.606   69.082  0.38 17.48 ? 30   LEU A O   1 
ATOM   239  O  O   B LEU A  1 30  ? 23.230  0.615   69.123  0.62 17.55 ? 30   LEU A O   1 
ATOM   240  C  CB  A LEU A  1 30  ? 20.364  -0.361  68.620  0.38 19.46 ? 30   LEU A CB  1 
ATOM   241  C  CB  B LEU A  1 30  ? 20.433  -0.198  68.578  0.62 19.33 ? 30   LEU A CB  1 
ATOM   242  C  CG  A LEU A  1 30  ? 19.268  -1.401  68.390  0.38 23.24 ? 30   LEU A CG  1 
ATOM   243  C  CG  B LEU A  1 30  ? 18.997  -0.696  68.468  0.62 22.26 ? 30   LEU A CG  1 
ATOM   244  C  CD1 A LEU A  1 30  ? 18.531  -1.712  69.683  0.38 22.57 ? 30   LEU A CD1 1 
ATOM   245  C  CD1 B LEU A  1 30  ? 18.388  -0.197  67.164  0.62 18.98 ? 30   LEU A CD1 1 
ATOM   246  C  CD2 A LEU A  1 30  ? 18.307  -0.927  67.305  0.38 23.21 ? 30   LEU A CD2 1 
ATOM   247  C  CD2 B LEU A  1 30  ? 18.980  -2.218  68.531  0.62 20.84 ? 30   LEU A CD2 1 
ATOM   248  N  N   . GLN A  1 31  ? 23.368  -1.584  69.577  1.00 14.83 ? 31   GLN A N   1 
ATOM   249  C  CA  . GLN A  1 31  ? 24.753  -1.699  69.137  1.00 15.64 ? 31   GLN A CA  1 
ATOM   250  C  C   . GLN A  1 31  ? 24.828  -2.315  67.736  1.00 14.64 ? 31   GLN A C   1 
ATOM   251  O  O   . GLN A  1 31  ? 25.715  -1.982  66.952  1.00 15.16 ? 31   GLN A O   1 
ATOM   252  C  CB  . GLN A  1 31  ? 25.551  -2.557  70.114  1.00 21.85 ? 31   GLN A CB  1 
ATOM   253  C  CG  . GLN A  1 31  ? 25.590  -2.006  71.533  1.00 33.27 ? 31   GLN A CG  1 
ATOM   254  C  CD  . GLN A  1 31  ? 26.289  -2.948  72.497  1.00 42.12 ? 31   GLN A CD  1 
ATOM   255  O  OE1 . GLN A  1 31  ? 27.066  -3.810  72.086  1.00 34.16 ? 31   GLN A OE1 1 
ATOM   256  N  NE2 . GLN A  1 31  ? 26.007  -2.796  73.786  1.00 49.13 ? 31   GLN A NE2 1 
ATOM   257  N  N   . ASN A  1 32  ? 23.889  -3.213  67.441  1.00 11.21 ? 32   ASN A N   1 
ATOM   258  C  CA  . ASN A  1 32  ? 23.803  -3.910  66.151  1.00 11.21 ? 32   ASN A CA  1 
ATOM   259  C  C   . ASN A  1 32  ? 22.354  -3.901  65.659  1.00 12.95 ? 32   ASN A C   1 
ATOM   260  O  O   . ASN A  1 32  ? 21.426  -4.061  66.455  1.00 13.20 ? 32   ASN A O   1 
ATOM   261  C  CB  . ASN A  1 32  ? 24.196  -5.385  66.298  1.00 13.73 ? 32   ASN A CB  1 
ATOM   262  C  CG  . ASN A  1 32  ? 25.575  -5.590  66.902  1.00 19.25 ? 32   ASN A CG  1 
ATOM   263  O  OD1 . ASN A  1 32  ? 26.554  -4.930  66.527  1.00 16.82 ? 32   ASN A OD1 1 
ATOM   264  N  ND2 . ASN A  1 32  ? 25.659  -6.545  67.826  1.00 20.25 ? 32   ASN A ND2 1 
ATOM   265  N  N   . PHE A  1 33  ? 22.136  -3.745  64.357  1.00 9.53  ? 33   PHE A N   1 
ATOM   266  C  CA  . PHE A  1 33  ? 20.797  -4.008  63.836  1.00 7.23  ? 33   PHE A CA  1 
ATOM   267  C  C   . PHE A  1 33  ? 20.831  -4.348  62.362  1.00 8.67  ? 33   PHE A C   1 
ATOM   268  O  O   . PHE A  1 33  ? 21.808  -4.074  61.667  1.00 8.39  ? 33   PHE A O   1 
ATOM   269  C  CB  . PHE A  1 33  ? 19.859  -2.806  64.043  1.00 6.74  ? 33   PHE A CB  1 
ATOM   270  C  CG  . PHE A  1 33  ? 20.151  -1.653  63.130  1.00 10.36 ? 33   PHE A CG  1 
ATOM   271  C  CD1 . PHE A  1 33  ? 19.583  -1.578  61.851  1.00 10.51 ? 33   PHE A CD1 1 
ATOM   272  C  CD2 . PHE A  1 33  ? 20.998  -0.643  63.546  1.00 9.94  ? 33   PHE A CD2 1 
ATOM   273  C  CE1 . PHE A  1 33  ? 19.875  -0.496  61.009  1.00 9.24  ? 33   PHE A CE1 1 
ATOM   274  C  CE2 . PHE A  1 33  ? 21.294  0.434   62.711  1.00 10.72 ? 33   PHE A CE2 1 
ATOM   275  C  CZ  . PHE A  1 33  ? 20.729  0.506   61.445  1.00 9.89  ? 33   PHE A CZ  1 
ATOM   276  N  N   . THR A  1 34  ? 19.746  -4.948  61.902  1.00 9.67  ? 34   THR A N   1 
ATOM   277  C  CA  . THR A  1 34  ? 19.501  -5.125  60.480  1.00 8.44  ? 34   THR A CA  1 
ATOM   278  C  C   . THR A  1 34  ? 18.053  -4.743  60.244  1.00 9.62  ? 34   THR A C   1 
ATOM   279  O  O   . THR A  1 34  ? 17.164  -5.101  61.027  1.00 9.76  ? 34   THR A O   1 
ATOM   280  C  CB  . THR A  1 34  ? 19.687  -6.583  60.029  1.00 7.88  ? 34   THR A CB  1 
ATOM   281  O  OG1 . THR A  1 34  ? 21.026  -7.023  60.311  1.00 9.65  ? 34   THR A OG1 1 
ATOM   282  C  CG2 . THR A  1 34  ? 19.422  -6.709  58.521  1.00 9.00  ? 34   THR A CG2 1 
ATOM   283  N  N   . LEU A  1 35  ? 17.814  -4.021  59.159  1.00 6.92  ? 35   LEU A N   1 
ATOM   284  C  CA  . LEU A  1 35  ? 16.462  -3.598  58.803  1.00 8.05  ? 35   LEU A CA  1 
ATOM   285  C  C   . LEU A  1 35  ? 16.220  -3.996  57.354  1.00 8.55  ? 35   LEU A C   1 
ATOM   286  O  O   . LEU A  1 35  ? 17.005  -3.627  56.485  1.00 10.01 ? 35   LEU A O   1 
ATOM   287  C  CB  . LEU A  1 35  ? 16.338  -2.080  58.961  1.00 9.23  ? 35   LEU A CB  1 
ATOM   288  C  CG  . LEU A  1 35  ? 15.111  -1.399  58.355  1.00 9.52  ? 35   LEU A CG  1 
ATOM   289  C  CD1 . LEU A  1 35  ? 13.844  -1.813  59.096  1.00 11.89 ? 35   LEU A CD1 1 
ATOM   290  C  CD2 . LEU A  1 35  ? 15.268  0.127   58.392  1.00 11.42 ? 35   LEU A CD2 1 
ATOM   291  N  N   . CYS A  1 36  ? 15.162  -4.768  57.096  1.00 8.17  ? 36   CYS A N   1 
ATOM   292  C  CA  . CYS A  1 36  ? 14.792  -5.132  55.719  1.00 8.54  ? 36   CYS A CA  1 
ATOM   293  C  C   . CYS A  1 36  ? 13.355  -4.699  55.444  1.00 8.92  ? 36   CYS A C   1 
ATOM   294  O  O   . CYS A  1 36  ? 12.518  -4.688  56.348  1.00 11.98 ? 36   CYS A O   1 
ATOM   295  C  CB  . CYS A  1 36  ? 14.863  -6.652  55.521  1.00 11.10 ? 36   CYS A CB  1 
ATOM   296  S  SG  . CYS A  1 36  ? 16.529  -7.357  55.601  1.00 14.05 ? 36   CYS A SG  1 
ATOM   297  N  N   . PHE A  1 37  ? 13.062  -4.334  54.198  1.00 10.85 ? 37   PHE A N   1 
ATOM   298  C  CA  . PHE A  1 37  ? 11.693  -4.033  53.797  1.00 8.55  ? 37   PHE A CA  1 
ATOM   299  C  C   . PHE A  1 37  ? 11.632  -3.962  52.280  1.00 7.41  ? 37   PHE A C   1 
ATOM   300  O  O   . PHE A  1 37  ? 12.658  -3.922  51.610  1.00 8.84  ? 37   PHE A O   1 
ATOM   301  C  CB  . PHE A  1 37  ? 11.172  -2.725  54.425  1.00 8.74  ? 37   PHE A CB  1 
ATOM   302  C  CG  . PHE A  1 37  ? 12.038  -1.526  54.138  1.00 9.52  ? 37   PHE A CG  1 
ATOM   303  C  CD1 . PHE A  1 37  ? 11.838  -0.761  52.992  1.00 11.38 ? 37   PHE A CD1 1 
ATOM   304  C  CD2 . PHE A  1 37  ? 13.070  -1.179  55.003  1.00 11.53 ? 37   PHE A CD2 1 
ATOM   305  C  CE1 . PHE A  1 37  ? 12.643  0.333   52.716  1.00 14.92 ? 37   PHE A CE1 1 
ATOM   306  C  CE2 . PHE A  1 37  ? 13.887  -0.083  54.727  1.00 13.24 ? 37   PHE A CE2 1 
ATOM   307  C  CZ  . PHE A  1 37  ? 13.665  0.675   53.580  1.00 10.85 ? 37   PHE A CZ  1 
ATOM   308  N  N   . ARG A  1 38  ? 10.420  -3.977  51.745  1.00 8.30  ? 38   ARG A N   1 
ATOM   309  C  CA  . ARG A  1 38  ? 10.218  -3.929  50.306  1.00 7.61  ? 38   ARG A CA  1 
ATOM   310  C  C   . ARG A  1 38  ? 9.487   -2.626  50.032  1.00 9.59  ? 38   ARG A C   1 
ATOM   311  O  O   . ARG A  1 38  ? 8.627   -2.234  50.814  1.00 11.29 ? 38   ARG A O   1 
ATOM   312  C  CB  . ARG A  1 38  ? 9.338   -5.116  49.906  1.00 11.04 ? 38   ARG A CB  1 
ATOM   313  C  CG  . ARG A  1 38  ? 9.787   -5.857  48.687  1.00 22.17 ? 38   ARG A CG  1 
ATOM   314  C  CD  . ARG A  1 38  ? 8.884   -7.069  48.462  1.00 18.53 ? 38   ARG A CD  1 
ATOM   315  N  NE  . ARG A  1 38  ? 9.211   -8.179  49.349  1.00 14.52 ? 38   ARG A NE  1 
ATOM   316  C  CZ  . ARG A  1 38  ? 10.173  -9.065  49.102  1.00 15.96 ? 38   ARG A CZ  1 
ATOM   317  N  NH1 . ARG A  1 38  ? 10.902  -8.969  47.994  1.00 14.90 ? 38   ARG A NH1 1 
ATOM   318  N  NH2 . ARG A  1 38  ? 10.410  -10.046 49.959  1.00 18.55 ? 38   ARG A NH2 1 
ATOM   319  N  N   . ALA A  1 39  ? 9.840   -1.936  48.951  1.00 7.80  ? 39   ALA A N   1 
ATOM   320  C  CA  . ALA A  1 39  ? 9.199   -0.665  48.633  1.00 9.18  ? 39   ALA A CA  1 
ATOM   321  C  C   . ALA A  1 39  ? 8.976   -0.518  47.133  1.00 8.65  ? 39   ALA A C   1 
ATOM   322  O  O   . ALA A  1 39  ? 9.718   -1.072  46.319  1.00 9.56  ? 39   ALA A O   1 
ATOM   323  C  CB  . ALA A  1 39  ? 10.034  0.521   49.165  1.00 9.74  ? 39   ALA A CB  1 
ATOM   324  N  N   . TYR A  1 40  ? 7.943   0.233   46.777  1.00 9.25  ? 40   TYR A N   1 
ATOM   325  C  CA  . TYR A  1 40  ? 7.625   0.463   45.378  1.00 7.17  ? 40   TYR A CA  1 
ATOM   326  C  C   . TYR A  1 40  ? 7.122   1.896   45.269  1.00 8.70  ? 40   TYR A C   1 
ATOM   327  O  O   . TYR A  1 40  ? 6.056   2.237   45.794  1.00 9.49  ? 40   TYR A O   1 
ATOM   328  C  CB  . TYR A  1 40  ? 6.567   -0.549  44.927  1.00 9.74  ? 40   TYR A CB  1 
ATOM   329  C  CG  . TYR A  1 40  ? 6.247   -0.568  43.445  1.00 7.47  ? 40   TYR A CG  1 
ATOM   330  C  CD1 . TYR A  1 40  ? 7.132   -0.047  42.509  1.00 8.80  ? 40   TYR A CD1 1 
ATOM   331  C  CD2 . TYR A  1 40  ? 5.064   -1.149  42.988  1.00 7.82  ? 40   TYR A CD2 1 
ATOM   332  C  CE1 . TYR A  1 40  ? 6.834   -0.082  41.147  1.00 8.26  ? 40   TYR A CE1 1 
ATOM   333  C  CE2 . TYR A  1 40  ? 4.756   -1.197  41.643  1.00 9.52  ? 40   TYR A CE2 1 
ATOM   334  C  CZ  . TYR A  1 40  ? 5.644   -0.657  40.724  1.00 8.27  ? 40   TYR A CZ  1 
ATOM   335  O  OH  . TYR A  1 40  ? 5.338   -0.710  39.382  1.00 11.06 ? 40   TYR A OH  1 
ATOM   336  N  N   . SER A  1 41  ? 7.913   2.740   44.610  1.00 9.21  ? 41   SER A N   1 
ATOM   337  C  CA  . SER A  1 41  ? 7.591   4.161   44.512  1.00 8.65  ? 41   SER A CA  1 
ATOM   338  C  C   . SER A  1 41  ? 8.008   4.647   43.142  1.00 8.26  ? 41   SER A C   1 
ATOM   339  O  O   . SER A  1 41  ? 9.006   4.165   42.608  1.00 12.73 ? 41   SER A O   1 
ATOM   340  C  CB  . SER A  1 41  ? 8.363   4.947   45.571  1.00 10.25 ? 41   SER A CB  1 
ATOM   341  O  OG  . SER A  1 41  ? 8.136   6.352   45.442  1.00 10.21 ? 41   SER A OG  1 
ATOM   342  N  N   . ASP A  1 42  ? 7.253   5.575   42.555  1.00 8.21  ? 42   ASP A N   1 
ATOM   343  C  CA  . ASP A  1 42  ? 7.718   6.202   41.317  1.00 8.82  ? 42   ASP A CA  1 
ATOM   344  C  C   . ASP A  1 42  ? 8.107   7.662   41.509  1.00 10.03 ? 42   ASP A C   1 
ATOM   345  O  O   . ASP A  1 42  ? 8.154   8.444   40.551  1.00 10.63 ? 42   ASP A O   1 
ATOM   346  C  CB  . ASP A  1 42  ? 6.775   5.997   40.115  1.00 9.00  ? 42   ASP A CB  1 
ATOM   347  C  CG  . ASP A  1 42  ? 5.358   6.486   40.367  1.00 10.41 ? 42   ASP A CG  1 
ATOM   348  O  OD1 . ASP A  1 42  ? 5.162   7.329   41.256  1.00 10.62 ? 42   ASP A OD1 1 
ATOM   349  O  OD2 . ASP A  1 42  ? 4.444   5.999   39.662  1.00 11.14 ? 42   ASP A OD2 1 
ATOM   350  N  N   . LEU A  1 43  ? 8.420   8.019   42.749  1.00 8.34  ? 43   LEU A N   1 
ATOM   351  C  CA  . LEU A  1 43  ? 9.037   9.321   43.011  1.00 9.58  ? 43   LEU A CA  1 
ATOM   352  C  C   . LEU A  1 43  ? 10.457  9.402   42.460  1.00 9.42  ? 43   LEU A C   1 
ATOM   353  O  O   . LEU A  1 43  ? 11.251  8.473   42.620  1.00 12.78 ? 43   LEU A O   1 
ATOM   354  C  CB  . LEU A  1 43  ? 9.103   9.602   44.511  1.00 9.08  ? 43   LEU A CB  1 
ATOM   355  C  CG  . LEU A  1 43  ? 7.785   9.872   45.240  1.00 10.76 ? 43   LEU A CG  1 
ATOM   356  C  CD1 . LEU A  1 43  ? 8.047   9.979   46.734  1.00 8.96  ? 43   LEU A CD1 1 
ATOM   357  C  CD2 . LEU A  1 43  ? 7.106   11.137  44.706  1.00 11.78 ? 43   LEU A CD2 1 
ATOM   358  N  N   . SER A  1 44  ? 10.781  10.545  41.853  1.00 10.58 ? 44   SER A N   1 
ATOM   359  C  CA  . SER A  1 44  ? 12.145  10.827  41.407  1.00 16.20 ? 44   SER A CA  1 
ATOM   360  C  C   . SER A  1 44  ? 12.895  11.704  42.395  1.00 12.73 ? 44   SER A C   1 
ATOM   361  O  O   . SER A  1 44  ? 14.117  11.650  42.474  1.00 15.42 ? 44   SER A O   1 
ATOM   362  C  CB  . SER A  1 44  ? 12.129  11.512  40.036  1.00 16.04 ? 44   SER A CB  1 
ATOM   363  O  OG  . SER A  1 44  ? 11.892  10.560  39.017  1.00 23.89 ? 44   SER A OG  1 
ATOM   364  N  N   . ARG A  1 45  ? 12.158  12.521  43.137  1.00 10.83 ? 45   ARG A N   1 
ATOM   365  C  CA  . ARG A  1 45  ? 12.760  13.381  44.139  1.00 9.79  ? 45   ARG A CA  1 
ATOM   366  C  C   . ARG A  1 45  ? 13.206  12.542  45.330  1.00 14.03 ? 45   ARG A C   1 
ATOM   367  O  O   . ARG A  1 45  ? 12.890  11.354  45.421  1.00 12.63 ? 45   ARG A O   1 
ATOM   368  C  CB  . ARG A  1 45  ? 11.765  14.450  44.611  1.00 10.42 ? 45   ARG A CB  1 
ATOM   369  C  CG  . ARG A  1 45  ? 10.515  13.899  45.313  1.00 12.01 ? 45   ARG A CG  1 
ATOM   370  C  CD  . ARG A  1 45  ? 9.891   14.942  46.259  1.00 13.38 ? 45   ARG A CD  1 
ATOM   371  N  NE  . ARG A  1 45  ? 8.533   14.566  46.631  1.00 12.77 ? 45   ARG A NE  1 
ATOM   372  C  CZ  . ARG A  1 45  ? 8.237   13.726  47.615  1.00 13.71 ? 45   ARG A CZ  1 
ATOM   373  N  NH1 . ARG A  1 45  ? 9.209   13.196  48.345  1.00 10.80 ? 45   ARG A NH1 1 
ATOM   374  N  NH2 . ARG A  1 45  ? 6.967   13.432  47.881  1.00 11.71 ? 45   ARG A NH2 1 
ATOM   375  N  N   . ALA A  1 46  ? 13.942  13.170  46.235  1.00 10.86 ? 46   ALA A N   1 
ATOM   376  C  CA  . ALA A  1 46  ? 14.387  12.519  47.459  1.00 12.05 ? 46   ALA A CA  1 
ATOM   377  C  C   . ALA A  1 46  ? 13.217  12.155  48.378  1.00 12.24 ? 46   ALA A C   1 
ATOM   378  O  O   . ALA A  1 46  ? 12.189  12.834  48.403  1.00 13.60 ? 46   ALA A O   1 
ATOM   379  C  CB  . ALA A  1 46  ? 15.368  13.415  48.194  1.00 10.74 ? 46   ALA A CB  1 
ATOM   380  N  N   . TYR A  1 47  ? 13.381  11.078  49.132  1.00 9.36  ? 47   TYR A N   1 
ATOM   381  C  CA  . TYR A  1 47  ? 12.389  10.700  50.131  1.00 9.65  ? 47   TYR A CA  1 
ATOM   382  C  C   . TYR A  1 47  ? 12.938  9.808   51.228  1.00 9.24  ? 47   TYR A C   1 
ATOM   383  O  O   . TYR A  1 47  ? 13.929  9.105   51.039  1.00 10.56 ? 47   TYR A O   1 
ATOM   384  C  CB  . TYR A  1 47  ? 11.174  10.032  49.479  1.00 11.88 ? 47   TYR A CB  1 
ATOM   385  C  CG  . TYR A  1 47  ? 11.480  8.831   48.601  1.00 9.60  ? 47   TYR A CG  1 
ATOM   386  C  CD1 . TYR A  1 47  ? 11.608  7.552   49.149  1.00 10.20 ? 47   TYR A CD1 1 
ATOM   387  C  CD2 . TYR A  1 47  ? 11.591  8.970   47.227  1.00 9.01  ? 47   TYR A CD2 1 
ATOM   388  C  CE1 . TYR A  1 47  ? 11.859  6.449   48.339  1.00 9.35  ? 47   TYR A CE1 1 
ATOM   389  C  CE2 . TYR A  1 47  ? 11.837  7.875   46.410  1.00 10.48 ? 47   TYR A CE2 1 
ATOM   390  C  CZ  . TYR A  1 47  ? 11.970  6.620   46.974  1.00 10.67 ? 47   TYR A CZ  1 
ATOM   391  O  OH  . TYR A  1 47  ? 12.202  5.537   46.154  1.00 11.71 ? 47   TYR A OH  1 
ATOM   392  N  N   . SER A  1 48  ? 12.269  9.840   52.381  1.00 9.13  ? 48   SER A N   1 
ATOM   393  C  CA  . SER A  1 48  ? 12.623  9.000   53.511  1.00 10.99 ? 48   SER A CA  1 
ATOM   394  C  C   . SER A  1 48  ? 11.914  7.650   53.434  1.00 10.85 ? 48   SER A C   1 
ATOM   395  O  O   . SER A  1 48  ? 10.719  7.585   53.155  1.00 10.06 ? 48   SER A O   1 
ATOM   396  C  CB  . SER A  1 48  ? 12.254  9.708   54.817  1.00 7.80  ? 48   SER A CB  1 
ATOM   397  O  OG  . SER A  1 48  ? 12.510  8.883   55.930  1.00 12.29 ? 48   SER A OG  1 
ATOM   398  N  N   . LEU A  1 49  ? 12.665  6.571   53.657  1.00 8.25  ? 49   LEU A N   1 
ATOM   399  C  CA  . LEU A  1 49  ? 12.082  5.234   53.701  1.00 8.06  ? 49   LEU A CA  1 
ATOM   400  C  C   . LEU A  1 49  ? 11.768  4.795   55.121  1.00 8.86  ? 49   LEU A C   1 
ATOM   401  O  O   . LEU A  1 49  ? 10.754  4.143   55.362  1.00 10.48 ? 49   LEU A O   1 
ATOM   402  C  CB  . LEU A  1 49  ? 13.018  4.216   53.032  1.00 9.09  ? 49   LEU A CB  1 
ATOM   403  C  CG  . LEU A  1 49  ? 13.036  4.336   51.510  1.00 11.60 ? 49   LEU A CG  1 
ATOM   404  C  CD1 . LEU A  1 49  ? 14.332  3.760   50.911  1.00 14.77 ? 49   LEU A CD1 1 
ATOM   405  C  CD2 . LEU A  1 49  ? 11.801  3.676   50.912  1.00 10.55 ? 49   LEU A CD2 1 
ATOM   406  N  N   . PHE A  1 50  ? 12.621  5.167   56.068  1.00 9.02  ? 50   PHE A N   1 
ATOM   407  C  CA  . PHE A  1 50  ? 12.484  4.700   57.454  1.00 10.04 ? 50   PHE A CA  1 
ATOM   408  C  C   . PHE A  1 50  ? 13.152  5.731   58.350  1.00 9.74  ? 50   PHE A C   1 
ATOM   409  O  O   . PHE A  1 50  ? 14.370  5.926   58.277  1.00 8.30  ? 50   PHE A O   1 
ATOM   410  C  CB  . PHE A  1 50  ? 13.172  3.338   57.623  1.00 7.55  ? 50   PHE A CB  1 
ATOM   411  C  CG  . PHE A  1 50  ? 13.055  2.738   59.011  1.00 9.29  ? 50   PHE A CG  1 
ATOM   412  C  CD1 . PHE A  1 50  ? 12.030  1.847   59.307  1.00 11.32 ? 50   PHE A CD1 1 
ATOM   413  C  CD2 . PHE A  1 50  ? 14.001  3.018   59.992  1.00 8.93  ? 50   PHE A CD2 1 
ATOM   414  C  CE1 . PHE A  1 50  ? 11.940  1.262   60.571  1.00 10.58 ? 50   PHE A CE1 1 
ATOM   415  C  CE2 . PHE A  1 50  ? 13.924  2.440   61.263  1.00 10.87 ? 50   PHE A CE2 1 
ATOM   416  C  CZ  . PHE A  1 50  ? 12.888  1.552   61.548  1.00 10.53 ? 50   PHE A CZ  1 
ATOM   417  N  N   . SER A  1 51  ? 12.350  6.382   59.188  1.00 11.46 ? 51   SER A N   1 
ATOM   418  C  CA  . SER A  1 51  ? 12.813  7.497   60.029  1.00 9.03  ? 51   SER A CA  1 
ATOM   419  C  C   . SER A  1 51  ? 12.688  7.164   61.518  1.00 11.13 ? 51   SER A C   1 
ATOM   420  O  O   . SER A  1 51  ? 11.585  6.941   62.029  1.00 12.23 ? 51   SER A O   1 
ATOM   421  C  CB  . SER A  1 51  ? 12.010  8.767   59.694  1.00 14.18 ? 51   SER A CB  1 
ATOM   422  O  OG  . SER A  1 51  ? 12.255  9.828   60.619  1.00 11.60 ? 51   SER A OG  1 
ATOM   423  N  N   . TYR A  1 52  ? 13.826  7.143   62.206  1.00 8.83  ? 52   TYR A N   1 
ATOM   424  C  CA  . TYR A  1 52  ? 13.893  6.764   63.619  1.00 14.03 ? 52   TYR A CA  1 
ATOM   425  C  C   . TYR A  1 52  ? 14.604  7.903   64.361  1.00 12.73 ? 52   TYR A C   1 
ATOM   426  O  O   . TYR A  1 52  ? 15.797  8.149   64.169  1.00 11.42 ? 52   TYR A O   1 
ATOM   427  C  CB  . TYR A  1 52  ? 14.619  5.410   63.702  1.00 10.25 ? 52   TYR A CB  1 
ATOM   428  C  CG  . TYR A  1 52  ? 15.078  4.832   65.040  1.00 10.08 ? 52   TYR A CG  1 
ATOM   429  C  CD1 . TYR A  1 52  ? 15.908  5.540   65.897  1.00 14.39 ? 52   TYR A CD1 1 
ATOM   430  C  CD2 . TYR A  1 52  ? 14.759  3.515   65.379  1.00 10.88 ? 52   TYR A CD2 1 
ATOM   431  C  CE1 . TYR A  1 52  ? 16.361  4.970   67.088  1.00 12.44 ? 52   TYR A CE1 1 
ATOM   432  C  CE2 . TYR A  1 52  ? 15.210  2.938   66.555  1.00 14.71 ? 52   TYR A CE2 1 
ATOM   433  C  CZ  . TYR A  1 52  ? 16.008  3.670   67.402  1.00 10.71 ? 52   TYR A CZ  1 
ATOM   434  O  OH  . TYR A  1 52  ? 16.452  3.098   68.575  1.00 15.38 ? 52   TYR A OH  1 
ATOM   435  N  N   . ASN A  1 53  ? 13.834  8.650   65.156  1.00 13.70 ? 53   ASN A N   1 
ATOM   436  C  CA  . ASN A  1 53  ? 14.363  9.785   65.911  1.00 13.64 ? 53   ASN A CA  1 
ATOM   437  C  C   . ASN A  1 53  ? 14.202  9.508   67.399  1.00 15.78 ? 53   ASN A C   1 
ATOM   438  O  O   . ASN A  1 53  ? 13.325  8.741   67.797  1.00 16.07 ? 53   ASN A O   1 
ATOM   439  C  CB  . ASN A  1 53  ? 13.622  11.083  65.557  1.00 17.47 ? 53   ASN A CB  1 
ATOM   440  C  CG  . ASN A  1 53  ? 14.197  11.782  64.336  1.00 18.76 ? 53   ASN A CG  1 
ATOM   441  O  OD1 . ASN A  1 53  ? 14.955  11.191  63.564  1.00 16.88 ? 53   ASN A OD1 1 
ATOM   442  N  ND2 . ASN A  1 53  ? 13.831  13.050  64.152  1.00 15.31 ? 53   ASN A ND2 1 
ATOM   443  N  N   . THR A  1 54  ? 15.068  10.108  68.212  1.00 14.55 ? 54   THR A N   1 
ATOM   444  C  CA  . THR A  1 54  ? 14.930  10.031  69.669  1.00 19.68 ? 54   THR A CA  1 
ATOM   445  C  C   . THR A  1 54  ? 14.881  11.447  70.240  1.00 18.86 ? 54   THR A C   1 
ATOM   446  O  O   . THR A  1 54  ? 15.107  12.409  69.524  1.00 19.51 ? 54   THR A O   1 
ATOM   447  C  CB  . THR A  1 54  ? 16.079  9.235   70.318  1.00 19.24 ? 54   THR A CB  1 
ATOM   448  O  OG1 . THR A  1 54  ? 17.327  9.878   70.037  1.00 21.49 ? 54   THR A OG1 1 
ATOM   449  C  CG2 . THR A  1 54  ? 16.106  7.805   69.778  1.00 16.01 ? 54   THR A CG2 1 
ATOM   450  N  N   . GLN A  1 55  ? 14.571  11.580  71.526  1.00 26.82 ? 55   GLN A N   1 
ATOM   451  C  CA  . GLN A  1 55  ? 14.409  12.910  72.111  1.00 28.09 ? 55   GLN A CA  1 
ATOM   452  C  C   . GLN A  1 55  ? 15.646  13.775  71.916  1.00 21.50 ? 55   GLN A C   1 
ATOM   453  O  O   . GLN A  1 55  ? 16.731  13.431  72.381  1.00 28.49 ? 55   GLN A O   1 
ATOM   454  C  CB  . GLN A  1 55  ? 14.070  12.814  73.600  1.00 35.21 ? 55   GLN A CB  1 
ATOM   455  C  CG  . GLN A  1 55  ? 13.549  14.115  74.182  1.00 41.91 ? 55   GLN A CG  1 
ATOM   456  C  CD  . GLN A  1 55  ? 12.162  14.464  73.670  1.00 44.11 ? 55   GLN A CD  1 
ATOM   457  O  OE1 . GLN A  1 55  ? 11.166  13.871  74.086  1.00 54.22 ? 55   GLN A OE1 1 
ATOM   458  N  NE2 . GLN A  1 55  ? 12.093  15.436  72.768  1.00 45.30 ? 55   GLN A NE2 1 
ATOM   459  N  N   . GLY A  1 56  ? 15.475  14.894  71.220  1.00 24.99 ? 56   GLY A N   1 
ATOM   460  C  CA  . GLY A  1 56  ? 16.553  15.839  71.001  1.00 24.06 ? 56   GLY A CA  1 
ATOM   461  C  C   . GLY A  1 56  ? 17.565  15.382  69.967  1.00 30.15 ? 56   GLY A C   1 
ATOM   462  O  O   . GLY A  1 56  ? 18.623  15.991  69.818  1.00 29.24 ? 56   GLY A O   1 
ATOM   463  N  N   . ARG A  1 57  ? 17.243  14.312  69.245  1.00 25.32 ? 57   ARG A N   1 
ATOM   464  C  CA  . ARG A  1 57  ? 18.188  13.754  68.277  1.00 19.90 ? 57   ARG A CA  1 
ATOM   465  C  C   . ARG A  1 57  ? 17.521  13.455  66.938  1.00 18.44 ? 57   ARG A C   1 
ATOM   466  O  O   . ARG A  1 57  ? 16.714  12.535  66.825  1.00 22.43 ? 57   ARG A O   1 
ATOM   467  C  CB  . ARG A  1 57  ? 18.874  12.509  68.851  1.00 18.18 ? 57   ARG A CB  1 
ATOM   468  C  CG  . ARG A  1 57  ? 19.824  12.838  70.011  1.00 25.27 ? 57   ARG A CG  1 
ATOM   469  C  CD  . ARG A  1 57  ? 20.681  11.652  70.445  1.00 28.95 ? 57   ARG A CD  1 
ATOM   470  N  NE  . ARG A  1 57  ? 21.765  11.374  69.502  1.00 23.39 ? 57   ARG A NE  1 
ATOM   471  C  CZ  . ARG A  1 57  ? 22.909  12.052  69.442  1.00 28.91 ? 57   ARG A CZ  1 
ATOM   472  N  NH1 . ARG A  1 57  ? 23.134  13.071  70.265  1.00 30.85 ? 57   ARG A NH1 1 
ATOM   473  N  NH2 . ARG A  1 57  ? 23.831  11.714  68.550  1.00 28.43 ? 57   ARG A NH2 1 
ATOM   474  N  N   . ASP A  1 58  ? 17.855  14.262  65.938  1.00 19.01 ? 58   ASP A N   1 
ATOM   475  C  CA  . ASP A  1 58  ? 17.323  14.086  64.599  1.00 17.05 ? 58   ASP A CA  1 
ATOM   476  C  C   . ASP A  1 58  ? 18.182  13.073  63.858  1.00 13.31 ? 58   ASP A C   1 
ATOM   477  O  O   . ASP A  1 58  ? 19.383  12.979  64.098  1.00 16.25 ? 58   ASP A O   1 
ATOM   478  C  CB  . ASP A  1 58  ? 17.345  15.419  63.843  1.00 20.53 ? 58   ASP A CB  1 
ATOM   479  C  CG  . ASP A  1 58  ? 16.577  15.362  62.541  1.00 18.54 ? 58   ASP A CG  1 
ATOM   480  O  OD1 . ASP A  1 58  ? 15.630  14.556  62.459  1.00 18.74 ? 58   ASP A OD1 1 
ATOM   481  O  OD2 . ASP A  1 58  ? 16.904  16.122  61.601  1.00 17.19 ? 58   ASP A OD2 1 
ATOM   482  N  N   . ASN A  1 59  ? 17.565  12.333  62.940  1.00 15.56 ? 59   ASN A N   1 
ATOM   483  C  CA  . ASN A  1 59  ? 18.308  11.405  62.089  1.00 15.24 ? 59   ASN A CA  1 
ATOM   484  C  C   . ASN A  1 59  ? 19.153  10.428  62.895  1.00 12.75 ? 59   ASN A C   1 
ATOM   485  O  O   . ASN A  1 59  ? 20.306  10.170  62.563  1.00 12.89 ? 59   ASN A O   1 
ATOM   486  C  CB  . ASN A  1 59  ? 19.160  12.180  61.067  1.00 12.17 ? 59   ASN A CB  1 
ATOM   487  C  CG  . ASN A  1 59  ? 18.314  13.083  60.193  1.00 13.66 ? 59   ASN A CG  1 
ATOM   488  O  OD1 . ASN A  1 59  ? 17.087  13.032  60.269  1.00 15.04 ? 59   ASN A OD1 1 
ATOM   489  N  ND2 . ASN A  1 59  ? 18.949  13.913  59.370  1.00 11.61 ? 59   ASN A ND2 1 
ATOM   490  N  N   . GLU A  1 60  ? 18.565  9.880   63.957  1.00 10.80 ? 60   GLU A N   1 
ATOM   491  C  CA  . GLU A  1 60  ? 19.281  8.951   64.824  1.00 9.63  ? 60   GLU A CA  1 
ATOM   492  C  C   . GLU A  1 60  ? 19.513  7.625   64.094  1.00 11.07 ? 60   GLU A C   1 
ATOM   493  O  O   . GLU A  1 60  ? 20.600  7.051   64.154  1.00 11.65 ? 60   GLU A O   1 
ATOM   494  C  CB  . GLU A  1 60  ? 18.526  8.757   66.144  1.00 12.44 ? 60   GLU A CB  1 
ATOM   495  C  CG  . GLU A  1 60  ? 19.231  7.865   67.148  1.00 14.79 ? 60   GLU A CG  1 
ATOM   496  C  CD  . GLU A  1 60  ? 20.533  8.465   67.675  1.00 13.21 ? 60   GLU A CD  1 
ATOM   497  O  OE1 . GLU A  1 60  ? 20.803  9.659   67.432  1.00 15.51 ? 60   GLU A OE1 1 
ATOM   498  O  OE2 . GLU A  1 60  ? 21.289  7.732   68.335  1.00 15.61 ? 60   GLU A OE2 1 
ATOM   499  N  N   . LEU A  1 61  ? 18.488  7.157   63.386  1.00 11.97 ? 61   LEU A N   1 
ATOM   500  C  CA  . LEU A  1 61  ? 18.649  6.043   62.449  1.00 11.57 ? 61   LEU A CA  1 
ATOM   501  C  C   . LEU A  1 61  ? 17.725  6.348   61.280  1.00 10.98 ? 61   LEU A C   1 
ATOM   502  O  O   . LEU A  1 61  ? 16.510  6.347   61.437  1.00 13.94 ? 61   LEU A O   1 
ATOM   503  C  CB  . LEU A  1 61  ? 18.276  4.715   63.116  1.00 9.70  ? 61   LEU A CB  1 
ATOM   504  C  CG  . LEU A  1 61  ? 18.573  3.382   62.422  1.00 11.53 ? 61   LEU A CG  1 
ATOM   505  C  CD1 . LEU A  1 61  ? 18.255  2.223   63.375  1.00 11.26 ? 61   LEU A CD1 1 
ATOM   506  C  CD2 . LEU A  1 61  ? 17.782  3.226   61.124  1.00 15.57 ? 61   LEU A CD2 1 
ATOM   507  N  N   . LEU A  1 62  ? 18.287  6.647   60.112  1.00 9.77  ? 62   LEU A N   1 
ATOM   508  C  CA  . LEU A  1 62  ? 17.460  7.080   58.989  1.00 7.90  ? 62   LEU A CA  1 
ATOM   509  C  C   . LEU A  1 62  ? 17.915  6.385   57.716  1.00 8.29  ? 62   LEU A C   1 
ATOM   510  O  O   . LEU A  1 62  ? 19.106  6.394   57.401  1.00 10.86 ? 62   LEU A O   1 
ATOM   511  C  CB  . LEU A  1 62  ? 17.553  8.609   58.808  1.00 8.37  ? 62   LEU A CB  1 
ATOM   512  C  CG  . LEU A  1 62  ? 16.951  9.254   57.551  1.00 9.23  ? 62   LEU A CG  1 
ATOM   513  C  CD1 . LEU A  1 62  ? 15.427  9.048   57.462  1.00 11.18 ? 62   LEU A CD1 1 
ATOM   514  C  CD2 . LEU A  1 62  ? 17.287  10.730  57.533  1.00 13.17 ? 62   LEU A CD2 1 
ATOM   515  N  N   . VAL A  1 63  ? 16.971  5.777   57.004  1.00 6.30  ? 63   VAL A N   1 
ATOM   516  C  CA  . VAL A  1 63  ? 17.250  5.252   55.677  1.00 6.94  ? 63   VAL A CA  1 
ATOM   517  C  C   . VAL A  1 63  ? 16.576  6.178   54.680  1.00 8.96  ? 63   VAL A C   1 
ATOM   518  O  O   . VAL A  1 63  ? 15.357  6.350   54.709  1.00 8.82  ? 63   VAL A O   1 
ATOM   519  C  CB  . VAL A  1 63  ? 16.717  3.826   55.515  1.00 7.23  ? 63   VAL A CB  1 
ATOM   520  C  CG1 . VAL A  1 63  ? 17.083  3.288   54.126  1.00 8.25  ? 63   VAL A CG1 1 
ATOM   521  C  CG2 . VAL A  1 63  ? 17.293  2.934   56.595  1.00 10.19 ? 63   VAL A CG2 1 
ATOM   522  N  N   . TYR A  1 64  ? 17.375  6.781   53.803  1.00 8.68  ? 64   TYR A N   1 
ATOM   523  C  CA  . TYR A  1 64  ? 16.923  7.903   52.984  1.00 8.63  ? 64   TYR A CA  1 
ATOM   524  C  C   . TYR A  1 64  ? 17.376  7.692   51.549  1.00 10.89 ? 64   TYR A C   1 
ATOM   525  O  O   . TYR A  1 64  ? 18.468  7.199   51.312  1.00 10.03 ? 64   TYR A O   1 
ATOM   526  C  CB  . TYR A  1 64  ? 17.539  9.194   53.541  1.00 9.74  ? 64   TYR A CB  1 
ATOM   527  C  CG  . TYR A  1 64  ? 16.962  10.480  53.000  1.00 10.28 ? 64   TYR A CG  1 
ATOM   528  C  CD1 . TYR A  1 64  ? 15.727  10.947  53.444  1.00 11.04 ? 64   TYR A CD1 1 
ATOM   529  C  CD2 . TYR A  1 64  ? 17.662  11.245  52.078  1.00 14.36 ? 64   TYR A CD2 1 
ATOM   530  C  CE1 . TYR A  1 64  ? 15.203  12.125  52.973  1.00 12.68 ? 64   TYR A CE1 1 
ATOM   531  C  CE2 . TYR A  1 64  ? 17.142  12.439  51.601  1.00 15.28 ? 64   TYR A CE2 1 
ATOM   532  C  CZ  . TYR A  1 64  ? 15.911  12.867  52.059  1.00 14.01 ? 64   TYR A CZ  1 
ATOM   533  O  OH  . TYR A  1 64  ? 15.372  14.044  51.596  1.00 17.46 ? 64   TYR A OH  1 
ATOM   534  N  N   . LYS A  1 65  ? 16.542  8.066   50.588  1.00 9.25  ? 65   LYS A N   1 
ATOM   535  C  CA  . LYS A  1 65  ? 16.869  7.854   49.187  1.00 8.36  ? 65   LYS A CA  1 
ATOM   536  C  C   . LYS A  1 65  ? 16.979  9.208   48.507  1.00 11.05 ? 65   LYS A C   1 
ATOM   537  O  O   . LYS A  1 65  ? 15.960  9.828   48.211  1.00 11.19 ? 65   LYS A O   1 
ATOM   538  C  CB  . LYS A  1 65  ? 15.764  7.018   48.522  1.00 12.32 ? 65   LYS A CB  1 
ATOM   539  C  CG  . LYS A  1 65  ? 16.046  6.637   47.084  1.00 16.14 ? 65   LYS A CG  1 
ATOM   540  C  CD  . LYS A  1 65  ? 16.691  5.282   46.990  1.00 20.40 ? 65   LYS A CD  1 
ATOM   541  C  CE  . LYS A  1 65  ? 16.972  4.906   45.532  1.00 18.65 ? 65   LYS A CE  1 
ATOM   542  N  NZ  . LYS A  1 65  ? 15.732  4.835   44.731  1.00 17.57 ? 65   LYS A NZ  1 
ATOM   543  N  N   . GLU A  1 66  ? 18.206  9.676   48.275  1.00 12.78 ? 66   GLU A N   1 
ATOM   544  C  CA  . GLU A  1 66  ? 18.395  11.011  47.697  1.00 18.57 ? 66   GLU A CA  1 
ATOM   545  C  C   . GLU A  1 66  ? 17.998  11.086  46.225  1.00 15.48 ? 66   GLU A C   1 
ATOM   546  O  O   . GLU A  1 66  ? 17.444  12.087  45.763  1.00 15.47 ? 66   GLU A O   1 
ATOM   547  C  CB  . GLU A  1 66  ? 19.839  11.483  47.886  1.00 24.63 ? 66   GLU A CB  1 
ATOM   548  C  CG  . GLU A  1 66  ? 19.979  12.585  48.909  1.00 25.86 ? 66   GLU A CG  1 
ATOM   549  C  CD  . GLU A  1 66  ? 19.337  13.880  48.429  1.00 34.81 ? 66   GLU A CD  1 
ATOM   550  O  OE1 . GLU A  1 66  ? 19.166  14.040  47.201  1.00 46.41 ? 66   GLU A OE1 1 
ATOM   551  O  OE2 . GLU A  1 66  ? 19.007  14.738  49.273  1.00 46.96 ? 66   GLU A OE2 1 
ATOM   552  N  N   . ARG A  1 67  ? 18.267  10.013  45.494  1.00 9.92  ? 67   ARG A N   1 
ATOM   553  C  CA  . ARG A  1 67  ? 17.994  9.974   44.066  1.00 11.71 ? 67   ARG A CA  1 
ATOM   554  C  C   . ARG A  1 67  ? 18.115  8.539   43.618  1.00 11.72 ? 67   ARG A C   1 
ATOM   555  O  O   . ARG A  1 67  ? 18.609  7.693   44.365  1.00 11.22 ? 67   ARG A O   1 
ATOM   556  C  CB  . ARG A  1 67  ? 18.997  10.841  43.296  1.00 13.62 ? 67   ARG A CB  1 
ATOM   557  C  CG  . ARG A  1 67  ? 20.455  10.405  43.457  1.00 12.80 ? 67   ARG A CG  1 
ATOM   558  C  CD  . ARG A  1 67  ? 21.417  11.359  42.742  1.00 19.45 ? 67   ARG A CD  1 
ATOM   559  N  NE  . ARG A  1 67  ? 21.262  12.726  43.226  1.00 18.59 ? 67   ARG A NE  1 
ATOM   560  C  CZ  . ARG A  1 67  ? 21.815  13.197  44.338  1.00 22.23 ? 67   ARG A CZ  1 
ATOM   561  N  NH1 . ARG A  1 67  ? 22.576  12.417  45.091  1.00 29.19 ? 67   ARG A NH1 1 
ATOM   562  N  NH2 . ARG A  1 67  ? 21.604  14.456  44.701  1.00 30.68 ? 67   ARG A NH2 1 
ATOM   563  N  N   . VAL A  1 68  ? 17.669  8.259   42.400  1.00 11.15 ? 68   VAL A N   1 
ATOM   564  C  CA  . VAL A  1 68  ? 17.742  6.900   41.882  1.00 11.18 ? 68   VAL A CA  1 
ATOM   565  C  C   . VAL A  1 68  ? 19.180  6.377   41.963  1.00 11.58 ? 68   VAL A C   1 
ATOM   566  O  O   . VAL A  1 68  ? 20.138  7.110   41.667  1.00 12.03 ? 68   VAL A O   1 
ATOM   567  C  CB  . VAL A  1 68  ? 17.214  6.827   40.442  1.00 14.38 ? 68   VAL A CB  1 
ATOM   568  C  CG1 . VAL A  1 68  ? 17.958  7.817   39.562  1.00 16.96 ? 68   VAL A CG1 1 
ATOM   569  C  CG2 . VAL A  1 68  ? 17.317  5.401   39.893  1.00 15.78 ? 68   VAL A CG2 1 
ATOM   570  N  N   . GLY A  1 69  ? 19.319  5.127   42.401  1.00 10.67 ? 69   GLY A N   1 
ATOM   571  C  CA  . GLY A  1 69  ? 20.605  4.447   42.408  1.00 12.03 ? 69   GLY A CA  1 
ATOM   572  C  C   . GLY A  1 69  ? 21.483  4.730   43.619  1.00 13.30 ? 69   GLY A C   1 
ATOM   573  O  O   . GLY A  1 69  ? 22.633  4.304   43.647  1.00 13.44 ? 69   GLY A O   1 
ATOM   574  N  N   . GLU A  1 70  ? 20.953  5.456   44.605  1.00 8.95  ? 70   GLU A N   1 
ATOM   575  C  CA  . GLU A  1 70  ? 21.747  5.859   45.769  1.00 11.23 ? 70   GLU A CA  1 
ATOM   576  C  C   . GLU A  1 70  ? 20.966  5.719   47.068  1.00 13.33 ? 70   GLU A C   1 
ATOM   577  O  O   . GLU A  1 70  ? 19.913  6.330   47.240  1.00 15.22 ? 70   GLU A O   1 
ATOM   578  C  CB  . GLU A  1 70  ? 22.222  7.308   45.626  1.00 10.62 ? 70   GLU A CB  1 
ATOM   579  C  CG  . GLU A  1 70  ? 23.277  7.474   44.529  1.00 19.67 ? 70   GLU A CG  1 
ATOM   580  C  CD  . GLU A  1 70  ? 23.702  8.916   44.326  1.00 23.82 ? 70   GLU A CD  1 
ATOM   581  O  OE1 . GLU A  1 70  ? 23.334  9.759   45.158  1.00 18.85 ? 70   GLU A OE1 1 
ATOM   582  O  OE2 . GLU A  1 70  ? 24.408  9.201   43.331  1.00 27.69 ? 70   GLU A OE2 1 
ATOM   583  N  N   . TYR A  1 71  ? 21.508  4.937   47.991  1.00 7.16  ? 71   TYR A N   1 
ATOM   584  C  CA  . TYR A  1 71  ? 20.855  4.709   49.271  1.00 8.11  ? 71   TYR A CA  1 
ATOM   585  C  C   . TYR A  1 71  ? 21.721  5.236   50.395  1.00 8.88  ? 71   TYR A C   1 
ATOM   586  O  O   . TYR A  1 71  ? 22.920  4.992   50.417  1.00 8.79  ? 71   TYR A O   1 
ATOM   587  C  CB  . TYR A  1 71  ? 20.604  3.215   49.473  1.00 11.95 ? 71   TYR A CB  1 
ATOM   588  C  CG  . TYR A  1 71  ? 19.553  2.703   48.531  1.00 10.06 ? 71   TYR A CG  1 
ATOM   589  C  CD1 . TYR A  1 71  ? 19.884  2.309   47.243  1.00 8.34  ? 71   TYR A CD1 1 
ATOM   590  C  CD2 . TYR A  1 71  ? 18.217  2.667   48.913  1.00 12.89 ? 71   TYR A CD2 1 
ATOM   591  C  CE1 . TYR A  1 71  ? 18.903  1.870   46.360  1.00 10.70 ? 71   TYR A CE1 1 
ATOM   592  C  CE2 . TYR A  1 71  ? 17.238  2.230   48.039  1.00 13.70 ? 71   TYR A CE2 1 
ATOM   593  C  CZ  . TYR A  1 71  ? 17.591  1.830   46.768  1.00 11.60 ? 71   TYR A CZ  1 
ATOM   594  O  OH  . TYR A  1 71  ? 16.618  1.398   45.907  1.00 13.84 ? 71   TYR A OH  1 
ATOM   595  N  N   . SER A  1 72  ? 21.107  5.963   51.329  1.00 8.54  ? 72   SER A N   1 
ATOM   596  C  CA  . SER A  1 72  ? 21.846  6.523   52.460  1.00 8.03  ? 72   SER A CA  1 
ATOM   597  C  C   . SER A  1 72  ? 21.374  5.956   53.779  1.00 8.19  ? 72   SER A C   1 
ATOM   598  O  O   . SER A  1 72  ? 20.177  5.746   53.985  1.00 9.06  ? 72   SER A O   1 
ATOM   599  C  CB  . SER A  1 72  ? 21.684  8.045   52.517  1.00 10.84 ? 72   SER A CB  1 
ATOM   600  O  OG  . SER A  1 72  ? 22.214  8.650   51.358  1.00 12.21 ? 72   SER A OG  1 
ATOM   601  N  N   . LEU A  1 73  ? 22.323  5.739   54.680  1.00 6.86  ? 73   LEU A N   1 
ATOM   602  C  CA  . LEU A  1 73  ? 22.010  5.409   56.058  1.00 6.73  ? 73   LEU A CA  1 
ATOM   603  C  C   . LEU A  1 73  ? 22.588  6.493   56.944  1.00 7.87  ? 73   LEU A C   1 
ATOM   604  O  O   . LEU A  1 73  ? 23.754  6.863   56.786  1.00 9.45  ? 73   LEU A O   1 
ATOM   605  C  CB  . LEU A  1 73  ? 22.633  4.067   56.435  1.00 6.98  ? 73   LEU A CB  1 
ATOM   606  C  CG  . LEU A  1 73  ? 22.543  3.719   57.925  1.00 5.73  ? 73   LEU A CG  1 
ATOM   607  C  CD1 . LEU A  1 73  ? 21.088  3.421   58.311  1.00 9.25  ? 73   LEU A CD1 1 
ATOM   608  C  CD2 . LEU A  1 73  ? 23.428  2.517   58.294  1.00 7.84  ? 73   LEU A CD2 1 
ATOM   609  N  N   . TYR A  1 74  ? 21.776  7.003   57.870  1.00 6.92  ? 74   TYR A N   1 
ATOM   610  C  CA  . TYR A  1 74  ? 22.255  7.928   58.889  1.00 9.06  ? 74   TYR A CA  1 
ATOM   611  C  C   . TYR A  1 74  ? 22.284  7.185   60.212  1.00 8.79  ? 74   TYR A C   1 
ATOM   612  O  O   . TYR A  1 74  ? 21.358  6.438   60.527  1.00 8.51  ? 74   TYR A O   1 
ATOM   613  C  CB  . TYR A  1 74  ? 21.313  9.131   59.024  1.00 7.71  ? 74   TYR A CB  1 
ATOM   614  C  CG  . TYR A  1 74  ? 21.231  10.039  57.813  1.00 10.15 ? 74   TYR A CG  1 
ATOM   615  C  CD1 . TYR A  1 74  ? 20.680  9.594   56.620  1.00 8.26  ? 74   TYR A CD1 1 
ATOM   616  C  CD2 . TYR A  1 74  ? 21.677  11.363  57.880  1.00 11.10 ? 74   TYR A CD2 1 
ATOM   617  C  CE1 . TYR A  1 74  ? 20.593  10.429  55.508  1.00 9.75  ? 74   TYR A CE1 1 
ATOM   618  C  CE2 . TYR A  1 74  ? 21.590  12.207  56.778  1.00 13.14 ? 74   TYR A CE2 1 
ATOM   619  C  CZ  . TYR A  1 74  ? 21.048  11.732  55.598  1.00 16.69 ? 74   TYR A CZ  1 
ATOM   620  O  OH  . TYR A  1 74  ? 20.963  12.569  54.504  1.00 17.45 ? 74   TYR A OH  1 
ATOM   621  N  N   . ILE A  1 75  ? 23.364  7.357   60.961  1.00 7.80  ? 75   ILE A N   1 
ATOM   622  C  CA  . ILE A  1 75  ? 23.433  6.869   62.333  1.00 10.86 ? 75   ILE A CA  1 
ATOM   623  C  C   . ILE A  1 75  ? 23.853  8.053   63.183  1.00 9.37  ? 75   ILE A C   1 
ATOM   624  O  O   . ILE A  1 75  ? 24.936  8.593   62.996  1.00 9.82  ? 75   ILE A O   1 
ATOM   625  C  CB  . ILE A  1 75  ? 24.482  5.746   62.492  1.00 10.81 ? 75   ILE A CB  1 
ATOM   626  C  CG1 . ILE A  1 75  ? 24.116  4.523   61.636  1.00 10.70 ? 75   ILE A CG1 1 
ATOM   627  C  CG2 . ILE A  1 75  ? 24.642  5.381   63.960  1.00 11.83 ? 75   ILE A CG2 1 
ATOM   628  C  CD1 . ILE A  1 75  ? 22.893  3.752   62.120  1.00 8.48  ? 75   ILE A CD1 1 
ATOM   629  N  N   . GLY A  1 76  ? 23.003  8.475   64.111  1.00 11.79 ? 76   GLY A N   1 
ATOM   630  C  CA  . GLY A  1 76  ? 23.350  9.609   64.949  1.00 11.53 ? 76   GLY A CA  1 
ATOM   631  C  C   . GLY A  1 76  ? 23.777  10.840  64.169  1.00 13.38 ? 76   GLY A C   1 
ATOM   632  O  O   . GLY A  1 76  ? 24.763  11.505  64.520  1.00 13.00 ? 76   GLY A O   1 
ATOM   633  N  N   . ARG A  1 77  ? 23.033  11.136  63.107  1.00 10.23 ? 77   ARG A N   1 
ATOM   634  C  CA  . ARG A  1 77  ? 23.217  12.345  62.300  1.00 12.70 ? 77   ARG A CA  1 
ATOM   635  C  C   . ARG A  1 77  ? 24.322  12.240  61.256  1.00 11.85 ? 77   ARG A C   1 
ATOM   636  O  O   . ARG A  1 77  ? 24.336  13.028  60.312  1.00 17.20 ? 77   ARG A O   1 
ATOM   637  C  CB  . ARG A  1 77  ? 23.397  13.599  63.178  1.00 18.36 ? 77   ARG A CB  1 
ATOM   638  C  CG  . ARG A  1 77  ? 22.075  14.223  63.613  1.00 31.62 ? 77   ARG A CG  1 
ATOM   639  C  CD  . ARG A  1 77  ? 22.254  15.365  64.614  1.00 36.03 ? 77   ARG A CD  1 
ATOM   640  N  NE  . ARG A  1 77  ? 21.332  16.468  64.336  1.00 35.47 ? 77   ARG A NE  1 
ATOM   641  C  CZ  . ARG A  1 77  ? 21.553  17.378  63.394  1.00 29.63 ? 77   ARG A CZ  1 
ATOM   642  N  NH1 . ARG A  1 77  ? 20.687  18.357  63.172  1.00 31.62 ? 77   ARG A NH1 1 
ATOM   643  N  NH2 . ARG A  1 77  ? 22.655  17.298  62.667  1.00 21.18 ? 77   ARG A NH2 1 
ATOM   644  N  N   . HIS A  1 78  ? 25.214  11.260  61.421  1.00 9.97  ? 78   HIS A N   1 
ATOM   645  C  CA  . HIS A  1 78  ? 26.274  10.978  60.447  1.00 11.63 ? 78   HIS A CA  1 
ATOM   646  C  C   . HIS A  1 78  ? 25.674  10.139  59.314  1.00 11.96 ? 78   HIS A C   1 
ATOM   647  O  O   . HIS A  1 78  ? 24.739  9.395   59.530  1.00 11.82 ? 78   HIS A O   1 
ATOM   648  C  CB  . HIS A  1 78  ? 27.424  10.183  61.090  1.00 13.70 ? 78   HIS A CB  1 
ATOM   649  C  CG  . HIS A  1 78  ? 28.144  10.906  62.193  1.00 13.06 ? 78   HIS A CG  1 
ATOM   650  N  ND1 . HIS A  1 78  ? 29.392  10.527  62.636  1.00 19.20 ? 78   HIS A ND1 1 
ATOM   651  C  CD2 . HIS A  1 78  ? 27.790  11.981  62.940  1.00 18.88 ? 78   HIS A CD2 1 
ATOM   652  C  CE1 . HIS A  1 78  ? 29.775  11.329  63.617  1.00 19.98 ? 78   HIS A CE1 1 
ATOM   653  N  NE2 . HIS A  1 78  ? 28.828  12.230  63.808  1.00 16.53 ? 78   HIS A NE2 1 
ATOM   654  N  N   . LYS A  1 79  ? 26.223  10.242  58.110  1.00 11.86 ? 79   LYS A N   1 
ATOM   655  C  CA  . LYS A  1 79  ? 25.631  9.525   56.983  1.00 9.81  ? 79   LYS A CA  1 
ATOM   656  C  C   . LYS A  1 79  ? 26.673  8.816   56.117  1.00 11.67 ? 79   LYS A C   1 
ATOM   657  O  O   . LYS A  1 79  ? 27.826  9.261   55.995  1.00 10.00 ? 79   LYS A O   1 
ATOM   658  C  CB  . LYS A  1 79  ? 24.813  10.495  56.122  1.00 21.51 ? 79   LYS A CB  1 
ATOM   659  C  CG  . LYS A  1 79  ? 24.625  10.067  54.680  1.00 27.50 ? 79   LYS A CG  1 
ATOM   660  C  CD  . LYS A  1 79  ? 23.955  11.159  53.838  1.00 24.64 ? 79   LYS A CD  1 
ATOM   661  C  CE  . LYS A  1 79  ? 24.873  12.347  53.624  1.00 32.58 ? 79   LYS A CE  1 
ATOM   662  N  NZ  . LYS A  1 79  ? 24.357  13.257  52.563  1.00 41.33 ? 79   LYS A NZ  1 
ATOM   663  N  N   . VAL A  1 80  ? 26.268  7.685   55.546  1.00 8.91  ? 80   VAL A N   1 
ATOM   664  C  CA  . VAL A  1 80  ? 27.020  7.080   54.457  1.00 8.52  ? 80   VAL A CA  1 
ATOM   665  C  C   . VAL A  1 80  ? 26.060  6.801   53.312  1.00 8.07  ? 80   VAL A C   1 
ATOM   666  O  O   . VAL A  1 80  ? 24.860  6.684   53.520  1.00 10.11 ? 80   VAL A O   1 
ATOM   667  C  CB  . VAL A  1 80  ? 27.700  5.766   54.858  1.00 9.17  ? 80   VAL A CB  1 
ATOM   668  C  CG1 . VAL A  1 80  ? 28.814  6.018   55.889  1.00 8.53  ? 80   VAL A CG1 1 
ATOM   669  C  CG2 . VAL A  1 80  ? 26.666  4.759   55.369  1.00 9.93  ? 80   VAL A CG2 1 
ATOM   670  N  N   . THR A  1 81  ? 26.597  6.719   52.100  1.00 7.26  ? 81   THR A N   1 
ATOM   671  C  CA  . THR A  1 81  ? 25.764  6.494   50.920  1.00 8.78  ? 81   THR A CA  1 
ATOM   672  C  C   . THR A  1 81  ? 26.467  5.496   50.016  1.00 9.75  ? 81   THR A C   1 
ATOM   673  O  O   . THR A  1 81  ? 27.674  5.599   49.794  1.00 9.73  ? 81   THR A O   1 
ATOM   674  C  CB  . THR A  1 81  ? 25.546  7.794   50.119  1.00 11.65 ? 81   THR A CB  1 
ATOM   675  O  OG1 . THR A  1 81  ? 24.895  8.769   50.946  1.00 12.66 ? 81   THR A OG1 1 
ATOM   676  C  CG2 . THR A  1 81  ? 24.692  7.526   48.882  1.00 13.17 ? 81   THR A CG2 1 
ATOM   677  N  N   . SER A  1 82  ? 25.717  4.525   49.503  1.00 6.23  ? 82   SER A N   1 
ATOM   678  C  CA  . SER A  1 82  ? 26.288  3.581   48.553  1.00 6.99  ? 82   SER A CA  1 
ATOM   679  C  C   . SER A  1 82  ? 25.408  3.490   47.316  1.00 8.13  ? 82   SER A C   1 
ATOM   680  O  O   . SER A  1 82  ? 24.202  3.742   47.368  1.00 8.67  ? 82   SER A O   1 
ATOM   681  C  CB  . SER A  1 82  ? 26.504  2.206   49.187  1.00 13.16 ? 82   SER A CB  1 
ATOM   682  O  OG  . SER A  1 82  ? 27.720  2.198   49.925  1.00 13.65 ? 82   SER A OG  1 
ATOM   683  N  N   . LYS A  1 83  ? 26.035  3.158   46.197  1.00 6.57  ? 83   LYS A N   1 
ATOM   684  C  CA  . LYS A  1 83  ? 25.382  3.252   44.892  1.00 8.77  ? 83   LYS A CA  1 
ATOM   685  C  C   . LYS A  1 83  ? 25.056  1.887   44.319  1.00 8.57  ? 83   LYS A C   1 
ATOM   686  O  O   . LYS A  1 83  ? 25.693  0.888   44.660  1.00 7.34  ? 83   LYS A O   1 
ATOM   687  C  CB  . LYS A  1 83  ? 26.276  4.015   43.917  1.00 7.85  ? 83   LYS A CB  1 
ATOM   688  C  CG  . LYS A  1 83  ? 26.491  5.451   44.340  1.00 14.35 ? 83   LYS A CG  1 
ATOM   689  C  CD  . LYS A  1 83  ? 27.294  6.239   43.310  1.00 19.69 ? 83   LYS A CD  1 
ATOM   690  C  CE  . LYS A  1 83  ? 27.313  7.717   43.689  1.00 21.80 ? 83   LYS A CE  1 
ATOM   691  N  NZ  . LYS A  1 83  ? 27.945  8.557   42.632  1.00 21.58 ? 83   LYS A NZ  1 
ATOM   692  N  N   . VAL A  1 84  ? 24.067  1.851   43.431  1.00 7.41  ? 84   VAL A N   1 
ATOM   693  C  CA  . VAL A  1 84  ? 23.665  0.596   42.823  1.00 8.16  ? 84   VAL A CA  1 
ATOM   694  C  C   . VAL A  1 84  ? 23.039  0.855   41.469  1.00 8.61  ? 84   VAL A C   1 
ATOM   695  O  O   . VAL A  1 84  ? 22.499  1.935   41.217  1.00 10.22 ? 84   VAL A O   1 
ATOM   696  C  CB  . VAL A  1 84  ? 22.681  -0.172  43.746  1.00 8.39  ? 84   VAL A CB  1 
ATOM   697  C  CG1 . VAL A  1 84  ? 21.359  0.597   43.884  1.00 11.09 ? 84   VAL A CG1 1 
ATOM   698  C  CG2 . VAL A  1 84  ? 22.439  -1.588  43.240  1.00 12.82 ? 84   VAL A CG2 1 
ATOM   699  N  N   . ILE A  1 85  ? 23.158  -0.132  40.584  1.00 8.29  ? 85   ILE A N   1 
ATOM   700  C  CA  . ILE A  1 85  ? 22.448  -0.097  39.320  1.00 10.05 ? 85   ILE A CA  1 
ATOM   701  C  C   . ILE A  1 85  ? 21.034  -0.611  39.555  1.00 10.38 ? 85   ILE A C   1 
ATOM   702  O  O   . ILE A  1 85  ? 20.850  -1.733  40.020  1.00 13.31 ? 85   ILE A O   1 
ATOM   703  C  CB  . ILE A  1 85  ? 23.118  -1.001  38.277  1.00 12.90 ? 85   ILE A CB  1 
ATOM   704  C  CG1 . ILE A  1 85  ? 24.570  -0.580  38.052  1.00 18.11 ? 85   ILE A CG1 1 
ATOM   705  C  CG2 . ILE A  1 85  ? 22.338  -0.963  36.971  1.00 16.25 ? 85   ILE A CG2 1 
ATOM   706  C  CD1 . ILE A  1 85  ? 25.381  -1.628  37.298  1.00 14.76 ? 85   ILE A CD1 1 
ATOM   707  N  N   . GLU A  1 86  ? 20.037  0.207   39.238  1.00 13.15 ? 86   GLU A N   1 
ATOM   708  C  CA  . GLU A  1 86  ? 18.643  -0.215  39.408  1.00 12.21 ? 86   GLU A CA  1 
ATOM   709  C  C   . GLU A  1 86  ? 17.762  0.404   38.330  1.00 12.72 ? 86   GLU A C   1 
ATOM   710  O  O   . GLU A  1 86  ? 18.103  1.437   37.751  1.00 14.00 ? 86   GLU A O   1 
ATOM   711  C  CB  . GLU A  1 86  ? 18.108  0.126   40.813  1.00 18.27 ? 86   GLU A CB  1 
ATOM   712  C  CG  . GLU A  1 86  ? 18.091  1.618   41.125  1.00 20.30 ? 86   GLU A CG  1 
ATOM   713  C  CD  . GLU A  1 86  ? 17.600  1.935   42.536  1.00 22.35 ? 86   GLU A CD  1 
ATOM   714  O  OE1 . GLU A  1 86  ? 17.427  0.988   43.344  1.00 15.01 ? 86   GLU A OE1 1 
ATOM   715  O  OE2 . GLU A  1 86  ? 17.388  3.139   42.829  1.00 14.44 ? 86   GLU A OE2 1 
ATOM   716  N  N   . LYS A  1 87  ? 16.647  -0.256  38.039  1.00 14.60 ? 87   LYS A N   1 
ATOM   717  C  CA  . LYS A  1 87  ? 15.690  0.261   37.074  1.00 15.92 ? 87   LYS A CA  1 
ATOM   718  C  C   . LYS A  1 87  ? 14.807  1.269   37.780  1.00 14.57 ? 87   LYS A C   1 
ATOM   719  O  O   . LYS A  1 87  ? 14.687  1.249   39.003  1.00 14.97 ? 87   LYS A O   1 
ATOM   720  C  CB  . LYS A  1 87  ? 14.800  -0.867  36.553  1.00 18.54 ? 87   LYS A CB  1 
ATOM   721  C  CG  . LYS A  1 87  ? 15.491  -2.212  36.465  1.00 36.78 ? 87   LYS A CG  1 
ATOM   722  C  CD  . LYS A  1 87  ? 16.138  -2.406  35.117  1.00 49.02 ? 87   LYS A CD  1 
ATOM   723  C  CE  . LYS A  1 87  ? 15.106  -2.794  34.077  1.00 51.39 ? 87   LYS A CE  1 
ATOM   724  N  NZ  . LYS A  1 87  ? 15.754  -3.249  32.818  1.00 58.48 ? 87   LYS A NZ  1 
ATOM   725  N  N   . PHE A  1 88  ? 14.184  2.147   37.006  1.00 14.88 ? 88   PHE A N   1 
ATOM   726  C  CA  . PHE A  1 88  ? 13.217  3.080   37.569  1.00 13.20 ? 88   PHE A CA  1 
ATOM   727  C  C   . PHE A  1 88  ? 12.037  3.307   36.633  1.00 13.13 ? 88   PHE A C   1 
ATOM   728  O  O   . PHE A  1 88  ? 12.226  3.588   35.452  1.00 13.06 ? 88   PHE A O   1 
ATOM   729  C  CB  . PHE A  1 88  ? 13.868  4.432   37.864  1.00 12.33 ? 88   PHE A CB  1 
ATOM   730  C  CG  . PHE A  1 88  ? 12.871  5.489   38.220  1.00 14.25 ? 88   PHE A CG  1 
ATOM   731  C  CD1 . PHE A  1 88  ? 12.384  5.593   39.511  1.00 17.00 ? 88   PHE A CD1 1 
ATOM   732  C  CD2 . PHE A  1 88  ? 12.379  6.348   37.247  1.00 13.86 ? 88   PHE A CD2 1 
ATOM   733  C  CE1 . PHE A  1 88  ? 11.435  6.548   39.833  1.00 13.64 ? 88   PHE A CE1 1 
ATOM   734  C  CE2 . PHE A  1 88  ? 11.428  7.306   37.560  1.00 16.28 ? 88   PHE A CE2 1 
ATOM   735  C  CZ  . PHE A  1 88  ? 10.956  7.404   38.857  1.00 14.99 ? 88   PHE A CZ  1 
ATOM   736  N  N   . PRO A  1 89  ? 10.805  3.199   37.156  1.00 10.13 ? 89   PRO A N   1 
ATOM   737  C  CA  . PRO A  1 89  ? 10.461  2.761   38.515  1.00 9.59  ? 89   PRO A CA  1 
ATOM   738  C  C   . PRO A  1 89  ? 10.516  1.244   38.621  1.00 13.36 ? 89   PRO A C   1 
ATOM   739  O  O   . PRO A  1 89  ? 10.340  0.543   37.625  1.00 12.63 ? 89   PRO A O   1 
ATOM   740  C  CB  . PRO A  1 89  ? 8.992   3.208   38.683  1.00 10.96 ? 89   PRO A CB  1 
ATOM   741  C  CG  . PRO A  1 89  ? 8.616   3.924   37.433  1.00 15.57 ? 89   PRO A CG  1 
ATOM   742  C  CD  . PRO A  1 89  ? 9.619   3.599   36.379  1.00 12.64 ? 89   PRO A CD  1 
ATOM   743  N  N   . ALA A  1 90  ? 10.715  0.733   39.832  1.00 10.17 ? 90   ALA A N   1 
ATOM   744  C  CA  . ALA A  1 90  ? 10.759  -0.703  40.026  1.00 9.87  ? 90   ALA A CA  1 
ATOM   745  C  C   . ALA A  1 90  ? 10.635  -1.016  41.496  1.00 10.88 ? 90   ALA A C   1 
ATOM   746  O  O   . ALA A  1 90  ? 11.175  -0.290  42.334  1.00 11.56 ? 90   ALA A O   1 
ATOM   747  C  CB  . ALA A  1 90  ? 12.061  -1.280  39.484  1.00 17.57 ? 90   ALA A CB  1 
ATOM   748  N  N   . PRO A  1 91  ? 9.922   -2.097  41.810  1.00 8.46  ? 91   PRO A N   1 
ATOM   749  C  CA  . PRO A  1 91  ? 9.907   -2.588  43.186  1.00 12.08 ? 91   PRO A CA  1 
ATOM   750  C  C   . PRO A  1 91  ? 11.333  -2.886  43.625  1.00 11.45 ? 91   PRO A C   1 
ATOM   751  O  O   . PRO A  1 91  ? 12.164  -3.288  42.798  1.00 12.86 ? 91   PRO A O   1 
ATOM   752  C  CB  . PRO A  1 91  ? 9.121   -3.898  43.079  1.00 17.09 ? 91   PRO A CB  1 
ATOM   753  C  CG  . PRO A  1 91  ? 8.278   -3.737  41.857  1.00 16.30 ? 91   PRO A CG  1 
ATOM   754  C  CD  . PRO A  1 91  ? 9.109   -2.934  40.910  1.00 12.36 ? 91   PRO A CD  1 
ATOM   755  N  N   . VAL A  1 92  ? 11.611  -2.696  44.906  1.00 9.47  ? 92   VAL A N   1 
ATOM   756  C  CA  . VAL A  1 92  ? 12.937  -2.959  45.423  1.00 5.95  ? 92   VAL A CA  1 
ATOM   757  C  C   . VAL A  1 92  ? 12.844  -3.631  46.778  1.00 9.18  ? 92   VAL A C   1 
ATOM   758  O  O   . VAL A  1 92  ? 11.908  -3.395  47.542  1.00 10.58 ? 92   VAL A O   1 
ATOM   759  C  CB  . VAL A  1 92  ? 13.786  -1.662  45.493  1.00 10.71 ? 92   VAL A CB  1 
ATOM   760  C  CG1 . VAL A  1 92  ? 13.269  -0.722  46.584  1.00 10.52 ? 92   VAL A CG1 1 
ATOM   761  C  CG2 . VAL A  1 92  ? 15.246  -1.998  45.718  1.00 11.39 ? 92   VAL A CG2 1 
ATOM   762  N  N   . HIS A  1 93  ? 13.792  -4.521  47.048  1.00 9.36  ? 93   HIS A N   1 
ATOM   763  C  CA  . HIS A  1 93  ? 13.945  -5.062  48.388  1.00 9.85  ? 93   HIS A CA  1 
ATOM   764  C  C   . HIS A  1 93  ? 15.232  -4.502  48.960  1.00 7.92  ? 93   HIS A C   1 
ATOM   765  O  O   . HIS A  1 93  ? 16.289  -4.574  48.326  1.00 8.68  ? 93   HIS A O   1 
ATOM   766  C  CB  . HIS A  1 93  ? 13.982  -6.595  48.370  1.00 8.38  ? 93   HIS A CB  1 
ATOM   767  C  CG  . HIS A  1 93  ? 14.057  -7.195  49.737  1.00 9.23  ? 93   HIS A CG  1 
ATOM   768  N  ND1 . HIS A  1 93  ? 15.247  -7.586  50.312  1.00 8.40  ? 93   HIS A ND1 1 
ATOM   769  C  CD2 . HIS A  1 93  ? 13.096  -7.423  50.665  1.00 9.78  ? 93   HIS A CD2 1 
ATOM   770  C  CE1 . HIS A  1 93  ? 15.012  -8.053  51.527  1.00 8.74  ? 93   HIS A CE1 1 
ATOM   771  N  NE2 . HIS A  1 93  ? 13.716  -7.965  51.764  1.00 9.97  ? 93   HIS A NE2 1 
ATOM   772  N  N   . ILE A  1 94  ? 15.137  -3.913  50.149  1.00 7.33  ? 94   ILE A N   1 
ATOM   773  C  CA  . ILE A  1 94  ? 16.263  -3.216  50.740  1.00 8.53  ? 94   ILE A CA  1 
ATOM   774  C  C   . ILE A  1 94  ? 16.541  -3.811  52.106  1.00 11.13 ? 94   ILE A C   1 
ATOM   775  O  O   . ILE A  1 94  ? 15.622  -3.963  52.927  1.00 11.36 ? 94   ILE A O   1 
ATOM   776  C  CB  . ILE A  1 94  ? 15.921  -1.733  50.935  1.00 8.39  ? 94   ILE A CB  1 
ATOM   777  C  CG1 . ILE A  1 94  ? 15.659  -1.049  49.592  1.00 11.14 ? 94   ILE A CG1 1 
ATOM   778  C  CG2 . ILE A  1 94  ? 17.041  -1.017  51.725  1.00 11.83 ? 94   ILE A CG2 1 
ATOM   779  C  CD1 . ILE A  1 94  ? 14.915  0.275   49.732  1.00 15.06 ? 94   ILE A CD1 1 
ATOM   780  N  N   . CYS A  1 95  ? 17.796  -4.180  52.340  1.00 8.53  ? 95   CYS A N   1 
ATOM   781  C  CA  . CYS A  1 95  ? 18.236  -4.506  53.688  1.00 8.22  ? 95   CYS A CA  1 
ATOM   782  C  C   . CYS A  1 95  ? 19.411  -3.607  54.025  1.00 10.12 ? 95   CYS A C   1 
ATOM   783  O  O   . CYS A  1 95  ? 20.244  -3.319  53.174  1.00 9.35  ? 95   CYS A O   1 
ATOM   784  C  CB  . CYS A  1 95  ? 18.707  -5.956  53.774  1.00 13.33 ? 95   CYS A CB  1 
ATOM   785  S  SG  . CYS A  1 95  ? 17.397  -7.216  53.765  1.00 16.77 ? 95   CYS A SG  1 
ATOM   786  N  N   . VAL A  1 96  ? 19.493  -3.173  55.273  1.00 8.82  ? 96   VAL A N   1 
ATOM   787  C  CA  . VAL A  1 96  ? 20.688  -2.467  55.711  1.00 6.92  ? 96   VAL A CA  1 
ATOM   788  C  C   . VAL A  1 96  ? 21.032  -2.912  57.124  1.00 8.79  ? 96   VAL A C   1 
ATOM   789  O  O   . VAL A  1 96  ? 20.146  -2.993  57.981  1.00 10.36 ? 96   VAL A O   1 
ATOM   790  C  CB  . VAL A  1 96  ? 20.534  -0.930  55.612  1.00 9.35  ? 96   VAL A CB  1 
ATOM   791  C  CG1 . VAL A  1 96  ? 19.408  -0.426  56.512  1.00 12.54 ? 96   VAL A CG1 1 
ATOM   792  C  CG2 . VAL A  1 96  ? 21.862  -0.240  55.925  1.00 11.60 ? 96   VAL A CG2 1 
ATOM   793  N  N   . SER A  1 97  ? 22.302  -3.245  57.356  1.00 8.21  ? 97   SER A N   1 
ATOM   794  C  CA  . SER A  1 97  ? 22.755  -3.581  58.705  1.00 8.02  ? 97   SER A CA  1 
ATOM   795  C  C   . SER A  1 97  ? 23.836  -2.604  59.151  1.00 9.11  ? 97   SER A C   1 
ATOM   796  O  O   . SER A  1 97  ? 24.510  -1.983  58.331  1.00 9.18  ? 97   SER A O   1 
ATOM   797  C  CB  . SER A  1 97  ? 23.287  -5.017  58.777  1.00 9.84  ? 97   SER A CB  1 
ATOM   798  O  OG  . SER A  1 97  ? 24.512  -5.172  58.070  1.00 10.39 ? 97   SER A OG  1 
ATOM   799  N  N   . TRP A  1 98  ? 23.992  -2.460  60.460  1.00 8.79  ? 98   TRP A N   1 
ATOM   800  C  CA  . TRP A  1 98  ? 25.054  -1.622  60.988  1.00 8.19  ? 98   TRP A CA  1 
ATOM   801  C  C   . TRP A  1 98  ? 25.565  -2.250  62.270  1.00 10.88 ? 98   TRP A C   1 
ATOM   802  O  O   . TRP A  1 98  ? 24.791  -2.777  63.063  1.00 11.87 ? 98   TRP A O   1 
ATOM   803  C  CB  . TRP A  1 98  ? 24.555  -0.200  61.245  1.00 9.43  ? 98   TRP A CB  1 
ATOM   804  C  CG  . TRP A  1 98  ? 25.594  0.694   61.866  1.00 10.51 ? 98   TRP A CG  1 
ATOM   805  C  CD1 . TRP A  1 98  ? 26.660  1.304   61.234  1.00 9.46  ? 98   TRP A CD1 1 
ATOM   806  C  CD2 . TRP A  1 98  ? 25.677  1.065   63.243  1.00 12.30 ? 98   TRP A CD2 1 
ATOM   807  N  NE1 . TRP A  1 98  ? 27.389  2.037   62.153  1.00 9.91  ? 98   TRP A NE1 1 
ATOM   808  C  CE2 . TRP A  1 98  ? 26.807  1.906   63.388  1.00 13.61 ? 98   TRP A CE2 1 
ATOM   809  C  CE3 . TRP A  1 98  ? 24.901  0.772   64.373  1.00 12.60 ? 98   TRP A CE3 1 
ATOM   810  C  CZ2 . TRP A  1 98  ? 27.176  2.456   64.616  1.00 11.29 ? 98   TRP A CZ2 1 
ATOM   811  C  CZ3 . TRP A  1 98  ? 25.279  1.315   65.596  1.00 14.03 ? 98   TRP A CZ3 1 
ATOM   812  C  CH2 . TRP A  1 98  ? 26.401  2.148   65.704  1.00 11.40 ? 98   TRP A CH2 1 
ATOM   813  N  N   . GLU A  1 99  ? 26.874  -2.187  62.465  1.00 8.40  ? 99   GLU A N   1 
ATOM   814  C  CA  . GLU A  1 99  ? 27.530  -2.843  63.591  1.00 11.14 ? 99   GLU A CA  1 
ATOM   815  C  C   . GLU A  1 99  ? 28.387  -1.804  64.303  1.00 12.69 ? 99   GLU A C   1 
ATOM   816  O  O   . GLU A  1 99  ? 29.345  -1.311  63.732  1.00 12.37 ? 99   GLU A O   1 
ATOM   817  C  CB  . GLU A  1 99  ? 28.424  -3.950  63.041  1.00 10.92 ? 99   GLU A CB  1 
ATOM   818  C  CG  . GLU A  1 99  ? 29.154  -4.778  64.076  1.00 15.51 ? 99   GLU A CG  1 
ATOM   819  C  CD  . GLU A  1 99  ? 30.082  -5.789  63.434  1.00 19.50 ? 99   GLU A CD  1 
ATOM   820  O  OE1 . GLU A  1 99  ? 29.926  -6.998  63.714  1.00 23.25 ? 99   GLU A OE1 1 
ATOM   821  O  OE2 . GLU A  1 99  ? 30.966  -5.385  62.643  1.00 13.57 ? 99   GLU A OE2 1 
ATOM   822  N  N   . SER A  1 100 ? 28.041  -1.455  65.537  1.00 10.82 ? 100  SER A N   1 
ATOM   823  C  CA  . SER A  1 100 ? 28.817  -0.439  66.263  1.00 11.64 ? 100  SER A CA  1 
ATOM   824  C  C   . SER A  1 100 ? 30.311  -0.750  66.367  1.00 12.38 ? 100  SER A C   1 
ATOM   825  O  O   . SER A  1 100 ? 31.148  0.148   66.234  1.00 14.37 ? 100  SER A O   1 
ATOM   826  C  CB  . SER A  1 100 ? 28.266  -0.263  67.676  1.00 13.04 ? 100  SER A CB  1 
ATOM   827  O  OG  . SER A  1 100 ? 29.100  0.608   68.429  1.00 13.90 ? 100  SER A OG  1 
ATOM   828  N  N   . SER A  1 101 ? 30.648  -2.010  66.619  1.00 11.39 ? 101  SER A N   1 
ATOM   829  C  CA  . SER A  1 101 ? 32.025  -2.375  66.940  1.00 14.88 ? 101  SER A CA  1 
ATOM   830  C  C   . SER A  1 101 ? 32.983  -2.039  65.809  1.00 15.27 ? 101  SER A C   1 
ATOM   831  O  O   . SER A  1 101 ? 34.130  -1.655  66.049  1.00 13.33 ? 101  SER A O   1 
ATOM   832  C  CB  . SER A  1 101 ? 32.130  -3.862  67.299  1.00 15.60 ? 101  SER A CB  1 
ATOM   833  O  OG  . SER A  1 101 ? 31.705  -4.676  66.218  1.00 17.17 ? 101  SER A OG  1 
ATOM   834  N  N   . SER A  1 102 ? 32.502  -2.180  64.576  1.00 12.38 ? 102  SER A N   1 
ATOM   835  C  CA  . SER A  1 102 ? 33.305  -1.876  63.398  1.00 10.71 ? 102  SER A CA  1 
ATOM   836  C  C   . SER A  1 102 ? 32.874  -0.589  62.709  1.00 11.14 ? 102  SER A C   1 
ATOM   837  O  O   . SER A  1 102 ? 33.627  -0.047  61.907  1.00 10.07 ? 102  SER A O   1 
ATOM   838  C  CB  . SER A  1 102 ? 33.176  -3.006  62.380  1.00 10.01 ? 102  SER A CB  1 
ATOM   839  O  OG  . SER A  1 102 ? 31.836  -3.079  61.924  1.00 9.79  ? 102  SER A OG  1 
ATOM   840  N  N   . GLY A  1 103 ? 31.658  -0.127  62.998  1.00 7.49  ? 103  GLY A N   1 
ATOM   841  C  CA  . GLY A  1 103 ? 31.040  0.977   62.281  1.00 8.33  ? 103  GLY A CA  1 
ATOM   842  C  C   . GLY A  1 103 ? 30.528  0.615   60.897  1.00 7.85  ? 103  GLY A C   1 
ATOM   843  O  O   . GLY A  1 103 ? 30.020  1.478   60.180  1.00 8.23  ? 103  GLY A O   1 
ATOM   844  N  N   . ILE A  1 104 ? 30.659  -0.652  60.515  1.00 7.83  ? 104  ILE A N   1 
ATOM   845  C  CA  . ILE A  1 104 ? 30.327  -1.058  59.140  1.00 8.06  ? 104  ILE A CA  1 
ATOM   846  C  C   . ILE A  1 104 ? 28.819  -1.082  58.868  1.00 8.59  ? 104  ILE A C   1 
ATOM   847  O  O   . ILE A  1 104 ? 28.043  -1.689  59.624  1.00 9.20  ? 104  ILE A O   1 
ATOM   848  C  CB  . ILE A  1 104 ? 30.927  -2.424  58.778  1.00 6.20  ? 104  ILE A CB  1 
ATOM   849  C  CG1 . ILE A  1 104 ? 32.459  -2.366  58.788  1.00 9.84  ? 104  ILE A CG1 1 
ATOM   850  C  CG2 . ILE A  1 104 ? 30.408  -2.884  57.414  1.00 9.54  ? 104  ILE A CG2 1 
ATOM   851  C  CD1 . ILE A  1 104 ? 33.041  -1.399  57.741  1.00 13.01 ? 104  ILE A CD1 1 
ATOM   852  N  N   . ALA A  1 105 ? 28.427  -0.417  57.783  1.00 7.93  ? 105  ALA A N   1 
ATOM   853  C  CA  . ALA A  1 105 ? 27.054  -0.417  57.294  1.00 8.04  ? 105  ALA A CA  1 
ATOM   854  C  C   . ALA A  1 105 ? 27.040  -1.224  56.000  1.00 8.99  ? 105  ALA A C   1 
ATOM   855  O  O   . ALA A  1 105 ? 27.841  -0.974  55.102  1.00 9.79  ? 105  ALA A O   1 
ATOM   856  C  CB  . ALA A  1 105 ? 26.579  1.004   57.040  1.00 9.75  ? 105  ALA A CB  1 
ATOM   857  N  N   A GLU A  1 106 ? 26.110  -2.164  55.883  0.45 7.49  ? 106  GLU A N   1 
ATOM   858  N  N   B GLU A  1 106 ? 26.152  -2.215  55.948  0.55 7.48  ? 106  GLU A N   1 
ATOM   859  C  CA  A GLU A  1 106 ? 26.076  -3.063  54.733  0.45 8.87  ? 106  GLU A CA  1 
ATOM   860  C  CA  B GLU A  1 106 ? 25.959  -3.057  54.774  0.55 8.90  ? 106  GLU A CA  1 
ATOM   861  C  C   A GLU A  1 106 ? 24.690  -3.068  54.067  0.45 10.44 ? 106  GLU A C   1 
ATOM   862  C  C   B GLU A  1 106 ? 24.589  -2.801  54.180  0.55 10.30 ? 106  GLU A C   1 
ATOM   863  O  O   A GLU A  1 106 ? 23.761  -3.678  54.602  0.45 9.30  ? 106  GLU A O   1 
ATOM   864  O  O   B GLU A  1 106 ? 23.575  -2.995  54.848  0.55 10.17 ? 106  GLU A O   1 
ATOM   865  C  CB  A GLU A  1 106 ? 26.462  -4.479  55.199  0.45 9.76  ? 106  GLU A CB  1 
ATOM   866  C  CB  B GLU A  1 106 ? 26.003  -4.539  55.162  0.55 10.96 ? 106  GLU A CB  1 
ATOM   867  C  CG  A GLU A  1 106 ? 26.565  -5.513  54.097  0.45 10.49 ? 106  GLU A CG  1 
ATOM   868  C  CG  B GLU A  1 106 ? 27.328  -5.050  55.638  0.55 10.46 ? 106  GLU A CG  1 
ATOM   869  C  CD  A GLU A  1 106 ? 26.897  -6.910  54.607  0.45 15.90 ? 106  GLU A CD  1 
ATOM   870  C  CD  B GLU A  1 106 ? 27.339  -6.567  55.804  0.55 15.62 ? 106  GLU A CD  1 
ATOM   871  O  OE1 A GLU A  1 106 ? 28.070  -7.327  54.503  0.45 15.12 ? 106  GLU A OE1 1 
ATOM   872  O  OE1 B GLU A  1 106 ? 26.452  -7.250  55.242  0.55 14.90 ? 106  GLU A OE1 1 
ATOM   873  O  OE2 A GLU A  1 106 ? 25.984  -7.597  55.108  0.45 11.73 ? 106  GLU A OE2 1 
ATOM   874  O  OE2 B GLU A  1 106 ? 28.240  -7.080  56.495  0.55 16.46 ? 106  GLU A OE2 1 
ATOM   875  N  N   . PHE A  1 107 ? 24.555  -2.385  52.919  1.00 9.98  ? 107  PHE A N   1 
ATOM   876  C  CA  . PHE A  1 107 ? 23.291  -2.317  52.176  1.00 9.63  ? 107  PHE A CA  1 
ATOM   877  C  C   . PHE A  1 107 ? 23.203  -3.522  51.240  1.00 8.69  ? 107  PHE A C   1 
ATOM   878  O  O   . PHE A  1 107 ? 24.203  -3.913  50.612  1.00 8.93  ? 107  PHE A O   1 
ATOM   879  C  CB  . PHE A  1 107 ? 23.202  -1.037  51.319  1.00 7.38  ? 107  PHE A CB  1 
ATOM   880  C  CG  . PHE A  1 107 ? 22.516  0.144   51.997  1.00 10.85 ? 107  PHE A CG  1 
ATOM   881  C  CD1 . PHE A  1 107 ? 21.140  0.174   52.165  1.00 10.00 ? 107  PHE A CD1 1 
ATOM   882  C  CD2 . PHE A  1 107 ? 23.252  1.238   52.410  1.00 12.15 ? 107  PHE A CD2 1 
ATOM   883  C  CE1 . PHE A  1 107 ? 20.509  1.271   52.764  1.00 13.56 ? 107  PHE A CE1 1 
ATOM   884  C  CE2 . PHE A  1 107 ? 22.643  2.336   53.005  1.00 10.39 ? 107  PHE A CE2 1 
ATOM   885  C  CZ  . PHE A  1 107 ? 21.265  2.356   53.187  1.00 13.02 ? 107  PHE A CZ  1 
ATOM   886  N  N   . TRP A  1 108 ? 22.017  -4.117  51.161  1.00 7.30  ? 108  TRP A N   1 
ATOM   887  C  CA  . TRP A  1 108 ? 21.711  -5.147  50.164  1.00 6.30  ? 108  TRP A CA  1 
ATOM   888  C  C   . TRP A  1 108 ? 20.477  -4.715  49.385  1.00 6.32  ? 108  TRP A C   1 
ATOM   889  O  O   . TRP A  1 108 ? 19.455  -4.379  49.974  1.00 7.87  ? 108  TRP A O   1 
ATOM   890  C  CB  . TRP A  1 108 ? 21.410  -6.480  50.844  1.00 8.41  ? 108  TRP A CB  1 
ATOM   891  C  CG  . TRP A  1 108 ? 22.588  -7.064  51.533  1.00 11.49 ? 108  TRP A CG  1 
ATOM   892  C  CD1 . TRP A  1 108 ? 23.162  -6.625  52.688  1.00 11.17 ? 108  TRP A CD1 1 
ATOM   893  C  CD2 . TRP A  1 108 ? 23.344  -8.203  51.110  1.00 8.36  ? 108  TRP A CD2 1 
ATOM   894  N  NE1 . TRP A  1 108 ? 24.235  -7.428  53.015  1.00 12.44 ? 108  TRP A NE1 1 
ATOM   895  C  CE2 . TRP A  1 108 ? 24.366  -8.403  52.063  1.00 12.40 ? 108  TRP A CE2 1 
ATOM   896  C  CE3 . TRP A  1 108 ? 23.248  -9.081  50.026  1.00 9.44  ? 108  TRP A CE3 1 
ATOM   897  C  CZ2 . TRP A  1 108 ? 25.295  -9.441  51.961  1.00 9.58  ? 108  TRP A CZ2 1 
ATOM   898  C  CZ3 . TRP A  1 108 ? 24.183  -10.110 49.918  1.00 12.70 ? 108  TRP A CZ3 1 
ATOM   899  C  CH2 . TRP A  1 108 ? 25.187  -10.281 50.885  1.00 14.28 ? 108  TRP A CH2 1 
ATOM   900  N  N   . ILE A  1 109 ? 20.564  -4.733  48.059  1.00 7.54  ? 109  ILE A N   1 
ATOM   901  C  CA  . ILE A  1 109 ? 19.466  -4.261  47.222  1.00 6.81  ? 109  ILE A CA  1 
ATOM   902  C  C   . ILE A  1 109 ? 19.075  -5.409  46.304  1.00 7.76  ? 109  ILE A C   1 
ATOM   903  O  O   . ILE A  1 109 ? 19.898  -5.900  45.535  1.00 11.92 ? 109  ILE A O   1 
ATOM   904  C  CB  . ILE A  1 109 ? 19.893  -3.036  46.388  1.00 9.16  ? 109  ILE A CB  1 
ATOM   905  C  CG1 . ILE A  1 109 ? 20.369  -1.903  47.314  1.00 9.02  ? 109  ILE A CG1 1 
ATOM   906  C  CG2 . ILE A  1 109 ? 18.764  -2.599  45.433  1.00 11.41 ? 109  ILE A CG2 1 
ATOM   907  C  CD1 . ILE A  1 109 ? 19.269  -1.330  48.221  1.00 8.38  ? 109  ILE A CD1 1 
ATOM   908  N  N   . ASN A  1 110 ? 17.833  -5.860  46.420  1.00 7.93  ? 110  ASN A N   1 
ATOM   909  C  CA  . ASN A  1 110 ? 17.391  -7.041  45.683  1.00 9.58  ? 110  ASN A CA  1 
ATOM   910  C  C   . ASN A  1 110 ? 18.356  -8.215  45.825  1.00 13.53 ? 110  ASN A C   1 
ATOM   911  O  O   . ASN A  1 110 ? 18.662  -8.908  44.847  1.00 12.50 ? 110  ASN A O   1 
ATOM   912  C  CB  . ASN A  1 110 ? 17.206  -6.707  44.211  1.00 10.67 ? 110  ASN A CB  1 
ATOM   913  C  CG  . ASN A  1 110 ? 16.149  -5.661  43.991  1.00 12.98 ? 110  ASN A CG  1 
ATOM   914  O  OD1 . ASN A  1 110 ? 15.184  -5.584  44.741  1.00 11.96 ? 110  ASN A OD1 1 
ATOM   915  N  ND2 . ASN A  1 110 ? 16.327  -4.844  42.965  1.00 16.86 ? 110  ASN A ND2 1 
ATOM   916  N  N   . GLY A  1 111 ? 18.829  -8.421  47.048  1.00 7.88  ? 111  GLY A N   1 
ATOM   917  C  CA  . GLY A  1 111 ? 19.694  -9.540  47.362  1.00 12.40 ? 111  GLY A CA  1 
ATOM   918  C  C   . GLY A  1 111 ? 21.126  -9.382  46.890  1.00 10.65 ? 111  GLY A C   1 
ATOM   919  O  O   . GLY A  1 111 ? 21.896  -10.336 46.936  1.00 15.70 ? 111  GLY A O   1 
ATOM   920  N  N   A THR A  1 112 ? 21.477  -8.177  46.442  0.53 9.52  ? 112  THR A N   1 
ATOM   921  N  N   B THR A  1 112 ? 21.495  -8.194  46.429  0.47 9.54  ? 112  THR A N   1 
ATOM   922  C  CA  A THR A  1 112 ? 22.831  -7.876  45.968  0.53 10.94 ? 112  THR A CA  1 
ATOM   923  C  CA  B THR A  1 112 ? 22.872  -7.975  45.998  0.47 10.92 ? 112  THR A CA  1 
ATOM   924  C  C   A THR A  1 112 ? 23.540  -6.936  46.943  0.53 8.62  ? 112  THR A C   1 
ATOM   925  C  C   B THR A  1 112 ? 23.557  -6.958  46.899  0.47 8.61  ? 112  THR A C   1 
ATOM   926  O  O   A THR A  1 112 ? 22.986  -5.898  47.315  0.53 9.28  ? 112  THR A O   1 
ATOM   927  O  O   B THR A  1 112 ? 23.005  -5.888  47.174  0.47 9.33  ? 112  THR A O   1 
ATOM   928  C  CB  A THR A  1 112 ? 22.795  -7.203  44.576  0.53 11.43 ? 112  THR A CB  1 
ATOM   929  C  CB  B THR A  1 112 ? 22.945  -7.493  44.546  0.47 12.02 ? 112  THR A CB  1 
ATOM   930  O  OG1 A THR A  1 112 ? 22.278  -8.122  43.606  0.53 14.71 ? 112  THR A OG1 1 
ATOM   931  O  OG1 B THR A  1 112 ? 22.339  -6.202  44.447  0.47 13.68 ? 112  THR A OG1 1 
ATOM   932  C  CG2 A THR A  1 112 ? 24.194  -6.761  44.148  0.53 12.15 ? 112  THR A CG2 1 
ATOM   933  C  CG2 B THR A  1 112 ? 22.229  -8.470  43.622  0.47 13.86 ? 112  THR A CG2 1 
ATOM   934  N  N   . PRO A  1 113 ? 24.768  -7.284  47.362  1.00 7.81  ? 113  PRO A N   1 
ATOM   935  C  CA  . PRO A  1 113 ? 25.444  -6.397  48.321  1.00 5.71  ? 113  PRO A CA  1 
ATOM   936  C  C   . PRO A  1 113 ? 26.035  -5.165  47.649  1.00 6.25  ? 113  PRO A C   1 
ATOM   937  O  O   . PRO A  1 113 ? 26.642  -5.253  46.585  1.00 8.12  ? 113  PRO A O   1 
ATOM   938  C  CB  . PRO A  1 113 ? 26.549  -7.271  48.904  1.00 6.71  ? 113  PRO A CB  1 
ATOM   939  C  CG  . PRO A  1 113 ? 26.792  -8.330  47.874  1.00 7.91  ? 113  PRO A CG  1 
ATOM   940  C  CD  . PRO A  1 113 ? 25.528  -8.522  47.094  1.00 8.15  ? 113  PRO A CD  1 
ATOM   941  N  N   . LEU A  1 114 ? 25.836  -4.018  48.284  1.00 6.41  ? 114  LEU A N   1 
ATOM   942  C  CA  . LEU A  1 114 ? 26.492  -2.782  47.858  1.00 5.63  ? 114  LEU A CA  1 
ATOM   943  C  C   . LEU A  1 114 ? 27.861  -2.688  48.536  1.00 5.84  ? 114  LEU A C   1 
ATOM   944  O  O   . LEU A  1 114 ? 28.191  -3.497  49.413  1.00 7.34  ? 114  LEU A O   1 
ATOM   945  C  CB  . LEU A  1 114 ? 25.634  -1.568  48.238  1.00 7.14  ? 114  LEU A CB  1 
ATOM   946  C  CG  . LEU A  1 114 ? 24.195  -1.534  47.712  1.00 8.78  ? 114  LEU A CG  1 
ATOM   947  C  CD1 . LEU A  1 114 ? 23.641  -0.086  47.713  1.00 7.72  ? 114  LEU A CD1 1 
ATOM   948  C  CD2 . LEU A  1 114 ? 24.108  -2.149  46.335  1.00 11.28 ? 114  LEU A CD2 1 
ATOM   949  N  N   . VAL A  1 115 ? 28.664  -1.698  48.150  1.00 6.08  ? 115  VAL A N   1 
ATOM   950  C  CA  . VAL A  1 115 ? 29.962  -1.523  48.790  1.00 6.49  ? 115  VAL A CA  1 
ATOM   951  C  C   . VAL A  1 115 ? 29.741  -1.149  50.257  1.00 7.57  ? 115  VAL A C   1 
ATOM   952  O  O   . VAL A  1 115 ? 28.939  -0.264  50.564  1.00 8.47  ? 115  VAL A O   1 
ATOM   953  C  CB  . VAL A  1 115 ? 30.807  -0.425  48.081  1.00 7.32  ? 115  VAL A CB  1 
ATOM   954  C  CG1 . VAL A  1 115 ? 32.176  -0.242  48.767  1.00 7.23  ? 115  VAL A CG1 1 
ATOM   955  C  CG2 . VAL A  1 115 ? 31.007  -0.781  46.601  1.00 7.53  ? 115  VAL A CG2 1 
ATOM   956  N  N   . LYS A  1 116 ? 30.445  -1.828  51.162  1.00 7.14  ? 116  LYS A N   1 
ATOM   957  C  CA  . LYS A  1 116 ? 30.354  -1.484  52.582  1.00 5.75  ? 116  LYS A CA  1 
ATOM   958  C  C   . LYS A  1 116 ? 30.935  -0.098  52.844  1.00 9.10  ? 116  LYS A C   1 
ATOM   959  O  O   . LYS A  1 116 ? 31.899  0.317   52.196  1.00 9.82  ? 116  LYS A O   1 
ATOM   960  C  CB  . LYS A  1 116 ? 31.105  -2.510  53.449  1.00 7.23  ? 116  LYS A CB  1 
ATOM   961  C  CG  . LYS A  1 116 ? 30.398  -3.846  53.681  1.00 10.17 ? 116  LYS A CG  1 
ATOM   962  C  CD  . LYS A  1 116 ? 31.430  -4.839  54.211  1.00 14.76 ? 116  LYS A CD  1 
ATOM   963  C  CE  . LYS A  1 116 ? 30.836  -6.184  54.571  1.00 24.32 ? 116  LYS A CE  1 
ATOM   964  N  NZ  . LYS A  1 116 ? 30.318  -6.892  53.371  1.00 17.98 ? 116  LYS A NZ  1 
ATOM   965  N  N   . LYS A  1 117 ? 30.336  0.613   53.791  1.00 7.54  ? 117  LYS A N   1 
ATOM   966  C  CA  . LYS A  1 117 ? 30.855  1.911   54.235  1.00 8.35  ? 117  LYS A CA  1 
ATOM   967  C  C   . LYS A  1 117 ? 30.895  1.860   55.749  1.00 9.40  ? 117  LYS A C   1 
ATOM   968  O  O   . LYS A  1 117 ? 30.391  0.909   56.346  1.00 11.71 ? 117  LYS A O   1 
ATOM   969  C  CB  . LYS A  1 117 ? 29.953  3.047   53.751  1.00 8.80  ? 117  LYS A CB  1 
ATOM   970  C  CG  . LYS A  1 117 ? 29.815  3.122   52.223  1.00 8.18  ? 117  LYS A CG  1 
ATOM   971  C  CD  . LYS A  1 117 ? 31.141  3.506   51.559  1.00 10.04 ? 117  LYS A CD  1 
ATOM   972  C  CE  . LYS A  1 117 ? 31.132  3.207   50.066  1.00 10.33 ? 117  LYS A CE  1 
ATOM   973  N  NZ  . LYS A  1 117 ? 30.158  4.081   49.360  1.00 11.84 ? 117  LYS A NZ  1 
ATOM   974  N  N   . GLY A  1 118 ? 31.513  2.850   56.381  1.00 7.70  ? 118  GLY A N   1 
ATOM   975  C  CA  . GLY A  1 118 ? 31.629  2.822   57.831  1.00 9.42  ? 118  GLY A CA  1 
ATOM   976  C  C   . GLY A  1 118 ? 31.378  4.182   58.454  1.00 10.38 ? 118  GLY A C   1 
ATOM   977  O  O   . GLY A  1 118 ? 31.787  5.210   57.912  1.00 9.85  ? 118  GLY A O   1 
ATOM   978  N  N   . LEU A  1 119 ? 30.695  4.183   59.595  1.00 9.40  ? 119  LEU A N   1 
ATOM   979  C  CA  . LEU A  1 119 ? 30.413  5.411   60.335  1.00 7.95  ? 119  LEU A CA  1 
ATOM   980  C  C   . LEU A  1 119 ? 30.131  5.078   61.798  1.00 8.33  ? 119  LEU A C   1 
ATOM   981  O  O   . LEU A  1 119 ? 29.723  3.962   62.129  1.00 8.55  ? 119  LEU A O   1 
ATOM   982  C  CB  . LEU A  1 119 ? 29.208  6.161   59.746  1.00 10.28 ? 119  LEU A CB  1 
ATOM   983  C  CG  . LEU A  1 119 ? 27.802  5.573   59.958  1.00 7.79  ? 119  LEU A CG  1 
ATOM   984  C  CD1 . LEU A  1 119 ? 26.746  6.574   59.523  1.00 8.89  ? 119  LEU A CD1 1 
ATOM   985  C  CD2 . LEU A  1 119 ? 27.606  4.253   59.213  1.00 9.16  ? 119  LEU A CD2 1 
ATOM   986  N  N   . ARG A  1 120 ? 30.352  6.062   62.663  1.00 8.85  ? 120  ARG A N   1 
ATOM   987  C  CA  . ARG A  1 120 ? 29.978  5.979   64.085  1.00 9.50  ? 120  ARG A CA  1 
ATOM   988  C  C   . ARG A  1 120 ? 30.478  4.718   64.816  1.00 11.33 ? 120  ARG A C   1 
ATOM   989  O  O   . ARG A  1 120 ? 29.774  4.148   65.640  1.00 10.56 ? 120  ARG A O   1 
ATOM   990  C  CB  . ARG A  1 120 ? 28.460  6.191   64.289  1.00 10.90 ? 120  ARG A CB  1 
ATOM   991  C  CG  . ARG A  1 120 ? 27.948  7.522   63.712  1.00 11.14 ? 120  ARG A CG  1 
ATOM   992  C  CD  . ARG A  1 120 ? 27.224  8.453   64.710  1.00 29.25 ? 120  ARG A CD  1 
ATOM   993  N  NE  . ARG A  1 120 ? 28.088  8.912   65.787  1.00 27.59 ? 120  ARG A NE  1 
ATOM   994  C  CZ  . ARG A  1 120 ? 27.898  10.010  66.531  1.00 14.35 ? 120  ARG A CZ  1 
ATOM   995  N  NH1 . ARG A  1 120 ? 26.876  10.835  66.332  1.00 17.59 ? 120  ARG A NH1 1 
ATOM   996  N  NH2 . ARG A  1 120 ? 28.763  10.287  67.485  1.00 18.39 ? 120  ARG A NH2 1 
ATOM   997  N  N   . GLN A  1 121 ? 31.702  4.291   64.518  1.00 10.08 ? 121  GLN A N   1 
ATOM   998  C  CA  . GLN A  1 121 ? 32.279  3.153   65.208  1.00 9.99  ? 121  GLN A CA  1 
ATOM   999  C  C   . GLN A  1 121 ? 32.276  3.428   66.706  1.00 16.36 ? 121  GLN A C   1 
ATOM   1000 O  O   . GLN A  1 121 ? 32.741  4.487   67.147  1.00 12.84 ? 121  GLN A O   1 
ATOM   1001 C  CB  . GLN A  1 121 ? 33.715  2.904   64.747  1.00 10.06 ? 121  GLN A CB  1 
ATOM   1002 C  CG  . GLN A  1 121 ? 34.385  1.737   65.475  1.00 9.57  ? 121  GLN A CG  1 
ATOM   1003 C  CD  . GLN A  1 121 ? 35.787  1.436   64.953  1.00 15.43 ? 121  GLN A CD  1 
ATOM   1004 O  OE1 . GLN A  1 121 ? 36.513  2.338   64.534  1.00 15.93 ? 121  GLN A OE1 1 
ATOM   1005 N  NE2 . GLN A  1 121 ? 36.175  0.169   64.994  1.00 13.40 ? 121  GLN A NE2 1 
ATOM   1006 N  N   . GLY A  1 122 ? 31.727  2.491   67.472  1.00 13.31 ? 122  GLY A N   1 
ATOM   1007 C  CA  . GLY A  1 122 ? 31.676  2.610   68.922  1.00 14.24 ? 122  GLY A CA  1 
ATOM   1008 C  C   . GLY A  1 122 ? 30.441  3.301   69.479  1.00 16.61 ? 122  GLY A C   1 
ATOM   1009 O  O   . GLY A  1 122 ? 30.256  3.355   70.698  1.00 16.48 ? 122  GLY A O   1 
ATOM   1010 N  N   . TYR A  1 123 ? 29.606  3.842   68.594  1.00 14.25 ? 123  TYR A N   1 
ATOM   1011 C  CA  . TYR A  1 123 ? 28.399  4.572   68.978  1.00 12.02 ? 123  TYR A CA  1 
ATOM   1012 C  C   . TYR A  1 123 ? 27.276  3.619   69.351  1.00 15.66 ? 123  TYR A C   1 
ATOM   1013 O  O   . TYR A  1 123 ? 27.229  2.506   68.851  1.00 13.71 ? 123  TYR A O   1 
ATOM   1014 C  CB  . TYR A  1 123 ? 27.950  5.424   67.794  1.00 12.89 ? 123  TYR A CB  1 
ATOM   1015 C  CG  . TYR A  1 123 ? 26.770  6.332   68.048  1.00 15.02 ? 123  TYR A CG  1 
ATOM   1016 C  CD1 . TYR A  1 123 ? 26.899  7.456   68.857  1.00 15.87 ? 123  TYR A CD1 1 
ATOM   1017 C  CD2 . TYR A  1 123 ? 25.543  6.094   67.446  1.00 14.30 ? 123  TYR A CD2 1 
ATOM   1018 C  CE1 . TYR A  1 123 ? 25.834  8.304   69.070  1.00 16.14 ? 123  TYR A CE1 1 
ATOM   1019 C  CE2 . TYR A  1 123 ? 24.466  6.937   67.659  1.00 14.85 ? 123  TYR A CE2 1 
ATOM   1020 C  CZ  . TYR A  1 123 ? 24.623  8.042   68.476  1.00 16.62 ? 123  TYR A CZ  1 
ATOM   1021 O  OH  . TYR A  1 123 ? 23.566  8.890   68.709  1.00 16.33 ? 123  TYR A OH  1 
ATOM   1022 N  N   . PHE A  1 124 ? 26.376  4.061   70.234  1.00 15.00 ? 124  PHE A N   1 
ATOM   1023 C  CA  . PHE A  1 124 ? 25.155  3.316   70.532  1.00 18.51 ? 124  PHE A CA  1 
ATOM   1024 C  C   . PHE A  1 124 ? 23.951  4.102   70.031  1.00 14.25 ? 124  PHE A C   1 
ATOM   1025 O  O   . PHE A  1 124 ? 23.759  5.255   70.408  1.00 15.38 ? 124  PHE A O   1 
ATOM   1026 C  CB  . PHE A  1 124 ? 25.015  3.093   72.037  1.00 17.92 ? 124  PHE A CB  1 
ATOM   1027 C  CG  . PHE A  1 124 ? 25.873  1.988   72.573  1.00 20.93 ? 124  PHE A CG  1 
ATOM   1028 C  CD1 . PHE A  1 124 ? 26.993  1.562   71.885  1.00 28.93 ? 124  PHE A CD1 1 
ATOM   1029 C  CD2 . PHE A  1 124 ? 25.574  1.396   73.788  1.00 31.09 ? 124  PHE A CD2 1 
ATOM   1030 C  CE1 . PHE A  1 124 ? 27.790  0.549   72.385  1.00 37.81 ? 124  PHE A CE1 1 
ATOM   1031 C  CE2 . PHE A  1 124 ? 26.366  0.385   74.295  1.00 28.41 ? 124  PHE A CE2 1 
ATOM   1032 C  CZ  . PHE A  1 124 ? 27.478  -0.039  73.593  1.00 39.58 ? 124  PHE A CZ  1 
ATOM   1033 N  N   . VAL A  1 125 ? 23.146  3.494   69.167  1.00 12.89 ? 125  VAL A N   1 
ATOM   1034 C  CA  . VAL A  1 125 ? 21.929  4.146   68.700  1.00 11.23 ? 125  VAL A CA  1 
ATOM   1035 C  C   . VAL A  1 125 ? 20.968  4.309   69.878  1.00 11.57 ? 125  VAL A C   1 
ATOM   1036 O  O   . VAL A  1 125 ? 20.661  3.342   70.572  1.00 17.26 ? 125  VAL A O   1 
ATOM   1037 C  CB  . VAL A  1 125 ? 21.257  3.346   67.563  1.00 12.73 ? 125  VAL A CB  1 
ATOM   1038 C  CG1 . VAL A  1 125 ? 19.871  3.902   67.258  1.00 14.24 ? 125  VAL A CG1 1 
ATOM   1039 C  CG2 . VAL A  1 125 ? 22.132  3.373   66.306  1.00 14.01 ? 125  VAL A CG2 1 
ATOM   1040 N  N   . GLU A  1 126 ? 20.510  5.536   70.107  1.00 16.50 ? 126  GLU A N   1 
ATOM   1041 C  CA  . GLU A  1 126 ? 19.706  5.818   71.297  1.00 19.29 ? 126  GLU A CA  1 
ATOM   1042 C  C   . GLU A  1 126 ? 18.375  5.083   71.297  1.00 23.59 ? 126  GLU A C   1 
ATOM   1043 O  O   . GLU A  1 126 ? 17.824  4.766   70.241  1.00 19.33 ? 126  GLU A O   1 
ATOM   1044 C  CB  . GLU A  1 126 ? 19.501  7.321   71.480  1.00 22.48 ? 126  GLU A CB  1 
ATOM   1045 C  CG  . GLU A  1 126 ? 20.609  7.987   72.275  1.00 34.14 ? 126  GLU A CG  1 
ATOM   1046 C  CD  . GLU A  1 126 ? 20.565  7.614   73.754  1.00 53.20 ? 126  GLU A CD  1 
ATOM   1047 O  OE1 . GLU A  1 126 ? 19.721  6.775   74.149  1.00 47.24 ? 126  GLU A OE1 1 
ATOM   1048 O  OE2 . GLU A  1 126 ? 21.379  8.164   74.525  1.00 65.23 ? 126  GLU A OE2 1 
ATOM   1049 N  N   . ALA A  1 127 ? 17.873  4.800   72.493  1.00 21.57 ? 127  ALA A N   1 
ATOM   1050 C  CA  . ALA A  1 127 ? 16.620  4.076   72.649  1.00 26.98 ? 127  ALA A CA  1 
ATOM   1051 C  C   . ALA A  1 127 ? 15.431  5.024   72.774  1.00 19.15 ? 127  ALA A C   1 
ATOM   1052 O  O   . ALA A  1 127 ? 15.573  6.240   72.622  1.00 20.74 ? 127  ALA A O   1 
ATOM   1053 C  CB  . ALA A  1 127 ? 16.694  3.153   73.856  1.00 30.89 ? 127  ALA A CB  1 
ATOM   1054 N  N   . GLN A  1 128 ? 14.267  4.450   73.072  1.00 20.25 ? 128  GLN A N   1 
ATOM   1055 C  CA  . GLN A  1 128 ? 13.008  5.195   73.154  1.00 24.89 ? 128  GLN A CA  1 
ATOM   1056 C  C   . GLN A  1 128 ? 12.726  5.967   71.870  1.00 20.84 ? 128  GLN A C   1 
ATOM   1057 O  O   . GLN A  1 128 ? 12.488  7.171   71.905  1.00 20.66 ? 128  GLN A O   1 
ATOM   1058 C  CB  . GLN A  1 128 ? 13.011  6.166   74.344  1.00 31.28 ? 128  GLN A CB  1 
ATOM   1059 C  CG  . GLN A  1 128 ? 13.800  5.700   75.561  1.00 44.86 ? 128  GLN A CG  1 
ATOM   1060 C  CD  . GLN A  1 128 ? 13.344  4.357   76.095  1.00 51.29 ? 128  GLN A CD  1 
ATOM   1061 O  OE1 . GLN A  1 128 ? 14.136  3.604   76.665  1.00 60.62 ? 128  GLN A OE1 1 
ATOM   1062 N  NE2 . GLN A  1 128 ? 12.065  4.048   75.915  1.00 54.58 ? 128  GLN A NE2 1 
ATOM   1063 N  N   . PRO A  1 129 ? 12.755  5.278   70.718  1.00 18.48 ? 129  PRO A N   1 
ATOM   1064 C  CA  . PRO A  1 129 ? 12.538  6.022   69.478  1.00 17.83 ? 129  PRO A CA  1 
ATOM   1065 C  C   . PRO A  1 129 ? 11.071  6.264   69.155  1.00 14.19 ? 129  PRO A C   1 
ATOM   1066 O  O   . PRO A  1 129 ? 10.183  5.575   69.674  1.00 20.55 ? 129  PRO A O   1 
ATOM   1067 C  CB  . PRO A  1 129 ? 13.104  5.071   68.434  1.00 16.65 ? 129  PRO A CB  1 
ATOM   1068 C  CG  . PRO A  1 129 ? 12.688  3.710   68.958  1.00 13.99 ? 129  PRO A CG  1 
ATOM   1069 C  CD  . PRO A  1 129 ? 12.850  3.827   70.479  1.00 19.46 ? 129  PRO A CD  1 
ATOM   1070 N  N   . LYS A  1 130 ? 10.838  7.252   68.297  1.00 15.47 ? 130  LYS A N   1 
ATOM   1071 C  CA  . LYS A  1 130 ? 9.618   7.328   67.510  1.00 16.23 ? 130  LYS A CA  1 
ATOM   1072 C  C   . LYS A  1 130 ? 10.027  6.869   66.113  1.00 16.99 ? 130  LYS A C   1 
ATOM   1073 O  O   . LYS A  1 130 ? 10.988  7.393   65.549  1.00 14.80 ? 130  LYS A O   1 
ATOM   1074 C  CB  . LYS A  1 130 ? 9.090   8.760   67.447  1.00 19.99 ? 130  LYS A CB  1 
ATOM   1075 C  CG  . LYS A  1 130 ? 8.450   9.252   68.744  1.00 26.80 ? 130  LYS A CG  1 
ATOM   1076 C  CD  . LYS A  1 130 ? 7.132   8.551   69.019  1.00 38.36 ? 130  LYS A CD  1 
ATOM   1077 C  CE  . LYS A  1 130 ? 6.513   9.029   70.331  1.00 44.69 ? 130  LYS A CE  1 
ATOM   1078 N  NZ  . LYS A  1 130 ? 6.533   10.514  70.439  1.00 39.40 ? 130  LYS A NZ  1 
ATOM   1079 N  N   . ILE A  1 131 ? 9.322   5.874   65.583  1.00 12.25 ? 131  ILE A N   1 
ATOM   1080 C  CA  . ILE A  1 131 ? 9.651   5.298   64.275  1.00 11.17 ? 131  ILE A CA  1 
ATOM   1081 C  C   . ILE A  1 131 ? 8.518   5.560   63.295  1.00 14.10 ? 131  ILE A C   1 
ATOM   1082 O  O   . ILE A  1 131 ? 7.370   5.213   63.561  1.00 14.34 ? 131  ILE A O   1 
ATOM   1083 C  CB  . ILE A  1 131 ? 9.882   3.798   64.393  1.00 9.38  ? 131  ILE A CB  1 
ATOM   1084 C  CG1 . ILE A  1 131 ? 10.978  3.529   65.433  1.00 13.51 ? 131  ILE A CG1 1 
ATOM   1085 C  CG2 . ILE A  1 131 ? 10.228  3.190   63.014  1.00 12.65 ? 131  ILE A CG2 1 
ATOM   1086 C  CD1 . ILE A  1 131 ? 11.258  2.064   65.672  1.00 11.90 ? 131  ILE A CD1 1 
ATOM   1087 N  N   . VAL A  1 132 ? 8.836   6.183   62.164  1.00 9.97  ? 132  VAL A N   1 
ATOM   1088 C  CA  . VAL A  1 132 ? 7.796   6.664   61.263  1.00 8.36  ? 132  VAL A CA  1 
ATOM   1089 C  C   . VAL A  1 132 ? 8.057   6.195   59.841  1.00 10.33 ? 132  VAL A C   1 
ATOM   1090 O  O   . VAL A  1 132 ? 9.191   6.262   59.360  1.00 12.09 ? 132  VAL A O   1 
ATOM   1091 C  CB  . VAL A  1 132 ? 7.733   8.208   61.262  1.00 10.48 ? 132  VAL A CB  1 
ATOM   1092 C  CG1 . VAL A  1 132 ? 6.756   8.717   60.193  1.00 14.27 ? 132  VAL A CG1 1 
ATOM   1093 C  CG2 . VAL A  1 132 ? 7.365   8.734   62.652  1.00 13.38 ? 132  VAL A CG2 1 
ATOM   1094 N  N   . LEU A  1 133 ? 7.010   5.694   59.197  1.00 10.93 ? 133  LEU A N   1 
ATOM   1095 C  CA  . LEU A  1 133 ? 7.015   5.428   57.764  1.00 8.65  ? 133  LEU A CA  1 
ATOM   1096 C  C   . LEU A  1 133 ? 6.163   6.489   57.104  1.00 11.39 ? 133  LEU A C   1 
ATOM   1097 O  O   . LEU A  1 133 ? 5.167   6.931   57.683  1.00 11.39 ? 133  LEU A O   1 
ATOM   1098 C  CB  . LEU A  1 133 ? 6.398   4.055   57.469  1.00 10.63 ? 133  LEU A CB  1 
ATOM   1099 C  CG  . LEU A  1 133 ? 7.082   2.795   58.003  1.00 11.73 ? 133  LEU A CG  1 
ATOM   1100 C  CD1 . LEU A  1 133 ? 6.330   1.548   57.534  1.00 9.76  ? 133  LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A  1 133 ? 8.535   2.728   57.572  1.00 12.34 ? 133  LEU A CD2 1 
ATOM   1102 N  N   . GLY A  1 134 ? 6.546   6.914   55.901  1.00 9.66  ? 134  GLY A N   1 
ATOM   1103 C  CA  . GLY A  1 134 ? 5.722   7.855   55.157  1.00 10.72 ? 134  GLY A CA  1 
ATOM   1104 C  C   . GLY A  1 134 ? 6.207   9.291   55.211  1.00 10.93 ? 134  GLY A C   1 
ATOM   1105 O  O   . GLY A  1 134 ? 5.932   10.061  54.307  1.00 10.93 ? 134  GLY A O   1 
ATOM   1106 N  N   . GLN A  1 135 ? 6.908   9.648   56.284  1.00 11.66 ? 135  GLN A N   1 
ATOM   1107 C  CA  . GLN A  1 135 ? 7.446   10.998  56.438  1.00 9.78  ? 135  GLN A CA  1 
ATOM   1108 C  C   . GLN A  1 135 ? 8.822   10.951  57.087  1.00 11.79 ? 135  GLN A C   1 
ATOM   1109 O  O   . GLN A  1 135 ? 9.174   9.989   57.763  1.00 13.93 ? 135  GLN A O   1 
ATOM   1110 C  CB  . GLN A  1 135 ? 6.513   11.864  57.308  1.00 8.27  ? 135  GLN A CB  1 
ATOM   1111 C  CG  . GLN A  1 135 ? 5.055   11.961  56.826  1.00 10.54 ? 135  GLN A CG  1 
ATOM   1112 C  CD  . GLN A  1 135 ? 4.888   12.873  55.626  1.00 13.32 ? 135  GLN A CD  1 
ATOM   1113 O  OE1 . GLN A  1 135 ? 5.716   13.751  55.372  1.00 13.29 ? 135  GLN A OE1 1 
ATOM   1114 N  NE2 . GLN A  1 135 ? 3.813   12.667  54.874  1.00 10.75 ? 135  GLN A NE2 1 
ATOM   1115 N  N   . GLU A  1 136 ? 9.585   12.021  56.896  1.00 11.33 ? 136  GLU A N   1 
ATOM   1116 C  CA  . GLU A  1 136 ? 10.890  12.158  57.509  1.00 8.64  ? 136  GLU A CA  1 
ATOM   1117 C  C   . GLU A  1 136 ? 10.710  13.055  58.739  1.00 14.83 ? 136  GLU A C   1 
ATOM   1118 O  O   . GLU A  1 136 ? 10.201  14.167  58.616  1.00 16.25 ? 136  GLU A O   1 
ATOM   1119 C  CB  . GLU A  1 136 ? 11.837  12.816  56.502  1.00 10.65 ? 136  GLU A CB  1 
ATOM   1120 C  CG  . GLU A  1 136 ? 13.309  12.491  56.706  1.00 12.31 ? 136  GLU A CG  1 
ATOM   1121 C  CD  . GLU A  1 136 ? 13.908  13.269  57.839  1.00 17.05 ? 136  GLU A CD  1 
ATOM   1122 O  OE1 . GLU A  1 136 ? 13.655  14.486  57.901  1.00 16.68 ? 136  GLU A OE1 1 
ATOM   1123 O  OE2 . GLU A  1 136 ? 14.618  12.688  58.673  1.00 11.49 ? 136  GLU A OE2 1 
ATOM   1124 N  N   . GLN A  1 137 ? 11.103  12.574  59.912  1.00 11.21 ? 137  GLN A N   1 
ATOM   1125 C  CA  . GLN A  1 137 ? 10.972  13.372  61.142  1.00 13.87 ? 137  GLN A CA  1 
ATOM   1126 C  C   . GLN A  1 137 ? 12.086  14.390  61.256  1.00 18.46 ? 137  GLN A C   1 
ATOM   1127 O  O   . GLN A  1 137 ? 13.234  14.062  61.015  1.00 15.22 ? 137  GLN A O   1 
ATOM   1128 C  CB  . GLN A  1 137 ? 11.045  12.479  62.379  1.00 12.25 ? 137  GLN A CB  1 
ATOM   1129 C  CG  . GLN A  1 137 ? 9.905   11.504  62.548  1.00 14.43 ? 137  GLN A CG  1 
ATOM   1130 C  CD  . GLN A  1 137 ? 10.160  10.559  63.694  1.00 16.81 ? 137  GLN A CD  1 
ATOM   1131 O  OE1 . GLN A  1 137 ? 9.846   10.861  64.851  1.00 17.09 ? 137  GLN A OE1 1 
ATOM   1132 N  NE2 . GLN A  1 137 ? 10.749  9.404   63.386  1.00 13.99 ? 137  GLN A NE2 1 
ATOM   1133 N  N   . ASP A  1 138 ? 11.750  15.617  61.645  1.00 16.24 ? 138  ASP A N   1 
ATOM   1134 C  CA  . ASP A  1 138 ? 12.763  16.597  62.045  1.00 19.31 ? 138  ASP A CA  1 
ATOM   1135 C  C   . ASP A  1 138 ? 12.654  16.908  63.537  1.00 22.29 ? 138  ASP A C   1 
ATOM   1136 O  O   . ASP A  1 138 ? 13.494  17.620  64.104  1.00 21.55 ? 138  ASP A O   1 
ATOM   1137 C  CB  . ASP A  1 138 ? 12.650  17.881  61.225  1.00 14.34 ? 138  ASP A CB  1 
ATOM   1138 C  CG  . ASP A  1 138 ? 13.373  17.786  59.911  1.00 18.14 ? 138  ASP A CG  1 
ATOM   1139 O  OD1 . ASP A  1 138 ? 14.174  16.840  59.757  1.00 16.91 ? 138  ASP A OD1 1 
ATOM   1140 O  OD2 . ASP A  1 138 ? 13.153  18.640  59.027  1.00 16.34 ? 138  ASP A OD2 1 
ATOM   1141 N  N   . SER A  1 139 ? 11.617  16.370  64.164  1.00 18.94 ? 139  SER A N   1 
ATOM   1142 C  CA  . SER A  1 139 ? 11.479  16.450  65.611  1.00 22.69 ? 139  SER A CA  1 
ATOM   1143 C  C   . SER A  1 139 ? 11.190  15.061  66.163  1.00 24.21 ? 139  SER A C   1 
ATOM   1144 O  O   . SER A  1 139 ? 11.210  14.076  65.425  1.00 22.35 ? 139  SER A O   1 
ATOM   1145 C  CB  . SER A  1 139 ? 10.355  17.421  65.988  1.00 19.45 ? 139  SER A CB  1 
ATOM   1146 O  OG  . SER A  1 139 ? 9.087   16.887  65.637  1.00 20.42 ? 139  SER A OG  1 
ATOM   1147 N  N   . TYR A  1 140 ? 10.920  14.973  67.461  1.00 21.83 ? 140  TYR A N   1 
ATOM   1148 C  CA  . TYR A  1 140 ? 10.586  13.692  68.073  1.00 18.02 ? 140  TYR A CA  1 
ATOM   1149 C  C   . TYR A  1 140 ? 9.136   13.317  67.783  1.00 28.69 ? 140  TYR A C   1 
ATOM   1150 O  O   . TYR A  1 140 ? 8.245   13.571  68.596  1.00 26.34 ? 140  TYR A O   1 
ATOM   1151 C  CB  . TYR A  1 140 ? 10.844  13.735  69.584  1.00 24.10 ? 140  TYR A CB  1 
ATOM   1152 C  CG  . TYR A  1 140 ? 10.709  12.407  70.303  1.00 20.95 ? 140  TYR A CG  1 
ATOM   1153 C  CD1 . TYR A  1 140 ? 11.454  11.296  69.916  1.00 20.53 ? 140  TYR A CD1 1 
ATOM   1154 C  CD2 . TYR A  1 140 ? 9.860   12.273  71.394  1.00 26.44 ? 140  TYR A CD2 1 
ATOM   1155 C  CE1 . TYR A  1 140 ? 11.340  10.089  70.584  1.00 18.57 ? 140  TYR A CE1 1 
ATOM   1156 C  CE2 . TYR A  1 140 ? 9.742   11.072  72.073  1.00 23.73 ? 140  TYR A CE2 1 
ATOM   1157 C  CZ  . TYR A  1 140 ? 10.481  9.984   71.668  1.00 28.68 ? 140  TYR A CZ  1 
ATOM   1158 O  OH  . TYR A  1 140 ? 10.357  8.795   72.343  1.00 24.19 ? 140  TYR A OH  1 
ATOM   1159 N  N   . GLY A  1 141 ? 8.903   12.729  66.611  1.00 21.58 ? 141  GLY A N   1 
ATOM   1160 C  CA  . GLY A  1 141 ? 7.570   12.312  66.209  1.00 21.62 ? 141  GLY A CA  1 
ATOM   1161 C  C   . GLY A  1 141 ? 6.923   13.173  65.136  1.00 19.29 ? 141  GLY A C   1 
ATOM   1162 O  O   . GLY A  1 141 ? 5.876   12.810  64.605  1.00 28.72 ? 141  GLY A O   1 
ATOM   1163 N  N   . GLY A  1 142 ? 7.530   14.314  64.813  1.00 17.86 ? 142  GLY A N   1 
ATOM   1164 C  CA  . GLY A  1 142 ? 6.924   15.236  63.869  1.00 17.77 ? 142  GLY A CA  1 
ATOM   1165 C  C   . GLY A  1 142 ? 7.868   16.096  63.054  1.00 22.10 ? 142  GLY A C   1 
ATOM   1166 O  O   . GLY A  1 142 ? 8.947   15.650  62.650  1.00 19.69 ? 142  GLY A O   1 
ATOM   1167 N  N   . LYS A  1 143 ? 7.443   17.336  62.811  1.00 17.38 ? 143  LYS A N   1 
ATOM   1168 C  CA  . LYS A  1 143 ? 8.112   18.264  61.892  1.00 18.50 ? 143  LYS A CA  1 
ATOM   1169 C  C   . LYS A  1 143 ? 8.424   17.633  60.534  1.00 21.53 ? 143  LYS A C   1 
ATOM   1170 O  O   . LYS A  1 143 ? 9.569   17.644  60.069  1.00 19.71 ? 143  LYS A O   1 
ATOM   1171 C  CB  . LYS A  1 143 ? 9.365   18.878  62.516  1.00 21.83 ? 143  LYS A CB  1 
ATOM   1172 C  CG  . LYS A  1 143 ? 9.075   20.046  63.444  1.00 26.65 ? 143  LYS A CG  1 
ATOM   1173 C  CD  . LYS A  1 143 ? 10.353  20.567  64.074  1.00 39.64 ? 143  LYS A CD  1 
ATOM   1174 C  CE  . LYS A  1 143 ? 10.064  21.506  65.234  1.00 41.80 ? 143  LYS A CE  1 
ATOM   1175 N  NZ  . LYS A  1 143 ? 11.325  21.896  65.926  1.00 54.50 ? 143  LYS A NZ  1 
ATOM   1176 N  N   . PHE A  1 144 ? 7.381   17.104  59.906  1.00 15.24 ? 144  PHE A N   1 
ATOM   1177 C  CA  . PHE A  1 144 ? 7.490   16.464  58.601  1.00 16.27 ? 144  PHE A CA  1 
ATOM   1178 C  C   . PHE A  1 144 ? 7.715   17.487  57.490  1.00 17.60 ? 144  PHE A C   1 
ATOM   1179 O  O   . PHE A  1 144 ? 7.537   18.690  57.693  1.00 17.54 ? 144  PHE A O   1 
ATOM   1180 C  CB  . PHE A  1 144 ? 6.232   15.643  58.317  1.00 12.94 ? 144  PHE A CB  1 
ATOM   1181 C  CG  . PHE A  1 144 ? 5.923   14.621  59.375  1.00 16.55 ? 144  PHE A CG  1 
ATOM   1182 C  CD1 . PHE A  1 144 ? 6.937   13.905  59.988  1.00 17.05 ? 144  PHE A CD1 1 
ATOM   1183 C  CD2 . PHE A  1 144 ? 4.613   14.362  59.740  1.00 15.46 ? 144  PHE A CD2 1 
ATOM   1184 C  CE1 . PHE A  1 144 ? 6.652   12.954  60.957  1.00 16.32 ? 144  PHE A CE1 1 
ATOM   1185 C  CE2 . PHE A  1 144 ? 4.314   13.408  60.707  1.00 18.54 ? 144  PHE A CE2 1 
ATOM   1186 C  CZ  . PHE A  1 144 ? 5.335   12.702  61.317  1.00 16.99 ? 144  PHE A CZ  1 
ATOM   1187 N  N   . ASP A  1 145 ? 8.106   16.997  56.317  1.00 12.39 ? 145  ASP A N   1 
ATOM   1188 C  CA  . ASP A  1 145 ? 8.441   17.843  55.182  1.00 18.89 ? 145  ASP A CA  1 
ATOM   1189 C  C   . ASP A  1 145 ? 7.869   17.174  53.944  1.00 18.19 ? 145  ASP A C   1 
ATOM   1190 O  O   . ASP A  1 145 ? 8.275   16.068  53.584  1.00 15.08 ? 145  ASP A O   1 
ATOM   1191 C  CB  . ASP A  1 145 ? 9.962   17.988  55.087  1.00 16.14 ? 145  ASP A CB  1 
ATOM   1192 C  CG  . ASP A  1 145 ? 10.418  18.811  53.893  1.00 20.53 ? 145  ASP A CG  1 
ATOM   1193 O  OD1 . ASP A  1 145 ? 9.599   19.113  52.992  1.00 19.77 ? 145  ASP A OD1 1 
ATOM   1194 O  OD2 . ASP A  1 145 ? 11.623  19.148  53.857  1.00 19.66 ? 145  ASP A OD2 1 
ATOM   1195 N  N   . ARG A  1 146 ? 6.908   17.832  53.309  1.00 14.20 ? 146  ARG A N   1 
ATOM   1196 C  CA  . ARG A  1 146 ? 6.211   17.252  52.167  1.00 14.61 ? 146  ARG A CA  1 
ATOM   1197 C  C   . ARG A  1 146 ? 7.168   16.810  51.063  1.00 14.85 ? 146  ARG A C   1 
ATOM   1198 O  O   . ARG A  1 146 ? 6.894   15.840  50.348  1.00 15.52 ? 146  ARG A O   1 
ATOM   1199 C  CB  . ARG A  1 146 ? 5.184   18.254  51.619  1.00 25.65 ? 146  ARG A CB  1 
ATOM   1200 C  CG  . ARG A  1 146 ? 4.807   18.040  50.172  1.00 26.94 ? 146  ARG A CG  1 
ATOM   1201 C  CD  . ARG A  1 146 ? 3.882   19.149  49.670  1.00 33.02 ? 146  ARG A CD  1 
ATOM   1202 N  NE  . ARG A  1 146 ? 2.532   19.013  50.206  1.00 45.29 ? 146  ARG A NE  1 
ATOM   1203 C  CZ  . ARG A  1 146 ? 1.490   18.565  49.513  1.00 43.58 ? 146  ARG A CZ  1 
ATOM   1204 N  NH1 . ARG A  1 146 ? 1.633   18.214  48.238  1.00 33.65 ? 146  ARG A NH1 1 
ATOM   1205 N  NH2 . ARG A  1 146 ? 0.301   18.475  50.095  1.00 43.60 ? 146  ARG A NH2 1 
ATOM   1206 N  N   . SER A  1 147 ? 8.288   17.521  50.923  1.00 14.00 ? 147  SER A N   1 
ATOM   1207 C  CA  . SER A  1 147 ? 9.247   17.226  49.859  1.00 16.36 ? 147  SER A CA  1 
ATOM   1208 C  C   . SER A  1 147 ? 10.119  16.005  50.167  1.00 10.08 ? 147  SER A C   1 
ATOM   1209 O  O   . SER A  1 147 ? 10.937  15.605  49.338  1.00 15.62 ? 147  SER A O   1 
ATOM   1210 C  CB  . SER A  1 147 ? 10.140  18.442  49.566  1.00 16.61 ? 147  SER A CB  1 
ATOM   1211 O  OG  . SER A  1 147 ? 11.017  18.706  50.648  1.00 21.91 ? 147  SER A OG  1 
ATOM   1212 N  N   . GLN A  1 148 ? 9.930   15.415  51.349  1.00 11.12 ? 148  GLN A N   1 
ATOM   1213 C  CA  . GLN A  1 148 ? 10.650  14.207  51.735  1.00 14.58 ? 148  GLN A CA  1 
ATOM   1214 C  C   . GLN A  1 148 ? 9.686   13.053  52.005  1.00 10.23 ? 148  GLN A C   1 
ATOM   1215 O  O   . GLN A  1 148 ? 10.105  11.960  52.403  1.00 12.62 ? 148  GLN A O   1 
ATOM   1216 C  CB  . GLN A  1 148 ? 11.494  14.479  52.980  1.00 11.82 ? 148  GLN A CB  1 
ATOM   1217 C  CG  . GLN A  1 148 ? 12.522  15.572  52.778  1.00 13.25 ? 148  GLN A CG  1 
ATOM   1218 C  CD  . GLN A  1 148 ? 13.298  15.860  54.039  1.00 14.70 ? 148  GLN A CD  1 
ATOM   1219 O  OE1 . GLN A  1 148 ? 12.740  15.850  55.129  1.00 15.53 ? 148  GLN A OE1 1 
ATOM   1220 N  NE2 . GLN A  1 148 ? 14.594  16.122  53.898  1.00 21.49 ? 148  GLN A NE2 1 
ATOM   1221 N  N   . SER A  1 149 ? 8.394   13.308  51.798  1.00 9.44  ? 149  SER A N   1 
ATOM   1222 C  CA  . SER A  1 149 ? 7.359   12.298  52.029  1.00 10.67 ? 149  SER A CA  1 
ATOM   1223 C  C   . SER A  1 149 ? 7.491   11.111  51.080  1.00 10.24 ? 149  SER A C   1 
ATOM   1224 O  O   . SER A  1 149 ? 7.876   11.258  49.916  1.00 10.22 ? 149  SER A O   1 
ATOM   1225 C  CB  . SER A  1 149 ? 5.952   12.904  51.919  1.00 13.09 ? 149  SER A CB  1 
ATOM   1226 O  OG  . SER A  1 149 ? 5.691   13.385  50.607  1.00 13.39 ? 149  SER A OG  1 
ATOM   1227 N  N   . PHE A  1 150 ? 7.184   9.925   51.594  1.00 8.78  ? 150  PHE A N   1 
ATOM   1228 C  CA  . PHE A  1 150 ? 7.205   8.730   50.766  1.00 13.31 ? 150  PHE A CA  1 
ATOM   1229 C  C   . PHE A  1 150 ? 5.827   8.498   50.179  1.00 11.98 ? 150  PHE A C   1 
ATOM   1230 O  O   . PHE A  1 150 ? 4.840   8.391   50.910  1.00 13.09 ? 150  PHE A O   1 
ATOM   1231 C  CB  . PHE A  1 150 ? 7.618   7.508   51.583  1.00 9.86  ? 150  PHE A CB  1 
ATOM   1232 C  CG  . PHE A  1 150 ? 7.543   6.224   50.806  1.00 8.92  ? 150  PHE A CG  1 
ATOM   1233 C  CD1 . PHE A  1 150 ? 8.580   5.855   49.972  1.00 10.24 ? 150  PHE A CD1 1 
ATOM   1234 C  CD2 . PHE A  1 150 ? 6.424   5.405   50.888  1.00 11.61 ? 150  PHE A CD2 1 
ATOM   1235 C  CE1 . PHE A  1 150 ? 8.518   4.677   49.240  1.00 7.84  ? 150  PHE A CE1 1 
ATOM   1236 C  CE2 . PHE A  1 150 ? 6.350   4.222   50.152  1.00 9.27  ? 150  PHE A CE2 1 
ATOM   1237 C  CZ  . PHE A  1 150 ? 7.403   3.860   49.329  1.00 10.98 ? 150  PHE A CZ  1 
ATOM   1238 N  N   . VAL A  1 151 ? 5.760   8.441   48.854  1.00 9.53  ? 151  VAL A N   1 
ATOM   1239 C  CA  . VAL A  1 151 ? 4.530   8.112   48.164  1.00 9.80  ? 151  VAL A CA  1 
ATOM   1240 C  C   . VAL A  1 151 ? 4.738   6.778   47.477  1.00 10.26 ? 151  VAL A C   1 
ATOM   1241 O  O   . VAL A  1 151 ? 5.712   6.601   46.733  1.00 11.12 ? 151  VAL A O   1 
ATOM   1242 C  CB  . VAL A  1 151 ? 4.171   9.177   47.099  1.00 8.71  ? 151  VAL A CB  1 
ATOM   1243 C  CG1 . VAL A  1 151 ? 2.814   8.843   46.471  1.00 12.53 ? 151  VAL A CG1 1 
ATOM   1244 C  CG2 . VAL A  1 151 ? 4.137   10.561  47.740  1.00 11.46 ? 151  VAL A CG2 1 
ATOM   1245 N  N   . GLY A  1 152 ? 3.841   5.837   47.735  1.00 9.15  ? 152  GLY A N   1 
ATOM   1246 C  CA  . GLY A  1 152 ? 3.992   4.504   47.185  1.00 8.21  ? 152  GLY A CA  1 
ATOM   1247 C  C   . GLY A  1 152 ? 3.673   3.452   48.228  1.00 7.59  ? 152  GLY A C   1 
ATOM   1248 O  O   . GLY A  1 152 ? 2.886   3.694   49.141  1.00 8.70  ? 152  GLY A O   1 
ATOM   1249 N  N   . GLU A  1 153 ? 4.290   2.283   48.101  1.00 9.54  ? 153  GLU A N   1 
ATOM   1250 C  CA  . GLU A  1 153 ? 3.905   1.130   48.906  1.00 9.69  ? 153  GLU A CA  1 
ATOM   1251 C  C   . GLU A  1 153 ? 5.092   0.548   49.646  1.00 8.53  ? 153  GLU A C   1 
ATOM   1252 O  O   . GLU A  1 153 ? 6.184   0.456   49.094  1.00 7.96  ? 153  GLU A O   1 
ATOM   1253 C  CB  . GLU A  1 153 ? 3.282   0.063   48.001  1.00 10.18 ? 153  GLU A CB  1 
ATOM   1254 C  CG  . GLU A  1 153 ? 2.134   0.625   47.155  1.00 8.92  ? 153  GLU A CG  1 
ATOM   1255 C  CD  . GLU A  1 153 ? 1.512   -0.414  46.255  1.00 11.42 ? 153  GLU A CD  1 
ATOM   1256 O  OE1 . GLU A  1 153 ? 1.316   -1.560  46.706  1.00 11.01 ? 153  GLU A OE1 1 
ATOM   1257 O  OE2 . GLU A  1 153 ? 1.219   -0.091  45.090  1.00 12.06 ? 153  GLU A OE2 1 
ATOM   1258 N  N   . ILE A  1 154 ? 4.890   0.178   50.907  1.00 7.32  ? 154  ILE A N   1 
ATOM   1259 C  CA  . ILE A  1 154 ? 5.954   -0.480  51.679  1.00 6.21  ? 154  ILE A CA  1 
ATOM   1260 C  C   . ILE A  1 154 ? 5.384   -1.721  52.327  1.00 9.33  ? 154  ILE A C   1 
ATOM   1261 O  O   . ILE A  1 154 ? 4.274   -1.694  52.863  1.00 10.48 ? 154  ILE A O   1 
ATOM   1262 C  CB  . ILE A  1 154 ? 6.485   0.437   52.800  1.00 10.83 ? 154  ILE A CB  1 
ATOM   1263 C  CG1 . ILE A  1 154 ? 7.255   1.612   52.203  1.00 12.55 ? 154  ILE A CG1 1 
ATOM   1264 C  CG2 . ILE A  1 154 ? 7.362   -0.352  53.795  1.00 11.25 ? 154  ILE A CG2 1 
ATOM   1265 C  CD1 . ILE A  1 154 ? 7.638   2.669   53.224  1.00 18.84 ? 154  ILE A CD1 1 
ATOM   1266 N  N   . GLY A  1 155 ? 6.127   -2.818  52.264  1.00 8.57  ? 155  GLY A N   1 
ATOM   1267 C  CA  . GLY A  1 155 ? 5.705   -4.026  52.953  1.00 9.68  ? 155  GLY A CA  1 
ATOM   1268 C  C   . GLY A  1 155 ? 6.889   -4.841  53.428  1.00 12.71 ? 155  GLY A C   1 
ATOM   1269 O  O   . GLY A  1 155 ? 8.043   -4.439  53.252  1.00 9.01  ? 155  GLY A O   1 
ATOM   1270 N  N   . ASP A  1 156 ? 6.591   -5.985  54.041  1.00 10.18 ? 156  ASP A N   1 
ATOM   1271 C  CA  . ASP A  1 156 ? 7.609   -6.944  54.456  1.00 10.56 ? 156  ASP A CA  1 
ATOM   1272 C  C   . ASP A  1 156 ? 8.734   -6.297  55.248  1.00 8.95  ? 156  ASP A C   1 
ATOM   1273 O  O   . ASP A  1 156 ? 9.910   -6.551  54.986  1.00 9.06  ? 156  ASP A O   1 
ATOM   1274 C  CB  . ASP A  1 156 ? 8.179   -7.663  53.243  1.00 9.09  ? 156  ASP A CB  1 
ATOM   1275 C  CG  . ASP A  1 156 ? 7.167   -8.542  52.564  1.00 17.73 ? 156  ASP A CG  1 
ATOM   1276 O  OD1 . ASP A  1 156 ? 6.132   -8.844  53.192  1.00 17.42 ? 156  ASP A OD1 1 
ATOM   1277 O  OD2 . ASP A  1 156 ? 7.411   -8.934  51.408  1.00 15.04 ? 156  ASP A OD2 1 
ATOM   1278 N  N   . LEU A  1 157 ? 8.370   -5.484  56.232  1.00 9.75  ? 157  LEU A N   1 
ATOM   1279 C  CA  . LEU A  1 157 ? 9.367   -4.776  57.026  1.00 7.13  ? 157  LEU A CA  1 
ATOM   1280 C  C   . LEU A  1 157 ? 9.715   -5.587  58.267  1.00 12.82 ? 157  LEU A C   1 
ATOM   1281 O  O   . LEU A  1 157 ? 8.829   -6.020  58.996  1.00 10.54 ? 157  LEU A O   1 
ATOM   1282 C  CB  . LEU A  1 157 ? 8.883   -3.368  57.383  1.00 9.09  ? 157  LEU A CB  1 
ATOM   1283 C  CG  . LEU A  1 157 ? 9.913   -2.497  58.096  1.00 7.62  ? 157  LEU A CG  1 
ATOM   1284 C  CD1 . LEU A  1 157 ? 9.727   -1.016  57.773  1.00 12.10 ? 157  LEU A CD1 1 
ATOM   1285 C  CD2 . LEU A  1 157 ? 9.846   -2.738  59.601  1.00 10.34 ? 157  LEU A CD2 1 
ATOM   1286 N  N   . TYR A  1 158 ? 11.010  -5.814  58.469  1.00 8.11  ? 158  TYR A N   1 
ATOM   1287 C  CA  . TYR A  1 158 ? 11.522  -6.522  59.634  1.00 7.61  ? 158  TYR A CA  1 
ATOM   1288 C  C   . TYR A  1 158 ? 12.735  -5.803  60.174  1.00 9.46  ? 158  TYR A C   1 
ATOM   1289 O  O   . TYR A  1 158 ? 13.541  -5.274  59.411  1.00 9.72  ? 158  TYR A O   1 
ATOM   1290 C  CB  . TYR A  1 158 ? 11.928  -7.945  59.246  1.00 7.13  ? 158  TYR A CB  1 
ATOM   1291 C  CG  . TYR A  1 158 ? 10.771  -8.749  58.705  1.00 8.66  ? 158  TYR A CG  1 
ATOM   1292 C  CD1 . TYR A  1 158 ? 10.439  -8.716  57.358  1.00 7.62  ? 158  TYR A CD1 1 
ATOM   1293 C  CD2 . TYR A  1 158 ? 9.974   -9.489  59.557  1.00 10.39 ? 158  TYR A CD2 1 
ATOM   1294 C  CE1 . TYR A  1 158 ? 9.352   -9.445  56.867  1.00 10.68 ? 158  TYR A CE1 1 
ATOM   1295 C  CE2 . TYR A  1 158 ? 8.896   -10.204 59.086  1.00 13.56 ? 158  TYR A CE2 1 
ATOM   1296 C  CZ  . TYR A  1 158 ? 8.584   -10.176 57.748  1.00 13.46 ? 158  TYR A CZ  1 
ATOM   1297 O  OH  . TYR A  1 158 ? 7.510   -10.902 57.300  1.00 14.95 ? 158  TYR A OH  1 
ATOM   1298 N  N   . MET A  1 159 ? 12.885  -5.801  61.495  1.00 9.47  ? 159  MET A N   1 
ATOM   1299 C  CA  . MET A  1 159 ? 14.083  -5.251  62.103  1.00 10.32 ? 159  MET A CA  1 
ATOM   1300 C  C   . MET A  1 159 ? 14.564  -6.180  63.219  1.00 9.21  ? 159  MET A C   1 
ATOM   1301 O  O   . MET A  1 159 ? 13.781  -6.567  64.097  1.00 11.71 ? 159  MET A O   1 
ATOM   1302 C  CB  . MET A  1 159 ? 13.811  -3.854  62.639  1.00 11.04 ? 159  MET A CB  1 
ATOM   1303 C  CG  . MET A  1 159 ? 15.067  -3.120  63.087  1.00 10.14 ? 159  MET A CG  1 
ATOM   1304 S  SD  . MET A  1 159 ? 14.701  -1.410  63.516  1.00 12.80 ? 159  MET A SD  1 
ATOM   1305 C  CE  . MET A  1 159 ? 16.337  -0.805  63.965  1.00 15.07 ? 159  MET A CE  1 
ATOM   1306 N  N   . TRP A  1 160 ? 15.843  -6.537  63.151  1.00 7.72  ? 160  TRP A N   1 
ATOM   1307 C  CA  . TRP A  1 160 ? 16.507  -7.435  64.102  1.00 9.71  ? 160  TRP A CA  1 
ATOM   1308 C  C   . TRP A  1 160 ? 17.569  -6.670  64.887  1.00 12.16 ? 160  TRP A C   1 
ATOM   1309 O  O   . TRP A  1 160 ? 18.191  -5.748  64.360  1.00 11.57 ? 160  TRP A O   1 
ATOM   1310 C  CB  . TRP A  1 160 ? 17.248  -8.545  63.344  1.00 11.08 ? 160  TRP A CB  1 
ATOM   1311 C  CG  . TRP A  1 160 ? 16.409  -9.463  62.525  1.00 11.86 ? 160  TRP A CG  1 
ATOM   1312 C  CD1 . TRP A  1 160 ? 15.945  -10.689 62.894  1.00 10.11 ? 160  TRP A CD1 1 
ATOM   1313 C  CD2 . TRP A  1 160 ? 15.975  -9.259  61.172  1.00 9.13  ? 160  TRP A CD2 1 
ATOM   1314 N  NE1 . TRP A  1 160 ? 15.239  -11.257 61.867  1.00 10.32 ? 160  TRP A NE1 1 
ATOM   1315 C  CE2 . TRP A  1 160 ? 15.244  -10.403 60.794  1.00 10.39 ? 160  TRP A CE2 1 
ATOM   1316 C  CE3 . TRP A  1 160 ? 16.130  -8.220  60.247  1.00 9.48  ? 160  TRP A CE3 1 
ATOM   1317 C  CZ2 . TRP A  1 160 ? 14.670  -10.538 59.535  1.00 8.71  ? 160  TRP A CZ2 1 
ATOM   1318 C  CZ3 . TRP A  1 160 ? 15.561  -8.356  58.993  1.00 9.33  ? 160  TRP A CZ3 1 
ATOM   1319 C  CH2 . TRP A  1 160 ? 14.838  -9.507  58.647  1.00 10.62 ? 160  TRP A CH2 1 
ATOM   1320 N  N   . ASP A  1 161 ? 17.813  -7.075  66.132  1.00 10.58 ? 161  ASP A N   1 
ATOM   1321 C  CA  . ASP A  1 161 ? 18.868  -6.447  66.928  1.00 13.07 ? 161  ASP A CA  1 
ATOM   1322 C  C   . ASP A  1 161 ? 20.245  -7.094  66.718  1.00 14.50 ? 161  ASP A C   1 
ATOM   1323 O  O   . ASP A  1 161 ? 21.098  -7.080  67.614  1.00 12.45 ? 161  ASP A O   1 
ATOM   1324 C  CB  . ASP A  1 161 ? 18.500  -6.428  68.416  1.00 13.12 ? 161  ASP A CB  1 
ATOM   1325 C  CG  . ASP A  1 161 ? 18.615  -7.790  69.073  1.00 17.44 ? 161  ASP A CG  1 
ATOM   1326 O  OD1 . ASP A  1 161 ? 18.714  -8.813  68.367  1.00 16.84 ? 161  ASP A OD1 1 
ATOM   1327 O  OD2 . ASP A  1 161 ? 18.603  -7.826  70.320  1.00 22.57 ? 161  ASP A OD2 1 
ATOM   1328 N  N   . SER A  1 162 ? 20.462  -7.639  65.525  1.00 11.88 ? 162  SER A N   1 
ATOM   1329 C  CA  . SER A  1 162 ? 21.736  -8.250  65.187  1.00 13.40 ? 162  SER A CA  1 
ATOM   1330 C  C   . SER A  1 162 ? 22.055  -7.982  63.723  1.00 11.68 ? 162  SER A C   1 
ATOM   1331 O  O   . SER A  1 162 ? 21.188  -7.520  62.973  1.00 10.99 ? 162  SER A O   1 
ATOM   1332 C  CB  . SER A  1 162 ? 21.698  -9.759  65.453  1.00 16.40 ? 162  SER A CB  1 
ATOM   1333 O  OG  . SER A  1 162 ? 20.730  -10.413 64.638  1.00 15.30 ? 162  SER A OG  1 
ATOM   1334 N  N   . VAL A  1 163 ? 23.301  -8.254  63.339  1.00 10.75 ? 163  VAL A N   1 
ATOM   1335 C  CA  . VAL A  1 163 ? 23.740  -8.139  61.949  1.00 8.77  ? 163  VAL A CA  1 
ATOM   1336 C  C   . VAL A  1 163 ? 23.517  -9.463  61.223  1.00 10.36 ? 163  VAL A C   1 
ATOM   1337 O  O   . VAL A  1 163 ? 24.177  -10.461 61.520  1.00 12.74 ? 163  VAL A O   1 
ATOM   1338 C  CB  . VAL A  1 163 ? 25.231  -7.788  61.872  1.00 10.36 ? 163  VAL A CB  1 
ATOM   1339 C  CG1 . VAL A  1 163 ? 25.708  -7.810  60.420  1.00 12.38 ? 163  VAL A CG1 1 
ATOM   1340 C  CG2 . VAL A  1 163 ? 25.481  -6.421  62.516  1.00 15.91 ? 163  VAL A CG2 1 
ATOM   1341 N  N   . LEU A  1 164 ? 22.599  -9.470  60.263  1.00 11.09 ? 164  LEU A N   1 
ATOM   1342 C  CA  . LEU A  1 164 ? 22.271  -10.692 59.538  1.00 13.39 ? 164  LEU A CA  1 
ATOM   1343 C  C   . LEU A  1 164 ? 23.370  -11.108 58.565  1.00 11.10 ? 164  LEU A C   1 
ATOM   1344 O  O   . LEU A  1 164 ? 23.928  -10.276 57.851  1.00 11.95 ? 164  LEU A O   1 
ATOM   1345 C  CB  . LEU A  1 164 ? 20.965  -10.500 58.771  1.00 9.46  ? 164  LEU A CB  1 
ATOM   1346 C  CG  . LEU A  1 164 ? 19.663  -10.987 59.409  1.00 22.64 ? 164  LEU A CG  1 
ATOM   1347 C  CD1 . LEU A  1 164 ? 19.598  -10.697 60.893  1.00 24.14 ? 164  LEU A CD1 1 
ATOM   1348 C  CD2 . LEU A  1 164 ? 18.484  -10.392 58.655  1.00 13.86 ? 164  LEU A CD2 1 
ATOM   1349 N  N   . PRO A  1 165 ? 23.676  -12.412 58.524  1.00 10.27 ? 165  PRO A N   1 
ATOM   1350 C  CA  . PRO A  1 165 ? 24.572  -12.933 57.492  1.00 13.45 ? 165  PRO A CA  1 
ATOM   1351 C  C   . PRO A  1 165 ? 23.851  -12.989 56.152  1.00 11.89 ? 165  PRO A C   1 
ATOM   1352 O  O   . PRO A  1 165 ? 22.613  -12.967 56.100  1.00 10.87 ? 165  PRO A O   1 
ATOM   1353 C  CB  . PRO A  1 165 ? 24.870  -14.356 57.973  1.00 16.47 ? 165  PRO A CB  1 
ATOM   1354 C  CG  . PRO A  1 165 ? 23.662  -14.749 58.751  1.00 14.63 ? 165  PRO A CG  1 
ATOM   1355 C  CD  . PRO A  1 165 ? 23.169  -13.471 59.418  1.00 13.66 ? 165  PRO A CD  1 
ATOM   1356 N  N   . PRO A  1 166 ? 24.617  -13.071 55.062  1.00 12.11 ? 166  PRO A N   1 
ATOM   1357 C  CA  . PRO A  1 166 ? 24.030  -13.065 53.722  1.00 9.65  ? 166  PRO A CA  1 
ATOM   1358 C  C   . PRO A  1 166 ? 22.897  -14.079 53.554  1.00 10.73 ? 166  PRO A C   1 
ATOM   1359 O  O   . PRO A  1 166 ? 21.907  -13.760 52.913  1.00 12.11 ? 166  PRO A O   1 
ATOM   1360 C  CB  . PRO A  1 166 ? 25.214  -13.427 52.829  1.00 12.92 ? 166  PRO A CB  1 
ATOM   1361 C  CG  . PRO A  1 166 ? 26.384  -12.856 53.560  1.00 10.51 ? 166  PRO A CG  1 
ATOM   1362 C  CD  . PRO A  1 166 ? 26.090  -13.068 55.022  1.00 14.98 ? 166  PRO A CD  1 
ATOM   1363 N  N   . GLU A  1 167 ? 23.044  -15.277 54.108  1.00 11.52 ? 167  GLU A N   1 
ATOM   1364 C  CA  . GLU A  1 167 ? 22.006  -16.290 53.933  1.00 15.35 ? 167  GLU A CA  1 
ATOM   1365 C  C   . GLU A  1 167 ? 20.657  -15.810 54.471  1.00 10.61 ? 167  GLU A C   1 
ATOM   1366 O  O   . GLU A  1 167 ? 19.617  -16.062 53.857  1.00 12.85 ? 167  GLU A O   1 
ATOM   1367 C  CB  . GLU A  1 167 ? 22.418  -17.618 54.582  1.00 15.94 ? 167  GLU A CB  1 
ATOM   1368 C  CG  . GLU A  1 167 ? 22.887  -17.494 56.026  1.00 26.36 ? 167  GLU A CG  1 
ATOM   1369 C  CD  . GLU A  1 167 ? 24.414  -17.403 56.183  1.00 32.53 ? 167  GLU A CD  1 
ATOM   1370 O  OE1 . GLU A  1 167 ? 25.097  -16.704 55.388  1.00 18.63 ? 167  GLU A OE1 1 
ATOM   1371 O  OE2 . GLU A  1 167 ? 24.935  -18.033 57.131  1.00 32.09 ? 167  GLU A OE2 1 
ATOM   1372 N  N   . ASN A  1 168 ? 20.678  -15.115 55.609  1.00 10.79 ? 168  ASN A N   1 
ATOM   1373 C  CA  . ASN A  1 168 ? 19.446  -14.603 56.211  1.00 10.48 ? 168  ASN A CA  1 
ATOM   1374 C  C   . ASN A  1 168 ? 18.871  -13.408 55.452  1.00 12.36 ? 168  ASN A C   1 
ATOM   1375 O  O   . ASN A  1 168 ? 17.662  -13.219 55.414  1.00 9.76  ? 168  ASN A O   1 
ATOM   1376 C  CB  . ASN A  1 168 ? 19.657  -14.230 57.676  1.00 10.03 ? 168  ASN A CB  1 
ATOM   1377 C  CG  . ASN A  1 168 ? 19.951  -15.434 58.552  1.00 16.95 ? 168  ASN A CG  1 
ATOM   1378 O  OD1 . ASN A  1 168 ? 19.727  -16.589 58.163  1.00 20.35 ? 168  ASN A OD1 1 
ATOM   1379 N  ND2 . ASN A  1 168 ? 20.443  -15.167 59.749  1.00 12.93 ? 168  ASN A ND2 1 
ATOM   1380 N  N   A ILE A  1 169 ? 19.746  -12.590 54.875  0.58 11.03 ? 169  ILE A N   1 
ATOM   1381 N  N   B ILE A  1 169 ? 19.746  -12.613 54.849  0.42 11.05 ? 169  ILE A N   1 
ATOM   1382 C  CA  A ILE A  1 169 ? 19.304  -11.511 53.998  0.58 10.66 ? 169  ILE A CA  1 
ATOM   1383 C  CA  B ILE A  1 169 ? 19.306  -11.505 54.013  0.42 10.67 ? 169  ILE A CA  1 
ATOM   1384 C  C   A ILE A  1 169 ? 18.581  -12.097 52.793  0.58 11.77 ? 169  ILE A C   1 
ATOM   1385 C  C   B ILE A  1 169 ? 18.646  -12.019 52.734  0.42 11.77 ? 169  ILE A C   1 
ATOM   1386 O  O   A ILE A  1 169 ? 17.474  -11.686 52.452  0.58 10.93 ? 169  ILE A O   1 
ATOM   1387 O  O   B ILE A  1 169 ? 17.631  -11.481 52.293  0.42 11.12 ? 169  ILE A O   1 
ATOM   1388 C  CB  A ILE A  1 169 ? 20.491  -10.669 53.495  0.58 10.50 ? 169  ILE A CB  1 
ATOM   1389 C  CB  B ILE A  1 169 ? 20.477  -10.562 53.687  0.42 10.52 ? 169  ILE A CB  1 
ATOM   1390 C  CG1 A ILE A  1 169 ? 21.181  -9.972  54.670  0.58 12.25 ? 169  ILE A CG1 1 
ATOM   1391 C  CG1 B ILE A  1 169 ? 20.987  -9.926  54.982  0.42 11.99 ? 169  ILE A CG1 1 
ATOM   1392 C  CG2 A ILE A  1 169 ? 20.027  -9.682  52.426  0.58 9.67  ? 169  ILE A CG2 1 
ATOM   1393 C  CG2 B ILE A  1 169 ? 20.048  -9.511  52.672  0.42 10.19 ? 169  ILE A CG2 1 
ATOM   1394 C  CD1 A ILE A  1 169 ? 20.383  -8.834  55.277  0.58 13.49 ? 169  ILE A CD1 1 
ATOM   1395 C  CD1 B ILE A  1 169 ? 22.314  -9.222  54.852  0.42 11.22 ? 169  ILE A CD1 1 
ATOM   1396 N  N   . LEU A  1 170 ? 19.212  -13.070 52.147  1.00 10.58 ? 170  LEU A N   1 
ATOM   1397 C  CA  . LEU A  1 170 ? 18.617  -13.676 50.965  1.00 11.29 ? 170  LEU A CA  1 
ATOM   1398 C  C   . LEU A  1 170 ? 17.269  -14.326 51.309  1.00 10.53 ? 170  LEU A C   1 
ATOM   1399 O  O   . LEU A  1 170 ? 16.321  -14.245 50.531  1.00 12.24 ? 170  LEU A O   1 
ATOM   1400 C  CB  . LEU A  1 170 ? 19.568  -14.678 50.311  1.00 14.02 ? 170  LEU A CB  1 
ATOM   1401 C  CG  . LEU A  1 170 ? 20.823  -14.049 49.708  1.00 20.13 ? 170  LEU A CG  1 
ATOM   1402 C  CD1 . LEU A  1 170 ? 21.545  -15.061 48.823  1.00 27.23 ? 170  LEU A CD1 1 
ATOM   1403 C  CD2 . LEU A  1 170 ? 20.473  -12.801 48.920  1.00 20.91 ? 170  LEU A CD2 1 
ATOM   1404 N  N   . SER A  1 171 ? 17.168  -14.937 52.483  1.00 12.61 ? 171  SER A N   1 
ATOM   1405 C  CA  . SER A  1 171 ? 15.881  -15.477 52.928  1.00 11.25 ? 171  SER A CA  1 
ATOM   1406 C  C   . SER A  1 171 ? 14.809  -14.389 52.991  1.00 12.18 ? 171  SER A C   1 
ATOM   1407 O  O   . SER A  1 171 ? 13.690  -14.587 52.522  1.00 14.15 ? 171  SER A O   1 
ATOM   1408 C  CB  . SER A  1 171 ? 16.008  -16.182 54.283  1.00 14.99 ? 171  SER A CB  1 
ATOM   1409 O  OG  . SER A  1 171 ? 16.721  -17.397 54.133  1.00 18.55 ? 171  SER A OG  1 
ATOM   1410 N  N   . ALA A  1 172 ? 15.150  -13.228 53.547  1.00 11.90 ? 172  ALA A N   1 
ATOM   1411 C  CA  . ALA A  1 172 ? 14.173  -12.150 53.618  1.00 11.78 ? 172  ALA A CA  1 
ATOM   1412 C  C   . ALA A  1 172 ? 13.774  -11.723 52.201  1.00 9.53  ? 172  ALA A C   1 
ATOM   1413 O  O   . ALA A  1 172 ? 12.588  -11.527 51.907  1.00 11.74 ? 172  ALA A O   1 
ATOM   1414 C  CB  . ALA A  1 172 ? 14.715  -10.964 54.426  1.00 12.45 ? 172  ALA A CB  1 
ATOM   1415 N  N   . TYR A  1 173 ? 14.767  -11.592 51.326  1.00 10.72 ? 173  TYR A N   1 
ATOM   1416 C  CA  . TYR A  1 173 ? 14.518  -11.160 49.956  1.00 9.17  ? 173  TYR A CA  1 
ATOM   1417 C  C   . TYR A  1 173 ? 13.568  -12.138 49.266  1.00 15.33 ? 173  TYR A C   1 
ATOM   1418 O  O   . TYR A  1 173 ? 12.637  -11.737 48.561  1.00 13.11 ? 173  TYR A O   1 
ATOM   1419 C  CB  . TYR A  1 173 ? 15.842  -11.043 49.198  1.00 10.77 ? 173  TYR A CB  1 
ATOM   1420 C  CG  . TYR A  1 173 ? 15.705  -10.778 47.712  1.00 12.14 ? 173  TYR A CG  1 
ATOM   1421 C  CD1 . TYR A  1 173 ? 14.904  -9.742  47.243  1.00 13.94 ? 173  TYR A CD1 1 
ATOM   1422 C  CD2 . TYR A  1 173 ? 16.380  -11.557 46.784  1.00 13.14 ? 173  TYR A CD2 1 
ATOM   1423 C  CE1 . TYR A  1 173 ? 14.773  -9.492  45.894  1.00 14.57 ? 173  TYR A CE1 1 
ATOM   1424 C  CE2 . TYR A  1 173 ? 16.261  -11.301 45.415  1.00 16.05 ? 173  TYR A CE2 1 
ATOM   1425 C  CZ  . TYR A  1 173 ? 15.450  -10.267 44.988  1.00 18.29 ? 173  TYR A CZ  1 
ATOM   1426 O  OH  . TYR A  1 173 ? 15.304  -10.007 43.638  1.00 22.36 ? 173  TYR A OH  1 
ATOM   1427 N  N   . GLN A  1 174 ? 13.803  -13.420 49.514  1.00 13.27 ? 174  GLN A N   1 
ATOM   1428 C  CA  . GLN A  1 174 ? 13.055  -14.502 48.873  1.00 16.13 ? 174  GLN A CA  1 
ATOM   1429 C  C   . GLN A  1 174 ? 11.676  -14.740 49.487  1.00 18.53 ? 174  GLN A C   1 
ATOM   1430 O  O   . GLN A  1 174 ? 10.903  -15.534 48.966  1.00 22.57 ? 174  GLN A O   1 
ATOM   1431 C  CB  . GLN A  1 174 ? 13.872  -15.790 48.913  1.00 17.46 ? 174  GLN A CB  1 
ATOM   1432 C  CG  . GLN A  1 174 ? 15.111  -15.740 48.028  1.00 21.71 ? 174  GLN A CG  1 
ATOM   1433 C  CD  . GLN A  1 174 ? 16.127  -16.817 48.369  1.00 27.62 ? 174  GLN A CD  1 
ATOM   1434 O  OE1 . GLN A  1 174 ? 15.874  -17.696 49.197  1.00 33.25 ? 174  GLN A OE1 1 
ATOM   1435 N  NE2 . GLN A  1 174 ? 17.289  -16.749 47.731  1.00 35.21 ? 174  GLN A NE2 1 
ATOM   1436 N  N   . GLY A  1 175 ? 11.369  -14.058 50.588  1.00 13.63 ? 175  GLY A N   1 
ATOM   1437 C  CA  . GLY A  1 175 ? 10.049  -14.145 51.184  1.00 16.92 ? 175  GLY A CA  1 
ATOM   1438 C  C   . GLY A  1 175 ? 9.927   -15.101 52.361  1.00 18.87 ? 175  GLY A C   1 
ATOM   1439 O  O   . GLY A  1 175 ? 8.815   -15.405 52.808  1.00 19.94 ? 175  GLY A O   1 
ATOM   1440 N  N   . THR A  1 176 ? 11.060  -15.565 52.879  1.00 13.61 ? 176  THR A N   1 
ATOM   1441 C  CA  . THR A  1 176 ? 11.055  -16.393 54.090  1.00 17.28 ? 176  THR A CA  1 
ATOM   1442 C  C   . THR A  1 176 ? 11.947  -15.802 55.191  1.00 15.26 ? 176  THR A C   1 
ATOM   1443 O  O   . THR A  1 176 ? 12.912  -16.429 55.646  1.00 14.12 ? 176  THR A O   1 
ATOM   1444 C  CB  . THR A  1 176 ? 11.465  -17.839 53.787  1.00 18.65 ? 176  THR A CB  1 
ATOM   1445 O  OG1 . THR A  1 176 ? 12.726  -17.845 53.108  1.00 19.38 ? 176  THR A OG1 1 
ATOM   1446 C  CG2 . THR A  1 176 ? 10.423  -18.509 52.889  1.00 22.31 ? 176  THR A CG2 1 
ATOM   1447 N  N   . PRO A  1 177 ? 11.620  -14.585 55.632  1.00 14.58 ? 177  PRO A N   1 
ATOM   1448 C  CA  . PRO A  1 177 ? 12.505  -13.945 56.610  1.00 11.21 ? 177  PRO A CA  1 
ATOM   1449 C  C   . PRO A  1 177 ? 12.517  -14.671 57.941  1.00 14.44 ? 177  PRO A C   1 
ATOM   1450 O  O   . PRO A  1 177 ? 11.502  -15.259 58.339  1.00 13.36 ? 177  PRO A O   1 
ATOM   1451 C  CB  . PRO A  1 177 ? 11.884  -12.564 56.802  1.00 10.21 ? 177  PRO A CB  1 
ATOM   1452 C  CG  . PRO A  1 177 ? 10.448  -12.709 56.364  1.00 14.52 ? 177  PRO A CG  1 
ATOM   1453 C  CD  . PRO A  1 177 ? 10.442  -13.764 55.299  1.00 16.19 ? 177  PRO A CD  1 
ATOM   1454 N  N   . LEU A  1 178 ? 13.653  -14.607 58.628  1.00 12.87 ? 178  LEU A N   1 
ATOM   1455 C  CA  . LEU A  1 178 ? 13.724  -15.043 60.020  1.00 15.95 ? 178  LEU A CA  1 
ATOM   1456 C  C   . LEU A  1 178 ? 12.853  -14.153 60.899  1.00 13.02 ? 178  LEU A C   1 
ATOM   1457 O  O   . LEU A  1 178 ? 12.655  -12.977 60.607  1.00 13.16 ? 178  LEU A O   1 
ATOM   1458 C  CB  . LEU A  1 178 ? 15.171  -15.028 60.521  1.00 15.45 ? 178  LEU A CB  1 
ATOM   1459 C  CG  . LEU A  1 178 ? 16.059  -16.196 60.086  1.00 24.04 ? 178  LEU A CG  1 
ATOM   1460 C  CD1 . LEU A  1 178 ? 16.264  -16.215 58.571  1.00 24.69 ? 178  LEU A CD1 1 
ATOM   1461 C  CD2 . LEU A  1 178 ? 17.392  -16.128 60.811  1.00 31.68 ? 178  LEU A CD2 1 
ATOM   1462 N  N   . PRO A  1 179 ? 12.309  -14.720 61.982  1.00 13.61 ? 179  PRO A N   1 
ATOM   1463 C  CA  . PRO A  1 179 ? 11.568  -13.920 62.956  1.00 12.53 ? 179  PRO A CA  1 
ATOM   1464 C  C   . PRO A  1 179 ? 12.440  -12.767 63.448  1.00 10.64 ? 179  PRO A C   1 
ATOM   1465 O  O   . PRO A  1 179 ? 13.643  -12.952 63.657  1.00 12.84 ? 179  PRO A O   1 
ATOM   1466 C  CB  . PRO A  1 179 ? 11.310  -14.914 64.097  1.00 17.18 ? 179  PRO A CB  1 
ATOM   1467 C  CG  . PRO A  1 179 ? 11.385  -16.263 63.451  1.00 20.24 ? 179  PRO A CG  1 
ATOM   1468 C  CD  . PRO A  1 179 ? 12.456  -16.123 62.405  1.00 20.29 ? 179  PRO A CD  1 
ATOM   1469 N  N   . ALA A  1 180 ? 11.829  -11.607 63.653  1.00 10.86 ? 180  ALA A N   1 
ATOM   1470 C  CA  . ALA A  1 180 ? 12.577  -10.375 63.939  1.00 10.38 ? 180  ALA A CA  1 
ATOM   1471 C  C   . ALA A  1 180 ? 12.114  -9.727  65.238  1.00 14.73 ? 180  ALA A C   1 
ATOM   1472 O  O   . ALA A  1 180 ? 10.917  -9.482  65.442  1.00 17.14 ? 180  ALA A O   1 
ATOM   1473 C  CB  . ALA A  1 180 ? 12.451  -9.398  62.769  1.00 11.41 ? 180  ALA A CB  1 
ATOM   1474 N  N   . ASN A  1 181 ? 13.077  -9.421  66.104  1.00 11.20 ? 181  ASN A N   1 
ATOM   1475 C  CA  . ASN A  1 181 ? 12.782  -9.039  67.480  1.00 10.31 ? 181  ASN A CA  1 
ATOM   1476 C  C   . ASN A  1 181 ? 12.650  -7.550  67.800  1.00 15.08 ? 181  ASN A C   1 
ATOM   1477 O  O   . ASN A  1 181 ? 12.340  -7.193  68.931  1.00 17.83 ? 181  ASN A O   1 
ATOM   1478 C  CB  . ASN A  1 181 ? 13.758  -9.733  68.445  1.00 12.26 ? 181  ASN A CB  1 
ATOM   1479 C  CG  . ASN A  1 181 ? 15.208  -9.307  68.232  1.00 19.10 ? 181  ASN A CG  1 
ATOM   1480 O  OD1 . ASN A  1 181 ? 15.503  -8.451  67.395  1.00 14.11 ? 181  ASN A OD1 1 
ATOM   1481 N  ND2 . ASN A  1 181 ? 16.117  -9.903  68.999  1.00 19.53 ? 181  ASN A ND2 1 
ATOM   1482 N  N   . ILE A  1 182 ? 12.848  -6.675  66.818  1.00 9.71  ? 182  ILE A N   1 
ATOM   1483 C  CA  . ILE A  1 182 ? 12.588  -5.261  67.047  1.00 10.27 ? 182  ILE A CA  1 
ATOM   1484 C  C   . ILE A  1 182 ? 11.284  -4.861  66.351  1.00 10.69 ? 182  ILE A C   1 
ATOM   1485 O  O   . ILE A  1 182 ? 10.391  -4.287  66.973  1.00 13.31 ? 182  ILE A O   1 
ATOM   1486 C  CB  . ILE A  1 182 ? 13.761  -4.366  66.589  1.00 11.02 ? 182  ILE A CB  1 
ATOM   1487 C  CG1 . ILE A  1 182 ? 15.027  -4.703  67.389  1.00 13.41 ? 182  ILE A CG1 1 
ATOM   1488 C  CG2 . ILE A  1 182 ? 13.408  -2.906  66.774  1.00 13.18 ? 182  ILE A CG2 1 
ATOM   1489 C  CD1 . ILE A  1 182 ? 16.276  -3.890  66.944  1.00 13.05 ? 182  ILE A CD1 1 
ATOM   1490 N  N   . LEU A  1 183 ? 11.170  -5.183  65.063  1.00 9.25  ? 183  LEU A N   1 
ATOM   1491 C  CA  . LEU A  1 183 ? 9.927   -4.982  64.313  1.00 9.91  ? 183  LEU A CA  1 
ATOM   1492 C  C   . LEU A  1 183 ? 9.674   -6.202  63.435  1.00 11.53 ? 183  LEU A C   1 
ATOM   1493 O  O   . LEU A  1 183 ? 10.592  -6.707  62.795  1.00 10.38 ? 183  LEU A O   1 
ATOM   1494 C  CB  . LEU A  1 183 ? 9.995   -3.720  63.434  1.00 8.95  ? 183  LEU A CB  1 
ATOM   1495 C  CG  . LEU A  1 183 ? 10.160  -2.376  64.145  1.00 9.85  ? 183  LEU A CG  1 
ATOM   1496 C  CD1 . LEU A  1 183 ? 10.507  -1.271  63.140  1.00 11.67 ? 183  LEU A CD1 1 
ATOM   1497 C  CD2 . LEU A  1 183 ? 8.905   -2.028  64.947  1.00 12.54 ? 183  LEU A CD2 1 
ATOM   1498 N  N   . ASP A  1 184 ? 8.435   -6.683  63.401  1.00 9.85  ? 184  ASP A N   1 
ATOM   1499 C  CA  . ASP A  1 184 ? 8.132   -7.891  62.634  1.00 9.07  ? 184  ASP A CA  1 
ATOM   1500 C  C   . ASP A  1 184 ? 6.803   -7.724  61.915  1.00 11.29 ? 184  ASP A C   1 
ATOM   1501 O  O   . ASP A  1 184 ? 5.756   -7.566  62.554  1.00 12.12 ? 184  ASP A O   1 
ATOM   1502 C  CB  . ASP A  1 184 ? 8.109   -9.116  63.577  1.00 14.51 ? 184  ASP A CB  1 
ATOM   1503 C  CG  . ASP A  1 184 ? 8.050   -10.445 62.831  1.00 19.35 ? 184  ASP A CG  1 
ATOM   1504 O  OD1 . ASP A  1 184 ? 7.244   -10.574 61.893  1.00 18.09 ? 184  ASP A OD1 1 
ATOM   1505 O  OD2 . ASP A  1 184 ? 8.797   -11.391 63.193  1.00 18.85 ? 184  ASP A OD2 1 
ATOM   1506 N  N   . TRP A  1 185 ? 6.860   -7.753  60.584  1.00 10.69 ? 185  TRP A N   1 
ATOM   1507 C  CA  . TRP A  1 185 ? 5.692   -7.539  59.735  1.00 10.09 ? 185  TRP A CA  1 
ATOM   1508 C  C   . TRP A  1 185 ? 4.552   -8.499  60.064  1.00 15.37 ? 185  TRP A C   1 
ATOM   1509 O  O   . TRP A  1 185 ? 3.377   -8.198  59.816  1.00 14.34 ? 185  TRP A O   1 
ATOM   1510 C  CB  . TRP A  1 185 ? 6.100   -7.723  58.267  1.00 9.30  ? 185  TRP A CB  1 
ATOM   1511 C  CG  . TRP A  1 185 ? 5.163   -7.088  57.281  1.00 11.64 ? 185  TRP A CG  1 
ATOM   1512 C  CD1 . TRP A  1 185 ? 4.400   -7.724  56.340  1.00 11.34 ? 185  TRP A CD1 1 
ATOM   1513 C  CD2 . TRP A  1 185 ? 4.912   -5.685  57.120  1.00 8.22  ? 185  TRP A CD2 1 
ATOM   1514 N  NE1 . TRP A  1 185 ? 3.684   -6.800  55.608  1.00 10.31 ? 185  TRP A NE1 1 
ATOM   1515 C  CE2 . TRP A  1 185 ? 3.976   -5.545  56.071  1.00 7.75  ? 185  TRP A CE2 1 
ATOM   1516 C  CE3 . TRP A  1 185 ? 5.377   -4.537  57.767  1.00 8.89  ? 185  TRP A CE3 1 
ATOM   1517 C  CZ2 . TRP A  1 185 ? 3.494   -4.300  55.656  1.00 9.99  ? 185  TRP A CZ2 1 
ATOM   1518 C  CZ3 . TRP A  1 185 ? 4.904   -3.301  57.350  1.00 9.75  ? 185  TRP A CZ3 1 
ATOM   1519 C  CH2 . TRP A  1 185 ? 3.973   -3.197  56.303  1.00 9.63  ? 185  TRP A CH2 1 
ATOM   1520 N  N   . GLN A  1 186 ? 4.910   -9.658  60.609  1.00 13.98 ? 186  GLN A N   1 
ATOM   1521 C  CA  . GLN A  1 186 ? 3.932   -10.712 60.883  1.00 16.36 ? 186  GLN A CA  1 
ATOM   1522 C  C   . GLN A  1 186 ? 3.339   -10.598 62.284  1.00 18.02 ? 186  GLN A C   1 
ATOM   1523 O  O   . GLN A  1 186 ? 2.462   -11.376 62.674  1.00 16.44 ? 186  GLN A O   1 
ATOM   1524 C  CB  . GLN A  1 186 ? 4.566   -12.082 60.648  1.00 10.17 ? 186  GLN A CB  1 
ATOM   1525 C  CG  . GLN A  1 186 ? 4.933   -12.314 59.182  1.00 12.10 ? 186  GLN A CG  1 
ATOM   1526 C  CD  . GLN A  1 186 ? 5.711   -13.590 58.957  1.00 19.07 ? 186  GLN A CD  1 
ATOM   1527 O  OE1 . GLN A  1 186 ? 6.794   -13.578 58.359  1.00 18.80 ? 186  GLN A OE1 1 
ATOM   1528 N  NE2 . GLN A  1 186 ? 5.168   -14.702 59.431  1.00 15.53 ? 186  GLN A NE2 1 
ATOM   1529 N  N   . ALA A  1 187 ? 3.807   -9.605  63.030  1.00 13.72 ? 187  ALA A N   1 
ATOM   1530 C  CA  . ALA A  1 187 ? 3.301   -9.346  64.370  1.00 15.03 ? 187  ALA A CA  1 
ATOM   1531 C  C   . ALA A  1 187 ? 3.596   -7.894  64.698  1.00 11.40 ? 187  ALA A C   1 
ATOM   1532 O  O   . ALA A  1 187 ? 4.373   -7.586  65.606  1.00 14.39 ? 187  ALA A O   1 
ATOM   1533 C  CB  . ALA A  1 187 ? 3.959   -10.291 65.377  1.00 16.34 ? 187  ALA A CB  1 
ATOM   1534 N  N   . LEU A  1 188 ? 2.966   -7.002  63.937  1.00 12.31 ? 188  LEU A N   1 
ATOM   1535 C  CA  . LEU A  1 188 ? 3.317   -5.594  63.931  1.00 13.22 ? 188  LEU A CA  1 
ATOM   1536 C  C   . LEU A  1 188 ? 2.349   -4.751  64.748  1.00 17.15 ? 188  LEU A C   1 
ATOM   1537 O  O   . LEU A  1 188 ? 1.127   -4.911  64.655  1.00 17.86 ? 188  LEU A O   1 
ATOM   1538 C  CB  . LEU A  1 188 ? 3.345   -5.068  62.486  1.00 12.64 ? 188  LEU A CB  1 
ATOM   1539 C  CG  . LEU A  1 188 ? 4.109   -3.760  62.289  1.00 14.12 ? 188  LEU A CG  1 
ATOM   1540 C  CD1 . LEU A  1 188 ? 5.610   -4.021  62.417  1.00 13.19 ? 188  LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A  1 188 ? 3.770   -3.149  60.926  1.00 14.70 ? 188  LEU A CD2 1 
ATOM   1542 N  N   . ASN A  1 189 ? 2.915   -3.859  65.550  1.00 13.39 ? 189  ASN A N   1 
ATOM   1543 C  CA  . ASN A  1 189 ? 2.142   -2.901  66.329  1.00 16.73 ? 189  ASN A CA  1 
ATOM   1544 C  C   . ASN A  1 189 ? 2.336   -1.539  65.689  1.00 20.10 ? 189  ASN A C   1 
ATOM   1545 O  O   . ASN A  1 189 ? 3.444   -1.009  65.678  1.00 20.27 ? 189  ASN A O   1 
ATOM   1546 C  CB  . ASN A  1 189 ? 2.640   -2.873  67.772  1.00 19.16 ? 189  ASN A CB  1 
ATOM   1547 C  CG  . ASN A  1 189 ? 1.792   -1.997  68.671  1.00 36.16 ? 189  ASN A CG  1 
ATOM   1548 O  OD1 . ASN A  1 189 ? 0.773   -1.451  68.247  1.00 38.60 ? 189  ASN A OD1 1 
ATOM   1549 N  ND2 . ASN A  1 189 ? 2.209   -1.860  69.929  1.00 33.94 ? 189  ASN A ND2 1 
ATOM   1550 N  N   . TYR A  1 190 ? 1.267   -0.980  65.142  1.00 14.00 ? 190  TYR A N   1 
ATOM   1551 C  CA  . TYR A  1 190 ? 1.387   0.245   64.364  1.00 14.74 ? 190  TYR A CA  1 
ATOM   1552 C  C   . TYR A  1 190 ? 0.195   1.161   64.595  1.00 20.12 ? 190  TYR A C   1 
ATOM   1553 O  O   . TYR A  1 190 ? -0.839  0.740   65.136  1.00 14.92 ? 190  TYR A O   1 
ATOM   1554 C  CB  . TYR A  1 190 ? 1.529   -0.090  62.867  1.00 12.89 ? 190  TYR A CB  1 
ATOM   1555 C  CG  . TYR A  1 190 ? 0.322   -0.791  62.305  1.00 12.39 ? 190  TYR A CG  1 
ATOM   1556 C  CD1 . TYR A  1 190 ? 0.217   -2.179  62.337  1.00 12.42 ? 190  TYR A CD1 1 
ATOM   1557 C  CD2 . TYR A  1 190 ? -0.728  -0.065  61.762  1.00 16.80 ? 190  TYR A CD2 1 
ATOM   1558 C  CE1 . TYR A  1 190 ? -0.909  -2.819  61.830  1.00 21.10 ? 190  TYR A CE1 1 
ATOM   1559 C  CE2 . TYR A  1 190 ? -1.849  -0.692  61.262  1.00 22.13 ? 190  TYR A CE2 1 
ATOM   1560 C  CZ  . TYR A  1 190 ? -1.937  -2.065  61.300  1.00 20.88 ? 190  TYR A CZ  1 
ATOM   1561 O  OH  . TYR A  1 190 ? -3.063  -2.674  60.794  1.00 27.46 ? 190  TYR A OH  1 
ATOM   1562 N  N   . GLU A  1 191 ? 0.358   2.418   64.201  1.00 15.30 ? 191  GLU A N   1 
ATOM   1563 C  CA  . GLU A  1 191 ? -0.720  3.400   64.211  1.00 15.09 ? 191  GLU A CA  1 
ATOM   1564 C  C   . GLU A  1 191 ? -0.766  4.111   62.863  1.00 16.60 ? 191  GLU A C   1 
ATOM   1565 O  O   . GLU A  1 191 ? 0.195   4.776   62.472  1.00 16.83 ? 191  GLU A O   1 
ATOM   1566 C  CB  . GLU A  1 191 ? -0.487  4.443   65.310  1.00 20.33 ? 191  GLU A CB  1 
ATOM   1567 C  CG  . GLU A  1 191 ? -0.308  3.855   66.703  1.00 25.85 ? 191  GLU A CG  1 
ATOM   1568 C  CD  . GLU A  1 191 ? 0.213   4.863   67.718  1.00 34.26 ? 191  GLU A CD  1 
ATOM   1569 O  OE1 . GLU A  1 191 ? 0.713   5.938   67.311  1.00 29.06 ? 191  GLU A OE1 1 
ATOM   1570 O  OE2 . GLU A  1 191 ? 0.128   4.573   68.930  1.00 41.37 ? 191  GLU A OE2 1 
ATOM   1571 N  N   . ILE A  1 192 ? -1.879  3.990   62.152  1.00 14.93 ? 192  ILE A N   1 
ATOM   1572 C  CA  . ILE A  1 192 ? -2.064  4.775   60.929  1.00 12.68 ? 192  ILE A CA  1 
ATOM   1573 C  C   . ILE A  1 192 ? -2.524  6.197   61.260  1.00 17.51 ? 192  ILE A C   1 
ATOM   1574 O  O   . ILE A  1 192 ? -3.444  6.391   62.061  1.00 16.52 ? 192  ILE A O   1 
ATOM   1575 C  CB  . ILE A  1 192 ? -3.057  4.097   59.966  1.00 13.23 ? 192  ILE A CB  1 
ATOM   1576 C  CG1 . ILE A  1 192 ? -2.380  2.914   59.265  1.00 14.25 ? 192  ILE A CG1 1 
ATOM   1577 C  CG2 . ILE A  1 192 ? -3.586  5.085   58.915  1.00 13.48 ? 192  ILE A CG2 1 
ATOM   1578 C  CD1 . ILE A  1 192 ? -3.324  2.030   58.501  1.00 18.64 ? 192  ILE A CD1 1 
ATOM   1579 N  N   . ARG A  1 193 ? -1.879  7.189   60.650  1.00 14.00 ? 193  ARG A N   1 
ATOM   1580 C  CA  . ARG A  1 193 ? -2.302  8.578   60.783  1.00 13.85 ? 193  ARG A CA  1 
ATOM   1581 C  C   . ARG A  1 193 ? -2.521  9.172   59.402  1.00 16.66 ? 193  ARG A C   1 
ATOM   1582 O  O   . ARG A  1 193 ? -1.681  9.034   58.517  1.00 15.81 ? 193  ARG A O   1 
ATOM   1583 C  CB  . ARG A  1 193 ? -1.267  9.402   61.551  1.00 14.71 ? 193  ARG A CB  1 
ATOM   1584 C  CG  . ARG A  1 193 ? -1.033  8.926   62.992  1.00 21.22 ? 193  ARG A CG  1 
ATOM   1585 C  CD  . ARG A  1 193 ? -2.249  9.202   63.876  1.00 30.42 ? 193  ARG A CD  1 
ATOM   1586 N  NE  . ARG A  1 193 ? -2.089  8.672   65.232  1.00 31.54 ? 193  ARG A NE  1 
ATOM   1587 C  CZ  . ARG A  1 193 ? -2.652  7.548   65.673  1.00 32.42 ? 193  ARG A CZ  1 
ATOM   1588 N  NH1 . ARG A  1 193 ? -3.421  6.826   64.868  1.00 29.51 ? 193  ARG A NH1 1 
ATOM   1589 N  NH2 . ARG A  1 193 ? -2.452  7.145   66.922  1.00 27.56 ? 193  ARG A NH2 1 
ATOM   1590 N  N   . GLY A  1 194 ? -3.660  9.823   59.202  1.00 15.12 ? 194  GLY A N   1 
ATOM   1591 C  CA  . GLY A  1 194 ? -3.941  10.402  57.903  1.00 15.46 ? 194  GLY A CA  1 
ATOM   1592 C  C   . GLY A  1 194 ? -4.293  9.344   56.870  1.00 12.66 ? 194  GLY A C   1 
ATOM   1593 O  O   . GLY A  1 194 ? -4.854  8.293   57.195  1.00 14.26 ? 194  GLY A O   1 
ATOM   1594 N  N   . TYR A  1 195 ? -3.945  9.627   55.619  1.00 12.57 ? 195  TYR A N   1 
ATOM   1595 C  CA  . TYR A  1 195 ? -4.343  8.781   54.495  1.00 11.51 ? 195  TYR A CA  1 
ATOM   1596 C  C   . TYR A  1 195 ? -3.294  7.714   54.206  1.00 12.22 ? 195  TYR A C   1 
ATOM   1597 O  O   . TYR A  1 195 ? -2.356  7.941   53.441  1.00 11.30 ? 195  TYR A O   1 
ATOM   1598 C  CB  . TYR A  1 195 ? -4.537  9.664   53.266  1.00 11.40 ? 195  TYR A CB  1 
ATOM   1599 C  CG  . TYR A  1 195 ? -5.194  9.015   52.068  1.00 12.03 ? 195  TYR A CG  1 
ATOM   1600 C  CD1 . TYR A  1 195 ? -6.148  8.014   52.216  1.00 10.28 ? 195  TYR A CD1 1 
ATOM   1601 C  CD2 . TYR A  1 195 ? -4.890  9.454   50.784  1.00 12.53 ? 195  TYR A CD2 1 
ATOM   1602 C  CE1 . TYR A  1 195 ? -6.766  7.445   51.106  1.00 12.07 ? 195  TYR A CE1 1 
ATOM   1603 C  CE2 . TYR A  1 195 ? -5.488  8.889   49.673  1.00 13.19 ? 195  TYR A CE2 1 
ATOM   1604 C  CZ  . TYR A  1 195 ? -6.430  7.897   49.838  1.00 11.01 ? 195  TYR A CZ  1 
ATOM   1605 O  OH  . TYR A  1 195 ? -7.026  7.354   48.731  1.00 11.54 ? 195  TYR A OH  1 
ATOM   1606 N  N   . VAL A  1 196 ? -3.471  6.554   54.831  1.00 10.68 ? 196  VAL A N   1 
ATOM   1607 C  CA  . VAL A  1 196 ? -2.657  5.371   54.570  1.00 11.48 ? 196  VAL A CA  1 
ATOM   1608 C  C   . VAL A  1 196 ? -3.643  4.211   54.493  1.00 15.76 ? 196  VAL A C   1 
ATOM   1609 O  O   . VAL A  1 196 ? -4.529  4.082   55.343  1.00 14.57 ? 196  VAL A O   1 
ATOM   1610 C  CB  . VAL A  1 196 ? -1.641  5.098   55.688  1.00 9.69  ? 196  VAL A CB  1 
ATOM   1611 C  CG1 . VAL A  1 196 ? -0.701  3.966   55.268  1.00 11.53 ? 196  VAL A CG1 1 
ATOM   1612 C  CG2 . VAL A  1 196 ? -0.826  6.348   55.998  1.00 13.45 ? 196  VAL A CG2 1 
ATOM   1613 N  N   . ILE A  1 197 ? -3.511  3.390   53.461  1.00 11.16 ? 197  ILE A N   1 
ATOM   1614 C  CA  . ILE A  1 197 ? -4.444  2.298   53.233  1.00 8.94  ? 197  ILE A CA  1 
ATOM   1615 C  C   . ILE A  1 197 ? -3.706  0.973   53.189  1.00 11.35 ? 197  ILE A C   1 
ATOM   1616 O  O   . ILE A  1 197 ? -2.668  0.858   52.560  1.00 10.85 ? 197  ILE A O   1 
ATOM   1617 C  CB  . ILE A  1 197 ? -5.184  2.469   51.888  1.00 11.38 ? 197  ILE A CB  1 
ATOM   1618 C  CG1 . ILE A  1 197 ? -5.918  3.813   51.836  1.00 11.99 ? 197  ILE A CG1 1 
ATOM   1619 C  CG2 . ILE A  1 197 ? -6.167  1.308   51.660  1.00 11.21 ? 197  ILE A CG2 1 
ATOM   1620 C  CD1 . ILE A  1 197 ? -7.081  3.946   52.835  1.00 10.64 ? 197  ILE A CD1 1 
ATOM   1621 N  N   . ILE A  1 198 ? -4.250  -0.037  53.851  1.00 10.11 ? 198  ILE A N   1 
ATOM   1622 C  CA  . ILE A  1 198 ? -3.670  -1.369  53.760  1.00 10.49 ? 198  ILE A CA  1 
ATOM   1623 C  C   . ILE A  1 198 ? -4.304  -2.137  52.606  1.00 13.55 ? 198  ILE A C   1 
ATOM   1624 O  O   . ILE A  1 198 ? -5.532  -2.264  52.528  1.00 13.34 ? 198  ILE A O   1 
ATOM   1625 C  CB  . ILE A  1 198 ? -3.847  -2.141  55.069  1.00 10.90 ? 198  ILE A CB  1 
ATOM   1626 C  CG1 . ILE A  1 198 ? -3.176  -1.368  56.211  1.00 13.79 ? 198  ILE A CG1 1 
ATOM   1627 C  CG2 . ILE A  1 198 ? -3.271  -3.541  54.929  1.00 12.47 ? 198  ILE A CG2 1 
ATOM   1628 C  CD1 . ILE A  1 198 ? -3.345  -2.007  57.591  1.00 18.30 ? 198  ILE A CD1 1 
ATOM   1629 N  N   . LYS A  1 199 ? -3.455  -2.634  51.707  1.00 9.46  ? 199  LYS A N   1 
ATOM   1630 C  CA  . LYS A  1 199 ? -3.881  -3.384  50.528  1.00 10.59 ? 199  LYS A CA  1 
ATOM   1631 C  C   . LYS A  1 199 ? -3.049  -4.657  50.389  1.00 8.76  ? 199  LYS A C   1 
ATOM   1632 O  O   . LYS A  1 199 ? -1.950  -4.746  50.933  1.00 11.68 ? 199  LYS A O   1 
ATOM   1633 C  CB  . LYS A  1 199 ? -3.693  -2.528  49.269  1.00 9.73  ? 199  LYS A CB  1 
ATOM   1634 C  CG  . LYS A  1 199 ? -4.755  -1.466  49.078  1.00 13.37 ? 199  LYS A CG  1 
ATOM   1635 C  CD  . LYS A  1 199 ? -6.049  -2.121  48.627  1.00 16.85 ? 199  LYS A CD  1 
ATOM   1636 C  CE  . LYS A  1 199 ? -7.164  -1.106  48.464  1.00 21.09 ? 199  LYS A CE  1 
ATOM   1637 N  NZ  . LYS A  1 199 ? -8.423  -1.812  48.093  1.00 27.64 ? 199  LYS A NZ  1 
ATOM   1638 N  N   . PRO A  1 200 ? -3.560  -5.646  49.638  1.00 10.17 ? 200  PRO A N   1 
ATOM   1639 C  CA  . PRO A  1 200 ? -2.716  -6.797  49.308  1.00 11.47 ? 200  PRO A CA  1 
ATOM   1640 C  C   . PRO A  1 200 ? -1.461  -6.350  48.562  1.00 14.09 ? 200  PRO A C   1 
ATOM   1641 O  O   . PRO A  1 200 ? -1.485  -5.386  47.799  1.00 13.28 ? 200  PRO A O   1 
ATOM   1642 C  CB  . PRO A  1 200 ? -3.596  -7.624  48.364  1.00 13.18 ? 200  PRO A CB  1 
ATOM   1643 C  CG  . PRO A  1 200 ? -5.007  -7.208  48.697  1.00 15.89 ? 200  PRO A CG  1 
ATOM   1644 C  CD  . PRO A  1 200 ? -4.908  -5.750  49.050  1.00 15.39 ? 200  PRO A CD  1 
ATOM   1645 N  N   . LEU A  1 201 ? -0.372  -7.073  48.783  1.00 9.68  ? 201  LEU A N   1 
ATOM   1646 C  CA  . LEU A  1 201 ? 0.855   -6.882  48.021  1.00 11.72 ? 201  LEU A CA  1 
ATOM   1647 C  C   . LEU A  1 201 ? 0.715   -7.579  46.673  1.00 14.56 ? 201  LEU A C   1 
ATOM   1648 O  O   . LEU A  1 201 ? 0.618   -8.806  46.616  1.00 18.54 ? 201  LEU A O   1 
ATOM   1649 C  CB  . LEU A  1 201 ? 2.020   -7.489  48.796  1.00 14.08 ? 201  LEU A CB  1 
ATOM   1650 C  CG  . LEU A  1 201 ? 3.309   -7.718  48.016  1.00 19.58 ? 201  LEU A CG  1 
ATOM   1651 C  CD1 . LEU A  1 201 ? 3.951   -6.387  47.712  1.00 13.60 ? 201  LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A  1 201 ? 4.250   -8.605  48.825  1.00 24.75 ? 201  LEU A CD2 1 
ATOM   1653 N  N   . VAL A  1 202 ? 0.696   -6.821  45.580  1.00 9.78  ? 202  VAL A N   1 
ATOM   1654 C  CA  . VAL A  1 202 ? 0.435   -7.453  44.286  1.00 10.73 ? 202  VAL A CA  1 
ATOM   1655 C  C   . VAL A  1 202 ? 1.635   -7.430  43.349  1.00 13.60 ? 202  VAL A C   1 
ATOM   1656 O  O   . VAL A  1 202 ? 1.579   -7.976  42.242  1.00 13.81 ? 202  VAL A O   1 
ATOM   1657 C  CB  . VAL A  1 202 ? -0.760  -6.795  43.555  1.00 12.05 ? 202  VAL A CB  1 
ATOM   1658 C  CG1 . VAL A  1 202 ? -2.018  -6.870  44.419  1.00 10.57 ? 202  VAL A CG1 1 
ATOM   1659 C  CG2 . VAL A  1 202 ? -0.438  -5.357  43.178  1.00 11.41 ? 202  VAL A CG2 1 
ATOM   1660 N  N   . TRP A  1 203 ? 2.712   -6.795  43.793  1.00 12.30 ? 203  TRP A N   1 
ATOM   1661 C  CA  . TRP A  1 203 ? 3.864   -6.561  42.931  1.00 11.74 ? 203  TRP A CA  1 
ATOM   1662 C  C   . TRP A  1 203 ? 5.077   -7.432  43.248  1.00 21.40 ? 203  TRP A C   1 
ATOM   1663 O  O   . TRP A  1 203 ? 6.145   -7.255  42.660  1.00 23.89 ? 203  TRP A O   1 
ATOM   1664 C  CB  . TRP A  1 203 ? 4.253   -5.075  42.913  1.00 12.86 ? 203  TRP A CB  1 
ATOM   1665 C  CG  . TRP A  1 203 ? 4.176   -4.354  44.238  1.00 11.33 ? 203  TRP A CG  1 
ATOM   1666 C  CD1 . TRP A  1 203 ? 3.109   -3.667  44.742  1.00 10.71 ? 203  TRP A CD1 1 
ATOM   1667 C  CD2 . TRP A  1 203 ? 5.230   -4.217  45.202  1.00 10.23 ? 203  TRP A CD2 1 
ATOM   1668 N  NE1 . TRP A  1 203 ? 3.426   -3.134  45.972  1.00 12.38 ? 203  TRP A NE1 1 
ATOM   1669 C  CE2 . TRP A  1 203 ? 4.723   -3.461  46.275  1.00 10.03 ? 203  TRP A CE2 1 
ATOM   1670 C  CE3 . TRP A  1 203 ? 6.546   -4.692  45.273  1.00 14.45 ? 203  TRP A CE3 1 
ATOM   1671 C  CZ2 . TRP A  1 203 ? 5.494   -3.141  47.399  1.00 9.90  ? 203  TRP A CZ2 1 
ATOM   1672 C  CZ3 . TRP A  1 203 ? 7.311   -4.377  46.385  1.00 11.20 ? 203  TRP A CZ3 1 
ATOM   1673 C  CH2 . TRP A  1 203 ? 6.783   -3.610  47.436  1.00 13.01 ? 203  TRP A CH2 1 
ATOM   1674 N  N   . VAL A  1 204 ? 4.927   -8.371  44.172  1.00 20.87 ? 204  VAL A N   1 
ATOM   1675 C  CA  . VAL A  1 204 ? 5.987   -9.358  44.369  1.00 38.07 ? 204  VAL A CA  1 
ATOM   1676 C  C   . VAL A  1 204 ? 5.654   -10.663 43.653  1.00 57.61 ? 204  VAL A C   1 
ATOM   1677 O  O   . VAL A  1 204 ? 6.330   -11.040 42.692  1.00 49.69 ? 204  VAL A O   1 
ATOM   1678 C  CB  . VAL A  1 204 ? 6.271   -9.619  45.860  1.00 39.86 ? 204  VAL A CB  1 
ATOM   1679 C  CG1 . VAL A  1 204 ? 7.134   -10.864 46.034  1.00 29.25 ? 204  VAL A CG1 1 
ATOM   1680 C  CG2 . VAL A  1 204 ? 6.965   -8.426  46.454  1.00 44.54 ? 204  VAL A CG2 1 
ATOM   1681 O  OXT . VAL A  1 204 ? 4.696   -11.354 44.007  1.00 69.84 ? 204  VAL A OXT 1 
ATOM   1682 N  N   . HIS B  1 1   ? -26.375 -5.899  20.037  1.00 46.72 ? 1    HIS B N   1 
ATOM   1683 C  CA  . HIS B  1 1   ? -25.312 -4.964  19.683  1.00 38.37 ? 1    HIS B CA  1 
ATOM   1684 C  C   . HIS B  1 1   ? -24.245 -5.628  18.819  1.00 34.63 ? 1    HIS B C   1 
ATOM   1685 O  O   . HIS B  1 1   ? -24.580 -6.433  17.954  1.00 30.95 ? 1    HIS B O   1 
ATOM   1686 C  CB  . HIS B  1 1   ? -24.720 -4.340  20.939  1.00 28.36 ? 1    HIS B CB  1 
ATOM   1687 C  CG  . HIS B  1 1   ? -25.742 -3.661  21.795  1.00 43.29 ? 1    HIS B CG  1 
ATOM   1688 N  ND1 . HIS B  1 1   ? -25.914 -3.955  23.131  1.00 47.49 ? 1    HIS B ND1 1 
ATOM   1689 C  CD2 . HIS B  1 1   ? -26.671 -2.723  21.493  1.00 38.06 ? 1    HIS B CD2 1 
ATOM   1690 C  CE1 . HIS B  1 1   ? -26.892 -3.212  23.619  1.00 45.55 ? 1    HIS B CE1 1 
ATOM   1691 N  NE2 . HIS B  1 1   ? -27.368 -2.457  22.645  1.00 46.91 ? 1    HIS B NE2 1 
ATOM   1692 N  N   . THR B  1 2   ? -22.969 -5.310  19.037  1.00 22.66 ? 2    THR B N   1 
ATOM   1693 C  CA  . THR B  1 2   ? -21.939 -5.820  18.134  1.00 16.16 ? 2    THR B CA  1 
ATOM   1694 C  C   . THR B  1 2   ? -20.793 -6.557  18.824  1.00 15.94 ? 2    THR B C   1 
ATOM   1695 O  O   . THR B  1 2   ? -20.228 -6.093  19.816  1.00 15.71 ? 2    THR B O   1 
ATOM   1696 C  CB  . THR B  1 2   ? -21.383 -4.702  17.233  1.00 24.97 ? 2    THR B CB  1 
ATOM   1697 O  OG1 . THR B  1 2   ? -22.458 -4.130  16.481  1.00 32.90 ? 2    THR B OG1 1 
ATOM   1698 C  CG2 . THR B  1 2   ? -20.343 -5.242  16.275  1.00 20.96 ? 2    THR B CG2 1 
ATOM   1699 N  N   . ASP B  1 3   ? -20.454 -7.719  18.281  1.00 13.62 ? 3    ASP B N   1 
ATOM   1700 C  CA  . ASP B  1 3   ? -19.323 -8.485  18.785  1.00 12.45 ? 3    ASP B CA  1 
ATOM   1701 C  C   . ASP B  1 3   ? -18.068 -8.077  18.020  1.00 11.66 ? 3    ASP B C   1 
ATOM   1702 O  O   . ASP B  1 3   ? -17.895 -8.424  16.850  1.00 12.53 ? 3    ASP B O   1 
ATOM   1703 C  CB  . ASP B  1 3   ? -19.606 -9.980  18.610  1.00 15.08 ? 3    ASP B CB  1 
ATOM   1704 C  CG  . ASP B  1 3   ? -18.518 -10.858 19.177  1.00 21.46 ? 3    ASP B CG  1 
ATOM   1705 O  OD1 . ASP B  1 3   ? -17.439 -10.342 19.531  1.00 16.09 ? 3    ASP B OD1 1 
ATOM   1706 O  OD2 . ASP B  1 3   ? -18.743 -12.087 19.274  1.00 23.48 ? 3    ASP B OD2 1 
ATOM   1707 N  N   . LEU B  1 4   ? -17.199 -7.313  18.675  1.00 11.25 ? 4    LEU B N   1 
ATOM   1708 C  CA  . LEU B  1 4   ? -15.970 -6.856  18.032  1.00 8.16  ? 4    LEU B CA  1 
ATOM   1709 C  C   . LEU B  1 4   ? -14.760 -7.754  18.306  1.00 12.97 ? 4    LEU B C   1 
ATOM   1710 O  O   . LEU B  1 4   ? -13.622 -7.347  18.100  1.00 11.45 ? 4    LEU B O   1 
ATOM   1711 C  CB  . LEU B  1 4   ? -15.672 -5.417  18.458  1.00 10.85 ? 4    LEU B CB  1 
ATOM   1712 C  CG  . LEU B  1 4   ? -16.698 -4.403  17.964  1.00 11.38 ? 4    LEU B CG  1 
ATOM   1713 C  CD1 . LEU B  1 4   ? -16.326 -3.001  18.458  1.00 12.05 ? 4    LEU B CD1 1 
ATOM   1714 C  CD2 . LEU B  1 4   ? -16.770 -4.416  16.448  1.00 13.10 ? 4    LEU B CD2 1 
ATOM   1715 N  N   . SER B  1 5   ? -15.004 -8.976  18.775  1.00 11.20 ? 5    SER B N   1 
ATOM   1716 C  CA  . SER B  1 5   ? -13.918 -9.951  18.924  1.00 11.56 ? 5    SER B CA  1 
ATOM   1717 C  C   . SER B  1 5   ? -12.972 -9.940  17.729  1.00 12.14 ? 5    SER B C   1 
ATOM   1718 O  O   . SER B  1 5   ? -13.410 -10.088 16.589  1.00 14.92 ? 5    SER B O   1 
ATOM   1719 C  CB  . SER B  1 5   ? -14.499 -11.360 19.053  1.00 14.75 ? 5    SER B CB  1 
ATOM   1720 O  OG  . SER B  1 5   ? -15.128 -11.533 20.299  1.00 20.63 ? 5    SER B OG  1 
ATOM   1721 N  N   . GLY B  1 6   ? -11.676 -9.782  18.002  1.00 13.86 ? 6    GLY B N   1 
ATOM   1722 C  CA  . GLY B  1 6   ? -10.657 -9.840  16.967  1.00 13.59 ? 6    GLY B CA  1 
ATOM   1723 C  C   . GLY B  1 6   ? -10.548 -8.596  16.103  1.00 11.31 ? 6    GLY B C   1 
ATOM   1724 O  O   . GLY B  1 6   ? -9.857  -8.602  15.075  1.00 11.37 ? 6    GLY B O   1 
ATOM   1725 N  N   . LYS B  1 7   ? -11.225 -7.528  16.514  1.00 12.02 ? 7    LYS B N   1 
ATOM   1726 C  CA  . LYS B  1 7   ? -11.231 -6.282  15.751  1.00 10.26 ? 7    LYS B CA  1 
ATOM   1727 C  C   . LYS B  1 7   ? -10.828 -5.097  16.624  1.00 11.50 ? 7    LYS B C   1 
ATOM   1728 O  O   . LYS B  1 7   ? -10.874 -5.172  17.851  1.00 12.90 ? 7    LYS B O   1 
ATOM   1729 C  CB  . LYS B  1 7   ? -12.620 -6.022  15.172  1.00 9.70  ? 7    LYS B CB  1 
ATOM   1730 C  CG  . LYS B  1 7   ? -13.063 -7.126  14.237  1.00 16.20 ? 7    LYS B CG  1 
ATOM   1731 C  CD  . LYS B  1 7   ? -14.423 -6.881  13.640  1.00 23.97 ? 7    LYS B CD  1 
ATOM   1732 C  CE  . LYS B  1 7   ? -14.744 -7.985  12.634  1.00 31.95 ? 7    LYS B CE  1 
ATOM   1733 N  NZ  . LYS B  1 7   ? -16.177 -8.013  12.245  1.00 39.72 ? 7    LYS B NZ  1 
ATOM   1734 N  N   . VAL B  1 8   ? -10.436 -4.011  15.969  1.00 9.09  ? 8    VAL B N   1 
ATOM   1735 C  CA  . VAL B  1 8   ? -10.082 -2.773  16.656  1.00 6.92  ? 8    VAL B CA  1 
ATOM   1736 C  C   . VAL B  1 8   ? -10.790 -1.604  16.000  1.00 7.45  ? 8    VAL B C   1 
ATOM   1737 O  O   . VAL B  1 8   ? -11.198 -1.680  14.832  1.00 9.59  ? 8    VAL B O   1 
ATOM   1738 C  CB  . VAL B  1 8   ? -8.561  -2.480  16.554  1.00 11.34 ? 8    VAL B CB  1 
ATOM   1739 C  CG1 . VAL B  1 8   ? -7.746  -3.489  17.349  1.00 13.58 ? 8    VAL B CG1 1 
ATOM   1740 C  CG2 . VAL B  1 8   ? -8.112  -2.429  15.085  1.00 10.54 ? 8    VAL B CG2 1 
ATOM   1741 N  N   . PHE B  1 9   ? -10.937 -0.509  16.743  1.00 7.15  ? 9    PHE B N   1 
ATOM   1742 C  CA  . PHE B  1 9   ? -11.229 0.778   16.110  1.00 7.54  ? 9    PHE B CA  1 
ATOM   1743 C  C   . PHE B  1 9   ? -9.912  1.417   15.692  1.00 10.61 ? 9    PHE B C   1 
ATOM   1744 O  O   . PHE B  1 9   ? -8.978  1.510   16.502  1.00 9.40  ? 9    PHE B O   1 
ATOM   1745 C  CB  . PHE B  1 9   ? -11.908 1.750   17.079  1.00 7.37  ? 9    PHE B CB  1 
ATOM   1746 C  CG  . PHE B  1 9   ? -13.310 1.373   17.459  1.00 7.95  ? 9    PHE B CG  1 
ATOM   1747 C  CD1 . PHE B  1 9   ? -14.289 1.193   16.488  1.00 9.31  ? 9    PHE B CD1 1 
ATOM   1748 C  CD2 . PHE B  1 9   ? -13.657 1.234   18.795  1.00 9.97  ? 9    PHE B CD2 1 
ATOM   1749 C  CE1 . PHE B  1 9   ? -15.591 0.849   16.842  1.00 11.35 ? 9    PHE B CE1 1 
ATOM   1750 C  CE2 . PHE B  1 9   ? -14.966 0.885   19.166  1.00 10.94 ? 9    PHE B CE2 1 
ATOM   1751 C  CZ  . PHE B  1 9   ? -15.929 0.692   18.183  1.00 10.40 ? 9    PHE B CZ  1 
ATOM   1752 N  N   . VAL B  1 10  ? -9.841  1.883   14.447  1.00 6.54  ? 10   VAL B N   1 
ATOM   1753 C  CA  . VAL B  1 10  ? -8.687  2.654   13.990  1.00 6.60  ? 10   VAL B CA  1 
ATOM   1754 C  C   . VAL B  1 10  ? -9.083  4.112   13.844  1.00 6.46  ? 10   VAL B C   1 
ATOM   1755 O  O   . VAL B  1 10  ? -10.023 4.435   13.124  1.00 8.84  ? 10   VAL B O   1 
ATOM   1756 C  CB  . VAL B  1 10  ? -8.143  2.151   12.631  1.00 8.10  ? 10   VAL B CB  1 
ATOM   1757 C  CG1 . VAL B  1 10  ? -6.802  2.824   12.303  1.00 9.34  ? 10   VAL B CG1 1 
ATOM   1758 C  CG2 . VAL B  1 10  ? -7.986  0.622   12.652  1.00 8.36  ? 10   VAL B CG2 1 
ATOM   1759 N  N   . PHE B  1 11  ? -8.385  4.977   14.579  1.00 6.68  ? 11   PHE B N   1 
ATOM   1760 C  CA  . PHE B  1 11  ? -8.526  6.425   14.471  1.00 8.54  ? 11   PHE B CA  1 
ATOM   1761 C  C   . PHE B  1 11  ? -7.327  6.863   13.636  1.00 10.94 ? 11   PHE B C   1 
ATOM   1762 O  O   . PHE B  1 11  ? -6.221  7.032   14.161  1.00 8.83  ? 11   PHE B O   1 
ATOM   1763 C  CB  . PHE B  1 11  ? -8.488  7.036   15.883  1.00 7.56  ? 11   PHE B CB  1 
ATOM   1764 C  CG  . PHE B  1 11  ? -9.536  6.469   16.807  1.00 6.34  ? 11   PHE B CG  1 
ATOM   1765 C  CD1 . PHE B  1 11  ? -9.323  5.263   17.488  1.00 8.72  ? 11   PHE B CD1 1 
ATOM   1766 C  CD2 . PHE B  1 11  ? -10.772 7.099   16.941  1.00 8.60  ? 11   PHE B CD2 1 
ATOM   1767 C  CE1 . PHE B  1 11  ? -10.309 4.728   18.320  1.00 9.67  ? 11   PHE B CE1 1 
ATOM   1768 C  CE2 . PHE B  1 11  ? -11.763 6.575   17.769  1.00 8.91  ? 11   PHE B CE2 1 
ATOM   1769 C  CZ  . PHE B  1 11  ? -11.539 5.394   18.459  1.00 8.90  ? 11   PHE B CZ  1 
ATOM   1770 N  N   . PRO B  1 12  ? -7.523  6.986   12.308  1.00 8.05  ? 12   PRO B N   1 
ATOM   1771 C  CA  . PRO B  1 12  ? -6.361  6.982   11.415  1.00 8.51  ? 12   PRO B CA  1 
ATOM   1772 C  C   . PRO B  1 12  ? -5.694  8.328   11.218  1.00 8.52  ? 12   PRO B C   1 
ATOM   1773 O  O   . PRO B  1 12  ? -4.645  8.383   10.577  1.00 8.59  ? 12   PRO B O   1 
ATOM   1774 C  CB  . PRO B  1 12  ? -6.945  6.487   10.074  1.00 8.69  ? 12   PRO B CB  1 
ATOM   1775 C  CG  . PRO B  1 12  ? -8.338  5.952   10.415  1.00 6.84  ? 12   PRO B CG  1 
ATOM   1776 C  CD  . PRO B  1 12  ? -8.778  6.811   11.563  1.00 10.24 ? 12   PRO B CD  1 
ATOM   1777 N  N   . ARG B  1 13  ? -6.271  9.396   11.756  1.00 8.58  ? 13   ARG B N   1 
ATOM   1778 C  CA  . ARG B  1 13  ? -5.669  10.709  11.579  1.00 6.82  ? 13   ARG B CA  1 
ATOM   1779 C  C   . ARG B  1 13  ? -6.045  11.583  12.753  1.00 11.06 ? 13   ARG B C   1 
ATOM   1780 O  O   . ARG B  1 13  ? -7.043  11.338  13.419  1.00 13.71 ? 13   ARG B O   1 
ATOM   1781 C  CB  . ARG B  1 13  ? -6.213  11.358  10.312  1.00 10.54 ? 13   ARG B CB  1 
ATOM   1782 C  CG  . ARG B  1 13  ? -7.732  11.426  10.350  1.00 15.59 ? 13   ARG B CG  1 
ATOM   1783 C  CD  . ARG B  1 13  ? -8.347  12.569  9.551   1.00 22.11 ? 13   ARG B CD  1 
ATOM   1784 N  NE  . ARG B  1 13  ? -9.729  12.820  9.983   1.00 16.42 ? 13   ARG B NE  1 
ATOM   1785 C  CZ  . ARG B  1 13  ? -10.638 13.459  9.254   1.00 36.76 ? 13   ARG B CZ  1 
ATOM   1786 N  NH1 . ARG B  1 13  ? -10.323 13.906  8.044   1.00 44.40 ? 13   ARG B NH1 1 
ATOM   1787 N  NH2 . ARG B  1 13  ? -11.864 13.643  9.728   1.00 35.33 ? 13   ARG B NH2 1 
ATOM   1788 N  N   . GLU B  1 14  ? -5.248  12.612  12.985  1.00 8.27  ? 14   GLU B N   1 
ATOM   1789 C  CA  . GLU B  1 14  ? -5.534  13.584  14.024  1.00 9.68  ? 14   GLU B CA  1 
ATOM   1790 C  C   . GLU B  1 14  ? -6.650  14.515  13.538  1.00 11.11 ? 14   GLU B C   1 
ATOM   1791 O  O   . GLU B  1 14  ? -6.677  14.889  12.357  1.00 14.14 ? 14   GLU B O   1 
ATOM   1792 C  CB  . GLU B  1 14  ? -4.232  14.317  14.305  1.00 18.35 ? 14   GLU B CB  1 
ATOM   1793 C  CG  . GLU B  1 14  ? -4.303  15.719  14.742  1.00 26.97 ? 14   GLU B CG  1 
ATOM   1794 C  CD  . GLU B  1 14  ? -2.913  16.237  14.992  1.00 26.19 ? 14   GLU B CD  1 
ATOM   1795 O  OE1 . GLU B  1 14  ? -2.277  15.750  15.944  1.00 19.65 ? 14   GLU B OE1 1 
ATOM   1796 O  OE2 . GLU B  1 14  ? -2.445  17.093  14.215  1.00 31.30 ? 14   GLU B OE2 1 
ATOM   1797 N  N   . SER B  1 15  ? -7.577  14.858  14.434  1.00 9.34  ? 15   SER B N   1 
ATOM   1798 C  CA  . SER B  1 15  ? -8.750  15.663  14.084  1.00 11.50 ? 15   SER B CA  1 
ATOM   1799 C  C   . SER B  1 15  ? -9.391  16.165  15.356  1.00 10.96 ? 15   SER B C   1 
ATOM   1800 O  O   . SER B  1 15  ? -9.016  15.727  16.438  1.00 9.42  ? 15   SER B O   1 
ATOM   1801 C  CB  . SER B  1 15  ? -9.784  14.817  13.335  1.00 11.05 ? 15   SER B CB  1 
ATOM   1802 O  OG  . SER B  1 15  ? -10.546 14.036  14.245  1.00 10.33 ? 15   SER B OG  1 
ATOM   1803 N  N   . VAL B  1 16  ? -10.339 17.100  15.232  1.00 8.74  ? 16   VAL B N   1 
ATOM   1804 C  CA  . VAL B  1 16  ? -11.158 17.515  16.369  1.00 9.44  ? 16   VAL B CA  1 
ATOM   1805 C  C   . VAL B  1 16  ? -12.556 16.887  16.271  1.00 13.14 ? 16   VAL B C   1 
ATOM   1806 O  O   . VAL B  1 16  ? -13.495 17.308  16.951  1.00 15.93 ? 16   VAL B O   1 
ATOM   1807 C  CB  . VAL B  1 16  ? -11.251 19.071  16.452  1.00 12.06 ? 16   VAL B CB  1 
ATOM   1808 C  CG1 . VAL B  1 16  ? -12.153 19.616  15.359  1.00 15.12 ? 16   VAL B CG1 1 
ATOM   1809 C  CG2 . VAL B  1 16  ? -11.739 19.524  17.830  1.00 15.42 ? 16   VAL B CG2 1 
ATOM   1810 N  N   . THR B  1 17  ? -12.690 15.876  15.419  1.00 9.70  ? 17   THR B N   1 
ATOM   1811 C  CA  . THR B  1 17  ? -14.006 15.327  15.095  1.00 10.13 ? 17   THR B CA  1 
ATOM   1812 C  C   . THR B  1 17  ? -14.161 13.814  15.261  1.00 12.35 ? 17   THR B C   1 
ATOM   1813 O  O   . THR B  1 17  ? -15.215 13.339  15.725  1.00 12.65 ? 17   THR B O   1 
ATOM   1814 C  CB  . THR B  1 17  ? -14.376 15.666  13.628  1.00 17.62 ? 17   THR B CB  1 
ATOM   1815 O  OG1 . THR B  1 17  ? -14.529 17.079  13.500  1.00 24.77 ? 17   THR B OG1 1 
ATOM   1816 C  CG2 . THR B  1 17  ? -15.683 14.995  13.232  1.00 28.14 ? 17   THR B CG2 1 
ATOM   1817 N  N   . ASP B  1 18  ? -13.141 13.054  14.866  1.00 10.96 ? 18   ASP B N   1 
ATOM   1818 C  CA  . ASP B  1 18  ? -13.281 11.600  14.783  1.00 9.86  ? 18   ASP B CA  1 
ATOM   1819 C  C   . ASP B  1 18  ? -13.367 10.984  16.168  1.00 10.74 ? 18   ASP B C   1 
ATOM   1820 O  O   . ASP B  1 18  ? -12.492 11.211  17.006  1.00 10.09 ? 18   ASP B O   1 
ATOM   1821 C  CB  . ASP B  1 18  ? -12.087 10.979  14.039  1.00 10.88 ? 18   ASP B CB  1 
ATOM   1822 C  CG  . ASP B  1 18  ? -11.819 11.638  12.697  1.00 13.30 ? 18   ASP B CG  1 
ATOM   1823 O  OD1 . ASP B  1 18  ? -12.771 12.156  12.076  1.00 14.72 ? 18   ASP B OD1 1 
ATOM   1824 O  OD2 . ASP B  1 18  ? -10.649 11.624  12.256  1.00 15.52 ? 18   ASP B OD2 1 
ATOM   1825 N  N   . HIS B  1 19  ? -14.413 10.196  16.408  1.00 7.52  ? 19   HIS B N   1 
ATOM   1826 C  CA  . HIS B  1 19  ? -14.571 9.566   17.716  1.00 7.90  ? 19   HIS B CA  1 
ATOM   1827 C  C   . HIS B  1 19  ? -15.574 8.432   17.695  1.00 9.63  ? 19   HIS B C   1 
ATOM   1828 O  O   . HIS B  1 19  ? -16.333 8.281   16.745  1.00 10.85 ? 19   HIS B O   1 
ATOM   1829 C  CB  . HIS B  1 19  ? -14.940 10.607  18.801  1.00 7.31  ? 19   HIS B CB  1 
ATOM   1830 C  CG  . HIS B  1 19  ? -16.336 11.163  18.707  1.00 8.05  ? 19   HIS B CG  1 
ATOM   1831 N  ND1 . HIS B  1 19  ? -16.695 12.133  17.795  1.00 11.94 ? 19   HIS B ND1 1 
ATOM   1832 C  CD2 . HIS B  1 19  ? -17.443 10.924  19.453  1.00 11.78 ? 19   HIS B CD2 1 
ATOM   1833 C  CE1 . HIS B  1 19  ? -17.966 12.455  17.970  1.00 13.36 ? 19   HIS B CE1 1 
ATOM   1834 N  NE2 . HIS B  1 19  ? -18.444 11.736  18.969  1.00 14.06 ? 19   HIS B NE2 1 
ATOM   1835 N  N   . VAL B  1 20  ? -15.552 7.624   18.752  1.00 7.66  ? 20   VAL B N   1 
ATOM   1836 C  CA  . VAL B  1 20  ? -16.587 6.623   18.960  1.00 7.87  ? 20   VAL B CA  1 
ATOM   1837 C  C   . VAL B  1 20  ? -17.310 6.912   20.262  1.00 9.00  ? 20   VAL B C   1 
ATOM   1838 O  O   . VAL B  1 20  ? -16.688 7.140   21.306  1.00 9.46  ? 20   VAL B O   1 
ATOM   1839 C  CB  . VAL B  1 20  ? -15.990 5.207   19.027  1.00 8.10  ? 20   VAL B CB  1 
ATOM   1840 C  CG1 . VAL B  1 20  ? -17.091 4.165   19.266  1.00 9.40  ? 20   VAL B CG1 1 
ATOM   1841 C  CG2 . VAL B  1 20  ? -15.255 4.895   17.743  1.00 8.89  ? 20   VAL B CG2 1 
ATOM   1842 N  N   A ASN B  1 21  ? -18.636 6.933   20.195  0.56 8.79  ? 21   ASN B N   1 
ATOM   1843 N  N   B ASN B  1 21  ? -18.635 6.881   20.201  0.44 8.81  ? 21   ASN B N   1 
ATOM   1844 C  CA  A ASN B  1 21  ? -19.443 7.009   21.399  0.56 9.15  ? 21   ASN B CA  1 
ATOM   1845 C  CA  B ASN B  1 21  ? -19.468 7.028   21.382  0.44 9.20  ? 21   ASN B CA  1 
ATOM   1846 C  C   A ASN B  1 21  ? -19.714 5.600   21.893  0.56 10.62 ? 21   ASN B C   1 
ATOM   1847 C  C   B ASN B  1 21  ? -19.825 5.645   21.922  0.44 10.66 ? 21   ASN B C   1 
ATOM   1848 O  O   A ASN B  1 21  ? -20.123 4.730   21.123  0.56 10.26 ? 21   ASN B O   1 
ATOM   1849 O  O   B ASN B  1 21  ? -20.408 4.832   21.202  0.44 11.05 ? 21   ASN B O   1 
ATOM   1850 C  CB  A ASN B  1 21  ? -20.758 7.735   21.112  0.56 13.41 ? 21   ASN B CB  1 
ATOM   1851 C  CB  B ASN B  1 21  ? -20.732 7.798   20.996  0.44 13.35 ? 21   ASN B CB  1 
ATOM   1852 C  CG  A ASN B  1 21  ? -20.555 9.199   20.792  0.56 15.89 ? 21   ASN B CG  1 
ATOM   1853 C  CG  B ASN B  1 21  ? -21.628 8.087   22.174  0.44 12.54 ? 21   ASN B CG  1 
ATOM   1854 O  OD1 A ASN B  1 21  ? -19.775 9.886   21.452  0.56 13.53 ? 21   ASN B OD1 1 
ATOM   1855 O  OD1 B ASN B  1 21  ? -21.168 8.501   23.239  0.44 17.96 ? 21   ASN B OD1 1 
ATOM   1856 N  ND2 A ASN B  1 21  ? -21.267 9.691   19.784  0.56 23.52 ? 21   ASN B ND2 1 
ATOM   1857 N  ND2 B ASN B  1 21  ? -22.926 7.899   21.979  0.44 15.13 ? 21   ASN B ND2 1 
ATOM   1858 N  N   . LEU B  1 22  ? -19.465 5.367   23.174  1.00 8.85  ? 22   LEU B N   1 
ATOM   1859 C  CA  . LEU B  1 22  ? -19.750 4.059   23.773  1.00 10.82 ? 22   LEU B CA  1 
ATOM   1860 C  C   . LEU B  1 22  ? -20.945 4.189   24.691  1.00 11.66 ? 22   LEU B C   1 
ATOM   1861 O  O   . LEU B  1 22  ? -20.981 5.085   25.536  1.00 12.53 ? 22   LEU B O   1 
ATOM   1862 C  CB  . LEU B  1 22  ? -18.560 3.543   24.575  1.00 9.45  ? 22   LEU B CB  1 
ATOM   1863 C  CG  . LEU B  1 22  ? -17.250 3.333   23.813  1.00 10.75 ? 22   LEU B CG  1 
ATOM   1864 C  CD1 . LEU B  1 22  ? -16.185 2.841   24.764  1.00 10.15 ? 22   LEU B CD1 1 
ATOM   1865 C  CD2 . LEU B  1 22  ? -17.446 2.359   22.644  1.00 15.79 ? 22   LEU B CD2 1 
ATOM   1866 N  N   . ILE B  1 23  ? -21.903 3.276   24.543  1.00 9.34  ? 23   ILE B N   1 
ATOM   1867 C  CA  . ILE B  1 23  ? -23.172 3.399   25.257  1.00 10.50 ? 23   ILE B CA  1 
ATOM   1868 C  C   . ILE B  1 23  ? -23.325 2.260   26.247  1.00 11.53 ? 23   ILE B C   1 
ATOM   1869 O  O   . ILE B  1 23  ? -23.258 1.093   25.862  1.00 14.02 ? 23   ILE B O   1 
ATOM   1870 C  CB  . ILE B  1 23  ? -24.336 3.377   24.254  1.00 14.74 ? 23   ILE B CB  1 
ATOM   1871 C  CG1 . ILE B  1 23  ? -24.155 4.511   23.233  1.00 19.31 ? 23   ILE B CG1 1 
ATOM   1872 C  CG2 . ILE B  1 23  ? -25.686 3.473   24.973  1.00 19.40 ? 23   ILE B CG2 1 
ATOM   1873 C  CD1 . ILE B  1 23  ? -25.055 4.411   22.012  1.00 22.47 ? 23   ILE B CD1 1 
ATOM   1874 N  N   . THR B  1 24  ? -23.499 2.599   27.525  1.00 12.00 ? 24   THR B N   1 
ATOM   1875 C  CA  . THR B  1 24  ? -23.771 1.579   28.525  1.00 11.65 ? 24   THR B CA  1 
ATOM   1876 C  C   . THR B  1 24  ? -25.213 1.738   29.011  1.00 12.28 ? 24   THR B C   1 
ATOM   1877 O  O   . THR B  1 24  ? -25.670 2.853   29.236  1.00 14.43 ? 24   THR B O   1 
ATOM   1878 C  CB  . THR B  1 24  ? -22.791 1.651   29.711  1.00 11.53 ? 24   THR B CB  1 
ATOM   1879 O  OG1 . THR B  1 24  ? -23.122 0.635   30.662  1.00 13.25 ? 24   THR B OG1 1 
ATOM   1880 C  CG2 . THR B  1 24  ? -22.855 3.024   30.393  1.00 18.17 ? 24   THR B CG2 1 
ATOM   1881 N  N   . PRO B  1 25  ? -25.932 0.618   29.152  1.00 13.94 ? 25   PRO B N   1 
ATOM   1882 C  CA  . PRO B  1 25  ? -27.310 0.648   29.655  1.00 16.99 ? 25   PRO B CA  1 
ATOM   1883 C  C   . PRO B  1 25  ? -27.345 0.566   31.172  1.00 20.99 ? 25   PRO B C   1 
ATOM   1884 O  O   . PRO B  1 25  ? -28.402 0.756   31.785  1.00 15.25 ? 25   PRO B O   1 
ATOM   1885 C  CB  . PRO B  1 25  ? -27.895 -0.630  29.066  1.00 17.52 ? 25   PRO B CB  1 
ATOM   1886 C  CG  . PRO B  1 25  ? -26.757 -1.581  29.139  1.00 17.97 ? 25   PRO B CG  1 
ATOM   1887 C  CD  . PRO B  1 25  ? -25.520 -0.750  28.798  1.00 19.18 ? 25   PRO B CD  1 
ATOM   1888 N  N   . LEU B  1 26  ? -26.196 0.274   31.772  1.00 19.66 ? 26   LEU B N   1 
ATOM   1889 C  CA  . LEU B  1 26  ? -26.103 0.175   33.220  1.00 21.72 ? 26   LEU B CA  1 
ATOM   1890 C  C   . LEU B  1 26  ? -26.020 1.572   33.767  1.00 32.48 ? 26   LEU B C   1 
ATOM   1891 O  O   . LEU B  1 26  ? -24.957 2.193   33.748  1.00 44.95 ? 26   LEU B O   1 
ATOM   1892 C  CB  . LEU B  1 26  ? -24.878 -0.637  33.637  1.00 27.48 ? 26   LEU B CB  1 
ATOM   1893 C  CG  . LEU B  1 26  ? -24.542 -0.661  35.131  1.00 32.77 ? 26   LEU B CG  1 
ATOM   1894 C  CD1 . LEU B  1 26  ? -23.860 -1.969  35.487  1.00 30.07 ? 26   LEU B CD1 1 
ATOM   1895 C  CD2 . LEU B  1 26  ? -23.674 0.525   35.519  1.00 32.24 ? 26   LEU B CD2 1 
ATOM   1896 N  N   . GLU B  1 27  ? -27.147 2.080   34.243  1.00 16.51 ? 27   GLU B N   1 
ATOM   1897 C  CA  . GLU B  1 27  ? -27.184 3.462   34.679  1.00 25.08 ? 27   GLU B CA  1 
ATOM   1898 C  C   . GLU B  1 27  ? -27.204 3.545   36.194  1.00 27.79 ? 27   GLU B C   1 
ATOM   1899 O  O   . GLU B  1 27  ? -28.223 3.302   36.841  1.00 31.04 ? 27   GLU B O   1 
ATOM   1900 C  CB  . GLU B  1 27  ? -28.385 4.195   34.100  1.00 19.19 ? 27   GLU B CB  1 
ATOM   1901 C  CG  . GLU B  1 27  ? -28.438 5.645   34.530  1.00 29.46 ? 27   GLU B CG  1 
ATOM   1902 C  CD  . GLU B  1 27  ? -29.793 6.267   34.290  1.00 21.65 ? 27   GLU B CD  1 
ATOM   1903 O  OE1 . GLU B  1 27  ? -30.151 6.482   33.110  1.00 24.93 ? 27   GLU B OE1 1 
ATOM   1904 O  OE2 . GLU B  1 27  ? -30.495 6.535   35.286  1.00 21.95 ? 27   GLU B OE2 1 
ATOM   1905 N  N   . LYS B  1 28  ? -26.057 3.887   36.753  1.00 16.58 ? 28   LYS B N   1 
ATOM   1906 C  CA  . LYS B  1 28  ? -25.911 3.992   38.190  1.00 14.28 ? 28   LYS B CA  1 
ATOM   1907 C  C   . LYS B  1 28  ? -24.640 4.771   38.405  1.00 14.09 ? 28   LYS B C   1 
ATOM   1908 O  O   . LYS B  1 28  ? -23.777 4.799   37.520  1.00 17.48 ? 28   LYS B O   1 
ATOM   1909 C  CB  . LYS B  1 28  ? -25.781 2.607   38.837  1.00 20.07 ? 28   LYS B CB  1 
ATOM   1910 C  CG  . LYS B  1 28  ? -24.638 1.764   38.281  1.00 28.88 ? 28   LYS B CG  1 
ATOM   1911 C  CD  . LYS B  1 28  ? -24.355 0.512   39.114  1.00 41.18 ? 28   LYS B CD  1 
ATOM   1912 C  CE  . LYS B  1 28  ? -23.322 0.788   40.201  1.00 39.56 ? 28   LYS B CE  1 
ATOM   1913 N  NZ  . LYS B  1 28  ? -22.844 -0.459  40.865  1.00 58.91 ? 28   LYS B NZ  1 
ATOM   1914 N  N   . PRO B  1 29  ? -24.523 5.429   39.561  1.00 16.08 ? 29   PRO B N   1 
ATOM   1915 C  CA  . PRO B  1 29  ? -23.240 6.053   39.880  1.00 15.94 ? 29   PRO B CA  1 
ATOM   1916 C  C   . PRO B  1 29  ? -22.254 4.934   40.161  1.00 13.02 ? 29   PRO B C   1 
ATOM   1917 O  O   . PRO B  1 29  ? -22.666 3.843   40.558  1.00 16.11 ? 29   PRO B O   1 
ATOM   1918 C  CB  . PRO B  1 29  ? -23.521 6.824   41.172  1.00 18.03 ? 29   PRO B CB  1 
ATOM   1919 C  CG  . PRO B  1 29  ? -25.021 6.812   41.344  1.00 23.27 ? 29   PRO B CG  1 
ATOM   1920 C  CD  . PRO B  1 29  ? -25.505 5.584   40.647  1.00 20.51 ? 29   PRO B CD  1 
ATOM   1921 N  N   . LEU B  1 30  ? -20.969 5.201   39.978  1.00 13.53 ? 30   LEU B N   1 
ATOM   1922 C  CA  . LEU B  1 30  ? -19.957 4.179   40.193  1.00 14.86 ? 30   LEU B CA  1 
ATOM   1923 C  C   . LEU B  1 30  ? -19.193 4.395   41.495  1.00 13.25 ? 30   LEU B C   1 
ATOM   1924 O  O   . LEU B  1 30  ? -18.627 5.452   41.720  1.00 13.14 ? 30   LEU B O   1 
ATOM   1925 C  CB  . LEU B  1 30  ? -18.981 4.167   39.018  1.00 13.26 ? 30   LEU B CB  1 
ATOM   1926 C  CG  . LEU B  1 30  ? -19.573 3.853   37.642  1.00 14.68 ? 30   LEU B CG  1 
ATOM   1927 C  CD1 . LEU B  1 30  ? -18.522 4.007   36.557  1.00 21.09 ? 30   LEU B CD1 1 
ATOM   1928 C  CD2 . LEU B  1 30  ? -20.173 2.460   37.620  1.00 16.86 ? 30   LEU B CD2 1 
ATOM   1929 N  N   . GLN B  1 31  ? -19.196 3.380   42.351  1.00 13.34 ? 31   GLN B N   1 
ATOM   1930 C  CA  . GLN B  1 31  ? -18.392 3.392   43.556  1.00 12.68 ? 31   GLN B CA  1 
ATOM   1931 C  C   . GLN B  1 31  ? -17.102 2.613   43.300  1.00 11.86 ? 31   GLN B C   1 
ATOM   1932 O  O   . GLN B  1 31  ? -16.066 2.920   43.865  1.00 15.43 ? 31   GLN B O   1 
ATOM   1933 C  CB  . GLN B  1 31  ? -19.169 2.753   44.710  1.00 20.85 ? 31   GLN B CB  1 
ATOM   1934 C  CG  . GLN B  1 31  ? -18.366 2.601   45.986  1.00 32.92 ? 31   GLN B CG  1 
ATOM   1935 C  CD  . GLN B  1 31  ? -19.235 2.288   47.192  1.00 50.28 ? 31   GLN B CD  1 
ATOM   1936 O  OE1 . GLN B  1 31  ? -20.467 2.235   47.094  1.00 38.20 ? 31   GLN B OE1 1 
ATOM   1937 N  NE2 . GLN B  1 31  ? -18.594 2.082   48.342  1.00 36.41 ? 31   GLN B NE2 1 
ATOM   1938 N  N   . ASN B  1 32  ? -17.201 1.599   42.445  1.00 9.41  ? 32   ASN B N   1 
ATOM   1939 C  CA  . ASN B  1 32  ? -16.079 0.735   42.086  1.00 11.95 ? 32   ASN B CA  1 
ATOM   1940 C  C   . ASN B  1 32  ? -16.115 0.537   40.578  1.00 9.68  ? 32   ASN B C   1 
ATOM   1941 O  O   . ASN B  1 32  ? -17.187 0.401   39.992  1.00 13.84 ? 32   ASN B O   1 
ATOM   1942 C  CB  . ASN B  1 32  ? -16.230 -0.673  42.696  1.00 13.38 ? 32   ASN B CB  1 
ATOM   1943 C  CG  . ASN B  1 32  ? -16.354 -0.680  44.209  1.00 18.49 ? 32   ASN B CG  1 
ATOM   1944 O  OD1 . ASN B  1 32  ? -15.614 -0.001  44.923  1.00 15.72 ? 32   ASN B OD1 1 
ATOM   1945 N  ND2 . ASN B  1 32  ? -17.295 -1.502  44.701  1.00 19.99 ? 32   ASN B ND2 1 
ATOM   1946 N  N   . PHE B  1 33  ? -14.956 0.500   39.930  1.00 9.90  ? 33   PHE B N   1 
ATOM   1947 C  CA  . PHE B  1 33  ? -14.928 0.055   38.541  1.00 9.76  ? 33   PHE B CA  1 
ATOM   1948 C  C   . PHE B  1 33  ? -13.546 -0.429  38.173  1.00 8.12  ? 33   PHE B C   1 
ATOM   1949 O  O   . PHE B  1 33  ? -12.564 -0.107  38.843  1.00 9.21  ? 33   PHE B O   1 
ATOM   1950 C  CB  . PHE B  1 33  ? -15.338 1.164   37.568  1.00 8.15  ? 33   PHE B CB  1 
ATOM   1951 C  CG  . PHE B  1 33  ? -14.308 2.255   37.417  1.00 11.18 ? 33   PHE B CG  1 
ATOM   1952 C  CD1 . PHE B  1 33  ? -13.268 2.131   36.498  1.00 11.43 ? 33   PHE B CD1 1 
ATOM   1953 C  CD2 . PHE B  1 33  ? -14.380 3.403   38.191  1.00 8.20  ? 33   PHE B CD2 1 
ATOM   1954 C  CE1 . PHE B  1 33  ? -12.312 3.133   36.374  1.00 9.55  ? 33   PHE B CE1 1 
ATOM   1955 C  CE2 . PHE B  1 33  ? -13.434 4.409   38.068  1.00 8.09  ? 33   PHE B CE2 1 
ATOM   1956 C  CZ  . PHE B  1 33  ? -12.395 4.274   37.158  1.00 9.43  ? 33   PHE B CZ  1 
ATOM   1957 N  N   . THR B  1 34  ? -13.502 -1.220  37.110  1.00 8.10  ? 34   THR B N   1 
ATOM   1958 C  CA  . THR B  1 34  ? -12.258 -1.547  36.430  1.00 9.52  ? 34   THR B CA  1 
ATOM   1959 C  C   . THR B  1 34  ? -12.485 -1.375  34.940  1.00 9.27  ? 34   THR B C   1 
ATOM   1960 O  O   . THR B  1 34  ? -13.524 -1.774  34.406  1.00 9.89  ? 34   THR B O   1 
ATOM   1961 C  CB  . THR B  1 34  ? -11.831 -3.003  36.689  1.00 7.84  ? 34   THR B CB  1 
ATOM   1962 O  OG1 . THR B  1 34  ? -11.742 -3.232  38.097  1.00 9.77  ? 34   THR B OG1 1 
ATOM   1963 C  CG2 . THR B  1 34  ? -10.482 -3.279  36.058  1.00 9.71  ? 34   THR B CG2 1 
ATOM   1964 N  N   . LEU B  1 35  ? -11.505 -0.782  34.270  1.00 8.25  ? 35   LEU B N   1 
ATOM   1965 C  CA  . LEU B  1 35  ? -11.537 -0.620  32.825  1.00 7.08  ? 35   LEU B CA  1 
ATOM   1966 C  C   . LEU B  1 35  ? -10.268 -1.229  32.212  1.00 8.92  ? 35   LEU B C   1 
ATOM   1967 O  O   . LEU B  1 35  ? -9.157  -0.878  32.625  1.00 8.65  ? 35   LEU B O   1 
ATOM   1968 C  CB  . LEU B  1 35  ? -11.579 0.874   32.503  1.00 7.49  ? 35   LEU B CB  1 
ATOM   1969 C  CG  . LEU B  1 35  ? -11.354 1.275   31.052  1.00 9.00  ? 35   LEU B CG  1 
ATOM   1970 C  CD1 . LEU B  1 35  ? -12.517 0.818   30.174  1.00 9.20  ? 35   LEU B CD1 1 
ATOM   1971 C  CD2 . LEU B  1 35  ? -11.174 2.795   30.980  1.00 9.02  ? 35   LEU B CD2 1 
ATOM   1972 N  N   . CYS B  1 36  ? -10.425 -2.139  31.244  1.00 9.27  ? 36   CYS B N   1 
ATOM   1973 C  CA  . CYS B  1 36  ? -9.277  -2.712  30.524  1.00 10.67 ? 36   CYS B CA  1 
ATOM   1974 C  C   . CYS B  1 36  ? -9.448  -2.503  29.019  1.00 7.89  ? 36   CYS B C   1 
ATOM   1975 O  O   . CYS B  1 36  ? -10.563 -2.539  28.506  1.00 9.65  ? 36   CYS B O   1 
ATOM   1976 C  CB  . CYS B  1 36  ? -9.127  -4.224  30.809  1.00 9.15  ? 36   CYS B CB  1 
ATOM   1977 S  SG  . CYS B  1 36  ? -8.836  -4.651  32.552  1.00 15.17 ? 36   CYS B SG  1 
ATOM   1978 N  N   . PHE B  1 37  ? -8.344  -2.268  28.317  1.00 8.87  ? 37   PHE B N   1 
ATOM   1979 C  CA  . PHE B  1 37  ? -8.357  -2.186  26.859  1.00 9.75  ? 37   PHE B CA  1 
ATOM   1980 C  C   . PHE B  1 37  ? -6.932  -2.271  26.329  1.00 9.21  ? 37   PHE B C   1 
ATOM   1981 O  O   . PHE B  1 37  ? -5.967  -2.130  27.083  1.00 9.77  ? 37   PHE B O   1 
ATOM   1982 C  CB  . PHE B  1 37  ? -9.015  -0.886  26.368  1.00 8.30  ? 37   PHE B CB  1 
ATOM   1983 C  CG  . PHE B  1 37  ? -8.402  0.366   26.954  1.00 8.74  ? 37   PHE B CG  1 
ATOM   1984 C  CD1 . PHE B  1 37  ? -7.408  1.046   26.277  1.00 10.09 ? 37   PHE B CD1 1 
ATOM   1985 C  CD2 . PHE B  1 37  ? -8.826  0.853   28.183  1.00 11.33 ? 37   PHE B CD2 1 
ATOM   1986 C  CE1 . PHE B  1 37  ? -6.841  2.201   26.823  1.00 10.72 ? 37   PHE B CE1 1 
ATOM   1987 C  CE2 . PHE B  1 37  ? -8.258  1.995   28.732  1.00 13.89 ? 37   PHE B CE2 1 
ATOM   1988 C  CZ  . PHE B  1 37  ? -7.268  2.666   28.049  1.00 12.54 ? 37   PHE B CZ  1 
ATOM   1989 N  N   . ARG B  1 38  ? -6.814  -2.527  25.032  1.00 7.61  ? 38   ARG B N   1 
ATOM   1990 C  CA  . ARG B  1 38  ? -5.526  -2.515  24.353  1.00 8.81  ? 38   ARG B CA  1 
ATOM   1991 C  C   . ARG B  1 38  ? -5.439  -1.283  23.464  1.00 6.99  ? 38   ARG B C   1 
ATOM   1992 O  O   . ARG B  1 38  ? -6.433  -0.864  22.870  1.00 9.87  ? 38   ARG B O   1 
ATOM   1993 C  CB  . ARG B  1 38  ? -5.366  -3.757  23.477  1.00 10.54 ? 38   ARG B CB  1 
ATOM   1994 C  CG  . ARG B  1 38  ? -5.313  -5.043  24.239  1.00 14.36 ? 38   ARG B CG  1 
ATOM   1995 C  CD  . ARG B  1 38  ? -5.094  -6.214  23.290  1.00 14.53 ? 38   ARG B CD  1 
ATOM   1996 N  NE  . ARG B  1 38  ? -5.586  -7.411  23.938  1.00 17.14 ? 38   ARG B NE  1 
ATOM   1997 C  CZ  . ARG B  1 38  ? -4.896  -8.102  24.832  1.00 23.93 ? 38   ARG B CZ  1 
ATOM   1998 N  NH1 . ARG B  1 38  ? -3.660  -7.727  25.153  1.00 17.75 ? 38   ARG B NH1 1 
ATOM   1999 N  NH2 . ARG B  1 38  ? -5.439  -9.174  25.390  1.00 21.38 ? 38   ARG B NH2 1 
ATOM   2000 N  N   . ALA B  1 39  ? -4.245  -0.709  23.367  1.00 8.16  ? 39   ALA B N   1 
ATOM   2001 C  CA  . ALA B  1 39  ? -4.043  0.459   22.527  1.00 6.83  ? 39   ALA B CA  1 
ATOM   2002 C  C   . ALA B  1 39  ? -2.693  0.404   21.824  1.00 8.83  ? 39   ALA B C   1 
ATOM   2003 O  O   . ALA B  1 39  ? -1.726  -0.159  22.335  1.00 8.42  ? 39   ALA B O   1 
ATOM   2004 C  CB  . ALA B  1 39  ? -4.167  1.739   23.351  1.00 8.04  ? 39   ALA B CB  1 
ATOM   2005 N  N   . TYR B  1 40  ? -2.630  0.998   20.640  1.00 7.01  ? 40   TYR B N   1 
ATOM   2006 C  CA  . TYR B  1 40  ? -1.387  1.052   19.888  1.00 7.30  ? 40   TYR B CA  1 
ATOM   2007 C  C   . TYR B  1 40  ? -1.361  2.405   19.196  1.00 8.59  ? 40   TYR B C   1 
ATOM   2008 O  O   . TYR B  1 40  ? -2.190  2.681   18.329  1.00 7.54  ? 40   TYR B O   1 
ATOM   2009 C  CB  . TYR B  1 40  ? -1.361  -0.090  18.869  1.00 10.01 ? 40   TYR B CB  1 
ATOM   2010 C  CG  . TYR B  1 40  ? -0.050  -0.313  18.137  1.00 7.69  ? 40   TYR B CG  1 
ATOM   2011 C  CD1 . TYR B  1 40  ? 1.165   0.123   18.662  1.00 7.38  ? 40   TYR B CD1 1 
ATOM   2012 C  CD2 . TYR B  1 40  ? -0.033  -0.990  16.931  1.00 7.56  ? 40   TYR B CD2 1 
ATOM   2013 C  CE1 . TYR B  1 40  ? 2.369   -0.111  17.983  1.00 9.30  ? 40   TYR B CE1 1 
ATOM   2014 C  CE2 . TYR B  1 40  ? 1.151   -1.239  16.260  1.00 7.39  ? 40   TYR B CE2 1 
ATOM   2015 C  CZ  . TYR B  1 40  ? 2.345   -0.791  16.779  1.00 8.30  ? 40   TYR B CZ  1 
ATOM   2016 O  OH  . TYR B  1 40  ? 3.530   -1.028  16.099  1.00 10.19 ? 40   TYR B OH  1 
ATOM   2017 N  N   . SER B  1 41  ? -0.419  3.250   19.602  1.00 6.47  ? 41   SER B N   1 
ATOM   2018 C  CA  . SER B  1 41  ? -0.315  4.602   19.055  1.00 7.04  ? 41   SER B CA  1 
ATOM   2019 C  C   . SER B  1 41  ? 1.142   4.989   18.994  1.00 6.87  ? 41   SER B C   1 
ATOM   2020 O  O   . SER B  1 41  ? 1.915   4.598   19.861  1.00 10.86 ? 41   SER B O   1 
ATOM   2021 C  CB  . SER B  1 41  ? -1.052  5.586   19.982  1.00 8.25  ? 41   SER B CB  1 
ATOM   2022 O  OG  . SER B  1 41  ? -0.865  6.938   19.562  1.00 8.18  ? 41   SER B OG  1 
ATOM   2023 N  N   . ASP B  1 42  ? 1.526   5.779   17.998  1.00 5.83  ? 42   ASP B N   1 
ATOM   2024 C  CA  . ASP B  1 42  ? 2.888   6.313   17.972  1.00 7.64  ? 42   ASP B CA  1 
ATOM   2025 C  C   . ASP B  1 42  ? 2.950   7.835   18.172  1.00 7.14  ? 42   ASP B C   1 
ATOM   2026 O  O   . ASP B  1 42  ? 3.938   8.494   17.830  1.00 9.27  ? 42   ASP B O   1 
ATOM   2027 C  CB  . ASP B  1 42  ? 3.694   5.814   16.757  1.00 7.41  ? 42   ASP B CB  1 
ATOM   2028 C  CG  . ASP B  1 42  ? 3.091   6.217   15.422  1.00 11.44 ? 42   ASP B CG  1 
ATOM   2029 O  OD1 . ASP B  1 42  ? 2.290   7.173   15.375  1.00 10.42 ? 42   ASP B OD1 1 
ATOM   2030 O  OD2 . ASP B  1 42  ? 3.441   5.565   14.402  1.00 10.45 ? 42   ASP B OD2 1 
ATOM   2031 N  N   . LEU B  1 43  ? 1.890   8.377   18.764  1.00 8.22  ? 43   LEU B N   1 
ATOM   2032 C  CA  . LEU B  1 43  ? 1.914   9.758   19.226  1.00 8.98  ? 43   LEU B CA  1 
ATOM   2033 C  C   . LEU B  1 43  ? 2.903   9.913   20.378  1.00 8.39  ? 43   LEU B C   1 
ATOM   2034 O  O   . LEU B  1 43  ? 2.994   9.039   21.244  1.00 8.99  ? 43   LEU B O   1 
ATOM   2035 C  CB  . LEU B  1 43  ? 0.527   10.153  19.737  1.00 8.46  ? 43   LEU B CB  1 
ATOM   2036 C  CG  . LEU B  1 43  ? -0.574  10.362  18.698  1.00 8.93  ? 43   LEU B CG  1 
ATOM   2037 C  CD1 . LEU B  1 43  ? -1.886  10.660  19.410  1.00 8.33  ? 43   LEU B CD1 1 
ATOM   2038 C  CD2 . LEU B  1 43  ? -0.196  11.515  17.777  1.00 8.21  ? 43   LEU B CD2 1 
ATOM   2039 N  N   . SER B  1 44  ? 3.635   11.031  20.383  1.00 7.36  ? 44   SER B N   1 
ATOM   2040 C  CA  . SER B  1 44  ? 4.465   11.404  21.530  1.00 10.13 ? 44   SER B CA  1 
ATOM   2041 C  C   . SER B  1 44  ? 3.801   12.476  22.380  1.00 9.48  ? 44   SER B C   1 
ATOM   2042 O  O   . SER B  1 44  ? 4.070   12.584  23.577  1.00 11.65 ? 44   SER B O   1 
ATOM   2043 C  CB  . SER B  1 44  ? 5.840   11.893  21.061  1.00 12.56 ? 44   SER B CB  1 
ATOM   2044 O  OG  . SER B  1 44  ? 6.550   10.831  20.461  1.00 16.77 ? 44   SER B OG  1 
ATOM   2045 N  N   . ARG B  1 45  ? 2.938   13.269  21.756  1.00 10.18 ? 45   ARG B N   1 
ATOM   2046 C  CA  . ARG B  1 45  ? 2.206   14.299  22.485  1.00 8.44  ? 45   ARG B CA  1 
ATOM   2047 C  C   . ARG B  1 45  ? 1.164   13.653  23.395  1.00 11.18 ? 45   ARG B C   1 
ATOM   2048 O  O   . ARG B  1 45  ? 0.908   12.441  23.308  1.00 10.10 ? 45   ARG B O   1 
ATOM   2049 C  CB  . ARG B  1 45  ? 1.524   15.266  21.508  1.00 11.17 ? 45   ARG B CB  1 
ATOM   2050 C  CG  . ARG B  1 45  ? 0.393   14.646  20.672  1.00 9.59  ? 45   ARG B CG  1 
ATOM   2051 C  CD  . ARG B  1 45  ? -0.564  15.737  20.154  1.00 9.21  ? 45   ARG B CD  1 
ATOM   2052 N  NE  . ARG B  1 45  ? -1.382  15.227  19.060  1.00 8.41  ? 45   ARG B NE  1 
ATOM   2053 C  CZ  . ARG B  1 45  ? -2.485  14.502  19.231  1.00 8.43  ? 45   ARG B CZ  1 
ATOM   2054 N  NH1 . ARG B  1 45  ? -2.928  14.217  20.460  1.00 7.84  ? 45   ARG B NH1 1 
ATOM   2055 N  NH2 . ARG B  1 45  ? -3.143  14.053  18.166  1.00 8.44  ? 45   ARG B NH2 1 
ATOM   2056 N  N   . ALA B  1 46  ? 0.567   14.466  24.266  1.00 10.95 ? 46   ALA B N   1 
ATOM   2057 C  CA  . ALA B  1 46  ? -0.477  14.002  25.170  1.00 11.09 ? 46   ALA B CA  1 
ATOM   2058 C  C   . ALA B  1 46  ? -1.722  13.583  24.394  1.00 11.14 ? 46   ALA B C   1 
ATOM   2059 O  O   . ALA B  1 46  ? -2.014  14.131  23.338  1.00 10.95 ? 46   ALA B O   1 
ATOM   2060 C  CB  . ALA B  1 46  ? -0.836  15.109  26.149  1.00 12.34 ? 46   ALA B CB  1 
ATOM   2061 N  N   . TYR B  1 47  ? -2.461  12.619  24.929  1.00 9.61  ? 47   TYR B N   1 
ATOM   2062 C  CA  . TYR B  1 47  ? -3.745  12.246  24.340  1.00 8.38  ? 47   TYR B CA  1 
ATOM   2063 C  C   . TYR B  1 47  ? -4.651  11.546  25.325  1.00 7.98  ? 47   TYR B C   1 
ATOM   2064 O  O   . TYR B  1 47  ? -4.176  10.962  26.299  1.00 12.00 ? 47   TYR B O   1 
ATOM   2065 C  CB  . TYR B  1 47  ? -3.570  11.359  23.110  1.00 9.49  ? 47   TYR B CB  1 
ATOM   2066 C  CG  . TYR B  1 47  ? -2.714  10.127  23.292  1.00 11.12 ? 47   TYR B CG  1 
ATOM   2067 C  CD1 . TYR B  1 47  ? -3.263  8.930   23.749  1.00 9.87  ? 47   TYR B CD1 1 
ATOM   2068 C  CD2 . TYR B  1 47  ? -1.363  10.151  22.966  1.00 8.42  ? 47   TYR B CD2 1 
ATOM   2069 C  CE1 . TYR B  1 47  ? -2.477  7.779   23.881  1.00 10.19 ? 47   TYR B CE1 1 
ATOM   2070 C  CE2 . TYR B  1 47  ? -0.571  9.010   23.101  1.00 10.31 ? 47   TYR B CE2 1 
ATOM   2071 C  CZ  . TYR B  1 47  ? -1.135  7.837   23.556  1.00 9.88  ? 47   TYR B CZ  1 
ATOM   2072 O  OH  . TYR B  1 47  ? -0.342  6.714   23.680  1.00 10.01 ? 47   TYR B OH  1 
ATOM   2073 N  N   . SER B  1 48  ? -5.959  11.611  25.058  1.00 6.65  ? 48   SER B N   1 
ATOM   2074 C  CA  . SER B  1 48  ? -6.951  10.909  25.857  1.00 8.48  ? 48   SER B CA  1 
ATOM   2075 C  C   . SER B  1 48  ? -7.144  9.480   25.358  1.00 7.85  ? 48   SER B C   1 
ATOM   2076 O  O   . SER B  1 48  ? -7.214  9.238   24.157  1.00 8.15  ? 48   SER B O   1 
ATOM   2077 C  CB  . SER B  1 48  ? -8.290  11.672  25.828  1.00 8.86  ? 48   SER B CB  1 
ATOM   2078 O  OG  . SER B  1 48  ? -9.276  10.998  26.591  1.00 10.28 ? 48   SER B OG  1 
ATOM   2079 N  N   . LEU B  1 49  ? -7.189  8.528   26.292  1.00 8.09  ? 49   LEU B N   1 
ATOM   2080 C  CA  . LEU B  1 49  ? -7.507  7.138   25.971  1.00 7.35  ? 49   LEU B CA  1 
ATOM   2081 C  C   . LEU B  1 49  ? -8.986  6.812   26.164  1.00 7.70  ? 49   LEU B C   1 
ATOM   2082 O  O   . LEU B  1 49  ? -9.585  6.118   25.346  1.00 9.41  ? 49   LEU B O   1 
ATOM   2083 C  CB  . LEU B  1 49  ? -6.649  6.189   26.819  1.00 7.36  ? 49   LEU B CB  1 
ATOM   2084 C  CG  . LEU B  1 49  ? -5.187  6.106   26.351  1.00 10.92 ? 49   LEU B CG  1 
ATOM   2085 C  CD1 . LEU B  1 49  ? -4.303  5.529   27.442  1.00 12.87 ? 49   LEU B CD1 1 
ATOM   2086 C  CD2 . LEU B  1 49  ? -5.068  5.302   25.060  1.00 12.62 ? 49   LEU B CD2 1 
ATOM   2087 N  N   . PHE B  1 50  ? -9.571  7.315   27.246  1.00 7.83  ? 50   PHE B N   1 
ATOM   2088 C  CA  . PHE B  1 50  ? -10.964 7.006   27.578  1.00 7.20  ? 50   PHE B CA  1 
ATOM   2089 C  C   . PHE B  1 50  ? -11.545 8.191   28.339  1.00 6.55  ? 50   PHE B C   1 
ATOM   2090 O  O   . PHE B  1 50  ? -11.062 8.535   29.416  1.00 6.95  ? 50   PHE B O   1 
ATOM   2091 C  CB  . PHE B  1 50  ? -11.004 5.732   28.423  1.00 8.76  ? 50   PHE B CB  1 
ATOM   2092 C  CG  . PHE B  1 50  ? -12.390 5.279   28.832  1.00 6.23  ? 50   PHE B CG  1 
ATOM   2093 C  CD1 . PHE B  1 50  ? -12.993 5.778   29.982  1.00 7.85  ? 50   PHE B CD1 1 
ATOM   2094 C  CD2 . PHE B  1 50  ? -13.048 4.292   28.108  1.00 7.38  ? 50   PHE B CD2 1 
ATOM   2095 C  CE1 . PHE B  1 50  ? -14.237 5.325   30.388  1.00 9.72  ? 50   PHE B CE1 1 
ATOM   2096 C  CE2 . PHE B  1 50  ? -14.298 3.830   28.512  1.00 9.58  ? 50   PHE B CE2 1 
ATOM   2097 C  CZ  . PHE B  1 50  ? -14.890 4.340   29.647  1.00 8.98  ? 50   PHE B CZ  1 
ATOM   2098 N  N   . SER B  1 51  ? -12.570 8.817   27.761  1.00 6.86  ? 51   SER B N   1 
ATOM   2099 C  CA  . SER B  1 51  ? -13.123 10.068  28.276  1.00 7.46  ? 51   SER B CA  1 
ATOM   2100 C  C   . SER B  1 51  ? -14.588 9.864   28.681  1.00 7.92  ? 51   SER B C   1 
ATOM   2101 O  O   . SER B  1 51  ? -15.426 9.530   27.846  1.00 8.46  ? 51   SER B O   1 
ATOM   2102 C  CB  . SER B  1 51  ? -13.009 11.159  27.197  1.00 7.84  ? 51   SER B CB  1 
ATOM   2103 O  OG  . SER B  1 51  ? -13.721 12.355  27.557  1.00 7.57  ? 51   SER B OG  1 
ATOM   2104 N  N   . TYR B  1 52  ? -14.884 10.080  29.963  1.00 9.01  ? 52   TYR B N   1 
ATOM   2105 C  CA  . TYR B  1 52  ? -16.217 9.853   30.525  1.00 7.86  ? 52   TYR B CA  1 
ATOM   2106 C  C   . TYR B  1 52  ? -16.617 11.160  31.228  1.00 7.32  ? 52   TYR B C   1 
ATOM   2107 O  O   . TYR B  1 52  ? -16.022 11.549  32.236  1.00 8.94  ? 52   TYR B O   1 
ATOM   2108 C  CB  . TYR B  1 52  ? -16.126 8.635   31.463  1.00 6.00  ? 52   TYR B CB  1 
ATOM   2109 C  CG  . TYR B  1 52  ? -17.299 8.234   32.365  1.00 6.42  ? 52   TYR B CG  1 
ATOM   2110 C  CD1 . TYR B  1 52  ? -17.793 9.097   33.340  1.00 9.81  ? 52   TYR B CD1 1 
ATOM   2111 C  CD2 . TYR B  1 52  ? -17.802 6.933   32.328  1.00 9.81  ? 52   TYR B CD2 1 
ATOM   2112 C  CE1 . TYR B  1 52  ? -18.814 8.690   34.213  1.00 8.36  ? 52   TYR B CE1 1 
ATOM   2113 C  CE2 . TYR B  1 52  ? -18.831 6.519   33.193  1.00 10.39 ? 52   TYR B CE2 1 
ATOM   2114 C  CZ  . TYR B  1 52  ? -19.326 7.408   34.130  1.00 10.70 ? 52   TYR B CZ  1 
ATOM   2115 O  OH  . TYR B  1 52  ? -20.336 6.998   34.986  1.00 12.83 ? 52   TYR B OH  1 
ATOM   2116 N  N   . ASN B  1 53  ? -17.562 11.881  30.622  1.00 8.48  ? 53   ASN B N   1 
ATOM   2117 C  CA  . ASN B  1 53  ? -18.069 13.137  31.172  1.00 9.39  ? 53   ASN B CA  1 
ATOM   2118 C  C   . ASN B  1 53  ? -19.542 13.000  31.517  1.00 11.06 ? 53   ASN B C   1 
ATOM   2119 O  O   . ASN B  1 53  ? -20.265 12.223  30.905  1.00 8.64  ? 53   ASN B O   1 
ATOM   2120 C  CB  . ASN B  1 53  ? -17.926 14.282  30.159  1.00 6.99  ? 53   ASN B CB  1 
ATOM   2121 C  CG  . ASN B  1 53  ? -16.558 14.942  30.193  1.00 9.63  ? 53   ASN B CG  1 
ATOM   2122 O  OD1 . ASN B  1 53  ? -15.586 14.377  30.678  1.00 10.31 ? 53   ASN B OD1 1 
ATOM   2123 N  ND2 . ASN B  1 53  ? -16.485 16.155  29.667  1.00 9.20  ? 53   ASN B ND2 1 
ATOM   2124 N  N   . THR B  1 54  ? -20.004 13.768  32.492  1.00 8.61  ? 54   THR B N   1 
ATOM   2125 C  CA  . THR B  1 54  ? -21.444 13.787  32.755  1.00 9.83  ? 54   THR B CA  1 
ATOM   2126 C  C   . THR B  1 54  ? -21.941 15.216  32.607  1.00 9.84  ? 54   THR B C   1 
ATOM   2127 O  O   . THR B  1 54  ? -21.148 16.129  32.382  1.00 11.54 ? 54   THR B O   1 
ATOM   2128 C  CB  . THR B  1 54  ? -21.801 13.196  34.122  1.00 11.02 ? 54   THR B CB  1 
ATOM   2129 O  OG1 . THR B  1 54  ? -21.091 13.897  35.146  1.00 13.13 ? 54   THR B OG1 1 
ATOM   2130 C  CG2 . THR B  1 54  ? -21.424 11.714  34.168  1.00 9.58  ? 54   THR B CG2 1 
ATOM   2131 N  N   . GLN B  1 55  ? -23.255 15.405  32.687  1.00 10.87 ? 55   GLN B N   1 
ATOM   2132 C  CA  . GLN B  1 55  ? -23.833 16.720  32.426  1.00 11.15 ? 55   GLN B CA  1 
ATOM   2133 C  C   . GLN B  1 55  ? -23.260 17.730  33.411  1.00 10.04 ? 55   GLN B C   1 
ATOM   2134 O  O   . GLN B  1 55  ? -23.353 17.532  34.624  1.00 13.55 ? 55   GLN B O   1 
ATOM   2135 C  CB  . GLN B  1 55  ? -25.354 16.655  32.548  1.00 14.23 ? 55   GLN B CB  1 
ATOM   2136 C  CG  . GLN B  1 55  ? -26.055 17.983  32.262  1.00 24.20 ? 55   GLN B CG  1 
ATOM   2137 C  CD  . GLN B  1 55  ? -25.665 18.579  30.917  1.00 25.45 ? 55   GLN B CD  1 
ATOM   2138 O  OE1 . GLN B  1 55  ? -25.054 19.649  30.851  1.00 40.43 ? 55   GLN B OE1 1 
ATOM   2139 N  NE2 . GLN B  1 55  ? -26.010 17.886  29.838  1.00 27.95 ? 55   GLN B NE2 1 
ATOM   2140 N  N   . GLY B  1 56  ? -22.643 18.783  32.883  1.00 11.96 ? 56   GLY B N   1 
ATOM   2141 C  CA  . GLY B  1 56  ? -22.041 19.825  33.702  1.00 14.64 ? 56   GLY B CA  1 
ATOM   2142 C  C   . GLY B  1 56  ? -20.756 19.444  34.424  1.00 12.44 ? 56   GLY B C   1 
ATOM   2143 O  O   . GLY B  1 56  ? -20.223 20.242  35.208  1.00 13.38 ? 56   GLY B O   1 
ATOM   2144 N  N   . ARG B  1 57  ? -20.248 18.237  34.176  1.00 11.24 ? 57   ARG B N   1 
ATOM   2145 C  CA  . ARG B  1 57  ? -19.047 17.773  34.874  1.00 8.97  ? 57   ARG B CA  1 
ATOM   2146 C  C   . ARG B  1 57  ? -17.979 17.262  33.914  1.00 10.39 ? 57   ARG B C   1 
ATOM   2147 O  O   . ARG B  1 57  ? -18.130 16.199  33.319  1.00 12.49 ? 57   ARG B O   1 
ATOM   2148 C  CB  . ARG B  1 57  ? -19.391 16.657  35.852  1.00 10.18 ? 57   ARG B CB  1 
ATOM   2149 C  CG  . ARG B  1 57  ? -20.350 17.083  36.961  1.00 13.89 ? 57   ARG B CG  1 
ATOM   2150 C  CD  . ARG B  1 57  ? -19.638 17.783  38.099  1.00 26.77 ? 57   ARG B CD  1 
ATOM   2151 N  NE  . ARG B  1 57  ? -20.511 17.913  39.265  1.00 38.56 ? 57   ARG B NE  1 
ATOM   2152 C  CZ  . ARG B  1 57  ? -20.924 19.071  39.772  1.00 27.81 ? 57   ARG B CZ  1 
ATOM   2153 N  NH1 . ARG B  1 57  ? -20.532 20.219  39.228  1.00 33.57 ? 57   ARG B NH1 1 
ATOM   2154 N  NH2 . ARG B  1 57  ? -21.721 19.079  40.833  1.00 31.42 ? 57   ARG B NH2 1 
ATOM   2155 N  N   . ASP B  1 58  ? -16.896 18.019  33.793  1.00 8.84  ? 58   ASP B N   1 
ATOM   2156 C  CA  . ASP B  1 58  ? -15.781 17.626  32.932  1.00 8.35  ? 58   ASP B CA  1 
ATOM   2157 C  C   . ASP B  1 58  ? -14.878 16.652  33.668  1.00 8.05  ? 58   ASP B C   1 
ATOM   2158 O  O   . ASP B  1 58  ? -14.799 16.676  34.894  1.00 9.56  ? 58   ASP B O   1 
ATOM   2159 C  CB  . ASP B  1 58  ? -14.968 18.864  32.549  1.00 10.79 ? 58   ASP B CB  1 
ATOM   2160 C  CG  . ASP B  1 58  ? -13.917 18.569  31.502  1.00 11.83 ? 58   ASP B CG  1 
ATOM   2161 O  OD1 . ASP B  1 58  ? -14.202 17.761  30.599  1.00 10.65 ? 58   ASP B OD1 1 
ATOM   2162 O  OD2 . ASP B  1 58  ? -12.812 19.147  31.579  1.00 11.11 ? 58   ASP B OD2 1 
ATOM   2163 N  N   . ASN B  1 59  ? -14.176 15.804  32.919  1.00 7.43  ? 59   ASN B N   1 
ATOM   2164 C  CA  . ASN B  1 59  ? -13.216 14.879  33.518  1.00 8.15  ? 59   ASN B CA  1 
ATOM   2165 C  C   . ASN B  1 59  ? -13.760 14.091  34.710  1.00 9.53  ? 59   ASN B C   1 
ATOM   2166 O  O   . ASN B  1 59  ? -13.102 13.973  35.754  1.00 9.17  ? 59   ASN B O   1 
ATOM   2167 C  CB  . ASN B  1 59  ? -11.938 15.641  33.900  1.00 9.70  ? 59   ASN B CB  1 
ATOM   2168 C  CG  . ASN B  1 59  ? -11.313 16.334  32.711  1.00 7.27  ? 59   ASN B CG  1 
ATOM   2169 O  OD1 . ASN B  1 59  ? -11.757 16.150  31.573  1.00 7.41  ? 59   ASN B OD1 1 
ATOM   2170 N  ND2 . ASN B  1 59  ? -10.282 17.140  32.958  1.00 10.44 ? 59   ASN B ND2 1 
ATOM   2171 N  N   . GLU B  1 60  ? -14.964 13.555  34.551  1.00 7.93  ? 60   GLU B N   1 
ATOM   2172 C  CA  . GLU B  1 60  ? -15.605 12.794  35.624  1.00 7.53  ? 60   GLU B CA  1 
ATOM   2173 C  C   . GLU B  1 60  ? -14.872 11.455  35.815  1.00 7.12  ? 60   GLU B C   1 
ATOM   2174 O  O   . GLU B  1 60  ? -14.628 11.024  36.934  1.00 8.14  ? 60   GLU B O   1 
ATOM   2175 C  CB  . GLU B  1 60  ? -17.101 12.613  35.322  1.00 10.29 ? 60   GLU B CB  1 
ATOM   2176 C  CG  . GLU B  1 60  ? -17.913 11.961  36.429  1.00 8.13  ? 60   GLU B CG  1 
ATOM   2177 C  CD  . GLU B  1 60  ? -17.932 12.747  37.741  1.00 10.39 ? 60   GLU B CD  1 
ATOM   2178 O  OE1 . GLU B  1 60  ? -17.557 13.934  37.756  1.00 11.60 ? 60   GLU B OE1 1 
ATOM   2179 O  OE2 . GLU B  1 60  ? -18.332 12.157  38.768  1.00 10.90 ? 60   GLU B OE2 1 
ATOM   2180 N  N   . LEU B  1 61  ? -14.491 10.833  34.707  1.00 7.69  ? 61   LEU B N   1 
ATOM   2181 C  CA  . LEU B  1 61  ? -13.634 9.651   34.731  1.00 6.92  ? 61   LEU B CA  1 
ATOM   2182 C  C   . LEU B  1 61  ? -12.817 9.735   33.447  1.00 7.97  ? 61   LEU B C   1 
ATOM   2183 O  O   . LEU B  1 61  ? -13.367 9.686   32.355  1.00 10.51 ? 61   LEU B O   1 
ATOM   2184 C  CB  . LEU B  1 61  ? -14.491 8.375   34.789  1.00 7.64  ? 61   LEU B CB  1 
ATOM   2185 C  CG  . LEU B  1 61  ? -13.814 7.023   35.057  1.00 10.05 ? 61   LEU B CG  1 
ATOM   2186 C  CD1 . LEU B  1 61  ? -14.867 5.933   35.195  1.00 9.35  ? 61   LEU B CD1 1 
ATOM   2187 C  CD2 . LEU B  1 61  ? -12.822 6.652   33.959  1.00 10.41 ? 61   LEU B CD2 1 
ATOM   2188 N  N   . LEU B  1 62  ? -11.510 9.927   33.568  1.00 7.82  ? 62   LEU B N   1 
ATOM   2189 C  CA  . LEU B  1 62  ? -10.688 10.135  32.372  1.00 6.06  ? 62   LEU B CA  1 
ATOM   2190 C  C   . LEU B  1 62  ? -9.373  9.393   32.478  1.00 8.19  ? 62   LEU B C   1 
ATOM   2191 O  O   . LEU B  1 62  ? -8.677  9.512   33.485  1.00 9.05  ? 62   LEU B O   1 
ATOM   2192 C  CB  . LEU B  1 62  ? -10.396 11.623  32.193  1.00 7.78  ? 62   LEU B CB  1 
ATOM   2193 C  CG  . LEU B  1 62  ? -9.366  12.020  31.135  1.00 7.72  ? 62   LEU B CG  1 
ATOM   2194 C  CD1 . LEU B  1 62  ? -9.827  11.647  29.731  1.00 10.39 ? 62   LEU B CD1 1 
ATOM   2195 C  CD2 . LEU B  1 62  ? -9.105  13.535  31.230  1.00 7.73  ? 62   LEU B CD2 1 
ATOM   2196 N  N   . VAL B  1 63  ? -9.041  8.627   31.441  1.00 7.06  ? 63   VAL B N   1 
ATOM   2197 C  CA  . VAL B  1 63  ? -7.742  7.958   31.378  1.00 6.05  ? 63   VAL B CA  1 
ATOM   2198 C  C   . VAL B  1 63  ? -6.941  8.691   30.311  1.00 6.97  ? 63   VAL B C   1 
ATOM   2199 O  O   . VAL B  1 63  ? -7.352  8.759   29.142  1.00 10.04 ? 63   VAL B O   1 
ATOM   2200 C  CB  . VAL B  1 63  ? -7.880  6.470   31.003  1.00 7.41  ? 63   VAL B CB  1 
ATOM   2201 C  CG1 . VAL B  1 63  ? -6.488  5.820   30.965  1.00 8.36  ? 63   VAL B CG1 1 
ATOM   2202 C  CG2 . VAL B  1 63  ? -8.797  5.762   32.010  1.00 9.11  ? 63   VAL B CG2 1 
ATOM   2203 N  N   . TYR B  1 64  ? -5.818  9.270   30.724  1.00 6.26  ? 64   TYR B N   1 
ATOM   2204 C  CA  . TYR B  1 64  ? -5.104  10.236  29.898  1.00 7.85  ? 64   TYR B CA  1 
ATOM   2205 C  C   . TYR B  1 64  ? -3.623  9.914   29.904  1.00 11.09 ? 64   TYR B C   1 
ATOM   2206 O  O   . TYR B  1 64  ? -3.062  9.613   30.946  1.00 9.51  ? 64   TYR B O   1 
ATOM   2207 C  CB  . TYR B  1 64  ? -5.286  11.622  30.507  1.00 8.46  ? 64   TYR B CB  1 
ATOM   2208 C  CG  . TYR B  1 64  ? -4.935  12.781  29.601  1.00 8.54  ? 64   TYR B CG  1 
ATOM   2209 C  CD1 . TYR B  1 64  ? -5.767  13.136  28.542  1.00 9.84  ? 64   TYR B CD1 1 
ATOM   2210 C  CD2 . TYR B  1 64  ? -3.797  13.540  29.831  1.00 12.54 ? 64   TYR B CD2 1 
ATOM   2211 C  CE1 . TYR B  1 64  ? -5.464  14.213  27.726  1.00 9.22  ? 64   TYR B CE1 1 
ATOM   2212 C  CE2 . TYR B  1 64  ? -3.482  14.623  29.019  1.00 12.04 ? 64   TYR B CE2 1 
ATOM   2213 C  CZ  . TYR B  1 64  ? -4.322  14.953  27.977  1.00 13.19 ? 64   TYR B CZ  1 
ATOM   2214 O  OH  . TYR B  1 64  ? -4.005  16.018  27.173  1.00 13.23 ? 64   TYR B OH  1 
ATOM   2215 N  N   . LYS B  1 65  ? -2.992  10.017  28.738  1.00 9.55  ? 65   LYS B N   1 
ATOM   2216 C  CA  . LYS B  1 65  ? -1.562  9.763   28.596  1.00 9.49  ? 65   LYS B CA  1 
ATOM   2217 C  C   . LYS B  1 65  ? -0.843  11.085  28.327  1.00 9.75  ? 65   LYS B C   1 
ATOM   2218 O  O   . LYS B  1 65  ? -0.887  11.597  27.223  1.00 12.26 ? 65   LYS B O   1 
ATOM   2219 C  CB  . LYS B  1 65  ? -1.350  8.822   27.403  1.00 8.19  ? 65   LYS B CB  1 
ATOM   2220 C  CG  . LYS B  1 65  ? 0.066   8.269   27.253  1.00 11.17 ? 65   LYS B CG  1 
ATOM   2221 C  CD  . LYS B  1 65  ? 0.220   7.021   28.104  1.00 16.22 ? 65   LYS B CD  1 
ATOM   2222 C  CE  . LYS B  1 65  ? 1.636   6.479   28.044  1.00 12.42 ? 65   LYS B CE  1 
ATOM   2223 N  NZ  . LYS B  1 65  ? 2.033   6.145   26.655  1.00 15.65 ? 65   LYS B NZ  1 
ATOM   2224 N  N   A GLU B  1 66  ? -0.187  11.647  29.332  0.45 14.66 ? 66   GLU B N   1 
ATOM   2225 N  N   B GLU B  1 66  ? -0.193  11.645  29.347  0.55 14.67 ? 66   GLU B N   1 
ATOM   2226 C  CA  A GLU B  1 66  ? 0.443   12.947  29.142  0.45 14.69 ? 66   GLU B CA  1 
ATOM   2227 C  CA  B GLU B  1 66  ? 0.462   12.951  29.211  0.55 14.73 ? 66   GLU B CA  1 
ATOM   2228 C  C   A GLU B  1 66  ? 1.719   12.832  28.311  0.45 11.81 ? 66   GLU B C   1 
ATOM   2229 C  C   B GLU B  1 66  ? 1.754   12.864  28.391  0.55 11.75 ? 66   GLU B C   1 
ATOM   2230 O  O   A GLU B  1 66  ? 2.034   13.719  27.520  0.45 14.65 ? 66   GLU B O   1 
ATOM   2231 O  O   B GLU B  1 66  ? 2.112   13.805  27.688  0.55 14.66 ? 66   GLU B O   1 
ATOM   2232 C  CB  A GLU B  1 66  ? 0.758   13.594  30.485  0.45 23.41 ? 66   GLU B CB  1 
ATOM   2233 C  CB  B GLU B  1 66  ? 0.760   13.571  30.587  0.55 23.54 ? 66   GLU B CB  1 
ATOM   2234 C  CG  A GLU B  1 66  ? 1.624   12.732  31.373  0.45 22.09 ? 66   GLU B CG  1 
ATOM   2235 C  CG  B GLU B  1 66  ? -0.396  14.351  31.232  0.55 10.10 ? 66   GLU B CG  1 
ATOM   2236 C  CD  A GLU B  1 66  ? 0.830   11.937  32.391  0.45 20.19 ? 66   GLU B CD  1 
ATOM   2237 C  CD  B GLU B  1 66  ? -0.499  15.782  30.731  0.55 26.77 ? 66   GLU B CD  1 
ATOM   2238 O  OE1 A GLU B  1 66  ? 1.114   12.121  33.591  0.45 25.09 ? 66   GLU B OE1 1 
ATOM   2239 O  OE1 B GLU B  1 66  ? -1.317  16.548  31.293  0.55 34.78 ? 66   GLU B OE1 1 
ATOM   2240 O  OE2 A GLU B  1 66  ? -0.060  11.135  32.008  0.45 9.17  ? 66   GLU B OE2 1 
ATOM   2241 O  OE2 B GLU B  1 66  ? 0.235   16.141  29.783  0.55 26.76 ? 66   GLU B OE2 1 
ATOM   2242 N  N   . ARG B  1 67  ? 2.442   11.732  28.491  1.00 10.55 ? 67   ARG B N   1 
ATOM   2243 C  CA  . ARG B  1 67  ? 3.692   11.507  27.767  1.00 9.78  ? 67   ARG B CA  1 
ATOM   2244 C  C   . ARG B  1 67  ? 4.082   10.049  27.921  1.00 11.94 ? 67   ARG B C   1 
ATOM   2245 O  O   . ARG B  1 67  ? 3.470   9.310   28.697  1.00 10.87 ? 67   ARG B O   1 
ATOM   2246 C  CB  . ARG B  1 67  ? 4.803   12.397  28.327  1.00 10.40 ? 67   ARG B CB  1 
ATOM   2247 C  CG  . ARG B  1 67  ? 5.091   12.153  29.800  1.00 11.88 ? 67   ARG B CG  1 
ATOM   2248 C  CD  . ARG B  1 67  ? 6.143   13.108  30.352  1.00 23.27 ? 67   ARG B CD  1 
ATOM   2249 N  NE  . ARG B  1 67  ? 5.750   14.494  30.134  1.00 23.10 ? 67   ARG B NE  1 
ATOM   2250 C  CZ  . ARG B  1 67  ? 4.913   15.171  30.910  1.00 28.16 ? 67   ARG B CZ  1 
ATOM   2251 N  NH1 . ARG B  1 67  ? 4.376   14.597  31.979  1.00 26.54 ? 67   ARG B NH1 1 
ATOM   2252 N  NH2 . ARG B  1 67  ? 4.615   16.431  30.618  1.00 35.98 ? 67   ARG B NH2 1 
ATOM   2253 N  N   . VAL B  1 68  ? 5.113   9.631   27.195  1.00 12.70 ? 68   VAL B N   1 
ATOM   2254 C  CA  . VAL B  1 68  ? 5.562   8.257   27.255  1.00 7.84  ? 68   VAL B CA  1 
ATOM   2255 C  C   . VAL B  1 68  ? 5.882   7.839   28.704  1.00 9.91  ? 68   VAL B C   1 
ATOM   2256 O  O   . VAL B  1 68  ? 6.456   8.613   29.480  1.00 12.91 ? 68   VAL B O   1 
ATOM   2257 C  CB  . VAL B  1 68  ? 6.773   8.027   26.305  1.00 12.54 ? 68   VAL B CB  1 
ATOM   2258 C  CG1 . VAL B  1 68  ? 7.976   8.847   26.758  1.00 15.44 ? 68   VAL B CG1 1 
ATOM   2259 C  CG2 . VAL B  1 68  ? 7.126   6.547   26.230  1.00 13.56 ? 68   VAL B CG2 1 
ATOM   2260 N  N   . GLY B  1 69  ? 5.450   6.637   29.074  1.00 8.42  ? 69   GLY B N   1 
ATOM   2261 C  CA  . GLY B  1 69  ? 5.752   6.093   30.389  1.00 13.64 ? 69   GLY B CA  1 
ATOM   2262 C  C   . GLY B  1 69  ? 4.929   6.639   31.546  1.00 13.49 ? 69   GLY B C   1 
ATOM   2263 O  O   . GLY B  1 69  ? 5.224   6.349   32.701  1.00 12.55 ? 69   GLY B O   1 
ATOM   2264 N  N   . GLU B  1 70  ? 3.901   7.433   31.258  1.00 10.37 ? 70   GLU B N   1 
ATOM   2265 C  CA  . GLU B  1 70  ? 3.110   8.036   32.335  1.00 11.65 ? 70   GLU B CA  1 
ATOM   2266 C  C   . GLU B  1 70  ? 1.615   7.951   32.054  1.00 12.00 ? 70   GLU B C   1 
ATOM   2267 O  O   . GLU B  1 70  ? 1.127   8.479   31.048  1.00 12.57 ? 70   GLU B O   1 
ATOM   2268 C  CB  . GLU B  1 70  ? 3.509   9.504   32.555  1.00 14.34 ? 70   GLU B CB  1 
ATOM   2269 C  CG  . GLU B  1 70  ? 4.993   9.691   32.825  1.00 16.04 ? 70   GLU B CG  1 
ATOM   2270 C  CD  . GLU B  1 70  ? 5.333   11.098  33.270  1.00 23.71 ? 70   GLU B CD  1 
ATOM   2271 O  OE1 . GLU B  1 70  ? 4.443   11.972  33.248  1.00 18.22 ? 70   GLU B OE1 1 
ATOM   2272 O  OE2 . GLU B  1 70  ? 6.501   11.323  33.643  1.00 31.21 ? 70   GLU B OE2 1 
ATOM   2273 N  N   . TYR B  1 71  ? 0.891   7.293   32.952  1.00 10.07 ? 71   TYR B N   1 
ATOM   2274 C  CA  . TYR B  1 71  ? -0.551  7.138   32.806  1.00 8.45  ? 71   TYR B CA  1 
ATOM   2275 C  C   . TYR B  1 71  ? -1.285  7.908   33.894  1.00 9.02  ? 71   TYR B C   1 
ATOM   2276 O  O   . TYR B  1 71  ? -0.934  7.815   35.069  1.00 9.26  ? 71   TYR B O   1 
ATOM   2277 C  CB  . TYR B  1 71  ? -0.939  5.663   32.873  1.00 10.08 ? 71   TYR B CB  1 
ATOM   2278 C  CG  . TYR B  1 71  ? -0.427  4.906   31.688  1.00 9.49  ? 71   TYR B CG  1 
ATOM   2279 C  CD1 . TYR B  1 71  ? -1.214  4.744   30.567  1.00 8.47  ? 71   TYR B CD1 1 
ATOM   2280 C  CD2 . TYR B  1 71  ? 0.874   4.406   31.672  1.00 9.45  ? 71   TYR B CD2 1 
ATOM   2281 C  CE1 . TYR B  1 71  ? -0.734  4.070   29.449  1.00 9.43  ? 71   TYR B CE1 1 
ATOM   2282 C  CE2 . TYR B  1 71  ? 1.366   3.740   30.571  1.00 11.31 ? 71   TYR B CE2 1 
ATOM   2283 C  CZ  . TYR B  1 71  ? 0.552   3.570   29.465  1.00 11.81 ? 71   TYR B CZ  1 
ATOM   2284 O  OH  . TYR B  1 71  ? 1.028   2.914   28.363  1.00 12.67 ? 71   TYR B OH  1 
ATOM   2285 N  N   . SER B  1 72  ? -2.321  8.654   33.516  1.00 8.50  ? 72   SER B N   1 
ATOM   2286 C  CA  . SER B  1 72  ? -3.109  9.407   34.498  1.00 9.10  ? 72   SER B CA  1 
ATOM   2287 C  C   . SER B  1 72  ? -4.555  8.938   34.560  1.00 7.83  ? 72   SER B C   1 
ATOM   2288 O  O   . SER B  1 72  ? -5.168  8.635   33.534  1.00 8.13  ? 72   SER B O   1 
ATOM   2289 C  CB  . SER B  1 72  ? -3.132  10.905  34.158  1.00 7.51  ? 72   SER B CB  1 
ATOM   2290 O  OG  . SER B  1 72  ? -1.848  11.499  34.259  1.00 9.25  ? 72   SER B OG  1 
ATOM   2291 N  N   . LEU B  1 73  ? -5.098  8.900   35.769  1.00 6.65  ? 73   LEU B N   1 
ATOM   2292 C  CA  . LEU B  1 73  ? -6.531  8.707   35.957  1.00 7.13  ? 73   LEU B CA  1 
ATOM   2293 C  C   . LEU B  1 73  ? -7.123  9.950   36.621  1.00 7.70  ? 73   LEU B C   1 
ATOM   2294 O  O   . LEU B  1 73  ? -6.616  10.414  37.645  1.00 9.53  ? 73   LEU B O   1 
ATOM   2295 C  CB  . LEU B  1 73  ? -6.794  7.494   36.846  1.00 8.47  ? 73   LEU B CB  1 
ATOM   2296 C  CG  . LEU B  1 73  ? -8.260  7.283   37.205  1.00 6.89  ? 73   LEU B CG  1 
ATOM   2297 C  CD1 . LEU B  1 73  ? -9.082  6.879   35.972  1.00 10.66 ? 73   LEU B CD1 1 
ATOM   2298 C  CD2 . LEU B  1 73  ? -8.393  6.236   38.325  1.00 8.36  ? 73   LEU B CD2 1 
ATOM   2299 N  N   . TYR B  1 74  ? -8.211  10.464  36.046  1.00 7.75  ? 74   TYR B N   1 
ATOM   2300 C  CA  . TYR B  1 74  ? -8.972  11.531  36.679  1.00 7.77  ? 74   TYR B CA  1 
ATOM   2301 C  C   . TYR B  1 74  ? -10.254 10.934  37.220  1.00 7.46  ? 74   TYR B C   1 
ATOM   2302 O  O   . TYR B  1 74  ? -10.914 10.179  36.521  1.00 7.43  ? 74   TYR B O   1 
ATOM   2303 C  CB  . TYR B  1 74  ? -9.369  12.604  35.657  1.00 6.47  ? 74   TYR B CB  1 
ATOM   2304 C  CG  . TYR B  1 74  ? -8.230  13.436  35.138  1.00 11.84 ? 74   TYR B CG  1 
ATOM   2305 C  CD1 . TYR B  1 74  ? -7.270  12.885  34.301  1.00 8.79  ? 74   TYR B CD1 1 
ATOM   2306 C  CD2 . TYR B  1 74  ? -8.124  14.785  35.468  1.00 12.59 ? 74   TYR B CD2 1 
ATOM   2307 C  CE1 . TYR B  1 74  ? -6.238  13.650  33.813  1.00 11.70 ? 74   TYR B CE1 1 
ATOM   2308 C  CE2 . TYR B  1 74  ? -7.088  15.555  34.979  1.00 12.80 ? 74   TYR B CE2 1 
ATOM   2309 C  CZ  . TYR B  1 74  ? -6.151  14.979  34.163  1.00 16.60 ? 74   TYR B CZ  1 
ATOM   2310 O  OH  . TYR B  1 74  ? -5.119  15.742  33.676  1.00 20.08 ? 74   TYR B OH  1 
ATOM   2311 N  N   . ILE B  1 75  ? -10.593 11.262  38.466  1.00 7.99  ? 75   ILE B N   1 
ATOM   2312 C  CA  . ILE B  1 75  ? -11.900 10.935  39.020  1.00 7.55  ? 75   ILE B CA  1 
ATOM   2313 C  C   . ILE B  1 75  ? -12.473 12.248  39.524  1.00 8.85  ? 75   ILE B C   1 
ATOM   2314 O  O   . ILE B  1 75  ? -11.889 12.887  40.406  1.00 9.53  ? 75   ILE B O   1 
ATOM   2315 C  CB  . ILE B  1 75  ? -11.814 9.958   40.226  1.00 7.86  ? 75   ILE B CB  1 
ATOM   2316 C  CG1 . ILE B  1 75  ? -11.239 8.598   39.812  1.00 8.07  ? 75   ILE B CG1 1 
ATOM   2317 C  CG2 . ILE B  1 75  ? -13.200 9.775   40.882  1.00 8.41  ? 75   ILE B CG2 1 
ATOM   2318 C  CD1 . ILE B  1 75  ? -12.118 7.816   38.861  1.00 9.22  ? 75   ILE B CD1 1 
ATOM   2319 N  N   . GLY B  1 76  ? -13.598 12.672  38.959  1.00 9.61  ? 76   GLY B N   1 
ATOM   2320 C  CA  . GLY B  1 76  ? -14.219 13.904  39.411  1.00 8.22  ? 76   GLY B CA  1 
ATOM   2321 C  C   . GLY B  1 76  ? -13.252 15.071  39.424  1.00 8.01  ? 76   GLY B C   1 
ATOM   2322 O  O   . GLY B  1 76  ? -13.146 15.801  40.410  1.00 10.16 ? 76   GLY B O   1 
ATOM   2323 N  N   . ARG B  1 77  ? -12.543 15.231  38.313  1.00 7.79  ? 77   ARG B N   1 
ATOM   2324 C  CA  . ARG B  1 77  ? -11.599 16.329  38.105  1.00 10.98 ? 77   ARG B CA  1 
ATOM   2325 C  C   . ARG B  1 77  ? -10.268 16.233  38.859  1.00 11.41 ? 77   ARG B C   1 
ATOM   2326 O  O   . ARG B  1 77  ? -9.303  16.891  38.474  1.00 19.17 ? 77   ARG B O   1 
ATOM   2327 C  CB  . ARG B  1 77  ? -12.297 17.686  38.310  1.00 10.30 ? 77   ARG B CB  1 
ATOM   2328 C  CG  . ARG B  1 77  ? -13.338 17.942  37.224  1.00 10.51 ? 77   ARG B CG  1 
ATOM   2329 C  CD  . ARG B  1 77  ? -14.576 18.687  37.750  1.00 9.75  ? 77   ARG B CD  1 
ATOM   2330 N  NE  . ARG B  1 77  ? -15.272 17.954  38.820  1.00 10.11 ? 77   ARG B NE  1 
ATOM   2331 C  CZ  . ARG B  1 77  ? -15.988 16.846  38.639  1.00 9.74  ? 77   ARG B CZ  1 
ATOM   2332 N  NH1 . ARG B  1 77  ? -16.101 16.317  37.427  1.00 8.24  ? 77   ARG B NH1 1 
ATOM   2333 N  NH2 . ARG B  1 77  ? -16.594 16.257  39.672  1.00 10.85 ? 77   ARG B NH2 1 
ATOM   2334 N  N   . HIS B  1 78  ? -10.192 15.404  39.898  1.00 9.27  ? 78   HIS B N   1 
ATOM   2335 C  CA  . HIS B  1 78  ? -8.911  15.170  40.569  1.00 9.09  ? 78   HIS B CA  1 
ATOM   2336 C  C   . HIS B  1 78  ? -8.111  14.143  39.781  1.00 11.30 ? 78   HIS B C   1 
ATOM   2337 O  O   . HIS B  1 78  ? -8.694  13.303  39.099  1.00 11.30 ? 78   HIS B O   1 
ATOM   2338 C  CB  . HIS B  1 78  ? -9.136  14.637  41.979  1.00 9.09  ? 78   HIS B CB  1 
ATOM   2339 C  CG  . HIS B  1 78  ? -9.902  15.576  42.859  1.00 10.65 ? 78   HIS B CG  1 
ATOM   2340 N  ND1 . HIS B  1 78  ? -10.000 15.402  44.222  1.00 14.40 ? 78   HIS B ND1 1 
ATOM   2341 C  CD2 . HIS B  1 78  ? -10.595 16.705  42.569  1.00 15.58 ? 78   HIS B CD2 1 
ATOM   2342 C  CE1 . HIS B  1 78  ? -10.735 16.376  44.734  1.00 16.16 ? 78   HIS B CE1 1 
ATOM   2343 N  NE2 . HIS B  1 78  ? -11.104 17.181  43.755  1.00 15.74 ? 78   HIS B NE2 1 
ATOM   2344 N  N   . LYS B  1 79  ? -6.786  14.202  39.869  1.00 8.52  ? 79   LYS B N   1 
ATOM   2345 C  CA  . LYS B  1 79  ? -5.985  13.274  39.077  1.00 10.26 ? 79   LYS B CA  1 
ATOM   2346 C  C   . LYS B  1 79  ? -4.864  12.622  39.870  1.00 11.91 ? 79   LYS B C   1 
ATOM   2347 O  O   . LYS B  1 79  ? -4.333  13.202  40.834  1.00 10.64 ? 79   LYS B O   1 
ATOM   2348 C  CB  . LYS B  1 79  ? -5.391  13.981  37.862  1.00 16.49 ? 79   LYS B CB  1 
ATOM   2349 C  CG  . LYS B  1 79  ? -4.292  14.945  38.205  1.00 20.30 ? 79   LYS B CG  1 
ATOM   2350 C  CD  . LYS B  1 79  ? -3.768  15.649  36.954  1.00 28.08 ? 79   LYS B CD  1 
ATOM   2351 C  CE  . LYS B  1 79  ? -3.086  14.671  36.013  1.00 26.12 ? 79   LYS B CE  1 
ATOM   2352 N  NZ  . LYS B  1 79  ? -2.535  15.352  34.802  1.00 39.35 ? 79   LYS B NZ  1 
ATOM   2353 N  N   . VAL B  1 80  ? -4.528  11.406  39.455  1.00 10.37 ? 80   VAL B N   1 
ATOM   2354 C  CA  . VAL B  1 80  ? -3.296  10.749  39.879  1.00 9.84  ? 80   VAL B CA  1 
ATOM   2355 C  C   . VAL B  1 80  ? -2.546  10.273  38.642  1.00 8.45  ? 80   VAL B C   1 
ATOM   2356 O  O   . VAL B  1 80  ? -3.137  10.066  37.576  1.00 8.12  ? 80   VAL B O   1 
ATOM   2357 C  CB  . VAL B  1 80  ? -3.568  9.564   40.809  1.00 8.87  ? 80   VAL B CB  1 
ATOM   2358 C  CG1 . VAL B  1 80  ? -4.169  10.056  42.139  1.00 9.12  ? 80   VAL B CG1 1 
ATOM   2359 C  CG2 . VAL B  1 80  ? -4.489  8.552   40.139  1.00 8.07  ? 80   VAL B CG2 1 
ATOM   2360 N  N   . THR B  1 81  ? -1.233  10.114  38.783  1.00 9.40  ? 81   THR B N   1 
ATOM   2361 C  CA  . THR B  1 81  ? -0.389  9.670   37.673  1.00 7.77  ? 81   THR B CA  1 
ATOM   2362 C  C   . THR B  1 81  ? 0.617   8.657   38.197  1.00 6.75  ? 81   THR B C   1 
ATOM   2363 O  O   . THR B  1 81  ? 1.201   8.859   39.266  1.00 9.62  ? 81   THR B O   1 
ATOM   2364 C  CB  . THR B  1 81  ? 0.392   10.843  37.070  1.00 7.34  ? 81   THR B CB  1 
ATOM   2365 O  OG1 . THR B  1 81  ? -0.530  11.830  36.588  1.00 11.59 ? 81   THR B OG1 1 
ATOM   2366 C  CG2 . THR B  1 81  ? 1.269   10.373  35.919  1.00 12.37 ? 81   THR B CG2 1 
ATOM   2367 N  N   . SER B  1 82  ? 0.805   7.568   37.460  1.00 8.12  ? 82   SER B N   1 
ATOM   2368 C  CA  . SER B  1 82  ? 1.839   6.606   37.812  1.00 7.03  ? 82   SER B CA  1 
ATOM   2369 C  C   . SER B  1 82  ? 2.698   6.297   36.601  1.00 8.94  ? 82   SER B C   1 
ATOM   2370 O  O   . SER B  1 82  ? 2.258   6.414   35.444  1.00 9.77  ? 82   SER B O   1 
ATOM   2371 C  CB  . SER B  1 82  ? 1.245   5.323   38.410  1.00 12.15 ? 82   SER B CB  1 
ATOM   2372 O  OG  . SER B  1 82  ? 0.812   5.557   39.745  1.00 13.32 ? 82   SER B OG  1 
ATOM   2373 N  N   . LYS B  1 83  ? 3.933   5.897   36.880  1.00 9.78  ? 83   LYS B N   1 
ATOM   2374 C  CA  . LYS B  1 83  ? 4.944   5.767   35.842  1.00 7.93  ? 83   LYS B CA  1 
ATOM   2375 C  C   . LYS B  1 83  ? 5.275   4.318   35.566  1.00 9.67  ? 83   LYS B C   1 
ATOM   2376 O  O   . LYS B  1 83  ? 5.113   3.451   36.429  1.00 10.21 ? 83   LYS B O   1 
ATOM   2377 C  CB  . LYS B  1 83  ? 6.223   6.492   36.255  1.00 6.65  ? 83   LYS B CB  1 
ATOM   2378 C  CG  . LYS B  1 83  ? 6.093   7.991   36.406  1.00 16.61 ? 83   LYS B CG  1 
ATOM   2379 C  CD  . LYS B  1 83  ? 7.440   8.600   36.802  1.00 18.16 ? 83   LYS B CD  1 
ATOM   2380 C  CE  . LYS B  1 83  ? 7.260   9.938   37.512  1.00 32.23 ? 83   LYS B CE  1 
ATOM   2381 N  NZ  . LYS B  1 83  ? 8.460   10.323  38.328  1.00 35.42 ? 83   LYS B NZ  1 
ATOM   2382 N  N   . VAL B  1 84  ? 5.759   4.058   34.359  1.00 8.05  ? 84   VAL B N   1 
ATOM   2383 C  CA  . VAL B  1 84  ? 6.125   2.697   34.004  1.00 9.15  ? 84   VAL B CA  1 
ATOM   2384 C  C   . VAL B  1 84  ? 7.221   2.707   32.955  1.00 10.70 ? 84   VAL B C   1 
ATOM   2385 O  O   . VAL B  1 84  ? 7.334   3.643   32.171  1.00 11.34 ? 84   VAL B O   1 
ATOM   2386 C  CB  . VAL B  1 84  ? 4.904   1.932   33.457  1.00 11.23 ? 84   VAL B CB  1 
ATOM   2387 C  CG1 . VAL B  1 84  ? 4.488   2.500   32.098  1.00 13.49 ? 84   VAL B CG1 1 
ATOM   2388 C  CG2 . VAL B  1 84  ? 5.205   0.433   33.350  1.00 14.13 ? 84   VAL B CG2 1 
ATOM   2389 N  N   . ILE B  1 85  ? 8.036   1.658   32.948  1.00 8.69  ? 85   ILE B N   1 
ATOM   2390 C  CA  . ILE B  1 85  ? 9.014   1.474   31.893  1.00 12.71 ? 85   ILE B CA  1 
ATOM   2391 C  C   . ILE B  1 85  ? 8.333   0.829   30.697  1.00 9.86  ? 85   ILE B C   1 
ATOM   2392 O  O   . ILE B  1 85  ? 7.795   -0.275  30.805  1.00 11.84 ? 85   ILE B O   1 
ATOM   2393 C  CB  . ILE B  1 85  ? 10.155  0.549   32.348  1.00 12.33 ? 85   ILE B CB  1 
ATOM   2394 C  CG1 . ILE B  1 85  ? 10.973  1.218   33.454  1.00 13.33 ? 85   ILE B CG1 1 
ATOM   2395 C  CG2 . ILE B  1 85  ? 11.030  0.197   31.159  1.00 13.39 ? 85   ILE B CG2 1 
ATOM   2396 C  CD1 . ILE B  1 85  ? 11.804  0.232   34.275  1.00 16.30 ? 85   ILE B CD1 1 
ATOM   2397 N  N   A GLU B  1 86  ? 8.355   1.519   29.558  0.56 12.49 ? 86   GLU B N   1 
ATOM   2398 N  N   B GLU B  1 86  ? 8.363   1.517   29.563  0.44 12.49 ? 86   GLU B N   1 
ATOM   2399 C  CA  A GLU B  1 86  ? 7.740   0.999   28.333  0.56 13.08 ? 86   GLU B CA  1 
ATOM   2400 C  CA  B GLU B  1 86  ? 7.795   0.982   28.332  0.44 13.08 ? 86   GLU B CA  1 
ATOM   2401 C  C   A GLU B  1 86  ? 8.527   1.390   27.088  0.56 13.27 ? 86   GLU B C   1 
ATOM   2402 C  C   B GLU B  1 86  ? 8.693   1.286   27.153  0.44 13.23 ? 86   GLU B C   1 
ATOM   2403 O  O   A GLU B  1 86  ? 9.104   2.473   27.030  0.56 15.53 ? 86   GLU B O   1 
ATOM   2404 O  O   B GLU B  1 86  ? 9.505   2.204   27.200  0.44 14.77 ? 86   GLU B O   1 
ATOM   2405 C  CB  A GLU B  1 86  ? 6.279   1.464   28.201  0.56 14.71 ? 86   GLU B CB  1 
ATOM   2406 C  CB  B GLU B  1 86  ? 6.406   1.570   28.065  0.44 14.66 ? 86   GLU B CB  1 
ATOM   2407 C  CG  A GLU B  1 86  ? 6.081   2.977   28.020  0.56 11.28 ? 86   GLU B CG  1 
ATOM   2408 C  CG  B GLU B  1 86  ? 5.248   0.715   28.543  0.44 15.58 ? 86   GLU B CG  1 
ATOM   2409 C  CD  A GLU B  1 86  ? 4.608   3.365   27.917  0.56 14.27 ? 86   GLU B CD  1 
ATOM   2410 C  CD  B GLU B  1 86  ? 3.909   1.260   28.087  0.44 14.00 ? 86   GLU B CD  1 
ATOM   2411 O  OE1 A GLU B  1 86  ? 3.753   2.516   28.257  0.56 12.40 ? 86   GLU B OE1 1 
ATOM   2412 O  OE1 B GLU B  1 86  ? 3.462   2.281   28.647  0.44 10.59 ? 86   GLU B OE1 1 
ATOM   2413 O  OE2 A GLU B  1 86  ? 4.305   4.509   27.493  0.56 6.11  ? 86   GLU B OE2 1 
ATOM   2414 O  OE2 B GLU B  1 86  ? 3.303   0.661   27.175  0.44 11.85 ? 86   GLU B OE2 1 
ATOM   2415 N  N   . LYS B  1 87  ? 8.538   0.500   26.095  1.00 14.44 ? 87   LYS B N   1 
ATOM   2416 C  CA  . LYS B  1 87  ? 9.189   0.787   24.826  1.00 16.03 ? 87   LYS B CA  1 
ATOM   2417 C  C   . LYS B  1 87  ? 8.265   1.701   24.037  1.00 14.34 ? 87   LYS B C   1 
ATOM   2418 O  O   . LYS B  1 87  ? 7.056   1.735   24.287  1.00 15.67 ? 87   LYS B O   1 
ATOM   2419 C  CB  . LYS B  1 87  ? 9.428   -0.508  24.051  1.00 18.08 ? 87   LYS B CB  1 
ATOM   2420 C  CG  . LYS B  1 87  ? 10.372  -1.472  24.759  1.00 25.18 ? 87   LYS B CG  1 
ATOM   2421 C  CD  . LYS B  1 87  ? 10.508  -2.781  24.001  1.00 39.55 ? 87   LYS B CD  1 
ATOM   2422 C  CE  . LYS B  1 87  ? 11.446  -3.734  24.733  1.00 46.56 ? 87   LYS B CE  1 
ATOM   2423 N  NZ  . LYS B  1 87  ? 11.474  -5.090  24.112  1.00 59.60 ? 87   LYS B NZ  1 
ATOM   2424 N  N   . PHE B  1 88  ? 8.837   2.461   23.112  1.00 13.25 ? 88   PHE B N   1 
ATOM   2425 C  CA  . PHE B  1 88  ? 8.044   3.346   22.276  1.00 12.35 ? 88   PHE B CA  1 
ATOM   2426 C  C   . PHE B  1 88  ? 8.534   3.328   20.841  1.00 10.13 ? 88   PHE B C   1 
ATOM   2427 O  O   . PHE B  1 88  ? 9.725   3.515   20.591  1.00 13.23 ? 88   PHE B O   1 
ATOM   2428 C  CB  . PHE B  1 88  ? 8.119   4.786   22.777  1.00 15.13 ? 88   PHE B CB  1 
ATOM   2429 C  CG  . PHE B  1 88  ? 7.479   5.763   21.835  1.00 12.92 ? 88   PHE B CG  1 
ATOM   2430 C  CD1 . PHE B  1 88  ? 6.103   5.931   21.831  1.00 14.43 ? 88   PHE B CD1 1 
ATOM   2431 C  CD2 . PHE B  1 88  ? 8.243   6.463   20.921  1.00 12.84 ? 88   PHE B CD2 1 
ATOM   2432 C  CE1 . PHE B  1 88  ? 5.503   6.798   20.937  1.00 12.91 ? 88   PHE B CE1 1 
ATOM   2433 C  CE2 . PHE B  1 88  ? 7.656   7.336   20.025  1.00 17.49 ? 88   PHE B CE2 1 
ATOM   2434 C  CZ  . PHE B  1 88  ? 6.282   7.509   20.036  1.00 14.83 ? 88   PHE B CZ  1 
ATOM   2435 N  N   . PRO B  1 89  ? 7.615   3.135   19.882  1.00 9.68  ? 89   PRO B N   1 
ATOM   2436 C  CA  . PRO B  1 89  ? 6.195   2.820   20.062  1.00 10.61 ? 89   PRO B CA  1 
ATOM   2437 C  C   . PRO B  1 89  ? 6.027   1.356   20.420  1.00 11.45 ? 89   PRO B C   1 
ATOM   2438 O  O   . PRO B  1 89  ? 6.876   0.536   20.065  1.00 12.78 ? 89   PRO B O   1 
ATOM   2439 C  CB  . PRO B  1 89  ? 5.591   3.052   18.663  1.00 10.28 ? 89   PRO B CB  1 
ATOM   2440 C  CG  . PRO B  1 89  ? 6.640   3.704   17.859  1.00 14.33 ? 89   PRO B CG  1 
ATOM   2441 C  CD  . PRO B  1 89  ? 7.953   3.373   18.469  1.00 10.26 ? 89   PRO B CD  1 
ATOM   2442 N  N   . ALA B  1 90  ? 4.945   1.027   21.109  1.00 9.75  ? 90   ALA B N   1 
ATOM   2443 C  CA  . ALA B  1 90  ? 4.637   -0.366  21.384  1.00 11.62 ? 90   ALA B CA  1 
ATOM   2444 C  C   . ALA B  1 90  ? 3.173   -0.527  21.735  1.00 7.27  ? 90   ALA B C   1 
ATOM   2445 O  O   . ALA B  1 90  ? 2.599   0.327   22.405  1.00 11.69 ? 90   ALA B O   1 
ATOM   2446 C  CB  . ALA B  1 90  ? 5.502   -0.901  22.519  1.00 15.10 ? 90   ALA B CB  1 
ATOM   2447 N  N   . PRO B  1 91  ? 2.571   -1.637  21.300  1.00 7.96  ? 91   PRO B N   1 
ATOM   2448 C  CA  . PRO B  1 91  ? 1.219   -1.944  21.759  1.00 9.40  ? 91   PRO B CA  1 
ATOM   2449 C  C   . PRO B  1 91  ? 1.222   -2.076  23.271  1.00 12.30 ? 91   PRO B C   1 
ATOM   2450 O  O   . PRO B  1 91  ? 2.229   -2.485  23.860  1.00 13.67 ? 91   PRO B O   1 
ATOM   2451 C  CB  . PRO B  1 91  ? 0.933   -3.315  21.130  1.00 11.80 ? 91   PRO B CB  1 
ATOM   2452 C  CG  . PRO B  1 91  ? 1.859   -3.408  19.960  1.00 12.90 ? 91   PRO B CG  1 
ATOM   2453 C  CD  . PRO B  1 91  ? 3.087   -2.648  20.356  1.00 12.16 ? 91   PRO B CD  1 
ATOM   2454 N  N   . VAL B  1 92  ? 0.102   -1.746  23.898  1.00 10.37 ? 92   VAL B N   1 
ATOM   2455 C  CA  . VAL B  1 92  ? 0.013   -1.855  25.345  1.00 10.05 ? 92   VAL B CA  1 
ATOM   2456 C  C   . VAL B  1 92  ? -1.342  -2.426  25.744  1.00 9.26  ? 92   VAL B C   1 
ATOM   2457 O  O   . VAL B  1 92  ? -2.336  -2.211  25.056  1.00 10.61 ? 92   VAL B O   1 
ATOM   2458 C  CB  . VAL B  1 92  ? 0.216   -0.473  26.000  1.00 8.30  ? 92   VAL B CB  1 
ATOM   2459 C  CG1 . VAL B  1 92  ? -0.946  0.466   25.641  1.00 12.15 ? 92   VAL B CG1 1 
ATOM   2460 C  CG2 . VAL B  1 92  ? 0.360   -0.606  27.506  1.00 13.48 ? 92   VAL B CG2 1 
ATOM   2461 N  N   . HIS B  1 93  ? -1.371  -3.185  26.836  1.00 8.03  ? 93   HIS B N   1 
ATOM   2462 C  CA  . HIS B  1 93  ? -2.638  -3.532  27.466  1.00 9.04  ? 93   HIS B CA  1 
ATOM   2463 C  C   . HIS B  1 93  ? -2.735  -2.743  28.761  1.00 9.18  ? 93   HIS B C   1 
ATOM   2464 O  O   . HIS B  1 93  ? -1.795  -2.727  29.555  1.00 8.94  ? 93   HIS B O   1 
ATOM   2465 C  CB  . HIS B  1 93  ? -2.730  -5.032  27.745  1.00 9.20  ? 93   HIS B CB  1 
ATOM   2466 C  CG  . HIS B  1 93  ? -4.033  -5.437  28.360  1.00 6.51  ? 93   HIS B CG  1 
ATOM   2467 N  ND1 . HIS B  1 93  ? -4.199  -5.581  29.721  1.00 9.88  ? 93   HIS B ND1 1 
ATOM   2468 C  CD2 . HIS B  1 93  ? -5.240  -5.685  27.800  1.00 10.95 ? 93   HIS B CD2 1 
ATOM   2469 C  CE1 . HIS B  1 93  ? -5.453  -5.925  29.968  1.00 11.92 ? 93   HIS B CE1 1 
ATOM   2470 N  NE2 . HIS B  1 93  ? -6.105  -5.988  28.824  1.00 11.03 ? 93   HIS B NE2 1 
ATOM   2471 N  N   . ILE B  1 94  ? -3.854  -2.049  28.952  1.00 8.49  ? 94   ILE B N   1 
ATOM   2472 C  CA  . ILE B  1 94  ? -4.015  -1.187  30.115  1.00 10.51 ? 94   ILE B CA  1 
ATOM   2473 C  C   . ILE B  1 94  ? -5.233  -1.625  30.902  1.00 10.30 ? 94   ILE B C   1 
ATOM   2474 O  O   . ILE B  1 94  ? -6.298  -1.862  30.337  1.00 11.74 ? 94   ILE B O   1 
ATOM   2475 C  CB  . ILE B  1 94  ? -4.224  0.280   29.693  1.00 8.87  ? 94   ILE B CB  1 
ATOM   2476 C  CG1 . ILE B  1 94  ? -2.980  0.821   28.982  1.00 12.40 ? 94   ILE B CG1 1 
ATOM   2477 C  CG2 . ILE B  1 94  ? -4.634  1.148   30.908  1.00 11.97 ? 94   ILE B CG2 1 
ATOM   2478 C  CD1 . ILE B  1 94  ? -3.288  1.960   28.017  1.00 11.39 ? 94   ILE B CD1 1 
ATOM   2479 N  N   . CYS B  1 95  ? -5.064  -1.762  32.211  1.00 8.13  ? 95   CYS B N   1 
ATOM   2480 C  CA  . CYS B  1 95  ? -6.198  -1.921  33.099  1.00 9.64  ? 95   CYS B CA  1 
ATOM   2481 C  C   . CYS B  1 95  ? -6.074  -0.833  34.147  1.00 9.37  ? 95   CYS B C   1 
ATOM   2482 O  O   . CYS B  1 95  ? -4.975  -0.524  34.603  1.00 11.70 ? 95   CYS B O   1 
ATOM   2483 C  CB  . CYS B  1 95  ? -6.166  -3.293  33.776  1.00 14.52 ? 95   CYS B CB  1 
ATOM   2484 S  SG  . CYS B  1 95  ? -6.803  -4.675  32.774  1.00 20.82 ? 95   CYS B SG  1 
ATOM   2485 N  N   . VAL B  1 96  ? -7.193  -0.225  34.519  1.00 7.88  ? 96   VAL B N   1 
ATOM   2486 C  CA  . VAL B  1 96  ? -7.190  0.698   35.650  1.00 9.34  ? 96   VAL B CA  1 
ATOM   2487 C  C   . VAL B  1 96  ? -8.452  0.451   36.478  1.00 9.01  ? 96   VAL B C   1 
ATOM   2488 O  O   . VAL B  1 96  ? -9.533  0.268   35.928  1.00 10.15 ? 96   VAL B O   1 
ATOM   2489 C  CB  . VAL B  1 96  ? -7.035  2.194   35.217  1.00 11.79 ? 96   VAL B CB  1 
ATOM   2490 C  CG1 . VAL B  1 96  ? -8.163  2.622   34.289  1.00 13.85 ? 96   VAL B CG1 1 
ATOM   2491 C  CG2 . VAL B  1 96  ? -6.930  3.099   36.440  1.00 11.38 ? 96   VAL B CG2 1 
ATOM   2492 N  N   . SER B  1 97  ? -8.297  0.375   37.797  1.00 10.61 ? 97   SER B N   1 
ATOM   2493 C  CA  . SER B  1 97  ? -9.452  0.217   38.683  1.00 8.48  ? 97   SER B CA  1 
ATOM   2494 C  C   . SER B  1 97  ? -9.442  1.339   39.712  1.00 8.83  ? 97   SER B C   1 
ATOM   2495 O  O   . SER B  1 97  ? -8.402  1.949   39.980  1.00 10.19 ? 97   SER B O   1 
ATOM   2496 C  CB  . SER B  1 97  ? -9.417  -1.128  39.396  1.00 8.41  ? 97   SER B CB  1 
ATOM   2497 O  OG  . SER B  1 97  ? -8.362  -1.174  40.343  1.00 10.27 ? 97   SER B OG  1 
ATOM   2498 N  N   . TRP B  1 98  ? -10.607 1.615   40.280  1.00 7.90  ? 98   TRP B N   1 
ATOM   2499 C  CA  . TRP B  1 98  ? -10.713 2.614   41.332  1.00 7.76  ? 98   TRP B CA  1 
ATOM   2500 C  C   . TRP B  1 98  ? -11.800 2.200   42.303  1.00 9.94  ? 98   TRP B C   1 
ATOM   2501 O  O   . TRP B  1 98  ? -12.840 1.667   41.902  1.00 9.26  ? 98   TRP B O   1 
ATOM   2502 C  CB  . TRP B  1 98  ? -11.011 3.994   40.746  1.00 10.95 ? 98   TRP B CB  1 
ATOM   2503 C  CG  . TRP B  1 98  ? -11.186 5.054   41.779  1.00 9.16  ? 98   TRP B CG  1 
ATOM   2504 C  CD1 . TRP B  1 98  ? -10.201 5.710   42.474  1.00 10.17 ? 98   TRP B CD1 1 
ATOM   2505 C  CD2 . TRP B  1 98  ? -12.431 5.593   42.237  1.00 9.12  ? 98   TRP B CD2 1 
ATOM   2506 N  NE1 . TRP B  1 98  ? -10.770 6.622   43.341  1.00 11.08 ? 98   TRP B NE1 1 
ATOM   2507 C  CE2 . TRP B  1 98  ? -12.135 6.572   43.209  1.00 11.60 ? 98   TRP B CE2 1 
ATOM   2508 C  CE3 . TRP B  1 98  ? -13.772 5.338   41.918  1.00 10.73 ? 98   TRP B CE3 1 
ATOM   2509 C  CZ2 . TRP B  1 98  ? -13.134 7.303   43.866  1.00 12.57 ? 98   TRP B CZ2 1 
ATOM   2510 C  CZ3 . TRP B  1 98  ? -14.764 6.068   42.570  1.00 11.33 ? 98   TRP B CZ3 1 
ATOM   2511 C  CH2 . TRP B  1 98  ? -14.434 7.038   43.529  1.00 10.06 ? 98   TRP B CH2 1 
ATOM   2512 N  N   . GLU B  1 99  ? -11.545 2.460   43.580  1.00 11.11 ? 99   GLU B N   1 
ATOM   2513 C  CA  . GLU B  1 99  ? -12.411 2.014   44.658  1.00 13.01 ? 99   GLU B CA  1 
ATOM   2514 C  C   . GLU B  1 99  ? -12.724 3.208   45.546  1.00 11.72 ? 99   GLU B C   1 
ATOM   2515 O  O   . GLU B  1 99  ? -11.831 3.745   46.176  1.00 12.28 ? 99   GLU B O   1 
ATOM   2516 C  CB  . GLU B  1 99  ? -11.657 0.960   45.465  1.00 11.77 ? 99   GLU B CB  1 
ATOM   2517 C  CG  . GLU B  1 99  ? -12.469 0.312   46.555  1.00 17.53 ? 99   GLU B CG  1 
ATOM   2518 C  CD  . GLU B  1 99  ? -11.624 -0.614  47.406  1.00 26.57 ? 99   GLU B CD  1 
ATOM   2519 O  OE1 . GLU B  1 99  ? -10.610 -0.147  47.973  1.00 17.43 ? 99   GLU B OE1 1 
ATOM   2520 O  OE2 . GLU B  1 99  ? -11.977 -1.806  47.512  1.00 25.69 ? 99   GLU B OE2 1 
ATOM   2521 N  N   . SER B  1 100 ? -13.986 3.636   45.599  1.00 11.09 ? 100  SER B N   1 
ATOM   2522 C  CA  . SER B  1 100 ? -14.334 4.835   46.370  1.00 9.29  ? 100  SER B CA  1 
ATOM   2523 C  C   . SER B  1 100 ? -13.995 4.704   47.855  1.00 10.54 ? 100  SER B C   1 
ATOM   2524 O  O   . SER B  1 100 ? -13.533 5.652   48.482  1.00 11.48 ? 100  SER B O   1 
ATOM   2525 C  CB  . SER B  1 100 ? -15.828 5.147   46.235  1.00 11.30 ? 100  SER B CB  1 
ATOM   2526 O  OG  . SER B  1 100 ? -16.195 6.237   47.071  1.00 13.82 ? 100  SER B OG  1 
ATOM   2527 N  N   . SER B  1 101 ? -14.212 3.520   48.410  1.00 11.74 ? 101  SER B N   1 
ATOM   2528 C  CA  . SER B  1 101 ? -14.081 3.346   49.852  1.00 13.35 ? 101  SER B CA  1 
ATOM   2529 C  C   . SER B  1 101 ? -12.677 3.704   50.344  1.00 14.76 ? 101  SER B C   1 
ATOM   2530 O  O   . SER B  1 101 ? -12.517 4.260   51.433  1.00 13.62 ? 101  SER B O   1 
ATOM   2531 C  CB  . SER B  1 101 ? -14.492 1.927   50.274  1.00 14.85 ? 101  SER B CB  1 
ATOM   2532 O  OG  . SER B  1 101 ? -13.668 0.932   49.689  1.00 18.34 ? 101  SER B OG  1 
ATOM   2533 N  N   . SER B  1 102 ? -11.670 3.394   49.528  1.00 12.25 ? 102  SER B N   1 
ATOM   2534 C  CA  . SER B  1 102 ? -10.278 3.685   49.859  1.00 11.69 ? 102  SER B CA  1 
ATOM   2535 C  C   . SER B  1 102 ? -9.705  4.830   49.045  1.00 11.96 ? 102  SER B C   1 
ATOM   2536 O  O   . SER B  1 102 ? -8.688  5.406   49.419  1.00 12.97 ? 102  SER B O   1 
ATOM   2537 C  CB  . SER B  1 102 ? -9.407  2.452   49.607  1.00 11.01 ? 102  SER B CB  1 
ATOM   2538 O  OG  . SER B  1 102 ? -9.460  2.083   48.237  1.00 9.80  ? 102  SER B OG  1 
ATOM   2539 N  N   . GLY B  1 103 ? -10.337 5.123   47.913  1.00 9.37  ? 103  GLY B N   1 
ATOM   2540 C  CA  . GLY B  1 103 ? -9.804  6.075   46.957  1.00 9.92  ? 103  GLY B CA  1 
ATOM   2541 C  C   . GLY B  1 103 ? -8.685  5.496   46.096  1.00 11.32 ? 103  GLY B C   1 
ATOM   2542 O  O   . GLY B  1 103 ? -8.142  6.180   45.241  1.00 9.65  ? 103  GLY B O   1 
ATOM   2543 N  N   . ILE B  1 104 ? -8.343  4.229   46.303  1.00 10.55 ? 104  ILE B N   1 
ATOM   2544 C  CA  . ILE B  1 104 ? -7.194  3.641   45.592  1.00 11.05 ? 104  ILE B CA  1 
ATOM   2545 C  C   . ILE B  1 104 ? -7.442  3.395   44.103  1.00 9.81  ? 104  ILE B C   1 
ATOM   2546 O  O   . ILE B  1 104 ? -8.433  2.770   43.715  1.00 9.78  ? 104  ILE B O   1 
ATOM   2547 C  CB  . ILE B  1 104 ? -6.734  2.323   46.249  1.00 12.83 ? 104  ILE B CB  1 
ATOM   2548 C  CG1 . ILE B  1 104 ? -6.240  2.589   47.672  1.00 10.17 ? 104  ILE B CG1 1 
ATOM   2549 C  CG2 . ILE B  1 104 ? -5.626  1.642   45.407  1.00 10.38 ? 104  ILE B CG2 1 
ATOM   2550 C  CD1 . ILE B  1 104 ? -5.049  3.539   47.758  1.00 12.68 ? 104  ILE B CD1 1 
ATOM   2551 N  N   . ALA B  1 105 ? -6.516  3.897   43.287  1.00 8.73  ? 105  ALA B N   1 
ATOM   2552 C  CA  . ALA B  1 105 ? -6.462  3.663   41.847  1.00 8.74  ? 105  ALA B CA  1 
ATOM   2553 C  C   . ALA B  1 105 ? -5.305  2.716   41.542  1.00 9.69  ? 105  ALA B C   1 
ATOM   2554 O  O   . ALA B  1 105 ? -4.178  2.962   41.973  1.00 10.04 ? 105  ALA B O   1 
ATOM   2555 C  CB  . ALA B  1 105 ? -6.248  4.983   41.114  1.00 8.51  ? 105  ALA B CB  1 
ATOM   2556 N  N   . GLU B  1 106 ? -5.588  1.635   40.816  1.00 8.96  ? 106  GLU B N   1 
ATOM   2557 C  CA  . GLU B  1 106 ? -4.560  0.687   40.387  1.00 9.42  ? 106  GLU B CA  1 
ATOM   2558 C  C   . GLU B  1 106 ? -4.449  0.662   38.876  1.00 10.42 ? 106  GLU B C   1 
ATOM   2559 O  O   . GLU B  1 106 ? -5.394  0.248   38.203  1.00 12.28 ? 106  GLU B O   1 
ATOM   2560 C  CB  . GLU B  1 106 ? -4.926  -0.755  40.773  1.00 14.17 ? 106  GLU B CB  1 
ATOM   2561 C  CG  . GLU B  1 106 ? -5.157  -1.053  42.219  1.00 13.05 ? 106  GLU B CG  1 
ATOM   2562 C  CD  . GLU B  1 106 ? -5.354  -2.555  42.466  1.00 17.49 ? 106  GLU B CD  1 
ATOM   2563 O  OE1 . GLU B  1 106 ? -5.178  -3.375  41.520  1.00 16.22 ? 106  GLU B OE1 1 
ATOM   2564 O  OE2 . GLU B  1 106 ? -5.682  -2.914  43.615  1.00 22.09 ? 106  GLU B OE2 1 
ATOM   2565 N  N   . PHE B  1 107 ? -3.291  1.041   38.341  1.00 9.02  ? 107  PHE B N   1 
ATOM   2566 C  CA  . PHE B  1 107 ? -3.000  0.823   36.924  1.00 8.69  ? 107  PHE B CA  1 
ATOM   2567 C  C   . PHE B  1 107 ? -2.222  -0.475  36.772  1.00 7.64  ? 107  PHE B C   1 
ATOM   2568 O  O   . PHE B  1 107 ? -1.350  -0.778  37.595  1.00 9.48  ? 107  PHE B O   1 
ATOM   2569 C  CB  . PHE B  1 107 ? -2.131  1.952   36.369  1.00 11.00 ? 107  PHE B CB  1 
ATOM   2570 C  CG  . PHE B  1 107 ? -2.907  3.133   35.829  1.00 10.23 ? 107  PHE B CG  1 
ATOM   2571 C  CD1 . PHE B  1 107 ? -3.522  3.067   34.584  1.00 12.98 ? 107  PHE B CD1 1 
ATOM   2572 C  CD2 . PHE B  1 107 ? -2.974  4.313   36.543  1.00 10.72 ? 107  PHE B CD2 1 
ATOM   2573 C  CE1 . PHE B  1 107 ? -4.211  4.159   34.078  1.00 12.80 ? 107  PHE B CE1 1 
ATOM   2574 C  CE2 . PHE B  1 107 ? -3.667  5.402   36.052  1.00 10.93 ? 107  PHE B CE2 1 
ATOM   2575 C  CZ  . PHE B  1 107 ? -4.277  5.333   34.816  1.00 11.12 ? 107  PHE B CZ  1 
ATOM   2576 N  N   . TRP B  1 108 ? -2.546  -1.239  35.732  1.00 8.28  ? 108  TRP B N   1 
ATOM   2577 C  CA  . TRP B  1 108 ? -1.768  -2.425  35.338  1.00 8.66  ? 108  TRP B CA  1 
ATOM   2578 C  C   . TRP B  1 108 ? -1.402  -2.245  33.871  1.00 8.75  ? 108  TRP B C   1 
ATOM   2579 O  O   . TRP B  1 108 ? -2.268  -1.992  33.043  1.00 10.76 ? 108  TRP B O   1 
ATOM   2580 C  CB  . TRP B  1 108 ? -2.612  -3.696  35.498  1.00 11.59 ? 108  TRP B CB  1 
ATOM   2581 C  CG  . TRP B  1 108 ? -2.932  -4.045  36.924  1.00 10.84 ? 108  TRP B CG  1 
ATOM   2582 C  CD1 . TRP B  1 108 ? -3.800  -3.401  37.750  1.00 12.31 ? 108  TRP B CD1 1 
ATOM   2583 C  CD2 . TRP B  1 108 ? -2.377  -5.128  37.685  1.00 9.10  ? 108  TRP B CD2 1 
ATOM   2584 N  NE1 . TRP B  1 108 ? -3.820  -4.013  38.987  1.00 13.61 ? 108  TRP B NE1 1 
ATOM   2585 C  CE2 . TRP B  1 108 ? -2.951  -5.072  38.971  1.00 12.93 ? 108  TRP B CE2 1 
ATOM   2586 C  CE3 . TRP B  1 108 ? -1.434  -6.124  37.408  1.00 12.70 ? 108  TRP B CE3 1 
ATOM   2587 C  CZ2 . TRP B  1 108 ? -2.629  -5.990  39.975  1.00 15.66 ? 108  TRP B CZ2 1 
ATOM   2588 C  CZ3 . TRP B  1 108 ? -1.112  -7.038  38.412  1.00 14.90 ? 108  TRP B CZ3 1 
ATOM   2589 C  CH2 . TRP B  1 108 ? -1.713  -6.963  39.674  1.00 15.25 ? 108  TRP B CH2 1 
ATOM   2590 N  N   . ILE B  1 109 ? -0.118  -2.365  33.548  1.00 8.56  ? 109  ILE B N   1 
ATOM   2591 C  CA  . ILE B  1 109 ? 0.345   -2.132  32.180  1.00 7.10  ? 109  ILE B CA  1 
ATOM   2592 C  C   . ILE B  1 109 ? 0.988   -3.433  31.711  1.00 10.41 ? 109  ILE B C   1 
ATOM   2593 O  O   . ILE B  1 109 ? 1.942   -3.898  32.318  1.00 11.69 ? 109  ILE B O   1 
ATOM   2594 C  CB  . ILE B  1 109 ? 1.361   -0.986  32.144  1.00 9.88  ? 109  ILE B CB  1 
ATOM   2595 C  CG1 . ILE B  1 109 ? 0.718   0.308   32.652  1.00 11.35 ? 109  ILE B CG1 1 
ATOM   2596 C  CG2 . ILE B  1 109 ? 1.938   -0.815  30.737  1.00 10.63 ? 109  ILE B CG2 1 
ATOM   2597 C  CD1 . ILE B  1 109 ? -0.440  0.828   31.795  1.00 13.13 ? 109  ILE B CD1 1 
ATOM   2598 N  N   . ASN B  1 110 ? 0.426   -4.036  30.665  1.00 8.42  ? 110  ASN B N   1 
ATOM   2599 C  CA  . ASN B  1 110 ? 0.875   -5.353  30.206  1.00 8.25  ? 110  ASN B CA  1 
ATOM   2600 C  C   . ASN B  1 110 ? 0.934   -6.373  31.332  1.00 13.80 ? 110  ASN B C   1 
ATOM   2601 O  O   . ASN B  1 110 ? 1.879   -7.174  31.414  1.00 14.42 ? 110  ASN B O   1 
ATOM   2602 C  CB  . ASN B  1 110 ? 2.229   -5.240  29.519  1.00 12.81 ? 110  ASN B CB  1 
ATOM   2603 C  CG  . ASN B  1 110 ? 2.170   -4.347  28.309  1.00 15.19 ? 110  ASN B CG  1 
ATOM   2604 O  OD1 . ASN B  1 110 ? 1.163   -4.332  27.591  1.00 12.78 ? 110  ASN B OD1 1 
ATOM   2605 N  ND2 . ASN B  1 110 ? 3.235   -3.591  28.075  1.00 16.67 ? 110  ASN B ND2 1 
ATOM   2606 N  N   . GLY B  1 111 ? -0.071  -6.324  32.202  1.00 10.85 ? 111  GLY B N   1 
ATOM   2607 C  CA  . GLY B  1 111 ? -0.187  -7.263  33.305  1.00 14.75 ? 111  GLY B CA  1 
ATOM   2608 C  C   . GLY B  1 111 ? 0.747   -7.017  34.480  1.00 14.56 ? 111  GLY B C   1 
ATOM   2609 O  O   . GLY B  1 111 ? 0.815   -7.838  35.395  1.00 18.92 ? 111  GLY B O   1 
ATOM   2610 N  N   . THR B  1 112 ? 1.460   -5.895  34.451  1.00 14.45 ? 112  THR B N   1 
ATOM   2611 C  CA  . THR B  1 112 ? 2.356   -5.488  35.533  1.00 16.35 ? 112  THR B CA  1 
ATOM   2612 C  C   . THR B  1 112 ? 1.744   -4.327  36.316  1.00 11.31 ? 112  THR B C   1 
ATOM   2613 O  O   . THR B  1 112 ? 1.353   -3.330  35.722  1.00 11.21 ? 112  THR B O   1 
ATOM   2614 C  CB  . THR B  1 112 ? 3.703   -5.016  34.957  1.00 19.73 ? 112  THR B CB  1 
ATOM   2615 O  OG1 . THR B  1 112 ? 4.370   -6.128  34.339  1.00 27.28 ? 112  THR B OG1 1 
ATOM   2616 C  CG2 . THR B  1 112 ? 4.590   -4.442  36.054  1.00 26.19 ? 112  THR B CG2 1 
ATOM   2617 N  N   . PRO B  1 113 ? 1.675   -4.446  37.655  1.00 12.54 ? 113  PRO B N   1 
ATOM   2618 C  CA  . PRO B  1 113 ? 1.067   -3.371  38.447  1.00 9.18  ? 113  PRO B CA  1 
ATOM   2619 C  C   . PRO B  1 113 ? 1.970   -2.146  38.577  1.00 9.32  ? 113  PRO B C   1 
ATOM   2620 O  O   . PRO B  1 113 ? 3.165   -2.291  38.833  1.00 10.97 ? 113  PRO B O   1 
ATOM   2621 C  CB  . PRO B  1 113 ? 0.872   -4.013  39.825  1.00 10.35 ? 113  PRO B CB  1 
ATOM   2622 C  CG  . PRO B  1 113 ? 1.958   -5.060  39.912  1.00 11.36 ? 113  PRO B CG  1 
ATOM   2623 C  CD  . PRO B  1 113 ? 2.177   -5.552  38.491  1.00 11.22 ? 113  PRO B CD  1 
ATOM   2624 N  N   . LEU B  1 114 ? 1.394   -0.958  38.394  1.00 7.85  ? 114  LEU B N   1 
ATOM   2625 C  CA  . LEU B  1 114 ? 2.085   0.288   38.697  1.00 7.48  ? 114  LEU B CA  1 
ATOM   2626 C  C   . LEU B  1 114 ? 1.899   0.589   40.180  1.00 9.01  ? 114  LEU B C   1 
ATOM   2627 O  O   . LEU B  1 114 ? 1.130   -0.084  40.869  1.00 8.89  ? 114  LEU B O   1 
ATOM   2628 C  CB  . LEU B  1 114 ? 1.528   1.437   37.849  1.00 8.65  ? 114  LEU B CB  1 
ATOM   2629 C  CG  . LEU B  1 114 ? 1.578   1.252   36.324  1.00 10.67 ? 114  LEU B CG  1 
ATOM   2630 C  CD1 . LEU B  1 114 ? 1.523   2.607   35.596  1.00 7.60  ? 114  LEU B CD1 1 
ATOM   2631 C  CD2 . LEU B  1 114 ? 2.809   0.472   35.903  1.00 12.79 ? 114  LEU B CD2 1 
ATOM   2632 N  N   . VAL B  1 115 ? 2.599   1.601   40.674  1.00 8.04  ? 115  VAL B N   1 
ATOM   2633 C  CA  . VAL B  1 115 ? 2.421   2.025   42.061  1.00 7.08  ? 115  VAL B CA  1 
ATOM   2634 C  C   . VAL B  1 115 ? 0.989   2.534   42.248  1.00 8.63  ? 115  VAL B C   1 
ATOM   2635 O  O   . VAL B  1 115 ? 0.490   3.315   41.426  1.00 10.67 ? 115  VAL B O   1 
ATOM   2636 C  CB  . VAL B  1 115 ? 3.409   3.146   42.423  1.00 7.35  ? 115  VAL B CB  1 
ATOM   2637 C  CG1 . VAL B  1 115 ? 3.238   3.547   43.889  1.00 9.51  ? 115  VAL B CG1 1 
ATOM   2638 C  CG2 . VAL B  1 115 ? 4.860   2.705   42.140  1.00 9.74  ? 115  VAL B CG2 1 
ATOM   2639 N  N   . LYS B  1 116 ? 0.333   2.087   43.317  1.00 7.71  ? 116  LYS B N   1 
ATOM   2640 C  CA  . LYS B  1 116 ? -1.021  2.540   43.623  1.00 8.78  ? 116  LYS B CA  1 
ATOM   2641 C  C   . LYS B  1 116 ? -0.990  4.007   44.028  1.00 10.71 ? 116  LYS B C   1 
ATOM   2642 O  O   . LYS B  1 116 ? -0.039  4.464   44.687  1.00 12.01 ? 116  LYS B O   1 
ATOM   2643 C  CB  . LYS B  1 116 ? -1.608  1.724   44.774  1.00 9.53  ? 116  LYS B CB  1 
ATOM   2644 C  CG  . LYS B  1 116 ? -2.060  0.314   44.412  1.00 10.45 ? 116  LYS B CG  1 
ATOM   2645 C  CD  . LYS B  1 116 ? -2.345  -0.466  45.719  1.00 12.50 ? 116  LYS B CD  1 
ATOM   2646 C  CE  . LYS B  1 116 ? -3.123  -1.749  45.472  1.00 20.97 ? 116  LYS B CE  1 
ATOM   2647 N  NZ  . LYS B  1 116 ? -2.303  -2.775  44.774  1.00 16.24 ? 116  LYS B NZ  1 
ATOM   2648 N  N   . LYS B  1 117 ? -2.031  4.743   43.640  1.00 7.13  ? 117  LYS B N   1 
ATOM   2649 C  CA  . LYS B  1 117 ? -2.201  6.110   44.101  1.00 7.07  ? 117  LYS B CA  1 
ATOM   2650 C  C   . LYS B  1 117 ? -3.630  6.234   44.608  1.00 11.86 ? 117  LYS B C   1 
ATOM   2651 O  O   . LYS B  1 117 ? -4.421  5.301   44.467  1.00 12.66 ? 117  LYS B O   1 
ATOM   2652 C  CB  . LYS B  1 117 ? -1.934  7.111   42.973  1.00 9.43  ? 117  LYS B CB  1 
ATOM   2653 C  CG  . LYS B  1 117 ? -0.520  7.013   42.372  1.00 10.27 ? 117  LYS B CG  1 
ATOM   2654 C  CD  . LYS B  1 117 ? 0.572   7.515   43.335  1.00 8.86  ? 117  LYS B CD  1 
ATOM   2655 C  CE  . LYS B  1 117 ? 1.978   7.039   42.866  1.00 8.84  ? 117  LYS B CE  1 
ATOM   2656 N  NZ  . LYS B  1 117 ? 2.392   7.677   41.577  1.00 13.44 ? 117  LYS B NZ  1 
ATOM   2657 N  N   . GLY B  1 118 ? -3.966  7.370   45.205  1.00 9.12  ? 118  GLY B N   1 
ATOM   2658 C  CA  . GLY B  1 118 ? -5.275  7.510   45.823  1.00 10.24 ? 118  GLY B CA  1 
ATOM   2659 C  C   . GLY B  1 118 ? -5.879  8.886   45.626  1.00 8.95  ? 118  GLY B C   1 
ATOM   2660 O  O   . GLY B  1 118 ? -5.173  9.898   45.698  1.00 12.19 ? 118  GLY B O   1 
ATOM   2661 N  N   . LEU B  1 119 ? -7.187  8.911   45.375  1.00 8.17  ? 119  LEU B N   1 
ATOM   2662 C  CA  . LEU B  1 119 ? -7.917  10.154  45.119  1.00 9.81  ? 119  LEU B CA  1 
ATOM   2663 C  C   . LEU B  1 119 ? -9.416  9.967   45.336  1.00 10.23 ? 119  LEU B C   1 
ATOM   2664 O  O   . LEU B  1 119 ? -9.958  8.875   45.148  1.00 9.65  ? 119  LEU B O   1 
ATOM   2665 C  CB  . LEU B  1 119 ? -7.670  10.654  43.680  1.00 8.42  ? 119  LEU B CB  1 
ATOM   2666 C  CG  . LEU B  1 119 ? -8.360  9.934   42.504  1.00 7.10  ? 119  LEU B CG  1 
ATOM   2667 C  CD1 . LEU B  1 119 ? -8.172  10.745  41.215  1.00 9.29  ? 119  LEU B CD1 1 
ATOM   2668 C  CD2 . LEU B  1 119 ? -7.844  8.502   42.296  1.00 9.08  ? 119  LEU B CD2 1 
ATOM   2669 N  N   . ARG B  1 120 ? -10.079 11.048  45.732  1.00 9.97  ? 120  ARG B N   1 
ATOM   2670 C  CA  . ARG B  1 120 ? -11.535 11.077  45.803  1.00 10.48 ? 120  ARG B CA  1 
ATOM   2671 C  C   . ARG B  1 120 ? -12.151 9.984   46.673  1.00 10.66 ? 120  ARG B C   1 
ATOM   2672 O  O   . ARG B  1 120 ? -13.205 9.455   46.357  1.00 12.24 ? 120  ARG B O   1 
ATOM   2673 C  CB  . ARG B  1 120 ? -12.121 11.030  44.385  1.00 9.07  ? 120  ARG B CB  1 
ATOM   2674 C  CG  . ARG B  1 120 ? -12.032 12.360  43.654  1.00 9.86  ? 120  ARG B CG  1 
ATOM   2675 C  CD  . ARG B  1 120 ? -12.981 13.381  44.288  1.00 13.16 ? 120  ARG B CD  1 
ATOM   2676 N  NE  . ARG B  1 120 ? -13.277 14.490  43.386  1.00 13.35 ? 120  ARG B NE  1 
ATOM   2677 C  CZ  . ARG B  1 120 ? -14.167 15.442  43.660  1.00 16.28 ? 120  ARG B CZ  1 
ATOM   2678 N  NH1 . ARG B  1 120 ? -14.392 16.426  42.795  1.00 16.49 ? 120  ARG B NH1 1 
ATOM   2679 N  NH2 . ARG B  1 120 ? -14.835 15.402  44.807  1.00 19.37 ? 120  ARG B NH2 1 
ATOM   2680 N  N   . GLN B  1 121 ? -11.501 9.646   47.782  1.00 12.83 ? 121  GLN B N   1 
ATOM   2681 C  CA  . GLN B  1 121 ? -12.073 8.654   48.686  1.00 10.13 ? 121  GLN B CA  1 
ATOM   2682 C  C   . GLN B  1 121 ? -13.471 9.111   49.108  1.00 9.91  ? 121  GLN B C   1 
ATOM   2683 O  O   . GLN B  1 121 ? -13.641 10.259  49.511  1.00 11.45 ? 121  GLN B O   1 
ATOM   2684 C  CB  . GLN B  1 121 ? -11.190 8.504   49.922  1.00 9.19  ? 121  GLN B CB  1 
ATOM   2685 C  CG  . GLN B  1 121 ? -11.690 7.458   50.907  1.00 10.94 ? 121  GLN B CG  1 
ATOM   2686 C  CD  . GLN B  1 121 ? -10.784 7.340   52.117  1.00 15.22 ? 121  GLN B CD  1 
ATOM   2687 O  OE1 . GLN B  1 121 ? -10.110 8.302   52.499  1.00 17.93 ? 121  GLN B OE1 1 
ATOM   2688 N  NE2 . GLN B  1 121 ? -10.758 6.157   52.727  1.00 14.48 ? 121  GLN B NE2 1 
ATOM   2689 N  N   . GLY B  1 122 ? -14.458 8.224   48.984  1.00 9.98  ? 122  GLY B N   1 
ATOM   2690 C  CA  . GLY B  1 122 ? -15.828 8.513   49.406  1.00 11.25 ? 122  GLY B CA  1 
ATOM   2691 C  C   . GLY B  1 122 ? -16.705 9.099   48.318  1.00 14.77 ? 122  GLY B C   1 
ATOM   2692 O  O   . GLY B  1 122 ? -17.925 9.234   48.493  1.00 14.30 ? 122  GLY B O   1 
ATOM   2693 N  N   . TYR B  1 123 ? -16.087 9.461   47.198  1.00 11.53 ? 123  TYR B N   1 
ATOM   2694 C  CA  . TYR B  1 123 ? -16.787 10.057  46.062  1.00 10.14 ? 123  TYR B CA  1 
ATOM   2695 C  C   . TYR B  1 123 ? -17.512 8.985   45.262  1.00 13.15 ? 123  TYR B C   1 
ATOM   2696 O  O   . TYR B  1 123 ? -17.089 7.829   45.244  1.00 13.75 ? 123  TYR B O   1 
ATOM   2697 C  CB  . TYR B  1 123 ? -15.779 10.790  45.165  1.00 9.70  ? 123  TYR B CB  1 
ATOM   2698 C  CG  . TYR B  1 123 ? -16.370 11.548  43.993  1.00 11.46 ? 123  TYR B CG  1 
ATOM   2699 C  CD1 . TYR B  1 123 ? -17.041 12.752  44.185  1.00 15.60 ? 123  TYR B CD1 1 
ATOM   2700 C  CD2 . TYR B  1 123 ? -16.231 11.079  42.693  1.00 10.09 ? 123  TYR B CD2 1 
ATOM   2701 C  CE1 . TYR B  1 123 ? -17.569 13.459  43.114  1.00 15.77 ? 123  TYR B CE1 1 
ATOM   2702 C  CE2 . TYR B  1 123 ? -16.755 11.779  41.609  1.00 8.98  ? 123  TYR B CE2 1 
ATOM   2703 C  CZ  . TYR B  1 123 ? -17.424 12.966  41.829  1.00 13.29 ? 123  TYR B CZ  1 
ATOM   2704 O  OH  . TYR B  1 123 ? -17.959 13.657  40.771  1.00 13.32 ? 123  TYR B OH  1 
ATOM   2705 N  N   . PHE B  1 124 ? -18.604 9.369   44.599  1.00 12.93 ? 124  PHE B N   1 
ATOM   2706 C  CA  . PHE B  1 124 ? -19.264 8.479   43.646  1.00 12.70 ? 124  PHE B CA  1 
ATOM   2707 C  C   . PHE B  1 124 ? -19.138 9.085   42.260  1.00 10.37 ? 124  PHE B C   1 
ATOM   2708 O  O   . PHE B  1 124 ? -19.510 10.243  42.057  1.00 14.50 ? 124  PHE B O   1 
ATOM   2709 C  CB  . PHE B  1 124 ? -20.758 8.310   43.962  1.00 20.19 ? 124  PHE B CB  1 
ATOM   2710 C  CG  . PHE B  1 124 ? -21.038 7.552   45.233  1.00 26.08 ? 124  PHE B CG  1 
ATOM   2711 C  CD1 . PHE B  1 124 ? -20.057 6.784   45.833  1.00 29.07 ? 124  PHE B CD1 1 
ATOM   2712 C  CD2 . PHE B  1 124 ? -22.295 7.594   45.809  1.00 43.66 ? 124  PHE B CD2 1 
ATOM   2713 C  CE1 . PHE B  1 124 ? -20.317 6.085   46.999  1.00 41.33 ? 124  PHE B CE1 1 
ATOM   2714 C  CE2 . PHE B  1 124 ? -22.564 6.896   46.971  1.00 42.14 ? 124  PHE B CE2 1 
ATOM   2715 C  CZ  . PHE B  1 124 ? -21.573 6.140   47.566  1.00 43.67 ? 124  PHE B CZ  1 
ATOM   2716 N  N   . VAL B  1 125 ? -18.600 8.319   41.310  1.00 11.73 ? 125  VAL B N   1 
ATOM   2717 C  CA  . VAL B  1 125 ? -18.556 8.777   39.929  1.00 11.03 ? 125  VAL B CA  1 
ATOM   2718 C  C   . VAL B  1 125 ? -19.987 8.886   39.409  1.00 11.82 ? 125  VAL B C   1 
ATOM   2719 O  O   . VAL B  1 125 ? -20.775 7.951   39.540  1.00 12.92 ? 125  VAL B O   1 
ATOM   2720 C  CB  . VAL B  1 125 ? -17.745 7.825   39.034  1.00 11.74 ? 125  VAL B CB  1 
ATOM   2721 C  CG1 . VAL B  1 125 ? -17.906 8.209   37.564  1.00 11.74 ? 125  VAL B CG1 1 
ATOM   2722 C  CG2 . VAL B  1 125 ? -16.268 7.837   39.442  1.00 13.20 ? 125  VAL B CG2 1 
ATOM   2723 N  N   . GLU B  1 126 ? -20.320 10.032  38.825  1.00 11.14 ? 126  GLU B N   1 
ATOM   2724 C  CA  . GLU B  1 126 ? -21.698 10.300  38.432  1.00 14.12 ? 126  GLU B CA  1 
ATOM   2725 C  C   . GLU B  1 126 ? -22.211 9.373   37.334  1.00 13.23 ? 126  GLU B C   1 
ATOM   2726 O  O   . GLU B  1 126 ? -21.451 8.919   36.469  1.00 11.39 ? 126  GLU B O   1 
ATOM   2727 C  CB  . GLU B  1 126 ? -21.851 11.752  37.995  1.00 15.69 ? 126  GLU B CB  1 
ATOM   2728 C  CG  . GLU B  1 126 ? -21.657 12.739  39.127  1.00 16.30 ? 126  GLU B CG  1 
ATOM   2729 C  CD  . GLU B  1 126 ? -22.162 14.117  38.780  1.00 28.53 ? 126  GLU B CD  1 
ATOM   2730 O  OE1 . GLU B  1 126 ? -22.376 14.382  37.578  1.00 30.59 ? 126  GLU B OE1 1 
ATOM   2731 O  OE2 . GLU B  1 126 ? -22.342 14.936  39.706  1.00 34.14 ? 126  GLU B OE2 1 
ATOM   2732 N  N   . ALA B  1 127 ? -23.515 9.119   37.370  1.00 13.50 ? 127  ALA B N   1 
ATOM   2733 C  CA  . ALA B  1 127 ? -24.179 8.280   36.378  1.00 11.09 ? 127  ALA B CA  1 
ATOM   2734 C  C   . ALA B  1 127 ? -24.486 9.062   35.098  1.00 11.01 ? 127  ALA B C   1 
ATOM   2735 O  O   . ALA B  1 127 ? -24.302 10.283  35.050  1.00 11.44 ? 127  ALA B O   1 
ATOM   2736 C  CB  . ALA B  1 127 ? -25.473 7.727   36.970  1.00 14.47 ? 127  ALA B CB  1 
ATOM   2737 N  N   . GLN B  1 128 ? -24.960 8.345   34.078  1.00 9.93  ? 128  GLN B N   1 
ATOM   2738 C  CA  . GLN B  1 128 ? -25.412 8.929   32.812  1.00 8.50  ? 128  GLN B CA  1 
ATOM   2739 C  C   . GLN B  1 128 ? -24.313 9.674   32.072  1.00 11.74 ? 128  GLN B C   1 
ATOM   2740 O  O   . GLN B  1 128 ? -24.443 10.850  31.747  1.00 10.55 ? 128  GLN B O   1 
ATOM   2741 C  CB  . GLN B  1 128 ? -26.621 9.843   33.043  1.00 13.32 ? 128  GLN B CB  1 
ATOM   2742 C  CG  . GLN B  1 128 ? -27.848 9.067   33.497  1.00 14.56 ? 128  GLN B CG  1 
ATOM   2743 C  CD  . GLN B  1 128 ? -29.008 9.973   33.843  1.00 23.87 ? 128  GLN B CD  1 
ATOM   2744 O  OE1 . GLN B  1 128 ? -29.381 10.105  35.009  1.00 34.11 ? 128  GLN B OE1 1 
ATOM   2745 N  NE2 . GLN B  1 128 ? -29.579 10.607  32.834  1.00 21.37 ? 128  GLN B NE2 1 
ATOM   2746 N  N   . PRO B  1 129 ? -23.214 8.976   31.789  1.00 12.39 ? 129  PRO B N   1 
ATOM   2747 C  CA  . PRO B  1 129 ? -22.104 9.613   31.079  1.00 8.65  ? 129  PRO B CA  1 
ATOM   2748 C  C   . PRO B  1 129 ? -22.316 9.667   29.571  1.00 11.35 ? 129  PRO B C   1 
ATOM   2749 O  O   . PRO B  1 129 ? -23.176 8.971   29.006  1.00 12.52 ? 129  PRO B O   1 
ATOM   2750 C  CB  . PRO B  1 129 ? -20.954 8.639   31.362  1.00 10.16 ? 129  PRO B CB  1 
ATOM   2751 C  CG  . PRO B  1 129 ? -21.664 7.308   31.271  1.00 12.19 ? 129  PRO B CG  1 
ATOM   2752 C  CD  . PRO B  1 129 ? -22.893 7.582   32.141  1.00 12.94 ? 129  PRO B CD  1 
ATOM   2753 N  N   . LYS B  1 130 ? -21.514 10.509  28.925  1.00 6.90  ? 130  LYS B N   1 
ATOM   2754 C  CA  . LYS B  1 130 ? -21.148 10.297  27.536  1.00 8.83  ? 130  LYS B CA  1 
ATOM   2755 C  C   . LYS B  1 130 ? -19.740 9.748   27.629  1.00 10.63 ? 130  LYS B C   1 
ATOM   2756 O  O   . LYS B  1 130 ? -18.884 10.327  28.305  1.00 7.26  ? 130  LYS B O   1 
ATOM   2757 C  CB  . LYS B  1 130 ? -21.156 11.603  26.735  1.00 9.45  ? 130  LYS B CB  1 
ATOM   2758 C  CG  . LYS B  1 130 ? -22.541 12.212  26.540  1.00 13.64 ? 130  LYS B CG  1 
ATOM   2759 C  CD  . LYS B  1 130 ? -23.414 11.345  25.647  1.00 20.38 ? 130  LYS B CD  1 
ATOM   2760 C  CE  . LYS B  1 130 ? -24.688 12.089  25.259  1.00 32.23 ? 130  LYS B CE  1 
ATOM   2761 N  NZ  . LYS B  1 130 ? -25.439 11.366  24.200  1.00 46.43 ? 130  LYS B NZ  1 
ATOM   2762 N  N   . ILE B  1 131 ? -19.517 8.617   26.974  1.00 8.85  ? 131  ILE B N   1 
ATOM   2763 C  CA  . ILE B  1 131 ? -18.225 7.944   26.994  1.00 7.03  ? 131  ILE B CA  1 
ATOM   2764 C  C   . ILE B  1 131 ? -17.676 7.988   25.581  1.00 8.24  ? 131  ILE B C   1 
ATOM   2765 O  O   . ILE B  1 131 ? -18.345 7.552   24.629  1.00 9.98  ? 131  ILE B O   1 
ATOM   2766 C  CB  . ILE B  1 131 ? -18.389 6.480   27.406  1.00 7.54  ? 131  ILE B CB  1 
ATOM   2767 C  CG1 . ILE B  1 131 ? -19.028 6.393   28.789  1.00 12.67 ? 131  ILE B CG1 1 
ATOM   2768 C  CG2 . ILE B  1 131 ? -17.041 5.761   27.393  1.00 8.00  ? 131  ILE B CG2 1 
ATOM   2769 C  CD1 . ILE B  1 131 ? -19.273 4.963   29.243  1.00 10.65 ? 131  ILE B CD1 1 
ATOM   2770 N  N   . VAL B  1 132 ? -16.468 8.519   25.440  1.00 6.66  ? 132  VAL B N   1 
ATOM   2771 C  CA  . VAL B  1 132 ? -15.899 8.762   24.110  1.00 6.41  ? 132  VAL B CA  1 
ATOM   2772 C  C   . VAL B  1 132 ? -14.491 8.184   24.002  1.00 7.29  ? 132  VAL B C   1 
ATOM   2773 O  O   . VAL B  1 132 ? -13.658 8.373   24.901  1.00 8.04  ? 132  VAL B O   1 
ATOM   2774 C  CB  . VAL B  1 132 ? -15.854 10.282  23.800  1.00 8.32  ? 132  VAL B CB  1 
ATOM   2775 C  CG1 . VAL B  1 132 ? -15.052 10.583  22.525  1.00 9.38  ? 132  VAL B CG1 1 
ATOM   2776 C  CG2 . VAL B  1 132 ? -17.272 10.850  23.704  1.00 9.91  ? 132  VAL B CG2 1 
ATOM   2777 N  N   . LEU B  1 133 ? -14.253 7.457   22.911  1.00 8.29  ? 133  LEU B N   1 
ATOM   2778 C  CA  . LEU B  1 133 ? -12.911 7.076   22.481  1.00 8.19  ? 133  LEU B CA  1 
ATOM   2779 C  C   . LEU B  1 133 ? -12.498 7.967   21.325  1.00 7.01  ? 133  LEU B C   1 
ATOM   2780 O  O   . LEU B  1 133 ? -13.320 8.283   20.453  1.00 9.24  ? 133  LEU B O   1 
ATOM   2781 C  CB  . LEU B  1 133 ? -12.899 5.629   21.974  1.00 7.35  ? 133  LEU B CB  1 
ATOM   2782 C  CG  . LEU B  1 133 ? -13.328 4.521   22.931  1.00 7.25  ? 133  LEU B CG  1 
ATOM   2783 C  CD1 . LEU B  1 133 ? -13.201 3.171   22.203  1.00 7.34  ? 133  LEU B CD1 1 
ATOM   2784 C  CD2 . LEU B  1 133 ? -12.471 4.562   24.182  1.00 10.89 ? 133  LEU B CD2 1 
ATOM   2785 N  N   . GLY B  1 134 ? -11.225 8.367   21.300  1.00 4.94  ? 134  GLY B N   1 
ATOM   2786 C  CA  . GLY B  1 134 ? -10.702 9.099   20.158  1.00 6.44  ? 134  GLY B CA  1 
ATOM   2787 C  C   . GLY B  1 134 ? -10.539 10.593  20.380  1.00 6.32  ? 134  GLY B C   1 
ATOM   2788 O  O   . GLY B  1 134 ? -9.736  11.238  19.716  1.00 7.73  ? 134  GLY B O   1 
ATOM   2789 N  N   . GLN B  1 135 ? -11.322 11.138  21.306  1.00 7.73  ? 135  GLN B N   1 
ATOM   2790 C  CA  . GLN B  1 135 ? -11.233 12.547  21.659  1.00 7.96  ? 135  GLN B CA  1 
ATOM   2791 C  C   . GLN B  1 135 ? -11.350 12.717  23.162  1.00 7.72  ? 135  GLN B C   1 
ATOM   2792 O  O   . GLN B  1 135 ? -11.859 11.841  23.863  1.00 10.15 ? 135  GLN B O   1 
ATOM   2793 C  CB  . GLN B  1 135 ? -12.339 13.366  20.983  1.00 9.19  ? 135  GLN B CB  1 
ATOM   2794 C  CG  . GLN B  1 135 ? -12.373 13.280  19.451  1.00 8.36  ? 135  GLN B CG  1 
ATOM   2795 C  CD  . GLN B  1 135 ? -11.216 14.012  18.800  1.00 9.54  ? 135  GLN B CD  1 
ATOM   2796 O  OE1 . GLN B  1 135 ? -10.637 14.930  19.378  1.00 9.84  ? 135  GLN B OE1 1 
ATOM   2797 N  NE2 . GLN B  1 135 ? -10.868 13.597  17.588  1.00 7.86  ? 135  GLN B NE2 1 
ATOM   2798 N  N   . GLU B  1 136 ? -10.869 13.855  23.649  1.00 7.38  ? 136  GLU B N   1 
ATOM   2799 C  CA  . GLU B  1 136 ? -11.039 14.217  25.047  1.00 4.38  ? 136  GLU B CA  1 
ATOM   2800 C  C   . GLU B  1 136 ? -12.209 15.195  25.108  1.00 7.99  ? 136  GLU B C   1 
ATOM   2801 O  O   . GLU B  1 136 ? -12.176 16.227  24.441  1.00 8.03  ? 136  GLU B O   1 
ATOM   2802 C  CB  . GLU B  1 136 ? -9.766  14.904  25.545  1.00 7.72  ? 136  GLU B CB  1 
ATOM   2803 C  CG  . GLU B  1 136 ? -9.544  14.799  27.046  1.00 9.39  ? 136  GLU B CG  1 
ATOM   2804 C  CD  . GLU B  1 136 ? -10.403 15.765  27.832  1.00 8.20  ? 136  GLU B CD  1 
ATOM   2805 O  OE1 . GLU B  1 136 ? -10.474 16.941  27.437  1.00 10.19 ? 136  GLU B OE1 1 
ATOM   2806 O  OE2 . GLU B  1 136 ? -11.000 15.364  28.846  1.00 8.25  ? 136  GLU B OE2 1 
ATOM   2807 N  N   . GLN B  1 137 ? -13.239 14.884  25.892  1.00 7.13  ? 137  GLN B N   1 
ATOM   2808 C  CA  . GLN B  1 137 ? -14.385 15.800  26.026  1.00 7.90  ? 137  GLN B CA  1 
ATOM   2809 C  C   . GLN B  1 137 ? -14.120 16.942  26.988  1.00 8.59  ? 137  GLN B C   1 
ATOM   2810 O  O   . GLN B  1 137 ? -13.546 16.722  28.033  1.00 7.71  ? 137  GLN B O   1 
ATOM   2811 C  CB  . GLN B  1 137 ? -15.578 15.051  26.598  1.00 7.03  ? 137  GLN B CB  1 
ATOM   2812 C  CG  . GLN B  1 137 ? -16.160 13.987  25.702  1.00 9.02  ? 137  GLN B CG  1 
ATOM   2813 C  CD  . GLN B  1 137 ? -17.184 13.151  26.442  1.00 10.53 ? 137  GLN B CD  1 
ATOM   2814 O  OE1 . GLN B  1 137 ? -18.371 13.485  26.467  1.00 10.51 ? 137  GLN B OE1 1 
ATOM   2815 N  NE2 . GLN B  1 137 ? -16.727 12.084  27.089  1.00 7.35  ? 137  GLN B NE2 1 
ATOM   2816 N  N   . ASP B  1 138 ? -14.605 18.143  26.663  1.00 6.73  ? 138  ASP B N   1 
ATOM   2817 C  CA  . ASP B  1 138 ? -14.673 19.234  27.644  1.00 9.73  ? 138  ASP B CA  1 
ATOM   2818 C  C   . ASP B  1 138 ? -16.117 19.648  27.932  1.00 11.52 ? 138  ASP B C   1 
ATOM   2819 O  O   . ASP B  1 138 ? -16.367 20.512  28.782  1.00 12.51 ? 138  ASP B O   1 
ATOM   2820 C  CB  . ASP B  1 138 ? -13.857 20.448  27.185  1.00 9.67  ? 138  ASP B CB  1 
ATOM   2821 C  CG  . ASP B  1 138 ? -12.362 20.255  27.361  1.00 10.12 ? 138  ASP B CG  1 
ATOM   2822 O  OD1 . ASP B  1 138 ? -11.945 19.381  28.159  1.00 8.84  ? 138  ASP B OD1 1 
ATOM   2823 O  OD2 . ASP B  1 138 ? -11.585 20.973  26.701  1.00 8.44  ? 138  ASP B OD2 1 
ATOM   2824 N  N   . SER B  1 139 ? -17.056 19.033  27.219  1.00 9.71  ? 139  SER B N   1 
ATOM   2825 C  CA  . SER B  1 139 ? -18.483 19.200  27.483  1.00 10.70 ? 139  SER B CA  1 
ATOM   2826 C  C   . SER B  1 139 ? -19.157 17.833  27.508  1.00 16.22 ? 139  SER B C   1 
ATOM   2827 O  O   . SER B  1 139 ? -18.490 16.805  27.387  1.00 12.58 ? 139  SER B O   1 
ATOM   2828 C  CB  . SER B  1 139 ? -19.114 20.054  26.384  1.00 10.67 ? 139  SER B CB  1 
ATOM   2829 O  OG  . SER B  1 139 ? -19.206 19.307  25.179  1.00 12.77 ? 139  SER B OG  1 
ATOM   2830 N  N   . TYR B  1 140 ? -20.479 17.822  27.651  1.00 12.82 ? 140  TYR B N   1 
ATOM   2831 C  CA  . TYR B  1 140 ? -21.228 16.575  27.662  1.00 12.09 ? 140  TYR B CA  1 
ATOM   2832 C  C   . TYR B  1 140 ? -21.366 16.054  26.236  1.00 12.50 ? 140  TYR B C   1 
ATOM   2833 O  O   . TYR B  1 140 ? -22.323 16.382  25.517  1.00 13.95 ? 140  TYR B O   1 
ATOM   2834 C  CB  . TYR B  1 140 ? -22.602 16.785  28.315  1.00 11.98 ? 140  TYR B CB  1 
ATOM   2835 C  CG  . TYR B  1 140 ? -23.369 15.514  28.610  1.00 11.55 ? 140  TYR B CG  1 
ATOM   2836 C  CD1 . TYR B  1 140 ? -22.812 14.499  29.391  1.00 11.00 ? 140  TYR B CD1 1 
ATOM   2837 C  CD2 . TYR B  1 140 ? -24.659 15.338  28.132  1.00 16.86 ? 140  TYR B CD2 1 
ATOM   2838 C  CE1 . TYR B  1 140 ? -23.516 13.355  29.676  1.00 11.91 ? 140  TYR B CE1 1 
ATOM   2839 C  CE2 . TYR B  1 140 ? -25.372 14.186  28.408  1.00 19.89 ? 140  TYR B CE2 1 
ATOM   2840 C  CZ  . TYR B  1 140 ? -24.795 13.200  29.184  1.00 18.32 ? 140  TYR B CZ  1 
ATOM   2841 O  OH  . TYR B  1 140 ? -25.511 12.064  29.460  1.00 17.01 ? 140  TYR B OH  1 
ATOM   2842 N  N   . GLY B  1 141 ? -20.383 15.260  25.824  1.00 8.98  ? 141  GLY B N   1 
ATOM   2843 C  CA  . GLY B  1 141 ? -20.366 14.683  24.490  1.00 10.94 ? 141  GLY B CA  1 
ATOM   2844 C  C   . GLY B  1 141 ? -19.565 15.451  23.447  1.00 11.99 ? 141  GLY B C   1 
ATOM   2845 O  O   . GLY B  1 141 ? -19.554 15.071  22.277  1.00 16.79 ? 141  GLY B O   1 
ATOM   2846 N  N   . GLY B  1 142 ? -18.896 16.523  23.845  1.00 9.37  ? 142  GLY B N   1 
ATOM   2847 C  CA  . GLY B  1 142 ? -18.237 17.363  22.860  1.00 11.56 ? 142  GLY B CA  1 
ATOM   2848 C  C   . GLY B  1 142 ? -17.119 18.244  23.370  1.00 10.06 ? 142  GLY B C   1 
ATOM   2849 O  O   . GLY B  1 142 ? -16.429 17.896  24.326  1.00 8.93  ? 142  GLY B O   1 
ATOM   2850 N  N   . LYS B  1 143 ? -16.953 19.395  22.713  1.00 9.89  ? 143  LYS B N   1 
ATOM   2851 C  CA  . LYS B  1 143 ? -15.870 20.337  22.986  1.00 9.90  ? 143  LYS B CA  1 
ATOM   2852 C  C   . LYS B  1 143 ? -14.523 19.618  22.987  1.00 10.53 ? 143  LYS B C   1 
ATOM   2853 O  O   . LYS B  1 143 ? -13.780 19.650  23.965  1.00 10.78 ? 143  LYS B O   1 
ATOM   2854 C  CB  . LYS B  1 143 ? -16.096 21.098  24.294  1.00 10.97 ? 143  LYS B CB  1 
ATOM   2855 C  CG  . LYS B  1 143 ? -17.164 22.189  24.205  1.00 26.97 ? 143  LYS B CG  1 
ATOM   2856 C  CD  . LYS B  1 143 ? -17.065 23.151  25.390  1.00 24.08 ? 143  LYS B CD  1 
ATOM   2857 C  CE  . LYS B  1 143 ? -18.079 24.287  25.288  1.00 39.14 ? 143  LYS B CE  1 
ATOM   2858 N  NZ  . LYS B  1 143 ? -19.481 23.808  25.453  1.00 51.26 ? 143  LYS B NZ  1 
ATOM   2859 N  N   . PHE B  1 144 ? -14.228 18.977  21.863  1.00 9.79  ? 144  PHE B N   1 
ATOM   2860 C  CA  . PHE B  1 144 ? -13.002 18.206  21.702  1.00 7.87  ? 144  PHE B CA  1 
ATOM   2861 C  C   . PHE B  1 144 ? -11.816 19.126  21.432  1.00 9.28  ? 144  PHE B C   1 
ATOM   2862 O  O   . PHE B  1 144 ? -11.981 20.340  21.215  1.00 11.45 ? 144  PHE B O   1 
ATOM   2863 C  CB  . PHE B  1 144 ? -13.153 17.225  20.533  1.00 8.66  ? 144  PHE B CB  1 
ATOM   2864 C  CG  . PHE B  1 144 ? -14.317 16.270  20.670  1.00 9.88  ? 144  PHE B CG  1 
ATOM   2865 C  CD1 . PHE B  1 144 ? -14.637 15.700  21.894  1.00 9.36  ? 144  PHE B CD1 1 
ATOM   2866 C  CD2 . PHE B  1 144 ? -15.061 15.909  19.554  1.00 12.02 ? 144  PHE B CD2 1 
ATOM   2867 C  CE1 . PHE B  1 144 ? -15.694 14.796  22.006  1.00 11.22 ? 144  PHE B CE1 1 
ATOM   2868 C  CE2 . PHE B  1 144 ? -16.120 15.005  19.662  1.00 14.60 ? 144  PHE B CE2 1 
ATOM   2869 C  CZ  . PHE B  1 144 ? -16.434 14.454  20.887  1.00 13.69 ? 144  PHE B CZ  1 
ATOM   2870 N  N   . ASP B  1 145 ? -10.618 18.543  21.413  1.00 7.44  ? 145  ASP B N   1 
ATOM   2871 C  CA  . ASP B  1 145 ? -9.381  19.296  21.239  1.00 7.27  ? 145  ASP B CA  1 
ATOM   2872 C  C   . ASP B  1 145 ? -8.461  18.443  20.392  1.00 11.29 ? 145  ASP B C   1 
ATOM   2873 O  O   . ASP B  1 145 ? -8.020  17.377  20.823  1.00 10.21 ? 145  ASP B O   1 
ATOM   2874 C  CB  . ASP B  1 145 ? -8.753  19.574  22.620  1.00 8.91  ? 145  ASP B CB  1 
ATOM   2875 C  CG  . ASP B  1 145 ? -7.445  20.365  22.550  1.00 11.68 ? 145  ASP B CG  1 
ATOM   2876 O  OD1 . ASP B  1 145 ? -6.834  20.504  21.468  1.00 11.18 ? 145  ASP B OD1 1 
ATOM   2877 O  OD2 . ASP B  1 145 ? -7.005  20.835  23.623  1.00 12.55 ? 145  ASP B OD2 1 
ATOM   2878 N  N   . ARG B  1 146 ? -8.179  18.893  19.172  1.00 8.90  ? 146  ARG B N   1 
ATOM   2879 C  CA  . ARG B  1 146 ? -7.335  18.094  18.287  1.00 12.13 ? 146  ARG B CA  1 
ATOM   2880 C  C   . ARG B  1 146 ? -5.975  17.741  18.903  1.00 11.30 ? 146  ARG B C   1 
ATOM   2881 O  O   . ARG B  1 146 ? -5.428  16.667  18.633  1.00 9.77  ? 146  ARG B O   1 
ATOM   2882 C  CB  . ARG B  1 146 ? -7.154  18.804  16.947  1.00 13.09 ? 146  ARG B CB  1 
ATOM   2883 C  CG  . ARG B  1 146 ? -6.320  18.018  15.949  1.00 10.58 ? 146  ARG B CG  1 
ATOM   2884 C  CD  . ARG B  1 146 ? -6.486  18.599  14.553  1.00 16.04 ? 146  ARG B CD  1 
ATOM   2885 N  NE  . ARG B  1 146 ? -5.832  19.900  14.445  1.00 16.43 ? 146  ARG B NE  1 
ATOM   2886 C  CZ  . ARG B  1 146 ? -5.825  20.638  13.337  1.00 17.36 ? 146  ARG B CZ  1 
ATOM   2887 N  NH1 . ARG B  1 146 ? -6.452  20.207  12.250  1.00 17.33 ? 146  ARG B NH1 1 
ATOM   2888 N  NH2 . ARG B  1 146 ? -5.201  21.808  13.323  1.00 19.15 ? 146  ARG B NH2 1 
ATOM   2889 N  N   . SER B  1 147 ? -5.436  18.621  19.745  1.00 8.62  ? 147  SER B N   1 
ATOM   2890 C  CA  . SER B  1 147 ? -4.137  18.373  20.368  1.00 11.18 ? 147  SER B CA  1 
ATOM   2891 C  C   . SER B  1 147 ? -4.191  17.307  21.474  1.00 9.86  ? 147  SER B C   1 
ATOM   2892 O  O   . SER B  1 147 ? -3.154  16.910  22.019  1.00 10.45 ? 147  SER B O   1 
ATOM   2893 C  CB  . SER B  1 147 ? -3.508  19.686  20.879  1.00 12.41 ? 147  SER B CB  1 
ATOM   2894 O  OG  . SER B  1 147 ? -4.107  20.118  22.092  1.00 13.86 ? 147  SER B OG  1 
ATOM   2895 N  N   . GLN B  1 148 ? -5.398  16.819  21.772  1.00 8.35  ? 148  GLN B N   1 
ATOM   2896 C  CA  . GLN B  1 148 ? -5.573  15.717  22.707  1.00 9.18  ? 148  GLN B CA  1 
ATOM   2897 C  C   . GLN B  1 148 ? -6.219  14.497  22.048  1.00 6.11  ? 148  GLN B C   1 
ATOM   2898 O  O   . GLN B  1 148 ? -6.538  13.517  22.730  1.00 8.69  ? 148  GLN B O   1 
ATOM   2899 C  CB  . GLN B  1 148 ? -6.457  16.167  23.873  1.00 10.57 ? 148  GLN B CB  1 
ATOM   2900 C  CG  . GLN B  1 148 ? -5.903  17.366  24.636  1.00 10.03 ? 148  GLN B CG  1 
ATOM   2901 C  CD  . GLN B  1 148 ? -6.850  17.809  25.734  1.00 9.53  ? 148  GLN B CD  1 
ATOM   2902 O  OE1 . GLN B  1 148 ? -8.044  17.981  25.505  1.00 9.83  ? 148  GLN B OE1 1 
ATOM   2903 N  NE2 . GLN B  1 148 ? -6.316  18.015  26.928  1.00 16.79 ? 148  GLN B NE2 1 
ATOM   2904 N  N   . SER B  1 149 ? -6.417  14.558  20.733  1.00 6.94  ? 149  SER B N   1 
ATOM   2905 C  CA  . SER B  1 149 ? -7.047  13.454  20.016  1.00 8.08  ? 149  SER B CA  1 
ATOM   2906 C  C   . SER B  1 149 ? -6.176  12.210  20.027  1.00 6.67  ? 149  SER B C   1 
ATOM   2907 O  O   . SER B  1 149 ? -4.955  12.289  20.051  1.00 8.78  ? 149  SER B O   1 
ATOM   2908 C  CB  . SER B  1 149 ? -7.402  13.847  18.573  1.00 9.15  ? 149  SER B CB  1 
ATOM   2909 O  OG  . SER B  1 149 ? -6.250  14.186  17.809  1.00 8.71  ? 149  SER B OG  1 
ATOM   2910 N  N   . PHE B  1 150 ? -6.822  11.048  20.002  1.00 4.42  ? 150  PHE B N   1 
ATOM   2911 C  CA  . PHE B  1 150 ? -6.087  9.789   19.911  1.00 5.84  ? 150  PHE B CA  1 
ATOM   2912 C  C   . PHE B  1 150 ? -5.962  9.354   18.459  1.00 7.41  ? 150  PHE B C   1 
ATOM   2913 O  O   . PHE B  1 150 ? -6.954  9.300   17.726  1.00 11.84 ? 150  PHE B O   1 
ATOM   2914 C  CB  . PHE B  1 150 ? -6.801  8.700   20.730  1.00 6.26  ? 150  PHE B CB  1 
ATOM   2915 C  CG  . PHE B  1 150 ? -6.156  7.338   20.605  1.00 6.82  ? 150  PHE B CG  1 
ATOM   2916 C  CD1 . PHE B  1 150 ? -5.059  7.013   21.373  1.00 8.18  ? 150  PHE B CD1 1 
ATOM   2917 C  CD2 . PHE B  1 150 ? -6.644  6.409   19.703  1.00 8.15  ? 150  PHE B CD2 1 
ATOM   2918 C  CE1 . PHE B  1 150 ? -4.450  5.774   21.249  1.00 9.79  ? 150  PHE B CE1 1 
ATOM   2919 C  CE2 . PHE B  1 150 ? -6.046  5.166   19.569  1.00 7.27  ? 150  PHE B CE2 1 
ATOM   2920 C  CZ  . PHE B  1 150 ? -4.954  4.845   20.349  1.00 9.44  ? 150  PHE B CZ  1 
ATOM   2921 N  N   . VAL B  1 151 ? -4.736  9.052   18.037  1.00 5.67  ? 151  VAL B N   1 
ATOM   2922 C  CA  . VAL B  1 151 ? -4.499  8.530   16.700  1.00 5.66  ? 151  VAL B CA  1 
ATOM   2923 C  C   . VAL B  1 151 ? -3.885  7.159   16.898  1.00 6.80  ? 151  VAL B C   1 
ATOM   2924 O  O   . VAL B  1 151 ? -2.916  7.012   17.651  1.00 9.39  ? 151  VAL B O   1 
ATOM   2925 C  CB  . VAL B  1 151 ? -3.535  9.410   15.907  1.00 8.02  ? 151  VAL B CB  1 
ATOM   2926 C  CG1 . VAL B  1 151 ? -3.326  8.820   14.505  1.00 9.24  ? 151  VAL B CG1 1 
ATOM   2927 C  CG2 . VAL B  1 151 ? -4.087  10.824  15.795  1.00 8.89  ? 151  VAL B CG2 1 
ATOM   2928 N  N   . GLY B  1 152 ? -4.477  6.158   16.265  1.00 7.69  ? 152  GLY B N   1 
ATOM   2929 C  CA  . GLY B  1 152 ? -4.011  4.791   16.418  1.00 7.67  ? 152  GLY B CA  1 
ATOM   2930 C  C   . GLY B  1 152 ? -5.170  3.839   16.617  1.00 7.04  ? 152  GLY B C   1 
ATOM   2931 O  O   . GLY B  1 152 ? -6.274  4.059   16.111  1.00 7.73  ? 152  GLY B O   1 
ATOM   2932 N  N   . GLU B  1 153 ? -4.923  2.772   17.369  1.00 6.73  ? 153  GLU B N   1 
ATOM   2933 C  CA  . GLU B  1 153 ? -5.882  1.671   17.434  1.00 6.17  ? 153  GLU B CA  1 
ATOM   2934 C  C   . GLU B  1 153 ? -6.235  1.300   18.869  1.00 6.44  ? 153  GLU B C   1 
ATOM   2935 O  O   . GLU B  1 153 ? -5.367  1.290   19.745  1.00 8.63  ? 153  GLU B O   1 
ATOM   2936 C  CB  . GLU B  1 153 ? -5.292  0.448   16.717  1.00 8.24  ? 153  GLU B CB  1 
ATOM   2937 C  CG  . GLU B  1 153 ? -4.757  0.783   15.310  1.00 7.83  ? 153  GLU B CG  1 
ATOM   2938 C  CD  . GLU B  1 153 ? -4.160  -0.419  14.599  1.00 12.47 ? 153  GLU B CD  1 
ATOM   2939 O  OE1 . GLU B  1 153 ? -4.738  -1.517  14.696  1.00 9.45  ? 153  GLU B OE1 1 
ATOM   2940 O  OE2 . GLU B  1 153 ? -3.133  -0.253  13.926  1.00 11.75 ? 153  GLU B OE2 1 
ATOM   2941 N  N   . ILE B  1 154 ? -7.512  1.005   19.100  1.00 7.48  ? 154  ILE B N   1 
ATOM   2942 C  CA  . ILE B  1 154 ? -7.989  0.544   20.403  1.00 7.21  ? 154  ILE B CA  1 
ATOM   2943 C  C   . ILE B  1 154 ? -8.860  -0.694  20.213  1.00 8.42  ? 154  ILE B C   1 
ATOM   2944 O  O   . ILE B  1 154 ? -9.692  -0.746  19.307  1.00 10.84 ? 154  ILE B O   1 
ATOM   2945 C  CB  . ILE B  1 154 ? -8.808  1.633   21.132  1.00 7.90  ? 154  ILE B CB  1 
ATOM   2946 C  CG1 . ILE B  1 154 ? -7.909  2.820   21.491  1.00 10.17 ? 154  ILE B CG1 1 
ATOM   2947 C  CG2 . ILE B  1 154 ? -9.457  1.067   22.404  1.00 10.60 ? 154  ILE B CG2 1 
ATOM   2948 C  CD1 . ILE B  1 154 ? -8.663  4.037   22.026  1.00 14.23 ? 154  ILE B CD1 1 
ATOM   2949 N  N   . GLY B  1 155 ? -8.662  -1.691  21.067  1.00 7.59  ? 155  GLY B N   1 
ATOM   2950 C  CA  . GLY B  1 155 ? -9.436  -2.921  20.986  1.00 11.59 ? 155  GLY B CA  1 
ATOM   2951 C  C   . GLY B  1 155 ? -9.604  -3.564  22.351  1.00 9.71  ? 155  GLY B C   1 
ATOM   2952 O  O   . GLY B  1 155 ? -9.061  -3.076  23.337  1.00 9.16  ? 155  GLY B O   1 
ATOM   2953 N  N   . ASP B  1 156 ? -10.361 -4.661  22.401  1.00 9.24  ? 156  ASP B N   1 
ATOM   2954 C  CA  . ASP B  1 156 ? -10.531 -5.443  23.625  1.00 7.60  ? 156  ASP B CA  1 
ATOM   2955 C  C   . ASP B  1 156 ? -10.867 -4.612  24.855  1.00 9.08  ? 156  ASP B C   1 
ATOM   2956 O  O   . ASP B  1 156 ? -10.263 -4.780  25.912  1.00 8.40  ? 156  ASP B O   1 
ATOM   2957 C  CB  . ASP B  1 156 ? -9.278  -6.294  23.892  1.00 9.70  ? 156  ASP B CB  1 
ATOM   2958 C  CG  . ASP B  1 156 ? -9.082  -7.366  22.844  1.00 19.55 ? 156  ASP B CG  1 
ATOM   2959 O  OD1 . ASP B  1 156 ? -10.032 -7.608  22.070  1.00 16.81 ? 156  ASP B OD1 1 
ATOM   2960 O  OD2 . ASP B  1 156 ? -7.983  -7.959  22.793  1.00 18.77 ? 156  ASP B OD2 1 
ATOM   2961 N  N   . LEU B  1 157 ? -11.849 -3.725  24.709  1.00 8.54  ? 157  LEU B N   1 
ATOM   2962 C  CA  . LEU B  1 157 ? -12.277 -2.863  25.805  1.00 9.26  ? 157  LEU B CA  1 
ATOM   2963 C  C   . LEU B  1 157 ? -13.394 -3.483  26.632  1.00 8.98  ? 157  LEU B C   1 
ATOM   2964 O  O   . LEU B  1 157 ? -14.409 -3.913  26.088  1.00 8.64  ? 157  LEU B O   1 
ATOM   2965 C  CB  . LEU B  1 157 ? -12.705 -1.488  25.274  1.00 9.05  ? 157  LEU B CB  1 
ATOM   2966 C  CG  . LEU B  1 157 ? -12.946 -0.424  26.356  1.00 8.70  ? 157  LEU B CG  1 
ATOM   2967 C  CD1 . LEU B  1 157 ? -12.582 0.952   25.823  1.00 9.89  ? 157  LEU B CD1 1 
ATOM   2968 C  CD2 . LEU B  1 157 ? -14.393 -0.431  26.846  1.00 10.50 ? 157  LEU B CD2 1 
ATOM   2969 N  N   . TYR B  1 158 ? -13.181 -3.520  27.944  1.00 7.62  ? 158  TYR B N   1 
ATOM   2970 C  CA  . TYR B  1 158 ? -14.138 -4.067  28.906  1.00 8.66  ? 158  TYR B CA  1 
ATOM   2971 C  C   . TYR B  1 158 ? -14.192 -3.172  30.120  1.00 9.13  ? 158  TYR B C   1 
ATOM   2972 O  O   . TYR B  1 158 ? -13.177 -2.608  30.522  1.00 9.14  ? 158  TYR B O   1 
ATOM   2973 C  CB  . TYR B  1 158 ? -13.698 -5.456  29.370  1.00 6.93  ? 158  TYR B CB  1 
ATOM   2974 C  CG  . TYR B  1 158 ? -13.655 -6.455  28.253  1.00 8.48  ? 158  TYR B CG  1 
ATOM   2975 C  CD1 . TYR B  1 158 ? -14.758 -7.253  27.957  1.00 10.98 ? 158  TYR B CD1 1 
ATOM   2976 C  CD2 . TYR B  1 158 ? -12.518 -6.589  27.472  1.00 9.82  ? 158  TYR B CD2 1 
ATOM   2977 C  CE1 . TYR B  1 158 ? -14.717 -8.167  26.908  1.00 13.67 ? 158  TYR B CE1 1 
ATOM   2978 C  CE2 . TYR B  1 158 ? -12.464 -7.492  26.432  1.00 10.54 ? 158  TYR B CE2 1 
ATOM   2979 C  CZ  . TYR B  1 158 ? -13.560 -8.281  26.154  1.00 15.39 ? 158  TYR B CZ  1 
ATOM   2980 O  OH  . TYR B  1 158 ? -13.481 -9.179  25.106  1.00 15.18 ? 158  TYR B OH  1 
ATOM   2981 N  N   . MET B  1 159 ? -15.375 -3.044  30.716  1.00 8.22  ? 159  MET B N   1 
ATOM   2982 C  CA  . MET B  1 159 ? -15.494 -2.239  31.922  1.00 9.46  ? 159  MET B CA  1 
ATOM   2983 C  C   . MET B  1 159 ? -16.465 -2.925  32.879  1.00 9.17  ? 159  MET B C   1 
ATOM   2984 O  O   . MET B  1 159 ? -17.564 -3.305  32.477  1.00 10.59 ? 159  MET B O   1 
ATOM   2985 C  CB  . MET B  1 159 ? -15.956 -0.823  31.576  1.00 10.59 ? 159  MET B CB  1 
ATOM   2986 C  CG  . MET B  1 159 ? -15.846 0.156   32.734  1.00 11.10 ? 159  MET B CG  1 
ATOM   2987 S  SD  . MET B  1 159 ? -16.376 1.815   32.249  1.00 11.37 ? 159  MET B SD  1 
ATOM   2988 C  CE  . MET B  1 159 ? -16.002 2.716   33.752  1.00 13.16 ? 159  MET B CE  1 
ATOM   2989 N  N   . TRP B  1 160 ? -16.034 -3.092  34.127  1.00 8.94  ? 160  TRP B N   1 
ATOM   2990 C  CA  . TRP B  1 160 ? -16.802 -3.797  35.153  1.00 9.98  ? 160  TRP B CA  1 
ATOM   2991 C  C   . TRP B  1 160 ? -17.127 -2.849  36.292  1.00 14.12 ? 160  TRP B C   1 
ATOM   2992 O  O   . TRP B  1 160 ? -16.348 -1.940  36.581  1.00 11.51 ? 160  TRP B O   1 
ATOM   2993 C  CB  . TRP B  1 160 ? -15.932 -4.895  35.765  1.00 10.44 ? 160  TRP B CB  1 
ATOM   2994 C  CG  . TRP B  1 160 ? -15.500 -5.998  34.864  1.00 11.29 ? 160  TRP B CG  1 
ATOM   2995 C  CD1 . TRP B  1 160 ? -16.078 -7.229  34.753  1.00 11.75 ? 160  TRP B CD1 1 
ATOM   2996 C  CD2 . TRP B  1 160 ? -14.352 -6.016  34.000  1.00 11.15 ? 160  TRP B CD2 1 
ATOM   2997 N  NE1 . TRP B  1 160 ? -15.381 -8.001  33.860  1.00 11.28 ? 160  TRP B NE1 1 
ATOM   2998 C  CE2 . TRP B  1 160 ? -14.317 -7.284  33.382  1.00 10.24 ? 160  TRP B CE2 1 
ATOM   2999 C  CE3 . TRP B  1 160 ? -13.363 -5.083  33.681  1.00 11.91 ? 160  TRP B CE3 1 
ATOM   3000 C  CZ2 . TRP B  1 160 ? -13.331 -7.644  32.464  1.00 12.23 ? 160  TRP B CZ2 1 
ATOM   3001 C  CZ3 . TRP B  1 160 ? -12.382 -5.444  32.769  1.00 11.29 ? 160  TRP B CZ3 1 
ATOM   3002 C  CH2 . TRP B  1 160 ? -12.379 -6.711  32.167  1.00 11.21 ? 160  TRP B CH2 1 
ATOM   3003 N  N   . ASP B  1 161 ? -18.239 -3.087  36.987  1.00 10.25 ? 161  ASP B N   1 
ATOM   3004 C  CA  . ASP B  1 161 ? -18.584 -2.246  38.128  1.00 10.97 ? 161  ASP B CA  1 
ATOM   3005 C  C   . ASP B  1 161 ? -17.999 -2.756  39.447  1.00 13.91 ? 161  ASP B C   1 
ATOM   3006 O  O   . ASP B  1 161 ? -18.574 -2.550  40.522  1.00 14.80 ? 161  ASP B O   1 
ATOM   3007 C  CB  . ASP B  1 161 ? -20.103 -2.056  38.228  1.00 11.00 ? 161  ASP B CB  1 
ATOM   3008 C  CG  . ASP B  1 161 ? -20.817 -3.295  38.734  1.00 17.04 ? 161  ASP B CG  1 
ATOM   3009 O  OD1 . ASP B  1 161 ? -20.227 -4.394  38.672  1.00 17.05 ? 161  ASP B OD1 1 
ATOM   3010 O  OD2 . ASP B  1 161 ? -21.980 -3.155  39.185  1.00 18.65 ? 161  ASP B OD2 1 
ATOM   3011 N  N   . SER B  1 162 ? -16.843 -3.407  39.361  1.00 10.89 ? 162  SER B N   1 
ATOM   3012 C  CA  . SER B  1 162 ? -16.121 -3.849  40.543  1.00 12.88 ? 162  SER B CA  1 
ATOM   3013 C  C   . SER B  1 162 ? -14.618 -3.703  40.340  1.00 13.85 ? 162  SER B C   1 
ATOM   3014 O  O   . SER B  1 162 ? -14.161 -3.497  39.221  1.00 13.22 ? 162  SER B O   1 
ATOM   3015 C  CB  . SER B  1 162 ? -16.447 -5.314  40.837  1.00 12.86 ? 162  SER B CB  1 
ATOM   3016 O  OG  . SER B  1 162 ? -16.043 -6.155  39.764  1.00 17.31 ? 162  SER B OG  1 
ATOM   3017 N  N   . VAL B  1 163 ? -13.861 -3.825  41.429  1.00 11.16 ? 163  VAL B N   1 
ATOM   3018 C  CA  . VAL B  1 163 ? -12.406 -3.806  41.356  1.00 14.78 ? 163  VAL B CA  1 
ATOM   3019 C  C   . VAL B  1 163 ? -11.871 -5.220  41.118  1.00 12.62 ? 163  VAL B C   1 
ATOM   3020 O  O   . VAL B  1 163 ? -11.994 -6.095  41.975  1.00 16.00 ? 163  VAL B O   1 
ATOM   3021 C  CB  . VAL B  1 163 ? -11.795 -3.244  42.653  1.00 13.61 ? 163  VAL B CB  1 
ATOM   3022 C  CG1 . VAL B  1 163 ? -10.272 -3.288  42.589  1.00 14.32 ? 163  VAL B CG1 1 
ATOM   3023 C  CG2 . VAL B  1 163 ? -12.299 -1.824  42.907  1.00 17.74 ? 163  VAL B CG2 1 
ATOM   3024 N  N   . LEU B  1 164 ? -11.269 -5.441  39.958  1.00 9.99  ? 164  LEU B N   1 
ATOM   3025 C  CA  . LEU B  1 164 ? -10.762 -6.770  39.615  1.00 12.21 ? 164  LEU B CA  1 
ATOM   3026 C  C   . LEU B  1 164 ? -9.528  -7.143  40.425  1.00 14.40 ? 164  LEU B C   1 
ATOM   3027 O  O   . LEU B  1 164 ? -8.612  -6.341  40.580  1.00 15.18 ? 164  LEU B O   1 
ATOM   3028 C  CB  . LEU B  1 164 ? -10.409 -6.840  38.125  1.00 12.78 ? 164  LEU B CB  1 
ATOM   3029 C  CG  . LEU B  1 164 ? -11.558 -6.761  37.117  1.00 19.79 ? 164  LEU B CG  1 
ATOM   3030 C  CD1 . LEU B  1 164 ? -11.039 -7.159  35.740  1.00 16.76 ? 164  LEU B CD1 1 
ATOM   3031 C  CD2 . LEU B  1 164 ? -12.714 -7.653  37.523  1.00 21.45 ? 164  LEU B CD2 1 
ATOM   3032 N  N   . PRO B  1 165 ? -9.489  -8.382  40.932  1.00 13.43 ? 165  PRO B N   1 
ATOM   3033 C  CA  . PRO B  1 165 ? -8.244  -8.865  41.541  1.00 14.71 ? 165  PRO B CA  1 
ATOM   3034 C  C   . PRO B  1 165 ? -7.212  -9.200  40.457  1.00 14.23 ? 165  PRO B C   1 
ATOM   3035 O  O   . PRO B  1 165 ? -7.570  -9.310  39.284  1.00 15.26 ? 165  PRO B O   1 
ATOM   3036 C  CB  . PRO B  1 165 ? -8.688  -10.134 42.278  1.00 21.73 ? 165  PRO B CB  1 
ATOM   3037 C  CG  . PRO B  1 165 ? -9.861  -10.633 41.491  1.00 18.53 ? 165  PRO B CG  1 
ATOM   3038 C  CD  . PRO B  1 165 ? -10.552 -9.406  40.913  1.00 13.89 ? 165  PRO B CD  1 
ATOM   3039 N  N   . PRO B  1 166 ? -5.939  -9.362  40.841  1.00 14.83 ? 166  PRO B N   1 
ATOM   3040 C  CA  . PRO B  1 166 ? -4.860  -9.577  39.870  1.00 14.34 ? 166  PRO B CA  1 
ATOM   3041 C  C   . PRO B  1 166 ? -5.123  -10.722 38.900  1.00 16.36 ? 166  PRO B C   1 
ATOM   3042 O  O   . PRO B  1 166 ? -4.804  -10.575 37.730  1.00 14.90 ? 166  PRO B O   1 
ATOM   3043 C  CB  . PRO B  1 166 ? -3.655  -9.883  40.758  1.00 18.29 ? 166  PRO B CB  1 
ATOM   3044 C  CG  . PRO B  1 166 ? -3.941  -9.124  42.014  1.00 16.71 ? 166  PRO B CG  1 
ATOM   3045 C  CD  . PRO B  1 166 ? -5.424  -9.241  42.216  1.00 18.30 ? 166  PRO B CD  1 
ATOM   3046 N  N   . GLU B  1 167 ? -5.697  -11.831 39.365  1.00 13.26 ? 167  GLU B N   1 
ATOM   3047 C  CA  . GLU B  1 167 ? -5.917  -12.963 38.474  1.00 21.20 ? 167  GLU B CA  1 
ATOM   3048 C  C   . GLU B  1 167 ? -6.864  -12.609 37.323  1.00 14.00 ? 167  GLU B C   1 
ATOM   3049 O  O   . GLU B  1 167 ? -6.678  -13.076 36.197  1.00 14.72 ? 167  GLU B O   1 
ATOM   3050 C  CB  . GLU B  1 167 ? -6.414  -14.194 39.241  1.00 21.59 ? 167  GLU B CB  1 
ATOM   3051 C  CG  . GLU B  1 167 ? -7.716  -13.993 40.001  1.00 20.42 ? 167  GLU B CG  1 
ATOM   3052 C  CD  . GLU B  1 167 ? -7.513  -13.513 41.434  1.00 29.09 ? 167  GLU B CD  1 
ATOM   3053 O  OE1 . GLU B  1 167 ? -6.473  -12.877 41.730  1.00 24.40 ? 167  GLU B OE1 1 
ATOM   3054 O  OE2 . GLU B  1 167 ? -8.405  -13.776 42.270  1.00 30.19 ? 167  GLU B OE2 1 
ATOM   3055 N  N   . ASN B  1 168 ? -7.858  -11.766 37.601  1.00 14.03 ? 168  ASN B N   1 
ATOM   3056 C  CA  . ASN B  1 168 ? -8.800  -11.338 36.569  1.00 13.34 ? 168  ASN B CA  1 
ATOM   3057 C  C   . ASN B  1 168 ? -8.157  -10.339 35.612  1.00 12.95 ? 168  ASN B C   1 
ATOM   3058 O  O   . ASN B  1 168 ? -8.463  -10.319 34.418  1.00 13.23 ? 168  ASN B O   1 
ATOM   3059 C  CB  . ASN B  1 168 ? -10.053 -10.717 37.190  1.00 14.16 ? 168  ASN B CB  1 
ATOM   3060 C  CG  . ASN B  1 168 ? -10.940 -11.739 37.890  1.00 22.27 ? 168  ASN B CG  1 
ATOM   3061 O  OD1 . ASN B  1 168 ? -10.794 -12.953 37.708  1.00 24.42 ? 168  ASN B OD1 1 
ATOM   3062 N  ND2 . ASN B  1 168 ? -11.866 -11.246 38.696  1.00 17.36 ? 168  ASN B ND2 1 
ATOM   3063 N  N   . ILE B  1 169 ? -7.286  -9.489  36.149  1.00 12.59 ? 169  ILE B N   1 
ATOM   3064 C  CA  . ILE B  1 169 ? -6.526  -8.574  35.311  1.00 13.68 ? 169  ILE B CA  1 
ATOM   3065 C  C   . ILE B  1 169 ? -5.647  -9.373  34.360  1.00 15.00 ? 169  ILE B C   1 
ATOM   3066 O  O   . ILE B  1 169 ? -5.577  -9.080  33.168  1.00 12.55 ? 169  ILE B O   1 
ATOM   3067 C  CB  . ILE B  1 169 ? -5.624  -7.642  36.141  1.00 12.60 ? 169  ILE B CB  1 
ATOM   3068 C  CG1 . ILE B  1 169 ? -6.456  -6.766  37.084  1.00 15.50 ? 169  ILE B CG1 1 
ATOM   3069 C  CG2 . ILE B  1 169 ? -4.777  -6.775  35.214  1.00 12.54 ? 169  ILE B CG2 1 
ATOM   3070 C  CD1 . ILE B  1 169 ? -7.230  -5.670  36.378  1.00 20.08 ? 169  ILE B CD1 1 
ATOM   3071 N  N   . LEU B  1 170 ? -4.976  -10.396 34.885  1.00 12.19 ? 170  LEU B N   1 
ATOM   3072 C  CA  . LEU B  1 170 ? -4.129  -11.219 34.034  1.00 15.72 ? 170  LEU B CA  1 
ATOM   3073 C  C   . LEU B  1 170 ? -4.944  -11.928 32.947  1.00 14.01 ? 170  LEU B C   1 
ATOM   3074 O  O   . LEU B  1 170 ? -4.519  -11.987 31.793  1.00 13.46 ? 170  LEU B O   1 
ATOM   3075 C  CB  . LEU B  1 170 ? -3.313  -12.212 34.869  1.00 14.75 ? 170  LEU B CB  1 
ATOM   3076 C  CG  . LEU B  1 170 ? -2.222  -11.569 35.738  1.00 32.91 ? 170  LEU B CG  1 
ATOM   3077 C  CD1 . LEU B  1 170 ? -1.294  -12.620 36.336  1.00 34.56 ? 170  LEU B CD1 1 
ATOM   3078 C  CD2 . LEU B  1 170 ? -1.414  -10.528 34.959  1.00 28.01 ? 170  LEU B CD2 1 
ATOM   3079 N  N   . SER B  1 171 ? -6.114  -12.447 33.314  1.00 14.34 ? 171  SER B N   1 
ATOM   3080 C  CA  . SER B  1 171 ? -7.024  -13.053 32.345  1.00 15.42 ? 171  SER B CA  1 
ATOM   3081 C  C   . SER B  1 171 ? -7.353  -12.106 31.197  1.00 13.32 ? 171  SER B C   1 
ATOM   3082 O  O   . SER B  1 171 ? -7.293  -12.487 30.034  1.00 15.61 ? 171  SER B O   1 
ATOM   3083 C  CB  . SER B  1 171 ? -8.313  -13.526 33.028  1.00 19.32 ? 171  SER B CB  1 
ATOM   3084 O  OG  . SER B  1 171 ? -8.035  -14.568 33.946  1.00 21.84 ? 171  SER B OG  1 
ATOM   3085 N  N   . ALA B  1 172 ? -7.686  -10.862 31.522  1.00 13.21 ? 172  ALA B N   1 
ATOM   3086 C  CA  . ALA B  1 172 ? -7.959  -9.870  30.478  1.00 12.64 ? 172  ALA B CA  1 
ATOM   3087 C  C   . ALA B  1 172 ? -6.733  -9.652  29.580  1.00 13.69 ? 172  ALA B C   1 
ATOM   3088 O  O   . ALA B  1 172 ? -6.831  -9.661  28.348  1.00 12.34 ? 172  ALA B O   1 
ATOM   3089 C  CB  . ALA B  1 172 ? -8.430  -8.545  31.111  1.00 11.82 ? 172  ALA B CB  1 
ATOM   3090 N  N   . TYR B  1 173 ? -5.574  -9.482  30.205  1.00 13.31 ? 173  TYR B N   1 
ATOM   3091 C  CA  . TYR B  1 173 ? -4.338  -9.245  29.474  1.00 13.47 ? 173  TYR B CA  1 
ATOM   3092 C  C   . TYR B  1 173 ? -4.083  -10.402 28.498  1.00 17.20 ? 173  TYR B C   1 
ATOM   3093 O  O   . TYR B  1 173 ? -3.683  -10.193 27.346  1.00 16.62 ? 173  TYR B O   1 
ATOM   3094 C  CB  . TYR B  1 173 ? -3.180  -9.093  30.463  1.00 13.03 ? 173  TYR B CB  1 
ATOM   3095 C  CG  . TYR B  1 173 ? -1.810  -9.061  29.819  1.00 11.67 ? 173  TYR B CG  1 
ATOM   3096 C  CD1 . TYR B  1 173 ? -1.513  -8.152  28.817  1.00 14.52 ? 173  TYR B CD1 1 
ATOM   3097 C  CD2 . TYR B  1 173 ? -0.815  -9.939  30.224  1.00 18.18 ? 173  TYR B CD2 1 
ATOM   3098 C  CE1 . TYR B  1 173 ? -0.259  -8.125  28.225  1.00 17.50 ? 173  TYR B CE1 1 
ATOM   3099 C  CE2 . TYR B  1 173 ? 0.432   -9.916  29.649  1.00 20.21 ? 173  TYR B CE2 1 
ATOM   3100 C  CZ  . TYR B  1 173 ? 0.708   -9.008  28.653  1.00 23.47 ? 173  TYR B CZ  1 
ATOM   3101 O  OH  . TYR B  1 173 ? 1.958   -8.990  28.077  1.00 24.52 ? 173  TYR B OH  1 
ATOM   3102 N  N   . GLN B  1 174 ? -4.368  -11.617 28.955  1.00 14.95 ? 174  GLN B N   1 
ATOM   3103 C  CA  . GLN B  1 174 ? -4.078  -12.816 28.168  1.00 17.25 ? 174  GLN B CA  1 
ATOM   3104 C  C   . GLN B  1 174 ? -5.110  -13.111 27.089  1.00 20.29 ? 174  GLN B C   1 
ATOM   3105 O  O   . GLN B  1 174 ? -4.905  -14.003 26.264  1.00 23.79 ? 174  GLN B O   1 
ATOM   3106 C  CB  . GLN B  1 174 ? -3.942  -14.035 29.081  1.00 19.13 ? 174  GLN B CB  1 
ATOM   3107 C  CG  . GLN B  1 174 ? -2.700  -14.026 29.958  1.00 23.43 ? 174  GLN B CG  1 
ATOM   3108 C  CD  . GLN B  1 174 ? -2.826  -14.991 31.119  1.00 29.70 ? 174  GLN B CD  1 
ATOM   3109 O  OE1 . GLN B  1 174 ? -3.817  -15.714 31.233  1.00 30.01 ? 174  GLN B OE1 1 
ATOM   3110 N  NE2 . GLN B  1 174 ? -1.828  -15.001 31.993  1.00 45.66 ? 174  GLN B NE2 1 
ATOM   3111 N  N   . GLY B  1 175 ? -6.227  -12.390 27.110  1.00 15.19 ? 175  GLY B N   1 
ATOM   3112 C  CA  . GLY B  1 175 ? -7.249  -12.538 26.093  1.00 17.45 ? 175  GLY B CA  1 
ATOM   3113 C  C   . GLY B  1 175 ? -8.445  -13.376 26.507  1.00 16.59 ? 175  GLY B C   1 
ATOM   3114 O  O   . GLY B  1 175 ? -9.262  -13.736 25.664  1.00 21.06 ? 175  GLY B O   1 
ATOM   3115 N  N   . THR B  1 176 ? -8.551  -13.686 27.798  1.00 14.46 ? 176  THR B N   1 
ATOM   3116 C  CA  . THR B  1 176 ? -9.712  -14.405 28.332  1.00 16.53 ? 176  THR B CA  1 
ATOM   3117 C  C   . THR B  1 176 ? -10.383 -13.638 29.480  1.00 13.77 ? 176  THR B C   1 
ATOM   3118 O  O   . THR B  1 176 ? -10.471 -14.130 30.606  1.00 19.74 ? 176  THR B O   1 
ATOM   3119 C  CB  . THR B  1 176 ? -9.325  -15.823 28.814  1.00 22.69 ? 176  THR B CB  1 
ATOM   3120 O  OG1 . THR B  1 176 ? -8.299  -15.730 29.809  1.00 24.34 ? 176  THR B OG1 1 
ATOM   3121 C  CG2 . THR B  1 176 ? -8.821  -16.662 27.642  1.00 22.65 ? 176  THR B CG2 1 
ATOM   3122 N  N   . PRO B  1 177 ? -10.863 -12.415 29.197  1.00 14.80 ? 177  PRO B N   1 
ATOM   3123 C  CA  . PRO B  1 177 ? -11.497 -11.608 30.248  1.00 12.52 ? 177  PRO B CA  1 
ATOM   3124 C  C   . PRO B  1 177 ? -12.782 -12.226 30.783  1.00 16.14 ? 177  PRO B C   1 
ATOM   3125 O  O   . PRO B  1 177 ? -13.499 -12.910 30.052  1.00 17.12 ? 177  PRO B O   1 
ATOM   3126 C  CB  . PRO B  1 177 ? -11.820 -10.291 29.535  1.00 14.29 ? 177  PRO B CB  1 
ATOM   3127 C  CG  . PRO B  1 177 ? -11.879 -10.651 28.068  1.00 14.13 ? 177  PRO B CG  1 
ATOM   3128 C  CD  . PRO B  1 177 ? -10.883 -11.755 27.880  1.00 16.62 ? 177  PRO B CD  1 
ATOM   3129 N  N   . LEU B  1 178 ? -13.067 -11.977 32.054  1.00 17.07 ? 178  LEU B N   1 
ATOM   3130 C  CA  . LEU B  1 178 ? -14.376 -12.299 32.601  1.00 21.69 ? 178  LEU B CA  1 
ATOM   3131 C  C   . LEU B  1 178 ? -15.394 -11.389 31.931  1.00 21.15 ? 178  LEU B C   1 
ATOM   3132 O  O   . LEU B  1 178 ? -15.089 -10.240 31.629  1.00 16.65 ? 178  LEU B O   1 
ATOM   3133 C  CB  . LEU B  1 178 ? -14.386 -12.083 34.111  1.00 24.86 ? 178  LEU B CB  1 
ATOM   3134 C  CG  . LEU B  1 178 ? -13.635 -13.151 34.909  1.00 29.43 ? 178  LEU B CG  1 
ATOM   3135 C  CD1 . LEU B  1 178 ? -12.130 -13.038 34.690  1.00 30.27 ? 178  LEU B CD1 1 
ATOM   3136 C  CD2 . LEU B  1 178 ? -13.979 -13.039 36.386  1.00 35.96 ? 178  LEU B CD2 1 
ATOM   3137 N  N   . PRO B  1 179 ? -16.606 -11.900 31.674  1.00 22.74 ? 179  PRO B N   1 
ATOM   3138 C  CA  . PRO B  1 179 ? -17.614 -11.024 31.062  1.00 22.66 ? 179  PRO B CA  1 
ATOM   3139 C  C   . PRO B  1 179 ? -17.796 -9.736  31.872  1.00 13.23 ? 179  PRO B C   1 
ATOM   3140 O  O   . PRO B  1 179 ? -17.749 -9.753  33.103  1.00 14.27 ? 179  PRO B O   1 
ATOM   3141 C  CB  . PRO B  1 179 ? -18.889 -11.876 31.098  1.00 30.18 ? 179  PRO B CB  1 
ATOM   3142 C  CG  . PRO B  1 179 ? -18.386 -13.299 31.120  1.00 32.90 ? 179  PRO B CG  1 
ATOM   3143 C  CD  . PRO B  1 179 ? -17.124 -13.255 31.938  1.00 33.50 ? 179  PRO B CD  1 
ATOM   3144 N  N   . ALA B  1 180 ? -17.999 -8.630  31.168  1.00 16.90 ? 180  ALA B N   1 
ATOM   3145 C  CA  . ALA B  1 180 ? -18.032 -7.314  31.798  1.00 11.95 ? 180  ALA B CA  1 
ATOM   3146 C  C   . ALA B  1 180 ? -19.438 -6.742  31.730  1.00 13.32 ? 180  ALA B C   1 
ATOM   3147 O  O   . ALA B  1 180 ? -20.153 -6.963  30.748  1.00 19.30 ? 180  ALA B O   1 
ATOM   3148 C  CB  . ALA B  1 180 ? -17.053 -6.372  31.100  1.00 11.14 ? 180  ALA B CB  1 
ATOM   3149 N  N   . ASN B  1 181 ? -19.825 -5.986  32.755  1.00 12.49 ? 181  ASN B N   1 
ATOM   3150 C  CA  . ASN B  1 181 ? -21.216 -5.541  32.861  1.00 10.89 ? 181  ASN B CA  1 
ATOM   3151 C  C   . ASN B  1 181 ? -21.500 -4.070  32.569  1.00 16.71 ? 181  ASN B C   1 
ATOM   3152 O  O   . ASN B  1 181 ? -22.661 -3.682  32.486  1.00 17.80 ? 181  ASN B O   1 
ATOM   3153 C  CB  . ASN B  1 181 ? -21.832 -5.952  34.210  1.00 12.50 ? 181  ASN B CB  1 
ATOM   3154 C  CG  . ASN B  1 181 ? -21.085 -5.389  35.405  1.00 16.11 ? 181  ASN B CG  1 
ATOM   3155 O  OD1 . ASN B  1 181 ? -20.018 -4.782  35.272  1.00 13.81 ? 181  ASN B OD1 1 
ATOM   3156 N  ND2 . ASN B  1 181 ? -21.642 -5.603  36.592  1.00 17.69 ? 181  ASN B ND2 1 
ATOM   3157 N  N   . ILE B  1 182 ? -20.464 -3.248  32.412  1.00 9.40  ? 182  ILE B N   1 
ATOM   3158 C  CA  . ILE B  1 182 ? -20.690 -1.864  32.020  1.00 9.70  ? 182  ILE B CA  1 
ATOM   3159 C  C   . ILE B  1 182 ? -20.457 -1.704  30.521  1.00 10.89 ? 182  ILE B C   1 
ATOM   3160 O  O   . ILE B  1 182 ? -21.305 -1.167  29.799  1.00 12.55 ? 182  ILE B O   1 
ATOM   3161 C  CB  . ILE B  1 182 ? -19.776 -0.893  32.783  1.00 8.32  ? 182  ILE B CB  1 
ATOM   3162 C  CG1 . ILE B  1 182 ? -20.017 -1.017  34.294  1.00 13.48 ? 182  ILE B CG1 1 
ATOM   3163 C  CG2 . ILE B  1 182 ? -20.036 0.541   32.331  1.00 11.42 ? 182  ILE B CG2 1 
ATOM   3164 C  CD1 . ILE B  1 182 ? -19.171 -0.057  35.145  1.00 11.85 ? 182  ILE B CD1 1 
ATOM   3165 N  N   . LEU B  1 183 ? -19.286 -2.151  30.065  1.00 10.07 ? 183  LEU B N   1 
ATOM   3166 C  CA  . LEU B  1 183 ? -18.971 -2.178  28.638  1.00 9.02  ? 183  LEU B CA  1 
ATOM   3167 C  C   . LEU B  1 183 ? -18.313 -3.511  28.320  1.00 10.34 ? 183  LEU B C   1 
ATOM   3168 O  O   . LEU B  1 183 ? -17.478 -3.998  29.076  1.00 11.03 ? 183  LEU B O   1 
ATOM   3169 C  CB  . LEU B  1 183 ? -18.035 -1.026  28.240  1.00 8.72  ? 183  LEU B CB  1 
ATOM   3170 C  CG  . LEU B  1 183 ? -18.558 0.403   28.398  1.00 9.67  ? 183  LEU B CG  1 
ATOM   3171 C  CD1 . LEU B  1 183 ? -17.425 1.397   28.222  1.00 11.11 ? 183  LEU B CD1 1 
ATOM   3172 C  CD2 . LEU B  1 183 ? -19.711 0.705   27.423  1.00 11.02 ? 183  LEU B CD2 1 
ATOM   3173 N  N   . ASP B  1 184 ? -18.707 -4.107  27.206  1.00 10.50 ? 184  ASP B N   1 
ATOM   3174 C  CA  . ASP B  1 184 ? -18.142 -5.403  26.823  1.00 9.30  ? 184  ASP B CA  1 
ATOM   3175 C  C   . ASP B  1 184 ? -17.885 -5.468  25.326  1.00 8.63  ? 184  ASP B C   1 
ATOM   3176 O  O   . ASP B  1 184 ? -18.800 -5.318  24.519  1.00 11.64 ? 184  ASP B O   1 
ATOM   3177 C  CB  . ASP B  1 184 ? -19.062 -6.546  27.273  1.00 13.00 ? 184  ASP B CB  1 
ATOM   3178 C  CG  . ASP B  1 184 ? -18.397 -7.905  27.142  1.00 17.68 ? 184  ASP B CG  1 
ATOM   3179 O  OD1 . ASP B  1 184 ? -18.134 -8.320  26.003  1.00 16.28 ? 184  ASP B OD1 1 
ATOM   3180 O  OD2 . ASP B  1 184 ? -18.125 -8.554  28.179  1.00 26.88 ? 184  ASP B OD2 1 
ATOM   3181 N  N   . TRP B  1 185 ? -16.617 -5.679  24.966  1.00 11.07 ? 185  TRP B N   1 
ATOM   3182 C  CA  . TRP B  1 185 ? -16.184 -5.717  23.577  1.00 10.67 ? 185  TRP B CA  1 
ATOM   3183 C  C   . TRP B  1 185 ? -16.937 -6.748  22.730  1.00 11.27 ? 185  TRP B C   1 
ATOM   3184 O  O   . TRP B  1 185 ? -17.064 -6.580  21.512  1.00 11.26 ? 185  TRP B O   1 
ATOM   3185 C  CB  . TRP B  1 185 ? -14.680 -6.006  23.523  1.00 12.29 ? 185  TRP B CB  1 
ATOM   3186 C  CG  . TRP B  1 185 ? -14.012 -5.585  22.251  1.00 10.51 ? 185  TRP B CG  1 
ATOM   3187 C  CD1 . TRP B  1 185 ? -13.441 -6.399  21.311  1.00 10.03 ? 185  TRP B CD1 1 
ATOM   3188 C  CD2 . TRP B  1 185 ? -13.826 -4.244  21.791  1.00 10.00 ? 185  TRP B CD2 1 
ATOM   3189 N  NE1 . TRP B  1 185 ? -12.902 -5.638  20.292  1.00 11.06 ? 185  TRP B NE1 1 
ATOM   3190 C  CE2 . TRP B  1 185 ? -13.131 -4.313  20.561  1.00 9.60  ? 185  TRP B CE2 1 
ATOM   3191 C  CE3 . TRP B  1 185 ? -14.174 -2.992  22.297  1.00 9.54  ? 185  TRP B CE3 1 
ATOM   3192 C  CZ2 . TRP B  1 185 ? -12.791 -3.177  19.831  1.00 10.83 ? 185  TRP B CZ2 1 
ATOM   3193 C  CZ3 . TRP B  1 185 ? -13.828 -1.853  21.564  1.00 11.71 ? 185  TRP B CZ3 1 
ATOM   3194 C  CH2 . TRP B  1 185 ? -13.147 -1.961  20.345  1.00 11.77 ? 185  TRP B CH2 1 
ATOM   3195 N  N   . GLN B  1 186 ? -17.435 -7.804  23.363  1.00 11.80 ? 186  GLN B N   1 
ATOM   3196 C  CA  . GLN B  1 186 ? -18.146 -8.852  22.621  1.00 12.28 ? 186  GLN B CA  1 
ATOM   3197 C  C   . GLN B  1 186 ? -19.639 -8.563  22.470  1.00 13.82 ? 186  GLN B C   1 
ATOM   3198 O  O   . GLN B  1 186 ? -20.366 -9.313  21.811  1.00 12.41 ? 186  GLN B O   1 
ATOM   3199 C  CB  . GLN B  1 186 ? -17.897 -10.221 23.249  1.00 16.79 ? 186  GLN B CB  1 
ATOM   3200 C  CG  . GLN B  1 186 ? -16.423 -10.593 23.222  1.00 19.72 ? 186  GLN B CG  1 
ATOM   3201 C  CD  . GLN B  1 186 ? -16.052 -11.580 24.293  1.00 43.09 ? 186  GLN B CD  1 
ATOM   3202 O  OE1 . GLN B  1 186 ? -15.210 -11.297 25.149  1.00 37.01 ? 186  GLN B OE1 1 
ATOM   3203 N  NE2 . GLN B  1 186 ? -16.684 -12.748 24.264  1.00 29.70 ? 186  GLN B NE2 1 
ATOM   3204 N  N   . ALA B  1 187 ? -20.084 -7.463  23.066  1.00 14.59 ? 187  ALA B N   1 
ATOM   3205 C  CA  . ALA B  1 187 ? -21.474 -7.033  22.961  1.00 15.99 ? 187  ALA B CA  1 
ATOM   3206 C  C   . ALA B  1 187 ? -21.562 -5.526  23.169  1.00 15.09 ? 187  ALA B C   1 
ATOM   3207 O  O   . ALA B  1 187 ? -22.150 -5.043  24.140  1.00 14.39 ? 187  ALA B O   1 
ATOM   3208 C  CB  . ALA B  1 187 ? -22.320 -7.769  23.977  1.00 14.08 ? 187  ALA B CB  1 
ATOM   3209 N  N   . LEU B  1 188 ? -20.967 -4.790  22.238  1.00 11.47 ? 188  LEU B N   1 
ATOM   3210 C  CA  . LEU B  1 188 ? -20.697 -3.379  22.420  1.00 11.86 ? 188  LEU B CA  1 
ATOM   3211 C  C   . LEU B  1 188 ? -21.724 -2.548  21.668  1.00 12.03 ? 188  LEU B C   1 
ATOM   3212 O  O   . LEU B  1 188 ? -21.993 -2.790  20.487  1.00 15.75 ? 188  LEU B O   1 
ATOM   3213 C  CB  . LEU B  1 188 ? -19.281 -3.040  21.932  1.00 8.77  ? 188  LEU B CB  1 
ATOM   3214 C  CG  . LEU B  1 188 ? -18.767 -1.646  22.321  1.00 11.68 ? 188  LEU B CG  1 
ATOM   3215 C  CD1 . LEU B  1 188 ? -18.477 -1.617  23.817  1.00 13.40 ? 188  LEU B CD1 1 
ATOM   3216 C  CD2 . LEU B  1 188 ? -17.526 -1.294  21.522  1.00 13.29 ? 188  LEU B CD2 1 
ATOM   3217 N  N   . ASN B  1 189 ? -22.302 -1.582  22.369  1.00 11.61 ? 189  ASN B N   1 
ATOM   3218 C  CA  . ASN B  1 189 ? -23.191 -0.614  21.741  1.00 13.22 ? 189  ASN B CA  1 
ATOM   3219 C  C   . ASN B  1 189 ? -22.388 0.646   21.496  1.00 13.40 ? 189  ASN B C   1 
ATOM   3220 O  O   . ASN B  1 189 ? -22.009 1.332   22.440  1.00 15.55 ? 189  ASN B O   1 
ATOM   3221 C  CB  . ASN B  1 189 ? -24.367 -0.313  22.667  1.00 17.10 ? 189  ASN B CB  1 
ATOM   3222 C  CG  . ASN B  1 189 ? -25.437 0.524   22.003  1.00 25.67 ? 189  ASN B CG  1 
ATOM   3223 O  OD1 . ASN B  1 189 ? -25.343 0.854   20.820  1.00 28.55 ? 189  ASN B OD1 1 
ATOM   3224 N  ND2 . ASN B  1 189 ? -26.474 0.868   22.762  1.00 20.25 ? 189  ASN B ND2 1 
ATOM   3225 N  N   . TYR B  1 190 ? -22.093 0.937   20.233  1.00 12.83 ? 190  TYR B N   1 
ATOM   3226 C  CA  . TYR B  1 190 ? -21.233 2.070   19.919  1.00 11.45 ? 190  TYR B CA  1 
ATOM   3227 C  C   . TYR B  1 190 ? -21.783 2.848   18.739  1.00 13.26 ? 190  TYR B C   1 
ATOM   3228 O  O   . TYR B  1 190 ? -22.614 2.344   17.975  1.00 14.70 ? 190  TYR B O   1 
ATOM   3229 C  CB  . TYR B  1 190 ? -19.809 1.601   19.583  1.00 10.76 ? 190  TYR B CB  1 
ATOM   3230 C  CG  . TYR B  1 190 ? -19.744 0.759   18.340  1.00 12.59 ? 190  TYR B CG  1 
ATOM   3231 C  CD1 . TYR B  1 190 ? -19.532 1.339   17.089  1.00 12.43 ? 190  TYR B CD1 1 
ATOM   3232 C  CD2 . TYR B  1 190 ? -19.911 -0.625  18.404  1.00 15.42 ? 190  TYR B CD2 1 
ATOM   3233 C  CE1 . TYR B  1 190 ? -19.497 0.565   15.932  1.00 18.66 ? 190  TYR B CE1 1 
ATOM   3234 C  CE2 . TYR B  1 190 ? -19.874 -1.403  17.260  1.00 18.91 ? 190  TYR B CE2 1 
ATOM   3235 C  CZ  . TYR B  1 190 ? -19.670 -0.805  16.029  1.00 21.82 ? 190  TYR B CZ  1 
ATOM   3236 O  OH  . TYR B  1 190 ? -19.632 -1.583  14.895  1.00 24.78 ? 190  TYR B OH  1 
ATOM   3237 N  N   . GLU B  1 191 ? -21.296 4.074   18.579  1.00 12.23 ? 191  GLU B N   1 
ATOM   3238 C  CA  . GLU B  1 191 ? -21.617 4.854   17.397  1.00 11.26 ? 191  GLU B CA  1 
ATOM   3239 C  C   . GLU B  1 191 ? -20.332 5.465   16.888  1.00 12.41 ? 191  GLU B C   1 
ATOM   3240 O  O   . GLU B  1 191 ? -19.639 6.167   17.625  1.00 12.52 ? 191  GLU B O   1 
ATOM   3241 C  CB  . GLU B  1 191 ? -22.628 5.960   17.733  1.00 14.51 ? 191  GLU B CB  1 
ATOM   3242 C  CG  . GLU B  1 191 ? -23.957 5.434   18.265  1.00 23.11 ? 191  GLU B CG  1 
ATOM   3243 C  CD  . GLU B  1 191 ? -24.855 6.525   18.841  1.00 35.91 ? 191  GLU B CD  1 
ATOM   3244 O  OE1 . GLU B  1 191 ? -24.340 7.485   19.459  1.00 34.40 ? 191  GLU B OE1 1 
ATOM   3245 O  OE2 . GLU B  1 191 ? -26.088 6.412   18.682  1.00 38.90 ? 191  GLU B OE2 1 
ATOM   3246 N  N   . ILE B  1 192 ? -20.004 5.195   15.631  1.00 10.46 ? 192  ILE B N   1 
ATOM   3247 C  CA  . ILE B  1 192 ? -18.856 5.853   15.019  1.00 13.19 ? 192  ILE B CA  1 
ATOM   3248 C  C   . ILE B  1 192 ? -19.248 7.232   14.500  1.00 13.04 ? 192  ILE B C   1 
ATOM   3249 O  O   . ILE B  1 192 ? -20.268 7.375   13.822  1.00 14.33 ? 192  ILE B O   1 
ATOM   3250 C  CB  . ILE B  1 192 ? -18.274 5.010   13.866  1.00 14.32 ? 192  ILE B CB  1 
ATOM   3251 C  CG1 . ILE B  1 192 ? -17.508 3.809   14.436  1.00 13.49 ? 192  ILE B CG1 1 
ATOM   3252 C  CG2 . ILE B  1 192 ? -17.364 5.868   12.975  1.00 14.46 ? 192  ILE B CG2 1 
ATOM   3253 C  CD1 . ILE B  1 192 ? -17.048 2.795   13.384  1.00 16.58 ? 192  ILE B CD1 1 
ATOM   3254 N  N   . ARG B  1 193 ? -18.443 8.243   14.830  1.00 13.13 ? 193  ARG B N   1 
ATOM   3255 C  CA  . ARG B  1 193 ? -18.632 9.593   14.290  1.00 12.93 ? 193  ARG B CA  1 
ATOM   3256 C  C   . ARG B  1 193 ? -17.379 10.027  13.552  1.00 11.54 ? 193  ARG B C   1 
ATOM   3257 O  O   . ARG B  1 193 ? -16.277 9.983   14.096  1.00 12.93 ? 193  ARG B O   1 
ATOM   3258 C  CB  . ARG B  1 193 ? -18.968 10.601  15.398  1.00 13.46 ? 193  ARG B CB  1 
ATOM   3259 C  CG  . ARG B  1 193 ? -20.447 10.623  15.805  1.00 22.46 ? 193  ARG B CG  1 
ATOM   3260 C  CD  . ARG B  1 193 ? -20.844 9.378   16.567  1.00 31.98 ? 193  ARG B CD  1 
ATOM   3261 N  NE  . ARG B  1 193 ? -22.293 9.303   16.771  1.00 48.95 ? 193  ARG B NE  1 
ATOM   3262 C  CZ  . ARG B  1 193 ? -23.156 8.839   15.868  1.00 48.72 ? 193  ARG B CZ  1 
ATOM   3263 N  NH1 . ARG B  1 193 ? -22.724 8.406   14.687  1.00 31.90 ? 193  ARG B NH1 1 
ATOM   3264 N  NH2 . ARG B  1 193 ? -24.455 8.806   16.140  1.00 35.75 ? 193  ARG B NH2 1 
ATOM   3265 N  N   . GLY B  1 194 ? -17.531 10.443  12.299  1.00 14.50 ? 194  GLY B N   1 
ATOM   3266 C  CA  . GLY B  1 194 ? -16.371 10.846  11.527  1.00 12.55 ? 194  GLY B CA  1 
ATOM   3267 C  C   . GLY B  1 194 ? -15.537 9.659   11.061  1.00 12.10 ? 194  GLY B C   1 
ATOM   3268 O  O   . GLY B  1 194 ? -16.064 8.577   10.792  1.00 14.18 ? 194  GLY B O   1 
ATOM   3269 N  N   . TYR B  1 195 ? -14.227 9.863   10.985  1.00 9.94  ? 195  TYR B N   1 
ATOM   3270 C  CA  . TYR B  1 195 ? -13.321 8.894   10.360  1.00 11.55 ? 195  TYR B CA  1 
ATOM   3271 C  C   . TYR B  1 195 ? -12.747 7.922   11.380  1.00 9.52  ? 195  TYR B C   1 
ATOM   3272 O  O   . TYR B  1 195 ? -11.694 8.161   11.966  1.00 11.78 ? 195  TYR B O   1 
ATOM   3273 C  CB  . TYR B  1 195 ? -12.200 9.641   9.646   1.00 10.27 ? 195  TYR B CB  1 
ATOM   3274 C  CG  . TYR B  1 195 ? -11.287 8.810   8.757   1.00 9.33  ? 195  TYR B CG  1 
ATOM   3275 C  CD1 . TYR B  1 195 ? -11.762 7.715   8.044   1.00 10.88 ? 195  TYR B CD1 1 
ATOM   3276 C  CD2 . TYR B  1 195 ? -9.959  9.173   8.593   1.00 10.97 ? 195  TYR B CD2 1 
ATOM   3277 C  CE1 . TYR B  1 195 ? -10.906 6.983   7.208   1.00 8.19  ? 195  TYR B CE1 1 
ATOM   3278 C  CE2 . TYR B  1 195 ? -9.107  8.461   7.770   1.00 14.10 ? 195  TYR B CE2 1 
ATOM   3279 C  CZ  . TYR B  1 195 ? -9.582  7.370   7.081   1.00 12.25 ? 195  TYR B CZ  1 
ATOM   3280 O  OH  . TYR B  1 195 ? -8.718  6.670   6.258   1.00 11.07 ? 195  TYR B OH  1 
ATOM   3281 N  N   . VAL B  1 196 ? -13.467 6.827   11.592  1.00 9.27  ? 196  VAL B N   1 
ATOM   3282 C  CA  . VAL B  1 196 ? -13.007 5.714   12.420  1.00 9.50  ? 196  VAL B CA  1 
ATOM   3283 C  C   . VAL B  1 196 ? -13.335 4.446   11.637  1.00 10.32 ? 196  VAL B C   1 
ATOM   3284 O  O   . VAL B  1 196 ? -14.451 4.290   11.124  1.00 10.86 ? 196  VAL B O   1 
ATOM   3285 C  CB  . VAL B  1 196 ? -13.728 5.667   13.787  1.00 11.23 ? 196  VAL B CB  1 
ATOM   3286 C  CG1 . VAL B  1 196 ? -13.121 4.574   14.693  1.00 9.28  ? 196  VAL B CG1 1 
ATOM   3287 C  CG2 . VAL B  1 196 ? -13.663 7.021   14.471  1.00 9.32  ? 196  VAL B CG2 1 
ATOM   3288 N  N   . ILE B  1 197 ? -12.360 3.552   11.530  1.00 10.15 ? 197  ILE B N   1 
ATOM   3289 C  CA  . ILE B  1 197 ? -12.517 2.370   10.693  1.00 8.55  ? 197  ILE B CA  1 
ATOM   3290 C  C   . ILE B  1 197 ? -12.339 1.127   11.539  1.00 8.78  ? 197  ILE B C   1 
ATOM   3291 O  O   . ILE B  1 197 ? -11.427 1.061   12.349  1.00 11.26 ? 197  ILE B O   1 
ATOM   3292 C  CB  . ILE B  1 197 ? -11.448 2.337   9.581   1.00 10.29 ? 197  ILE B CB  1 
ATOM   3293 C  CG1 . ILE B  1 197 ? -11.518 3.597   8.705   1.00 11.33 ? 197  ILE B CG1 1 
ATOM   3294 C  CG2 . ILE B  1 197 ? -11.597 1.053   8.739   1.00 11.22 ? 197  ILE B CG2 1 
ATOM   3295 C  CD1 . ILE B  1 197 ? -12.725 3.663   7.796   1.00 12.36 ? 197  ILE B CD1 1 
ATOM   3296 N  N   . ILE B  1 198 ? -13.214 0.139   11.370  1.00 7.89  ? 198  ILE B N   1 
ATOM   3297 C  CA  . ILE B  1 198 ? -13.025 -1.113  12.090  1.00 8.16  ? 198  ILE B CA  1 
ATOM   3298 C  C   . ILE B  1 198 ? -12.172 -2.066  11.253  1.00 12.67 ? 198  ILE B C   1 
ATOM   3299 O  O   . ILE B  1 198 ? -12.480 -2.323  10.086  1.00 12.45 ? 198  ILE B O   1 
ATOM   3300 C  CB  . ILE B  1 198 ? -14.359 -1.775  12.433  1.00 10.37 ? 198  ILE B CB  1 
ATOM   3301 C  CG1 . ILE B  1 198 ? -15.178 -0.849  13.333  1.00 14.80 ? 198  ILE B CG1 1 
ATOM   3302 C  CG2 . ILE B  1 198 ? -14.112 -3.102  13.123  1.00 10.52 ? 198  ILE B CG2 1 
ATOM   3303 C  CD1 . ILE B  1 198 ? -16.600 -1.329  13.554  1.00 12.36 ? 198  ILE B CD1 1 
ATOM   3304 N  N   . LYS B  1 199 ? -11.091 -2.562  11.851  1.00 9.44  ? 199  LYS B N   1 
ATOM   3305 C  CA  . LYS B  1 199 ? -10.164 -3.483  11.186  1.00 11.74 ? 199  LYS B CA  1 
ATOM   3306 C  C   . LYS B  1 199 ? -9.866  -4.664  12.087  1.00 10.15 ? 199  LYS B C   1 
ATOM   3307 O  O   . LYS B  1 199 ? -10.077 -4.600  13.297  1.00 10.21 ? 199  LYS B O   1 
ATOM   3308 C  CB  . LYS B  1 199 ? -8.854  -2.772  10.845  1.00 11.04 ? 199  LYS B CB  1 
ATOM   3309 C  CG  . LYS B  1 199 ? -8.959  -1.805  9.684   1.00 10.57 ? 199  LYS B CG  1 
ATOM   3310 C  CD  . LYS B  1 199 ? -9.239  -2.588  8.401   1.00 17.16 ? 199  LYS B CD  1 
ATOM   3311 C  CE  . LYS B  1 199 ? -9.106  -1.720  7.161   1.00 18.25 ? 199  LYS B CE  1 
ATOM   3312 N  NZ  . LYS B  1 199 ? -9.197  -2.557  5.923   1.00 23.34 ? 199  LYS B NZ  1 
ATOM   3313 N  N   . PRO B  1 200 ? -9.364  -5.763  11.503  1.00 10.27 ? 200  PRO B N   1 
ATOM   3314 C  CA  . PRO B  1 200 ? -8.868  -6.838  12.367  1.00 10.05 ? 200  PRO B CA  1 
ATOM   3315 C  C   . PRO B  1 200 ? -7.750  -6.339  13.280  1.00 11.87 ? 200  PRO B C   1 
ATOM   3316 O  O   . PRO B  1 200 ? -6.987  -5.428  12.912  1.00 11.13 ? 200  PRO B O   1 
ATOM   3317 C  CB  . PRO B  1 200 ? -8.283  -7.841  11.367  1.00 14.58 ? 200  PRO B CB  1 
ATOM   3318 C  CG  . PRO B  1 200 ? -8.994  -7.552  10.077  1.00 18.45 ? 200  PRO B CG  1 
ATOM   3319 C  CD  . PRO B  1 200 ? -9.179  -6.064  10.074  1.00 15.02 ? 200  PRO B CD  1 
ATOM   3320 N  N   . LEU B  1 201 ? -7.652  -6.930  14.464  1.00 9.42  ? 201  LEU B N   1 
ATOM   3321 C  CA  . LEU B  1 201 ? -6.538  -6.666  15.370  1.00 10.29 ? 201  LEU B CA  1 
ATOM   3322 C  C   . LEU B  1 201 ? -5.369  -7.518  14.908  1.00 15.54 ? 201  LEU B C   1 
ATOM   3323 O  O   . LEU B  1 201 ? -5.453  -8.739  14.969  1.00 17.53 ? 201  LEU B O   1 
ATOM   3324 C  CB  . LEU B  1 201 ? -6.934  -7.066  16.790  1.00 11.43 ? 201  LEU B CB  1 
ATOM   3325 C  CG  . LEU B  1 201 ? -5.811  -7.235  17.807  1.00 17.60 ? 201  LEU B CG  1 
ATOM   3326 C  CD1 . LEU B  1 201 ? -5.152  -5.902  18.079  1.00 22.52 ? 201  LEU B CD1 1 
ATOM   3327 C  CD2 . LEU B  1 201 ? -6.352  -7.845  19.089  1.00 17.46 ? 201  LEU B CD2 1 
ATOM   3328 N  N   . VAL B  1 202 ? -4.292  -6.890  14.431  1.00 8.90  ? 202  VAL B N   1 
ATOM   3329 C  CA  . VAL B  1 202 ? -3.163  -7.664  13.891  1.00 11.02 ? 202  VAL B CA  1 
ATOM   3330 C  C   . VAL B  1 202 ? -1.906  -7.635  14.752  1.00 13.36 ? 202  VAL B C   1 
ATOM   3331 O  O   . VAL B  1 202 ? -0.895  -8.270  14.413  1.00 13.87 ? 202  VAL B O   1 
ATOM   3332 C  CB  . VAL B  1 202 ? -2.783  -7.208  12.467  1.00 10.75 ? 202  VAL B CB  1 
ATOM   3333 C  CG1 . VAL B  1 202 ? -3.991  -7.298  11.542  1.00 14.95 ? 202  VAL B CG1 1 
ATOM   3334 C  CG2 . VAL B  1 202 ? -2.185  -5.781  12.482  1.00 13.03 ? 202  VAL B CG2 1 
ATOM   3335 N  N   . TRP B  1 203 ? -1.957  -6.890  15.855  1.00 13.04 ? 203  TRP B N   1 
ATOM   3336 C  CA  . TRP B  1 203 ? -0.757  -6.626  16.631  1.00 13.70 ? 203  TRP B CA  1 
ATOM   3337 C  C   . TRP B  1 203 ? -0.793  -7.304  17.996  1.00 21.09 ? 203  TRP B C   1 
ATOM   3338 O  O   . TRP B  1 203 ? 0.143   -7.180  18.783  1.00 24.97 ? 203  TRP B O   1 
ATOM   3339 C  CB  . TRP B  1 203 ? -0.506  -5.119  16.763  1.00 13.03 ? 203  TRP B CB  1 
ATOM   3340 C  CG  . TRP B  1 203 ? -1.730  -4.265  16.998  1.00 12.14 ? 203  TRP B CG  1 
ATOM   3341 C  CD1 . TRP B  1 203 ? -2.493  -3.651  16.050  1.00 11.50 ? 203  TRP B CD1 1 
ATOM   3342 C  CD2 . TRP B  1 203 ? -2.293  -3.893  18.266  1.00 11.98 ? 203  TRP B CD2 1 
ATOM   3343 N  NE1 . TRP B  1 203 ? -3.507  -2.935  16.643  1.00 9.96  ? 203  TRP B NE1 1 
ATOM   3344 C  CE2 . TRP B  1 203 ? -3.408  -3.068  18.002  1.00 9.18  ? 203  TRP B CE2 1 
ATOM   3345 C  CE3 . TRP B  1 203 ? -1.976  -4.198  19.598  1.00 13.39 ? 203  TRP B CE3 1 
ATOM   3346 C  CZ2 . TRP B  1 203 ? -4.200  -2.528  19.019  1.00 10.14 ? 203  TRP B CZ2 1 
ATOM   3347 C  CZ3 . TRP B  1 203 ? -2.765  -3.661  20.610  1.00 11.46 ? 203  TRP B CZ3 1 
ATOM   3348 C  CH2 . TRP B  1 203 ? -3.865  -2.834  20.314  1.00 11.04 ? 203  TRP B CH2 1 
ATOM   3349 N  N   . VAL B  1 204 ? -1.894  -7.999  18.261  1.00 16.82 ? 204  VAL B N   1 
ATOM   3350 C  CA  . VAL B  1 204 ? -2.022  -8.886  19.413  1.00 40.93 ? 204  VAL B CA  1 
ATOM   3351 C  C   . VAL B  1 204 ? -2.716  -10.172 18.958  1.00 52.15 ? 204  VAL B C   1 
ATOM   3352 O  O   . VAL B  1 204 ? -3.365  -10.194 17.907  1.00 46.07 ? 204  VAL B O   1 
ATOM   3353 C  CB  . VAL B  1 204 ? -2.802  -8.220  20.586  1.00 26.49 ? 204  VAL B CB  1 
ATOM   3354 C  CG1 . VAL B  1 204 ? -3.470  -9.273  21.466  1.00 43.98 ? 204  VAL B CG1 1 
ATOM   3355 C  CG2 . VAL B  1 204 ? -1.868  -7.349  21.408  1.00 43.60 ? 204  VAL B CG2 1 
ATOM   3356 O  OXT . VAL B  1 204 ? -2.633  -11.224 19.598  1.00 64.62 ? 204  VAL B OXT 1 
ATOM   3357 N  N   . HIS C  1 1   ? 10.727  -10.115 -16.704 1.00 23.13 ? 1    HIS C N   1 
ATOM   3358 C  CA  . HIS C  1 1   ? 11.602  -10.549 -17.786 1.00 31.03 ? 1    HIS C CA  1 
ATOM   3359 C  C   . HIS C  1 1   ? 12.992  -10.976 -17.311 1.00 16.32 ? 1    HIS C C   1 
ATOM   3360 O  O   . HIS C  1 1   ? 13.623  -11.787 -17.966 1.00 19.15 ? 1    HIS C O   1 
ATOM   3361 C  CB  . HIS C  1 1   ? 11.622  -9.504  -18.903 1.00 23.17 ? 1    HIS C CB  1 
ATOM   3362 C  CG  . HIS C  1 1   ? 10.264  -8.906  -19.150 1.00 22.34 ? 1    HIS C CG  1 
ATOM   3363 N  ND1 . HIS C  1 1   ? 9.222   -9.064  -18.262 1.00 31.32 ? 1    HIS C ND1 1 
ATOM   3364 C  CD2 . HIS C  1 1   ? 9.782   -8.150  -20.164 1.00 41.15 ? 1    HIS C CD2 1 
ATOM   3365 C  CE1 . HIS C  1 1   ? 8.152   -8.437  -18.719 1.00 25.07 ? 1    HIS C CE1 1 
ATOM   3366 N  NE2 . HIS C  1 1   ? 8.465   -7.874  -19.870 1.00 33.69 ? 1    HIS C NE2 1 
ATOM   3367 N  N   . THR C  1 2   ? 13.446  -10.478 -16.157 1.00 12.26 ? 2    THR C N   1 
ATOM   3368 C  CA  . THR C  1 2   ? 14.629  -11.036 -15.496 1.00 9.67  ? 2    THR C CA  1 
ATOM   3369 C  C   . THR C  1 2   ? 14.273  -11.541 -14.099 1.00 11.82 ? 2    THR C C   1 
ATOM   3370 O  O   . THR C  1 2   ? 13.541  -10.878 -13.371 1.00 12.28 ? 2    THR C O   1 
ATOM   3371 C  CB  . THR C  1 2   ? 15.757  -9.988  -15.367 1.00 16.03 ? 2    THR C CB  1 
ATOM   3372 O  OG1 . THR C  1 2   ? 16.186  -9.600  -16.673 1.00 20.29 ? 2    THR C OG1 1 
ATOM   3373 C  CG2 . THR C  1 2   ? 16.948  -10.562 -14.615 1.00 18.15 ? 2    THR C CG2 1 
ATOM   3374 N  N   . ASP C  1 3   ? 14.781  -12.721 -13.741 1.00 10.26 ? 3    ASP C N   1 
ATOM   3375 C  CA  . ASP C  1 3   ? 14.584  -13.284 -12.407 1.00 9.80  ? 3    ASP C CA  1 
ATOM   3376 C  C   . ASP C  1 3   ? 15.725  -12.838 -11.498 1.00 10.00 ? 3    ASP C C   1 
ATOM   3377 O  O   . ASP C  1 3   ? 16.860  -13.313 -11.632 1.00 11.25 ? 3    ASP C O   1 
ATOM   3378 C  CB  . ASP C  1 3   ? 14.569  -14.813 -12.497 1.00 11.06 ? 3    ASP C CB  1 
ATOM   3379 C  CG  . ASP C  1 3   ? 14.328  -15.493 -11.157 1.00 16.58 ? 3    ASP C CG  1 
ATOM   3380 O  OD1 . ASP C  1 3   ? 14.193  -14.811 -10.116 1.00 10.76 ? 3    ASP C OD1 1 
ATOM   3381 O  OD2 . ASP C  1 3   ? 14.271  -16.742 -11.147 1.00 16.72 ? 3    ASP C OD2 1 
ATOM   3382 N  N   . LEU C  1 4   ? 15.433  -11.925 -10.577 1.00 10.40 ? 4    LEU C N   1 
ATOM   3383 C  CA  . LEU C  1 4   ? 16.457  -11.405 -9.682  1.00 8.71  ? 4    LEU C CA  1 
ATOM   3384 C  C   . LEU C  1 4   ? 16.487  -12.121 -8.328  1.00 11.52 ? 4    LEU C C   1 
ATOM   3385 O  O   . LEU C  1 4   ? 17.092  -11.628 -7.371  1.00 11.12 ? 4    LEU C O   1 
ATOM   3386 C  CB  . LEU C  1 4   ? 16.275  -9.889  -9.496  1.00 8.00  ? 4    LEU C CB  1 
ATOM   3387 C  CG  . LEU C  1 4   ? 16.519  -9.076  -10.772 1.00 11.61 ? 4    LEU C CG  1 
ATOM   3388 C  CD1 . LEU C  1 4   ? 16.287  -7.587  -10.496 1.00 13.06 ? 4    LEU C CD1 1 
ATOM   3389 C  CD2 . LEU C  1 4   ? 17.923  -9.301  -11.296 1.00 12.49 ? 4    LEU C CD2 1 
ATOM   3390 N  N   . SER C  1 5   ? 15.848  -13.291 -8.245  1.00 9.41  ? 5    SER C N   1 
ATOM   3391 C  CA  . SER C  1 5   ? 15.952  -14.118 -7.041  1.00 11.28 ? 5    SER C CA  1 
ATOM   3392 C  C   . SER C  1 5   ? 17.396  -14.176 -6.554  1.00 8.73  ? 5    SER C C   1 
ATOM   3393 O  O   . SER C  1 5   ? 18.305  -14.517 -7.321  1.00 12.10 ? 5    SER C O   1 
ATOM   3394 C  CB  . SER C  1 5   ? 15.508  -15.561 -7.334  1.00 15.06 ? 5    SER C CB  1 
ATOM   3395 O  OG  . SER C  1 5   ? 14.126  -15.651 -7.595  1.00 19.32 ? 5    SER C OG  1 
ATOM   3396 N  N   . GLY C  1 6   ? 17.602  -13.887 -5.268  1.00 11.49 ? 6    GLY C N   1 
ATOM   3397 C  CA  . GLY C  1 6   ? 18.921  -13.998 -4.669  1.00 13.02 ? 6    GLY C CA  1 
ATOM   3398 C  C   . GLY C  1 6   ? 19.874  -12.868 -5.016  1.00 12.22 ? 6    GLY C C   1 
ATOM   3399 O  O   . GLY C  1 6   ? 21.059  -12.930 -4.687  1.00 11.42 ? 6    GLY C O   1 
ATOM   3400 N  N   . LYS C  1 7   ? 19.350  -11.831 -5.665  1.00 9.91  ? 7    LYS C N   1 
ATOM   3401 C  CA  . LYS C  1 7   ? 20.160  -10.694 -6.104  1.00 7.00  ? 7    LYS C CA  1 
ATOM   3402 C  C   . LYS C  1 7   ? 19.556  -9.375  -5.643  1.00 7.58  ? 7    LYS C C   1 
ATOM   3403 O  O   . LYS C  1 7   ? 18.372  -9.297  -5.323  1.00 12.17 ? 7    LYS C O   1 
ATOM   3404 C  CB  . LYS C  1 7   ? 20.281  -10.669 -7.624  1.00 9.35  ? 7    LYS C CB  1 
ATOM   3405 C  CG  . LYS C  1 7   ? 20.907  -11.951 -8.198  1.00 12.58 ? 7    LYS C CG  1 
ATOM   3406 C  CD  . LYS C  1 7   ? 21.028  -11.883 -9.707  1.00 13.71 ? 7    LYS C CD  1 
ATOM   3407 C  CE  . LYS C  1 7   ? 21.678  -13.158 -10.255 1.00 25.02 ? 7    LYS C CE  1 
ATOM   3408 N  NZ  . LYS C  1 7   ? 22.955  -13.489 -9.556  1.00 44.55 ? 7    LYS C NZ  1 
ATOM   3409 N  N   . VAL C  1 8   ? 20.392  -8.345  -5.621  1.00 10.17 ? 8    VAL C N   1 
ATOM   3410 C  CA  . VAL C  1 8   ? 19.958  -7.001  -5.252  1.00 5.91  ? 8    VAL C CA  1 
ATOM   3411 C  C   . VAL C  1 8   ? 20.413  -6.019  -6.303  1.00 7.66  ? 8    VAL C C   1 
ATOM   3412 O  O   . VAL C  1 8   ? 21.345  -6.300  -7.051  1.00 10.01 ? 8    VAL C O   1 
ATOM   3413 C  CB  . VAL C  1 8   ? 20.584  -6.541  -3.914  1.00 8.20  ? 8    VAL C CB  1 
ATOM   3414 C  CG1 . VAL C  1 8   ? 20.001  -7.325  -2.746  1.00 14.99 ? 8    VAL C CG1 1 
ATOM   3415 C  CG2 . VAL C  1 8   ? 22.119  -6.687  -3.966  1.00 9.29  ? 8    VAL C CG2 1 
ATOM   3416 N  N   . PHE C  1 9   ? 19.747  -4.861  -6.360  1.00 6.61  ? 9    PHE C N   1 
ATOM   3417 C  CA  . PHE C  1 9   ? 20.325  -3.700  -7.019  1.00 9.16  ? 9    PHE C CA  1 
ATOM   3418 C  C   . PHE C  1 9   ? 21.212  -2.995  -6.007  1.00 9.55  ? 9    PHE C C   1 
ATOM   3419 O  O   . PHE C  1 9   ? 20.765  -2.716  -4.895  1.00 8.81  ? 9    PHE C O   1 
ATOM   3420 C  CB  . PHE C  1 9   ? 19.244  -2.713  -7.455  1.00 8.43  ? 9    PHE C CB  1 
ATOM   3421 C  CG  . PHE C  1 9   ? 18.432  -3.168  -8.627  1.00 7.24  ? 9    PHE C CG  1 
ATOM   3422 C  CD1 . PHE C  1 9   ? 19.046  -3.528  -9.816  1.00 11.14 ? 9    PHE C CD1 1 
ATOM   3423 C  CD2 . PHE C  1 9   ? 17.047  -3.187  -8.549  1.00 9.00  ? 9    PHE C CD2 1 
ATOM   3424 C  CE1 . PHE C  1 9   ? 18.280  -3.937  -10.911 1.00 13.10 ? 9    PHE C CE1 1 
ATOM   3425 C  CE2 . PHE C  1 9   ? 16.276  -3.590  -9.632  1.00 10.89 ? 9    PHE C CE2 1 
ATOM   3426 C  CZ  . PHE C  1 9   ? 16.895  -3.958  -10.814 1.00 11.84 ? 9    PHE C CZ  1 
ATOM   3427 N  N   . VAL C  1 10  ? 22.466  -2.738  -6.373  1.00 8.48  ? 10   VAL C N   1 
ATOM   3428 C  CA  . VAL C  1 10  ? 23.348  -1.908  -5.546  1.00 8.05  ? 10   VAL C CA  1 
ATOM   3429 C  C   . VAL C  1 10  ? 23.446  -0.521  -6.161  1.00 7.93  ? 10   VAL C C   1 
ATOM   3430 O  O   . VAL C  1 10  ? 23.854  -0.368  -7.307  1.00 9.13  ? 10   VAL C O   1 
ATOM   3431 C  CB  . VAL C  1 10  ? 24.768  -2.486  -5.410  1.00 8.21  ? 10   VAL C CB  1 
ATOM   3432 C  CG1 . VAL C  1 10  ? 25.600  -1.632  -4.426  1.00 10.77 ? 10   VAL C CG1 1 
ATOM   3433 C  CG2 . VAL C  1 10  ? 24.719  -3.959  -4.976  1.00 9.60  ? 10   VAL C CG2 1 
ATOM   3434 N  N   . PHE C  1 11  ? 23.026  0.482   -5.394  1.00 7.92  ? 11   PHE C N   1 
ATOM   3435 C  CA  . PHE C  1 11  ? 23.237  1.883   -5.741  1.00 8.43  ? 11   PHE C CA  1 
ATOM   3436 C  C   . PHE C  1 11  ? 24.462  2.335   -4.953  1.00 11.49 ? 11   PHE C C   1 
ATOM   3437 O  O   . PHE C  1 11  ? 24.353  2.702   -3.776  1.00 9.87  ? 11   PHE C O   1 
ATOM   3438 C  CB  . PHE C  1 11  ? 21.977  2.690   -5.372  1.00 6.93  ? 11   PHE C CB  1 
ATOM   3439 C  CG  . PHE C  1 11  ? 20.730  2.188   -6.050  1.00 8.27  ? 11   PHE C CG  1 
ATOM   3440 C  CD1 . PHE C  1 11  ? 19.991  1.153   -5.487  1.00 8.31  ? 11   PHE C CD1 1 
ATOM   3441 C  CD2 . PHE C  1 11  ? 20.309  2.730   -7.259  1.00 11.19 ? 11   PHE C CD2 1 
ATOM   3442 C  CE1 . PHE C  1 11  ? 18.841  0.662   -6.118  1.00 8.47  ? 11   PHE C CE1 1 
ATOM   3443 C  CE2 . PHE C  1 11  ? 19.160  2.251   -7.892  1.00 9.30  ? 11   PHE C CE2 1 
ATOM   3444 C  CZ  . PHE C  1 11  ? 18.425  1.214   -7.315  1.00 8.90  ? 11   PHE C CZ  1 
ATOM   3445 N  N   . PRO C  1 12  ? 25.651  2.283   -5.588  1.00 9.22  ? 12   PRO C N   1 
ATOM   3446 C  CA  . PRO C  1 12  ? 26.875  2.281   -4.778  1.00 9.70  ? 12   PRO C CA  1 
ATOM   3447 C  C   . PRO C  1 12  ? 27.384  3.656   -4.367  1.00 8.22  ? 12   PRO C C   1 
ATOM   3448 O  O   . PRO C  1 12  ? 28.373  3.728   -3.627  1.00 9.16  ? 12   PRO C O   1 
ATOM   3449 C  CB  . PRO C  1 12  ? 27.912  1.585   -5.691  1.00 11.86 ? 12   PRO C CB  1 
ATOM   3450 C  CG  . PRO C  1 12  ? 27.117  1.059   -6.898  1.00 9.28  ? 12   PRO C CG  1 
ATOM   3451 C  CD  . PRO C  1 12  ? 25.938  1.991   -7.004  1.00 9.17  ? 12   PRO C CD  1 
ATOM   3452 N  N   . ARG C  1 13  ? 26.735  4.724   -4.829  1.00 9.42  ? 13   ARG C N   1 
ATOM   3453 C  CA  . ARG C  1 13  ? 27.195  6.067   -4.505  1.00 11.85 ? 13   ARG C CA  1 
ATOM   3454 C  C   . ARG C  1 13  ? 26.034  7.051   -4.511  1.00 15.18 ? 13   ARG C C   1 
ATOM   3455 O  O   . ARG C  1 13  ? 24.978  6.796   -5.097  1.00 12.81 ? 13   ARG C O   1 
ATOM   3456 C  CB  . ARG C  1 13  ? 28.233  6.523   -5.531  1.00 12.73 ? 13   ARG C CB  1 
ATOM   3457 C  CG  . ARG C  1 13  ? 27.572  6.730   -6.875  1.00 11.22 ? 13   ARG C CG  1 
ATOM   3458 C  CD  . ARG C  1 13  ? 28.501  7.184   -7.973  1.00 15.38 ? 13   ARG C CD  1 
ATOM   3459 N  NE  . ARG C  1 13  ? 27.727  7.293   -9.205  1.00 13.23 ? 13   ARG C NE  1 
ATOM   3460 C  CZ  . ARG C  1 13  ? 28.199  7.771   -10.344 1.00 14.59 ? 13   ARG C CZ  1 
ATOM   3461 N  NH1 . ARG C  1 13  ? 29.457  8.198   -10.411 1.00 21.45 ? 13   ARG C NH1 1 
ATOM   3462 N  NH2 . ARG C  1 13  ? 27.418  7.823   -11.411 1.00 17.90 ? 13   ARG C NH2 1 
ATOM   3463 N  N   . GLU C  1 14  ? 26.239  8.184   -3.855  1.00 11.61 ? 14   GLU C N   1 
ATOM   3464 C  CA  . GLU C  1 14  ? 25.293  9.287   -3.935  1.00 12.06 ? 14   GLU C CA  1 
ATOM   3465 C  C   . GLU C  1 14  ? 25.407  9.953   -5.308  1.00 14.66 ? 14   GLU C C   1 
ATOM   3466 O  O   . GLU C  1 14  ? 26.510  10.136  -5.838  1.00 14.05 ? 14   GLU C O   1 
ATOM   3467 C  CB  . GLU C  1 14  ? 25.566  10.291  -2.812  1.00 12.34 ? 14   GLU C CB  1 
ATOM   3468 C  CG  . GLU C  1 14  ? 24.637  11.487  -2.806  1.00 15.58 ? 14   GLU C CG  1 
ATOM   3469 C  CD  . GLU C  1 14  ? 24.824  12.356  -1.578  1.00 24.68 ? 14   GLU C CD  1 
ATOM   3470 O  OE1 . GLU C  1 14  ? 24.412  11.933  -0.482  1.00 18.80 ? 14   GLU C OE1 1 
ATOM   3471 O  OE2 . GLU C  1 14  ? 25.384  13.463  -1.715  1.00 23.12 ? 14   GLU C OE2 1 
ATOM   3472 N  N   . SER C  1 15  ? 24.266  10.285  -5.900  1.00 10.35 ? 15   SER C N   1 
ATOM   3473 C  CA  . SER C  1 15  ? 24.260  10.888  -7.227  1.00 13.21 ? 15   SER C CA  1 
ATOM   3474 C  C   . SER C  1 15  ? 22.899  11.466  -7.533  1.00 11.67 ? 15   SER C C   1 
ATOM   3475 O  O   . SER C  1 15  ? 21.951  11.292  -6.774  1.00 11.35 ? 15   SER C O   1 
ATOM   3476 C  CB  . SER C  1 15  ? 24.561  9.838   -8.294  1.00 13.03 ? 15   SER C CB  1 
ATOM   3477 O  OG  . SER C  1 15  ? 23.378  9.107   -8.598  1.00 12.17 ? 15   SER C OG  1 
ATOM   3478 N  N   . VAL C  1 16  ? 22.803  12.153  -8.664  1.00 13.30 ? 16   VAL C N   1 
ATOM   3479 C  CA  . VAL C  1 16  ? 21.502  12.548  -9.170  1.00 13.44 ? 16   VAL C CA  1 
ATOM   3480 C  C   . VAL C  1 16  ? 21.208  11.761  -10.449 1.00 15.40 ? 16   VAL C C   1 
ATOM   3481 O  O   . VAL C  1 16  ? 20.185  11.961  -11.101 1.00 19.27 ? 16   VAL C O   1 
ATOM   3482 C  CB  . VAL C  1 16  ? 21.442  14.070  -9.416  1.00 17.60 ? 16   VAL C CB  1 
ATOM   3483 C  CG1 . VAL C  1 16  ? 22.301  14.442  -10.612 1.00 17.38 ? 16   VAL C CG1 1 
ATOM   3484 C  CG2 . VAL C  1 16  ? 20.006  14.528  -9.593  1.00 21.23 ? 16   VAL C CG2 1 
ATOM   3485 N  N   . THR C  1 17  ? 22.108  10.843  -10.789 1.00 11.98 ? 17   THR C N   1 
ATOM   3486 C  CA  . THR C  1 17  ? 22.044  10.133  -12.064 1.00 13.53 ? 17   THR C CA  1 
ATOM   3487 C  C   . THR C  1 17  ? 21.603  8.675   -11.952 1.00 14.90 ? 17   THR C C   1 
ATOM   3488 O  O   . THR C  1 17  ? 20.974  8.139   -12.865 1.00 14.97 ? 17   THR C O   1 
ATOM   3489 C  CB  . THR C  1 17  ? 23.421  10.123  -12.755 1.00 17.82 ? 17   THR C CB  1 
ATOM   3490 O  OG1 . THR C  1 17  ? 24.417  9.641   -11.837 1.00 16.99 ? 17   THR C OG1 1 
ATOM   3491 C  CG2 . THR C  1 17  ? 23.792  11.516  -13.219 1.00 25.87 ? 17   THR C CG2 1 
ATOM   3492 N  N   . ASP C  1 18  ? 21.971  8.027   -10.855 1.00 11.82 ? 18   ASP C N   1 
ATOM   3493 C  CA  . ASP C  1 18  ? 21.870  6.569   -10.784 1.00 11.37 ? 18   ASP C CA  1 
ATOM   3494 C  C   . ASP C  1 18  ? 20.461  6.141   -10.390 1.00 9.96  ? 18   ASP C C   1 
ATOM   3495 O  O   . ASP C  1 18  ? 19.968  6.516   -9.327  1.00 12.03 ? 18   ASP C O   1 
ATOM   3496 C  CB  . ASP C  1 18  ? 22.886  6.028   -9.775  1.00 10.48 ? 18   ASP C CB  1 
ATOM   3497 C  CG  . ASP C  1 18  ? 24.309  6.526   -10.046 1.00 11.08 ? 18   ASP C CG  1 
ATOM   3498 O  OD1 . ASP C  1 18  ? 24.628  6.882   -11.209 1.00 11.25 ? 18   ASP C OD1 1 
ATOM   3499 O  OD2 . ASP C  1 18  ? 25.117  6.542   -9.094  1.00 14.51 ? 18   ASP C OD2 1 
ATOM   3500 N  N   . HIS C  1 19  ? 19.814  5.348   -11.241 1.00 9.87  ? 19   HIS C N   1 
ATOM   3501 C  CA  . HIS C  1 19  ? 18.460  4.884   -10.945 1.00 9.09  ? 19   HIS C CA  1 
ATOM   3502 C  C   . HIS C  1 19  ? 18.046  3.645   -11.730 1.00 9.09  ? 19   HIS C C   1 
ATOM   3503 O  O   . HIS C  1 19  ? 18.669  3.286   -12.717 1.00 11.35 ? 19   HIS C O   1 
ATOM   3504 C  CB  . HIS C  1 19  ? 17.425  5.999   -11.149 1.00 8.83  ? 19   HIS C CB  1 
ATOM   3505 C  CG  . HIS C  1 19  ? 17.296  6.470   -12.567 1.00 12.10 ? 19   HIS C CG  1 
ATOM   3506 N  ND1 . HIS C  1 19  ? 18.252  7.252   -13.181 1.00 14.30 ? 19   HIS C ND1 1 
ATOM   3507 C  CD2 . HIS C  1 19  ? 16.295  6.318   -13.466 1.00 12.07 ? 19   HIS C CD2 1 
ATOM   3508 C  CE1 . HIS C  1 19  ? 17.852  7.541   -14.410 1.00 16.64 ? 19   HIS C CE1 1 
ATOM   3509 N  NE2 . HIS C  1 19  ? 16.668  6.991   -14.605 1.00 12.72 ? 19   HIS C NE2 1 
ATOM   3510 N  N   . VAL C  1 20  ? 16.983  2.995   -11.275 1.00 8.81  ? 20   VAL C N   1 
ATOM   3511 C  CA  . VAL C  1 20  ? 16.387  1.905   -12.037 1.00 9.11  ? 20   VAL C CA  1 
ATOM   3512 C  C   . VAL C  1 20  ? 14.935  2.249   -12.327 1.00 11.08 ? 20   VAL C C   1 
ATOM   3513 O  O   . VAL C  1 20  ? 14.194  2.637   -11.428 1.00 10.90 ? 20   VAL C O   1 
ATOM   3514 C  CB  . VAL C  1 20  ? 16.423  0.573   -11.266 1.00 10.53 ? 20   VAL C CB  1 
ATOM   3515 C  CG1 . VAL C  1 20  ? 15.757  -0.539  -12.097 1.00 9.40  ? 20   VAL C CG1 1 
ATOM   3516 C  CG2 . VAL C  1 20  ? 17.861  0.194   -10.911 1.00 9.93  ? 20   VAL C CG2 1 
ATOM   3517 N  N   . ASN C  1 21  ? 14.527  2.134   -13.588 1.00 7.89  ? 21   ASN C N   1 
ATOM   3518 C  CA  . ASN C  1 21  ? 13.118  2.268   -13.927 1.00 8.27  ? 21   ASN C CA  1 
ATOM   3519 C  C   . ASN C  1 21  ? 12.466  0.912   -13.880 1.00 8.40  ? 21   ASN C C   1 
ATOM   3520 O  O   . ASN C  1 21  ? 12.981  -0.030  -14.473 1.00 11.88 ? 21   ASN C O   1 
ATOM   3521 C  CB  . ASN C  1 21  ? 12.953  2.818   -15.353 1.00 12.62 ? 21   ASN C CB  1 
ATOM   3522 C  CG  . ASN C  1 21  ? 13.551  4.185   -15.513 1.00 14.60 ? 21   ASN C CG  1 
ATOM   3523 O  OD1 . ASN C  1 21  ? 13.396  5.037   -14.647 1.00 14.65 ? 21   ASN C OD1 1 
ATOM   3524 N  ND2 . ASN C  1 21  ? 14.240  4.409   -16.630 1.00 15.61 ? 21   ASN C ND2 1 
ATOM   3525 N  N   . LEU C  1 22  ? 11.346  0.812   -13.169 1.00 9.07  ? 22   LEU C N   1 
ATOM   3526 C  CA  . LEU C  1 22  ? 10.575  -0.426  -13.133 1.00 10.00 ? 22   LEU C CA  1 
ATOM   3527 C  C   . LEU C  1 22  ? 9.361   -0.300  -14.032 1.00 15.48 ? 22   LEU C C   1 
ATOM   3528 O  O   . LEU C  1 22  ? 8.598   0.670   -13.944 1.00 11.97 ? 22   LEU C O   1 
ATOM   3529 C  CB  . LEU C  1 22  ? 10.151  -0.775  -11.710 1.00 8.28  ? 22   LEU C CB  1 
ATOM   3530 C  CG  . LEU C  1 22  ? 11.253  -0.877  -10.655 1.00 10.23 ? 22   LEU C CG  1 
ATOM   3531 C  CD1 . LEU C  1 22  ? 10.631  -1.215  -9.304  1.00 11.35 ? 22   LEU C CD1 1 
ATOM   3532 C  CD2 . LEU C  1 22  ? 12.306  -1.922  -11.065 1.00 10.63 ? 22   LEU C CD2 1 
ATOM   3533 N  N   . ILE C  1 23  ? 9.185   -1.295  -14.895 1.00 13.55 ? 23   ILE C N   1 
ATOM   3534 C  CA  . ILE C  1 23  ? 8.159   -1.246  -15.926 1.00 12.97 ? 23   ILE C CA  1 
ATOM   3535 C  C   . ILE C  1 23  ? 7.023   -2.217  -15.645 1.00 16.53 ? 23   ILE C C   1 
ATOM   3536 O  O   . ILE C  1 23  ? 7.232   -3.415  -15.479 1.00 17.24 ? 23   ILE C O   1 
ATOM   3537 C  CB  . ILE C  1 23  ? 8.754   -1.539  -17.309 1.00 16.01 ? 23   ILE C CB  1 
ATOM   3538 C  CG1 . ILE C  1 23  ? 9.910   -0.577  -17.582 1.00 20.97 ? 23   ILE C CG1 1 
ATOM   3539 C  CG2 . ILE C  1 23  ? 7.673   -1.438  -18.381 1.00 20.65 ? 23   ILE C CG2 1 
ATOM   3540 C  CD1 . ILE C  1 23  ? 10.760  -0.962  -18.767 1.00 30.69 ? 23   ILE C CD1 1 
ATOM   3541 N  N   . THR C  1 24  ? 5.815   -1.677  -15.578 1.00 17.15 ? 24   THR C N   1 
ATOM   3542 C  CA  . THR C  1 24  ? 4.629   -2.491  -15.366 1.00 21.20 ? 24   THR C CA  1 
ATOM   3543 C  C   . THR C  1 24  ? 3.557   -1.935  -16.288 1.00 23.29 ? 24   THR C C   1 
ATOM   3544 O  O   . THR C  1 24  ? 3.467   -0.719  -16.477 1.00 27.57 ? 24   THR C O   1 
ATOM   3545 C  CB  . THR C  1 24  ? 4.165   -2.425  -13.903 1.00 20.70 ? 24   THR C CB  1 
ATOM   3546 O  OG1 . THR C  1 24  ? 3.131   -3.392  -13.672 1.00 27.25 ? 24   THR C OG1 1 
ATOM   3547 C  CG2 . THR C  1 24  ? 3.641   -1.036  -13.574 1.00 23.30 ? 24   THR C CG2 1 
ATOM   3548 N  N   . PRO C  1 25  ? 2.765   -2.822  -16.893 1.00 25.63 ? 25   PRO C N   1 
ATOM   3549 C  CA  . PRO C  1 25  ? 1.691   -2.426  -17.807 1.00 33.82 ? 25   PRO C CA  1 
ATOM   3550 C  C   . PRO C  1 25  ? 0.439   -2.090  -17.013 1.00 41.79 ? 25   PRO C C   1 
ATOM   3551 O  O   . PRO C  1 25  ? -0.579  -2.769  -17.148 1.00 47.69 ? 25   PRO C O   1 
ATOM   3552 C  CB  . PRO C  1 25  ? 1.459   -3.695  -18.622 1.00 36.81 ? 25   PRO C CB  1 
ATOM   3553 C  CG  . PRO C  1 25  ? 1.805   -4.809  -17.675 1.00 34.04 ? 25   PRO C CG  1 
ATOM   3554 C  CD  . PRO C  1 25  ? 2.815   -4.281  -16.689 1.00 26.94 ? 25   PRO C CD  1 
ATOM   3555 N  N   . LEU C  1 26  ? 0.525   -1.056  -16.182 1.00 26.55 ? 26   LEU C N   1 
ATOM   3556 C  CA  . LEU C  1 26  ? -0.576  -0.696  -15.310 1.00 23.26 ? 26   LEU C CA  1 
ATOM   3557 C  C   . LEU C  1 26  ? -1.461  0.357   -15.964 1.00 38.51 ? 26   LEU C C   1 
ATOM   3558 O  O   . LEU C  1 26  ? -1.154  1.550   -15.929 1.00 29.61 ? 26   LEU C O   1 
ATOM   3559 C  CB  . LEU C  1 26  ? -0.053  -0.180  -13.964 1.00 24.45 ? 26   LEU C CB  1 
ATOM   3560 C  CG  . LEU C  1 26  ? -1.166  0.018   -12.932 1.00 32.20 ? 26   LEU C CG  1 
ATOM   3561 C  CD1 . LEU C  1 26  ? -1.481  -1.293  -12.217 1.00 34.56 ? 26   LEU C CD1 1 
ATOM   3562 C  CD2 . LEU C  1 26  ? -0.809  1.107   -11.932 1.00 33.86 ? 26   LEU C CD2 1 
ATOM   3563 N  N   . GLU C  1 27  ? -2.566  -0.100  -16.545 1.00 27.69 ? 27   GLU C N   1 
ATOM   3564 C  CA  . GLU C  1 27  ? -3.460  0.753   -17.321 1.00 31.72 ? 27   GLU C CA  1 
ATOM   3565 C  C   . GLU C  1 27  ? -4.656  1.264   -16.529 1.00 26.88 ? 27   GLU C C   1 
ATOM   3566 O  O   . GLU C  1 27  ? -5.267  2.268   -16.893 1.00 31.59 ? 27   GLU C O   1 
ATOM   3567 C  CB  . GLU C  1 27  ? -3.946  -0.003  -18.560 1.00 38.12 ? 27   GLU C CB  1 
ATOM   3568 C  CG  . GLU C  1 27  ? -3.665  -1.511  -18.535 1.00 53.52 ? 27   GLU C CG  1 
ATOM   3569 C  CD  . GLU C  1 27  ? -4.426  -2.270  -17.445 1.00 70.53 ? 27   GLU C CD  1 
ATOM   3570 O  OE1 . GLU C  1 27  ? -4.206  -2.001  -16.242 1.00 59.12 ? 27   GLU C OE1 1 
ATOM   3571 O  OE2 . GLU C  1 27  ? -5.230  -3.161  -17.797 1.00 78.58 ? 27   GLU C OE2 1 
ATOM   3572 N  N   . LYS C  1 28  ? -4.998  0.572   -15.449 1.00 21.74 ? 28   LYS C N   1 
ATOM   3573 C  CA  . LYS C  1 28  ? -6.162  0.956   -14.670 1.00 23.04 ? 28   LYS C CA  1 
ATOM   3574 C  C   . LYS C  1 28  ? -5.730  1.541   -13.338 1.00 20.08 ? 28   LYS C C   1 
ATOM   3575 O  O   . LYS C  1 28  ? -4.795  1.044   -12.716 1.00 20.70 ? 28   LYS C O   1 
ATOM   3576 C  CB  . LYS C  1 28  ? -7.076  -0.246  -14.433 1.00 26.38 ? 28   LYS C CB  1 
ATOM   3577 C  CG  . LYS C  1 28  ? -7.529  -0.932  -15.710 1.00 42.44 ? 28   LYS C CG  1 
ATOM   3578 C  CD  . LYS C  1 28  ? -8.509  -2.056  -15.418 1.00 49.12 ? 28   LYS C CD  1 
ATOM   3579 C  CE  . LYS C  1 28  ? -8.889  -2.797  -16.694 1.00 60.08 ? 28   LYS C CE  1 
ATOM   3580 N  NZ  . LYS C  1 28  ? -9.369  -1.867  -17.755 1.00 68.77 ? 28   LYS C NZ  1 
ATOM   3581 N  N   . PRO C  1 29  ? -6.415  2.605   -12.903 1.00 21.73 ? 29   PRO C N   1 
ATOM   3582 C  CA  . PRO C  1 29  ? -6.115  3.217   -11.610 1.00 16.40 ? 29   PRO C CA  1 
ATOM   3583 C  C   . PRO C  1 29  ? -6.197  2.178   -10.499 1.00 14.85 ? 29   PRO C C   1 
ATOM   3584 O  O   . PRO C  1 29  ? -7.039  1.274   -10.551 1.00 18.17 ? 29   PRO C O   1 
ATOM   3585 C  CB  . PRO C  1 29  ? -7.232  4.246   -11.448 1.00 14.98 ? 29   PRO C CB  1 
ATOM   3586 C  CG  . PRO C  1 29  ? -7.576  4.628   -12.851 1.00 23.67 ? 29   PRO C CG  1 
ATOM   3587 C  CD  . PRO C  1 29  ? -7.442  3.353   -13.644 1.00 23.36 ? 29   PRO C CD  1 
ATOM   3588 N  N   . LEU C  1 30  ? -5.324  2.327   -9.509  1.00 12.68 ? 30   LEU C N   1 
ATOM   3589 C  CA  . LEU C  1 30  ? -5.207  1.393   -8.401  1.00 13.71 ? 30   LEU C CA  1 
ATOM   3590 C  C   . LEU C  1 30  ? -6.087  1.790   -7.238  1.00 14.38 ? 30   LEU C C   1 
ATOM   3591 O  O   . LEU C  1 30  ? -5.975  2.903   -6.719  1.00 15.23 ? 30   LEU C O   1 
ATOM   3592 C  CB  . LEU C  1 30  ? -3.772  1.383   -7.879  1.00 18.33 ? 30   LEU C CB  1 
ATOM   3593 C  CG  . LEU C  1 30  ? -2.700  0.560   -8.564  1.00 24.91 ? 30   LEU C CG  1 
ATOM   3594 C  CD1 . LEU C  1 30  ? -1.379  0.820   -7.857  1.00 18.94 ? 30   LEU C CD1 1 
ATOM   3595 C  CD2 . LEU C  1 30  ? -3.087  -0.907  -8.486  1.00 21.90 ? 30   LEU C CD2 1 
ATOM   3596 N  N   A GLN C  1 31  ? -6.957  0.874   -6.820  0.51 12.70 ? 31   GLN C N   1 
ATOM   3597 N  N   B GLN C  1 31  ? -6.946  0.869   -6.820  0.49 12.71 ? 31   GLN C N   1 
ATOM   3598 C  CA  A GLN C  1 31  ? -7.809  1.091   -5.656  0.51 15.02 ? 31   GLN C CA  1 
ATOM   3599 C  CA  B GLN C  1 31  ? -7.803  1.079   -5.666  0.49 15.03 ? 31   GLN C CA  1 
ATOM   3600 C  C   A GLN C  1 31  ? -7.196  0.463   -4.403  0.51 13.25 ? 31   GLN C C   1 
ATOM   3601 C  C   B GLN C  1 31  ? -7.126  0.509   -4.421  0.49 13.22 ? 31   GLN C C   1 
ATOM   3602 O  O   A GLN C  1 31  ? -7.396  0.960   -3.299  0.51 13.61 ? 31   GLN C O   1 
ATOM   3603 O  O   B GLN C  1 31  ? -7.190  1.099   -3.345  0.49 13.89 ? 31   GLN C O   1 
ATOM   3604 C  CB  A GLN C  1 31  ? -9.207  0.510   -5.883  0.51 17.52 ? 31   GLN C CB  1 
ATOM   3605 C  CB  B GLN C  1 31  ? -9.154  0.401   -5.893  0.49 17.43 ? 31   GLN C CB  1 
ATOM   3606 C  CG  A GLN C  1 31  ? -10.177 0.788   -4.742  0.51 20.66 ? 31   GLN C CG  1 
ATOM   3607 C  CG  B GLN C  1 31  ? -9.695  0.619   -7.302  0.49 23.46 ? 31   GLN C CG  1 
ATOM   3608 C  CD  A GLN C  1 31  ? -11.548 0.166   -4.952  0.51 25.08 ? 31   GLN C CD  1 
ATOM   3609 C  CD  B GLN C  1 31  ? -11.056 -0.014  -7.532  0.49 30.62 ? 31   GLN C CD  1 
ATOM   3610 O  OE1 A GLN C  1 31  ? -11.853 -0.355  -6.027  0.51 32.49 ? 31   GLN C OE1 1 
ATOM   3611 O  OE1 B GLN C  1 31  ? -11.640 -0.619  -6.631  0.49 28.71 ? 31   GLN C OE1 1 
ATOM   3612 N  NE2 A GLN C  1 31  ? -12.382 0.217   -3.921  0.51 16.55 ? 31   GLN C NE2 1 
ATOM   3613 N  NE2 B GLN C  1 31  ? -11.569 0.124   -8.749  0.49 23.91 ? 31   GLN C NE2 1 
ATOM   3614 N  N   . ASN C  1 32  ? -6.470  -0.637  -4.587  1.00 10.40 ? 32   ASN C N   1 
ATOM   3615 C  CA  . ASN C  1 32  ? -5.800  -1.337  -3.484  1.00 11.65 ? 32   ASN C CA  1 
ATOM   3616 C  C   . ASN C  1 32  ? -4.399  -1.780  -3.916  1.00 12.84 ? 32   ASN C C   1 
ATOM   3617 O  O   . ASN C  1 32  ? -4.198  -2.171  -5.067  1.00 12.56 ? 32   ASN C O   1 
ATOM   3618 C  CB  . ASN C  1 32  ? -6.532  -2.635  -3.105  1.00 13.18 ? 32   ASN C CB  1 
ATOM   3619 C  CG  . ASN C  1 32  ? -8.036  -2.474  -2.931  1.00 15.53 ? 32   ASN C CG  1 
ATOM   3620 O  OD1 . ASN C  1 32  ? -8.512  -1.629  -2.168  1.00 14.89 ? 32   ASN C OD1 1 
ATOM   3621 N  ND2 . ASN C  1 32  ? -8.784  -3.354  -3.614  1.00 16.85 ? 32   ASN C ND2 1 
ATOM   3622 N  N   . PHE C  1 33  ? -3.433  -1.765  -3.003  1.00 8.47  ? 33   PHE C N   1 
ATOM   3623 C  CA  . PHE C  1 33  ? -2.127  -2.351  -3.320  1.00 8.48  ? 33   PHE C CA  1 
ATOM   3624 C  C   . PHE C  1 33  ? -1.355  -2.724  -2.071  1.00 9.35  ? 33   PHE C C   1 
ATOM   3625 O  O   . PHE C  1 33  ? -1.627  -2.223  -0.976  1.00 9.45  ? 33   PHE C O   1 
ATOM   3626 C  CB  . PHE C  1 33  ? -1.273  -1.404  -4.180  1.00 6.86  ? 33   PHE C CB  1 
ATOM   3627 C  CG  . PHE C  1 33  ? -0.720  -0.232  -3.416  1.00 9.19  ? 33   PHE C CG  1 
ATOM   3628 C  CD1 . PHE C  1 33  ? 0.477   -0.340  -2.726  1.00 8.82  ? 33   PHE C CD1 1 
ATOM   3629 C  CD2 . PHE C  1 33  ? -1.407  0.973   -3.387  1.00 9.44  ? 33   PHE C CD2 1 
ATOM   3630 C  CE1 . PHE C  1 33  ? 0.980   0.742   -1.998  1.00 8.75  ? 33   PHE C CE1 1 
ATOM   3631 C  CE2 . PHE C  1 33  ? -0.906  2.062   -2.673  1.00 9.97  ? 33   PHE C CE2 1 
ATOM   3632 C  CZ  . PHE C  1 33  ? 0.282   1.946   -1.984  1.00 9.86  ? 33   PHE C CZ  1 
ATOM   3633 N  N   . THR C  1 34  ? -0.399  -3.630  -2.251  1.00 8.26  ? 34   THR C N   1 
ATOM   3634 C  CA  . THR C  1 34  ? 0.624   -3.874  -1.248  1.00 8.51  ? 34   THR C CA  1 
ATOM   3635 C  C   . THR C  1 34  ? 1.964   -3.880  -1.966  1.00 9.58  ? 34   THR C C   1 
ATOM   3636 O  O   . THR C  1 34  ? 2.086   -4.433  -3.052  1.00 9.30  ? 34   THR C O   1 
ATOM   3637 C  CB  . THR C  1 34  ? 0.455   -5.246  -0.580  1.00 8.12  ? 34   THR C CB  1 
ATOM   3638 O  OG1 . THR C  1 34  ? -0.861  -5.348  -0.034  1.00 9.02  ? 34   THR C OG1 1 
ATOM   3639 C  CG2 . THR C  1 34  ? 1.478   -5.403  0.546   1.00 8.85  ? 34   THR C CG2 1 
ATOM   3640 N  N   . LEU C  1 35  ? 2.968   -3.254  -1.360  1.00 7.44  ? 35   LEU C N   1 
ATOM   3641 C  CA  . LEU C  1 35  ? 4.327   -3.269  -1.892  1.00 10.17 ? 35   LEU C CA  1 
ATOM   3642 C  C   . LEU C  1 35  ? 5.280   -3.771  -0.804  1.00 9.01  ? 35   LEU C C   1 
ATOM   3643 O  O   . LEU C  1 35  ? 5.251   -3.265  0.312   1.00 8.82  ? 35   LEU C O   1 
ATOM   3644 C  CB  . LEU C  1 35  ? 4.704   -1.845  -2.300  1.00 8.23  ? 35   LEU C CB  1 
ATOM   3645 C  CG  . LEU C  1 35  ? 6.177   -1.571  -2.591  1.00 10.34 ? 35   LEU C CG  1 
ATOM   3646 C  CD1 . LEU C  1 35  ? 6.615   -2.230  -3.893  1.00 13.36 ? 35   LEU C CD1 1 
ATOM   3647 C  CD2 . LEU C  1 35  ? 6.396   -0.067  -2.647  1.00 12.13 ? 35   LEU C CD2 1 
ATOM   3648 N  N   . CYS C  1 36  ? 6.104   -4.775  -1.118  1.00 8.56  ? 36   CYS C N   1 
ATOM   3649 C  CA  . CYS C  1 36  ? 7.088   -5.306  -0.167  1.00 9.25  ? 36   CYS C CA  1 
ATOM   3650 C  C   . CYS C  1 36  ? 8.453   -5.281  -0.828  1.00 8.88  ? 36   CYS C C   1 
ATOM   3651 O  O   . CYS C  1 36  ? 8.565   -5.504  -2.028  1.00 9.19  ? 36   CYS C O   1 
ATOM   3652 C  CB  . CYS C  1 36  ? 6.778   -6.758  0.218   1.00 11.05 ? 36   CYS C CB  1 
ATOM   3653 S  SG  . CYS C  1 36  ? 5.253   -7.024  1.159   1.00 14.48 ? 36   CYS C SG  1 
ATOM   3654 N  N   . PHE C  1 37  ? 9.490   -4.988  -0.052  1.00 7.84  ? 37   PHE C N   1 
ATOM   3655 C  CA  . PHE C  1 37  ? 10.863  -5.084  -0.552  1.00 8.63  ? 37   PHE C CA  1 
ATOM   3656 C  C   . PHE C  1 37  ? 11.830  -5.098  0.630   1.00 9.56  ? 37   PHE C C   1 
ATOM   3657 O  O   . PHE C  1 37  ? 11.421  -4.824  1.764   1.00 9.07  ? 37   PHE C O   1 
ATOM   3658 C  CB  . PHE C  1 37  ? 11.183  -3.922  -1.511  1.00 8.65  ? 37   PHE C CB  1 
ATOM   3659 C  CG  . PHE C  1 37  ? 10.966  -2.562  -0.905  1.00 9.80  ? 37   PHE C CG  1 
ATOM   3660 C  CD1 . PHE C  1 37  ? 9.727   -1.943  -0.998  1.00 10.60 ? 37   PHE C CD1 1 
ATOM   3661 C  CD2 . PHE C  1 37  ? 11.993  -1.917  -0.219  1.00 11.43 ? 37   PHE C CD2 1 
ATOM   3662 C  CE1 . PHE C  1 37  ? 9.511   -0.695  -0.416  1.00 15.52 ? 37   PHE C CE1 1 
ATOM   3663 C  CE2 . PHE C  1 37  ? 11.782  -0.674  0.358   1.00 11.78 ? 37   PHE C CE2 1 
ATOM   3664 C  CZ  . PHE C  1 37  ? 10.551  -0.065  0.259   1.00 11.88 ? 37   PHE C CZ  1 
ATOM   3665 N  N   . ARG C  1 38  ? 13.091  -5.462  0.373   1.00 7.27  ? 38   ARG C N   1 
ATOM   3666 C  CA  . ARG C  1 38  ? 14.148  -5.373  1.379   1.00 8.87  ? 38   ARG C CA  1 
ATOM   3667 C  C   . ARG C  1 38  ? 15.108  -4.264  1.025   1.00 10.90 ? 38   ARG C C   1 
ATOM   3668 O  O   . ARG C  1 38  ? 15.407  -4.040  -0.144  1.00 9.91  ? 38   ARG C O   1 
ATOM   3669 C  CB  . ARG C  1 38  ? 14.961  -6.655  1.425   1.00 13.88 ? 38   ARG C CB  1 
ATOM   3670 C  CG  . ARG C  1 38  ? 14.265  -7.769  2.058   1.00 18.46 ? 38   ARG C CG  1 
ATOM   3671 C  CD  . ARG C  1 38  ? 15.129  -8.999  2.029   1.00 16.51 ? 38   ARG C CD  1 
ATOM   3672 N  NE  . ARG C  1 38  ? 14.242  -10.135 1.918   1.00 13.71 ? 38   ARG C NE  1 
ATOM   3673 C  CZ  . ARG C  1 38  ? 13.589  -10.666 2.940   1.00 17.03 ? 38   ARG C CZ  1 
ATOM   3674 N  NH1 . ARG C  1 38  ? 13.762  -10.189 4.168   1.00 16.81 ? 38   ARG C NH1 1 
ATOM   3675 N  NH2 . ARG C  1 38  ? 12.783  -11.687 2.729   1.00 20.24 ? 38   ARG C NH2 1 
ATOM   3676 N  N   . ALA C  1 39  ? 15.635  -3.590  2.036   1.00 7.22  ? 39   ALA C N   1 
ATOM   3677 C  CA  . ALA C  1 39  ? 16.586  -2.516  1.764   1.00 6.72  ? 39   ALA C CA  1 
ATOM   3678 C  C   . ALA C  1 39  ? 17.677  -2.494  2.817   1.00 7.21  ? 39   ALA C C   1 
ATOM   3679 O  O   . ALA C  1 39  ? 17.442  -2.844  3.968   1.00 10.66 ? 39   ALA C O   1 
ATOM   3680 C  CB  . ALA C  1 39  ? 15.869  -1.160  1.724   1.00 7.82  ? 39   ALA C CB  1 
ATOM   3681 N  N   . TYR C  1 40  ? 18.879  -2.097  2.406   1.00 8.19  ? 40   TYR C N   1 
ATOM   3682 C  CA  . TYR C  1 40  ? 20.006  -2.006  3.320   1.00 8.84  ? 40   TYR C CA  1 
ATOM   3683 C  C   . TYR C  1 40  ? 20.786  -0.736  2.969   1.00 7.98  ? 40   TYR C C   1 
ATOM   3684 O  O   . TYR C  1 40  ? 21.397  -0.631  1.897   1.00 8.70  ? 40   TYR C O   1 
ATOM   3685 C  CB  . TYR C  1 40  ? 20.875  -3.266  3.191   1.00 8.44  ? 40   TYR C CB  1 
ATOM   3686 C  CG  . TYR C  1 40  ? 21.969  -3.434  4.223   1.00 8.34  ? 40   TYR C CG  1 
ATOM   3687 C  CD1 . TYR C  1 40  ? 21.916  -2.783  5.452   1.00 8.80  ? 40   TYR C CD1 1 
ATOM   3688 C  CD2 . TYR C  1 40  ? 23.036  -4.288  3.976   1.00 8.40  ? 40   TYR C CD2 1 
ATOM   3689 C  CE1 . TYR C  1 40  ? 22.925  -2.961  6.398   1.00 7.39  ? 40   TYR C CE1 1 
ATOM   3690 C  CE2 . TYR C  1 40  ? 24.040  -4.483  4.910   1.00 9.18  ? 40   TYR C CE2 1 
ATOM   3691 C  CZ  . TYR C  1 40  ? 23.983  -3.816  6.120   1.00 9.76  ? 40   TYR C CZ  1 
ATOM   3692 O  OH  . TYR C  1 40  ? 24.984  -4.006  7.054   1.00 9.57  ? 40   TYR C OH  1 
ATOM   3693 N  N   . SER C  1 41  ? 20.740  0.239   3.872   1.00 8.36  ? 41   SER C N   1 
ATOM   3694 C  CA  . SER C  1 41  ? 21.395  1.526   3.635   1.00 7.17  ? 41   SER C CA  1 
ATOM   3695 C  C   . SER C  1 41  ? 21.978  2.055   4.933   1.00 7.29  ? 41   SER C C   1 
ATOM   3696 O  O   . SER C  1 41  ? 21.393  1.844   6.003   1.00 11.34 ? 41   SER C O   1 
ATOM   3697 C  CB  . SER C  1 41  ? 20.370  2.533   3.100   1.00 10.51 ? 41   SER C CB  1 
ATOM   3698 O  OG  . SER C  1 41  ? 20.950  3.823   2.935   1.00 9.10  ? 41   SER C OG  1 
ATOM   3699 N  N   . ASP C  1 42  ? 23.112  2.748   4.856   1.00 9.15  ? 42   ASP C N   1 
ATOM   3700 C  CA  . ASP C  1 42  ? 23.634  3.399   6.057   1.00 8.29  ? 42   ASP C CA  1 
ATOM   3701 C  C   . ASP C  1 42  ? 23.556  4.922   5.945   1.00 7.74  ? 42   ASP C C   1 
ATOM   3702 O  O   . ASP C  1 42  ? 24.252  5.656   6.656   1.00 12.90 ? 42   ASP C O   1 
ATOM   3703 C  CB  . ASP C  1 42  ? 25.031  2.890   6.469   1.00 9.17  ? 42   ASP C CB  1 
ATOM   3704 C  CG  . ASP C  1 42  ? 26.080  3.040   5.378   1.00 11.17 ? 42   ASP C CG  1 
ATOM   3705 O  OD1 . ASP C  1 42  ? 25.890  3.854   4.462   1.00 13.57 ? 42   ASP C OD1 1 
ATOM   3706 O  OD2 . ASP C  1 42  ? 27.117  2.336   5.453   1.00 11.31 ? 42   ASP C OD2 1 
ATOM   3707 N  N   . LEU C  1 43  ? 22.659  5.392   5.081   1.00 10.25 ? 43   LEU C N   1 
ATOM   3708 C  CA  . LEU C  1 43  ? 22.298  6.812   5.068   1.00 11.74 ? 43   LEU C CA  1 
ATOM   3709 C  C   . LEU C  1 43  ? 21.527  7.211   6.318   1.00 7.57  ? 43   LEU C C   1 
ATOM   3710 O  O   . LEU C  1 43  ? 20.656  6.466   6.779   1.00 12.40 ? 43   LEU C O   1 
ATOM   3711 C  CB  . LEU C  1 43  ? 21.415  7.146   3.865   1.00 8.42  ? 43   LEU C CB  1 
ATOM   3712 C  CG  . LEU C  1 43  ? 22.089  7.140   2.490   1.00 8.01  ? 43   LEU C CG  1 
ATOM   3713 C  CD1 . LEU C  1 43  ? 21.030  7.355   1.425   1.00 8.34  ? 43   LEU C CD1 1 
ATOM   3714 C  CD2 . LEU C  1 43  ? 23.186  8.212   2.412   1.00 11.18 ? 43   LEU C CD2 1 
ATOM   3715 N  N   . SER C  1 44  ? 21.836  8.402   6.840   1.00 9.43  ? 44   SER C N   1 
ATOM   3716 C  CA  . SER C  1 44  ? 21.079  8.995   7.945   1.00 13.53 ? 44   SER C CA  1 
ATOM   3717 C  C   . SER C  1 44  ? 20.112  10.072  7.467   1.00 11.32 ? 44   SER C C   1 
ATOM   3718 O  O   . SER C  1 44  ? 19.090  10.327  8.108   1.00 13.55 ? 44   SER C O   1 
ATOM   3719 C  CB  . SER C  1 44  ? 22.029  9.612   8.973   1.00 16.02 ? 44   SER C CB  1 
ATOM   3720 O  OG  . SER C  1 44  ? 22.735  8.614   9.669   1.00 19.65 ? 44   SER C OG  1 
ATOM   3721 N  N   . ARG C  1 45  ? 20.447  10.720  6.360   1.00 13.61 ? 45   ARG C N   1 
ATOM   3722 C  CA  . ARG C  1 45  ? 19.559  11.718  5.783   1.00 11.39 ? 45   ARG C CA  1 
ATOM   3723 C  C   . ARG C  1 45  ? 18.323  11.061  5.187   1.00 10.96 ? 45   ARG C C   1 
ATOM   3724 O  O   . ARG C  1 45  ? 18.249  9.833   5.092   1.00 13.87 ? 45   ARG C O   1 
ATOM   3725 C  CB  . ARG C  1 45  ? 20.277  12.515  4.694   1.00 15.44 ? 45   ARG C CB  1 
ATOM   3726 C  CG  . ARG C  1 45  ? 20.669  11.693  3.459   1.00 13.48 ? 45   ARG C CG  1 
ATOM   3727 C  CD  . ARG C  1 45  ? 20.997  12.613  2.271   1.00 11.66 ? 45   ARG C CD  1 
ATOM   3728 N  NE  . ARG C  1 45  ? 21.725  11.901  1.227   1.00 12.00 ? 45   ARG C NE  1 
ATOM   3729 C  CZ  . ARG C  1 45  ? 21.163  11.070  0.354   1.00 10.33 ? 45   ARG C CZ  1 
ATOM   3730 N  NH1 . ARG C  1 45  ? 19.855  10.855  0.388   1.00 10.17 ? 45   ARG C NH1 1 
ATOM   3731 N  NH2 . ARG C  1 45  ? 21.916  10.461  -0.562  1.00 11.43 ? 45   ARG C NH2 1 
ATOM   3732 N  N   . ALA C  1 46  ? 17.367  11.889  4.772   1.00 13.12 ? 46   ALA C N   1 
ATOM   3733 C  CA  . ALA C  1 46  ? 16.140  11.419  4.141   1.00 12.70 ? 46   ALA C CA  1 
ATOM   3734 C  C   . ALA C  1 46  ? 16.433  10.808  2.781   1.00 12.76 ? 46   ALA C C   1 
ATOM   3735 O  O   . ALA C  1 46  ? 17.366  11.224  2.096   1.00 13.77 ? 46   ALA C O   1 
ATOM   3736 C  CB  . ALA C  1 46  ? 15.142  12.579  3.988   1.00 17.11 ? 46   ALA C CB  1 
ATOM   3737 N  N   . TYR C  1 47  ? 15.635  9.824   2.383   1.00 11.60 ? 47   TYR C N   1 
ATOM   3738 C  CA  . TYR C  1 47  ? 15.769  9.266   1.040   1.00 10.73 ? 47   TYR C CA  1 
ATOM   3739 C  C   . TYR C  1 47  ? 14.497  8.577   0.582   1.00 9.77  ? 47   TYR C C   1 
ATOM   3740 O  O   . TYR C  1 47  ? 13.701  8.130   1.396   1.00 10.65 ? 47   TYR C O   1 
ATOM   3741 C  CB  . TYR C  1 47  ? 16.948  8.287   0.965   1.00 10.92 ? 47   TYR C CB  1 
ATOM   3742 C  CG  . TYR C  1 47  ? 16.964  7.169   1.989   1.00 9.22  ? 47   TYR C CG  1 
ATOM   3743 C  CD1 . TYR C  1 47  ? 16.252  5.987   1.782   1.00 8.61  ? 47   TYR C CD1 1 
ATOM   3744 C  CD2 . TYR C  1 47  ? 17.740  7.270   3.140   1.00 11.71 ? 47   TYR C CD2 1 
ATOM   3745 C  CE1 . TYR C  1 47  ? 16.304  4.954   2.704   1.00 8.86  ? 47   TYR C CE1 1 
ATOM   3746 C  CE2 . TYR C  1 47  ? 17.787  6.245   4.074   1.00 11.05 ? 47   TYR C CE2 1 
ATOM   3747 C  CZ  . TYR C  1 47  ? 17.074  5.086   3.845   1.00 11.75 ? 47   TYR C CZ  1 
ATOM   3748 O  OH  . TYR C  1 47  ? 17.124  4.050   4.763   1.00 11.67 ? 47   TYR C OH  1 
ATOM   3749 N  N   . SER C  1 48  ? 14.317  8.492   -0.735  1.00 9.49  ? 48   SER C N   1 
ATOM   3750 C  CA  . SER C  1 48  ? 13.169  7.816   -1.315  1.00 7.20  ? 48   SER C CA  1 
ATOM   3751 C  C   . SER C  1 48  ? 13.482  6.349   -1.498  1.00 8.39  ? 48   SER C C   1 
ATOM   3752 O  O   . SER C  1 48  ? 14.564  6.005   -1.956  1.00 10.21 ? 48   SER C O   1 
ATOM   3753 C  CB  . SER C  1 48  ? 12.865  8.410   -2.693  1.00 8.10  ? 48   SER C CB  1 
ATOM   3754 O  OG  . SER C  1 48  ? 11.779  7.729   -3.311  1.00 11.78 ? 48   SER C OG  1 
ATOM   3755 N  N   . LEU C  1 49  ? 12.533  5.488   -1.135  1.00 7.20  ? 49   LEU C N   1 
ATOM   3756 C  CA  . LEU C  1 49  ? 12.669  4.051   -1.357  1.00 5.90  ? 49   LEU C CA  1 
ATOM   3757 C  C   . LEU C  1 49  ? 11.966  3.588   -2.628  1.00 8.10  ? 49   LEU C C   1 
ATOM   3758 O  O   . LEU C  1 49  ? 12.466  2.707   -3.318  1.00 10.35 ? 49   LEU C O   1 
ATOM   3759 C  CB  . LEU C  1 49  ? 12.118  3.281   -0.156  1.00 8.56  ? 49   LEU C CB  1 
ATOM   3760 C  CG  . LEU C  1 49  ? 13.005  3.327   1.090   1.00 11.37 ? 49   LEU C CG  1 
ATOM   3761 C  CD1 . LEU C  1 49  ? 12.202  3.028   2.358   1.00 16.03 ? 49   LEU C CD1 1 
ATOM   3762 C  CD2 . LEU C  1 49  ? 14.176  2.368   0.931   1.00 13.96 ? 49   LEU C CD2 1 
ATOM   3763 N  N   . PHE C  1 50  ? 10.814  4.181   -2.944  1.00 6.76  ? 50   PHE C N   1 
ATOM   3764 C  CA  . PHE C  1 50  ? 10.011  3.746   -4.088  1.00 8.65  ? 50   PHE C CA  1 
ATOM   3765 C  C   . PHE C  1 50  ? 9.211   4.949   -4.541  1.00 9.11  ? 50   PHE C C   1 
ATOM   3766 O  O   . PHE C  1 50  ? 8.379   5.474   -3.781  1.00 7.81  ? 50   PHE C O   1 
ATOM   3767 C  CB  . PHE C  1 50  ? 9.083   2.594   -3.668  1.00 8.26  ? 50   PHE C CB  1 
ATOM   3768 C  CG  . PHE C  1 50  ? 8.213   2.026   -4.779  1.00 8.25  ? 50   PHE C CG  1 
ATOM   3769 C  CD1 . PHE C  1 50  ? 6.951   2.570   -5.046  1.00 8.10  ? 50   PHE C CD1 1 
ATOM   3770 C  CD2 . PHE C  1 50  ? 8.619   0.906   -5.493  1.00 11.73 ? 50   PHE C CD2 1 
ATOM   3771 C  CE1 . PHE C  1 50  ? 6.128   2.026   -6.024  1.00 8.30  ? 50   PHE C CE1 1 
ATOM   3772 C  CE2 . PHE C  1 50  ? 7.804   0.357   -6.481  1.00 9.32  ? 50   PHE C CE2 1 
ATOM   3773 C  CZ  . PHE C  1 50  ? 6.559   0.908   -6.746  1.00 8.73  ? 50   PHE C CZ  1 
ATOM   3774 N  N   . SER C  1 51  ? 9.486   5.391   -5.768  1.00 9.17  ? 51   SER C N   1 
ATOM   3775 C  CA  . SER C  1 51  ? 8.915   6.623   -6.311  1.00 7.48  ? 51   SER C CA  1 
ATOM   3776 C  C   . SER C  1 51  ? 8.022   6.331   -7.524  1.00 8.53  ? 51   SER C C   1 
ATOM   3777 O  O   . SER C  1 51  ? 8.493   5.827   -8.541  1.00 9.17  ? 51   SER C O   1 
ATOM   3778 C  CB  . SER C  1 51  ? 10.055  7.581   -6.679  1.00 7.30  ? 51   SER C CB  1 
ATOM   3779 O  OG  . SER C  1 51  ? 9.591   8.758   -7.340  1.00 8.70  ? 51   SER C OG  1 
ATOM   3780 N  N   . TYR C  1 52  ? 6.742   6.678   -7.416  1.00 8.01  ? 52   TYR C N   1 
ATOM   3781 C  CA  . TYR C  1 52  ? 5.756   6.383   -8.461  1.00 9.15  ? 52   TYR C CA  1 
ATOM   3782 C  C   . TYR C  1 52  ? 5.043   7.691   -8.788  1.00 9.78  ? 52   TYR C C   1 
ATOM   3783 O  O   . TYR C  1 52  ? 4.311   8.234   -7.956  1.00 9.43  ? 52   TYR C O   1 
ATOM   3784 C  CB  . TYR C  1 52  ? 4.813   5.297   -7.920  1.00 8.96  ? 52   TYR C CB  1 
ATOM   3785 C  CG  . TYR C  1 52  ? 3.542   4.889   -8.671  1.00 8.78  ? 52   TYR C CG  1 
ATOM   3786 C  CD1 . TYR C  1 52  ? 2.543   5.812   -8.986  1.00 10.77 ? 52   TYR C CD1 1 
ATOM   3787 C  CD2 . TYR C  1 52  ? 3.294   3.538   -8.940  1.00 9.30  ? 52   TYR C CD2 1 
ATOM   3788 C  CE1 . TYR C  1 52  ? 1.349   5.406   -9.621  1.00 10.06 ? 52   TYR C CE1 1 
ATOM   3789 C  CE2 . TYR C  1 52  ? 2.121   3.125   -9.557  1.00 10.14 ? 52   TYR C CE2 1 
ATOM   3790 C  CZ  . TYR C  1 52  ? 1.156   4.059   -9.896  1.00 10.76 ? 52   TYR C CZ  1 
ATOM   3791 O  OH  . TYR C  1 52  ? 0.005   3.623   -10.507 1.00 13.72 ? 52   TYR C OH  1 
ATOM   3792 N  N   . ASN C  1 53  ? 5.316   8.221   -9.983  1.00 9.39  ? 53   ASN C N   1 
ATOM   3793 C  CA  . ASN C  1 53  ? 4.688   9.452   -10.456 1.00 9.59  ? 53   ASN C CA  1 
ATOM   3794 C  C   . ASN C  1 53  ? 3.884   9.163   -11.713 1.00 10.37 ? 53   ASN C C   1 
ATOM   3795 O  O   . ASN C  1 53  ? 4.153   8.197   -12.415 1.00 10.74 ? 53   ASN C O   1 
ATOM   3796 C  CB  . ASN C  1 53  ? 5.736   10.516  -10.786 1.00 9.45  ? 53   ASN C CB  1 
ATOM   3797 C  CG  . ASN C  1 53  ? 6.195   11.283  -9.574  1.00 12.17 ? 53   ASN C CG  1 
ATOM   3798 O  OD1 . ASN C  1 53  ? 5.873   10.920  -8.442  1.00 10.71 ? 53   ASN C OD1 1 
ATOM   3799 N  ND2 . ASN C  1 53  ? 6.963   12.350  -9.800  1.00 11.23 ? 53   ASN C ND2 1 
ATOM   3800 N  N   . THR C  1 54  ? 2.893   10.000  -11.995 1.00 10.96 ? 54   THR C N   1 
ATOM   3801 C  CA  . THR C  1 54  ? 2.143   9.870   -13.243 1.00 14.54 ? 54   THR C CA  1 
ATOM   3802 C  C   . THR C  1 54  ? 2.152   11.216  -13.960 1.00 16.92 ? 54   THR C C   1 
ATOM   3803 O  O   . THR C  1 54  ? 2.656   12.203  -13.425 1.00 15.99 ? 54   THR C O   1 
ATOM   3804 C  CB  . THR C  1 54  ? 0.704   9.360   -13.015 1.00 13.08 ? 54   THR C CB  1 
ATOM   3805 O  OG1 . THR C  1 54  ? -0.053  10.332  -12.276 1.00 15.62 ? 54   THR C OG1 1 
ATOM   3806 C  CG2 . THR C  1 54  ? 0.721   8.053   -12.248 1.00 11.18 ? 54   THR C CG2 1 
ATOM   3807 N  N   . GLN C  1 55  ? 1.633   11.259  -15.181 1.00 15.66 ? 55   GLN C N   1 
ATOM   3808 C  CA  . GLN C  1 55  ? 1.712   12.497  -15.949 1.00 19.42 ? 55   GLN C CA  1 
ATOM   3809 C  C   . GLN C  1 55  ? 0.984   13.620  -15.211 1.00 17.35 ? 55   GLN C C   1 
ATOM   3810 O  O   . GLN C  1 55  ? -0.201  13.502  -14.903 1.00 18.99 ? 55   GLN C O   1 
ATOM   3811 C  CB  . GLN C  1 55  ? 1.129   12.305  -17.352 1.00 19.23 ? 55   GLN C CB  1 
ATOM   3812 C  CG  . GLN C  1 55  ? 1.192   13.560  -18.224 1.00 22.59 ? 55   GLN C CG  1 
ATOM   3813 C  CD  . GLN C  1 55  ? 2.597   14.125  -18.349 1.00 27.51 ? 55   GLN C CD  1 
ATOM   3814 O  OE1 . GLN C  1 55  ? 2.829   15.303  -18.077 1.00 35.49 ? 55   GLN C OE1 1 
ATOM   3815 N  NE2 . GLN C  1 55  ? 3.539   13.289  -18.763 1.00 28.70 ? 55   GLN C NE2 1 
ATOM   3816 N  N   . GLY C  1 56  ? 1.718   14.686  -14.904 1.00 16.57 ? 56   GLY C N   1 
ATOM   3817 C  CA  . GLY C  1 56  ? 1.176   15.839  -14.207 1.00 17.23 ? 56   GLY C CA  1 
ATOM   3818 C  C   . GLY C  1 56  ? 0.999   15.652  -12.709 1.00 19.33 ? 56   GLY C C   1 
ATOM   3819 O  O   . GLY C  1 56  ? 0.500   16.542  -12.022 1.00 14.89 ? 56   GLY C O   1 
ATOM   3820 N  N   . ARG C  1 57  ? 1.411   14.497  -12.196 1.00 14.87 ? 57   ARG C N   1 
ATOM   3821 C  CA  . ARG C  1 57  ? 1.196   14.191  -10.788 1.00 13.27 ? 57   ARG C CA  1 
ATOM   3822 C  C   . ARG C  1 57  ? 2.457   13.681  -10.104 1.00 13.41 ? 57   ARG C C   1 
ATOM   3823 O  O   . ARG C  1 57  ? 2.908   12.547  -10.321 1.00 15.00 ? 57   ARG C O   1 
ATOM   3824 C  CB  . ARG C  1 57  ? 0.049   13.198  -10.621 1.00 11.45 ? 57   ARG C CB  1 
ATOM   3825 C  CG  . ARG C  1 57  ? -1.268  13.672  -11.230 1.00 13.84 ? 57   ARG C CG  1 
ATOM   3826 C  CD  . ARG C  1 57  ? -2.413  12.767  -10.826 1.00 16.93 ? 57   ARG C CD  1 
ATOM   3827 N  NE  . ARG C  1 57  ? -2.706  12.862  -9.395  1.00 11.96 ? 57   ARG C NE  1 
ATOM   3828 C  CZ  . ARG C  1 57  ? -3.457  13.806  -8.842  1.00 16.03 ? 57   ARG C CZ  1 
ATOM   3829 N  NH1 . ARG C  1 57  ? -3.993  14.772  -9.592  1.00 15.69 ? 57   ARG C NH1 1 
ATOM   3830 N  NH2 . ARG C  1 57  ? -3.661  13.793  -7.533  1.00 14.71 ? 57   ARG C NH2 1 
ATOM   3831 N  N   . ASP C  1 58  ? 3.026   14.542  -9.274  1.00 8.72  ? 58   ASP C N   1 
ATOM   3832 C  CA  . ASP C  1 58  ? 4.170   14.183  -8.466  1.00 10.64 ? 58   ASP C CA  1 
ATOM   3833 C  C   . ASP C  1 58  ? 3.721   13.561  -7.131  1.00 10.45 ? 58   ASP C C   1 
ATOM   3834 O  O   . ASP C  1 58  ? 2.664   13.895  -6.594  1.00 11.84 ? 58   ASP C O   1 
ATOM   3835 C  CB  . ASP C  1 58  ? 5.003   15.434  -8.212  1.00 14.14 ? 58   ASP C CB  1 
ATOM   3836 C  CG  . ASP C  1 58  ? 6.181   15.174  -7.319  1.00 12.53 ? 58   ASP C CG  1 
ATOM   3837 O  OD1 . ASP C  1 58  ? 6.960   14.253  -7.633  1.00 12.36 ? 58   ASP C OD1 1 
ATOM   3838 O  OD2 . ASP C  1 58  ? 6.349   15.899  -6.312  1.00 13.87 ? 58   ASP C OD2 1 
ATOM   3839 N  N   . ASN C  1 59  ? 4.557   12.685  -6.586  1.00 8.13  ? 59   ASN C N   1 
ATOM   3840 C  CA  . ASN C  1 59  ? 4.240   11.989  -5.335  1.00 10.90 ? 59   ASN C CA  1 
ATOM   3841 C  C   . ASN C  1 59  ? 2.894   11.290  -5.352  1.00 11.40 ? 59   ASN C C   1 
ATOM   3842 O  O   . ASN C  1 59  ? 2.131   11.354  -4.382  1.00 10.05 ? 59   ASN C O   1 
ATOM   3843 C  CB  . ASN C  1 59  ? 4.328   12.939  -4.139  1.00 13.80 ? 59   ASN C CB  1 
ATOM   3844 C  CG  . ASN C  1 59  ? 5.682   13.565  -4.018  1.00 9.51  ? 59   ASN C CG  1 
ATOM   3845 O  OD1 . ASN C  1 59  ? 6.604   13.195  -4.743  1.00 10.07 ? 59   ASN C OD1 1 
ATOM   3846 N  ND2 . ASN C  1 59  ? 5.826   14.526  -3.102  1.00 10.77 ? 59   ASN C ND2 1 
ATOM   3847 N  N   . GLU C  1 60  ? 2.614   10.601  -6.454  1.00 9.19  ? 60   GLU C N   1 
ATOM   3848 C  CA  . GLU C  1 60  ? 1.337   9.927   -6.611  1.00 7.67  ? 60   GLU C CA  1 
ATOM   3849 C  C   . GLU C  1 60  ? 1.309   8.694   -5.704  1.00 9.66  ? 60   GLU C C   1 
ATOM   3850 O  O   . GLU C  1 60  ? 0.306   8.406   -5.059  1.00 9.16  ? 60   GLU C O   1 
ATOM   3851 C  CB  . GLU C  1 60  ? 1.116   9.542   -8.076  1.00 8.56  ? 60   GLU C CB  1 
ATOM   3852 C  CG  . GLU C  1 60  ? -0.244  8.905   -8.344  1.00 9.57  ? 60   GLU C CG  1 
ATOM   3853 C  CD  . GLU C  1 60  ? -1.416  9.853   -8.092  1.00 10.65 ? 60   GLU C CD  1 
ATOM   3854 O  OE1 . GLU C  1 60  ? -1.197  11.074  -7.924  1.00 12.70 ? 60   GLU C OE1 1 
ATOM   3855 O  OE2 . GLU C  1 60  ? -2.558  9.362   -8.093  1.00 11.05 ? 60   GLU C OE2 1 
ATOM   3856 N  N   . LEU C  1 61  ? 2.428   7.983   -5.651  1.00 8.67  ? 61   LEU C N   1 
ATOM   3857 C  CA  . LEU C  1 61  ? 2.608   6.918   -4.669  1.00 8.36  ? 61   LEU C CA  1 
ATOM   3858 C  C   . LEU C  1 61  ? 4.092   6.930   -4.316  1.00 9.43  ? 61   LEU C C   1 
ATOM   3859 O  O   . LEU C  1 61  ? 4.946   6.695   -5.170  1.00 9.99  ? 61   LEU C O   1 
ATOM   3860 C  CB  . LEU C  1 61  ? 2.170   5.568   -5.260  1.00 7.66  ? 61   LEU C CB  1 
ATOM   3861 C  CG  . LEU C  1 61  ? 2.036   4.338   -4.356  1.00 13.46 ? 61   LEU C CG  1 
ATOM   3862 C  CD1 . LEU C  1 61  ? 1.485   3.178   -5.172  1.00 13.39 ? 61   LEU C CD1 1 
ATOM   3863 C  CD2 . LEU C  1 61  ? 3.368   3.940   -3.720  1.00 12.31 ? 61   LEU C CD2 1 
ATOM   3864 N  N   . LEU C  1 62  ? 4.415   7.262   -3.067  1.00 6.11  ? 62   LEU C N   1 
ATOM   3865 C  CA  . LEU C  1 62  ? 5.816   7.415   -2.695  1.00 6.34  ? 62   LEU C CA  1 
ATOM   3866 C  C   . LEU C  1 62  ? 6.054   6.795   -1.328  1.00 7.94  ? 62   LEU C C   1 
ATOM   3867 O  O   . LEU C  1 62  ? 5.302   7.066   -0.389  1.00 8.57  ? 62   LEU C O   1 
ATOM   3868 C  CB  . LEU C  1 62  ? 6.231   8.898   -2.696  1.00 9.84  ? 62   LEU C CB  1 
ATOM   3869 C  CG  . LEU C  1 62  ? 7.595   9.270   -2.099  1.00 8.19  ? 62   LEU C CG  1 
ATOM   3870 C  CD1 . LEU C  1 62  ? 8.729   8.764   -2.972  1.00 8.20  ? 62   LEU C CD1 1 
ATOM   3871 C  CD2 . LEU C  1 62  ? 7.713   10.787  -1.939  1.00 10.38 ? 62   LEU C CD2 1 
ATOM   3872 N  N   . VAL C  1 63  ? 7.060   5.927   -1.246  1.00 7.21  ? 63   VAL C N   1 
ATOM   3873 C  CA  . VAL C  1 63  ? 7.514   5.390   0.037   1.00 7.01  ? 63   VAL C CA  1 
ATOM   3874 C  C   . VAL C  1 63  ? 8.819   6.088   0.382   1.00 8.67  ? 63   VAL C C   1 
ATOM   3875 O  O   . VAL C  1 63  ? 9.812   5.969   -0.334  1.00 7.72  ? 63   VAL C O   1 
ATOM   3876 C  CB  . VAL C  1 63  ? 7.688   3.851   -0.002  1.00 7.18  ? 63   VAL C CB  1 
ATOM   3877 C  CG1 . VAL C  1 63  ? 8.080   3.321   1.382   1.00 9.07  ? 63   VAL C CG1 1 
ATOM   3878 C  CG2 . VAL C  1 63  ? 6.395   3.199   -0.467  1.00 8.55  ? 63   VAL C CG2 1 
ATOM   3879 N  N   . TYR C  1 64  ? 8.810   6.851   1.473   1.00 7.75  ? 64   TYR C N   1 
ATOM   3880 C  CA  . TYR C  1 64  ? 9.898   7.772   1.744   1.00 7.40  ? 64   TYR C CA  1 
ATOM   3881 C  C   . TYR C  1 64  ? 10.385  7.573   3.178   1.00 8.03  ? 64   TYR C C   1 
ATOM   3882 O  O   . TYR C  1 64  ? 9.579   7.381   4.084   1.00 8.56  ? 64   TYR C O   1 
ATOM   3883 C  CB  . TYR C  1 64  ? 9.379   9.205   1.550   1.00 8.84  ? 64   TYR C CB  1 
ATOM   3884 C  CG  . TYR C  1 64  ? 10.426  10.297  1.481   1.00 9.68  ? 64   TYR C CG  1 
ATOM   3885 C  CD1 . TYR C  1 64  ? 11.215  10.465  0.344   1.00 12.03 ? 64   TYR C CD1 1 
ATOM   3886 C  CD2 . TYR C  1 64  ? 10.596  11.190  2.534   1.00 13.17 ? 64   TYR C CD2 1 
ATOM   3887 C  CE1 . TYR C  1 64  ? 12.158  11.470  0.272   1.00 13.06 ? 64   TYR C CE1 1 
ATOM   3888 C  CE2 . TYR C  1 64  ? 11.541  12.213  2.461   1.00 14.78 ? 64   TYR C CE2 1 
ATOM   3889 C  CZ  . TYR C  1 64  ? 12.315  12.341  1.328   1.00 17.90 ? 64   TYR C CZ  1 
ATOM   3890 O  OH  . TYR C  1 64  ? 13.256  13.343  1.238   1.00 16.05 ? 64   TYR C OH  1 
ATOM   3891 N  N   . LYS C  1 65  ? 11.699  7.603   3.369   1.00 9.83  ? 65   LYS C N   1 
ATOM   3892 C  CA  . LYS C  1 65  ? 12.287  7.462   4.706   1.00 8.27  ? 65   LYS C CA  1 
ATOM   3893 C  C   . LYS C  1 65  ? 12.806  8.816   5.203   1.00 10.40 ? 65   LYS C C   1 
ATOM   3894 O  O   . LYS C  1 65  ? 13.848  9.286   4.766   1.00 12.34 ? 65   LYS C O   1 
ATOM   3895 C  CB  . LYS C  1 65  ? 13.439  6.461   4.661   1.00 11.72 ? 65   LYS C CB  1 
ATOM   3896 C  CG  . LYS C  1 65  ? 13.981  6.085   6.031   1.00 14.78 ? 65   LYS C CG  1 
ATOM   3897 C  CD  . LYS C  1 65  ? 13.179  4.946   6.617   1.00 15.88 ? 65   LYS C CD  1 
ATOM   3898 C  CE  . LYS C  1 65  ? 13.646  4.598   8.023   1.00 14.36 ? 65   LYS C CE  1 
ATOM   3899 N  NZ  . LYS C  1 65  ? 15.060  4.151   8.002   1.00 14.03 ? 65   LYS C NZ  1 
ATOM   3900 N  N   A GLU C  1 66  ? 12.075  9.439   6.124   0.63 17.78 ? 66   GLU C N   1 
ATOM   3901 N  N   B GLU C  1 66  ? 12.069  9.420   6.127   0.37 17.75 ? 66   GLU C N   1 
ATOM   3902 C  CA  A GLU C  1 66  ? 12.420  10.777  6.599   0.63 20.08 ? 66   GLU C CA  1 
ATOM   3903 C  CA  B GLU C  1 66  ? 12.395  10.745  6.631   0.37 20.03 ? 66   GLU C CA  1 
ATOM   3904 C  C   A GLU C  1 66  ? 13.675  10.769  7.478   0.63 13.50 ? 66   GLU C C   1 
ATOM   3905 C  C   B GLU C  1 66  ? 13.676  10.743  7.456   0.37 13.63 ? 66   GLU C C   1 
ATOM   3906 O  O   A GLU C  1 66  ? 14.532  11.655  7.376   0.63 16.28 ? 66   GLU C O   1 
ATOM   3907 O  O   B GLU C  1 66  ? 14.546  11.607  7.302   0.37 16.32 ? 66   GLU C O   1 
ATOM   3908 C  CB  A GLU C  1 66  ? 11.250  11.366  7.393   0.63 25.21 ? 66   GLU C CB  1 
ATOM   3909 C  CB  B GLU C  1 66  ? 11.251  11.253  7.502   0.37 24.63 ? 66   GLU C CB  1 
ATOM   3910 C  CG  A GLU C  1 66  ? 9.870   11.051  6.822   0.63 26.55 ? 66   GLU C CG  1 
ATOM   3911 C  CG  B GLU C  1 66  ? 11.360  12.718  7.798   0.37 28.10 ? 66   GLU C CG  1 
ATOM   3912 C  CD  A GLU C  1 66  ? 9.341   12.123  5.923   0.63 21.81 ? 66   GLU C CD  1 
ATOM   3913 C  CD  B GLU C  1 66  ? 11.696  13.497  6.558   0.37 24.22 ? 66   GLU C CD  1 
ATOM   3914 O  OE1 A GLU C  1 66  ? 9.945   13.211  5.929   0.63 22.13 ? 66   GLU C OE1 1 
ATOM   3915 O  OE1 B GLU C  1 66  ? 10.924  13.414  5.580   0.37 30.42 ? 66   GLU C OE1 1 
ATOM   3916 O  OE2 A GLU C  1 66  ? 8.322   11.884  5.221   0.63 16.71 ? 66   GLU C OE2 1 
ATOM   3917 O  OE2 B GLU C  1 66  ? 12.735  14.178  6.556   0.37 17.10 ? 66   GLU C OE2 1 
ATOM   3918 N  N   . ARG C  1 67  ? 13.768  9.758   8.337   1.00 12.63 ? 67   ARG C N   1 
ATOM   3919 C  CA  . ARG C  1 67  ? 14.877  9.628   9.263   1.00 13.43 ? 67   ARG C CA  1 
ATOM   3920 C  C   . ARG C  1 67  ? 14.761  8.257   9.886   1.00 12.82 ? 67   ARG C C   1 
ATOM   3921 O  O   . ARG C  1 67  ? 13.787  7.536   9.639   1.00 10.56 ? 67   ARG C O   1 
ATOM   3922 C  CB  . ARG C  1 67  ? 14.782  10.693  10.351  1.00 12.17 ? 67   ARG C CB  1 
ATOM   3923 C  CG  . ARG C  1 67  ? 13.471  10.678  11.109  1.00 13.79 ? 67   ARG C CG  1 
ATOM   3924 C  CD  . ARG C  1 67  ? 13.418  11.803  12.148  1.00 18.73 ? 67   ARG C CD  1 
ATOM   3925 N  NE  . ARG C  1 67  ? 13.551  13.115  11.524  1.00 18.87 ? 67   ARG C NE  1 
ATOM   3926 C  CZ  . ARG C  1 67  ? 12.563  13.749  10.902  1.00 24.77 ? 67   ARG C CZ  1 
ATOM   3927 N  NH1 . ARG C  1 67  ? 11.366  13.192  10.820  1.00 25.27 ? 67   ARG C NH1 1 
ATOM   3928 N  NH2 . ARG C  1 67  ? 12.771  14.943  10.360  1.00 30.91 ? 67   ARG C NH2 1 
ATOM   3929 N  N   . VAL C  1 68  ? 15.744  7.885   10.697  1.00 12.58 ? 68   VAL C N   1 
ATOM   3930 C  CA  . VAL C  1 68  ? 15.731  6.559   11.308  1.00 11.15 ? 68   VAL C CA  1 
ATOM   3931 C  C   . VAL C  1 68  ? 14.435  6.340   12.100  1.00 10.30 ? 68   VAL C C   1 
ATOM   3932 O  O   . VAL C  1 68  ? 13.955  7.237   12.796  1.00 12.10 ? 68   VAL C O   1 
ATOM   3933 C  CB  . VAL C  1 68  ? 16.998  6.317   12.180  1.00 16.30 ? 68   VAL C CB  1 
ATOM   3934 C  CG1 . VAL C  1 68  ? 17.133  7.399   13.239  1.00 15.51 ? 68   VAL C CG1 1 
ATOM   3935 C  CG2 . VAL C  1 68  ? 16.972  4.929   12.813  1.00 17.88 ? 68   VAL C CG2 1 
ATOM   3936 N  N   . GLY C  1 69  ? 13.847  5.157   11.945  1.00 8.93  ? 69   GLY C N   1 
ATOM   3937 C  CA  . GLY C  1 69  ? 12.645  4.787   12.674  1.00 12.22 ? 69   GLY C CA  1 
ATOM   3938 C  C   . GLY C  1 69  ? 11.328  5.394   12.206  1.00 10.25 ? 69   GLY C C   1 
ATOM   3939 O  O   . GLY C  1 69  ? 10.321  5.265   12.899  1.00 10.89 ? 69   GLY C O   1 
ATOM   3940 N  N   . GLU C  1 70  ? 11.324  6.050   11.046  1.00 9.18  ? 70   GLU C N   1 
ATOM   3941 C  CA  . GLU C  1 70  ? 10.107  6.702   10.544  1.00 9.36  ? 70   GLU C CA  1 
ATOM   3942 C  C   . GLU C  1 70  ? 9.890   6.440   9.056   1.00 9.73  ? 70   GLU C C   1 
ATOM   3943 O  O   . GLU C  1 70  ? 10.740  6.777   8.223   1.00 13.23 ? 70   GLU C O   1 
ATOM   3944 C  CB  . GLU C  1 70  ? 10.164  8.214   10.794  1.00 12.32 ? 70   GLU C CB  1 
ATOM   3945 C  CG  . GLU C  1 70  ? 10.267  8.599   12.276  1.00 17.75 ? 70   GLU C CG  1 
ATOM   3946 C  CD  . GLU C  1 70  ? 10.174  10.105  12.506  1.00 21.47 ? 70   GLU C CD  1 
ATOM   3947 O  OE1 . GLU C  1 70  ? 9.964   10.845  11.531  1.00 17.89 ? 70   GLU C OE1 1 
ATOM   3948 O  OE2 . GLU C  1 70  ? 10.309  10.547  13.669  1.00 21.66 ? 70   GLU C OE2 1 
ATOM   3949 N  N   . TYR C  1 71  ? 8.751   5.838   8.733   1.00 6.10  ? 71   TYR C N   1 
ATOM   3950 C  CA  . TYR C  1 71  ? 8.411   5.496   7.356   1.00 6.78  ? 71   TYR C CA  1 
ATOM   3951 C  C   . TYR C  1 71  ? 7.179   6.265   6.906   1.00 7.94  ? 71   TYR C C   1 
ATOM   3952 O  O   . TYR C  1 71  ? 6.184   6.328   7.626   1.00 7.67  ? 71   TYR C O   1 
ATOM   3953 C  CB  . TYR C  1 71  ? 8.136   3.989   7.263   1.00 10.09 ? 71   TYR C CB  1 
ATOM   3954 C  CG  . TYR C  1 71  ? 9.390   3.177   7.463   1.00 9.06  ? 71   TYR C CG  1 
ATOM   3955 C  CD1 . TYR C  1 71  ? 9.809   2.808   8.742   1.00 8.46  ? 71   TYR C CD1 1 
ATOM   3956 C  CD2 . TYR C  1 71  ? 10.175  2.814   6.386   1.00 11.95 ? 71   TYR C CD2 1 
ATOM   3957 C  CE1 . TYR C  1 71  ? 10.958  2.073   8.930   1.00 8.81  ? 71   TYR C CE1 1 
ATOM   3958 C  CE2 . TYR C  1 71  ? 11.340  2.078   6.569   1.00 11.56 ? 71   TYR C CE2 1 
ATOM   3959 C  CZ  . TYR C  1 71  ? 11.719  1.720   7.845   1.00 11.25 ? 71   TYR C CZ  1 
ATOM   3960 O  OH  . TYR C  1 71  ? 12.876  0.996   8.041   1.00 12.88 ? 71   TYR C OH  1 
ATOM   3961 N  N   . SER C  1 72  ? 7.235   6.843   5.705   1.00 8.12  ? 72   SER C N   1 
ATOM   3962 C  CA  . SER C  1 72  ? 6.104   7.616   5.183   1.00 8.37  ? 72   SER C CA  1 
ATOM   3963 C  C   . SER C  1 72  ? 5.577   7.027   3.880   1.00 6.29  ? 72   SER C C   1 
ATOM   3964 O  O   . SER C  1 72  ? 6.355   6.565   3.043   1.00 8.78  ? 72   SER C O   1 
ATOM   3965 C  CB  . SER C  1 72  ? 6.504   9.076   4.925   1.00 10.06 ? 72   SER C CB  1 
ATOM   3966 O  OG  . SER C  1 72  ? 6.845   9.736   6.130   1.00 12.75 ? 72   SER C OG  1 
ATOM   3967 N  N   . LEU C  1 73  ? 4.252   7.045   3.729   1.00 6.63  ? 73   LEU C N   1 
ATOM   3968 C  CA  . LEU C  1 73  ? 3.600   6.696   2.468   1.00 7.60  ? 73   LEU C CA  1 
ATOM   3969 C  C   . LEU C  1 73  ? 2.861   7.932   1.976   1.00 10.12 ? 73   LEU C C   1 
ATOM   3970 O  O   . LEU C  1 73  ? 2.083   8.521   2.726   1.00 8.92  ? 73   LEU C O   1 
ATOM   3971 C  CB  . LEU C  1 73  ? 2.566   5.590   2.683   1.00 6.32  ? 73   LEU C CB  1 
ATOM   3972 C  CG  . LEU C  1 73  ? 1.691   5.292   1.453   1.00 7.32  ? 73   LEU C CG  1 
ATOM   3973 C  CD1 . LEU C  1 73  ? 2.534   4.710   0.331   1.00 9.44  ? 73   LEU C CD1 1 
ATOM   3974 C  CD2 . LEU C  1 73  ? 0.538   4.336   1.786   1.00 9.80  ? 73   LEU C CD2 1 
ATOM   3975 N  N   . TYR C  1 74  ? 3.098   8.311   0.722   1.00 8.22  ? 74   TYR C N   1 
ATOM   3976 C  CA  . TYR C  1 74  ? 2.339   9.381   0.084   1.00 8.82  ? 74   TYR C CA  1 
ATOM   3977 C  C   . TYR C  1 74  ? 1.364   8.763   -0.894  1.00 5.30  ? 74   TYR C C   1 
ATOM   3978 O  O   . TYR C  1 74  ? 1.724   7.829   -1.630  1.00 7.86  ? 74   TYR C O   1 
ATOM   3979 C  CB  . TYR C  1 74  ? 3.250   10.303  -0.730  1.00 7.18  ? 74   TYR C CB  1 
ATOM   3980 C  CG  . TYR C  1 74  ? 4.207   11.149  0.069   1.00 11.64 ? 74   TYR C CG  1 
ATOM   3981 C  CD1 . TYR C  1 74  ? 5.230   10.570  0.798   1.00 9.34  ? 74   TYR C CD1 1 
ATOM   3982 C  CD2 . TYR C  1 74  ? 4.102   12.539  0.067   1.00 13.31 ? 74   TYR C CD2 1 
ATOM   3983 C  CE1 . TYR C  1 74  ? 6.114   11.340  1.527   1.00 10.15 ? 74   TYR C CE1 1 
ATOM   3984 C  CE2 . TYR C  1 74  ? 4.990   13.321  0.787   1.00 16.23 ? 74   TYR C CE2 1 
ATOM   3985 C  CZ  . TYR C  1 74  ? 5.989   12.717  1.516   1.00 17.08 ? 74   TYR C CZ  1 
ATOM   3986 O  OH  . TYR C  1 74  ? 6.876   13.490  2.238   1.00 19.80 ? 74   TYR C OH  1 
ATOM   3987 N  N   . ILE C  1 75  ? 0.139   9.289   -0.903  1.00 6.87  ? 75   ILE C N   1 
ATOM   3988 C  CA  . ILE C  1 75  ? -0.875  8.910   -1.882  1.00 10.13 ? 75   ILE C CA  1 
ATOM   3989 C  C   . ILE C  1 75  ? -1.426  10.208  -2.456  1.00 9.39  ? 75   ILE C C   1 
ATOM   3990 O  O   . ILE C  1 75  ? -2.032  10.998  -1.743  1.00 8.85  ? 75   ILE C O   1 
ATOM   3991 C  CB  . ILE C  1 75  ? -2.040  8.097   -1.250  1.00 8.78  ? 75   ILE C CB  1 
ATOM   3992 C  CG1 . ILE C  1 75  ? -1.538  6.771   -0.652  1.00 8.56  ? 75   ILE C CG1 1 
ATOM   3993 C  CG2 . ILE C  1 75  ? -3.176  7.860   -2.285  1.00 9.54  ? 75   ILE C CG2 1 
ATOM   3994 C  CD1 . ILE C  1 75  ? -1.047  5.777   -1.710  1.00 9.13  ? 75   ILE C CD1 1 
ATOM   3995 N  N   . GLY C  1 76  ? -1.188  10.453  -3.737  1.00 11.05 ? 76   GLY C N   1 
ATOM   3996 C  CA  . GLY C  1 76  ? -1.658  11.691  -4.340  1.00 10.08 ? 76   GLY C CA  1 
ATOM   3997 C  C   . GLY C  1 76  ? -1.264  12.932  -3.548  1.00 9.16  ? 76   GLY C C   1 
ATOM   3998 O  O   . GLY C  1 76  ? -2.108  13.802  -3.267  1.00 11.74 ? 76   GLY C O   1 
ATOM   3999 N  N   . ARG C  1 77  ? 0.011   12.988  -3.172  1.00 11.01 ? 77   ARG C N   1 
ATOM   4000 C  CA  . ARG C  1 77  ? 0.640   14.115  -2.464  1.00 13.05 ? 77   ARG C CA  1 
ATOM   4001 C  C   . ARG C  1 77  ? 0.415   14.163  -0.955  1.00 10.61 ? 77   ARG C C   1 
ATOM   4002 O  O   . ARG C  1 77  ? 1.184   14.804  -0.238  1.00 12.10 ? 77   ARG C O   1 
ATOM   4003 C  CB  . ARG C  1 77  ? 0.289   15.477  -3.085  1.00 15.29 ? 77   ARG C CB  1 
ATOM   4004 C  CG  . ARG C  1 77  ? 0.980   15.761  -4.415  1.00 22.58 ? 77   ARG C CG  1 
ATOM   4005 C  CD  . ARG C  1 77  ? 1.496   17.213  -4.468  1.00 12.43 ? 77   ARG C CD  1 
ATOM   4006 N  NE  . ARG C  1 77  ? 2.640   17.325  -5.360  1.00 38.43 ? 77   ARG C NE  1 
ATOM   4007 C  CZ  . ARG C  1 77  ? 3.823   17.810  -5.009  1.00 36.24 ? 77   ARG C CZ  1 
ATOM   4008 N  NH1 . ARG C  1 77  ? 4.031   18.259  -3.775  1.00 16.37 ? 77   ARG C NH1 1 
ATOM   4009 N  NH2 . ARG C  1 77  ? 4.792   17.875  -5.910  1.00 47.93 ? 77   ARG C NH2 1 
ATOM   4010 N  N   . HIS C  1 78  ? -0.638  13.501  -0.482  1.00 10.32 ? 78   HIS C N   1 
ATOM   4011 C  CA  . HIS C  1 78  ? -0.915  13.451  0.946   1.00 8.63  ? 78   HIS C CA  1 
ATOM   4012 C  C   . HIS C  1 78  ? -0.087  12.337  1.571   1.00 10.76 ? 78   HIS C C   1 
ATOM   4013 O  O   . HIS C  1 78  ? 0.254   11.374  0.898   1.00 9.63  ? 78   HIS C O   1 
ATOM   4014 C  CB  . HIS C  1 78  ? -2.409  13.232  1.188   1.00 8.66  ? 78   HIS C CB  1 
ATOM   4015 C  CG  . HIS C  1 78  ? -3.244  14.407  0.787   1.00 11.58 ? 78   HIS C CG  1 
ATOM   4016 N  ND1 . HIS C  1 78  ? -3.880  15.215  1.706   1.00 16.22 ? 78   HIS C ND1 1 
ATOM   4017 C  CD2 . HIS C  1 78  ? -3.488  14.952  -0.430  1.00 10.60 ? 78   HIS C CD2 1 
ATOM   4018 C  CE1 . HIS C  1 78  ? -4.498  16.196  1.069   1.00 14.47 ? 78   HIS C CE1 1 
ATOM   4019 N  NE2 . HIS C  1 78  ? -4.285  16.055  -0.227  1.00 10.27 ? 78   HIS C NE2 1 
ATOM   4020 N  N   . LYS C  1 79  ? 0.245   12.473  2.848   1.00 9.79  ? 79   LYS C N   1 
ATOM   4021 C  CA  . LYS C  1 79  ? 1.141   11.499  3.458   1.00 11.15 ? 79   LYS C CA  1 
ATOM   4022 C  C   . LYS C  1 79  ? 0.696   11.059  4.838   1.00 10.82 ? 79   LYS C C   1 
ATOM   4023 O  O   . LYS C  1 79  ? -0.061  11.756  5.534   1.00 10.00 ? 79   LYS C O   1 
ATOM   4024 C  CB  . LYS C  1 79  ? 2.558   12.061  3.534   1.00 13.07 ? 79   LYS C CB  1 
ATOM   4025 C  CG  . LYS C  1 79  ? 2.707   13.144  4.585   1.00 17.46 ? 79   LYS C CG  1 
ATOM   4026 C  CD  . LYS C  1 79  ? 4.057   13.820  4.498   1.00 21.99 ? 79   LYS C CD  1 
ATOM   4027 C  CE  . LYS C  1 79  ? 5.158   12.906  4.973   1.00 20.65 ? 79   LYS C CE  1 
ATOM   4028 N  NZ  . LYS C  1 79  ? 6.470   13.616  4.911   1.00 28.11 ? 79   LYS C NZ  1 
ATOM   4029 N  N   . VAL C  1 80  ? 1.154   9.875   5.217   1.00 8.57  ? 80   VAL C N   1 
ATOM   4030 C  CA  . VAL C  1 80  ? 1.051   9.418   6.594   1.00 7.89  ? 80   VAL C CA  1 
ATOM   4031 C  C   . VAL C  1 80  ? 2.429   8.900   6.976   1.00 9.24  ? 80   VAL C C   1 
ATOM   4032 O  O   . VAL C  1 80  ? 3.201   8.484   6.113   1.00 11.06 ? 80   VAL C O   1 
ATOM   4033 C  CB  . VAL C  1 80  ? -0.006  8.313   6.760   1.00 8.93  ? 80   VAL C CB  1 
ATOM   4034 C  CG1 . VAL C  1 80  ? -1.414  8.891   6.539   1.00 9.92  ? 80   VAL C CG1 1 
ATOM   4035 C  CG2 . VAL C  1 80  ? 0.282   7.164   5.804   1.00 8.86  ? 80   VAL C CG2 1 
ATOM   4036 N  N   . THR C  1 81  ? 2.753   8.961   8.265   1.00 8.90  ? 81   THR C N   1 
ATOM   4037 C  CA  . THR C  1 81  ? 4.053   8.499   8.741   1.00 7.73  ? 81   THR C CA  1 
ATOM   4038 C  C   . THR C  1 81  ? 3.832   7.657   9.979   1.00 6.98  ? 81   THR C C   1 
ATOM   4039 O  O   . THR C  1 81  ? 3.039   8.029   10.846  1.00 9.23  ? 81   THR C O   1 
ATOM   4040 C  CB  . THR C  1 81  ? 4.942   9.695   9.126   1.00 9.86  ? 81   THR C CB  1 
ATOM   4041 O  OG1 . THR C  1 81  ? 5.170   10.502  7.966   1.00 14.02 ? 81   THR C OG1 1 
ATOM   4042 C  CG2 . THR C  1 81  ? 6.275   9.215   9.675   1.00 10.22 ? 81   THR C CG2 1 
ATOM   4043 N  N   . SER C  1 82  ? 4.516   6.518   10.054  1.00 8.42  ? 82   SER C N   1 
ATOM   4044 C  CA  . SER C  1 82  ? 4.442   5.686   11.245  1.00 8.45  ? 82   SER C CA  1 
ATOM   4045 C  C   . SER C  1 82  ? 5.839   5.338   11.718  1.00 9.59  ? 82   SER C C   1 
ATOM   4046 O  O   . SER C  1 82  ? 6.784   5.308   10.936  1.00 8.81  ? 82   SER C O   1 
ATOM   4047 C  CB  . SER C  1 82  ? 3.587   4.440   11.000  1.00 13.46 ? 82   SER C CB  1 
ATOM   4048 O  OG  . SER C  1 82  ? 2.214   4.788   11.117  1.00 13.88 ? 82   SER C OG  1 
ATOM   4049 N  N   . LYS C  1 83  ? 5.968   5.135   13.023  1.00 8.52  ? 83   LYS C N   1 
ATOM   4050 C  CA  . LYS C  1 83  ? 7.274   4.980   13.649  1.00 7.26  ? 83   LYS C CA  1 
ATOM   4051 C  C   . LYS C  1 83  ? 7.524   3.551   14.082  1.00 8.95  ? 83   LYS C C   1 
ATOM   4052 O  O   . LYS C  1 83  ? 6.588   2.787   14.321  1.00 9.45  ? 83   LYS C O   1 
ATOM   4053 C  CB  . LYS C  1 83  ? 7.354   5.905   14.861  1.00 9.14  ? 83   LYS C CB  1 
ATOM   4054 C  CG  . LYS C  1 83  ? 7.262   7.366   14.468  1.00 12.95 ? 83   LYS C CG  1 
ATOM   4055 C  CD  . LYS C  1 83  ? 7.335   8.278   15.682  1.00 19.44 ? 83   LYS C CD  1 
ATOM   4056 C  CE  . LYS C  1 83  ? 7.306   9.732   15.240  1.00 24.23 ? 83   LYS C CE  1 
ATOM   4057 N  NZ  . LYS C  1 83  ? 7.836   10.641  16.300  1.00 23.55 ? 83   LYS C NZ  1 
ATOM   4058 N  N   . VAL C  1 84  ? 8.797   3.197   14.180  1.00 8.64  ? 84   VAL C N   1 
ATOM   4059 C  CA  . VAL C  1 84  ? 9.168   1.864   14.622  1.00 10.34 ? 84   VAL C CA  1 
ATOM   4060 C  C   . VAL C  1 84  ? 10.507  1.940   15.330  1.00 12.39 ? 84   VAL C C   1 
ATOM   4061 O  O   . VAL C  1 84  ? 11.318  2.827   15.059  1.00 10.04 ? 84   VAL C O   1 
ATOM   4062 C  CB  . VAL C  1 84  ? 9.255   0.894   13.424  1.00 12.49 ? 84   VAL C CB  1 
ATOM   4063 C  CG1 . VAL C  1 84  ? 10.420  1.265   12.521  1.00 15.84 ? 84   VAL C CG1 1 
ATOM   4064 C  CG2 . VAL C  1 84  ? 9.392   -0.544  13.908  1.00 9.77  ? 84   VAL C CG2 1 
ATOM   4065 N  N   . ILE C  1 85  ? 10.722  1.025   16.266  1.00 9.63  ? 85   ILE C N   1 
ATOM   4066 C  CA  . ILE C  1 85  ? 12.038  0.842   16.851  1.00 9.97  ? 85   ILE C CA  1 
ATOM   4067 C  C   . ILE C  1 85  ? 12.881  0.007   15.893  1.00 12.00 ? 85   ILE C C   1 
ATOM   4068 O  O   . ILE C  1 85  ? 12.496  -1.106  15.532  1.00 12.63 ? 85   ILE C O   1 
ATOM   4069 C  CB  . ILE C  1 85  ? 11.936  0.080   18.166  1.00 14.72 ? 85   ILE C CB  1 
ATOM   4070 C  CG1 . ILE C  1 85  ? 11.135  0.882   19.185  1.00 16.43 ? 85   ILE C CG1 1 
ATOM   4071 C  CG2 . ILE C  1 85  ? 13.325  -0.259  18.700  1.00 13.61 ? 85   ILE C CG2 1 
ATOM   4072 C  CD1 . ILE C  1 85  ? 10.610  0.020   20.311  1.00 14.37 ? 85   ILE C CD1 1 
ATOM   4073 N  N   A GLU C  1 86  ? 14.021  0.549   15.469  0.59 13.17 ? 86   GLU C N   1 
ATOM   4074 N  N   B GLU C  1 86  ? 14.025  0.548   15.497  0.41 13.17 ? 86   GLU C N   1 
ATOM   4075 C  CA  A GLU C  1 86  ? 14.922  -0.176  14.563  0.59 13.62 ? 86   GLU C CA  1 
ATOM   4076 C  CA  B GLU C  1 86  ? 14.946  -0.173  14.627  0.41 13.63 ? 86   GLU C CA  1 
ATOM   4077 C  C   A GLU C  1 86  ? 16.386  0.149   14.848  0.59 11.92 ? 86   GLU C C   1 
ATOM   4078 C  C   B GLU C  1 86  ? 16.383  0.062   15.049  0.41 11.99 ? 86   GLU C C   1 
ATOM   4079 O  O   A GLU C  1 86  ? 16.708  1.255   15.284  0.59 14.73 ? 86   GLU C O   1 
ATOM   4080 O  O   B GLU C  1 86  ? 16.683  1.014   15.768  0.41 13.54 ? 86   GLU C O   1 
ATOM   4081 C  CB  A GLU C  1 86  ? 14.583  0.108   13.088  0.59 15.77 ? 86   GLU C CB  1 
ATOM   4082 C  CB  B GLU C  1 86  ? 14.766  0.253   13.168  0.41 15.43 ? 86   GLU C CB  1 
ATOM   4083 C  CG  A GLU C  1 86  ? 14.798  1.550   12.638  0.59 13.29 ? 86   GLU C CG  1 
ATOM   4084 C  CG  B GLU C  1 86  ? 13.877  -0.667  12.356  0.41 13.77 ? 86   GLU C CG  1 
ATOM   4085 C  CD  A GLU C  1 86  ? 14.456  1.772   11.167  0.59 16.42 ? 86   GLU C CD  1 
ATOM   4086 C  CD  B GLU C  1 86  ? 13.929  -0.344  10.876  0.41 14.87 ? 86   GLU C CD  1 
ATOM   4087 O  OE1 A GLU C  1 86  ? 14.809  2.841   10.617  0.59 7.70  ? 86   GLU C OE1 1 
ATOM   4088 O  OE1 B GLU C  1 86  ? 13.337  0.677   10.474  0.41 12.47 ? 86   GLU C OE1 1 
ATOM   4089 O  OE2 A GLU C  1 86  ? 13.838  0.870   10.559  0.59 14.41 ? 86   GLU C OE2 1 
ATOM   4090 O  OE2 B GLU C  1 86  ? 14.564  -1.106  10.118  0.41 11.52 ? 86   GLU C OE2 1 
ATOM   4091 N  N   . LYS C  1 87  ? 17.265  -0.823  14.602  1.00 13.40 ? 87   LYS C N   1 
ATOM   4092 C  CA  . LYS C  1 87  ? 18.693  -0.632  14.776  1.00 14.62 ? 87   LYS C CA  1 
ATOM   4093 C  C   . LYS C  1 87  ? 19.219  0.132   13.570  1.00 12.76 ? 87   LYS C C   1 
ATOM   4094 O  O   . LYS C  1 87  ? 18.593  0.129   12.505  1.00 15.08 ? 87   LYS C O   1 
ATOM   4095 C  CB  . LYS C  1 87  ? 19.400  -1.985  14.885  1.00 15.56 ? 87   LYS C CB  1 
ATOM   4096 C  CG  . LYS C  1 87  ? 19.004  -2.791  16.107  1.00 22.79 ? 87   LYS C CG  1 
ATOM   4097 C  CD  . LYS C  1 87  ? 19.773  -4.104  16.149  1.00 30.95 ? 87   LYS C CD  1 
ATOM   4098 C  CE  . LYS C  1 87  ? 19.520  -4.853  17.447  1.00 44.31 ? 87   LYS C CE  1 
ATOM   4099 N  NZ  . LYS C  1 87  ? 20.258  -6.147  17.487  1.00 52.62 ? 87   LYS C NZ  1 
ATOM   4100 N  N   . PHE C  1 88  ? 20.358  0.795   13.741  1.00 10.91 ? 88   PHE C N   1 
ATOM   4101 C  CA  . PHE C  1 88  ? 20.975  1.515   12.638  1.00 11.67 ? 88   PHE C CA  1 
ATOM   4102 C  C   . PHE C  1 88  ? 22.491  1.378   12.649  1.00 11.79 ? 88   PHE C C   1 
ATOM   4103 O  O   . PHE C  1 88  ? 23.130  1.632   13.665  1.00 12.50 ? 88   PHE C O   1 
ATOM   4104 C  CB  . PHE C  1 88  ? 20.638  3.002   12.685  1.00 10.70 ? 88   PHE C CB  1 
ATOM   4105 C  CG  . PHE C  1 88  ? 21.406  3.803   11.678  1.00 11.02 ? 88   PHE C CG  1 
ATOM   4106 C  CD1 . PHE C  1 88  ? 21.028  3.791   10.348  1.00 11.21 ? 88   PHE C CD1 1 
ATOM   4107 C  CD2 . PHE C  1 88  ? 22.539  4.512   12.046  1.00 13.01 ? 88   PHE C CD2 1 
ATOM   4108 C  CE1 . PHE C  1 88  ? 21.750  4.503   9.400   1.00 12.65 ? 88   PHE C CE1 1 
ATOM   4109 C  CE2 . PHE C  1 88  ? 23.264  5.227   11.109  1.00 15.38 ? 88   PHE C CE2 1 
ATOM   4110 C  CZ  . PHE C  1 88  ? 22.870  5.219   9.783   1.00 16.71 ? 88   PHE C CZ  1 
ATOM   4111 N  N   . PRO C  1 89  ? 23.079  1.003   11.511  1.00 11.00 ? 89   PRO C N   1 
ATOM   4112 C  CA  . PRO C  1 89  ? 22.438  0.583   10.260  1.00 7.91  ? 89   PRO C CA  1 
ATOM   4113 C  C   . PRO C  1 89  ? 21.930  -0.828  10.415  1.00 10.55 ? 89   PRO C C   1 
ATOM   4114 O  O   . PRO C  1 89  ? 22.459  -1.556  11.243  1.00 13.06 ? 89   PRO C O   1 
ATOM   4115 C  CB  . PRO C  1 89  ? 23.600  0.574   9.254   1.00 8.93  ? 89   PRO C CB  1 
ATOM   4116 C  CG  . PRO C  1 89  ? 24.721  1.295   9.919   1.00 15.41 ? 89   PRO C CG  1 
ATOM   4117 C  CD  . PRO C  1 89  ? 24.540  1.088   11.375  1.00 10.93 ? 89   PRO C CD  1 
ATOM   4118 N  N   . ALA C  1 90  ? 20.915  -1.209  9.646   1.00 9.98  ? 90   ALA C N   1 
ATOM   4119 C  CA  . ALA C  1 90  ? 20.442  -2.580  9.662   1.00 9.77  ? 90   ALA C CA  1 
ATOM   4120 C  C   . ALA C  1 90  ? 19.636  -2.843  8.403   1.00 9.20  ? 90   ALA C C   1 
ATOM   4121 O  O   . ALA C  1 90  ? 18.897  -1.971  7.962   1.00 10.86 ? 90   ALA C O   1 
ATOM   4122 C  CB  . ALA C  1 90  ? 19.570  -2.815  10.896  1.00 11.17 ? 90   ALA C CB  1 
ATOM   4123 N  N   . PRO C  1 91  ? 19.767  -4.049  7.836   1.00 9.24  ? 91   PRO C N   1 
ATOM   4124 C  CA  . PRO C  1 91  ? 18.845  -4.446  6.772   1.00 10.73 ? 91   PRO C CA  1 
ATOM   4125 C  C   . PRO C  1 91  ? 17.417  -4.378  7.287   1.00 10.46 ? 91   PRO C C   1 
ATOM   4126 O  O   . PRO C  1 91  ? 17.177  -4.579  8.478   1.00 12.83 ? 91   PRO C O   1 
ATOM   4127 C  CB  . PRO C  1 91  ? 19.219  -5.907  6.507   1.00 13.45 ? 91   PRO C CB  1 
ATOM   4128 C  CG  . PRO C  1 91  ? 20.614  -6.042  6.972   1.00 13.28 ? 91   PRO C CG  1 
ATOM   4129 C  CD  . PRO C  1 91  ? 20.747  -5.106  8.146   1.00 12.17 ? 91   PRO C CD  1 
ATOM   4130 N  N   . VAL C  1 92  ? 16.475  -4.104  6.402   1.00 9.02  ? 92   VAL C N   1 
ATOM   4131 C  CA  . VAL C  1 92  ? 15.076  -4.072  6.802   1.00 9.24  ? 92   VAL C CA  1 
ATOM   4132 C  C   . VAL C  1 92  ? 14.208  -4.686  5.713   1.00 9.33  ? 92   VAL C C   1 
ATOM   4133 O  O   . VAL C  1 92  ? 14.529  -4.585  4.520   1.00 10.05 ? 92   VAL C O   1 
ATOM   4134 C  CB  . VAL C  1 92  ? 14.616  -2.627  7.033   1.00 9.64  ? 92   VAL C CB  1 
ATOM   4135 C  CG1 . VAL C  1 92  ? 14.551  -1.868  5.707   1.00 11.38 ? 92   VAL C CG1 1 
ATOM   4136 C  CG2 . VAL C  1 92  ? 13.272  -2.609  7.723   1.00 8.90  ? 92   VAL C CG2 1 
ATOM   4137 N  N   . HIS C  1 93  ? 13.133  -5.350  6.126   1.00 6.33  ? 93   HIS C N   1 
ATOM   4138 C  CA  . HIS C  1 93  ? 12.103  -5.764  5.188   1.00 7.25  ? 93   HIS C CA  1 
ATOM   4139 C  C   . HIS C  1 93  ? 10.887  -4.865  5.417   1.00 8.04  ? 93   HIS C C   1 
ATOM   4140 O  O   . HIS C  1 93  ? 10.406  -4.723  6.547   1.00 8.76  ? 93   HIS C O   1 
ATOM   4141 C  CB  . HIS C  1 93  ? 11.703  -7.227  5.400   1.00 8.52  ? 93   HIS C CB  1 
ATOM   4142 C  CG  . HIS C  1 93  ? 10.657  -7.703  4.439   1.00 8.13  ? 93   HIS C CG  1 
ATOM   4143 N  ND1 . HIS C  1 93  ? 9.324   -7.799  4.773   1.00 8.81  ? 93   HIS C ND1 1 
ATOM   4144 C  CD2 . HIS C  1 93  ? 10.751  -8.092  3.143   1.00 9.67  ? 93   HIS C CD2 1 
ATOM   4145 C  CE1 . HIS C  1 93  ? 8.639   -8.228  3.726   1.00 9.57  ? 93   HIS C CE1 1 
ATOM   4146 N  NE2 . HIS C  1 93  ? 9.482   -8.424  2.726   1.00 7.79  ? 93   HIS C NE2 1 
ATOM   4147 N  N   . ILE C  1 94  ? 10.408  -4.250  4.346   1.00 6.21  ? 94   ILE C N   1 
ATOM   4148 C  CA  . ILE C  1 94  ? 9.301   -3.312  4.441   1.00 8.24  ? 94   ILE C CA  1 
ATOM   4149 C  C   . ILE C  1 94  ? 8.119   -3.783  3.599   1.00 11.06 ? 94   ILE C C   1 
ATOM   4150 O  O   . ILE C  1 94  ? 8.276   -4.156  2.436   1.00 13.18 ? 94   ILE C O   1 
ATOM   4151 C  CB  . ILE C  1 94  ? 9.739   -1.929  3.938   1.00 8.52  ? 94   ILE C CB  1 
ATOM   4152 C  CG1 . ILE C  1 94  ? 10.914  -1.398  4.765   1.00 11.26 ? 94   ILE C CG1 1 
ATOM   4153 C  CG2 . ILE C  1 94  ? 8.553   -0.950  3.947   1.00 13.05 ? 94   ILE C CG2 1 
ATOM   4154 C  CD1 . ILE C  1 94  ? 11.780  -0.404  4.017   1.00 14.64 ? 94   ILE C CD1 1 
ATOM   4155 N  N   . CYS C  1 95  ? 6.931   -3.776  4.188   1.00 7.72  ? 95   CYS C N   1 
ATOM   4156 C  CA  . CYS C  1 95  ? 5.713   -3.942  3.406   1.00 7.97  ? 95   CYS C CA  1 
ATOM   4157 C  C   . CYS C  1 95  ? 4.840   -2.737  3.692   1.00 9.41  ? 95   CYS C C   1 
ATOM   4158 O  O   . CYS C  1 95  ? 4.773   -2.271  4.828   1.00 9.55  ? 95   CYS C O   1 
ATOM   4159 C  CB  . CYS C  1 95  ? 4.956   -5.193  3.826   1.00 13.79 ? 95   CYS C CB  1 
ATOM   4160 S  SG  . CYS C  1 95  ? 5.609   -6.740  3.141   1.00 17.54 ? 95   CYS C SG  1 
ATOM   4161 N  N   . VAL C  1 96  ? 4.181   -2.221  2.667   1.00 7.71  ? 96   VAL C N   1 
ATOM   4162 C  CA  . VAL C  1 96  ? 3.165   -1.206  2.910   1.00 7.89  ? 96   VAL C CA  1 
ATOM   4163 C  C   . VAL C  1 96  ? 1.953   -1.475  2.036   1.00 9.41  ? 96   VAL C C   1 
ATOM   4164 O  O   . VAL C  1 96  ? 2.089   -1.791  0.863   1.00 8.82  ? 96   VAL C O   1 
ATOM   4165 C  CB  . VAL C  1 96  ? 3.696   0.223   2.681   1.00 9.67  ? 96   VAL C CB  1 
ATOM   4166 C  CG1 . VAL C  1 96  ? 4.090   0.430   1.216   1.00 12.59 ? 96   VAL C CG1 1 
ATOM   4167 C  CG2 . VAL C  1 96  ? 2.665   1.235   3.133   1.00 11.58 ? 96   VAL C CG2 1 
ATOM   4168 N  N   . SER C  1 97  ? 0.764   -1.380  2.618   1.00 9.52  ? 97   SER C N   1 
ATOM   4169 C  CA  . SER C  1 97  ? -0.451  -1.546  1.829   1.00 6.15  ? 97   SER C CA  1 
ATOM   4170 C  C   . SER C  1 97  ? -1.350  -0.340  1.999   1.00 9.10  ? 97   SER C C   1 
ATOM   4171 O  O   . SER C  1 97  ? -1.251  0.396   2.982   1.00 9.47  ? 97   SER C O   1 
ATOM   4172 C  CB  . SER C  1 97  ? -1.209  -2.824  2.219   1.00 8.96  ? 97   SER C CB  1 
ATOM   4173 O  OG  . SER C  1 97  ? -1.809  -2.716  3.508   1.00 10.97 ? 97   SER C OG  1 
ATOM   4174 N  N   . TRP C  1 98  ? -2.236  -0.143  1.036   1.00 7.38  ? 98   TRP C N   1 
ATOM   4175 C  CA  . TRP C  1 98  ? -3.207  0.928   1.134   1.00 7.12  ? 98   TRP C CA  1 
ATOM   4176 C  C   . TRP C  1 98  ? -4.489  0.508   0.442   1.00 9.70  ? 98   TRP C C   1 
ATOM   4177 O  O   . TRP C  1 98  ? -4.459  -0.144  -0.590  1.00 9.11  ? 98   TRP C O   1 
ATOM   4178 C  CB  . TRP C  1 98  ? -2.646  2.201   0.483   1.00 6.60  ? 98   TRP C CB  1 
ATOM   4179 C  CG  . TRP C  1 98  ? -3.625  3.343   0.479   1.00 8.52  ? 98   TRP C CG  1 
ATOM   4180 C  CD1 . TRP C  1 98  ? -3.931  4.178   1.526   1.00 8.22  ? 98   TRP C CD1 1 
ATOM   4181 C  CD2 . TRP C  1 98  ? -4.420  3.778   -0.627  1.00 8.79  ? 98   TRP C CD2 1 
ATOM   4182 N  NE1 . TRP C  1 98  ? -4.877  5.106   1.129   1.00 11.06 ? 98   TRP C NE1 1 
ATOM   4183 C  CE2 . TRP C  1 98  ? -5.188  4.882   -0.188  1.00 15.26 ? 98   TRP C CE2 1 
ATOM   4184 C  CE3 . TRP C  1 98  ? -4.554  3.346   -1.952  1.00 13.01 ? 98   TRP C CE3 1 
ATOM   4185 C  CZ2 . TRP C  1 98  ? -6.077  5.553   -1.029  1.00 11.54 ? 98   TRP C CZ2 1 
ATOM   4186 C  CZ3 . TRP C  1 98  ? -5.437  4.015   -2.783  1.00 11.50 ? 98   TRP C CZ3 1 
ATOM   4187 C  CH2 . TRP C  1 98  ? -6.191  5.101   -2.318  1.00 11.29 ? 98   TRP C CH2 1 
ATOM   4188 N  N   . GLU C  1 99  ? -5.614  0.915   1.014   1.00 9.21  ? 99   GLU C N   1 
ATOM   4189 C  CA  . GLU C  1 99  ? -6.923  0.487   0.560   1.00 9.99  ? 99   GLU C CA  1 
ATOM   4190 C  C   . GLU C  1 99  ? -7.806  1.726   0.389   1.00 10.76 ? 99   GLU C C   1 
ATOM   4191 O  O   . GLU C  1 99  ? -8.114  2.403   1.362   1.00 11.58 ? 99   GLU C O   1 
ATOM   4192 C  CB  . GLU C  1 99  ? -7.499  -0.405  1.650   1.00 12.48 ? 99   GLU C CB  1 
ATOM   4193 C  CG  . GLU C  1 99  ? -8.838  -0.986  1.367   1.00 16.79 ? 99   GLU C CG  1 
ATOM   4194 C  CD  . GLU C  1 99  ? -9.327  -1.788  2.548   1.00 22.54 ? 99   GLU C CD  1 
ATOM   4195 O  OE1 . GLU C  1 99  ? -9.397  -3.025  2.417   1.00 25.70 ? 99   GLU C OE1 1 
ATOM   4196 O  OE2 . GLU C  1 99  ? -9.618  -1.185  3.610   1.00 15.98 ? 99   GLU C OE2 1 
ATOM   4197 N  N   . SER C  1 100 ? -8.209  2.026   -0.842  1.00 9.79  ? 100  SER C N   1 
ATOM   4198 C  CA  . SER C  1 100 ? -9.009  3.224   -1.087  1.00 11.36 ? 100  SER C CA  1 
ATOM   4199 C  C   . SER C  1 100 ? -10.285 3.281   -0.254  1.00 12.43 ? 100  SER C C   1 
ATOM   4200 O  O   . SER C  1 100 ? -10.663 4.346   0.252   1.00 12.33 ? 100  SER C O   1 
ATOM   4201 C  CB  . SER C  1 100 ? -9.377  3.337   -2.563  1.00 12.60 ? 100  SER C CB  1 
ATOM   4202 O  OG  . SER C  1 100 ? -10.306 4.404   -2.742  1.00 12.74 ? 100  SER C OG  1 
ATOM   4203 N  N   . SER C  1 101 ? -10.954 2.141   -0.101  1.00 10.86 ? 101  SER C N   1 
ATOM   4204 C  CA  . SER C  1 101 ? -12.291 2.155   0.481   1.00 11.40 ? 101  SER C CA  1 
ATOM   4205 C  C   . SER C  1 101 ? -12.281 2.687   1.918   1.00 16.01 ? 101  SER C C   1 
ATOM   4206 O  O   . SER C  1 101 ? -13.204 3.392   2.324   1.00 13.80 ? 101  SER C O   1 
ATOM   4207 C  CB  . SER C  1 101 ? -12.954 0.774   0.389   1.00 16.16 ? 101  SER C CB  1 
ATOM   4208 O  OG  . SER C  1 101 ? -12.224 -0.190  1.120   1.00 19.75 ? 101  SER C OG  1 
ATOM   4209 N  N   . SER C  1 102 ? -11.215 2.379   2.661   1.00 11.08 ? 102  SER C N   1 
ATOM   4210 C  CA  . SER C  1 102 ? -11.060 2.830   4.037   1.00 8.82  ? 102  SER C CA  1 
ATOM   4211 C  C   . SER C  1 102 ? -10.034 3.946   4.176   1.00 9.45  ? 102  SER C C   1 
ATOM   4212 O  O   . SER C  1 102 ? -10.006 4.631   5.187   1.00 10.43 ? 102  SER C O   1 
ATOM   4213 C  CB  . SER C  1 102 ? -10.612 1.665   4.913   1.00 10.29 ? 102  SER C CB  1 
ATOM   4214 O  OG  . SER C  1 102 ? -9.330  1.223   4.494   1.00 9.72  ? 102  SER C OG  1 
ATOM   4215 N  N   . GLY C  1 103 ? -9.172  4.085   3.174   1.00 7.48  ? 103  GLY C N   1 
ATOM   4216 C  CA  . GLY C  1 103 ? -8.000  4.943   3.244   1.00 9.49  ? 103  GLY C CA  1 
ATOM   4217 C  C   . GLY C  1 103 ? -6.875  4.408   4.130   1.00 8.73  ? 103  GLY C C   1 
ATOM   4218 O  O   . GLY C  1 103 ? -5.853  5.065   4.309   1.00 7.66  ? 103  GLY C O   1 
ATOM   4219 N  N   . ILE C  1 104 ? -7.054  3.217   4.691   1.00 9.51  ? 104  ILE C N   1 
ATOM   4220 C  CA  . ILE C  1 104 ? -6.072  2.691   5.648   1.00 9.16  ? 104  ILE C CA  1 
ATOM   4221 C  C   . ILE C  1 104 ? -4.749  2.278   4.991   1.00 9.88  ? 104  ILE C C   1 
ATOM   4222 O  O   . ILE C  1 104 ? -4.734  1.555   3.989   1.00 9.01  ? 104  ILE C O   1 
ATOM   4223 C  CB  . ILE C  1 104 ? -6.646  1.500   6.444   1.00 9.99  ? 104  ILE C CB  1 
ATOM   4224 C  CG1 . ILE C  1 104 ? -7.810  1.955   7.330   1.00 8.94  ? 104  ILE C CG1 1 
ATOM   4225 C  CG2 . ILE C  1 104 ? -5.549  0.804   7.264   1.00 10.78 ? 104  ILE C CG2 1 
ATOM   4226 C  CD1 . ILE C  1 104 ? -7.433  3.012   8.381   1.00 13.21 ? 104  ILE C CD1 1 
ATOM   4227 N  N   . ALA C  1 105 ? -3.646  2.763   5.562   1.00 8.83  ? 105  ALA C N   1 
ATOM   4228 C  CA  . ALA C  1 105 ? -2.292  2.404   5.148   1.00 8.43  ? 105  ALA C CA  1 
ATOM   4229 C  C   . ALA C  1 105 ? -1.675  1.546   6.242   1.00 12.44 ? 105  ALA C C   1 
ATOM   4230 O  O   . ALA C  1 105 ? -1.692  1.930   7.408   1.00 10.16 ? 105  ALA C O   1 
ATOM   4231 C  CB  . ALA C  1 105 ? -1.443  3.669   4.942   1.00 7.12  ? 105  ALA C CB  1 
ATOM   4232 N  N   . GLU C  1 106 ? -1.135  0.385   5.872   1.00 9.34  ? 106  GLU C N   1 
ATOM   4233 C  CA  . GLU C  1 106 ? -0.506  -0.503  6.840   1.00 9.47  ? 106  GLU C CA  1 
ATOM   4234 C  C   . GLU C  1 106 ? 0.961   -0.670  6.515   1.00 12.73 ? 106  GLU C C   1 
ATOM   4235 O  O   . GLU C  1 106 ? 1.287   -1.218  5.468   1.00 13.80 ? 106  GLU C O   1 
ATOM   4236 C  CB  . GLU C  1 106 ? -1.108  -1.904  6.744   1.00 14.91 ? 106  GLU C CB  1 
ATOM   4237 C  CG  . GLU C  1 106 ? -2.454  -2.078  7.329   1.00 13.68 ? 106  GLU C CG  1 
ATOM   4238 C  CD  . GLU C  1 106 ? -2.928  -3.525  7.236   1.00 19.67 ? 106  GLU C CD  1 
ATOM   4239 O  OE1 . GLU C  1 106 ? -2.077  -4.463  7.177   1.00 15.43 ? 106  GLU C OE1 1 
ATOM   4240 O  OE2 . GLU C  1 106 ? -4.162  -3.713  7.222   1.00 20.60 ? 106  GLU C OE2 1 
ATOM   4241 N  N   . PHE C  1 107 ? 1.844   -0.227  7.406   1.00 8.01  ? 107  PHE C N   1 
ATOM   4242 C  CA  . PHE C  1 107 ? 3.274   -0.521  7.264   1.00 7.15  ? 107  PHE C CA  1 
ATOM   4243 C  C   . PHE C  1 107 ? 3.604   -1.745  8.114   1.00 8.39  ? 107  PHE C C   1 
ATOM   4244 O  O   . PHE C  1 107 ? 3.115   -1.874  9.246   1.00 8.93  ? 107  PHE C O   1 
ATOM   4245 C  CB  . PHE C  1 107 ? 4.136   0.654   7.766   1.00 8.29  ? 107  PHE C CB  1 
ATOM   4246 C  CG  . PHE C  1 107 ? 4.531   1.657   6.690   1.00 10.75 ? 107  PHE C CG  1 
ATOM   4247 C  CD1 . PHE C  1 107 ? 5.508   1.346   5.744   1.00 9.25  ? 107  PHE C CD1 1 
ATOM   4248 C  CD2 . PHE C  1 107 ? 3.940   2.911   6.646   1.00 13.89 ? 107  PHE C CD2 1 
ATOM   4249 C  CE1 . PHE C  1 107 ? 5.891   2.264   4.768   1.00 10.16 ? 107  PHE C CE1 1 
ATOM   4250 C  CE2 . PHE C  1 107 ? 4.313   3.841   5.680   1.00 11.27 ? 107  PHE C CE2 1 
ATOM   4251 C  CZ  . PHE C  1 107 ? 5.287   3.523   4.734   1.00 10.16 ? 107  PHE C CZ  1 
ATOM   4252 N  N   . TRP C  1 108 ? 4.444   -2.635  7.577   1.00 7.08  ? 108  TRP C N   1 
ATOM   4253 C  CA  . TRP C  1 108 ? 4.974   -3.757  8.342   1.00 8.72  ? 108  TRP C CA  1 
ATOM   4254 C  C   . TRP C  1 108 ? 6.481   -3.721  8.194   1.00 8.53  ? 108  TRP C C   1 
ATOM   4255 O  O   . TRP C  1 108 ? 6.982   -3.647  7.078   1.00 9.16  ? 108  TRP C O   1 
ATOM   4256 C  CB  . TRP C  1 108 ? 4.448   -5.082  7.779   1.00 9.97  ? 108  TRP C CB  1 
ATOM   4257 C  CG  . TRP C  1 108 ? 2.988   -5.295  8.001   1.00 9.03  ? 108  TRP C CG  1 
ATOM   4258 C  CD1 . TRP C  1 108 ? 1.951   -4.648  7.373   1.00 14.44 ? 108  TRP C CD1 1 
ATOM   4259 C  CD2 . TRP C  1 108 ? 2.393   -6.226  8.906   1.00 9.66  ? 108  TRP C CD2 1 
ATOM   4260 N  NE1 . TRP C  1 108 ? 0.745   -5.128  7.843   1.00 14.02 ? 108  TRP C NE1 1 
ATOM   4261 C  CE2 . TRP C  1 108 ? 0.990   -6.090  8.790   1.00 12.46 ? 108  TRP C CE2 1 
ATOM   4262 C  CE3 . TRP C  1 108 ? 2.910   -7.161  9.814   1.00 9.38  ? 108  TRP C CE3 1 
ATOM   4263 C  CZ2 . TRP C  1 108 ? 0.100   -6.860  9.539   1.00 12.39 ? 108  TRP C CZ2 1 
ATOM   4264 C  CZ3 . TRP C  1 108 ? 2.019   -7.922  10.561  1.00 13.87 ? 108  TRP C CZ3 1 
ATOM   4265 C  CH2 . TRP C  1 108 ? 0.630   -7.759  10.421  1.00 12.87 ? 108  TRP C CH2 1 
ATOM   4266 N  N   . ILE C  1 109 ? 7.202   -3.729  9.317   1.00 6.65  ? 109  ILE C N   1 
ATOM   4267 C  CA  . ILE C  1 109 ? 8.656   -3.632  9.285   1.00 6.40  ? 109  ILE C CA  1 
ATOM   4268 C  C   . ILE C  1 109 ? 9.222   -4.896  9.917   1.00 10.36 ? 109  ILE C C   1 
ATOM   4269 O  O   . ILE C  1 109 ? 8.932   -5.201  11.081  1.00 12.41 ? 109  ILE C O   1 
ATOM   4270 C  CB  . ILE C  1 109 ? 9.126   -2.410  10.084  1.00 10.11 ? 109  ILE C CB  1 
ATOM   4271 C  CG1 . ILE C  1 109 ? 8.548   -1.128  9.484   1.00 8.73  ? 109  ILE C CG1 1 
ATOM   4272 C  CG2 . ILE C  1 109 ? 10.656  -2.348  10.152  1.00 9.83  ? 109  ILE C CG2 1 
ATOM   4273 C  CD1 . ILE C  1 109 ? 8.980   -0.876  8.049   1.00 10.93 ? 109  ILE C CD1 1 
ATOM   4274 N  N   . ASN C  1 110 ? 10.015  -5.643  9.154   1.00 9.55  ? 110  ASN C N   1 
ATOM   4275 C  CA  . ASN C  1 110 ? 10.522  -6.922  9.643   1.00 9.08  ? 110  ASN C CA  1 
ATOM   4276 C  C   . ASN C  1 110 ? 9.423   -7.795  10.232  1.00 12.94 ? 110  ASN C C   1 
ATOM   4277 O  O   . ASN C  1 110 ? 9.610   -8.423  11.279  1.00 13.02 ? 110  ASN C O   1 
ATOM   4278 C  CB  . ASN C  1 110 ? 11.637  -6.700  10.664  1.00 11.82 ? 110  ASN C CB  1 
ATOM   4279 C  CG  . ASN C  1 110 ? 12.805  -5.956  10.073  1.00 14.49 ? 110  ASN C CG  1 
ATOM   4280 O  OD1 . ASN C  1 110 ? 13.123  -6.127  8.897   1.00 11.44 ? 110  ASN C OD1 1 
ATOM   4281 N  ND2 . ASN C  1 110 ? 13.445  -5.119  10.875  1.00 16.43 ? 110  ASN C ND2 1 
ATOM   4282 N  N   . GLY C  1 111 ? 8.278   -7.805  9.554   1.00 10.59 ? 111  GLY C N   1 
ATOM   4283 C  CA  . GLY C  1 111 ? 7.170   -8.677  9.892   1.00 10.66 ? 111  GLY C CA  1 
ATOM   4284 C  C   . GLY C  1 111 ? 6.370   -8.199  11.090  1.00 11.65 ? 111  GLY C C   1 
ATOM   4285 O  O   . GLY C  1 111 ? 5.504   -8.925  11.587  1.00 12.57 ? 111  GLY C O   1 
ATOM   4286 N  N   . THR C  1 112 ? 6.659   -6.983  11.547  1.00 11.83 ? 112  THR C N   1 
ATOM   4287 C  CA  . THR C  1 112 ? 5.954   -6.379  12.680  1.00 12.06 ? 112  THR C CA  1 
ATOM   4288 C  C   . THR C  1 112 ? 5.059   -5.230  12.206  1.00 7.96  ? 112  THR C C   1 
ATOM   4289 O  O   . THR C  1 112 ? 5.517   -4.339  11.498  1.00 10.98 ? 112  THR C O   1 
ATOM   4290 C  CB  . THR C  1 112 ? 6.948   -5.823  13.715  1.00 18.35 ? 112  THR C CB  1 
ATOM   4291 O  OG1 . THR C  1 112 ? 7.668   -6.913  14.312  1.00 22.04 ? 112  THR C OG1 1 
ATOM   4292 C  CG2 . THR C  1 112 ? 6.204   -5.060  14.802  1.00 26.64 ? 112  THR C CG2 1 
ATOM   4293 N  N   . PRO C  1 113 ? 3.786   -5.227  12.624  1.00 8.71  ? 113  PRO C N   1 
ATOM   4294 C  CA  . PRO C  1 113 ? 2.908   -4.156  12.133  1.00 6.48  ? 113  PRO C CA  1 
ATOM   4295 C  C   . PRO C  1 113 ? 3.147   -2.834  12.855  1.00 8.60  ? 113  PRO C C   1 
ATOM   4296 O  O   . PRO C  1 113 ? 3.263   -2.805  14.081  1.00 8.86  ? 113  PRO C O   1 
ATOM   4297 C  CB  . PRO C  1 113 ? 1.507   -4.683  12.433  1.00 7.98  ? 113  PRO C CB  1 
ATOM   4298 C  CG  . PRO C  1 113 ? 1.697   -5.616  13.627  1.00 9.17  ? 113  PRO C CG  1 
ATOM   4299 C  CD  . PRO C  1 113 ? 3.091   -6.197  13.485  1.00 8.77  ? 113  PRO C CD  1 
ATOM   4300 N  N   . LEU C  1 114 ? 3.227   -1.753  12.086  1.00 7.33  ? 114  LEU C N   1 
ATOM   4301 C  CA  . LEU C  1 114 ? 3.234   -0.422  12.679  1.00 7.13  ? 114  LEU C CA  1 
ATOM   4302 C  C   . LEU C  1 114 ? 1.790   0.010   12.932  1.00 7.14  ? 114  LEU C C   1 
ATOM   4303 O  O   . LEU C  1 114 ? 0.836   -0.668  12.534  1.00 7.74  ? 114  LEU C O   1 
ATOM   4304 C  CB  . LEU C  1 114 ? 3.936   0.580   11.760  1.00 5.93  ? 114  LEU C CB  1 
ATOM   4305 C  CG  . LEU C  1 114 ? 5.349   0.203   11.298  1.00 10.47 ? 114  LEU C CG  1 
ATOM   4306 C  CD1 . LEU C  1 114 ? 6.080   1.447   10.800  1.00 9.22  ? 114  LEU C CD1 1 
ATOM   4307 C  CD2 . LEU C  1 114 ? 6.127   -0.441  12.419  1.00 12.36 ? 114  LEU C CD2 1 
ATOM   4308 N  N   . VAL C  1 115 ? 1.622   1.148   13.588  1.00 8.21  ? 115  VAL C N   1 
ATOM   4309 C  CA  . VAL C  1 115 ? 0.279   1.689   13.794  1.00 6.88  ? 115  VAL C CA  1 
ATOM   4310 C  C   . VAL C  1 115 ? -0.358  2.061   12.444  1.00 7.89  ? 115  VAL C C   1 
ATOM   4311 O  O   . VAL C  1 115 ? 0.264   2.743   11.608  1.00 8.01  ? 115  VAL C O   1 
ATOM   4312 C  CB  . VAL C  1 115 ? 0.326   2.942   14.692  1.00 6.20  ? 115  VAL C CB  1 
ATOM   4313 C  CG1 . VAL C  1 115 ? -1.096  3.517   14.896  1.00 7.19  ? 115  VAL C CG1 1 
ATOM   4314 C  CG2 . VAL C  1 115 ? 0.949   2.595   16.060  1.00 7.13  ? 115  VAL C CG2 1 
ATOM   4315 N  N   . LYS C  1 116 ? -1.583  1.592   12.219  1.00 7.84  ? 116  LYS C N   1 
ATOM   4316 C  CA  . LYS C  1 116 ? -2.325  1.964   11.013  1.00 9.41  ? 116  LYS C CA  1 
ATOM   4317 C  C   . LYS C  1 116 ? -2.590  3.463   10.991  1.00 10.72 ? 116  LYS C C   1 
ATOM   4318 O  O   . LYS C  1 116 ? -2.851  4.071   12.034  1.00 10.64 ? 116  LYS C O   1 
ATOM   4319 C  CB  . LYS C  1 116 ? -3.663  1.226   10.955  1.00 9.06  ? 116  LYS C CB  1 
ATOM   4320 C  CG  . LYS C  1 116 ? -3.563  -0.234  10.509  1.00 13.88 ? 116  LYS C CG  1 
ATOM   4321 C  CD  . LYS C  1 116 ? -4.902  -0.939  10.753  1.00 13.59 ? 116  LYS C CD  1 
ATOM   4322 C  CE  . LYS C  1 116 ? -4.963  -2.339  10.151  1.00 19.29 ? 116  LYS C CE  1 
ATOM   4323 N  NZ  . LYS C  1 116 ? -4.124  -3.323  10.889  1.00 16.50 ? 116  LYS C NZ  1 
ATOM   4324 N  N   . LYS C  1 117 ? -2.501  4.053   9.802   1.00 8.36  ? 117  LYS C N   1 
ATOM   4325 C  CA  . LYS C  1 117 ? -2.882  5.452   9.589   1.00 6.48  ? 117  LYS C CA  1 
ATOM   4326 C  C   . LYS C  1 117 ? -3.819  5.470   8.399   1.00 9.44  ? 117  LYS C C   1 
ATOM   4327 O  O   . LYS C  1 117 ? -4.054  4.427   7.788   1.00 13.09 ? 117  LYS C O   1 
ATOM   4328 C  CB  . LYS C  1 117 ? -1.646  6.315   9.314   1.00 9.31  ? 117  LYS C CB  1 
ATOM   4329 C  CG  . LYS C  1 117 ? -0.601  6.293   10.427  1.00 10.28 ? 117  LYS C CG  1 
ATOM   4330 C  CD  . LYS C  1 117 ? -1.166  6.893   11.715  1.00 10.74 ? 117  LYS C CD  1 
ATOM   4331 C  CE  . LYS C  1 117 ? -0.264  6.579   12.894  1.00 9.42  ? 117  LYS C CE  1 
ATOM   4332 N  NZ  . LYS C  1 117 ? 1.027   7.302   12.736  1.00 11.07 ? 117  LYS C NZ  1 
ATOM   4333 N  N   . GLY C  1 118 ? -4.388  6.627   8.079   1.00 9.56  ? 118  GLY C N   1 
ATOM   4334 C  CA  . GLY C  1 118 ? -5.363  6.667   7.006   1.00 8.99  ? 118  GLY C CA  1 
ATOM   4335 C  C   . GLY C  1 118 ? -5.299  7.954   6.209   1.00 9.32  ? 118  GLY C C   1 
ATOM   4336 O  O   . GLY C  1 118 ? -5.065  9.031   6.759   1.00 11.06 ? 118  GLY C O   1 
ATOM   4337 N  N   . LEU C  1 119 ? -5.520  7.835   4.906   1.00 8.46  ? 119  LEU C N   1 
ATOM   4338 C  CA  . LEU C  1 119 ? -5.458  8.989   4.014   1.00 8.51  ? 119  LEU C CA  1 
ATOM   4339 C  C   . LEU C  1 119 ? -6.161  8.695   2.695   1.00 10.57 ? 119  LEU C C   1 
ATOM   4340 O  O   . LEU C  1 119 ? -6.228  7.547   2.258   1.00 8.75  ? 119  LEU C O   1 
ATOM   4341 C  CB  . LEU C  1 119 ? -4.006  9.406   3.735   1.00 8.11  ? 119  LEU C CB  1 
ATOM   4342 C  CG  . LEU C  1 119 ? -3.160  8.577   2.752   1.00 7.31  ? 119  LEU C CG  1 
ATOM   4343 C  CD1 . LEU C  1 119 ? -1.839  9.312   2.407   1.00 8.32  ? 119  LEU C CD1 1 
ATOM   4344 C  CD2 . LEU C  1 119 ? -2.842  7.177   3.307   1.00 9.69  ? 119  LEU C CD2 1 
ATOM   4345 N  N   . ARG C  1 120 ? -6.691  9.744   2.072   1.00 11.12 ? 120  ARG C N   1 
ATOM   4346 C  CA  . ARG C  1 120 ? -7.208  9.660   0.700   1.00 9.37  ? 120  ARG C CA  1 
ATOM   4347 C  C   . ARG C  1 120 ? -8.284  8.584   0.508   1.00 10.25 ? 120  ARG C C   1 
ATOM   4348 O  O   . ARG C  1 120 ? -8.326  7.916   -0.526  1.00 10.93 ? 120  ARG C O   1 
ATOM   4349 C  CB  . ARG C  1 120 ? -6.056  9.490   -0.309  1.00 11.19 ? 120  ARG C CB  1 
ATOM   4350 C  CG  . ARG C  1 120 ? -5.024  10.648  -0.281  1.00 13.94 ? 120  ARG C CG  1 
ATOM   4351 C  CD  . ARG C  1 120 ? -4.923  11.507  -1.579  1.00 22.73 ? 120  ARG C CD  1 
ATOM   4352 N  NE  . ARG C  1 120 ? -6.189  12.050  -2.046  1.00 34.01 ? 120  ARG C NE  1 
ATOM   4353 C  CZ  . ARG C  1 120 ? -6.312  12.986  -2.989  1.00 19.72 ? 120  ARG C CZ  1 
ATOM   4354 N  NH1 . ARG C  1 120 ? -5.248  13.516  -3.592  1.00 17.33 ? 120  ARG C NH1 1 
ATOM   4355 N  NH2 . ARG C  1 120 ? -7.518  13.386  -3.334  1.00 25.58 ? 120  ARG C NH2 1 
ATOM   4356 N  N   . GLN C  1 121 ? -9.160  8.427   1.499   1.00 10.20 ? 121  GLN C N   1 
ATOM   4357 C  CA  . GLN C  1 121 ? -10.278 7.492   1.368   1.00 8.75  ? 121  GLN C CA  1 
ATOM   4358 C  C   . GLN C  1 121 ? -11.082 7.875   0.132   1.00 10.62 ? 121  GLN C C   1 
ATOM   4359 O  O   . GLN C  1 121 ? -11.446 9.045   -0.032  1.00 12.76 ? 121  GLN C O   1 
ATOM   4360 C  CB  . GLN C  1 121 ? -11.168 7.554   2.608   1.00 9.34  ? 121  GLN C CB  1 
ATOM   4361 C  CG  . GLN C  1 121 ? -12.360 6.600   2.579   1.00 11.18 ? 121  GLN C CG  1 
ATOM   4362 C  CD  . GLN C  1 121 ? -13.177 6.678   3.848   1.00 14.07 ? 121  GLN C CD  1 
ATOM   4363 O  OE1 . GLN C  1 121 ? -13.317 7.748   4.447   1.00 18.83 ? 121  GLN C OE1 1 
ATOM   4364 N  NE2 . GLN C  1 121 ? -13.729 5.542   4.268   1.00 16.63 ? 121  GLN C NE2 1 
ATOM   4365 N  N   . GLY C  1 122 ? -11.343 6.897   -0.730  1.00 11.16 ? 122  GLY C N   1 
ATOM   4366 C  CA  . GLY C  1 122 ? -12.137 7.115   -1.925  1.00 13.50 ? 122  GLY C CA  1 
ATOM   4367 C  C   . GLY C  1 122 ? -11.309 7.438   -3.156  1.00 14.01 ? 122  GLY C C   1 
ATOM   4368 O  O   . GLY C  1 122 ? -11.822 7.401   -4.273  1.00 16.54 ? 122  GLY C O   1 
ATOM   4369 N  N   . TYR C  1 123 ? -10.036 7.767   -2.949  1.00 11.51 ? 123  TYR C N   1 
ATOM   4370 C  CA  . TYR C  1 123 ? -9.127  8.134   -4.037  1.00 10.94 ? 123  TYR C CA  1 
ATOM   4371 C  C   . TYR C  1 123 ? -8.704  6.907   -4.839  1.00 13.50 ? 123  TYR C C   1 
ATOM   4372 O  O   . TYR C  1 123 ? -8.658  5.801   -4.304  1.00 13.31 ? 123  TYR C O   1 
ATOM   4373 C  CB  . TYR C  1 123 ? -7.882  8.825   -3.455  1.00 10.64 ? 123  TYR C CB  1 
ATOM   4374 C  CG  . TYR C  1 123 ? -6.933  9.383   -4.477  1.00 14.14 ? 123  TYR C CG  1 
ATOM   4375 C  CD1 . TYR C  1 123 ? -7.275  10.504  -5.223  1.00 14.43 ? 123  TYR C CD1 1 
ATOM   4376 C  CD2 . TYR C  1 123 ? -5.683  8.805   -4.687  1.00 10.30 ? 123  TYR C CD2 1 
ATOM   4377 C  CE1 . TYR C  1 123 ? -6.400  11.036  -6.158  1.00 11.88 ? 123  TYR C CE1 1 
ATOM   4378 C  CE2 . TYR C  1 123 ? -4.797  9.327   -5.618  1.00 12.27 ? 123  TYR C CE2 1 
ATOM   4379 C  CZ  . TYR C  1 123 ? -5.166  10.448  -6.353  1.00 13.04 ? 123  TYR C CZ  1 
ATOM   4380 O  OH  . TYR C  1 123 ? -4.311  10.972  -7.284  1.00 12.94 ? 123  TYR C OH  1 
ATOM   4381 N  N   . PHE C  1 124 ? -8.404  7.108   -6.122  1.00 13.53 ? 124  PHE C N   1 
ATOM   4382 C  CA  . PHE C  1 124 ? -7.778  6.071   -6.941  1.00 16.46 ? 124  PHE C CA  1 
ATOM   4383 C  C   . PHE C  1 124 ? -6.388  6.533   -7.373  1.00 10.59 ? 124  PHE C C   1 
ATOM   4384 O  O   . PHE C  1 124 ? -6.232  7.624   -7.929  1.00 13.24 ? 124  PHE C O   1 
ATOM   4385 C  CB  . PHE C  1 124 ? -8.623  5.779   -8.190  1.00 16.90 ? 124  PHE C CB  1 
ATOM   4386 C  CG  . PHE C  1 124 ? -9.951  5.132   -7.894  1.00 24.52 ? 124  PHE C CG  1 
ATOM   4387 C  CD1 . PHE C  1 124 ? -10.159 3.791   -8.160  1.00 35.34 ? 124  PHE C CD1 1 
ATOM   4388 C  CD2 . PHE C  1 124 ? -10.991 5.868   -7.355  1.00 36.68 ? 124  PHE C CD2 1 
ATOM   4389 C  CE1 . PHE C  1 124 ? -11.381 3.194   -7.892  1.00 40.49 ? 124  PHE C CE1 1 
ATOM   4390 C  CE2 . PHE C  1 124 ? -12.213 5.274   -7.085  1.00 33.87 ? 124  PHE C CE2 1 
ATOM   4391 C  CZ  . PHE C  1 124 ? -12.403 3.934   -7.354  1.00 36.23 ? 124  PHE C CZ  1 
ATOM   4392 N  N   . VAL C  1 125 ? -5.367  5.718   -7.107  1.00 12.25 ? 125  VAL C N   1 
ATOM   4393 C  CA  . VAL C  1 125 ? -4.009  6.042   -7.538  1.00 10.95 ? 125  VAL C CA  1 
ATOM   4394 C  C   . VAL C  1 125 ? -3.974  5.977   -9.069  1.00 11.84 ? 125  VAL C C   1 
ATOM   4395 O  O   . VAL C  1 125 ? -4.397  4.981   -9.666  1.00 13.85 ? 125  VAL C O   1 
ATOM   4396 C  CB  . VAL C  1 125 ? -2.966  5.076   -6.913  1.00 11.98 ? 125  VAL C CB  1 
ATOM   4397 C  CG1 . VAL C  1 125 ? -1.593  5.275   -7.536  1.00 11.98 ? 125  VAL C CG1 1 
ATOM   4398 C  CG2 . VAL C  1 125 ? -2.893  5.282   -5.390  1.00 13.32 ? 125  VAL C CG2 1 
ATOM   4399 N  N   A GLU C  1 126 ? -3.482  7.036   -9.704  0.48 11.56 ? 126  GLU C N   1 
ATOM   4400 N  N   B GLU C  1 126 ? -3.473  7.035   -9.698  0.52 11.54 ? 126  GLU C N   1 
ATOM   4401 C  CA  A GLU C  1 126 ? -3.560  7.122   -11.160 0.48 14.76 ? 126  GLU C CA  1 
ATOM   4402 C  CA  B GLU C  1 126 ? -3.520  7.123   -11.153 0.52 14.75 ? 126  GLU C CA  1 
ATOM   4403 C  C   A GLU C  1 126 ? -2.633  6.137   -11.868 0.48 16.72 ? 126  GLU C C   1 
ATOM   4404 C  C   B GLU C  1 126 ? -2.697  6.029   -11.816 0.52 16.75 ? 126  GLU C C   1 
ATOM   4405 O  O   A GLU C  1 126 ? -1.577  5.774   -11.349 0.48 13.45 ? 126  GLU C O   1 
ATOM   4406 O  O   B GLU C  1 126 ? -1.773  5.481   -11.217 0.52 12.97 ? 126  GLU C O   1 
ATOM   4407 C  CB  A GLU C  1 126 ? -3.327  8.557   -11.647 0.48 15.80 ? 126  GLU C CB  1 
ATOM   4408 C  CB  B GLU C  1 126 ? -3.068  8.502   -11.640 0.52 15.64 ? 126  GLU C CB  1 
ATOM   4409 C  CG  A GLU C  1 126 ? -4.385  9.545   -11.164 0.48 16.05 ? 126  GLU C CG  1 
ATOM   4410 C  CG  B GLU C  1 126 ? -3.435  8.774   -13.086 0.52 20.56 ? 126  GLU C CG  1 
ATOM   4411 C  CD  A GLU C  1 126 ? -4.800  10.533  -12.242 0.48 23.12 ? 126  GLU C CD  1 
ATOM   4412 C  CD  B GLU C  1 126 ? -4.892  8.451   -13.382 0.52 21.88 ? 126  GLU C CD  1 
ATOM   4413 O  OE1 A GLU C  1 126 ? -4.410  10.319  -13.407 0.48 24.25 ? 126  GLU C OE1 1 
ATOM   4414 O  OE1 B GLU C  1 126 ? -5.772  9.232   -12.965 0.52 24.32 ? 126  GLU C OE1 1 
ATOM   4415 O  OE2 A GLU C  1 126 ? -5.521  11.513  -11.933 0.48 16.67 ? 126  GLU C OE2 1 
ATOM   4416 O  OE2 B GLU C  1 126 ? -5.156  7.417   -14.036 0.52 20.37 ? 126  GLU C OE2 1 
ATOM   4417 N  N   . ALA C  1 127 ? -3.053  5.714   -13.059 1.00 15.59 ? 127  ALA C N   1 
ATOM   4418 C  CA  . ALA C  1 127 ? -2.365  4.693   -13.837 1.00 17.46 ? 127  ALA C CA  1 
ATOM   4419 C  C   . ALA C  1 127 ? -1.258  5.252   -14.736 1.00 14.46 ? 127  ALA C C   1 
ATOM   4420 O  O   . ALA C  1 127 ? -0.954  6.451   -14.708 1.00 15.46 ? 127  ALA C O   1 
ATOM   4421 C  CB  . ALA C  1 127 ? -3.390  3.932   -14.676 1.00 20.96 ? 127  ALA C CB  1 
ATOM   4422 N  N   . GLN C  1 128 ? -0.670  4.366   -15.537 1.00 13.50 ? 128  GLN C N   1 
ATOM   4423 C  CA  . GLN C  1 128 ? 0.444   4.704   -16.428 1.00 14.82 ? 128  GLN C CA  1 
ATOM   4424 C  C   . GLN C  1 128 ? 1.592   5.401   -15.702 1.00 16.96 ? 128  GLN C C   1 
ATOM   4425 O  O   . GLN C  1 128 ? 1.986   6.510   -16.053 1.00 14.59 ? 128  GLN C O   1 
ATOM   4426 C  CB  . GLN C  1 128 ? -0.042  5.529   -17.630 1.00 18.22 ? 128  GLN C CB  1 
ATOM   4427 C  CG  . GLN C  1 128 ? -1.118  4.816   -18.434 1.00 22.37 ? 128  GLN C CG  1 
ATOM   4428 C  CD  . GLN C  1 128 ? -1.375  5.454   -19.785 1.00 49.60 ? 128  GLN C CD  1 
ATOM   4429 O  OE1 . GLN C  1 128 ? -0.592  6.279   -20.258 1.00 58.09 ? 128  GLN C OE1 1 
ATOM   4430 N  NE2 . GLN C  1 128 ? -2.477  5.066   -20.419 1.00 51.88 ? 128  GLN C NE2 1 
ATOM   4431 N  N   . PRO C  1 129 ? 2.149   4.736   -14.682 1.00 12.96 ? 129  PRO C N   1 
ATOM   4432 C  CA  . PRO C  1 129 ? 3.170   5.416   -13.883 1.00 12.66 ? 129  PRO C CA  1 
ATOM   4433 C  C   . PRO C  1 129 ? 4.556   5.316   -14.484 1.00 13.77 ? 129  PRO C C   1 
ATOM   4434 O  O   . PRO C  1 129 ? 4.816   4.484   -15.356 1.00 14.93 ? 129  PRO C O   1 
ATOM   4435 C  CB  . PRO C  1 129 ? 3.156   4.623   -12.579 1.00 13.97 ? 129  PRO C CB  1 
ATOM   4436 C  CG  . PRO C  1 129 ? 2.789   3.230   -13.010 1.00 14.18 ? 129  PRO C CG  1 
ATOM   4437 C  CD  . PRO C  1 129 ? 1.811   3.403   -14.153 1.00 16.70 ? 129  PRO C CD  1 
ATOM   4438 N  N   . LYS C  1 130 ? 5.442   6.179   -14.006 1.00 8.14  ? 130  LYS C N   1 
ATOM   4439 C  CA  . LYS C  1 130 ? 6.866   5.913   -14.082 1.00 9.94  ? 130  LYS C CA  1 
ATOM   4440 C  C   . LYS C  1 130 ? 7.294   5.573   -12.660 1.00 9.83  ? 130  LYS C C   1 
ATOM   4441 O  O   . LYS C  1 130 ? 6.992   6.299   -11.710 1.00 11.07 ? 130  LYS C O   1 
ATOM   4442 C  CB  . LYS C  1 130 ? 7.643   7.099   -14.660 1.00 13.20 ? 130  LYS C CB  1 
ATOM   4443 C  CG  . LYS C  1 130 ? 7.416   7.222   -16.176 1.00 17.74 ? 130  LYS C CG  1 
ATOM   4444 C  CD  . LYS C  1 130 ? 8.312   8.240   -16.832 1.00 24.21 ? 130  LYS C CD  1 
ATOM   4445 C  CE  . LYS C  1 130 ? 8.150   8.190   -18.351 1.00 31.69 ? 130  LYS C CE  1 
ATOM   4446 N  NZ  . LYS C  1 130 ? 8.639   6.911   -18.939 1.00 34.33 ? 130  LYS C NZ  1 
ATOM   4447 N  N   . ILE C  1 131 ? 7.952   4.433   -12.522 1.00 8.54  ? 131  ILE C N   1 
ATOM   4448 C  CA  . ILE C  1 131 ? 8.337   3.914   -11.213 1.00 8.60  ? 131  ILE C CA  1 
ATOM   4449 C  C   . ILE C  1 131 ? 9.849   3.858   -11.143 1.00 9.83  ? 131  ILE C C   1 
ATOM   4450 O  O   . ILE C  1 131 ? 10.511  3.292   -12.028 1.00 11.15 ? 131  ILE C O   1 
ATOM   4451 C  CB  . ILE C  1 131 ? 7.749   2.500   -10.954 1.00 7.97  ? 131  ILE C CB  1 
ATOM   4452 C  CG1 . ILE C  1 131 ? 6.216   2.534   -11.037 1.00 10.79 ? 131  ILE C CG1 1 
ATOM   4453 C  CG2 . ILE C  1 131 ? 8.221   1.972   -9.588  1.00 6.84  ? 131  ILE C CG2 1 
ATOM   4454 C  CD1 . ILE C  1 131 ? 5.566   1.128   -11.052 1.00 9.63  ? 131  ILE C CD1 1 
ATOM   4455 N  N   . VAL C  1 132 ? 10.414  4.464   -10.103 1.00 8.68  ? 132  VAL C N   1 
ATOM   4456 C  CA  . VAL C  1 132 ? 11.859  4.624   -10.025 1.00 8.40  ? 132  VAL C CA  1 
ATOM   4457 C  C   . VAL C  1 132 ? 12.393  4.177   -8.671  1.00 7.26  ? 132  VAL C C   1 
ATOM   4458 O  O   . VAL C  1 132 ? 11.829  4.528   -7.634  1.00 8.16  ? 132  VAL C O   1 
ATOM   4459 C  CB  . VAL C  1 132 ? 12.261  6.100   -10.258 1.00 7.41  ? 132  VAL C CB  1 
ATOM   4460 C  CG1 . VAL C  1 132 ? 13.751  6.303   -10.032 1.00 10.76 ? 132  VAL C CG1 1 
ATOM   4461 C  CG2 . VAL C  1 132 ? 11.869  6.538   -11.673 1.00 8.79  ? 132  VAL C CG2 1 
ATOM   4462 N  N   . LEU C  1 133 ? 13.466  3.382   -8.698  1.00 9.42  ? 133  LEU C N   1 
ATOM   4463 C  CA  . LEU C  1 133 ? 14.276  3.108   -7.517  1.00 7.76  ? 133  LEU C CA  1 
ATOM   4464 C  C   . LEU C  1 133 ? 15.567  3.903   -7.598  1.00 8.98  ? 133  LEU C C   1 
ATOM   4465 O  O   . LEU C  1 133 ? 16.129  4.069   -8.680  1.00 10.55 ? 133  LEU C O   1 
ATOM   4466 C  CB  . LEU C  1 133 ? 14.644  1.626   -7.445  1.00 7.93  ? 133  LEU C CB  1 
ATOM   4467 C  CG  . LEU C  1 133 ? 13.496  0.615   -7.501  1.00 6.24  ? 133  LEU C CG  1 
ATOM   4468 C  CD1 . LEU C  1 133 ? 14.084  -0.800  -7.375  1.00 8.07  ? 133  LEU C CD1 1 
ATOM   4469 C  CD2 . LEU C  1 133 ? 12.511  0.858   -6.389  1.00 10.90 ? 133  LEU C CD2 1 
ATOM   4470 N  N   . GLY C  1 134 ? 16.041  4.396   -6.457  1.00 7.04  ? 134  GLY C N   1 
ATOM   4471 C  CA  . GLY C  1 134 ? 17.343  5.038   -6.422  1.00 8.98  ? 134  GLY C CA  1 
ATOM   4472 C  C   . GLY C  1 134 ? 17.280  6.551   -6.401  1.00 8.99  ? 134  GLY C C   1 
ATOM   4473 O  O   . GLY C  1 134 ? 18.215  7.202   -5.951  1.00 9.81  ? 134  GLY C O   1 
ATOM   4474 N  N   . GLN C  1 135 ? 16.183  7.104   -6.912  1.00 8.54  ? 135  GLN C N   1 
ATOM   4475 C  CA  . GLN C  1 135 ? 15.990  8.552   -6.927  1.00 9.28  ? 135  GLN C CA  1 
ATOM   4476 C  C   . GLN C  1 135 ? 14.531  8.866   -6.642  1.00 11.45 ? 135  GLN C C   1 
ATOM   4477 O  O   . GLN C  1 135 ? 13.646  8.029   -6.834  1.00 11.14 ? 135  GLN C O   1 
ATOM   4478 C  CB  . GLN C  1 135 ? 16.371  9.133   -8.298  1.00 7.46  ? 135  GLN C CB  1 
ATOM   4479 C  CG  . GLN C  1 135 ? 17.815  8.890   -8.753  1.00 7.97  ? 135  GLN C CG  1 
ATOM   4480 C  CD  . GLN C  1 135 ? 18.864  9.665   -7.958  1.00 10.54 ? 135  GLN C CD  1 
ATOM   4481 O  OE1 . GLN C  1 135 ? 18.572  10.706  -7.372  1.00 12.85 ? 135  GLN C OE1 1 
ATOM   4482 N  NE2 . GLN C  1 135 ? 20.101  9.146   -7.933  1.00 8.99  ? 135  GLN C NE2 1 
ATOM   4483 N  N   . GLU C  1 136 ? 14.283  10.085  -6.180  1.00 8.76  ? 136  GLU C N   1 
ATOM   4484 C  CA  . GLU C  1 136 ? 12.939  10.554  -5.942  1.00 8.45  ? 136  GLU C CA  1 
ATOM   4485 C  C   . GLU C  1 136 ? 12.545  11.419  -7.137  1.00 8.90  ? 136  GLU C C   1 
ATOM   4486 O  O   . GLU C  1 136 ? 13.230  12.389  -7.454  1.00 9.96  ? 136  GLU C O   1 
ATOM   4487 C  CB  . GLU C  1 136 ? 12.908  11.402  -4.669  1.00 10.70 ? 136  GLU C CB  1 
ATOM   4488 C  CG  . GLU C  1 136 ? 11.562  11.459  -3.976  1.00 8.16  ? 136  GLU C CG  1 
ATOM   4489 C  CD  . GLU C  1 136 ? 10.593  12.429  -4.619  1.00 11.63 ? 136  GLU C CD  1 
ATOM   4490 O  OE1 . GLU C  1 136 ? 11.023  13.561  -4.928  1.00 9.84  ? 136  GLU C OE1 1 
ATOM   4491 O  OE2 . GLU C  1 136 ? 9.414   12.075  -4.814  1.00 10.29 ? 136  GLU C OE2 1 
ATOM   4492 N  N   . GLN C  1 137 ? 11.451  11.073  -7.807  1.00 7.34  ? 137  GLN C N   1 
ATOM   4493 C  CA  . GLN C  1 137 ? 11.028  11.875  -8.971  1.00 10.03 ? 137  GLN C CA  1 
ATOM   4494 C  C   . GLN C  1 137 ? 10.296  13.135  -8.543  1.00 10.00 ? 137  GLN C C   1 
ATOM   4495 O  O   . GLN C  1 137 ? 9.496   13.089  -7.621  1.00 10.08 ? 137  GLN C O   1 
ATOM   4496 C  CB  . GLN C  1 137 ? 10.050  11.097  -9.831  1.00 8.65  ? 137  GLN C CB  1 
ATOM   4497 C  CG  . GLN C  1 137 ? 10.581  9.849   -10.478 1.00 9.36  ? 137  GLN C CG  1 
ATOM   4498 C  CD  . GLN C  1 137 ? 9.444   9.079   -11.109 1.00 12.13 ? 137  GLN C CD  1 
ATOM   4499 O  OE1 . GLN C  1 137 ? 9.063   9.339   -12.256 1.00 13.09 ? 137  GLN C OE1 1 
ATOM   4500 N  NE2 . GLN C  1 137 ? 8.863   8.147   -10.350 1.00 9.51  ? 137  GLN C NE2 1 
ATOM   4501 N  N   . ASP C  1 138 ? 10.552  14.248  -9.240  1.00 11.25 ? 138  ASP C N   1 
ATOM   4502 C  CA  . ASP C  1 138 ? 9.701   15.437  -9.147  1.00 11.59 ? 138  ASP C CA  1 
ATOM   4503 C  C   . ASP C  1 138 ? 8.982   15.727  -10.467 1.00 16.05 ? 138  ASP C C   1 
ATOM   4504 O  O   . ASP C  1 138 ? 8.207   16.682  -10.567 1.00 16.87 ? 138  ASP C O   1 
ATOM   4505 C  CB  . ASP C  1 138 ? 10.505  16.666  -8.697  1.00 11.53 ? 138  ASP C CB  1 
ATOM   4506 C  CG  . ASP C  1 138 ? 10.742  16.689  -7.210  1.00 9.96  ? 138  ASP C CG  1 
ATOM   4507 O  OD1 . ASP C  1 138 ? 9.989   15.995  -6.487  1.00 12.94 ? 138  ASP C OD1 1 
ATOM   4508 O  OD2 . ASP C  1 138 ? 11.673  17.380  -6.754  1.00 12.23 ? 138  ASP C OD2 1 
ATOM   4509 N  N   . SER C  1 139 ? 9.229   14.896  -11.477 1.00 11.08 ? 139  SER C N   1 
ATOM   4510 C  CA  . SER C  1 139 ? 8.531   14.997  -12.756 1.00 14.05 ? 139  SER C CA  1 
ATOM   4511 C  C   . SER C  1 139 ? 8.092   13.612  -13.222 1.00 15.65 ? 139  SER C C   1 
ATOM   4512 O  O   . SER C  1 139 ? 8.256   12.629  -12.501 1.00 14.70 ? 139  SER C O   1 
ATOM   4513 C  CB  . SER C  1 139 ? 9.443   15.622  -13.816 1.00 14.95 ? 139  SER C CB  1 
ATOM   4514 O  OG  . SER C  1 139 ? 10.468  14.714  -14.198 1.00 16.17 ? 139  SER C OG  1 
ATOM   4515 N  N   . TYR C  1 140 ? 7.542   13.524  -14.428 1.00 13.23 ? 140  TYR C N   1 
ATOM   4516 C  CA  . TYR C  1 140 ? 7.121   12.224  -14.936 1.00 15.57 ? 140  TYR C CA  1 
ATOM   4517 C  C   . TYR C  1 140 ? 8.355   11.511  -15.464 1.00 14.37 ? 140  TYR C C   1 
ATOM   4518 O  O   . TYR C  1 140 ? 8.673   11.570  -16.660 1.00 16.28 ? 140  TYR C O   1 
ATOM   4519 C  CB  . TYR C  1 140 ? 6.036   12.371  -16.007 1.00 14.35 ? 140  TYR C CB  1 
ATOM   4520 C  CG  . TYR C  1 140 ? 5.443   11.063  -16.502 1.00 13.04 ? 140  TYR C CG  1 
ATOM   4521 C  CD1 . TYR C  1 140 ? 4.848   10.161  -15.620 1.00 13.93 ? 140  TYR C CD1 1 
ATOM   4522 C  CD2 . TYR C  1 140 ? 5.453   10.744  -17.856 1.00 17.12 ? 140  TYR C CD2 1 
ATOM   4523 C  CE1 . TYR C  1 140 ? 4.284   8.974   -16.074 1.00 11.27 ? 140  TYR C CE1 1 
ATOM   4524 C  CE2 . TYR C  1 140 ? 4.900   9.559   -18.319 1.00 20.35 ? 140  TYR C CE2 1 
ATOM   4525 C  CZ  . TYR C  1 140 ? 4.319   8.678   -17.426 1.00 19.39 ? 140  TYR C CZ  1 
ATOM   4526 O  OH  . TYR C  1 140 ? 3.775   7.500   -17.895 1.00 18.00 ? 140  TYR C OH  1 
ATOM   4527 N  N   . GLY C  1 141 ? 9.085   10.883  -14.548 1.00 13.37 ? 141  GLY C N   1 
ATOM   4528 C  CA  . GLY C  1 141 ? 10.263  10.120  -14.917 1.00 13.83 ? 141  GLY C CA  1 
ATOM   4529 C  C   . GLY C  1 141 ? 11.595  10.734  -14.536 1.00 12.78 ? 141  GLY C C   1 
ATOM   4530 O  O   . GLY C  1 141 ? 12.631  10.096  -14.719 1.00 18.98 ? 141  GLY C O   1 
ATOM   4531 N  N   . GLY C  1 142 ? 11.593  11.960  -14.014 1.00 14.25 ? 142  GLY C N   1 
ATOM   4532 C  CA  . GLY C  1 142 ? 12.844  12.666  -13.784 1.00 11.24 ? 142  GLY C CA  1 
ATOM   4533 C  C   . GLY C  1 142 ? 12.804  13.724  -12.698 1.00 14.31 ? 142  GLY C C   1 
ATOM   4534 O  O   . GLY C  1 142 ? 12.054  13.592  -11.732 1.00 13.45 ? 142  GLY C O   1 
ATOM   4535 N  N   . LYS C  1 143 ? 13.609  14.773  -12.872 1.00 15.79 ? 143  LYS C N   1 
ATOM   4536 C  CA  . LYS C  1 143 ? 13.766  15.835  -11.883 1.00 13.89 ? 143  LYS C CA  1 
ATOM   4537 C  C   . LYS C  1 143 ? 14.169  15.269  -10.526 1.00 12.84 ? 143  LYS C C   1 
ATOM   4538 O  O   . LYS C  1 143 ? 13.498  15.480  -9.511  1.00 13.97 ? 143  LYS C O   1 
ATOM   4539 C  CB  . LYS C  1 143 ? 12.501  16.706  -11.781 1.00 17.41 ? 143  LYS C CB  1 
ATOM   4540 C  CG  . LYS C  1 143 ? 12.359  17.704  -12.917 1.00 30.02 ? 143  LYS C CG  1 
ATOM   4541 C  CD  . LYS C  1 143 ? 11.160  18.619  -12.712 1.00 35.25 ? 143  LYS C CD  1 
ATOM   4542 C  CE  . LYS C  1 143 ? 11.221  19.348  -11.373 1.00 41.62 ? 143  LYS C CE  1 
ATOM   4543 N  NZ  . LYS C  1 143 ? 12.185  20.484  -11.369 1.00 46.82 ? 143  LYS C NZ  1 
ATOM   4544 N  N   . PHE C  1 144 ? 15.290  14.552  -10.530 1.00 12.69 ? 144  PHE C N   1 
ATOM   4545 C  CA  . PHE C  1 144 ? 15.814  13.905  -9.338  1.00 9.39  ? 144  PHE C CA  1 
ATOM   4546 C  C   . PHE C  1 144 ? 16.524  14.915  -8.435  1.00 14.71 ? 144  PHE C C   1 
ATOM   4547 O  O   . PHE C  1 144 ? 16.844  16.036  -8.862  1.00 14.81 ? 144  PHE C O   1 
ATOM   4548 C  CB  . PHE C  1 144 ? 16.791  12.789  -9.741  1.00 10.84 ? 144  PHE C CB  1 
ATOM   4549 C  CG  . PHE C  1 144 ? 16.188  11.742  -10.640 1.00 11.47 ? 144  PHE C CG  1 
ATOM   4550 C  CD1 . PHE C  1 144 ? 14.878  11.325  -10.465 1.00 12.81 ? 144  PHE C CD1 1 
ATOM   4551 C  CD2 . PHE C  1 144 ? 16.951  11.142  -11.639 1.00 14.06 ? 144  PHE C CD2 1 
ATOM   4552 C  CE1 . PHE C  1 144 ? 14.327  10.345  -11.275 1.00 15.60 ? 144  PHE C CE1 1 
ATOM   4553 C  CE2 . PHE C  1 144 ? 16.398  10.164  -12.460 1.00 12.13 ? 144  PHE C CE2 1 
ATOM   4554 C  CZ  . PHE C  1 144 ? 15.092  9.765   -12.272 1.00 13.45 ? 144  PHE C CZ  1 
ATOM   4555 N  N   . ASP C  1 145 ? 16.792  14.500  -7.198  1.00 10.99 ? 145  ASP C N   1 
ATOM   4556 C  CA  . ASP C  1 145 ? 17.415  15.353  -6.186  1.00 13.58 ? 145  ASP C CA  1 
ATOM   4557 C  C   . ASP C  1 145 ? 18.462  14.526  -5.436  1.00 14.11 ? 145  ASP C C   1 
ATOM   4558 O  O   . ASP C  1 145 ? 18.135  13.544  -4.765  1.00 12.86 ? 145  ASP C O   1 
ATOM   4559 C  CB  . ASP C  1 145 ? 16.337  15.871  -5.224  1.00 11.17 ? 145  ASP C CB  1 
ATOM   4560 C  CG  . ASP C  1 145 ? 16.885  16.797  -4.143  1.00 17.87 ? 145  ASP C CG  1 
ATOM   4561 O  OD1 . ASP C  1 145 ? 18.116  16.854  -3.932  1.00 16.89 ? 145  ASP C OD1 1 
ATOM   4562 O  OD2 . ASP C  1 145 ? 16.057  17.471  -3.490  1.00 18.14 ? 145  ASP C OD2 1 
ATOM   4563 N  N   . ARG C  1 146 ? 19.727  14.905  -5.577  1.00 12.90 ? 146  ARG C N   1 
ATOM   4564 C  CA  . ARG C  1 146 ? 20.826  14.166  -4.965  1.00 14.36 ? 146  ARG C CA  1 
ATOM   4565 C  C   . ARG C  1 146 ? 20.607  13.941  -3.463  1.00 12.64 ? 146  ARG C C   1 
ATOM   4566 O  O   . ARG C  1 146 ? 20.965  12.894  -2.918  1.00 14.30 ? 146  ARG C O   1 
ATOM   4567 C  CB  . ARG C  1 146 ? 22.134  14.923  -5.216  1.00 20.75 ? 146  ARG C CB  1 
ATOM   4568 C  CG  . ARG C  1 146 ? 23.348  14.316  -4.576  1.00 23.61 ? 146  ARG C CG  1 
ATOM   4569 C  CD  . ARG C  1 146 ? 24.564  15.210  -4.786  1.00 29.69 ? 146  ARG C CD  1 
ATOM   4570 N  NE  . ARG C  1 146 ? 25.761  14.619  -4.203  1.00 39.57 ? 146  ARG C NE  1 
ATOM   4571 C  CZ  . ARG C  1 146 ? 26.665  13.933  -4.893  1.00 33.87 ? 146  ARG C CZ  1 
ATOM   4572 N  NH1 . ARG C  1 146 ? 26.512  13.755  -6.201  1.00 32.61 ? 146  ARG C NH1 1 
ATOM   4573 N  NH2 . ARG C  1 146 ? 27.724  13.428  -4.274  1.00 37.14 ? 146  ARG C NH2 1 
ATOM   4574 N  N   . SER C  1 147 ? 19.988  14.911  -2.799  1.00 14.03 ? 147  SER C N   1 
ATOM   4575 C  CA  . SER C  1 147 ? 19.794  14.834  -1.356  1.00 12.91 ? 147  SER C CA  1 
ATOM   4576 C  C   . SER C  1 147 ? 18.677  13.872  -0.946  1.00 10.37 ? 147  SER C C   1 
ATOM   4577 O  O   . SER C  1 147 ? 18.446  13.666  0.250   1.00 12.83 ? 147  SER C O   1 
ATOM   4578 C  CB  . SER C  1 147 ? 19.520  16.231  -0.779  1.00 13.97 ? 147  SER C CB  1 
ATOM   4579 O  OG  . SER C  1 147 ? 18.254  16.723  -1.197  1.00 21.59 ? 147  SER C OG  1 
ATOM   4580 N  N   . GLN C  1 148 ? 17.997  13.285  -1.933  1.00 11.14 ? 148  GLN C N   1 
ATOM   4581 C  CA  . GLN C  1 148 ? 16.929  12.309  -1.682  1.00 12.30 ? 148  GLN C CA  1 
ATOM   4582 C  C   . GLN C  1 148 ? 17.273  10.963  -2.305  1.00 8.46  ? 148  GLN C C   1 
ATOM   4583 O  O   . GLN C  1 148 ? 16.462  10.024  -2.263  1.00 10.89 ? 148  GLN C O   1 
ATOM   4584 C  CB  . GLN C  1 148 ? 15.600  12.799  -2.260  1.00 11.85 ? 148  GLN C CB  1 
ATOM   4585 C  CG  . GLN C  1 148 ? 15.107  14.095  -1.636  1.00 11.02 ? 148  GLN C CG  1 
ATOM   4586 C  CD  . GLN C  1 148 ? 13.818  14.588  -2.276  1.00 11.54 ? 148  GLN C CD  1 
ATOM   4587 O  OE1 . GLN C  1 148 ? 13.713  14.666  -3.495  1.00 11.11 ? 148  GLN C OE1 1 
ATOM   4588 N  NE2 . GLN C  1 148 ? 12.841  14.933  -1.451  1.00 19.17 ? 148  GLN C NE2 1 
ATOM   4589 N  N   . SER C  1 149 ? 18.464  10.877  -2.894  1.00 8.57  ? 149  SER C N   1 
ATOM   4590 C  CA  . SER C  1 149 ? 18.897  9.644   -3.568  1.00 9.63  ? 149  SER C CA  1 
ATOM   4591 C  C   . SER C  1 149 ? 19.073  8.496   -2.577  1.00 12.79 ? 149  SER C C   1 
ATOM   4592 O  O   . SER C  1 149 ? 19.455  8.708   -1.424  1.00 9.46  ? 149  SER C O   1 
ATOM   4593 C  CB  . SER C  1 149 ? 20.186  9.866   -4.371  1.00 10.00 ? 149  SER C CB  1 
ATOM   4594 O  OG  . SER C  1 149 ? 21.285  10.204  -3.537  1.00 11.27 ? 149  SER C OG  1 
ATOM   4595 N  N   . PHE C  1 150 ? 18.791  7.278   -3.029  1.00 8.15  ? 150  PHE C N   1 
ATOM   4596 C  CA  . PHE C  1 150 ? 19.002  6.107   -2.189  1.00 7.76  ? 150  PHE C CA  1 
ATOM   4597 C  C   . PHE C  1 150 ? 20.377  5.522   -2.501  1.00 9.14  ? 150  PHE C C   1 
ATOM   4598 O  O   . PHE C  1 150 ? 20.692  5.235   -3.655  1.00 11.11 ? 150  PHE C O   1 
ATOM   4599 C  CB  . PHE C  1 150 ? 17.908  5.057   -2.430  1.00 7.57  ? 150  PHE C CB  1 
ATOM   4600 C  CG  . PHE C  1 150 ? 18.155  3.761   -1.708  1.00 8.95  ? 150  PHE C CG  1 
ATOM   4601 C  CD1 . PHE C  1 150 ? 17.772  3.607   -0.386  1.00 11.22 ? 150  PHE C CD1 1 
ATOM   4602 C  CD2 . PHE C  1 150 ? 18.789  2.707   -2.348  1.00 9.11  ? 150  PHE C CD2 1 
ATOM   4603 C  CE1 . PHE C  1 150 ? 18.012  2.421   0.289   1.00 7.35  ? 150  PHE C CE1 1 
ATOM   4604 C  CE2 . PHE C  1 150 ? 19.036  1.512   -1.675  1.00 8.11  ? 150  PHE C CE2 1 
ATOM   4605 C  CZ  . PHE C  1 150 ? 18.638  1.368   -0.359  1.00 11.09 ? 150  PHE C CZ  1 
ATOM   4606 N  N   . VAL C  1 151 ? 21.197  5.375   -1.466  1.00 7.96  ? 151  VAL C N   1 
ATOM   4607 C  CA  . VAL C  1 151 ? 22.495  4.735   -1.573  1.00 9.45  ? 151  VAL C CA  1 
ATOM   4608 C  C   . VAL C  1 151 ? 22.434  3.473   -0.734  1.00 10.51 ? 151  VAL C C   1 
ATOM   4609 O  O   . VAL C  1 151 ? 22.073  3.511   0.448   1.00 10.13 ? 151  VAL C O   1 
ATOM   4610 C  CB  . VAL C  1 151 ? 23.630  5.636   -1.055  1.00 8.26  ? 151  VAL C CB  1 
ATOM   4611 C  CG1 . VAL C  1 151 ? 24.983  4.961   -1.291  1.00 8.97  ? 151  VAL C CG1 1 
ATOM   4612 C  CG2 . VAL C  1 151 ? 23.584  6.979   -1.758  1.00 10.06 ? 151  VAL C CG2 1 
ATOM   4613 N  N   . GLY C  1 152 ? 22.770  2.349   -1.344  1.00 8.55  ? 152  GLY C N   1 
ATOM   4614 C  CA  . GLY C  1 152 ? 22.633  1.076   -0.664  1.00 7.80  ? 152  GLY C CA  1 
ATOM   4615 C  C   . GLY C  1 152 ? 22.018  0.035   -1.576  1.00 10.23 ? 152  GLY C C   1 
ATOM   4616 O  O   . GLY C  1 152 ? 22.133  0.122   -2.795  1.00 8.97  ? 152  GLY C O   1 
ATOM   4617 N  N   . GLU C  1 153 ? 21.344  -0.940  -0.977  1.00 7.16  ? 153  GLU C N   1 
ATOM   4618 C  CA  . GLU C  1 153 ? 20.921  -2.123  -1.705  1.00 7.75  ? 153  GLU C CA  1 
ATOM   4619 C  C   . GLU C  1 153 ? 19.430  -2.371  -1.546  1.00 6.41  ? 153  GLU C C   1 
ATOM   4620 O  O   . GLU C  1 153 ? 18.880  -2.226  -0.448  1.00 6.76  ? 153  GLU C O   1 
ATOM   4621 C  CB  . GLU C  1 153 ? 21.707  -3.333  -1.172  1.00 7.07  ? 153  GLU C CB  1 
ATOM   4622 C  CG  . GLU C  1 153 ? 23.216  -3.109  -1.240  1.00 10.61 ? 153  GLU C CG  1 
ATOM   4623 C  CD  . GLU C  1 153 ? 24.010  -4.298  -0.743  1.00 12.30 ? 153  GLU C CD  1 
ATOM   4624 O  OE1 . GLU C  1 153 ? 23.623  -5.444  -1.068  1.00 12.13 ? 153  GLU C OE1 1 
ATOM   4625 O  OE2 . GLU C  1 153 ? 25.022  -4.092  -0.033  1.00 11.75 ? 153  GLU C OE2 1 
ATOM   4626 N  N   . ILE C  1 154 ? 18.773  -2.755  -2.646  1.00 6.99  ? 154  ILE C N   1 
ATOM   4627 C  CA  . ILE C  1 154 ? 17.358  -3.118  -2.592  1.00 7.05  ? 154  ILE C CA  1 
ATOM   4628 C  C   . ILE C  1 154 ? 17.156  -4.453  -3.283  1.00 9.99  ? 154  ILE C C   1 
ATOM   4629 O  O   . ILE C  1 154 ? 17.725  -4.695  -4.346  1.00 10.61 ? 154  ILE C O   1 
ATOM   4630 C  CB  . ILE C  1 154 ? 16.471  -2.078  -3.315  1.00 10.15 ? 154  ILE C CB  1 
ATOM   4631 C  CG1 . ILE C  1 154 ? 16.481  -0.759  -2.553  1.00 11.66 ? 154  ILE C CG1 1 
ATOM   4632 C  CG2 . ILE C  1 154 ? 15.028  -2.597  -3.466  1.00 11.16 ? 154  ILE C CG2 1 
ATOM   4633 C  CD1 . ILE C  1 154 ? 15.739  0.379   -3.285  1.00 17.25 ? 154  ILE C CD1 1 
ATOM   4634 N  N   . GLY C  1 155 ? 16.352  -5.314  -2.675  1.00 10.51 ? 155  GLY C N   1 
ATOM   4635 C  CA  . GLY C  1 155 ? 16.029  -6.591  -3.295  1.00 10.20 ? 155  GLY C CA  1 
ATOM   4636 C  C   . GLY C  1 155 ? 14.643  -7.072  -2.916  1.00 11.26 ? 155  GLY C C   1 
ATOM   4637 O  O   . GLY C  1 155 ? 13.917  -6.395  -2.177  1.00 8.45  ? 155  GLY C O   1 
ATOM   4638 N  N   . ASP C  1 156 ? 14.269  -8.241  -3.440  1.00 7.82  ? 156  ASP C N   1 
ATOM   4639 C  CA  . ASP C  1 156 ? 13.017  -8.893  -3.073  1.00 8.49  ? 156  ASP C CA  1 
ATOM   4640 C  C   . ASP C  1 156 ? 11.813  -7.961  -3.126  1.00 7.35  ? 156  ASP C C   1 
ATOM   4641 O  O   . ASP C  1 156 ? 10.991  -7.950  -2.214  1.00 8.03  ? 156  ASP C O   1 
ATOM   4642 C  CB  . ASP C  1 156 ? 13.126  -9.508  -1.675  1.00 11.63 ? 156  ASP C CB  1 
ATOM   4643 C  CG  . ASP C  1 156 ? 13.981  -10.753 -1.659  1.00 19.00 ? 156  ASP C CG  1 
ATOM   4644 O  OD1 . ASP C  1 156 ? 14.289  -11.272 -2.752  1.00 21.63 ? 156  ASP C OD1 1 
ATOM   4645 O  OD2 . ASP C  1 156 ? 14.344  -11.209 -0.557  1.00 16.20 ? 156  ASP C OD2 1 
ATOM   4646 N  N   . LEU C  1 157 ? 11.697  -7.217  -4.217  1.00 7.56  ? 157  LEU C N   1 
ATOM   4647 C  CA  . LEU C  1 157 ? 10.601  -6.268  -4.381  1.00 9.29  ? 157  LEU C CA  1 
ATOM   4648 C  C   . LEU C  1 157 ? 9.410   -6.880  -5.123  1.00 9.38  ? 157  LEU C C   1 
ATOM   4649 O  O   . LEU C  1 157 ? 9.555   -7.414  -6.226  1.00 8.31  ? 157  LEU C O   1 
ATOM   4650 C  CB  . LEU C  1 157 ? 11.105  -5.008  -5.094  1.00 7.85  ? 157  LEU C CB  1 
ATOM   4651 C  CG  . LEU C  1 157 ? 10.067  -3.877  -5.159  1.00 8.86  ? 157  LEU C CG  1 
ATOM   4652 C  CD1 . LEU C  1 157 ? 10.800  -2.535  -5.189  1.00 9.73  ? 157  LEU C CD1 1 
ATOM   4653 C  CD2 . LEU C  1 157 ? 9.144   -4.016  -6.368  1.00 9.80  ? 157  LEU C CD2 1 
ATOM   4654 N  N   . TYR C  1 158 ? 8.238   -6.804  -4.496  1.00 8.05  ? 158  TYR C N   1 
ATOM   4655 C  CA  . TYR C  1 158 ? 6.996   -7.316  -5.073  1.00 8.52  ? 158  TYR C CA  1 
ATOM   4656 C  C   . TYR C  1 158 ? 5.872   -6.329  -4.847  1.00 9.04  ? 158  TYR C C   1 
ATOM   4657 O  O   . TYR C  1 158 ? 5.835   -5.645  -3.821  1.00 8.50  ? 158  TYR C O   1 
ATOM   4658 C  CB  . TYR C  1 158 ? 6.609   -8.641  -4.416  1.00 7.20  ? 158  TYR C CB  1 
ATOM   4659 C  CG  . TYR C  1 158 ? 7.637   -9.706  -4.598  1.00 8.88  ? 158  TYR C CG  1 
ATOM   4660 C  CD1 . TYR C  1 158 ? 7.529   -10.624 -5.642  1.00 8.48  ? 158  TYR C CD1 1 
ATOM   4661 C  CD2 . TYR C  1 158 ? 8.721   -9.805  -3.735  1.00 8.28  ? 158  TYR C CD2 1 
ATOM   4662 C  CE1 . TYR C  1 158 ? 8.490   -11.608 -5.824  1.00 10.88 ? 158  TYR C CE1 1 
ATOM   4663 C  CE2 . TYR C  1 158 ? 9.680   -10.790 -3.905  1.00 8.41  ? 158  TYR C CE2 1 
ATOM   4664 C  CZ  . TYR C  1 158 ? 9.556   -11.683 -4.953  1.00 11.57 ? 158  TYR C CZ  1 
ATOM   4665 O  OH  . TYR C  1 158 ? 10.508  -12.660 -5.114  1.00 13.48 ? 158  TYR C OH  1 
ATOM   4666 N  N   . MET C  1 159 ? 4.937   -6.275  -5.791  1.00 5.94  ? 159  MET C N   1 
ATOM   4667 C  CA  . MET C  1 159 ? 3.780   -5.398  -5.663  1.00 8.41  ? 159  MET C CA  1 
ATOM   4668 C  C   . MET C  1 159 ? 2.527   -6.120  -6.152  1.00 10.35 ? 159  MET C C   1 
ATOM   4669 O  O   . MET C  1 159 ? 2.522   -6.721  -7.234  1.00 7.98  ? 159  MET C O   1 
ATOM   4670 C  CB  . MET C  1 159 ? 4.000   -4.091  -6.424  1.00 8.80  ? 159  MET C CB  1 
ATOM   4671 C  CG  . MET C  1 159 ? 2.908   -3.038  -6.145  1.00 7.26  ? 159  MET C CG  1 
ATOM   4672 S  SD  . MET C  1 159 ? 3.320   -1.459  -6.918  1.00 11.86 ? 159  MET C SD  1 
ATOM   4673 C  CE  . MET C  1 159 ? 1.870   -0.501  -6.466  1.00 11.72 ? 159  MET C CE  1 
ATOM   4674 N  N   . TRP C  1 160 ? 1.490   -6.070  -5.321  1.00 8.59  ? 160  TRP C N   1 
ATOM   4675 C  CA  . TRP C  1 160 ? 0.219   -6.738  -5.562  1.00 11.14 ? 160  TRP C CA  1 
ATOM   4676 C  C   . TRP C  1 160 ? -0.886  -5.694  -5.694  1.00 12.03 ? 160  TRP C C   1 
ATOM   4677 O  O   . TRP C  1 160 ? -0.819  -4.635  -5.056  1.00 9.29  ? 160  TRP C O   1 
ATOM   4678 C  CB  . TRP C  1 160 ? -0.134  -7.607  -4.353  1.00 9.05  ? 160  TRP C CB  1 
ATOM   4679 C  CG  . TRP C  1 160 ? 0.773   -8.762  -4.045  1.00 12.27 ? 160  TRP C CG  1 
ATOM   4680 C  CD1 . TRP C  1 160 ? 0.556   -10.073 -4.373  1.00 10.12 ? 160  TRP C CD1 1 
ATOM   4681 C  CD2 . TRP C  1 160 ? 1.991   -8.735  -3.280  1.00 7.39  ? 160  TRP C CD2 1 
ATOM   4682 N  NE1 . TRP C  1 160 ? 1.575   -10.859 -3.881  1.00 10.01 ? 160  TRP C NE1 1 
ATOM   4683 C  CE2 . TRP C  1 160 ? 2.467   -10.063 -3.207  1.00 9.02  ? 160  TRP C CE2 1 
ATOM   4684 C  CE3 . TRP C  1 160 ? 2.732   -7.715  -2.659  1.00 10.44 ? 160  TRP C CE3 1 
ATOM   4685 C  CZ2 . TRP C  1 160 ? 3.654   -10.400 -2.544  1.00 10.85 ? 160  TRP C CZ2 1 
ATOM   4686 C  CZ3 . TRP C  1 160 ? 3.909   -8.049  -1.995  1.00 11.90 ? 160  TRP C CZ3 1 
ATOM   4687 C  CH2 . TRP C  1 160 ? 4.367   -9.384  -1.951  1.00 8.54  ? 160  TRP C CH2 1 
ATOM   4688 N  N   . ASP C  1 161 ? -1.930  -5.998  -6.470  1.00 9.05  ? 161  ASP C N   1 
ATOM   4689 C  CA  . ASP C  1 161 ? -3.074  -5.084  -6.591  1.00 9.92  ? 161  ASP C CA  1 
ATOM   4690 C  C   . ASP C  1 161 ? -4.157  -5.355  -5.536  1.00 14.69 ? 161  ASP C C   1 
ATOM   4691 O  O   . ASP C  1 161 ? -5.338  -5.078  -5.753  1.00 13.10 ? 161  ASP C O   1 
ATOM   4692 C  CB  . ASP C  1 161 ? -3.666  -5.119  -8.007  1.00 14.12 ? 161  ASP C CB  1 
ATOM   4693 C  CG  . ASP C  1 161 ? -4.467  -6.395  -8.294  1.00 18.89 ? 161  ASP C CG  1 
ATOM   4694 O  OD1 . ASP C  1 161 ? -4.351  -7.399  -7.550  1.00 14.44 ? 161  ASP C OD1 1 
ATOM   4695 O  OD2 . ASP C  1 161 ? -5.222  -6.385  -9.292  1.00 20.31 ? 161  ASP C OD2 1 
ATOM   4696 N  N   . SER C  1 162 ? -3.742  -5.872  -4.384  1.00 9.97  ? 162  SER C N   1 
ATOM   4697 C  CA  . SER C  1 162 ? -4.659  -6.112  -3.286  1.00 11.95 ? 162  SER C CA  1 
ATOM   4698 C  C   . SER C  1 162 ? -3.939  -5.871  -1.970  1.00 8.29  ? 162  SER C C   1 
ATOM   4699 O  O   . SER C  1 162 ? -2.718  -5.706  -1.945  1.00 10.96 ? 162  SER C O   1 
ATOM   4700 C  CB  . SER C  1 162 ? -5.185  -7.550  -3.329  1.00 13.89 ? 162  SER C CB  1 
ATOM   4701 O  OG  . SER C  1 162 ? -4.122  -8.478  -3.164  1.00 14.84 ? 162  SER C OG  1 
ATOM   4702 N  N   . VAL C  1 163 ? -4.708  -5.835  -0.885  1.00 10.55 ? 163  VAL C N   1 
ATOM   4703 C  CA  . VAL C  1 163 ? -4.144  -5.662  0.449   1.00 10.67 ? 163  VAL C CA  1 
ATOM   4704 C  C   . VAL C  1 163 ? -3.825  -7.027  1.038   1.00 11.60 ? 163  VAL C C   1 
ATOM   4705 O  O   . VAL C  1 163 ? -4.737  -7.828  1.299   1.00 12.46 ? 163  VAL C O   1 
ATOM   4706 C  CB  . VAL C  1 163 ? -5.116  -4.925  1.380   1.00 12.31 ? 163  VAL C CB  1 
ATOM   4707 C  CG1 . VAL C  1 163 ? -4.564  -4.875  2.806   1.00 10.55 ? 163  VAL C CG1 1 
ATOM   4708 C  CG2 . VAL C  1 163 ? -5.365  -3.518  0.863   1.00 12.20 ? 163  VAL C CG2 1 
ATOM   4709 N  N   . LEU C  1 164 ? -2.538  -7.304  1.240   1.00 10.38 ? 164  LEU C N   1 
ATOM   4710 C  CA  . LEU C  1 164 ? -2.151  -8.592  1.805   1.00 12.42 ? 164  LEU C CA  1 
ATOM   4711 C  C   . LEU C  1 164 ? -2.573  -8.722  3.260   1.00 13.49 ? 164  LEU C C   1 
ATOM   4712 O  O   . LEU C  1 164 ? -2.364  -7.807  4.060   1.00 11.58 ? 164  LEU C O   1 
ATOM   4713 C  CB  . LEU C  1 164 ? -0.639  -8.803  1.716   1.00 9.93  ? 164  LEU C CB  1 
ATOM   4714 C  CG  . LEU C  1 164 ? 0.002   -8.931  0.343   1.00 13.72 ? 164  LEU C CG  1 
ATOM   4715 C  CD1 . LEU C  1 164 ? 1.455   -9.353  0.528   1.00 13.06 ? 164  LEU C CD1 1 
ATOM   4716 C  CD2 . LEU C  1 164 ? -0.736  -9.918  -0.546  1.00 17.49 ? 164  LEU C CD2 1 
ATOM   4717 N  N   . PRO C  1 165 ? -3.137  -9.881  3.621   1.00 12.88 ? 165  PRO C N   1 
ATOM   4718 C  CA  . PRO C  1 165 ? -3.391  -10.191 5.033   1.00 12.37 ? 165  PRO C CA  1 
ATOM   4719 C  C   . PRO C  1 165 ? -2.089  -10.493 5.760   1.00 9.93  ? 165  PRO C C   1 
ATOM   4720 O  O   . PRO C  1 165 ? -1.087  -10.807 5.125   1.00 9.28  ? 165  PRO C O   1 
ATOM   4721 C  CB  . PRO C  1 165 ? -4.254  -11.454 4.967   1.00 12.08 ? 165  PRO C CB  1 
ATOM   4722 C  CG  . PRO C  1 165 ? -3.872  -12.100 3.675   1.00 14.39 ? 165  PRO C CG  1 
ATOM   4723 C  CD  . PRO C  1 165 ? -3.494  -10.993 2.723   1.00 10.31 ? 165  PRO C CD  1 
ATOM   4724 N  N   . PRO C  1 166 ? -2.098  -10.410 7.096   1.00 10.46 ? 166  PRO C N   1 
ATOM   4725 C  CA  . PRO C  1 166 ? -0.867  -10.560 7.876   1.00 10.20 ? 166  PRO C CA  1 
ATOM   4726 C  C   . PRO C  1 166 ? -0.044  -11.793 7.539   1.00 11.07 ? 166  PRO C C   1 
ATOM   4727 O  O   . PRO C  1 166 ? 1.172   -11.688 7.425   1.00 9.04  ? 166  PRO C O   1 
ATOM   4728 C  CB  . PRO C  1 166 ? -1.390  -10.637 9.311   1.00 10.88 ? 166  PRO C CB  1 
ATOM   4729 C  CG  . PRO C  1 166 ? -2.577  -9.730  9.278   1.00 12.65 ? 166  PRO C CG  1 
ATOM   4730 C  CD  . PRO C  1 166 ? -3.226  -9.957  7.934   1.00 13.38 ? 166  PRO C CD  1 
ATOM   4731 N  N   . GLU C  1 167 ? -0.677  -12.949 7.384   1.00 9.07  ? 167  GLU C N   1 
ATOM   4732 C  CA  . GLU C  1 167 ? 0.117   -14.149 7.139   1.00 10.31 ? 167  GLU C CA  1 
ATOM   4733 C  C   . GLU C  1 167 ? 0.794   -14.158 5.768   1.00 10.44 ? 167  GLU C C   1 
ATOM   4734 O  O   . GLU C  1 167 ? 1.804   -14.854 5.586   1.00 9.02  ? 167  GLU C O   1 
ATOM   4735 C  CB  . GLU C  1 167 ? -0.703  -15.427 7.370   1.00 9.08  ? 167  GLU C CB  1 
ATOM   4736 C  CG  . GLU C  1 167 ? -1.166  -15.553 8.824   1.00 10.37 ? 167  GLU C CG  1 
ATOM   4737 C  CD  . GLU C  1 167 ? -1.993  -16.806 9.072   1.00 17.48 ? 167  GLU C CD  1 
ATOM   4738 O  OE1 . GLU C  1 167 ? -2.971  -16.743 9.853   1.00 17.75 ? 167  GLU C OE1 1 
ATOM   4739 O  OE2 . GLU C  1 167 ? -1.655  -17.854 8.487   1.00 13.68 ? 167  GLU C OE2 1 
ATOM   4740 N  N   . ASN C  1 168 ? 0.269   -13.380 4.817   1.00 8.88  ? 168  ASN C N   1 
ATOM   4741 C  CA  . ASN C  1 168 ? 0.943   -13.254 3.514   1.00 8.08  ? 168  ASN C CA  1 
ATOM   4742 C  C   . ASN C  1 168 ? 2.101   -12.270 3.548   1.00 9.13  ? 168  ASN C C   1 
ATOM   4743 O  O   . ASN C  1 168 ? 3.085   -12.430 2.832   1.00 11.10 ? 168  ASN C O   1 
ATOM   4744 C  CB  . ASN C  1 168 ? -0.047  -12.945 2.383   1.00 7.97  ? 168  ASN C CB  1 
ATOM   4745 C  CG  . ASN C  1 168 ? -0.980  -14.125 2.109   1.00 9.56  ? 168  ASN C CG  1 
ATOM   4746 O  OD1 . ASN C  1 168 ? -0.805  -15.188 2.697   1.00 12.90 ? 168  ASN C OD1 1 
ATOM   4747 N  ND2 . ASN C  1 168 ? -1.968  -13.941 1.237   1.00 11.09 ? 168  ASN C ND2 1 
ATOM   4748 N  N   A ILE C  1 169 ? 1.989   -11.255 4.396   0.51 10.46 ? 169  ILE C N   1 
ATOM   4749 N  N   B ILE C  1 169 ? 1.966   -11.244 4.386   0.49 10.45 ? 169  ILE C N   1 
ATOM   4750 C  CA  A ILE C  1 169 ? 3.108   -10.356 4.629   0.51 9.35  ? 169  ILE C CA  1 
ATOM   4751 C  CA  B ILE C  1 169 ? 3.069   -10.338 4.670   0.49 9.34  ? 169  ILE C CA  1 
ATOM   4752 C  C   A ILE C  1 169 ? 4.238   -11.134 5.294   0.51 9.43  ? 169  ILE C C   1 
ATOM   4753 C  C   B ILE C  1 169 ? 4.214   -11.145 5.274   0.49 9.44  ? 169  ILE C C   1 
ATOM   4754 O  O   A ILE C  1 169 ? 5.403   -10.984 4.942   0.51 9.28  ? 169  ILE C O   1 
ATOM   4755 O  O   B ILE C  1 169 ? 5.363   -11.025 4.861   0.49 9.27  ? 169  ILE C O   1 
ATOM   4756 C  CB  A ILE C  1 169 ? 2.693   -9.187  5.514   0.51 8.49  ? 169  ILE C CB  1 
ATOM   4757 C  CB  B ILE C  1 169 ? 2.652   -9.242  5.666   0.49 8.47  ? 169  ILE C CB  1 
ATOM   4758 C  CG1 A ILE C  1 169 ? 1.584   -8.391  4.824   0.51 11.62 ? 169  ILE C CG1 1 
ATOM   4759 C  CG1 B ILE C  1 169 ? 1.644   -8.281  5.023   0.49 11.66 ? 169  ILE C CG1 1 
ATOM   4760 C  CG2 A ILE C  1 169 ? 3.896   -8.307  5.832   0.51 8.86  ? 169  ILE C CG2 1 
ATOM   4761 C  CG2 B ILE C  1 169 ? 3.879   -8.496  6.180   0.49 8.19  ? 169  ILE C CG2 1 
ATOM   4762 C  CD1 A ILE C  1 169 ? 0.911   -7.405  5.716   0.51 8.92  ? 169  ILE C CD1 1 
ATOM   4763 C  CD1 B ILE C  1 169 ? 2.205   -7.494  3.854   0.49 9.78  ? 169  ILE C CD1 1 
ATOM   4764 N  N   . LEU C  1 170 ? 3.886   -11.985 6.250   1.00 10.73 ? 170  LEU C N   1 
ATOM   4765 C  CA  . LEU C  1 170 ? 4.885   -12.797 6.913   1.00 10.01 ? 170  LEU C CA  1 
ATOM   4766 C  C   . LEU C  1 170 ? 5.583   -13.731 5.934   1.00 9.60  ? 170  LEU C C   1 
ATOM   4767 O  O   . LEU C  1 170 ? 6.797   -13.912 6.002   1.00 10.33 ? 170  LEU C O   1 
ATOM   4768 C  CB  . LEU C  1 170 ? 4.282   -13.562 8.091   1.00 10.78 ? 170  LEU C CB  1 
ATOM   4769 C  CG  . LEU C  1 170 ? 3.946   -12.661 9.284   1.00 18.43 ? 170  LEU C CG  1 
ATOM   4770 C  CD1 . LEU C  1 170 ? 3.315   -13.458 10.421  1.00 26.08 ? 170  LEU C CD1 1 
ATOM   4771 C  CD2 . LEU C  1 170 ? 5.188   -11.934 9.768   1.00 24.98 ? 170  LEU C CD2 1 
ATOM   4772 N  N   . SER C  1 171 ? 4.819   -14.306 5.010   1.00 10.73 ? 171  SER C N   1 
ATOM   4773 C  CA  . SER C  1 171 ? 5.424   -15.182 4.018   1.00 9.95  ? 171  SER C CA  1 
ATOM   4774 C  C   . SER C  1 171 ? 6.446   -14.408 3.172   1.00 10.87 ? 171  SER C C   1 
ATOM   4775 O  O   . SER C  1 171 ? 7.541   -14.903 2.932   1.00 11.70 ? 171  SER C O   1 
ATOM   4776 C  CB  . SER C  1 171 ? 4.352   -15.853 3.146   1.00 11.10 ? 171  SER C CB  1 
ATOM   4777 O  OG  . SER C  1 171 ? 4.744   -17.182 2.813   1.00 12.13 ? 171  SER C OG  1 
ATOM   4778 N  N   . ALA C  1 172 ? 6.111   -13.186 2.753   1.00 9.02  ? 172  ALA C N   1 
ATOM   4779 C  CA  . ALA C  1 172 ? 7.072   -12.359 2.013   1.00 8.68  ? 172  ALA C CA  1 
ATOM   4780 C  C   . ALA C  1 172 ? 8.328   -12.065 2.848   1.00 8.63  ? 172  ALA C C   1 
ATOM   4781 O  O   . ALA C  1 172 ? 9.454   -12.167 2.358   1.00 9.36  ? 172  ALA C O   1 
ATOM   4782 C  CB  . ALA C  1 172 ? 6.405   -11.040 1.541   1.00 8.26  ? 172  ALA C CB  1 
ATOM   4783 N  N   . TYR C  1 173 ? 8.124   -11.708 4.114   1.00 9.45  ? 173  TYR C N   1 
ATOM   4784 C  CA  . TYR C  1 173 ? 9.227   -11.395 5.016   1.00 9.07  ? 173  TYR C CA  1 
ATOM   4785 C  C   . TYR C  1 173 ? 10.164  -12.595 5.124   1.00 12.67 ? 173  TYR C C   1 
ATOM   4786 O  O   . TYR C  1 173 ? 11.389  -12.448 5.168   1.00 11.65 ? 173  TYR C O   1 
ATOM   4787 C  CB  . TYR C  1 173 ? 8.677   -11.013 6.393   1.00 9.92  ? 173  TYR C CB  1 
ATOM   4788 C  CG  . TYR C  1 173 ? 9.732   -10.901 7.479   1.00 8.33  ? 173  TYR C CG  1 
ATOM   4789 C  CD1 . TYR C  1 173 ? 10.803  -10.034 7.341   1.00 11.04 ? 173  TYR C CD1 1 
ATOM   4790 C  CD2 . TYR C  1 173 ? 9.632   -11.635 8.645   1.00 14.11 ? 173  TYR C CD2 1 
ATOM   4791 C  CE1 . TYR C  1 173 ? 11.763  -9.919  8.328   1.00 14.30 ? 173  TYR C CE1 1 
ATOM   4792 C  CE2 . TYR C  1 173 ? 10.587  -11.525 9.643   1.00 16.86 ? 173  TYR C CE2 1 
ATOM   4793 C  CZ  . TYR C  1 173 ? 11.647  -10.667 9.477   1.00 17.61 ? 173  TYR C CZ  1 
ATOM   4794 O  OH  . TYR C  1 173 ? 12.603  -10.556 10.462  1.00 19.20 ? 173  TYR C OH  1 
ATOM   4795 N  N   . GLN C  1 174 ? 9.581   -13.785 5.141   1.00 11.62 ? 174  GLN C N   1 
ATOM   4796 C  CA  . GLN C  1 174 ? 10.376  -15.009 5.257   1.00 13.99 ? 174  GLN C CA  1 
ATOM   4797 C  C   . GLN C  1 174 ? 11.034  -15.441 3.953   1.00 15.81 ? 174  GLN C C   1 
ATOM   4798 O  O   . GLN C  1 174 ? 11.746  -16.447 3.928   1.00 18.42 ? 174  GLN C O   1 
ATOM   4799 C  CB  . GLN C  1 174 ? 9.506   -16.148 5.773   1.00 12.20 ? 174  GLN C CB  1 
ATOM   4800 C  CG  . GLN C  1 174 ? 9.061   -15.939 7.192   1.00 16.27 ? 174  GLN C CG  1 
ATOM   4801 C  CD  . GLN C  1 174 ? 7.808   -16.699 7.503   1.00 25.81 ? 174  GLN C CD  1 
ATOM   4802 O  OE1 . GLN C  1 174 ? 7.322   -17.466 6.674   1.00 22.80 ? 174  GLN C OE1 1 
ATOM   4803 N  NE2 . GLN C  1 174 ? 7.260   -16.486 8.698   1.00 29.08 ? 174  GLN C NE2 1 
ATOM   4804 N  N   . GLY C  1 175 ? 10.775  -14.711 2.874   1.00 10.53 ? 175  GLY C N   1 
ATOM   4805 C  CA  . GLY C  1 175 ? 11.394  -15.002 1.591   1.00 14.07 ? 175  GLY C CA  1 
ATOM   4806 C  C   . GLY C  1 175 ? 10.571  -15.886 0.674   1.00 15.66 ? 175  GLY C C   1 
ATOM   4807 O  O   . GLY C  1 175 ? 11.088  -16.421 -0.314  1.00 14.69 ? 175  GLY C O   1 
ATOM   4808 N  N   . THR C  1 176 ? 9.292   -16.047 1.000   1.00 11.72 ? 176  THR C N   1 
ATOM   4809 C  CA  . THR C  1 176 ? 8.377   -16.829 0.168   1.00 14.45 ? 176  THR C CA  1 
ATOM   4810 C  C   . THR C  1 176 ? 7.102   -16.042 -0.143  1.00 12.40 ? 176  THR C C   1 
ATOM   4811 O  O   . THR C  1 176 ? 6.016   -16.395 0.298   1.00 9.54  ? 176  THR C O   1 
ATOM   4812 C  CB  . THR C  1 176 ? 8.030   -18.187 0.834   1.00 10.92 ? 176  THR C CB  1 
ATOM   4813 O  OG1 . THR C  1 176 ? 7.444   -17.965 2.127   1.00 12.23 ? 176  THR C OG1 1 
ATOM   4814 C  CG2 . THR C  1 176 ? 9.289   -19.009 1.005   1.00 13.76 ? 176  THR C CG2 1 
ATOM   4815 N  N   . PRO C  1 177 ? 7.234   -14.958 -0.921  1.00 12.02 ? 177  PRO C N   1 
ATOM   4816 C  CA  . PRO C  1 177 ? 6.093   -14.099 -1.245  1.00 12.34 ? 177  PRO C CA  1 
ATOM   4817 C  C   . PRO C  1 177 ? 5.053   -14.864 -2.065  1.00 11.55 ? 177  PRO C C   1 
ATOM   4818 O  O   . PRO C  1 177 ? 5.432   -15.704 -2.886  1.00 13.25 ? 177  PRO C O   1 
ATOM   4819 C  CB  . PRO C  1 177 ? 6.727   -13.013 -2.119  1.00 13.24 ? 177  PRO C CB  1 
ATOM   4820 C  CG  . PRO C  1 177 ? 7.951   -13.697 -2.698  1.00 12.41 ? 177  PRO C CG  1 
ATOM   4821 C  CD  . PRO C  1 177 ? 8.475   -14.469 -1.546  1.00 14.51 ? 177  PRO C CD  1 
ATOM   4822 N  N   . LEU C  1 178 ? 3.778   -14.570 -1.835  1.00 11.05 ? 178  LEU C N   1 
ATOM   4823 C  CA  . LEU C  1 178 ? 2.698   -15.098 -2.656  1.00 11.17 ? 178  LEU C CA  1 
ATOM   4824 C  C   . LEU C  1 178 ? 2.763   -14.420 -4.021  1.00 15.49 ? 178  LEU C C   1 
ATOM   4825 O  O   . LEU C  1 178 ? 3.354   -13.337 -4.161  1.00 11.45 ? 178  LEU C O   1 
ATOM   4826 C  CB  . LEU C  1 178 ? 1.349   -14.835 -1.984  1.00 14.51 ? 178  LEU C CB  1 
ATOM   4827 C  CG  . LEU C  1 178 ? 0.918   -15.721 -0.802  1.00 14.14 ? 178  LEU C CG  1 
ATOM   4828 C  CD1 . LEU C  1 178 ? 0.706   -17.166 -1.247  1.00 20.82 ? 178  LEU C CD1 1 
ATOM   4829 C  CD2 . LEU C  1 178 ? 1.896   -15.656 0.369   1.00 11.47 ? 178  LEU C CD2 1 
ATOM   4830 N  N   . PRO C  1 179 ? 2.187   -15.065 -5.045  1.00 16.22 ? 179  PRO C N   1 
ATOM   4831 C  CA  . PRO C  1 179 ? 2.265   -14.544 -6.415  1.00 15.10 ? 179  PRO C CA  1 
ATOM   4832 C  C   . PRO C  1 179 ? 1.865   -13.078 -6.498  1.00 9.58  ? 179  PRO C C   1 
ATOM   4833 O  O   . PRO C  1 179 ? 0.802   -12.709 -6.000  1.00 12.02 ? 179  PRO C O   1 
ATOM   4834 C  CB  . PRO C  1 179 ? 1.243   -15.408 -7.163  1.00 17.45 ? 179  PRO C CB  1 
ATOM   4835 C  CG  . PRO C  1 179 ? 1.298   -16.711 -6.439  1.00 17.99 ? 179  PRO C CG  1 
ATOM   4836 C  CD  . PRO C  1 179 ? 1.435   -16.335 -4.981  1.00 13.33 ? 179  PRO C CD  1 
ATOM   4837 N  N   . ALA C  1 180 ? 2.708   -12.274 -7.147  1.00 12.12 ? 180  ALA C N   1 
ATOM   4838 C  CA  . ALA C  1 180 ? 2.486   -10.829 -7.253  1.00 9.60  ? 180  ALA C CA  1 
ATOM   4839 C  C   . ALA C  1 180 ? 2.202   -10.414 -8.692  1.00 11.82 ? 180  ALA C C   1 
ATOM   4840 O  O   . ALA C  1 180 ? 2.890   -10.851 -9.611  1.00 16.57 ? 180  ALA C O   1 
ATOM   4841 C  CB  . ALA C  1 180 ? 3.699   -10.067 -6.701  1.00 10.75 ? 180  ALA C CB  1 
ATOM   4842 N  N   . ASN C  1 181 ? 1.216   -9.540  -8.883  1.00 10.18 ? 181  ASN C N   1 
ATOM   4843 C  CA  . ASN C  1 181 ? 0.722   -9.240  -10.223 1.00 10.48 ? 181  ASN C CA  1 
ATOM   4844 C  C   . ASN C  1 181 ? 1.004   -7.839  -10.775 1.00 16.09 ? 181  ASN C C   1 
ATOM   4845 O  O   . ASN C  1 181 ? 0.648   -7.554  -11.919 1.00 14.34 ? 181  ASN C O   1 
ATOM   4846 C  CB  . ASN C  1 181 ? -0.782  -9.577  -10.344 1.00 11.70 ? 181  ASN C CB  1 
ATOM   4847 C  CG  . ASN C  1 181 ? -1.644  -8.804  -9.358  1.00 18.27 ? 181  ASN C CG  1 
ATOM   4848 O  OD1 . ASN C  1 181 ? -1.145  -7.983  -8.596  1.00 12.95 ? 181  ASN C OD1 1 
ATOM   4849 N  ND2 . ASN C  1 181 ? -2.952  -9.081  -9.361  1.00 17.75 ? 181  ASN C ND2 1 
ATOM   4850 N  N   . ILE C  1 182 ? 1.628   -6.963  -9.984  1.00 9.94  ? 182  ILE C N   1 
ATOM   4851 C  CA  . ILE C  1 182 ? 2.010   -5.649  -10.500 1.00 9.10  ? 182  ILE C CA  1 
ATOM   4852 C  C   . ILE C  1 182 ? 3.522   -5.584  -10.740 1.00 8.56  ? 182  ILE C C   1 
ATOM   4853 O  O   . ILE C  1 182 ? 3.961   -5.208  -11.821 1.00 9.88  ? 182  ILE C O   1 
ATOM   4854 C  CB  . ILE C  1 182 ? 1.546   -4.475  -9.577  1.00 7.85  ? 182  ILE C CB  1 
ATOM   4855 C  CG1 . ILE C  1 182 ? 0.015   -4.463  -9.464  1.00 12.54 ? 182  ILE C CG1 1 
ATOM   4856 C  CG2 . ILE C  1 182 ? 2.070   -3.143  -10.106 1.00 11.36 ? 182  ILE C CG2 1 
ATOM   4857 C  CD1 . ILE C  1 182 ? -0.525  -3.438  -8.456  1.00 13.85 ? 182  ILE C CD1 1 
ATOM   4858 N  N   . LEU C  1 183 ? 4.313   -5.938  -9.729  1.00 7.21  ? 183  LEU C N   1 
ATOM   4859 C  CA  . LEU C  1 183 ? 5.766   -6.046  -9.881  1.00 8.18  ? 183  LEU C CA  1 
ATOM   4860 C  C   . LEU C  1 183 ? 6.214   -7.335  -9.209  1.00 7.73  ? 183  LEU C C   1 
ATOM   4861 O  O   . LEU C  1 183 ? 5.690   -7.703  -8.151  1.00 8.04  ? 183  LEU C O   1 
ATOM   4862 C  CB  . LEU C  1 183 ? 6.516   -4.845  -9.269  1.00 8.80  ? 183  LEU C CB  1 
ATOM   4863 C  CG  . LEU C  1 183 ? 6.304   -3.469  -9.909  1.00 5.85  ? 183  LEU C CG  1 
ATOM   4864 C  CD1 . LEU C  1 183 ? 6.883   -2.373  -9.008  1.00 10.68 ? 183  LEU C CD1 1 
ATOM   4865 C  CD2 . LEU C  1 183 ? 6.917   -3.413  -11.300 1.00 10.55 ? 183  LEU C CD2 1 
ATOM   4866 N  N   . ASP C  1 184 ? 7.182   -8.013  -9.824  1.00 9.46  ? 184  ASP C N   1 
ATOM   4867 C  CA  . ASP C  1 184 ? 7.591   -9.347  -9.381  1.00 11.11 ? 184  ASP C CA  1 
ATOM   4868 C  C   . ASP C  1 184 ? 9.103   -9.490  -9.541  1.00 9.90  ? 184  ASP C C   1 
ATOM   4869 O  O   . ASP C  1 184 ? 9.607   -9.492  -10.660 1.00 9.62  ? 184  ASP C O   1 
ATOM   4870 C  CB  . ASP C  1 184 ? 6.841   -10.387 -10.228 1.00 11.99 ? 184  ASP C CB  1 
ATOM   4871 C  CG  . ASP C  1 184 ? 7.032   -11.820 -9.745  1.00 17.89 ? 184  ASP C CG  1 
ATOM   4872 O  OD1 . ASP C  1 184 ? 7.980   -12.105 -8.984  1.00 10.89 ? 184  ASP C OD1 1 
ATOM   4873 O  OD2 . ASP C  1 184 ? 6.212   -12.678 -10.157 1.00 19.52 ? 184  ASP C OD2 1 
ATOM   4874 N  N   . TRP C  1 185 ? 9.826   -9.576  -8.419  1.00 7.75  ? 185  TRP C N   1 
ATOM   4875 C  CA  . TRP C  1 185 ? 11.288  -9.676  -8.427  1.00 6.93  ? 185  TRP C CA  1 
ATOM   4876 C  C   . TRP C  1 185 ? 11.758  -10.871 -9.239  1.00 11.81 ? 185  TRP C C   1 
ATOM   4877 O  O   . TRP C  1 185 ? 12.868  -10.862 -9.767  1.00 8.86  ? 185  TRP C O   1 
ATOM   4878 C  CB  . TRP C  1 185 ? 11.811  -9.821  -6.991  1.00 9.09  ? 185  TRP C CB  1 
ATOM   4879 C  CG  . TRP C  1 185 ? 13.237  -9.433  -6.794  1.00 10.43 ? 185  TRP C CG  1 
ATOM   4880 C  CD1 . TRP C  1 185 ? 14.267  -10.247 -6.404  1.00 9.07  ? 185  TRP C CD1 1 
ATOM   4881 C  CD2 . TRP C  1 185 ? 13.798  -8.123  -6.948  1.00 7.66  ? 185  TRP C CD2 1 
ATOM   4882 N  NE1 . TRP C  1 185 ? 15.435  -9.518  -6.304  1.00 9.85  ? 185  TRP C NE1 1 
ATOM   4883 C  CE2 . TRP C  1 185 ? 15.176  -8.218  -6.646  1.00 9.81  ? 185  TRP C CE2 1 
ATOM   4884 C  CE3 . TRP C  1 185 ? 13.272  -6.881  -7.325  1.00 8.10  ? 185  TRP C CE3 1 
ATOM   4885 C  CZ2 . TRP C  1 185 ? 16.033  -7.116  -6.705  1.00 9.22  ? 185  TRP C CZ2 1 
ATOM   4886 C  CZ3 . TRP C  1 185 ? 14.134  -5.778  -7.370  1.00 10.39 ? 185  TRP C CZ3 1 
ATOM   4887 C  CH2 . TRP C  1 185 ? 15.492  -5.910  -7.071  1.00 10.38 ? 185  TRP C CH2 1 
ATOM   4888 N  N   . GLN C  1 186 ? 10.913  -11.899 -9.320  1.00 9.03  ? 186  GLN C N   1 
ATOM   4889 C  CA  . GLN C  1 186 ? 11.265  -13.116 -10.064 1.00 9.29  ? 186  GLN C CA  1 
ATOM   4890 C  C   . GLN C  1 186 ? 10.970  -13.043 -11.571 1.00 11.33 ? 186  GLN C C   1 
ATOM   4891 O  O   . GLN C  1 186 ? 11.320  -13.955 -12.318 1.00 11.08 ? 186  GLN C O   1 
ATOM   4892 C  CB  . GLN C  1 186 ? 10.595  -14.327 -9.421  1.00 11.79 ? 186  GLN C CB  1 
ATOM   4893 C  CG  . GLN C  1 186 ? 11.041  -14.483 -7.973  1.00 16.83 ? 186  GLN C CG  1 
ATOM   4894 C  CD  . GLN C  1 186 ? 10.368  -15.627 -7.266  1.00 24.73 ? 186  GLN C CD  1 
ATOM   4895 O  OE1 . GLN C  1 186 ? 10.308  -16.742 -7.782  1.00 24.29 ? 186  GLN C OE1 1 
ATOM   4896 N  NE2 . GLN C  1 186 ? 9.873   -15.366 -6.066  1.00 22.53 ? 186  GLN C NE2 1 
ATOM   4897 N  N   . ALA C  1 187 ? 10.339  -11.958 -12.013 1.00 10.79 ? 187  ALA C N   1 
ATOM   4898 C  CA  . ALA C  1 187 ? 10.149  -11.699 -13.441 1.00 9.66  ? 187  ALA C CA  1 
ATOM   4899 C  C   . ALA C  1 187 ? 9.991   -10.199 -13.628 1.00 9.03  ? 187  ALA C C   1 
ATOM   4900 O  O   . ALA C  1 187 ? 8.891   -9.689  -13.874 1.00 11.51 ? 187  ALA C O   1 
ATOM   4901 C  CB  . ALA C  1 187 ? 8.931   -12.453 -13.983 1.00 11.77 ? 187  ALA C CB  1 
ATOM   4902 N  N   . LEU C  1 188 ? 11.104  -9.496  -13.456 1.00 9.49  ? 188  LEU C N   1 
ATOM   4903 C  CA  . LEU C  1 188 ? 11.092  -8.047  -13.354 1.00 12.20 ? 188  LEU C CA  1 
ATOM   4904 C  C   . LEU C  1 188 ? 11.546  -7.421  -14.655 1.00 9.01  ? 188  LEU C C   1 
ATOM   4905 O  O   . LEU C  1 188 ? 12.565  -7.817  -15.229 1.00 10.12 ? 188  LEU C O   1 
ATOM   4906 C  CB  . LEU C  1 188 ? 12.010  -7.599  -12.209 1.00 7.66  ? 188  LEU C CB  1 
ATOM   4907 C  CG  . LEU C  1 188 ? 11.843  -6.143  -11.768 1.00 8.72  ? 188  LEU C CG  1 
ATOM   4908 C  CD1 . LEU C  1 188 ? 10.496  -5.991  -11.089 1.00 12.96 ? 188  LEU C CD1 1 
ATOM   4909 C  CD2 . LEU C  1 188 ? 12.980  -5.735  -10.842 1.00 10.55 ? 188  LEU C CD2 1 
ATOM   4910 N  N   . ASN C  1 189 ? 10.764  -6.453  -15.125 1.00 9.68  ? 189  ASN C N   1 
ATOM   4911 C  CA  . ASN C  1 189 ? 11.107  -5.705  -16.322 1.00 12.38 ? 189  ASN C CA  1 
ATOM   4912 C  C   . ASN C  1 189 ? 11.662  -4.368  -15.867 1.00 11.01 ? 189  ASN C C   1 
ATOM   4913 O  O   . ASN C  1 189 ? 10.941  -3.560  -15.269 1.00 12.68 ? 189  ASN C O   1 
ATOM   4914 C  CB  . ASN C  1 189 ? 9.850   -5.478  -17.157 1.00 11.23 ? 189  ASN C CB  1 
ATOM   4915 C  CG  . ASN C  1 189 ? 10.159  -5.023  -18.566 1.00 21.70 ? 189  ASN C CG  1 
ATOM   4916 O  OD1 . ASN C  1 189 ? 11.315  -5.018  -18.990 1.00 21.59 ? 189  ASN C OD1 1 
ATOM   4917 N  ND2 . ASN C  1 189 ? 9.122   -4.640  -19.303 1.00 19.29 ? 189  ASN C ND2 1 
ATOM   4918 N  N   . TYR C  1 190 ? 12.939  -4.131  -16.124 1.00 12.14 ? 190  TYR C N   1 
ATOM   4919 C  CA  . TYR C  1 190 ? 13.575  -2.928  -15.587 1.00 12.71 ? 190  TYR C CA  1 
ATOM   4920 C  C   . TYR C  1 190 ? 14.607  -2.336  -16.536 1.00 14.76 ? 190  TYR C C   1 
ATOM   4921 O  O   . TYR C  1 190 ? 15.026  -2.975  -17.515 1.00 13.08 ? 190  TYR C O   1 
ATOM   4922 C  CB  . TYR C  1 190 ? 14.233  -3.237  -14.237 1.00 7.90  ? 190  TYR C CB  1 
ATOM   4923 C  CG  . TYR C  1 190 ? 15.370  -4.211  -14.354 1.00 13.40 ? 190  TYR C CG  1 
ATOM   4924 C  CD1 . TYR C  1 190 ? 16.652  -3.778  -14.636 1.00 11.93 ? 190  TYR C CD1 1 
ATOM   4925 C  CD2 . TYR C  1 190 ? 15.153  -5.578  -14.205 1.00 15.29 ? 190  TYR C CD2 1 
ATOM   4926 C  CE1 . TYR C  1 190 ? 17.698  -4.674  -14.766 1.00 17.38 ? 190  TYR C CE1 1 
ATOM   4927 C  CE2 . TYR C  1 190 ? 16.190  -6.476  -14.329 1.00 15.47 ? 190  TYR C CE2 1 
ATOM   4928 C  CZ  . TYR C  1 190 ? 17.456  -6.024  -14.612 1.00 21.75 ? 190  TYR C CZ  1 
ATOM   4929 O  OH  . TYR C  1 190 ? 18.496  -6.926  -14.738 1.00 26.56 ? 190  TYR C OH  1 
ATOM   4930 N  N   . GLU C  1 191 ? 15.024  -1.114  -16.219 1.00 10.45 ? 191  GLU C N   1 
ATOM   4931 C  CA  . GLU C  1 191 ? 16.059  -0.412  -16.963 1.00 12.09 ? 191  GLU C CA  1 
ATOM   4932 C  C   . GLU C  1 191 ? 17.041  0.206   -15.983 1.00 12.19 ? 191  GLU C C   1 
ATOM   4933 O  O   . GLU C  1 191 ? 16.661  1.061   -15.182 1.00 14.55 ? 191  GLU C O   1 
ATOM   4934 C  CB  . GLU C  1 191 ? 15.437  0.719   -17.788 1.00 13.15 ? 191  GLU C CB  1 
ATOM   4935 C  CG  . GLU C  1 191 ? 14.523  0.256   -18.903 1.00 19.02 ? 191  GLU C CG  1 
ATOM   4936 C  CD  . GLU C  1 191 ? 13.731  1.396   -19.532 1.00 32.56 ? 191  GLU C CD  1 
ATOM   4937 O  OE1 . GLU C  1 191 ? 13.626  2.476   -18.908 1.00 25.62 ? 191  GLU C OE1 1 
ATOM   4938 O  OE2 . GLU C  1 191 ? 13.203  1.206   -20.650 1.00 33.28 ? 191  GLU C OE2 1 
ATOM   4939 N  N   . ILE C  1 192 ? 18.298  -0.217  -16.043 1.00 11.12 ? 192  ILE C N   1 
ATOM   4940 C  CA  . ILE C  1 192 ? 19.341  0.430   -15.250 1.00 9.54  ? 192  ILE C CA  1 
ATOM   4941 C  C   . ILE C  1 192 ? 19.863  1.675   -15.965 1.00 10.17 ? 192  ILE C C   1 
ATOM   4942 O  O   . ILE C  1 192 ? 20.184  1.631   -17.156 1.00 13.67 ? 192  ILE C O   1 
ATOM   4943 C  CB  . ILE C  1 192 ? 20.508  -0.512  -14.977 1.00 10.31 ? 192  ILE C CB  1 
ATOM   4944 C  CG1 . ILE C  1 192 ? 20.091  -1.561  -13.938 1.00 12.92 ? 192  ILE C CG1 1 
ATOM   4945 C  CG2 . ILE C  1 192 ? 21.711  0.279   -14.487 1.00 12.19 ? 192  ILE C CG2 1 
ATOM   4946 C  CD1 . ILE C  1 192 ? 21.146  -2.640  -13.654 1.00 14.12 ? 192  ILE C CD1 1 
ATOM   4947 N  N   . ARG C  1 193 ? 19.954  2.778   -15.232 1.00 12.87 ? 193  ARG C N   1 
ATOM   4948 C  CA  . ARG C  1 193 ? 20.508  4.013   -15.767 1.00 11.30 ? 193  ARG C CA  1 
ATOM   4949 C  C   . ARG C  1 193 ? 21.589  4.497   -14.823 1.00 11.62 ? 193  ARG C C   1 
ATOM   4950 O  O   . ARG C  1 193 ? 21.414  4.479   -13.600 1.00 12.43 ? 193  ARG C O   1 
ATOM   4951 C  CB  . ARG C  1 193 ? 19.413  5.072   -15.906 1.00 12.47 ? 193  ARG C CB  1 
ATOM   4952 C  CG  . ARG C  1 193 ? 18.335  4.696   -16.917 1.00 17.48 ? 193  ARG C CG  1 
ATOM   4953 C  CD  . ARG C  1 193 ? 18.930  4.691   -18.314 1.00 17.30 ? 193  ARG C CD  1 
ATOM   4954 N  NE  . ARG C  1 193 ? 17.942  4.394   -19.351 1.00 29.45 ? 193  ARG C NE  1 
ATOM   4955 C  CZ  . ARG C  1 193 ? 17.757  3.188   -19.880 1.00 26.95 ? 193  ARG C CZ  1 
ATOM   4956 N  NH1 . ARG C  1 193 ? 18.479  2.156   -19.458 1.00 26.07 ? 193  ARG C NH1 1 
ATOM   4957 N  NH2 . ARG C  1 193 ? 16.844  3.007   -20.826 1.00 25.47 ? 193  ARG C NH2 1 
ATOM   4958 N  N   . GLY C  1 194 ? 22.724  4.909   -15.376 1.00 14.36 ? 194  GLY C N   1 
ATOM   4959 C  CA  . GLY C  1 194 ? 23.823  5.343   -14.532 1.00 13.04 ? 194  GLY C CA  1 
ATOM   4960 C  C   . GLY C  1 194 ? 24.482  4.176   -13.815 1.00 14.02 ? 194  GLY C C   1 
ATOM   4961 O  O   . GLY C  1 194 ? 24.485  3.056   -14.324 1.00 14.83 ? 194  GLY C O   1 
ATOM   4962 N  N   . TYR C  1 195 ? 25.008  4.436   -12.619 1.00 12.89 ? 195  TYR C N   1 
ATOM   4963 C  CA  . TYR C  1 195 ? 25.804  3.452   -11.864 1.00 10.41 ? 195  TYR C CA  1 
ATOM   4964 C  C   . TYR C  1 195 ? 24.935  2.631   -10.916 1.00 9.43  ? 195  TYR C C   1 
ATOM   4965 O  O   . TYR C  1 195 ? 24.729  3.000   -9.751  1.00 10.57 ? 195  TYR C O   1 
ATOM   4966 C  CB  . TYR C  1 195 ? 26.892  4.183   -11.072 1.00 10.62 ? 195  TYR C CB  1 
ATOM   4967 C  CG  . TYR C  1 195 ? 27.971  3.325   -10.419 1.00 9.53  ? 195  TYR C CG  1 
ATOM   4968 C  CD1 . TYR C  1 195 ? 28.358  2.100   -10.959 1.00 11.82 ? 195  TYR C CD1 1 
ATOM   4969 C  CD2 . TYR C  1 195 ? 28.652  3.785   -9.297  1.00 10.38 ? 195  TYR C CD2 1 
ATOM   4970 C  CE1 . TYR C  1 195 ? 29.375  1.340   -10.355 1.00 12.28 ? 195  TYR C CE1 1 
ATOM   4971 C  CE2 . TYR C  1 195 ? 29.662  3.044   -8.701  1.00 11.49 ? 195  TYR C CE2 1 
ATOM   4972 C  CZ  . TYR C  1 195 ? 30.021  1.831   -9.232  1.00 11.02 ? 195  TYR C CZ  1 
ATOM   4973 O  OH  . TYR C  1 195 ? 31.037  1.108   -8.633  1.00 11.44 ? 195  TYR C OH  1 
ATOM   4974 N  N   . VAL C  1 196 ? 24.415  1.521   -11.421 1.00 8.68  ? 196  VAL C N   1 
ATOM   4975 C  CA  . VAL C  1 196 ? 23.682  0.571   -10.584 1.00 10.08 ? 196  VAL C CA  1 
ATOM   4976 C  C   . VAL C  1 196 ? 24.215  -0.825  -10.926 1.00 11.48 ? 196  VAL C C   1 
ATOM   4977 O  O   . VAL C  1 196 ? 24.335  -1.182  -12.104 1.00 12.45 ? 196  VAL C O   1 
ATOM   4978 C  CB  . VAL C  1 196 ? 22.164  0.624   -10.824 1.00 10.14 ? 196  VAL C CB  1 
ATOM   4979 C  CG1 . VAL C  1 196 ? 21.435  -0.274  -9.819  1.00 10.52 ? 196  VAL C CG1 1 
ATOM   4980 C  CG2 . VAL C  1 196 ? 21.644  2.078   -10.752 1.00 11.14 ? 196  VAL C CG2 1 
ATOM   4981 N  N   . ILE C  1 197 ? 24.570  -1.594  -9.902  1.00 9.58  ? 197  ILE C N   1 
ATOM   4982 C  CA  . ILE C  1 197 ? 25.202  -2.898  -10.117 1.00 9.19  ? 197  ILE C CA  1 
ATOM   4983 C  C   . ILE C  1 197 ? 24.349  -3.997  -9.518  1.00 10.56 ? 197  ILE C C   1 
ATOM   4984 O  O   . ILE C  1 197 ? 23.888  -3.878  -8.385  1.00 9.42  ? 197  ILE C O   1 
ATOM   4985 C  CB  . ILE C  1 197 ? 26.593  -2.966  -9.460  1.00 12.45 ? 197  ILE C CB  1 
ATOM   4986 C  CG1 . ILE C  1 197 ? 27.507  -1.860  -10.002 1.00 11.41 ? 197  ILE C CG1 1 
ATOM   4987 C  CG2 . ILE C  1 197 ? 27.212  -4.350  -9.668  1.00 9.31  ? 197  ILE C CG2 1 
ATOM   4988 C  CD1 . ILE C  1 197 ? 27.918  -2.032  -11.471 1.00 12.07 ? 197  ILE C CD1 1 
ATOM   4989 N  N   . ILE C  1 198 ? 24.120  -5.063  -10.276 1.00 7.64  ? 198  ILE C N   1 
ATOM   4990 C  CA  . ILE C  1 198 ? 23.422  -6.220  -9.716  1.00 7.23  ? 198  ILE C CA  1 
ATOM   4991 C  C   . ILE C  1 198 ? 24.409  -7.163  -9.041  1.00 7.03  ? 198  ILE C C   1 
ATOM   4992 O  O   . ILE C  1 198 ? 25.415  -7.562  -9.640  1.00 11.11 ? 198  ILE C O   1 
ATOM   4993 C  CB  . ILE C  1 198 ? 22.625  -6.988  -10.784 1.00 9.90  ? 198  ILE C CB  1 
ATOM   4994 C  CG1 . ILE C  1 198 ? 21.577  -6.064  -11.416 1.00 10.44 ? 198  ILE C CG1 1 
ATOM   4995 C  CG2 . ILE C  1 198 ? 21.950  -8.211  -10.161 1.00 9.90  ? 198  ILE C CG2 1 
ATOM   4996 C  CD1 . ILE C  1 198 ? 20.818  -6.678  -12.582 1.00 13.82 ? 198  ILE C CD1 1 
ATOM   4997 N  N   . LYS C  1 199 ? 24.129  -7.505  -7.785  1.00 8.77  ? 199  LYS C N   1 
ATOM   4998 C  CA  . LYS C  1 199 ? 24.994  -8.387  -7.006  1.00 12.41 ? 199  LYS C CA  1 
ATOM   4999 C  C   . LYS C  1 199 ? 24.153  -9.404  -6.251  1.00 9.49  ? 199  LYS C C   1 
ATOM   5000 O  O   . LYS C  1 199 ? 22.960  -9.203  -6.032  1.00 8.89  ? 199  LYS C O   1 
ATOM   5001 C  CB  . LYS C  1 199 ? 25.812  -7.581  -5.986  1.00 12.28 ? 199  LYS C CB  1 
ATOM   5002 C  CG  . LYS C  1 199 ? 26.987  -6.825  -6.572  1.00 10.60 ? 199  LYS C CG  1 
ATOM   5003 C  CD  . LYS C  1 199 ? 28.099  -7.796  -6.933  1.00 14.96 ? 199  LYS C CD  1 
ATOM   5004 C  CE  . LYS C  1 199 ? 29.308  -7.084  -7.513  1.00 21.17 ? 199  LYS C CE  1 
ATOM   5005 N  NZ  . LYS C  1 199 ? 30.352  -8.083  -7.893  1.00 21.43 ? 199  LYS C NZ  1 
ATOM   5006 N  N   . PRO C  1 200 ? 24.787  -10.491 -5.815  1.00 9.51  ? 200  PRO C N   1 
ATOM   5007 C  CA  . PRO C  1 200 ? 24.095  -11.439 -4.941  1.00 10.02 ? 200  PRO C CA  1 
ATOM   5008 C  C   . PRO C  1 200 ? 23.635  -10.732 -3.668  1.00 11.91 ? 200  PRO C C   1 
ATOM   5009 O  O   . PRO C  1 200 ? 24.319  -9.822  -3.180  1.00 11.05 ? 200  PRO C O   1 
ATOM   5010 C  CB  . PRO C  1 200 ? 25.195  -12.443 -4.585  1.00 15.42 ? 200  PRO C CB  1 
ATOM   5011 C  CG  . PRO C  1 200 ? 26.193  -12.318 -5.685  1.00 18.29 ? 200  PRO C CG  1 
ATOM   5012 C  CD  . PRO C  1 200 ? 26.187  -10.876 -6.056  1.00 12.74 ? 200  PRO C CD  1 
ATOM   5013 N  N   . LEU C  1 201 ? 22.486  -11.141 -3.145  1.00 10.82 ? 201  LEU C N   1 
ATOM   5014 C  CA  . LEU C  1 201 ? 22.026  -10.699 -1.837  1.00 12.12 ? 201  LEU C CA  1 
ATOM   5015 C  C   . LEU C  1 201 ? 22.795  -11.488 -0.780  1.00 14.47 ? 201  LEU C C   1 
ATOM   5016 O  O   . LEU C  1 201 ? 22.650  -12.709 -0.696  1.00 18.37 ? 201  LEU C O   1 
ATOM   5017 C  CB  . LEU C  1 201 ? 20.529  -10.976 -1.701  1.00 11.26 ? 201  LEU C CB  1 
ATOM   5018 C  CG  . LEU C  1 201 ? 19.926  -10.892 -0.298  1.00 17.01 ? 201  LEU C CG  1 
ATOM   5019 C  CD1 . LEU C  1 201 ? 20.034  -9.481  0.255   1.00 14.96 ? 201  LEU C CD1 1 
ATOM   5020 C  CD2 . LEU C  1 201 ? 18.465  -11.350 -0.293  1.00 19.06 ? 201  LEU C CD2 1 
ATOM   5021 N  N   . VAL C  1 202 ? 23.617  -10.813 0.025   1.00 10.78 ? 202  VAL C N   1 
ATOM   5022 C  CA  . VAL C  1 202 ? 24.420  -11.534 1.016   1.00 9.15  ? 202  VAL C CA  1 
ATOM   5023 C  C   . VAL C  1 202 ? 24.016  -11.252 2.456   1.00 11.51 ? 202  VAL C C   1 
ATOM   5024 O  O   . VAL C  1 202 ? 24.600  -11.822 3.388   1.00 13.55 ? 202  VAL C O   1 
ATOM   5025 C  CB  . VAL C  1 202 ? 25.930  -11.242 0.878   1.00 11.48 ? 202  VAL C CB  1 
ATOM   5026 C  CG1 . VAL C  1 202 ? 26.412  -11.565 -0.532  1.00 14.21 ? 202  VAL C CG1 1 
ATOM   5027 C  CG2 . VAL C  1 202 ? 26.228  -9.786  1.229   1.00 11.44 ? 202  VAL C CG2 1 
ATOM   5028 N  N   . TRP C  1 203 ? 23.025  -10.383 2.641   1.00 10.66 ? 203  TRP C N   1 
ATOM   5029 C  CA  . TRP C  1 203 ? 22.665  -9.931  3.977   1.00 11.88 ? 203  TRP C CA  1 
ATOM   5030 C  C   . TRP C  1 203 ? 21.347  -10.496 4.502   1.00 17.33 ? 203  TRP C C   1 
ATOM   5031 O  O   . TRP C  1 203 ? 20.928  -10.181 5.613   1.00 27.80 ? 203  TRP C O   1 
ATOM   5032 C  CB  . TRP C  1 203 ? 22.701  -8.399  4.071   1.00 12.76 ? 203  TRP C CB  1 
ATOM   5033 C  CG  . TRP C  1 203 ? 22.183  -7.641  2.883   1.00 9.09  ? 203  TRP C CG  1 
ATOM   5034 C  CD1 . TRP C  1 203 ? 22.904  -7.189  1.826   1.00 10.95 ? 203  TRP C CD1 1 
ATOM   5035 C  CD2 . TRP C  1 203 ? 20.843  -7.172  2.683   1.00 9.51  ? 203  TRP C CD2 1 
ATOM   5036 N  NE1 . TRP C  1 203 ? 22.095  -6.495  0.956   1.00 10.33 ? 203  TRP C NE1 1 
ATOM   5037 C  CE2 . TRP C  1 203 ? 20.823  -6.470  1.462   1.00 8.84  ? 203  TRP C CE2 1 
ATOM   5038 C  CE3 . TRP C  1 203 ? 19.653  -7.299  3.409   1.00 13.09 ? 203  TRP C CE3 1 
ATOM   5039 C  CZ2 . TRP C  1 203 ? 19.666  -5.886  0.951   1.00 9.84  ? 203  TRP C CZ2 1 
ATOM   5040 C  CZ3 . TRP C  1 203 ? 18.501  -6.718  2.898   1.00 11.58 ? 203  TRP C CZ3 1 
ATOM   5041 C  CH2 . TRP C  1 203 ? 18.516  -6.017  1.682   1.00 7.59  ? 203  TRP C CH2 1 
ATOM   5042 N  N   . VAL C  1 204 ? 20.696  -11.330 3.706   1.00 17.48 ? 204  VAL C N   1 
ATOM   5043 C  CA  . VAL C  1 204 ? 19.612  -12.151 4.234   1.00 39.30 ? 204  VAL C CA  1 
ATOM   5044 C  C   . VAL C  1 204 ? 20.148  -13.536 4.583   1.00 52.79 ? 204  VAL C C   1 
ATOM   5045 O  O   . VAL C  1 204 ? 20.020  -13.987 5.723   1.00 49.50 ? 204  VAL C O   1 
ATOM   5046 C  CB  . VAL C  1 204 ? 18.433  -12.270 3.245   1.00 41.60 ? 204  VAL C CB  1 
ATOM   5047 C  CG1 . VAL C  1 204 ? 17.622  -13.530 3.523   1.00 49.65 ? 204  VAL C CG1 1 
ATOM   5048 C  CG2 . VAL C  1 204 ? 17.551  -11.037 3.333   1.00 27.05 ? 204  VAL C CG2 1 
ATOM   5049 O  OXT . VAL C  1 204 ? 20.738  -14.222 3.743   1.00 57.98 ? 204  VAL C OXT 1 
ATOM   5050 N  N   . HIS D  1 1   ? 60.354  -16.579 5.158   1.00 29.03 ? 1    HIS D N   1 
ATOM   5051 C  CA  . HIS D  1 1   ? 58.958  -16.380 5.537   1.00 28.01 ? 1    HIS D CA  1 
ATOM   5052 C  C   . HIS D  1 1   ? 58.628  -17.142 6.809   1.00 28.99 ? 1    HIS D C   1 
ATOM   5053 O  O   . HIS D  1 1   ? 59.219  -18.186 7.097   1.00 25.01 ? 1    HIS D O   1 
ATOM   5054 C  CB  . HIS D  1 1   ? 58.034  -16.804 4.404   1.00 22.08 ? 1    HIS D CB  1 
ATOM   5055 C  CG  . HIS D  1 1   ? 58.353  -16.141 3.101   1.00 35.40 ? 1    HIS D CG  1 
ATOM   5056 N  ND1 . HIS D  1 1   ? 59.566  -15.533 2.858   1.00 43.22 ? 1    HIS D ND1 1 
ATOM   5057 C  CD2 . HIS D  1 1   ? 57.629  -16.004 1.965   1.00 37.94 ? 1    HIS D CD2 1 
ATOM   5058 C  CE1 . HIS D  1 1   ? 59.572  -15.041 1.632   1.00 38.45 ? 1    HIS D CE1 1 
ATOM   5059 N  NE2 . HIS D  1 1   ? 58.408  -15.312 1.070   1.00 48.43 ? 1    HIS D NE2 1 
ATOM   5060 N  N   . THR D  1 2   ? 57.666  -16.615 7.558   1.00 17.97 ? 2    THR D N   1 
ATOM   5061 C  CA  . THR D  1 2   ? 57.416  -17.059 8.919   1.00 13.71 ? 2    THR D CA  1 
ATOM   5062 C  C   . THR D  1 2   ? 55.958  -17.438 9.065   1.00 14.22 ? 2    THR D C   1 
ATOM   5063 O  O   . THR D  1 2   ? 55.087  -16.776 8.506   1.00 15.25 ? 2    THR D O   1 
ATOM   5064 C  CB  . THR D  1 2   ? 57.733  -15.927 9.917   1.00 19.37 ? 2    THR D CB  1 
ATOM   5065 O  OG1 . THR D  1 2   ? 59.126  -15.607 9.843   1.00 27.62 ? 2    THR D OG1 1 
ATOM   5066 C  CG2 . THR D  1 2   ? 57.379  -16.328 11.341  1.00 20.11 ? 2    THR D CG2 1 
ATOM   5067 N  N   . ASP D  1 3   ? 55.693  -18.502 9.811   1.00 13.48 ? 3    ASP D N   1 
ATOM   5068 C  CA  . ASP D  1 3   ? 54.323  -18.898 10.098  1.00 12.51 ? 3    ASP D CA  1 
ATOM   5069 C  C   . ASP D  1 3   ? 53.892  -18.240 11.403  1.00 13.90 ? 3    ASP D C   1 
ATOM   5070 O  O   . ASP D  1 3   ? 54.355  -18.617 12.480  1.00 14.82 ? 3    ASP D O   1 
ATOM   5071 C  CB  . ASP D  1 3   ? 54.236  -20.426 10.210  1.00 12.49 ? 3    ASP D CB  1 
ATOM   5072 C  CG  . ASP D  1 3   ? 52.828  -20.923 10.466  1.00 15.98 ? 3    ASP D CG  1 
ATOM   5073 O  OD1 . ASP D  1 3   ? 51.919  -20.101 10.724  1.00 14.66 ? 3    ASP D OD1 1 
ATOM   5074 O  OD2 . ASP D  1 3   ? 52.621  -22.153 10.402  1.00 19.68 ? 3    ASP D OD2 1 
ATOM   5075 N  N   . LEU D  1 4   ? 53.011  -17.249 11.307  1.00 12.11 ? 4    LEU D N   1 
ATOM   5076 C  CA  . LEU D  1 4   ? 52.567  -16.525 12.498  1.00 10.67 ? 4    LEU D CA  1 
ATOM   5077 C  C   . LEU D  1 4   ? 51.249  -17.053 13.061  1.00 13.67 ? 4    LEU D C   1 
ATOM   5078 O  O   . LEU D  1 4   ? 50.595  -16.380 13.860  1.00 11.04 ? 4    LEU D O   1 
ATOM   5079 C  CB  . LEU D  1 4   ? 52.460  -15.029 12.192  1.00 9.02  ? 4    LEU D CB  1 
ATOM   5080 C  CG  . LEU D  1 4   ? 53.788  -14.362 11.853  1.00 11.03 ? 4    LEU D CG  1 
ATOM   5081 C  CD1 . LEU D  1 4   ? 53.556  -12.916 11.434  1.00 12.73 ? 4    LEU D CD1 1 
ATOM   5082 C  CD2 . LEU D  1 4   ? 54.746  -14.425 13.039  1.00 15.41 ? 4    LEU D CD2 1 
ATOM   5083 N  N   . SER D  1 5   ? 50.861  -18.266 12.671  1.00 12.77 ? 5    SER D N   1 
ATOM   5084 C  CA  . SER D  1 5   ? 49.647  -18.875 13.226  1.00 12.17 ? 5    SER D CA  1 
ATOM   5085 C  C   . SER D  1 5   ? 49.624  -18.740 14.741  1.00 12.71 ? 5    SER D C   1 
ATOM   5086 O  O   . SER D  1 5   ? 50.594  -19.068 15.413  1.00 12.46 ? 5    SER D O   1 
ATOM   5087 C  CB  . SER D  1 5   ? 49.560  -20.363 12.872  1.00 15.87 ? 5    SER D CB  1 
ATOM   5088 O  OG  . SER D  1 5   ? 49.420  -20.532 11.481  1.00 17.09 ? 5    SER D OG  1 
ATOM   5089 N  N   . GLY D  1 6   ? 48.508  -18.245 15.266  1.00 10.30 ? 6    GLY D N   1 
ATOM   5090 C  CA  . GLY D  1 6   ? 48.329  -18.139 16.704  1.00 12.45 ? 6    GLY D CA  1 
ATOM   5091 C  C   . GLY D  1 6   ? 49.058  -16.969 17.339  1.00 11.47 ? 6    GLY D C   1 
ATOM   5092 O  O   . GLY D  1 6   ? 49.102  -16.865 18.569  1.00 11.83 ? 6    GLY D O   1 
ATOM   5093 N  N   . LYS D  1 7   ? 49.629  -16.094 16.512  1.00 10.08 ? 7    LYS D N   1 
ATOM   5094 C  CA  . LYS D  1 7   ? 50.385  -14.947 17.004  1.00 7.63  ? 7    LYS D CA  1 
ATOM   5095 C  C   . LYS D  1 7   ? 49.886  -13.636 16.408  1.00 8.91  ? 7    LYS D C   1 
ATOM   5096 O  O   . LYS D  1 7   ? 49.232  -13.628 15.365  1.00 11.98 ? 7    LYS D O   1 
ATOM   5097 C  CB  . LYS D  1 7   ? 51.881  -15.108 16.707  1.00 10.65 ? 7    LYS D CB  1 
ATOM   5098 C  CG  . LYS D  1 7   ? 52.514  -16.286 17.418  1.00 15.28 ? 7    LYS D CG  1 
ATOM   5099 C  CD  . LYS D  1 7   ? 53.925  -16.539 16.912  1.00 19.04 ? 7    LYS D CD  1 
ATOM   5100 C  CE  . LYS D  1 7   ? 54.495  -17.807 17.535  1.00 25.06 ? 7    LYS D CE  1 
ATOM   5101 N  NZ  . LYS D  1 7   ? 55.890  -18.062 17.066  1.00 29.10 ? 7    LYS D NZ  1 
ATOM   5102 N  N   . VAL D  1 8   ? 50.205  -12.531 17.075  1.00 8.86  ? 8    VAL D N   1 
ATOM   5103 C  CA  . VAL D  1 8   ? 49.831  -11.201 16.598  1.00 5.45  ? 8    VAL D CA  1 
ATOM   5104 C  C   . VAL D  1 8   ? 51.042  -10.288 16.594  1.00 7.14  ? 8    VAL D C   1 
ATOM   5105 O  O   . VAL D  1 8   ? 52.007  -10.527 17.313  1.00 9.84  ? 8    VAL D O   1 
ATOM   5106 C  CB  . VAL D  1 8   ? 48.753  -10.527 17.501  1.00 9.14  ? 8    VAL D CB  1 
ATOM   5107 C  CG1 . VAL D  1 8   ? 47.420  -11.245 17.394  1.00 12.10 ? 8    VAL D CG1 1 
ATOM   5108 C  CG2 . VAL D  1 8   ? 49.234  -10.451 18.950  1.00 10.21 ? 8    VAL D CG2 1 
ATOM   5109 N  N   . PHE D  1 9   ? 51.002  -9.247  15.771  1.00 7.77  ? 9    PHE D N   1 
ATOM   5110 C  CA  . PHE D  1 9   ? 51.902  -8.115  15.971  1.00 7.03  ? 9    PHE D CA  1 
ATOM   5111 C  C   . PHE D  1 9   ? 51.285  -7.203  17.008  1.00 9.63  ? 9    PHE D C   1 
ATOM   5112 O  O   . PHE D  1 9   ? 50.110  -6.842  16.891  1.00 8.96  ? 9    PHE D O   1 
ATOM   5113 C  CB  . PHE D  1 9   ? 52.072  -7.307  14.682  1.00 9.58  ? 9    PHE D CB  1 
ATOM   5114 C  CG  . PHE D  1 9   ? 52.868  -7.999  13.616  1.00 8.41  ? 9    PHE D CG  1 
ATOM   5115 C  CD1 . PHE D  1 9   ? 54.139  -8.479  13.880  1.00 12.44 ? 9    PHE D CD1 1 
ATOM   5116 C  CD2 . PHE D  1 9   ? 52.356  -8.125  12.332  1.00 11.49 ? 9    PHE D CD2 1 
ATOM   5117 C  CE1 . PHE D  1 9   ? 54.883  -9.106  12.882  1.00 13.20 ? 9    PHE D CE1 1 
ATOM   5118 C  CE2 . PHE D  1 9   ? 53.091  -8.743  11.331  1.00 10.80 ? 9    PHE D CE2 1 
ATOM   5119 C  CZ  . PHE D  1 9   ? 54.352  -9.238  11.609  1.00 9.34  ? 9    PHE D CZ  1 
ATOM   5120 N  N   . VAL D  1 10  ? 52.077  -6.822  18.011  1.00 7.97  ? 10   VAL D N   1 
ATOM   5121 C  CA  . VAL D  1 10  ? 51.646  -5.829  18.984  1.00 8.11  ? 10   VAL D CA  1 
ATOM   5122 C  C   . VAL D  1 10  ? 52.394  -4.530  18.731  1.00 7.51  ? 10   VAL D C   1 
ATOM   5123 O  O   . VAL D  1 10  ? 53.620  -4.507  18.773  1.00 8.12  ? 10   VAL D O   1 
ATOM   5124 C  CB  . VAL D  1 10  ? 51.931  -6.279  20.427  1.00 9.11  ? 10   VAL D CB  1 
ATOM   5125 C  CG1 . VAL D  1 10  ? 51.359  -5.256  21.415  1.00 7.63  ? 10   VAL D CG1 1 
ATOM   5126 C  CG2 . VAL D  1 10  ? 51.341  -7.662  20.676  1.00 10.18 ? 10   VAL D CG2 1 
ATOM   5127 N  N   . PHE D  1 11  ? 51.644  -3.470  18.440  1.00 7.46  ? 11   PHE D N   1 
ATOM   5128 C  CA  . PHE D  1 11  ? 52.175  -2.117  18.332  1.00 7.97  ? 11   PHE D CA  1 
ATOM   5129 C  C   . PHE D  1 11  ? 51.846  -1.470  19.682  1.00 8.48  ? 11   PHE D C   1 
ATOM   5130 O  O   . PHE D  1 11  ? 50.734  -0.977  19.891  1.00 9.08  ? 11   PHE D O   1 
ATOM   5131 C  CB  . PHE D  1 11  ? 51.494  -1.390  17.160  1.00 7.24  ? 11   PHE D CB  1 
ATOM   5132 C  CG  . PHE D  1 11  ? 51.667  -2.092  15.839  1.00 9.00  ? 11   PHE D CG  1 
ATOM   5133 C  CD1 . PHE D  1 11  ? 50.814  -3.131  15.478  1.00 10.15 ? 11   PHE D CD1 1 
ATOM   5134 C  CD2 . PHE D  1 11  ? 52.705  -1.749  14.981  1.00 11.91 ? 11   PHE D CD2 1 
ATOM   5135 C  CE1 . PHE D  1 11  ? 50.982  -3.809  14.274  1.00 11.27 ? 11   PHE D CE1 1 
ATOM   5136 C  CE2 . PHE D  1 11  ? 52.872  -2.418  13.778  1.00 10.64 ? 11   PHE D CE2 1 
ATOM   5137 C  CZ  . PHE D  1 11  ? 52.008  -3.446  13.425  1.00 11.26 ? 11   PHE D CZ  1 
ATOM   5138 N  N   . PRO D  1 12  ? 52.794  -1.531  20.634  1.00 7.87  ? 12   PRO D N   1 
ATOM   5139 C  CA  . PRO D  1 12  ? 52.431  -1.289  22.037  1.00 7.75  ? 12   PRO D CA  1 
ATOM   5140 C  C   . PRO D  1 12  ? 52.334  0.174   22.453  1.00 8.85  ? 12   PRO D C   1 
ATOM   5141 O  O   . PRO D  1 12  ? 52.008  0.454   23.609  1.00 8.06  ? 12   PRO D O   1 
ATOM   5142 C  CB  . PRO D  1 12  ? 53.559  -1.990  22.823  1.00 8.72  ? 12   PRO D CB  1 
ATOM   5143 C  CG  . PRO D  1 12  ? 54.374  -2.769  21.779  1.00 7.71  ? 12   PRO D CG  1 
ATOM   5144 C  CD  . PRO D  1 12  ? 54.170  -2.037  20.500  1.00 9.64  ? 12   PRO D CD  1 
ATOM   5145 N  N   . ARG D  1 13  ? 52.617  1.093   21.539  1.00 9.58  ? 13   ARG D N   1 
ATOM   5146 C  CA  . ARG D  1 13  ? 52.603  2.506   21.876  1.00 8.85  ? 13   ARG D CA  1 
ATOM   5147 C  C   . ARG D  1 13  ? 52.369  3.345   20.636  1.00 10.19 ? 13   ARG D C   1 
ATOM   5148 O  O   . ARG D  1 13  ? 52.606  2.903   19.511  1.00 10.52 ? 13   ARG D O   1 
ATOM   5149 C  CB  . ARG D  1 13  ? 53.945  2.933   22.487  1.00 10.48 ? 13   ARG D CB  1 
ATOM   5150 C  CG  . ARG D  1 13  ? 55.073  2.819   21.478  1.00 12.05 ? 13   ARG D CG  1 
ATOM   5151 C  CD  . ARG D  1 13  ? 56.422  3.367   21.920  1.00 16.65 ? 13   ARG D CD  1 
ATOM   5152 N  NE  . ARG D  1 13  ? 57.359  3.217   20.807  1.00 12.78 ? 13   ARG D NE  1 
ATOM   5153 C  CZ  . ARG D  1 13  ? 58.666  3.443   20.880  1.00 18.31 ? 13   ARG D CZ  1 
ATOM   5154 N  NH1 . ARG D  1 13  ? 59.221  3.831   22.027  1.00 20.80 ? 13   ARG D NH1 1 
ATOM   5155 N  NH2 . ARG D  1 13  ? 59.418  3.268   19.807  1.00 17.84 ? 13   ARG D NH2 1 
ATOM   5156 N  N   . GLU D  1 14  ? 51.925  4.575   20.864  1.00 10.89 ? 14   GLU D N   1 
ATOM   5157 C  CA  . GLU D  1 14  ? 51.800  5.549   19.794  1.00 10.07 ? 14   GLU D CA  1 
ATOM   5158 C  C   . GLU D  1 14  ? 53.192  6.060   19.430  1.00 11.67 ? 14   GLU D C   1 
ATOM   5159 O  O   . GLU D  1 14  ? 54.035  6.282   20.313  1.00 12.03 ? 14   GLU D O   1 
ATOM   5160 C  CB  . GLU D  1 14  ? 50.906  6.701   20.246  1.00 11.55 ? 14   GLU D CB  1 
ATOM   5161 C  CG  . GLU D  1 14  ? 50.743  7.807   19.229  1.00 12.00 ? 14   GLU D CG  1 
ATOM   5162 C  CD  . GLU D  1 14  ? 49.746  8.846   19.691  1.00 19.55 ? 14   GLU D CD  1 
ATOM   5163 O  OE1 . GLU D  1 14  ? 50.180  9.953   20.072  1.00 24.52 ? 14   GLU D OE1 1 
ATOM   5164 O  OE2 . GLU D  1 14  ? 48.537  8.546   19.702  1.00 16.03 ? 14   GLU D OE2 1 
ATOM   5165 N  N   . SER D  1 15  ? 53.436  6.217   18.133  1.00 10.15 ? 15   SER D N   1 
ATOM   5166 C  CA  . SER D  1 15  ? 54.735  6.661   17.629  1.00 14.76 ? 15   SER D CA  1 
ATOM   5167 C  C   . SER D  1 15  ? 54.588  7.048   16.175  1.00 13.82 ? 15   SER D C   1 
ATOM   5168 O  O   . SER D  1 15  ? 53.543  6.823   15.569  1.00 12.23 ? 15   SER D O   1 
ATOM   5169 C  CB  . SER D  1 15  ? 55.763  5.525   17.685  1.00 12.18 ? 15   SER D CB  1 
ATOM   5170 O  OG  . SER D  1 15  ? 55.559  4.611   16.615  1.00 11.65 ? 15   SER D OG  1 
ATOM   5171 N  N   . VAL D  1 16  ? 55.665  7.589   15.614  1.00 11.51 ? 16   VAL D N   1 
ATOM   5172 C  CA  . VAL D  1 16  ? 55.775  7.795   14.180  1.00 12.14 ? 16   VAL D CA  1 
ATOM   5173 C  C   . VAL D  1 16  ? 56.836  6.841   13.617  1.00 16.77 ? 16   VAL D C   1 
ATOM   5174 O  O   . VAL D  1 16  ? 57.152  6.875   12.416  1.00 18.91 ? 16   VAL D O   1 
ATOM   5175 C  CB  . VAL D  1 16  ? 56.128  9.282   13.876  1.00 17.36 ? 16   VAL D CB  1 
ATOM   5176 C  CG1 . VAL D  1 16  ? 57.590  9.568   14.214  1.00 14.87 ? 16   VAL D CG1 1 
ATOM   5177 C  CG2 . VAL D  1 16  ? 55.797  9.640   12.435  1.00 24.17 ? 16   VAL D CG2 1 
ATOM   5178 N  N   . THR D  1 17  ? 57.372  5.979   14.483  1.00 12.94 ? 17   THR D N   1 
ATOM   5179 C  CA  . THR D  1 17  ? 58.498  5.106   14.136  1.00 14.10 ? 17   THR D CA  1 
ATOM   5180 C  C   . THR D  1 17  ? 58.151  3.633   13.966  1.00 15.03 ? 17   THR D C   1 
ATOM   5181 O  O   . THR D  1 17  ? 58.757  2.937   13.152  1.00 17.88 ? 17   THR D O   1 
ATOM   5182 C  CB  . THR D  1 17  ? 59.584  5.128   15.230  1.00 16.85 ? 17   THR D CB  1 
ATOM   5183 O  OG1 . THR D  1 17  ? 58.994  4.817   16.507  1.00 16.09 ? 17   THR D OG1 1 
ATOM   5184 C  CG2 . THR D  1 17  ? 60.257  6.489   15.290  1.00 25.68 ? 17   THR D CG2 1 
ATOM   5185 N  N   . ASP D  1 18  ? 57.220  3.148   14.776  1.00 12.60 ? 18   ASP D N   1 
ATOM   5186 C  CA  . ASP D  1 18  ? 56.972  1.710   14.859  1.00 11.20 ? 18   ASP D CA  1 
ATOM   5187 C  C   . ASP D  1 18  ? 56.086  1.230   13.715  1.00 10.83 ? 18   ASP D C   1 
ATOM   5188 O  O   . ASP D  1 18  ? 54.976  1.738   13.518  1.00 11.04 ? 18   ASP D O   1 
ATOM   5189 C  CB  . ASP D  1 18  ? 56.314  1.356   16.193  1.00 11.70 ? 18   ASP D CB  1 
ATOM   5190 C  CG  . ASP D  1 18  ? 57.023  1.980   17.384  1.00 14.78 ? 18   ASP D CG  1 
ATOM   5191 O  OD1 . ASP D  1 18  ? 58.249  2.249   17.299  1.00 15.10 ? 18   ASP D OD1 1 
ATOM   5192 O  OD2 . ASP D  1 18  ? 56.344  2.200   18.411  1.00 12.09 ? 18   ASP D OD2 1 
ATOM   5193 N  N   . HIS D  1 19  ? 56.571  0.243   12.967  1.00 10.49 ? 19   HIS D N   1 
ATOM   5194 C  CA  . HIS D  1 19  ? 55.809  -0.296  11.847  1.00 10.34 ? 19   HIS D CA  1 
ATOM   5195 C  C   . HIS D  1 19  ? 56.306  -1.657  11.394  1.00 10.97 ? 19   HIS D C   1 
ATOM   5196 O  O   . HIS D  1 19  ? 57.402  -2.084  11.762  1.00 12.51 ? 19   HIS D O   1 
ATOM   5197 C  CB  . HIS D  1 19  ? 55.770  0.696   10.666  1.00 8.04  ? 19   HIS D CB  1 
ATOM   5198 C  CG  . HIS D  1 19  ? 57.098  0.949   10.008  1.00 10.38 ? 19   HIS D CG  1 
ATOM   5199 N  ND1 . HIS D  1 19  ? 58.103  1.683   10.606  1.00 11.71 ? 19   HIS D ND1 1 
ATOM   5200 C  CD2 . HIS D  1 19  ? 57.558  0.620   8.776   1.00 14.80 ? 19   HIS D CD2 1 
ATOM   5201 C  CE1 . HIS D  1 19  ? 59.133  1.772   9.780   1.00 16.21 ? 19   HIS D CE1 1 
ATOM   5202 N  NE2 . HIS D  1 19  ? 58.827  1.139   8.662   1.00 13.61 ? 19   HIS D NE2 1 
ATOM   5203 N  N   . VAL D  1 20  ? 55.477  -2.345  10.610  1.00 9.39  ? 20   VAL D N   1 
ATOM   5204 C  CA  . VAL D  1 20  ? 55.891  -3.569  9.958   1.00 8.52  ? 20   VAL D CA  1 
ATOM   5205 C  C   . VAL D  1 20  ? 55.733  -3.391  8.457   1.00 11.38 ? 20   VAL D C   1 
ATOM   5206 O  O   . VAL D  1 20  ? 54.698  -2.919  7.990   1.00 10.13 ? 20   VAL D O   1 
ATOM   5207 C  CB  . VAL D  1 20  ? 55.044  -4.777  10.395  1.00 11.09 ? 20   VAL D CB  1 
ATOM   5208 C  CG1 . VAL D  1 20  ? 55.509  -6.036  9.644   1.00 12.41 ? 20   VAL D CG1 1 
ATOM   5209 C  CG2 . VAL D  1 20  ? 55.150  -4.981  11.898  1.00 11.78 ? 20   VAL D CG2 1 
ATOM   5210 N  N   . ASN D  1 21  ? 56.775  -3.759  7.708   1.00 9.45  ? 21   ASN D N   1 
ATOM   5211 C  CA  . ASN D  1 21  ? 56.695  -3.804  6.255   1.00 10.60 ? 21   ASN D CA  1 
ATOM   5212 C  C   . ASN D  1 21  ? 56.321  -5.212  5.819   1.00 10.38 ? 21   ASN D C   1 
ATOM   5213 O  O   . ASN D  1 21  ? 56.946  -6.192  6.252   1.00 12.76 ? 21   ASN D O   1 
ATOM   5214 C  CB  . ASN D  1 21  ? 58.051  -3.438  5.637   1.00 11.57 ? 21   ASN D CB  1 
ATOM   5215 C  CG  . ASN D  1 21  ? 58.455  -2.001  5.916   1.00 15.18 ? 21   ASN D CG  1 
ATOM   5216 O  OD1 . ASN D  1 21  ? 57.627  -1.096  5.886   1.00 15.36 ? 21   ASN D OD1 1 
ATOM   5217 N  ND2 . ASN D  1 21  ? 59.743  -1.785  6.169   1.00 20.40 ? 21   ASN D ND2 1 
ATOM   5218 N  N   . LEU D  1 22  ? 55.312  -5.314  4.963   1.00 9.91  ? 22   LEU D N   1 
ATOM   5219 C  CA  . LEU D  1 22  ? 54.889  -6.606  4.442   1.00 11.06 ? 22   LEU D CA  1 
ATOM   5220 C  C   . LEU D  1 22  ? 55.389  -6.719  3.017   1.00 15.87 ? 22   LEU D C   1 
ATOM   5221 O  O   . LEU D  1 22  ? 55.180  -5.816  2.211   1.00 14.35 ? 22   LEU D O   1 
ATOM   5222 C  CB  . LEU D  1 22  ? 53.365  -6.753  4.489   1.00 10.30 ? 22   LEU D CB  1 
ATOM   5223 C  CG  . LEU D  1 22  ? 52.737  -6.627  5.873   1.00 10.62 ? 22   LEU D CG  1 
ATOM   5224 C  CD1 . LEU D  1 22  ? 51.232  -6.829  5.771   1.00 11.65 ? 22   LEU D CD1 1 
ATOM   5225 C  CD2 . LEU D  1 22  ? 53.370  -7.625  6.857   1.00 14.36 ? 22   LEU D CD2 1 
ATOM   5226 N  N   . ILE D  1 23  ? 56.050  -7.832  2.721   1.00 13.27 ? 23   ILE D N   1 
ATOM   5227 C  CA  . ILE D  1 23  ? 56.720  -8.016  1.438   1.00 16.20 ? 23   ILE D CA  1 
ATOM   5228 C  C   . ILE D  1 23  ? 55.994  -9.031  0.573   1.00 15.60 ? 23   ILE D C   1 
ATOM   5229 O  O   . ILE D  1 23  ? 55.762  -10.162 0.990   1.00 16.77 ? 23   ILE D O   1 
ATOM   5230 C  CB  . ILE D  1 23  ? 58.182  -8.456  1.654   1.00 18.65 ? 23   ILE D CB  1 
ATOM   5231 C  CG1 . ILE D  1 23  ? 58.941  -7.372  2.421   1.00 20.77 ? 23   ILE D CG1 1 
ATOM   5232 C  CG2 . ILE D  1 23  ? 58.860  -8.765  0.318   1.00 22.07 ? 23   ILE D CG2 1 
ATOM   5233 C  CD1 . ILE D  1 23  ? 60.174  -7.877  3.128   1.00 29.59 ? 23   ILE D CD1 1 
ATOM   5234 N  N   . THR D  1 24  ? 55.621  -8.608  -0.632  1.00 19.79 ? 24   THR D N   1 
ATOM   5235 C  CA  . THR D  1 24  ? 54.951  -9.483  -1.582  1.00 18.60 ? 24   THR D CA  1 
ATOM   5236 C  C   . THR D  1 24  ? 55.508  -9.189  -2.967  1.00 20.76 ? 24   THR D C   1 
ATOM   5237 O  O   . THR D  1 24  ? 55.730  -8.031  -3.314  1.00 26.25 ? 24   THR D O   1 
ATOM   5238 C  CB  . THR D  1 24  ? 53.412  -9.282  -1.561  1.00 29.52 ? 24   THR D CB  1 
ATOM   5239 O  OG1 . THR D  1 24  ? 52.772  -10.291 -2.358  1.00 29.70 ? 24   THR D OG1 1 
ATOM   5240 C  CG2 . THR D  1 24  ? 53.034  -7.898  -2.080  1.00 27.67 ? 24   THR D CG2 1 
ATOM   5241 N  N   . PRO D  1 25  ? 55.767  -10.240 -3.749  1.00 27.57 ? 25   PRO D N   1 
ATOM   5242 C  CA  . PRO D  1 25  ? 56.307  -10.065 -5.101  1.00 34.85 ? 25   PRO D CA  1 
ATOM   5243 C  C   . PRO D  1 25  ? 55.179  -9.754  -6.071  1.00 35.36 ? 25   PRO D C   1 
ATOM   5244 O  O   . PRO D  1 25  ? 54.927  -10.520 -7.004  1.00 43.44 ? 25   PRO D O   1 
ATOM   5245 C  CB  . PRO D  1 25  ? 56.903  -11.435 -5.410  1.00 31.17 ? 25   PRO D CB  1 
ATOM   5246 C  CG  . PRO D  1 25  ? 56.079  -12.391 -4.614  1.00 31.98 ? 25   PRO D CG  1 
ATOM   5247 C  CD  . PRO D  1 25  ? 55.550  -11.657 -3.410  1.00 29.01 ? 25   PRO D CD  1 
ATOM   5248 N  N   . LEU D  1 26  ? 54.498  -8.639  -5.838  1.00 23.28 ? 26   LEU D N   1 
ATOM   5249 C  CA  . LEU D  1 26  ? 53.352  -8.265  -6.650  1.00 22.95 ? 26   LEU D CA  1 
ATOM   5250 C  C   . LEU D  1 26  ? 53.802  -7.433  -7.841  1.00 29.32 ? 26   LEU D C   1 
ATOM   5251 O  O   . LEU D  1 26  ? 54.085  -6.242  -7.713  1.00 29.17 ? 26   LEU D O   1 
ATOM   5252 C  CB  . LEU D  1 26  ? 52.325  -7.499  -5.811  1.00 31.92 ? 26   LEU D CB  1 
ATOM   5253 C  CG  . LEU D  1 26  ? 50.937  -7.320  -6.426  1.00 35.61 ? 26   LEU D CG  1 
ATOM   5254 C  CD1 . LEU D  1 26  ? 50.400  -8.644  -6.949  1.00 34.84 ? 26   LEU D CD1 1 
ATOM   5255 C  CD2 . LEU D  1 26  ? 49.982  -6.714  -5.409  1.00 34.66 ? 26   LEU D CD2 1 
ATOM   5256 N  N   . GLU D  1 27  ? 53.859  -8.074  -9.003  1.00 25.18 ? 27   GLU D N   1 
ATOM   5257 C  CA  . GLU D  1 27  ? 54.407  -7.443  -10.197 1.00 31.77 ? 27   GLU D CA  1 
ATOM   5258 C  C   . GLU D  1 27  ? 53.344  -6.943  -11.164 1.00 23.72 ? 27   GLU D C   1 
ATOM   5259 O  O   . GLU D  1 27  ? 53.593  -6.020  -11.943 1.00 28.92 ? 27   GLU D O   1 
ATOM   5260 C  CB  . GLU D  1 27  ? 55.364  -8.403  -10.911 1.00 35.00 ? 27   GLU D CB  1 
ATOM   5261 C  CG  . GLU D  1 27  ? 56.823  -8.190  -10.561 1.00 51.02 ? 27   GLU D CG  1 
ATOM   5262 C  CD  . GLU D  1 27  ? 57.425  -7.009  -11.302 1.00 71.55 ? 27   GLU D CD  1 
ATOM   5263 O  OE1 . GLU D  1 27  ? 57.584  -7.097  -12.540 1.00 79.55 ? 27   GLU D OE1 1 
ATOM   5264 O  OE2 . GLU D  1 27  ? 57.744  -5.994  -10.647 1.00 69.19 ? 27   GLU D OE2 1 
ATOM   5265 N  N   . LYS D  1 28  ? 52.165  -7.555  -11.135 1.00 21.85 ? 28   LYS D N   1 
ATOM   5266 C  CA  . LYS D  1 28  ? 51.098  -7.122  -12.023 1.00 23.82 ? 28   LYS D CA  1 
ATOM   5267 C  C   . LYS D  1 28  ? 49.996  -6.384  -11.272 1.00 20.43 ? 28   LYS D C   1 
ATOM   5268 O  O   . LYS D  1 28  ? 49.645  -6.749  -10.145 1.00 20.96 ? 28   LYS D O   1 
ATOM   5269 C  CB  . LYS D  1 28  ? 50.520  -8.293  -12.820 1.00 30.46 ? 28   LYS D CB  1 
ATOM   5270 C  CG  . LYS D  1 28  ? 49.727  -9.291  -11.995 1.00 41.12 ? 28   LYS D CG  1 
ATOM   5271 C  CD  . LYS D  1 28  ? 49.110  -10.375 -12.873 1.00 61.36 ? 28   LYS D CD  1 
ATOM   5272 C  CE  . LYS D  1 28  ? 50.166  -11.321 -13.434 1.00 60.92 ? 28   LYS D CE  1 
ATOM   5273 N  NZ  . LYS D  1 28  ? 51.019  -10.681 -14.477 1.00 60.67 ? 28   LYS D NZ  1 
ATOM   5274 N  N   . PRO D  1 29  ? 49.459  -5.333  -11.898 1.00 18.29 ? 29   PRO D N   1 
ATOM   5275 C  CA  . PRO D  1 29  ? 48.366  -4.552  -11.308 1.00 17.58 ? 29   PRO D CA  1 
ATOM   5276 C  C   . PRO D  1 29  ? 47.206  -5.445  -10.886 1.00 16.82 ? 29   PRO D C   1 
ATOM   5277 O  O   . PRO D  1 29  ? 46.927  -6.454  -11.545 1.00 16.13 ? 29   PRO D O   1 
ATOM   5278 C  CB  . PRO D  1 29  ? 47.940  -3.636  -12.452 1.00 22.36 ? 29   PRO D CB  1 
ATOM   5279 C  CG  . PRO D  1 29  ? 49.199  -3.445  -13.251 1.00 28.09 ? 29   PRO D CG  1 
ATOM   5280 C  CD  . PRO D  1 29  ? 49.934  -4.754  -13.167 1.00 22.62 ? 29   PRO D CD  1 
ATOM   5281 N  N   . LEU D  1 30  ? 46.551  -5.062  -9.794  1.00 14.51 ? 30   LEU D N   1 
ATOM   5282 C  CA  . LEU D  1 30  ? 45.445  -5.820  -9.215  1.00 14.90 ? 30   LEU D CA  1 
ATOM   5283 C  C   . LEU D  1 30  ? 44.107  -5.342  -9.759  1.00 14.67 ? 30   LEU D C   1 
ATOM   5284 O  O   . LEU D  1 30  ? 43.798  -4.153  -9.702  1.00 16.80 ? 30   LEU D O   1 
ATOM   5285 C  CB  . LEU D  1 30  ? 45.422  -5.622  -7.701  1.00 16.86 ? 30   LEU D CB  1 
ATOM   5286 C  CG  . LEU D  1 30  ? 46.424  -6.387  -6.848  1.00 24.96 ? 30   LEU D CG  1 
ATOM   5287 C  CD1 . LEU D  1 30  ? 46.250  -5.977  -5.396  1.00 20.69 ? 30   LEU D CD1 1 
ATOM   5288 C  CD2 . LEU D  1 30  ? 46.221  -7.885  -7.017  1.00 23.97 ? 30   LEU D CD2 1 
ATOM   5289 N  N   . GLN D  1 31  ? 43.314  -6.276  -10.269 1.00 13.41 ? 31   GLN D N   1 
ATOM   5290 C  CA  . GLN D  1 31  ? 41.967  -5.980  -10.730 1.00 14.72 ? 31   GLN D CA  1 
ATOM   5291 C  C   . GLN D  1 31  ? 40.964  -6.292  -9.627  1.00 15.37 ? 31   GLN D C   1 
ATOM   5292 O  O   . GLN D  1 31  ? 39.946  -5.614  -9.491  1.00 13.11 ? 31   GLN D O   1 
ATOM   5293 C  CB  . GLN D  1 31  ? 41.626  -6.825  -11.963 1.00 19.16 ? 31   GLN D CB  1 
ATOM   5294 C  CG  . GLN D  1 31  ? 42.488  -6.533  -13.177 1.00 31.60 ? 31   GLN D CG  1 
ATOM   5295 C  CD  . GLN D  1 31  ? 42.124  -7.393  -14.375 1.00 38.89 ? 31   GLN D CD  1 
ATOM   5296 O  OE1 . GLN D  1 31  ? 41.030  -7.965  -14.444 1.00 30.43 ? 31   GLN D OE1 1 
ATOM   5297 N  NE2 . GLN D  1 31  ? 43.045  -7.492  -15.328 1.00 41.11 ? 31   GLN D NE2 1 
ATOM   5298 N  N   . ASN D  1 32  ? 41.265  -7.332  -8.851  1.00 9.59  ? 32   ASN D N   1 
ATOM   5299 C  CA  . ASN D  1 32  ? 40.389  -7.804  -7.778  1.00 9.71  ? 32   ASN D CA  1 
ATOM   5300 C  C   . ASN D  1 32  ? 41.221  -8.156  -6.555  1.00 12.87 ? 32   ASN D C   1 
ATOM   5301 O  O   . ASN D  1 32  ? 42.347  -8.638  -6.678  1.00 13.74 ? 32   ASN D O   1 
ATOM   5302 C  CB  . ASN D  1 32  ? 39.642  -9.089  -8.176  1.00 12.22 ? 32   ASN D CB  1 
ATOM   5303 C  CG  . ASN D  1 32  ? 39.020  -9.029  -9.558  1.00 18.59 ? 32   ASN D CG  1 
ATOM   5304 O  OD1 . ASN D  1 32  ? 38.201  -8.154  -9.853  1.00 14.76 ? 32   ASN D OD1 1 
ATOM   5305 N  ND2 . ASN D  1 32  ? 39.387  -10.009 -10.399 1.00 20.91 ? 32   ASN D ND2 1 
ATOM   5306 N  N   . PHE D  1 33  ? 40.673  -7.946  -5.362  1.00 9.81  ? 33   PHE D N   1 
ATOM   5307 C  CA  . PHE D  1 33  ? 41.349  -8.463  -4.176  1.00 8.91  ? 33   PHE D CA  1 
ATOM   5308 C  C   . PHE D  1 33  ? 40.391  -8.619  -3.017  1.00 9.65  ? 33   PHE D C   1 
ATOM   5309 O  O   . PHE D  1 33  ? 39.301  -8.032  -3.003  1.00 8.61  ? 33   PHE D O   1 
ATOM   5310 C  CB  . PHE D  1 33  ? 42.510  -7.556  -3.745  1.00 7.63  ? 33   PHE D CB  1 
ATOM   5311 C  CG  . PHE D  1 33  ? 42.065  -6.255  -3.129  1.00 10.95 ? 33   PHE D CG  1 
ATOM   5312 C  CD1 . PHE D  1 33  ? 41.784  -6.175  -1.766  1.00 10.53 ? 33   PHE D CD1 1 
ATOM   5313 C  CD2 . PHE D  1 33  ? 41.926  -5.120  -3.907  1.00 11.32 ? 33   PHE D CD2 1 
ATOM   5314 C  CE1 . PHE D  1 33  ? 41.365  -4.975  -1.198  1.00 12.63 ? 33   PHE D CE1 1 
ATOM   5315 C  CE2 . PHE D  1 33  ? 41.510  -3.916  -3.349  1.00 9.82  ? 33   PHE D CE2 1 
ATOM   5316 C  CZ  . PHE D  1 33  ? 41.226  -3.843  -1.993  1.00 11.27 ? 33   PHE D CZ  1 
ATOM   5317 N  N   . THR D  1 34  ? 40.813  -9.434  -2.053  1.00 8.55  ? 34   THR D N   1 
ATOM   5318 C  CA  . THR D  1 34  ? 40.163  -9.478  -0.756  1.00 10.30 ? 34   THR D CA  1 
ATOM   5319 C  C   . THR D  1 34  ? 41.252  -9.431  0.300   1.00 10.88 ? 34   THR D C   1 
ATOM   5320 O  O   . THR D  1 34  ? 42.277  -10.080 0.161   1.00 9.44  ? 34   THR D O   1 
ATOM   5321 C  CB  . THR D  1 34  ? 39.345  -10.754 -0.567  1.00 7.57  ? 34   THR D CB  1 
ATOM   5322 O  OG1 . THR D  1 34  ? 38.361  -10.841 -1.602  1.00 10.22 ? 34   THR D OG1 1 
ATOM   5323 C  CG2 . THR D  1 34  ? 38.635  -10.704 0.775   1.00 9.30  ? 34   THR D CG2 1 
ATOM   5324 N  N   . LEU D  1 35  ? 41.032  -8.640  1.343   1.00 9.08  ? 35   LEU D N   1 
ATOM   5325 C  CA  . LEU D  1 35  ? 41.976  -8.545  2.462   1.00 6.21  ? 35   LEU D CA  1 
ATOM   5326 C  C   . LEU D  1 35  ? 41.218  -8.814  3.757   1.00 8.25  ? 35   LEU D C   1 
ATOM   5327 O  O   . LEU D  1 35  ? 40.203  -8.175  4.012   1.00 7.93  ? 35   LEU D O   1 
ATOM   5328 C  CB  . LEU D  1 35  ? 42.589  -7.142  2.503   1.00 7.18  ? 35   LEU D CB  1 
ATOM   5329 C  CG  . LEU D  1 35  ? 43.418  -6.791  3.733   1.00 11.59 ? 35   LEU D CG  1 
ATOM   5330 C  CD1 . LEU D  1 35  ? 44.736  -7.566  3.764   1.00 12.55 ? 35   LEU D CD1 1 
ATOM   5331 C  CD2 . LEU D  1 35  ? 43.672  -5.286  3.754   1.00 11.03 ? 35   LEU D CD2 1 
ATOM   5332 N  N   . CYS D  1 36  ? 41.687  -9.779  4.549   1.00 9.38  ? 36   CYS D N   1 
ATOM   5333 C  CA  . CYS D  1 36  ? 41.080  -10.076 5.861   1.00 9.17  ? 36   CYS D CA  1 
ATOM   5334 C  C   . CYS D  1 36  ? 42.147  -10.004 6.941   1.00 9.32  ? 36   CYS D C   1 
ATOM   5335 O  O   . CYS D  1 36  ? 43.306  -10.329 6.694   1.00 11.16 ? 36   CYS D O   1 
ATOM   5336 C  CB  . CYS D  1 36  ? 40.463  -11.485 5.893   1.00 9.62  ? 36   CYS D CB  1 
ATOM   5337 S  SG  . CYS D  1 36  ? 39.090  -11.772 4.737   1.00 14.65 ? 36   CYS D SG  1 
ATOM   5338 N  N   . PHE D  1 37  ? 41.756  -9.562  8.138   1.00 7.99  ? 37   PHE D N   1 
ATOM   5339 C  CA  . PHE D  1 37  ? 42.651  -9.570  9.300   1.00 9.02  ? 37   PHE D CA  1 
ATOM   5340 C  C   . PHE D  1 37  ? 41.838  -9.335  10.569  1.00 8.66  ? 37   PHE D C   1 
ATOM   5341 O  O   . PHE D  1 37  ? 40.677  -8.919  10.508  1.00 8.45  ? 37   PHE D O   1 
ATOM   5342 C  CB  . PHE D  1 37  ? 43.757  -8.503  9.184   1.00 8.61  ? 37   PHE D CB  1 
ATOM   5343 C  CG  . PHE D  1 37  ? 43.234  -7.115  8.908   1.00 9.03  ? 37   PHE D CG  1 
ATOM   5344 C  CD1 . PHE D  1 37  ? 43.045  -6.680  7.604   1.00 13.35 ? 37   PHE D CD1 1 
ATOM   5345 C  CD2 . PHE D  1 37  ? 42.914  -6.258  9.954   1.00 13.80 ? 37   PHE D CD2 1 
ATOM   5346 C  CE1 . PHE D  1 37  ? 42.549  -5.405  7.340   1.00 15.03 ? 37   PHE D CE1 1 
ATOM   5347 C  CE2 . PHE D  1 37  ? 42.414  -4.983  9.705   1.00 11.39 ? 37   PHE D CE2 1 
ATOM   5348 C  CZ  . PHE D  1 37  ? 42.230  -4.556  8.397   1.00 13.30 ? 37   PHE D CZ  1 
ATOM   5349 N  N   . ARG D  1 38  ? 42.454  -9.617  11.715  1.00 9.03  ? 38   ARG D N   1 
ATOM   5350 C  CA  . ARG D  1 38  ? 41.844  -9.362  13.019  1.00 9.13  ? 38   ARG D CA  1 
ATOM   5351 C  C   . ARG D  1 38  ? 42.593  -8.241  13.697  1.00 8.66  ? 38   ARG D C   1 
ATOM   5352 O  O   . ARG D  1 38  ? 43.810  -8.165  13.603  1.00 10.30 ? 38   ARG D O   1 
ATOM   5353 C  CB  . ARG D  1 38  ? 41.992  -10.592 13.914  1.00 13.89 ? 38   ARG D CB  1 
ATOM   5354 C  CG  . ARG D  1 38  ? 40.829  -11.509 13.927  1.00 27.03 ? 38   ARG D CG  1 
ATOM   5355 C  CD  . ARG D  1 38  ? 41.162  -12.742 14.750  1.00 18.83 ? 38   ARG D CD  1 
ATOM   5356 N  NE  . ARG D  1 38  ? 40.948  -13.906 13.917  1.00 17.01 ? 38   ARG D NE  1 
ATOM   5357 C  CZ  . ARG D  1 38  ? 39.751  -14.368 13.590  1.00 15.15 ? 38   ARG D CZ  1 
ATOM   5358 N  NH1 . ARG D  1 38  ? 38.655  -13.785 14.071  1.00 15.15 ? 38   ARG D NH1 1 
ATOM   5359 N  NH2 . ARG D  1 38  ? 39.651  -15.426 12.798  1.00 21.66 ? 38   ARG D NH2 1 
ATOM   5360 N  N   . ALA D  1 39  ? 41.881  -7.359  14.383  1.00 6.60  ? 39   ALA D N   1 
ATOM   5361 C  CA  . ALA D  1 39  ? 42.551  -6.266  15.068  1.00 7.41  ? 39   ALA D CA  1 
ATOM   5362 C  C   . ALA D  1 39  ? 41.900  -6.020  16.420  1.00 8.03  ? 39   ALA D C   1 
ATOM   5363 O  O   . ALA D  1 39  ? 40.711  -6.284  16.604  1.00 9.60  ? 39   ALA D O   1 
ATOM   5364 C  CB  . ALA D  1 39  ? 42.514  -4.986  14.227  1.00 7.09  ? 39   ALA D CB  1 
ATOM   5365 N  N   . TYR D  1 40  ? 42.695  -5.512  17.354  1.00 7.32  ? 40   TYR D N   1 
ATOM   5366 C  CA  . TYR D  1 40  ? 42.190  -5.163  18.678  1.00 6.78  ? 40   TYR D CA  1 
ATOM   5367 C  C   . TYR D  1 40  ? 42.880  -3.872  19.115  1.00 7.02  ? 40   TYR D C   1 
ATOM   5368 O  O   . TYR D  1 40  ? 44.098  -3.835  19.305  1.00 8.05  ? 40   TYR D O   1 
ATOM   5369 C  CB  . TYR D  1 40  ? 42.469  -6.316  19.642  1.00 8.15  ? 40   TYR D CB  1 
ATOM   5370 C  CG  . TYR D  1 40  ? 41.845  -6.221  21.014  1.00 6.85  ? 40   TYR D CG  1 
ATOM   5371 C  CD1 . TYR D  1 40  ? 40.710  -5.448  21.246  1.00 6.97  ? 40   TYR D CD1 1 
ATOM   5372 C  CD2 . TYR D  1 40  ? 42.371  -6.961  22.074  1.00 5.87  ? 40   TYR D CD2 1 
ATOM   5373 C  CE1 . TYR D  1 40  ? 40.125  -5.393  22.516  1.00 10.23 ? 40   TYR D CE1 1 
ATOM   5374 C  CE2 . TYR D  1 40  ? 41.796  -6.921  23.339  1.00 5.30  ? 40   TYR D CE2 1 
ATOM   5375 C  CZ  . TYR D  1 40  ? 40.679  -6.138  23.555  1.00 8.91  ? 40   TYR D CZ  1 
ATOM   5376 O  OH  . TYR D  1 40  ? 40.121  -6.101  24.811  1.00 10.12 ? 40   TYR D OH  1 
ATOM   5377 N  N   . SER D  1 41  ? 42.104  -2.798  19.235  1.00 6.97  ? 41   SER D N   1 
ATOM   5378 C  CA  . SER D  1 41  ? 42.685  -1.505  19.571  1.00 7.20  ? 41   SER D CA  1 
ATOM   5379 C  C   . SER D  1 41  ? 41.696  -0.750  20.426  1.00 8.85  ? 41   SER D C   1 
ATOM   5380 O  O   . SER D  1 41  ? 40.493  -0.857  20.203  1.00 10.69 ? 41   SER D O   1 
ATOM   5381 C  CB  . SER D  1 41  ? 42.943  -0.704  18.286  1.00 9.51  ? 41   SER D CB  1 
ATOM   5382 O  OG  . SER D  1 41  ? 43.396  0.622   18.556  1.00 7.58  ? 41   SER D OG  1 
ATOM   5383 N  N   . ASP D  1 42  ? 42.186  0.029   21.384  1.00 7.98  ? 42   ASP D N   1 
ATOM   5384 C  CA  . ASP D  1 42  ? 41.279  0.896   22.140  1.00 7.80  ? 42   ASP D CA  1 
ATOM   5385 C  C   . ASP D  1 42  ? 41.491  2.380   21.805  1.00 8.25  ? 42   ASP D C   1 
ATOM   5386 O  O   . ASP D  1 42  ? 41.125  3.285   22.571  1.00 10.68 ? 42   ASP D O   1 
ATOM   5387 C  CB  . ASP D  1 42  ? 41.281  0.599   23.655  1.00 8.25  ? 42   ASP D CB  1 
ATOM   5388 C  CG  . ASP D  1 42  ? 42.657  0.731   24.295  1.00 10.45 ? 42   ASP D CG  1 
ATOM   5389 O  OD1 . ASP D  1 42  ? 43.538  1.391   23.720  1.00 11.00 ? 42   ASP D OD1 1 
ATOM   5390 O  OD2 . ASP D  1 42  ? 42.837  0.178   25.398  1.00 9.26  ? 42   ASP D OD2 1 
ATOM   5391 N  N   . LEU D  1 43  ? 42.047  2.639   20.634  1.00 9.13  ? 43   LEU D N   1 
ATOM   5392 C  CA  . LEU D  1 43  ? 42.117  4.022   20.152  1.00 8.43  ? 43   LEU D CA  1 
ATOM   5393 C  C   . LEU D  1 43  ? 40.728  4.534   19.768  1.00 9.57  ? 43   LEU D C   1 
ATOM   5394 O  O   . LEU D  1 43  ? 39.950  3.817   19.140  1.00 9.93  ? 43   LEU D O   1 
ATOM   5395 C  CB  . LEU D  1 43  ? 43.014  4.099   18.914  1.00 7.32  ? 43   LEU D CB  1 
ATOM   5396 C  CG  . LEU D  1 43  ? 44.512  3.950   19.093  1.00 8.92  ? 43   LEU D CG  1 
ATOM   5397 C  CD1 . LEU D  1 43  ? 45.156  3.866   17.710  1.00 11.46 ? 43   LEU D CD1 1 
ATOM   5398 C  CD2 . LEU D  1 43  ? 45.060  5.158   19.867  1.00 8.85  ? 43   LEU D CD2 1 
ATOM   5399 N  N   . SER D  1 44  ? 40.426  5.783   20.126  1.00 9.69  ? 44   SER D N   1 
ATOM   5400 C  CA  . SER D  1 44  ? 39.201  6.436   19.659  1.00 11.28 ? 44   SER D CA  1 
ATOM   5401 C  C   . SER D  1 44  ? 39.445  7.328   18.450  1.00 13.47 ? 44   SER D C   1 
ATOM   5402 O  O   . SER D  1 44  ? 38.531  7.582   17.659  1.00 16.11 ? 44   SER D O   1 
ATOM   5403 C  CB  . SER D  1 44  ? 38.598  7.275   20.782  1.00 16.86 ? 44   SER D CB  1 
ATOM   5404 O  OG  . SER D  1 44  ? 38.089  6.432   21.788  1.00 20.33 ? 44   SER D OG  1 
ATOM   5405 N  N   . ARG D  1 45  ? 40.667  7.830   18.320  1.00 10.99 ? 45   ARG D N   1 
ATOM   5406 C  CA  . ARG D  1 45  ? 41.005  8.670   17.180  1.00 10.67 ? 45   ARG D CA  1 
ATOM   5407 C  C   . ARG D  1 45  ? 41.078  7.824   15.918  1.00 11.61 ? 45   ARG D C   1 
ATOM   5408 O  O   . ARG D  1 45  ? 41.015  6.594   15.984  1.00 11.66 ? 45   ARG D O   1 
ATOM   5409 C  CB  . ARG D  1 45  ? 42.346  9.389   17.392  1.00 12.30 ? 45   ARG D CB  1 
ATOM   5410 C  CG  . ARG D  1 45  ? 43.543  8.462   17.533  1.00 13.00 ? 45   ARG D CG  1 
ATOM   5411 C  CD  . ARG D  1 45  ? 44.847  9.195   17.221  1.00 12.97 ? 45   ARG D CD  1 
ATOM   5412 N  NE  . ARG D  1 45  ? 46.009  8.447   17.688  1.00 11.87 ? 45   ARG D NE  1 
ATOM   5413 C  CZ  . ARG D  1 45  ? 46.588  7.458   17.012  1.00 13.57 ? 45   ARG D CZ  1 
ATOM   5414 N  NH1 . ARG D  1 45  ? 46.117  7.093   15.821  1.00 10.20 ? 45   ARG D NH1 1 
ATOM   5415 N  NH2 . ARG D  1 45  ? 47.633  6.829   17.541  1.00 11.03 ? 45   ARG D NH2 1 
ATOM   5416 N  N   . ALA D  1 46  ? 41.217  8.493   14.775  1.00 12.11 ? 46   ALA D N   1 
ATOM   5417 C  CA  . ALA D  1 46  ? 41.395  7.814   13.495  1.00 13.51 ? 46   ALA D CA  1 
ATOM   5418 C  C   . ALA D  1 46  ? 42.727  7.064   13.445  1.00 13.10 ? 46   ALA D C   1 
ATOM   5419 O  O   . ALA D  1 46  ? 43.697  7.454   14.090  1.00 12.92 ? 46   ALA D O   1 
ATOM   5420 C  CB  . ALA D  1 46  ? 41.324  8.825   12.357  1.00 14.88 ? 46   ALA D CB  1 
ATOM   5421 N  N   . TYR D  1 47  ? 42.772  5.987   12.673  1.00 8.92  ? 47   TYR D N   1 
ATOM   5422 C  CA  . TYR D  1 47  ? 44.023  5.279   12.438  1.00 9.89  ? 47   TYR D CA  1 
ATOM   5423 C  C   . TYR D  1 47  ? 43.971  4.414   11.188  1.00 11.00 ? 47   TYR D C   1 
ATOM   5424 O  O   . TYR D  1 47  ? 42.901  4.002   10.755  1.00 10.88 ? 47   TYR D O   1 
ATOM   5425 C  CB  . TYR D  1 47  ? 44.416  4.428   13.652  1.00 9.79  ? 47   TYR D CB  1 
ATOM   5426 C  CG  . TYR D  1 47  ? 43.358  3.451   14.144  1.00 10.24 ? 47   TYR D CG  1 
ATOM   5427 C  CD1 . TYR D  1 47  ? 43.234  2.186   13.580  1.00 8.68  ? 47   TYR D CD1 1 
ATOM   5428 C  CD2 . TYR D  1 47  ? 42.502  3.789   15.189  1.00 8.63  ? 47   TYR D CD2 1 
ATOM   5429 C  CE1 . TYR D  1 47  ? 42.281  1.279   14.048  1.00 9.97  ? 47   TYR D CE1 1 
ATOM   5430 C  CE2 . TYR D  1 47  ? 41.546  2.892   15.662  1.00 12.30 ? 47   TYR D CE2 1 
ATOM   5431 C  CZ  . TYR D  1 47  ? 41.443  1.640   15.087  1.00 11.33 ? 47   TYR D CZ  1 
ATOM   5432 O  OH  . TYR D  1 47  ? 40.492  0.758   15.564  1.00 11.13 ? 47   TYR D OH  1 
ATOM   5433 N  N   . SER D  1 48  ? 45.142  4.165   10.616  1.00 9.67  ? 48   SER D N   1 
ATOM   5434 C  CA  . SER D  1 48  ? 45.298  3.285   9.467   1.00 10.20 ? 48   SER D CA  1 
ATOM   5435 C  C   . SER D  1 48  ? 45.418  1.831   9.905   1.00 10.97 ? 48   SER D C   1 
ATOM   5436 O  O   . SER D  1 48  ? 46.191  1.514   10.799  1.00 11.02 ? 48   SER D O   1 
ATOM   5437 C  CB  . SER D  1 48  ? 46.574  3.663   8.705   1.00 9.24  ? 48   SER D CB  1 
ATOM   5438 O  OG  . SER D  1 48  ? 46.784  2.799   7.600   1.00 11.74 ? 48   SER D OG  1 
ATOM   5439 N  N   . LEU D  1 49  ? 44.664  0.946   9.263   1.00 9.46  ? 49   LEU D N   1 
ATOM   5440 C  CA  . LEU D  1 49  ? 44.815  -0.490  9.508   1.00 8.36  ? 49   LEU D CA  1 
ATOM   5441 C  C   . LEU D  1 49  ? 45.746  -1.167  8.506   1.00 9.09  ? 49   LEU D C   1 
ATOM   5442 O  O   . LEU D  1 49  ? 46.484  -2.084  8.864   1.00 8.67  ? 49   LEU D O   1 
ATOM   5443 C  CB  . LEU D  1 49  ? 43.443  -1.178  9.478   1.00 7.53  ? 49   LEU D CB  1 
ATOM   5444 C  CG  . LEU D  1 49  ? 42.575  -0.899  10.704  1.00 10.25 ? 49   LEU D CG  1 
ATOM   5445 C  CD1 . LEU D  1 49  ? 41.129  -1.229  10.402  1.00 12.70 ? 49   LEU D CD1 1 
ATOM   5446 C  CD2 . LEU D  1 49  ? 43.096  -1.707  11.891  1.00 11.61 ? 49   LEU D CD2 1 
ATOM   5447 N  N   . PHE D  1 50  ? 45.719  -0.727  7.249   1.00 7.19  ? 50   PHE D N   1 
ATOM   5448 C  CA  . PHE D  1 50  ? 46.508  -1.390  6.204   1.00 8.51  ? 50   PHE D CA  1 
ATOM   5449 C  C   . PHE D  1 50  ? 46.797  -0.342  5.157   1.00 8.51  ? 50   PHE D C   1 
ATOM   5450 O  O   . PHE D  1 50  ? 45.877  0.191   4.540   1.00 8.37  ? 50   PHE D O   1 
ATOM   5451 C  CB  . PHE D  1 50  ? 45.704  -2.536  5.581   1.00 8.91  ? 50   PHE D CB  1 
ATOM   5452 C  CG  . PHE D  1 50  ? 46.434  -3.315  4.502   1.00 8.77  ? 50   PHE D CG  1 
ATOM   5453 C  CD1 . PHE D  1 50  ? 47.161  -4.460  4.822   1.00 9.18  ? 50   PHE D CD1 1 
ATOM   5454 C  CD2 . PHE D  1 50  ? 46.337  -2.938  3.163   1.00 10.05 ? 50   PHE D CD2 1 
ATOM   5455 C  CE1 . PHE D  1 50  ? 47.800  -5.199  3.825   1.00 9.55  ? 50   PHE D CE1 1 
ATOM   5456 C  CE2 . PHE D  1 50  ? 46.975  -3.670  2.164   1.00 9.34  ? 50   PHE D CE2 1 
ATOM   5457 C  CZ  . PHE D  1 50  ? 47.706  -4.803  2.497   1.00 10.13 ? 50   PHE D CZ  1 
ATOM   5458 N  N   . SER D  1 51  ? 48.077  -0.042  4.963   1.00 8.58  ? 51   SER D N   1 
ATOM   5459 C  CA  . SER D  1 51  ? 48.487  1.053   4.088   1.00 8.98  ? 51   SER D CA  1 
ATOM   5460 C  C   . SER D  1 51  ? 49.333  0.537   2.920   1.00 10.40 ? 51   SER D C   1 
ATOM   5461 O  O   . SER D  1 51  ? 50.389  -0.044  3.124   1.00 7.83  ? 51   SER D O   1 
ATOM   5462 C  CB  . SER D  1 51  ? 49.269  2.096   4.911   1.00 8.57  ? 51   SER D CB  1 
ATOM   5463 O  OG  . SER D  1 51  ? 49.910  3.064   4.086   1.00 8.79  ? 51   SER D OG  1 
ATOM   5464 N  N   . TYR D  1 52  ? 48.844  0.731   1.697   1.00 7.03  ? 52   TYR D N   1 
ATOM   5465 C  CA  . TYR D  1 52  ? 49.491  0.204   0.484   1.00 9.85  ? 52   TYR D CA  1 
ATOM   5466 C  C   . TYR D  1 52  ? 49.671  1.382   -0.474  1.00 9.84  ? 52   TYR D C   1 
ATOM   5467 O  O   . TYR D  1 52  ? 48.697  1.969   -0.958  1.00 10.28 ? 52   TYR D O   1 
ATOM   5468 C  CB  . TYR D  1 52  ? 48.569  -0.894  -0.083  1.00 8.75  ? 52   TYR D CB  1 
ATOM   5469 C  CG  . TYR D  1 52  ? 48.842  -1.541  -1.444  1.00 7.99  ? 52   TYR D CG  1 
ATOM   5470 C  CD1 . TYR D  1 52  ? 48.901  -0.789  -2.618  1.00 9.90  ? 52   TYR D CD1 1 
ATOM   5471 C  CD2 . TYR D  1 52  ? 48.914  -2.930  -1.554  1.00 9.86  ? 52   TYR D CD2 1 
ATOM   5472 C  CE1 . TYR D  1 52  ? 49.082  -1.420  -3.869  1.00 10.22 ? 52   TYR D CE1 1 
ATOM   5473 C  CE2 . TYR D  1 52  ? 49.097  -3.558  -2.784  1.00 11.07 ? 52   TYR D CE2 1 
ATOM   5474 C  CZ  . TYR D  1 52  ? 49.180  -2.798  -3.930  1.00 13.79 ? 52   TYR D CZ  1 
ATOM   5475 O  OH  . TYR D  1 52  ? 49.363  -3.442  -5.136  1.00 14.84 ? 52   TYR D OH  1 
ATOM   5476 N  N   . ASN D  1 53  ? 50.928  1.769   -0.682  1.00 9.78  ? 53   ASN D N   1 
ATOM   5477 C  CA  . ASN D  1 53  ? 51.271  2.890   -1.562  1.00 11.58 ? 53   ASN D CA  1 
ATOM   5478 C  C   . ASN D  1 53  ? 52.174  2.395   -2.687  1.00 11.02 ? 53   ASN D C   1 
ATOM   5479 O  O   . ASN D  1 53  ? 52.909  1.431   -2.507  1.00 11.32 ? 53   ASN D O   1 
ATOM   5480 C  CB  . ASN D  1 53  ? 52.018  3.971   -0.783  1.00 8.96  ? 53   ASN D CB  1 
ATOM   5481 C  CG  . ASN D  1 53  ? 51.089  4.978   -0.128  1.00 9.79  ? 53   ASN D CG  1 
ATOM   5482 O  OD1 . ASN D  1 53  ? 49.899  4.731   0.040   1.00 10.45 ? 53   ASN D OD1 1 
ATOM   5483 N  ND2 . ASN D  1 53  ? 51.643  6.125   0.255   1.00 8.54  ? 53   ASN D ND2 1 
ATOM   5484 N  N   . THR D  1 54  ? 52.126  3.058   -3.841  1.00 9.79  ? 54   THR D N   1 
ATOM   5485 C  CA  . THR D  1 54  ? 53.056  2.720   -4.919  1.00 11.28 ? 54   THR D CA  1 
ATOM   5486 C  C   . THR D  1 54  ? 53.807  3.974   -5.340  1.00 13.87 ? 54   THR D C   1 
ATOM   5487 O  O   . THR D  1 54  ? 53.496  5.074   -4.882  1.00 12.22 ? 54   THR D O   1 
ATOM   5488 C  CB  . THR D  1 54  ? 52.343  2.085   -6.135  1.00 14.77 ? 54   THR D CB  1 
ATOM   5489 O  OG1 . THR D  1 54  ? 51.429  3.030   -6.699  1.00 15.70 ? 54   THR D OG1 1 
ATOM   5490 C  CG2 . THR D  1 54  ? 51.571  0.831   -5.711  1.00 13.57 ? 54   THR D CG2 1 
ATOM   5491 N  N   . GLN D  1 55  ? 54.804  3.814   -6.204  1.00 13.87 ? 55   GLN D N   1 
ATOM   5492 C  CA  . GLN D  1 55  ? 55.636  4.954   -6.576  1.00 17.07 ? 55   GLN D CA  1 
ATOM   5493 C  C   . GLN D  1 55  ? 54.787  6.080   -7.161  1.00 14.81 ? 55   GLN D C   1 
ATOM   5494 O  O   . GLN D  1 55  ? 54.109  5.891   -8.172  1.00 16.05 ? 55   GLN D O   1 
ATOM   5495 C  CB  . GLN D  1 55  ? 56.730  4.537   -7.561  1.00 19.31 ? 55   GLN D CB  1 
ATOM   5496 C  CG  . GLN D  1 55  ? 57.815  5.589   -7.719  1.00 28.05 ? 55   GLN D CG  1 
ATOM   5497 C  CD  . GLN D  1 55  ? 58.573  5.827   -6.422  1.00 21.59 ? 55   GLN D CD  1 
ATOM   5498 O  OE1 . GLN D  1 55  ? 58.336  6.808   -5.722  1.00 26.77 ? 55   GLN D OE1 1 
ATOM   5499 N  NE2 . GLN D  1 55  ? 59.479  4.913   -6.091  1.00 37.33 ? 55   GLN D NE2 1 
ATOM   5500 N  N   . GLY D  1 56  ? 54.812  7.241   -6.503  1.00 14.46 ? 56   GLY D N   1 
ATOM   5501 C  CA  . GLY D  1 56  ? 54.055  8.402   -6.936  1.00 18.37 ? 56   GLY D CA  1 
ATOM   5502 C  C   . GLY D  1 56  ? 52.565  8.396   -6.615  1.00 18.48 ? 56   GLY D C   1 
ATOM   5503 O  O   . GLY D  1 56  ? 51.841  9.319   -6.999  1.00 15.21 ? 56   GLY D O   1 
ATOM   5504 N  N   . ARG D  1 57  ? 52.100  7.373   -5.902  1.00 15.53 ? 57   ARG D N   1 
ATOM   5505 C  CA  . ARG D  1 57  ? 50.672  7.230   -5.640  1.00 10.40 ? 57   ARG D CA  1 
ATOM   5506 C  C   . ARG D  1 57  ? 50.373  6.973   -4.169  1.00 12.72 ? 57   ARG D C   1 
ATOM   5507 O  O   . ARG D  1 57  ? 50.698  5.906   -3.638  1.00 13.49 ? 57   ARG D O   1 
ATOM   5508 C  CB  . ARG D  1 57  ? 50.079  6.116   -6.499  1.00 11.24 ? 57   ARG D CB  1 
ATOM   5509 C  CG  . ARG D  1 57  ? 50.220  6.375   -8.000  1.00 15.98 ? 57   ARG D CG  1 
ATOM   5510 C  CD  . ARG D  1 57  ? 49.436  5.378   -8.831  1.00 19.29 ? 57   ARG D CD  1 
ATOM   5511 N  NE  . ARG D  1 57  ? 47.997  5.629   -8.774  1.00 21.94 ? 57   ARG D NE  1 
ATOM   5512 C  CZ  . ARG D  1 57  ? 47.368  6.570   -9.476  1.00 23.71 ? 57   ARG D CZ  1 
ATOM   5513 N  NH1 . ARG D  1 57  ? 48.049  7.373   -10.291 1.00 24.95 ? 57   ARG D NH1 1 
ATOM   5514 N  NH2 . ARG D  1 57  ? 46.054  6.719   -9.356  1.00 23.04 ? 57   ARG D NH2 1 
ATOM   5515 N  N   . ASP D  1 58  ? 49.750  7.954   -3.526  1.00 10.44 ? 58   ASP D N   1 
ATOM   5516 C  CA  . ASP D  1 58  ? 49.342  7.813   -2.122  1.00 10.33 ? 58   ASP D CA  1 
ATOM   5517 C  C   . ASP D  1 58  ? 47.987  7.139   -2.017  1.00 9.42  ? 58   ASP D C   1 
ATOM   5518 O  O   . ASP D  1 58  ? 47.127  7.310   -2.882  1.00 11.39 ? 58   ASP D O   1 
ATOM   5519 C  CB  . ASP D  1 58  ? 49.252  9.186   -1.456  1.00 10.28 ? 58   ASP D CB  1 
ATOM   5520 C  CG  . ASP D  1 58  ? 49.001  9.098   0.033   1.00 10.56 ? 58   ASP D CG  1 
ATOM   5521 O  OD1 . ASP D  1 58  ? 49.694  8.300   0.695   1.00 12.27 ? 58   ASP D OD1 1 
ATOM   5522 O  OD2 . ASP D  1 58  ? 48.130  9.846   0.538   1.00 11.65 ? 58   ASP D OD2 1 
ATOM   5523 N  N   . ASN D  1 59  ? 47.789  6.388   -0.936  1.00 9.19  ? 59   ASN D N   1 
ATOM   5524 C  CA  . ASN D  1 59  ? 46.487  5.772   -0.673  1.00 9.24  ? 59   ASN D CA  1 
ATOM   5525 C  C   . ASN D  1 59  ? 46.012  4.962   -1.868  1.00 8.55  ? 59   ASN D C   1 
ATOM   5526 O  O   . ASN D  1 59  ? 44.843  5.024   -2.257  1.00 9.69  ? 59   ASN D O   1 
ATOM   5527 C  CB  . ASN D  1 59  ? 45.445  6.827   -0.284  1.00 9.67  ? 59   ASN D CB  1 
ATOM   5528 C  CG  . ASN D  1 59  ? 45.837  7.592   0.958   1.00 10.24 ? 59   ASN D CG  1 
ATOM   5529 O  OD1 . ASN D  1 59  ? 46.835  7.267   1.604   1.00 10.21 ? 59   ASN D OD1 1 
ATOM   5530 N  ND2 . ASN D  1 59  ? 45.063  8.615   1.299   1.00 12.16 ? 59   ASN D ND2 1 
ATOM   5531 N  N   . GLU D  1 60  ? 46.935  4.198   -2.448  1.00 10.69 ? 60   GLU D N   1 
ATOM   5532 C  CA  . GLU D  1 60  ? 46.630  3.365   -3.606  1.00 10.66 ? 60   GLU D CA  1 
ATOM   5533 C  C   . GLU D  1 60  ? 45.656  2.265   -3.179  1.00 11.79 ? 60   GLU D C   1 
ATOM   5534 O  O   . GLU D  1 60  ? 44.728  1.928   -3.899  1.00 10.14 ? 60   GLU D O   1 
ATOM   5535 C  CB  . GLU D  1 60  ? 47.924  2.795   -4.207  1.00 11.25 ? 60   GLU D CB  1 
ATOM   5536 C  CG  . GLU D  1 60  ? 47.732  2.015   -5.516  1.00 11.65 ? 60   GLU D CG  1 
ATOM   5537 C  CD  . GLU D  1 60  ? 47.148  2.844   -6.658  1.00 14.21 ? 60   GLU D CD  1 
ATOM   5538 O  OE1 . GLU D  1 60  ? 47.058  4.085   -6.545  1.00 15.86 ? 60   GLU D OE1 1 
ATOM   5539 O  OE2 . GLU D  1 60  ? 46.781  2.237   -7.687  1.00 14.23 ? 60   GLU D OE2 1 
ATOM   5540 N  N   . LEU D  1 61  ? 45.867  1.728   -1.982  1.00 9.73  ? 61   LEU D N   1 
ATOM   5541 C  CA  . LEU D  1 61  ? 44.905  0.819   -1.365  1.00 9.74  ? 61   LEU D CA  1 
ATOM   5542 C  C   . LEU D  1 61  ? 45.067  1.046   0.128   1.00 7.60  ? 61   LEU D C   1 
ATOM   5543 O  O   . LEU D  1 61  ? 46.110  0.741   0.698   1.00 9.79  ? 61   LEU D O   1 
ATOM   5544 C  CB  . LEU D  1 61  ? 45.206  -0.630  -1.747  1.00 8.12  ? 61   LEU D CB  1 
ATOM   5545 C  CG  . LEU D  1 61  ? 44.187  -1.734  -1.413  1.00 11.10 ? 61   LEU D CG  1 
ATOM   5546 C  CD1 . LEU D  1 61  ? 44.621  -3.059  -2.019  1.00 12.61 ? 61   LEU D CD1 1 
ATOM   5547 C  CD2 . LEU D  1 61  ? 44.000  -1.888  0.088   1.00 9.58  ? 61   LEU D CD2 1 
ATOM   5548 N  N   . LEU D  1 62  ? 44.060  1.646   0.752   1.00 6.49  ? 62   LEU D N   1 
ATOM   5549 C  CA  . LEU D  1 62  ? 44.148  1.974   2.170   1.00 6.49  ? 62   LEU D CA  1 
ATOM   5550 C  C   . LEU D  1 62  ? 42.869  1.578   2.910   1.00 6.84  ? 62   LEU D C   1 
ATOM   5551 O  O   . LEU D  1 62  ? 41.758  1.904   2.480   1.00 9.62  ? 62   LEU D O   1 
ATOM   5552 C  CB  . LEU D  1 62  ? 44.427  3.479   2.349   1.00 8.15  ? 62   LEU D CB  1 
ATOM   5553 C  CG  . LEU D  1 62  ? 44.326  4.068   3.763   1.00 8.48  ? 62   LEU D CG  1 
ATOM   5554 C  CD1 . LEU D  1 62  ? 45.397  3.520   4.701   1.00 11.28 ? 62   LEU D CD1 1 
ATOM   5555 C  CD2 . LEU D  1 62  ? 44.415  5.595   3.688   1.00 9.97  ? 62   LEU D CD2 1 
ATOM   5556 N  N   . VAL D  1 63  ? 43.033  0.847   4.010   1.00 6.79  ? 63   VAL D N   1 
ATOM   5557 C  CA  . VAL D  1 63  ? 41.914  0.538   4.897   1.00 7.42  ? 63   VAL D CA  1 
ATOM   5558 C  C   . VAL D  1 63  ? 42.123  1.375   6.142   1.00 9.12  ? 63   VAL D C   1 
ATOM   5559 O  O   . VAL D  1 63  ? 43.137  1.226   6.822   1.00 8.17  ? 63   VAL D O   1 
ATOM   5560 C  CB  . VAL D  1 63  ? 41.881  -0.956  5.285   1.00 8.69  ? 63   VAL D CB  1 
ATOM   5561 C  CG1 . VAL D  1 63  ? 40.690  -1.218  6.239   1.00 10.23 ? 63   VAL D CG1 1 
ATOM   5562 C  CG2 . VAL D  1 63  ? 41.767  -1.807  4.034   1.00 10.41 ? 63   VAL D CG2 1 
ATOM   5563 N  N   . TYR D  1 64  ? 41.162  2.252   6.427   1.00 7.11  ? 64   TYR D N   1 
ATOM   5564 C  CA  . TYR D  1 64  ? 41.351  3.319   7.397   1.00 9.43  ? 64   TYR D CA  1 
ATOM   5565 C  C   . TYR D  1 64  ? 40.137  3.366   8.308   1.00 10.06 ? 64   TYR D C   1 
ATOM   5566 O  O   . TYR D  1 64  ? 39.009  3.239   7.843   1.00 10.43 ? 64   TYR D O   1 
ATOM   5567 C  CB  . TYR D  1 64  ? 41.481  4.644   6.632   1.00 7.70  ? 64   TYR D CB  1 
ATOM   5568 C  CG  . TYR D  1 64  ? 41.981  5.818   7.434   1.00 8.76  ? 64   TYR D CG  1 
ATOM   5569 C  CD1 . TYR D  1 64  ? 43.324  5.934   7.769   1.00 10.72 ? 64   TYR D CD1 1 
ATOM   5570 C  CD2 . TYR D  1 64  ? 41.118  6.838   7.815   1.00 12.63 ? 64   TYR D CD2 1 
ATOM   5571 C  CE1 . TYR D  1 64  ? 43.795  7.026   8.496   1.00 10.13 ? 64   TYR D CE1 1 
ATOM   5572 C  CE2 . TYR D  1 64  ? 41.578  7.931   8.530   1.00 15.51 ? 64   TYR D CE2 1 
ATOM   5573 C  CZ  . TYR D  1 64  ? 42.914  8.021   8.861   1.00 13.02 ? 64   TYR D CZ  1 
ATOM   5574 O  OH  . TYR D  1 64  ? 43.357  9.115   9.576   1.00 15.48 ? 64   TYR D OH  1 
ATOM   5575 N  N   . LYS D  1 65  ? 40.364  3.549   9.605   1.00 9.56  ? 65   LYS D N   1 
ATOM   5576 C  CA  . LYS D  1 65  ? 39.266  3.652   10.565  1.00 10.14 ? 65   LYS D CA  1 
ATOM   5577 C  C   . LYS D  1 65  ? 39.125  5.100   11.038  1.00 9.99  ? 65   LYS D C   1 
ATOM   5578 O  O   . LYS D  1 65  ? 39.933  5.572   11.836  1.00 12.14 ? 65   LYS D O   1 
ATOM   5579 C  CB  . LYS D  1 65  ? 39.551  2.752   11.764  1.00 9.24  ? 65   LYS D CB  1 
ATOM   5580 C  CG  . LYS D  1 65  ? 38.392  2.622   12.738  1.00 16.22 ? 65   LYS D CG  1 
ATOM   5581 C  CD  . LYS D  1 65  ? 37.477  1.500   12.324  1.00 18.02 ? 65   LYS D CD  1 
ATOM   5582 C  CE  . LYS D  1 65  ? 36.288  1.371   13.271  1.00 16.40 ? 65   LYS D CE  1 
ATOM   5583 N  NZ  . LYS D  1 65  ? 36.686  1.141   14.686  1.00 15.76 ? 65   LYS D NZ  1 
ATOM   5584 N  N   A GLU D  1 66  ? 38.063  5.742   10.552  0.56 14.31 ? 66   GLU D N   1 
ATOM   5585 N  N   B GLU D  1 66  ? 38.132  5.844   10.560  0.44 14.39 ? 66   GLU D N   1 
ATOM   5586 C  CA  A GLU D  1 66  ? 37.749  7.148   10.782  0.56 18.61 ? 66   GLU D CA  1 
ATOM   5587 C  CA  B GLU D  1 66  ? 38.072  7.251   10.969  0.44 16.69 ? 66   GLU D CA  1 
ATOM   5588 C  C   A GLU D  1 66  ? 37.422  7.418   12.241  0.56 15.30 ? 66   GLU D C   1 
ATOM   5589 C  C   B GLU D  1 66  ? 37.521  7.407   12.385  0.44 15.34 ? 66   GLU D C   1 
ATOM   5590 O  O   A GLU D  1 66  ? 37.882  8.391   12.843  0.56 16.35 ? 66   GLU D O   1 
ATOM   5591 O  O   B GLU D  1 66  ? 37.933  8.312   13.113  0.44 16.74 ? 66   GLU D O   1 
ATOM   5592 C  CB  A GLU D  1 66  ? 36.509  7.505   9.955   0.56 17.56 ? 66   GLU D CB  1 
ATOM   5593 C  CB  B GLU D  1 66  ? 37.265  8.120   9.999   0.44 18.27 ? 66   GLU D CB  1 
ATOM   5594 C  CG  A GLU D  1 66  ? 36.574  7.058   8.495   0.56 20.49 ? 66   GLU D CG  1 
ATOM   5595 C  CG  B GLU D  1 66  ? 37.168  7.582   8.604   0.44 22.72 ? 66   GLU D CG  1 
ATOM   5596 C  CD  A GLU D  1 66  ? 37.504  7.930   7.678   0.56 18.76 ? 66   GLU D CD  1 
ATOM   5597 C  CD  B GLU D  1 66  ? 36.016  6.625   8.479   0.44 17.96 ? 66   GLU D CD  1 
ATOM   5598 O  OE1 A GLU D  1 66  ? 37.966  8.947   8.236   0.56 18.26 ? 66   GLU D OE1 1 
ATOM   5599 O  OE1 B GLU D  1 66  ? 34.856  7.101   8.440   0.44 21.10 ? 66   GLU D OE1 1 
ATOM   5600 O  OE2 A GLU D  1 66  ? 37.774  7.609   6.495   0.56 17.29 ? 66   GLU D OE2 1 
ATOM   5601 O  OE2 B GLU D  1 66  ? 36.275  5.404   8.435   0.44 10.23 ? 66   GLU D OE2 1 
ATOM   5602 N  N   . ARG D  1 67  ? 36.596  6.535   12.775  1.00 11.60 ? 67   ARG D N   1 
ATOM   5603 C  CA  . ARG D  1 67  ? 36.047  6.615   14.121  1.00 10.35 ? 67   ARG D CA  1 
ATOM   5604 C  C   . ARG D  1 67  ? 35.304  5.325   14.389  1.00 12.79 ? 67   ARG D C   1 
ATOM   5605 O  O   . ARG D  1 67  ? 35.103  4.523   13.479  1.00 13.60 ? 67   ARG D O   1 
ATOM   5606 C  CB  . ARG D  1 67  ? 35.090  7.806   14.221  1.00 13.88 ? 67   ARG D CB  1 
ATOM   5607 C  CG  . ARG D  1 67  ? 33.954  7.771   13.206  1.00 13.39 ? 67   ARG D CG  1 
ATOM   5608 C  CD  . ARG D  1 67  ? 33.060  9.007   13.331  1.00 22.14 ? 67   ARG D CD  1 
ATOM   5609 N  NE  . ARG D  1 67  ? 33.816  10.241  13.127  1.00 21.11 ? 67   ARG D NE  1 
ATOM   5610 C  CZ  . ARG D  1 67  ? 34.106  10.752  11.936  1.00 25.81 ? 67   ARG D CZ  1 
ATOM   5611 N  NH1 . ARG D  1 67  ? 33.706  10.140  10.829  1.00 26.29 ? 67   ARG D NH1 1 
ATOM   5612 N  NH2 . ARG D  1 67  ? 34.804  11.879  11.850  1.00 35.86 ? 67   ARG D NH2 1 
ATOM   5613 N  N   A VAL D  1 68  ? 34.891  5.114   15.635  0.47 12.73 ? 68   VAL D N   1 
ATOM   5614 N  N   B VAL D  1 68  ? 34.894  5.110   15.634  0.53 12.72 ? 68   VAL D N   1 
ATOM   5615 C  CA  A VAL D  1 68  ? 34.117  3.922   15.962  0.47 13.16 ? 68   VAL D CA  1 
ATOM   5616 C  CA  B VAL D  1 68  ? 34.128  3.914   15.967  0.53 13.16 ? 68   VAL D CA  1 
ATOM   5617 C  C   A VAL D  1 68  ? 32.958  3.752   14.993  0.47 12.68 ? 68   VAL D C   1 
ATOM   5618 C  C   B VAL D  1 68  ? 32.938  3.742   15.031  0.53 12.66 ? 68   VAL D C   1 
ATOM   5619 O  O   A VAL D  1 68  ? 32.286  4.721   14.633  0.47 13.73 ? 68   VAL D O   1 
ATOM   5620 O  O   B VAL D  1 68  ? 32.224  4.701   14.733  0.53 13.77 ? 68   VAL D O   1 
ATOM   5621 C  CB  A VAL D  1 68  ? 33.562  3.939   17.406  0.47 15.66 ? 68   VAL D CB  1 
ATOM   5622 C  CB  B VAL D  1 68  ? 33.628  3.930   17.424  0.53 15.65 ? 68   VAL D CB  1 
ATOM   5623 C  CG1 A VAL D  1 68  ? 34.677  3.728   18.405  0.47 21.67 ? 68   VAL D CG1 1 
ATOM   5624 C  CG1 B VAL D  1 68  ? 32.641  2.792   17.658  0.53 11.91 ? 68   VAL D CG1 1 
ATOM   5625 C  CG2 A VAL D  1 68  ? 32.799  5.228   17.684  0.47 10.89 ? 68   VAL D CG2 1 
ATOM   5626 C  CG2 B VAL D  1 68  ? 34.792  3.811   18.369  0.53 21.78 ? 68   VAL D CG2 1 
ATOM   5627 N  N   . GLY D  1 69  ? 32.746  2.515   14.558  1.00 11.89 ? 69   GLY D N   1 
ATOM   5628 C  CA  . GLY D  1 69  ? 31.612  2.185   13.720  1.00 11.13 ? 69   GLY D CA  1 
ATOM   5629 C  C   . GLY D  1 69  ? 31.698  2.580   12.259  1.00 11.61 ? 69   GLY D C   1 
ATOM   5630 O  O   . GLY D  1 69  ? 30.705  2.448   11.541  1.00 13.42 ? 69   GLY D O   1 
ATOM   5631 N  N   . GLU D  1 70  ? 32.858  3.061   11.814  1.00 8.48  ? 70   GLU D N   1 
ATOM   5632 C  CA  . GLU D  1 70  ? 33.006  3.521   10.428  1.00 13.65 ? 70   GLU D CA  1 
ATOM   5633 C  C   . GLU D  1 70  ? 34.313  3.048   9.799   1.00 10.59 ? 70   GLU D C   1 
ATOM   5634 O  O   . GLU D  1 70  ? 35.400  3.370   10.279  1.00 12.72 ? 70   GLU D O   1 
ATOM   5635 C  CB  . GLU D  1 70  ? 32.947  5.049   10.331  1.00 12.59 ? 70   GLU D CB  1 
ATOM   5636 C  CG  . GLU D  1 70  ? 31.644  5.656   10.828  1.00 19.30 ? 70   GLU D CG  1 
ATOM   5637 C  CD  . GLU D  1 70  ? 31.561  7.154   10.596  1.00 24.19 ? 70   GLU D CD  1 
ATOM   5638 O  OE1 . GLU D  1 70  ? 30.552  7.760   11.019  1.00 29.91 ? 70   GLU D OE1 1 
ATOM   5639 O  OE2 . GLU D  1 70  ? 32.495  7.728   9.998   1.00 21.81 ? 70   GLU D OE2 1 
ATOM   5640 N  N   . TYR D  1 71  ? 34.192  2.319   8.701   1.00 6.53  ? 71   TYR D N   1 
ATOM   5641 C  CA  . TYR D  1 71  ? 35.342  1.757   7.998   1.00 10.74 ? 71   TYR D CA  1 
ATOM   5642 C  C   . TYR D  1 71  ? 35.440  2.355   6.603   1.00 9.60  ? 71   TYR D C   1 
ATOM   5643 O  O   . TYR D  1 71  ? 34.436  2.443   5.895   1.00 11.09 ? 71   TYR D O   1 
ATOM   5644 C  CB  . TYR D  1 71  ? 35.218  0.229   7.917   1.00 10.96 ? 71   TYR D CB  1 
ATOM   5645 C  CG  . TYR D  1 71  ? 35.354  -0.419  9.269   1.00 9.50  ? 71   TYR D CG  1 
ATOM   5646 C  CD1 . TYR D  1 71  ? 34.253  -0.572  10.104  1.00 9.62  ? 71   TYR D CD1 1 
ATOM   5647 C  CD2 . TYR D  1 71  ? 36.596  -0.821  9.733   1.00 12.29 ? 71   TYR D CD2 1 
ATOM   5648 C  CE1 . TYR D  1 71  ? 34.392  -1.157  11.371  1.00 11.84 ? 71   TYR D CE1 1 
ATOM   5649 C  CE2 . TYR D  1 71  ? 36.742  -1.398  10.986  1.00 14.00 ? 71   TYR D CE2 1 
ATOM   5650 C  CZ  . TYR D  1 71  ? 35.641  -1.554  11.797  1.00 13.75 ? 71   TYR D CZ  1 
ATOM   5651 O  OH  . TYR D  1 71  ? 35.814  -2.125  13.033  1.00 13.86 ? 71   TYR D OH  1 
ATOM   5652 N  N   . SER D  1 72  ? 36.645  2.777   6.212   1.00 7.38  ? 72   SER D N   1 
ATOM   5653 C  CA  . SER D  1 72  ? 36.859  3.339   4.884   1.00 9.55  ? 72   SER D CA  1 
ATOM   5654 C  C   . SER D  1 72  ? 37.842  2.509   4.081   1.00 7.39  ? 72   SER D C   1 
ATOM   5655 O  O   . SER D  1 72  ? 38.807  1.956   4.629   1.00 9.61  ? 72   SER D O   1 
ATOM   5656 C  CB  . SER D  1 72  ? 37.420  4.761   4.982   1.00 10.38 ? 72   SER D CB  1 
ATOM   5657 O  OG  . SER D  1 72  ? 36.468  5.630   5.547   1.00 12.03 ? 72   SER D OG  1 
ATOM   5658 N  N   . LEU D  1 73  ? 37.596  2.442   2.778   1.00 6.47  ? 73   LEU D N   1 
ATOM   5659 C  CA  . LEU D  1 73  ? 38.542  1.853   1.839   1.00 6.34  ? 73   LEU D CA  1 
ATOM   5660 C  C   . LEU D  1 73  ? 38.900  2.939   0.838   1.00 9.81  ? 73   LEU D C   1 
ATOM   5661 O  O   . LEU D  1 73  ? 38.006  3.597   0.284   1.00 10.74 ? 73   LEU D O   1 
ATOM   5662 C  CB  . LEU D  1 73  ? 37.901  0.692   1.080   1.00 6.95  ? 73   LEU D CB  1 
ATOM   5663 C  CG  . LEU D  1 73  ? 38.770  0.114   -0.055  1.00 8.78  ? 73   LEU D CG  1 
ATOM   5664 C  CD1 . LEU D  1 73  ? 40.038  -0.489  0.507   1.00 12.09 ? 73   LEU D CD1 1 
ATOM   5665 C  CD2 . LEU D  1 73  ? 37.986  -0.925  -0.879  1.00 7.51  ? 73   LEU D CD2 1 
ATOM   5666 N  N   . TYR D  1 74  ? 40.197  3.136   0.620   1.00 7.47  ? 74   TYR D N   1 
ATOM   5667 C  CA  . TYR D  1 74  ? 40.671  3.964   -0.486  1.00 8.45  ? 74   TYR D CA  1 
ATOM   5668 C  C   . TYR D  1 74  ? 41.200  3.082   -1.605  1.00 7.76  ? 74   TYR D C   1 
ATOM   5669 O  O   . TYR D  1 74  ? 41.911  2.104   -1.360  1.00 8.64  ? 74   TYR D O   1 
ATOM   5670 C  CB  . TYR D  1 74  ? 41.809  4.899   -0.054  1.00 8.17  ? 74   TYR D CB  1 
ATOM   5671 C  CG  . TYR D  1 74  ? 41.419  5.937   0.958   1.00 11.78 ? 74   TYR D CG  1 
ATOM   5672 C  CD1 . TYR D  1 74  ? 41.059  5.571   2.248   1.00 10.94 ? 74   TYR D CD1 1 
ATOM   5673 C  CD2 . TYR D  1 74  ? 41.443  7.292   0.637   1.00 13.60 ? 74   TYR D CD2 1 
ATOM   5674 C  CE1 . TYR D  1 74  ? 40.705  6.519   3.190   1.00 15.36 ? 74   TYR D CE1 1 
ATOM   5675 C  CE2 . TYR D  1 74  ? 41.095  8.253   1.584   1.00 18.12 ? 74   TYR D CE2 1 
ATOM   5676 C  CZ  . TYR D  1 74  ? 40.725  7.851   2.856   1.00 19.04 ? 74   TYR D CZ  1 
ATOM   5677 O  OH  . TYR D  1 74  ? 40.374  8.779   3.816   1.00 20.53 ? 74   TYR D OH  1 
ATOM   5678 N  N   . ILE D  1 75  ? 40.855  3.441   -2.839  1.00 8.02  ? 75   ILE D N   1 
ATOM   5679 C  CA  . ILE D  1 75  ? 41.430  2.811   -4.016  1.00 8.92  ? 75   ILE D CA  1 
ATOM   5680 C  C   . ILE D  1 75  ? 41.917  3.949   -4.900  1.00 11.10 ? 75   ILE D C   1 
ATOM   5681 O  O   . ILE D  1 75  ? 41.128  4.792   -5.312  1.00 11.01 ? 75   ILE D O   1 
ATOM   5682 C  CB  . ILE D  1 75  ? 40.380  1.996   -4.797  1.00 9.78  ? 75   ILE D CB  1 
ATOM   5683 C  CG1 . ILE D  1 75  ? 39.853  0.828   -3.952  1.00 10.49 ? 75   ILE D CG1 1 
ATOM   5684 C  CG2 . ILE D  1 75  ? 40.970  1.483   -6.111  1.00 12.27 ? 75   ILE D CG2 1 
ATOM   5685 C  CD1 . ILE D  1 75  ? 40.899  -0.231  -3.647  1.00 10.80 ? 75   ILE D CD1 1 
ATOM   5686 N  N   . GLY D  1 76  ? 43.214  3.987   -5.181  1.00 13.52 ? 76   GLY D N   1 
ATOM   5687 C  CA  . GLY D  1 76  ? 43.768  5.078   -5.970  1.00 15.29 ? 76   GLY D CA  1 
ATOM   5688 C  C   . GLY D  1 76  ? 43.321  6.458   -5.511  1.00 13.78 ? 76   GLY D C   1 
ATOM   5689 O  O   . GLY D  1 76  ? 42.892  7.284   -6.324  1.00 14.28 ? 76   GLY D O   1 
ATOM   5690 N  N   . ARG D  1 77  ? 43.416  6.698   -4.203  1.00 9.62  ? 77   ARG D N   1 
ATOM   5691 C  CA  . ARG D  1 77  ? 43.072  7.980   -3.580  1.00 10.42 ? 77   ARG D CA  1 
ATOM   5692 C  C   . ARG D  1 77  ? 41.580  8.271   -3.401  1.00 13.74 ? 77   ARG D C   1 
ATOM   5693 O  O   . ARG D  1 77  ? 41.222  9.156   -2.632  1.00 19.15 ? 77   ARG D O   1 
ATOM   5694 C  CB  . ARG D  1 77  ? 43.754  9.166   -4.302  1.00 15.04 ? 77   ARG D CB  1 
ATOM   5695 C  CG  . ARG D  1 77  ? 45.239  9.273   -4.102  1.00 27.47 ? 77   ARG D CG  1 
ATOM   5696 C  CD  . ARG D  1 77  ? 45.755  10.656  -4.512  1.00 26.91 ? 77   ARG D CD  1 
ATOM   5697 N  NE  . ARG D  1 77  ? 45.833  11.574  -3.374  1.00 28.92 ? 77   ARG D NE  1 
ATOM   5698 C  CZ  . ARG D  1 77  ? 46.100  12.876  -3.474  1.00 35.10 ? 77   ARG D CZ  1 
ATOM   5699 N  NH1 . ARG D  1 77  ? 46.301  13.430  -4.663  1.00 30.01 ? 77   ARG D NH1 1 
ATOM   5700 N  NH2 . ARG D  1 77  ? 46.158  13.629  -2.381  1.00 24.83 ? 77   ARG D NH2 1 
ATOM   5701 N  N   . HIS D  1 78  ? 40.720  7.537   -4.105  1.00 10.67 ? 78   HIS D N   1 
ATOM   5702 C  CA  . HIS D  1 78  ? 39.273  7.701   -3.968  1.00 8.91  ? 78   HIS D CA  1 
ATOM   5703 C  C   . HIS D  1 78  ? 38.816  6.900   -2.751  1.00 10.04 ? 78   HIS D C   1 
ATOM   5704 O  O   . HIS D  1 78  ? 39.433  5.902   -2.413  1.00 11.81 ? 78   HIS D O   1 
ATOM   5705 C  CB  . HIS D  1 78  ? 38.547  7.165   -5.209  1.00 11.06 ? 78   HIS D CB  1 
ATOM   5706 C  CG  . HIS D  1 78  ? 38.827  7.936   -6.467  1.00 14.21 ? 78   HIS D CG  1 
ATOM   5707 N  ND1 . HIS D  1 78  ? 37.978  7.913   -7.553  1.00 18.14 ? 78   HIS D ND1 1 
ATOM   5708 C  CD2 . HIS D  1 78  ? 39.851  8.758   -6.806  1.00 19.12 ? 78   HIS D CD2 1 
ATOM   5709 C  CE1 . HIS D  1 78  ? 38.471  8.679   -8.512  1.00 22.53 ? 78   HIS D CE1 1 
ATOM   5710 N  NE2 . HIS D  1 78  ? 39.606  9.202   -8.085  1.00 16.81 ? 78   HIS D NE2 1 
ATOM   5711 N  N   . LYS D  1 79  ? 37.747  7.330   -2.094  1.00 9.12  ? 79   LYS D N   1 
ATOM   5712 C  CA  . LYS D  1 79  ? 37.330  6.619   -0.890  1.00 11.14 ? 79   LYS D CA  1 
ATOM   5713 C  C   . LYS D  1 79  ? 35.848  6.316   -0.820  1.00 11.68 ? 79   LYS D C   1 
ATOM   5714 O  O   . LYS D  1 79  ? 35.007  7.037   -1.390  1.00 12.25 ? 79   LYS D O   1 
ATOM   5715 C  CB  . LYS D  1 79  ? 37.768  7.358   0.376   1.00 18.54 ? 79   LYS D CB  1 
ATOM   5716 C  CG  . LYS D  1 79  ? 37.007  8.617   0.658   1.00 24.03 ? 79   LYS D CG  1 
ATOM   5717 C  CD  . LYS D  1 79  ? 37.541  9.306   1.909   1.00 24.19 ? 79   LYS D CD  1 
ATOM   5718 C  CE  . LYS D  1 79  ? 37.170  8.538   3.162   1.00 21.22 ? 79   LYS D CE  1 
ATOM   5719 N  NZ  . LYS D  1 79  ? 37.534  9.284   4.402   1.00 34.84 ? 79   LYS D NZ  1 
ATOM   5720 N  N   . VAL D  1 80  ? 35.546  5.215   -0.135  1.00 9.38  ? 80   VAL D N   1 
ATOM   5721 C  CA  . VAL D  1 80  ? 34.196  4.907   0.293   1.00 7.92  ? 80   VAL D CA  1 
ATOM   5722 C  C   . VAL D  1 80  ? 34.222  4.573   1.781   1.00 8.54  ? 80   VAL D C   1 
ATOM   5723 O  O   . VAL D  1 80  ? 35.254  4.182   2.316   1.00 10.00 ? 80   VAL D O   1 
ATOM   5724 C  CB  . VAL D  1 80  ? 33.577  3.715   -0.483  1.00 10.17 ? 80   VAL D CB  1 
ATOM   5725 C  CG1 . VAL D  1 80  ? 33.388  4.079   -1.961  1.00 10.18 ? 80   VAL D CG1 1 
ATOM   5726 C  CG2 . VAL D  1 80  ? 34.418  2.453   -0.312  1.00 10.03 ? 80   VAL D CG2 1 
ATOM   5727 N  N   . THR D  1 81  ? 33.078  4.735   2.435   1.00 8.16  ? 81   THR D N   1 
ATOM   5728 C  CA  . THR D  1 81  ? 32.957  4.501   3.868   1.00 6.53  ? 81   THR D CA  1 
ATOM   5729 C  C   . THR D  1 81  ? 31.629  3.825   4.146   1.00 8.45  ? 81   THR D C   1 
ATOM   5730 O  O   . THR D  1 81  ? 30.607  4.230   3.601   1.00 10.69 ? 81   THR D O   1 
ATOM   5731 C  CB  . THR D  1 81  ? 32.973  5.835   4.626   1.00 10.61 ? 81   THR D CB  1 
ATOM   5732 O  OG1 . THR D  1 81  ? 34.204  6.513   4.352   1.00 12.11 ? 81   THR D OG1 1 
ATOM   5733 C  CG2 . THR D  1 81  ? 32.845  5.597   6.108   1.00 13.62 ? 81   THR D CG2 1 
ATOM   5734 N  N   . SER D  1 82  ? 31.637  2.792   4.982   1.00 8.19  ? 82   SER D N   1 
ATOM   5735 C  CA  . SER D  1 82  ? 30.398  2.159   5.407   1.00 7.83  ? 82   SER D CA  1 
ATOM   5736 C  C   . SER D  1 82  ? 30.381  1.985   6.928   1.00 9.89  ? 82   SER D C   1 
ATOM   5737 O  O   . SER D  1 82  ? 31.426  1.877   7.578   1.00 10.01 ? 82   SER D O   1 
ATOM   5738 C  CB  . SER D  1 82  ? 30.168  0.808   4.713   1.00 13.81 ? 82   SER D CB  1 
ATOM   5739 O  OG  . SER D  1 82  ? 29.708  1.007   3.389   1.00 13.52 ? 82   SER D OG  1 
ATOM   5740 N  N   . LYS D  1 83  ? 29.172  1.958   7.476   1.00 7.41  ? 83   LYS D N   1 
ATOM   5741 C  CA  . LYS D  1 83  ? 28.978  2.006   8.917   1.00 9.01  ? 83   LYS D CA  1 
ATOM   5742 C  C   . LYS D  1 83  ? 28.541  0.675   9.489   1.00 11.19 ? 83   LYS D C   1 
ATOM   5743 O  O   . LYS D  1 83  ? 27.941  -0.155  8.793   1.00 10.72 ? 83   LYS D O   1 
ATOM   5744 C  CB  . LYS D  1 83  ? 27.930  3.066   9.256   1.00 8.88  ? 83   LYS D CB  1 
ATOM   5745 C  CG  . LYS D  1 83  ? 28.362  4.474   8.865   1.00 10.87 ? 83   LYS D CG  1 
ATOM   5746 C  CD  . LYS D  1 83  ? 27.315  5.503   9.274   1.00 17.50 ? 83   LYS D CD  1 
ATOM   5747 C  CE  . LYS D  1 83  ? 27.813  6.900   8.937   1.00 24.62 ? 83   LYS D CE  1 
ATOM   5748 N  NZ  . LYS D  1 83  ? 26.996  7.959   9.598   1.00 25.74 ? 83   LYS D NZ  1 
ATOM   5749 N  N   . VAL D  1 84  ? 28.832  0.466   10.769  1.00 8.28  ? 84   VAL D N   1 
ATOM   5750 C  CA  . VAL D  1 84  ? 28.388  -0.759  11.424  1.00 9.09  ? 84   VAL D CA  1 
ATOM   5751 C  C   . VAL D  1 84  ? 28.190  -0.498  12.899  1.00 10.19 ? 84   VAL D C   1 
ATOM   5752 O  O   . VAL D  1 84  ? 28.820  0.387   13.471  1.00 10.92 ? 84   VAL D O   1 
ATOM   5753 C  CB  . VAL D  1 84  ? 29.404  -1.919  11.223  1.00 9.16  ? 84   VAL D CB  1 
ATOM   5754 C  CG1 . VAL D  1 84  ? 30.722  -1.607  11.927  1.00 14.40 ? 84   VAL D CG1 1 
ATOM   5755 C  CG2 . VAL D  1 84  ? 28.816  -3.244  11.703  1.00 11.95 ? 84   VAL D CG2 1 
ATOM   5756 N  N   . ILE D  1 85  ? 27.289  -1.267  13.498  1.00 9.21  ? 85   ILE D N   1 
ATOM   5757 C  CA  . ILE D  1 85  ? 27.132  -1.287  14.946  1.00 10.65 ? 85   ILE D CA  1 
ATOM   5758 C  C   . ILE D  1 85  ? 28.239  -2.144  15.545  1.00 13.01 ? 85   ILE D C   1 
ATOM   5759 O  O   . ILE D  1 85  ? 28.355  -3.324  15.220  1.00 13.49 ? 85   ILE D O   1 
ATOM   5760 C  CB  . ILE D  1 85  ? 25.771  -1.903  15.329  1.00 11.67 ? 85   ILE D CB  1 
ATOM   5761 C  CG1 . ILE D  1 85  ? 24.630  -1.028  14.799  1.00 13.47 ? 85   ILE D CG1 1 
ATOM   5762 C  CG2 . ILE D  1 85  ? 25.688  -2.099  16.847  1.00 16.81 ? 85   ILE D CG2 1 
ATOM   5763 C  CD1 . ILE D  1 85  ? 23.263  -1.713  14.850  1.00 15.45 ? 85   ILE D CD1 1 
ATOM   5764 N  N   . GLU D  1 86  ? 29.064  -1.559  16.410  1.00 13.75 ? 86   GLU D N   1 
ATOM   5765 C  CA  . GLU D  1 86  ? 30.097  -2.347  17.093  1.00 10.70 ? 86   GLU D CA  1 
ATOM   5766 C  C   . GLU D  1 86  ? 30.310  -1.845  18.521  1.00 13.91 ? 86   GLU D C   1 
ATOM   5767 O  O   . GLU D  1 86  ? 30.040  -0.687  18.835  1.00 14.38 ? 86   GLU D O   1 
ATOM   5768 C  CB  . GLU D  1 86  ? 31.423  -2.341  16.320  1.00 17.99 ? 86   GLU D CB  1 
ATOM   5769 C  CG  . GLU D  1 86  ? 32.082  -0.968  16.234  1.00 21.77 ? 86   GLU D CG  1 
ATOM   5770 C  CD  . GLU D  1 86  ? 33.300  -0.944  15.319  1.00 20.25 ? 86   GLU D CD  1 
ATOM   5771 O  OE1 . GLU D  1 86  ? 33.575  -1.962  14.620  1.00 15.47 ? 86   GLU D OE1 1 
ATOM   5772 O  OE2 . GLU D  1 86  ? 33.975  0.115   15.299  1.00 15.98 ? 86   GLU D OE2 1 
ATOM   5773 N  N   . LYS D  1 87  ? 30.772  -2.738  19.382  1.00 12.80 ? 87   LYS D N   1 
ATOM   5774 C  CA  . LYS D  1 87  ? 31.108  -2.368  20.746  1.00 14.69 ? 87   LYS D CA  1 
ATOM   5775 C  C   . LYS D  1 87  ? 32.476  -1.721  20.745  1.00 13.83 ? 87   LYS D C   1 
ATOM   5776 O  O   . LYS D  1 87  ? 33.272  -1.947  19.837  1.00 16.58 ? 87   LYS D O   1 
ATOM   5777 C  CB  . LYS D  1 87  ? 31.148  -3.610  21.629  1.00 17.52 ? 87   LYS D CB  1 
ATOM   5778 C  CG  . LYS D  1 87  ? 29.776  -4.208  21.918  1.00 25.03 ? 87   LYS D CG  1 
ATOM   5779 C  CD  . LYS D  1 87  ? 29.917  -5.467  22.752  1.00 28.04 ? 87   LYS D CD  1 
ATOM   5780 C  CE  . LYS D  1 87  ? 28.657  -5.742  23.563  1.00 48.34 ? 87   LYS D CE  1 
ATOM   5781 N  NZ  . LYS D  1 87  ? 27.439  -5.794  22.712  1.00 44.12 ? 87   LYS D NZ  1 
ATOM   5782 N  N   . PHE D  1 88  ? 32.752  -0.924  21.770  1.00 13.24 ? 88   PHE D N   1 
ATOM   5783 C  CA  . PHE D  1 88  ? 34.068  -0.316  21.913  1.00 12.88 ? 88   PHE D CA  1 
ATOM   5784 C  C   . PHE D  1 88  ? 34.530  -0.252  23.374  1.00 10.57 ? 88   PHE D C   1 
ATOM   5785 O  O   . PHE D  1 88  ? 33.797  0.228   24.232  1.00 12.87 ? 88   PHE D O   1 
ATOM   5786 C  CB  . PHE D  1 88  ? 34.093  1.098   21.342  1.00 14.58 ? 88   PHE D CB  1 
ATOM   5787 C  CG  . PHE D  1 88  ? 35.354  1.835   21.676  1.00 14.87 ? 88   PHE D CG  1 
ATOM   5788 C  CD1 . PHE D  1 88  ? 36.502  1.642   20.925  1.00 12.72 ? 88   PHE D CD1 1 
ATOM   5789 C  CD2 . PHE D  1 88  ? 35.413  2.667   22.784  1.00 13.62 ? 88   PHE D CD2 1 
ATOM   5790 C  CE1 . PHE D  1 88  ? 37.673  2.292   21.252  1.00 13.57 ? 88   PHE D CE1 1 
ATOM   5791 C  CE2 . PHE D  1 88  ? 36.581  3.313   23.121  1.00 17.43 ? 88   PHE D CE2 1 
ATOM   5792 C  CZ  . PHE D  1 88  ? 37.719  3.125   22.346  1.00 14.98 ? 88   PHE D CZ  1 
ATOM   5793 N  N   . PRO D  1 89  ? 35.762  -0.714  23.651  1.00 9.34  ? 89   PRO D N   1 
ATOM   5794 C  CA  . PRO D  1 89  ? 36.652  -1.381  22.693  1.00 7.53  ? 89   PRO D CA  1 
ATOM   5795 C  C   . PRO D  1 89  ? 36.234  -2.828  22.505  1.00 11.43 ? 89   PRO D C   1 
ATOM   5796 O  O   . PRO D  1 89  ? 35.583  -3.405  23.381  1.00 11.51 ? 89   PRO D O   1 
ATOM   5797 C  CB  . PRO D  1 89  ? 38.027  -1.354  23.391  1.00 10.96 ? 89   PRO D CB  1 
ATOM   5798 C  CG  . PRO D  1 89  ? 37.854  -0.499  24.619  1.00 15.79 ? 89   PRO D CG  1 
ATOM   5799 C  CD  . PRO D  1 89  ? 36.413  -0.501  24.957  1.00 11.32 ? 89   PRO D CD  1 
ATOM   5800 N  N   . ALA D  1 90  ? 36.610  -3.413  21.373  1.00 10.53 ? 90   ALA D N   1 
ATOM   5801 C  CA  . ALA D  1 90  ? 36.323  -4.816  21.125  1.00 12.68 ? 90   ALA D CA  1 
ATOM   5802 C  C   . ALA D  1 90  ? 37.198  -5.343  20.003  1.00 8.21  ? 90   ALA D C   1 
ATOM   5803 O  O   . ALA D  1 90  ? 37.476  -4.632  19.046  1.00 10.77 ? 90   ALA D O   1 
ATOM   5804 C  CB  . ALA D  1 90  ? 34.859  -4.996  20.770  1.00 14.31 ? 90   ALA D CB  1 
ATOM   5805 N  N   . PRO D  1 91  ? 37.634  -6.597  20.123  1.00 8.99  ? 91   PRO D N   1 
ATOM   5806 C  CA  . PRO D  1 91  ? 38.329  -7.236  19.004  1.00 10.29 ? 91   PRO D CA  1 
ATOM   5807 C  C   . PRO D  1 91  ? 37.409  -7.238  17.798  1.00 11.39 ? 91   PRO D C   1 
ATOM   5808 O  O   . PRO D  1 91  ? 36.188  -7.330  17.954  1.00 11.13 ? 91   PRO D O   1 
ATOM   5809 C  CB  . PRO D  1 91  ? 38.510  -8.672  19.489  1.00 11.98 ? 91   PRO D CB  1 
ATOM   5810 C  CG  . PRO D  1 91  ? 38.536  -8.562  20.972  1.00 12.56 ? 91   PRO D CG  1 
ATOM   5811 C  CD  . PRO D  1 91  ? 37.545  -7.479  21.296  1.00 11.62 ? 91   PRO D CD  1 
ATOM   5812 N  N   . VAL D  1 92  ? 37.981  -7.140  16.608  1.00 7.17  ? 92   VAL D N   1 
ATOM   5813 C  CA  . VAL D  1 92  ? 37.180  -7.169  15.395  1.00 6.75  ? 92   VAL D CA  1 
ATOM   5814 C  C   . VAL D  1 92  ? 37.840  -8.045  14.338  1.00 8.23  ? 92   VAL D C   1 
ATOM   5815 O  O   . VAL D  1 92  ? 39.062  -8.140  14.282  1.00 10.72 ? 92   VAL D O   1 
ATOM   5816 C  CB  . VAL D  1 92  ? 36.961  -5.742  14.845  1.00 10.01 ? 92   VAL D CB  1 
ATOM   5817 C  CG1 . VAL D  1 92  ? 38.258  -5.160  14.305  1.00 13.06 ? 92   VAL D CG1 1 
ATOM   5818 C  CG2 . VAL D  1 92  ? 35.884  -5.743  13.765  1.00 12.98 ? 92   VAL D CG2 1 
ATOM   5819 N  N   . HIS D  1 93  ? 37.020  -8.694  13.511  1.00 6.86  ? 93   HIS D N   1 
ATOM   5820 C  CA  . HIS D  1 93  ? 37.527  -9.327  12.304  1.00 6.77  ? 93   HIS D CA  1 
ATOM   5821 C  C   . HIS D  1 93  ? 37.013  -8.529  11.106  1.00 6.44  ? 93   HIS D C   1 
ATOM   5822 O  O   . HIS D  1 93  ? 35.811  -8.254  10.993  1.00 7.67  ? 93   HIS D O   1 
ATOM   5823 C  CB  . HIS D  1 93  ? 37.079  -10.787 12.191  1.00 8.26  ? 93   HIS D CB  1 
ATOM   5824 C  CG  . HIS D  1 93  ? 37.625  -11.473 10.978  1.00 7.67  ? 93   HIS D CG  1 
ATOM   5825 N  ND1 . HIS D  1 93  ? 36.920  -11.567 9.798   1.00 9.00  ? 93   HIS D ND1 1 
ATOM   5826 C  CD2 . HIS D  1 93  ? 38.827  -12.054 10.745  1.00 12.47 ? 93   HIS D CD2 1 
ATOM   5827 C  CE1 . HIS D  1 93  ? 37.656  -12.195 8.899   1.00 9.45  ? 93   HIS D CE1 1 
ATOM   5828 N  NE2 . HIS D  1 93  ? 38.819  -12.499 9.448   1.00 8.11  ? 93   HIS D NE2 1 
ATOM   5829 N  N   . ILE D  1 94  ? 37.928  -8.146  10.224  1.00 6.91  ? 94   ILE D N   1 
ATOM   5830 C  CA  . ILE D  1 94  ? 37.583  -7.324  9.076   1.00 8.59  ? 94   ILE D CA  1 
ATOM   5831 C  C   . ILE D  1 94  ? 37.986  -8.018  7.789   1.00 11.25 ? 94   ILE D C   1 
ATOM   5832 O  O   . ILE D  1 94  ? 39.116  -8.501  7.654   1.00 11.44 ? 94   ILE D O   1 
ATOM   5833 C  CB  . ILE D  1 94  ? 38.336  -5.990  9.137   1.00 9.81  ? 94   ILE D CB  1 
ATOM   5834 C  CG1 . ILE D  1 94  ? 37.967  -5.221  10.410  1.00 12.50 ? 94   ILE D CG1 1 
ATOM   5835 C  CG2 . ILE D  1 94  ? 38.074  -5.144  7.866   1.00 14.38 ? 94   ILE D CG2 1 
ATOM   5836 C  CD1 . ILE D  1 94  ? 39.029  -4.202  10.812  1.00 14.35 ? 94   ILE D CD1 1 
ATOM   5837 N  N   . CYS D  1 95  ? 37.060  -8.075  6.838   1.00 8.83  ? 95   CYS D N   1 
ATOM   5838 C  CA  . CYS D  1 95  ? 37.408  -8.432  5.473   1.00 7.93  ? 95   CYS D CA  1 
ATOM   5839 C  C   . CYS D  1 95  ? 36.924  -7.302  4.588   1.00 9.82  ? 95   CYS D C   1 
ATOM   5840 O  O   . CYS D  1 95  ? 35.858  -6.733  4.820   1.00 11.04 ? 95   CYS D O   1 
ATOM   5841 C  CB  . CYS D  1 95  ? 36.717  -9.722  5.028   1.00 16.51 ? 95   CYS D CB  1 
ATOM   5842 S  SG  . CYS D  1 95  ? 37.380  -11.262 5.706   1.00 18.27 ? 95   CYS D SG  1 
ATOM   5843 N  N   . VAL D  1 96  ? 37.712  -6.952  3.586   1.00 8.18  ? 96   VAL D N   1 
ATOM   5844 C  CA  . VAL D  1 96  ? 37.236  -6.013  2.588   1.00 6.26  ? 96   VAL D CA  1 
ATOM   5845 C  C   . VAL D  1 96  ? 37.670  -6.525  1.220   1.00 8.66  ? 96   VAL D C   1 
ATOM   5846 O  O   . VAL D  1 96  ? 38.812  -6.957  1.042   1.00 9.25  ? 96   VAL D O   1 
ATOM   5847 C  CB  . VAL D  1 96  ? 37.752  -4.574  2.857   1.00 9.38  ? 96   VAL D CB  1 
ATOM   5848 C  CG1 . VAL D  1 96  ? 39.273  -4.542  2.894   1.00 13.06 ? 96   VAL D CG1 1 
ATOM   5849 C  CG2 . VAL D  1 96  ? 37.188  -3.592  1.826   1.00 12.41 ? 96   VAL D CG2 1 
ATOM   5850 N  N   . SER D  1 97  ? 36.746  -6.514  0.265   1.00 10.20 ? 97   SER D N   1 
ATOM   5851 C  CA  . SER D  1 97  ? 37.091  -6.874  -1.104  1.00 6.57  ? 97   SER D CA  1 
ATOM   5852 C  C   . SER D  1 97  ? 36.753  -5.734  -2.046  1.00 9.11  ? 97   SER D C   1 
ATOM   5853 O  O   . SER D  1 97  ? 35.930  -4.870  -1.732  1.00 10.05 ? 97   SER D O   1 
ATOM   5854 C  CB  . SER D  1 97  ? 36.351  -8.143  -1.556  1.00 7.69  ? 97   SER D CB  1 
ATOM   5855 O  OG  . SER D  1 97  ? 34.955  -7.917  -1.619  1.00 11.07 ? 97   SER D OG  1 
ATOM   5856 N  N   . TRP D  1 98  ? 37.385  -5.737  -3.210  1.00 6.85  ? 98   TRP D N   1 
ATOM   5857 C  CA  . TRP D  1 98  ? 37.069  -4.754  -4.228  1.00 8.28  ? 98   TRP D CA  1 
ATOM   5858 C  C   . TRP D  1 98  ? 37.256  -5.393  -5.597  1.00 8.90  ? 98   TRP D C   1 
ATOM   5859 O  O   . TRP D  1 98  ? 38.157  -6.200  -5.797  1.00 8.83  ? 98   TRP D O   1 
ATOM   5860 C  CB  . TRP D  1 98  ? 37.951  -3.506  -4.063  1.00 10.91 ? 98   TRP D CB  1 
ATOM   5861 C  CG  . TRP D  1 98  ? 37.771  -2.486  -5.150  1.00 10.52 ? 98   TRP D CG  1 
ATOM   5862 C  CD1 . TRP D  1 98  ? 36.780  -1.546  -5.259  1.00 10.07 ? 98   TRP D CD1 1 
ATOM   5863 C  CD2 . TRP D  1 98  ? 38.620  -2.307  -6.286  1.00 7.97  ? 98   TRP D CD2 1 
ATOM   5864 N  NE1 . TRP D  1 98  ? 36.965  -0.800  -6.400  1.00 11.19 ? 98   TRP D NE1 1 
ATOM   5865 C  CE2 . TRP D  1 98  ? 38.089  -1.246  -7.043  1.00 11.41 ? 98   TRP D CE2 1 
ATOM   5866 C  CE3 . TRP D  1 98  ? 39.781  -2.946  -6.737  1.00 13.36 ? 98   TRP D CE3 1 
ATOM   5867 C  CZ2 . TRP D  1 98  ? 38.678  -0.809  -8.231  1.00 13.44 ? 98   TRP D CZ2 1 
ATOM   5868 C  CZ3 . TRP D  1 98  ? 40.364  -2.506  -7.916  1.00 13.30 ? 98   TRP D CZ3 1 
ATOM   5869 C  CH2 . TRP D  1 98  ? 39.810  -1.451  -8.647  1.00 10.15 ? 98   TRP D CH2 1 
ATOM   5870 N  N   . GLU D  1 99  ? 36.397  -5.013  -6.535  1.00 11.62 ? 99   GLU D N   1 
ATOM   5871 C  CA  . GLU D  1 99  ? 36.358  -5.642  -7.850  1.00 10.38 ? 99   GLU D CA  1 
ATOM   5872 C  C   . GLU D  1 99  ? 36.344  -4.530  -8.883  1.00 8.54  ? 99   GLU D C   1 
ATOM   5873 O  O   . GLU D  1 99  ? 35.396  -3.759  -8.944  1.00 11.45 ? 99   GLU D O   1 
ATOM   5874 C  CB  . GLU D  1 99  ? 35.069  -6.456  -7.940  1.00 11.25 ? 99   GLU D CB  1 
ATOM   5875 C  CG  . GLU D  1 99  ? 34.785  -7.096  -9.283  1.00 18.59 ? 99   GLU D CG  1 
ATOM   5876 C  CD  . GLU D  1 99  ? 33.461  -7.845  -9.285  1.00 19.24 ? 99   GLU D CD  1 
ATOM   5877 O  OE1 . GLU D  1 99  ? 33.494  -9.093  -9.329  1.00 22.83 ? 99   GLU D OE1 1 
ATOM   5878 O  OE2 . GLU D  1 99  ? 32.391  -7.194  -9.236  1.00 18.02 ? 99   GLU D OE2 1 
ATOM   5879 N  N   . SER D  1 100 ? 37.412  -4.423  -9.676  1.00 10.56 ? 100  SER D N   1 
ATOM   5880 C  CA  . SER D  1 100 ? 37.495  -3.360  -10.670 1.00 10.49 ? 100  SER D CA  1 
ATOM   5881 C  C   . SER D  1 100 ? 36.299  -3.308  -11.621 1.00 11.61 ? 100  SER D C   1 
ATOM   5882 O  O   . SER D  1 100 ? 35.813  -2.227  -11.949 1.00 12.04 ? 100  SER D O   1 
ATOM   5883 C  CB  . SER D  1 100 ? 38.771  -3.499  -11.500 1.00 15.80 ? 100  SER D CB  1 
ATOM   5884 O  OG  . SER D  1 100 ? 38.778  -2.535  -12.542 1.00 14.55 ? 100  SER D OG  1 
ATOM   5885 N  N   . SER D  1 101 ? 35.834  -4.462  -12.084 1.00 11.62 ? 101  SER D N   1 
ATOM   5886 C  CA  . SER D  1 101 ? 34.849  -4.448  -13.168 1.00 16.20 ? 101  SER D CA  1 
ATOM   5887 C  C   . SER D  1 101 ? 33.551  -3.746  -12.774 1.00 15.51 ? 101  SER D C   1 
ATOM   5888 O  O   . SER D  1 101 ? 32.886  -3.145  -13.618 1.00 13.77 ? 101  SER D O   1 
ATOM   5889 C  CB  . SER D  1 101 ? 34.586  -5.861  -13.714 1.00 16.61 ? 101  SER D CB  1 
ATOM   5890 O  OG  . SER D  1 101 ? 34.112  -6.738  -12.706 1.00 21.16 ? 101  SER D OG  1 
ATOM   5891 N  N   . SER D  1 102 ? 33.198  -3.820  -11.491 1.00 12.07 ? 102  SER D N   1 
ATOM   5892 C  CA  . SER D  1 102 ? 31.985  -3.186  -10.992 1.00 10.31 ? 102  SER D CA  1 
ATOM   5893 C  C   . SER D  1 102 ? 32.282  -1.963  -10.124 1.00 11.50 ? 102  SER D C   1 
ATOM   5894 O  O   . SER D  1 102 ? 31.405  -1.130  -9.903  1.00 12.62 ? 102  SER D O   1 
ATOM   5895 C  CB  . SER D  1 102 ? 31.186  -4.187  -10.152 1.00 11.93 ? 102  SER D CB  1 
ATOM   5896 O  OG  . SER D  1 102 ? 31.947  -4.572  -9.020  1.00 9.75  ? 102  SER D OG  1 
ATOM   5897 N  N   . GLY D  1 103 ? 33.503  -1.887  -9.607  1.00 8.80  ? 103  GLY D N   1 
ATOM   5898 C  CA  . GLY D  1 103 ? 33.874  -0.887  -8.607  1.00 9.08  ? 103  GLY D CA  1 
ATOM   5899 C  C   . GLY D  1 103 ? 33.396  -1.197  -7.195  1.00 9.49  ? 103  GLY D C   1 
ATOM   5900 O  O   . GLY D  1 103 ? 33.604  -0.408  -6.273  1.00 8.48  ? 103  GLY D O   1 
ATOM   5901 N  N   . ILE D  1 104 ? 32.773  -2.352  -7.007  1.00 9.56  ? 104  ILE D N   1 
ATOM   5902 C  CA  . ILE D  1 104 ? 32.110  -2.648  -5.734  1.00 6.64  ? 104  ILE D CA  1 
ATOM   5903 C  C   . ILE D  1 104 ? 33.092  -3.030  -4.640  1.00 8.26  ? 104  ILE D C   1 
ATOM   5904 O  O   . ILE D  1 104 ? 33.940  -3.906  -4.835  1.00 11.21 ? 104  ILE D O   1 
ATOM   5905 C  CB  . ILE D  1 104 ? 31.064  -3.775  -5.886  1.00 7.69  ? 104  ILE D CB  1 
ATOM   5906 C  CG1 . ILE D  1 104 ? 29.895  -3.288  -6.741  1.00 10.28 ? 104  ILE D CG1 1 
ATOM   5907 C  CG2 . ILE D  1 104 ? 30.549  -4.213  -4.499  1.00 10.87 ? 104  ILE D CG2 1 
ATOM   5908 C  CD1 . ILE D  1 104 ? 29.146  -2.106  -6.133  1.00 12.25 ? 104  ILE D CD1 1 
ATOM   5909 N  N   . ALA D  1 105 ? 32.962  -2.366  -3.492  1.00 10.11 ? 105  ALA D N   1 
ATOM   5910 C  CA  . ALA D  1 105 ? 33.732  -2.680  -2.291  1.00 10.82 ? 105  ALA D CA  1 
ATOM   5911 C  C   . ALA D  1 105 ? 32.791  -3.313  -1.282  1.00 7.51  ? 105  ALA D C   1 
ATOM   5912 O  O   . ALA D  1 105 ? 31.710  -2.777  -1.032  1.00 10.72 ? 105  ALA D O   1 
ATOM   5913 C  CB  . ALA D  1 105 ? 34.348  -1.398  -1.700  1.00 8.34  ? 105  ALA D CB  1 
ATOM   5914 N  N   . GLU D  1 106 ? 33.182  -4.462  -0.727  1.00 8.23  ? 106  GLU D N   1 
ATOM   5915 C  CA  . GLU D  1 106 ? 32.388  -5.147  0.288   1.00 7.49  ? 106  GLU D CA  1 
ATOM   5916 C  C   . GLU D  1 106 ? 33.171  -5.231  1.578   1.00 10.95 ? 106  GLU D C   1 
ATOM   5917 O  O   . GLU D  1 106 ? 34.187  -5.926  1.619   1.00 12.46 ? 106  GLU D O   1 
ATOM   5918 C  CB  . GLU D  1 106 ? 32.140  -6.616  -0.096  1.00 12.14 ? 106  GLU D CB  1 
ATOM   5919 C  CG  . GLU D  1 106 ? 31.335  -6.879  -1.318  1.00 18.05 ? 106  GLU D CG  1 
ATOM   5920 C  CD  . GLU D  1 106 ? 30.992  -8.364  -1.470  1.00 25.89 ? 106  GLU D CD  1 
ATOM   5921 O  OE1 . GLU D  1 106 ? 31.174  -9.158  -0.500  1.00 17.62 ? 106  GLU D OE1 1 
ATOM   5922 O  OE2 . GLU D  1 106 ? 30.530  -8.726  -2.571  1.00 29.60 ? 106  GLU D OE2 1 
ATOM   5923 N  N   . PHE D  1 107 ? 32.688  -4.580  2.633   1.00 9.44  ? 107  PHE D N   1 
ATOM   5924 C  CA  . PHE D  1 107 ? 33.245  -4.789  3.969   1.00 9.45  ? 107  PHE D CA  1 
ATOM   5925 C  C   . PHE D  1 107 ? 32.443  -5.855  4.706   1.00 7.78  ? 107  PHE D C   1 
ATOM   5926 O  O   . PHE D  1 107 ? 31.208  -5.885  4.622   1.00 8.36  ? 107  PHE D O   1 
ATOM   5927 C  CB  . PHE D  1 107 ? 33.172  -3.498  4.794   1.00 7.72  ? 107  PHE D CB  1 
ATOM   5928 C  CG  . PHE D  1 107 ? 34.378  -2.599  4.662   1.00 11.35 ? 107  PHE D CG  1 
ATOM   5929 C  CD1 . PHE D  1 107 ? 35.573  -2.912  5.296   1.00 10.30 ? 107  PHE D CD1 1 
ATOM   5930 C  CD2 . PHE D  1 107 ? 34.301  -1.425  3.947   1.00 14.71 ? 107  PHE D CD2 1 
ATOM   5931 C  CE1 . PHE D  1 107 ? 36.670  -2.079  5.196   1.00 13.41 ? 107  PHE D CE1 1 
ATOM   5932 C  CE2 . PHE D  1 107 ? 35.393  -0.584  3.841   1.00 10.20 ? 107  PHE D CE2 1 
ATOM   5933 C  CZ  . PHE D  1 107 ? 36.576  -0.903  4.458   1.00 13.14 ? 107  PHE D CZ  1 
ATOM   5934 N  N   . TRP D  1 108 ? 33.144  -6.715  5.439   1.00 8.46  ? 108  TRP D N   1 
ATOM   5935 C  CA  . TRP D  1 108 ? 32.514  -7.667  6.347   1.00 7.33  ? 108  TRP D CA  1 
ATOM   5936 C  C   . TRP D  1 108 ? 33.138  -7.474  7.717   1.00 6.79  ? 108  TRP D C   1 
ATOM   5937 O  O   . TRP D  1 108 ? 34.361  -7.534  7.849   1.00 9.75  ? 108  TRP D O   1 
ATOM   5938 C  CB  . TRP D  1 108 ? 32.780  -9.105  5.883   1.00 9.87  ? 108  TRP D CB  1 
ATOM   5939 C  CG  . TRP D  1 108 ? 32.093  -9.438  4.594   1.00 10.72 ? 108  TRP D CG  1 
ATOM   5940 C  CD1 . TRP D  1 108 ? 32.442  -9.005  3.348   1.00 15.18 ? 108  TRP D CD1 1 
ATOM   5941 C  CD2 . TRP D  1 108 ? 30.950  -10.285 4.422   1.00 13.97 ? 108  TRP D CD2 1 
ATOM   5942 N  NE1 . TRP D  1 108 ? 31.578  -9.525  2.409   1.00 15.64 ? 108  TRP D NE1 1 
ATOM   5943 C  CE2 . TRP D  1 108 ? 30.653  -10.309 3.043   1.00 11.48 ? 108  TRP D CE2 1 
ATOM   5944 C  CE3 . TRP D  1 108 ? 30.145  -11.019 5.300   1.00 11.02 ? 108  TRP D CE3 1 
ATOM   5945 C  CZ2 . TRP D  1 108 ? 29.585  -11.047 2.521   1.00 10.67 ? 108  TRP D CZ2 1 
ATOM   5946 C  CZ3 . TRP D  1 108 ? 29.086  -11.741 4.783   1.00 12.12 ? 108  TRP D CZ3 1 
ATOM   5947 C  CH2 . TRP D  1 108 ? 28.822  -11.755 3.405   1.00 13.27 ? 108  TRP D CH2 1 
ATOM   5948 N  N   . ILE D  1 109 ? 32.307  -7.244  8.732   1.00 5.72  ? 109  ILE D N   1 
ATOM   5949 C  CA  . ILE D  1 109 ? 32.798  -7.002  10.087  1.00 6.43  ? 109  ILE D CA  1 
ATOM   5950 C  C   . ILE D  1 109 ? 32.257  -8.099  11.000  1.00 8.68  ? 109  ILE D C   1 
ATOM   5951 O  O   . ILE D  1 109 ? 31.045  -8.246  11.145  1.00 11.79 ? 109  ILE D O   1 
ATOM   5952 C  CB  . ILE D  1 109 ? 32.343  -5.611  10.597  1.00 12.54 ? 109  ILE D CB  1 
ATOM   5953 C  CG1 . ILE D  1 109 ? 32.812  -4.495  9.652   1.00 9.89  ? 109  ILE D CG1 1 
ATOM   5954 C  CG2 . ILE D  1 109 ? 32.807  -5.375  12.039  1.00 13.55 ? 109  ILE D CG2 1 
ATOM   5955 C  CD1 . ILE D  1 109 ? 34.337  -4.375  9.503   1.00 12.62 ? 109  ILE D CD1 1 
ATOM   5956 N  N   . ASN D  1 110 ? 33.157  -8.881  11.594  1.00 8.69  ? 110  ASN D N   1 
ATOM   5957 C  CA  . ASN D  1 110 ? 32.755  -10.036 12.395  1.00 10.44 ? 110  ASN D CA  1 
ATOM   5958 C  C   . ASN D  1 110 ? 31.769  -10.923 11.656  1.00 13.84 ? 110  ASN D C   1 
ATOM   5959 O  O   . ASN D  1 110 ? 30.791  -11.409 12.238  1.00 14.86 ? 110  ASN D O   1 
ATOM   5960 C  CB  . ASN D  1 110 ? 32.168  -9.576  13.729  1.00 15.65 ? 110  ASN D CB  1 
ATOM   5961 C  CG  . ASN D  1 110 ? 33.156  -8.777  14.536  1.00 17.00 ? 110  ASN D CG  1 
ATOM   5962 O  OD1 . ASN D  1 110 ? 34.358  -9.033  14.480  1.00 13.35 ? 110  ASN D OD1 1 
ATOM   5963 N  ND2 . ASN D  1 110 ? 32.665  -7.791  15.275  1.00 18.19 ? 110  ASN D ND2 1 
ATOM   5964 N  N   . GLY D  1 111 ? 32.036  -11.128 10.371  1.00 11.11 ? 111  GLY D N   1 
ATOM   5965 C  CA  . GLY D  1 111 ? 31.228  -12.024 9.562   1.00 15.66 ? 111  GLY D CA  1 
ATOM   5966 C  C   . GLY D  1 111 ? 29.921  -11.429 9.071   1.00 13.84 ? 111  GLY D C   1 
ATOM   5967 O  O   . GLY D  1 111 ? 29.132  -12.121 8.421   1.00 17.38 ? 111  GLY D O   1 
ATOM   5968 N  N   . THR D  1 112 ? 29.680  -10.161 9.375   1.00 12.43 ? 112  THR D N   1 
ATOM   5969 C  CA  . THR D  1 112 ? 28.449  -9.507  8.928   1.00 16.55 ? 112  THR D CA  1 
ATOM   5970 C  C   . THR D  1 112 ? 28.747  -8.492  7.835   1.00 11.24 ? 112  THR D C   1 
ATOM   5971 O  O   . THR D  1 112 ? 29.665  -7.674  7.966   1.00 12.10 ? 112  THR D O   1 
ATOM   5972 C  CB  . THR D  1 112 ? 27.682  -8.828  10.077  1.00 21.35 ? 112  THR D CB  1 
ATOM   5973 O  OG1 . THR D  1 112 ? 28.437  -7.726  10.580  1.00 28.65 ? 112  THR D OG1 1 
ATOM   5974 C  CG2 . THR D  1 112 ? 27.408  -9.813  11.208  1.00 20.17 ? 112  THR D CG2 1 
ATOM   5975 N  N   . PRO D  1 113 ? 27.992  -8.561  6.734   1.00 7.92  ? 113  PRO D N   1 
ATOM   5976 C  CA  . PRO D  1 113 ? 28.270  -7.665  5.610   1.00 6.42  ? 113  PRO D CA  1 
ATOM   5977 C  C   . PRO D  1 113 ? 27.777  -6.251  5.875   1.00 9.51  ? 113  PRO D C   1 
ATOM   5978 O  O   . PRO D  1 113 ? 26.654  -6.079  6.347   1.00 11.16 ? 113  PRO D O   1 
ATOM   5979 C  CB  . PRO D  1 113 ? 27.480  -8.296  4.455   1.00 7.39  ? 113  PRO D CB  1 
ATOM   5980 C  CG  . PRO D  1 113 ? 26.352  -9.044  5.121   1.00 10.22 ? 113  PRO D CG  1 
ATOM   5981 C  CD  . PRO D  1 113 ? 26.885  -9.498  6.463   1.00 12.08 ? 113  PRO D CD  1 
ATOM   5982 N  N   . LEU D  1 114 ? 28.613  -5.260  5.570   1.00 8.08  ? 114  LEU D N   1 
ATOM   5983 C  CA  . LEU D  1 114 ? 28.170  -3.868  5.568   1.00 7.57  ? 114  LEU D CA  1 
ATOM   5984 C  C   . LEU D  1 114 ? 27.523  -3.555  4.214   1.00 9.44  ? 114  LEU D C   1 
ATOM   5985 O  O   . LEU D  1 114 ? 27.553  -4.380  3.273   1.00 9.20  ? 114  LEU D O   1 
ATOM   5986 C  CB  . LEU D  1 114 ? 29.343  -2.909  5.817   1.00 7.78  ? 114  LEU D CB  1 
ATOM   5987 C  CG  . LEU D  1 114 ? 30.206  -3.228  7.038   1.00 11.55 ? 114  LEU D CG  1 
ATOM   5988 C  CD1 . LEU D  1 114 ? 31.096  -2.015  7.413   1.00 8.61  ? 114  LEU D CD1 1 
ATOM   5989 C  CD2 . LEU D  1 114 ? 29.345  -3.666  8.204   1.00 13.09 ? 114  LEU D CD2 1 
ATOM   5990 N  N   . VAL D  1 115 ? 26.929  -2.370  4.114   1.00 7.94  ? 115  VAL D N   1 
ATOM   5991 C  CA  . VAL D  1 115 ? 26.353  -1.933  2.848   1.00 6.34  ? 115  VAL D CA  1 
ATOM   5992 C  C   . VAL D  1 115 ? 27.463  -1.791  1.807   1.00 10.16 ? 115  VAL D C   1 
ATOM   5993 O  O   . VAL D  1 115 ? 28.513  -1.197  2.080   1.00 7.86  ? 115  VAL D O   1 
ATOM   5994 C  CB  . VAL D  1 115 ? 25.640  -0.578  3.003   1.00 6.93  ? 115  VAL D CB  1 
ATOM   5995 C  CG1 . VAL D  1 115 ? 25.063  -0.142  1.673   1.00 10.62 ? 115  VAL D CG1 1 
ATOM   5996 C  CG2 . VAL D  1 115 ? 24.541  -0.673  4.074   1.00 7.20  ? 115  VAL D CG2 1 
ATOM   5997 N  N   . LYS D  1 116 ? 27.242  -2.355  0.618   1.00 9.73  ? 116  LYS D N   1 
ATOM   5998 C  CA  . LYS D  1 116 ? 28.197  -2.202  -0.478  1.00 9.43  ? 116  LYS D CA  1 
ATOM   5999 C  C   . LYS D  1 116 ? 28.298  -0.754  -0.944  1.00 9.10  ? 116  LYS D C   1 
ATOM   6000 O  O   . LYS D  1 116 ? 27.310  -0.026  -0.979  1.00 10.54 ? 116  LYS D O   1 
ATOM   6001 C  CB  . LYS D  1 116 ? 27.795  -3.097  -1.663  1.00 7.08  ? 116  LYS D CB  1 
ATOM   6002 C  CG  . LYS D  1 116 ? 28.135  -4.584  -1.499  1.00 13.93 ? 116  LYS D CG  1 
ATOM   6003 C  CD  . LYS D  1 116 ? 27.560  -5.378  -2.685  1.00 14.84 ? 116  LYS D CD  1 
ATOM   6004 C  CE  . LYS D  1 116 ? 27.845  -6.864  -2.586  1.00 20.89 ? 116  LYS D CE  1 
ATOM   6005 N  NZ  . LYS D  1 116 ? 27.220  -7.490  -1.374  1.00 14.91 ? 116  LYS D NZ  1 
ATOM   6006 N  N   . LYS D  1 117 ? 29.505  -0.334  -1.300  1.00 8.66  ? 117  LYS D N   1 
ATOM   6007 C  CA  . LYS D  1 117 ? 29.704  0.964   -1.933  1.00 8.69  ? 117  LYS D CA  1 
ATOM   6008 C  C   . LYS D  1 117 ? 30.543  0.739   -3.181  1.00 12.72 ? 117  LYS D C   1 
ATOM   6009 O  O   . LYS D  1 117 ? 31.042  -0.364  -3.406  1.00 12.89 ? 117  LYS D O   1 
ATOM   6010 C  CB  . LYS D  1 117 ? 30.387  1.939   -0.978  1.00 10.86 ? 117  LYS D CB  1 
ATOM   6011 C  CG  . LYS D  1 117 ? 29.614  2.147   0.332   1.00 8.29  ? 117  LYS D CG  1 
ATOM   6012 C  CD  . LYS D  1 117 ? 28.367  3.019   0.128   1.00 8.55  ? 117  LYS D CD  1 
ATOM   6013 C  CE  . LYS D  1 117 ? 27.424  2.864   1.333   1.00 10.82 ? 117  LYS D CE  1 
ATOM   6014 N  NZ  . LYS D  1 117 ? 27.983  3.507   2.558   1.00 10.74 ? 117  LYS D NZ  1 
ATOM   6015 N  N   . GLY D  1 118 ? 30.682  1.767   -4.006  1.00 7.72  ? 118  GLY D N   1 
ATOM   6016 C  CA  . GLY D  1 118 ? 31.369  1.588   -5.273  1.00 8.45  ? 118  GLY D CA  1 
ATOM   6017 C  C   . GLY D  1 118 ? 32.295  2.743   -5.596  1.00 7.11  ? 118  GLY D C   1 
ATOM   6018 O  O   . GLY D  1 118 ? 31.941  3.913   -5.376  1.00 13.09 ? 118  GLY D O   1 
ATOM   6019 N  N   . LEU D  1 119 ? 33.470  2.404   -6.125  1.00 7.90  ? 119  LEU D N   1 
ATOM   6020 C  CA  . LEU D  1 119 ? 34.484  3.395   -6.515  1.00 10.16 ? 119  LEU D CA  1 
ATOM   6021 C  C   . LEU D  1 119 ? 35.453  2.821   -7.544  1.00 10.01 ? 119  LEU D C   1 
ATOM   6022 O  O   . LEU D  1 119 ? 35.676  1.603   -7.603  1.00 10.52 ? 119  LEU D O   1 
ATOM   6023 C  CB  . LEU D  1 119 ? 35.291  3.881   -5.299  1.00 10.03 ? 119  LEU D CB  1 
ATOM   6024 C  CG  . LEU D  1 119 ? 36.340  2.939   -4.686  1.00 9.26  ? 119  LEU D CG  1 
ATOM   6025 C  CD1 . LEU D  1 119 ? 37.161  3.686   -3.629  1.00 13.63 ? 119  LEU D CD1 1 
ATOM   6026 C  CD2 . LEU D  1 119 ? 35.678  1.720   -4.070  1.00 9.17  ? 119  LEU D CD2 1 
ATOM   6027 N  N   . ARG D  1 120 ? 36.033  3.718   -8.341  1.00 11.07 ? 120  ARG D N   1 
ATOM   6028 C  CA  . ARG D  1 120 ? 37.124  3.392   -9.272  1.00 13.49 ? 120  ARG D CA  1 
ATOM   6029 C  C   . ARG D  1 120 ? 36.810  2.224   -10.203 1.00 14.35 ? 120  ARG D C   1 
ATOM   6030 O  O   . ARG D  1 120 ? 37.681  1.409   -10.505 1.00 11.25 ? 120  ARG D O   1 
ATOM   6031 C  CB  . ARG D  1 120 ? 38.455  3.174   -8.519  1.00 12.98 ? 120  ARG D CB  1 
ATOM   6032 C  CG  . ARG D  1 120 ? 38.866  4.413   -7.697  1.00 14.46 ? 120  ARG D CG  1 
ATOM   6033 C  CD  . ARG D  1 120 ? 40.251  4.992   -8.001  1.00 35.03 ? 120  ARG D CD  1 
ATOM   6034 N  NE  . ARG D  1 120 ? 40.297  5.560   -9.335  1.00 31.40 ? 120  ARG D NE  1 
ATOM   6035 C  CZ  . ARG D  1 120 ? 41.162  6.478   -9.768  1.00 23.84 ? 120  ARG D CZ  1 
ATOM   6036 N  NH1 . ARG D  1 120 ? 42.107  7.000   -8.987  1.00 25.57 ? 120  ARG D NH1 1 
ATOM   6037 N  NH2 . ARG D  1 120 ? 41.076  6.874   -11.021 1.00 18.65 ? 120  ARG D NH2 1 
ATOM   6038 N  N   . GLN D  1 121 ? 35.559  2.140   -10.655 1.00 14.17 ? 121  GLN D N   1 
ATOM   6039 C  CA  . GLN D  1 121 ? 35.200  1.103   -11.614 1.00 9.81  ? 121  GLN D CA  1 
ATOM   6040 C  C   . GLN D  1 121 ? 36.122  1.219   -12.829 1.00 15.79 ? 121  GLN D C   1 
ATOM   6041 O  O   . GLN D  1 121 ? 36.322  2.321   -13.368 1.00 16.13 ? 121  GLN D O   1 
ATOM   6042 C  CB  . GLN D  1 121 ? 33.735  1.236   -12.047 1.00 12.22 ? 121  GLN D CB  1 
ATOM   6043 C  CG  . GLN D  1 121 ? 33.304  0.212   -13.093 1.00 13.32 ? 121  GLN D CG  1 
ATOM   6044 C  CD  . GLN D  1 121 ? 31.850  0.370   -13.503 1.00 20.17 ? 121  GLN D CD  1 
ATOM   6045 O  OE1 . GLN D  1 121 ? 31.324  1.484   -13.550 1.00 19.81 ? 121  GLN D OE1 1 
ATOM   6046 N  NE2 . GLN D  1 121 ? 31.196  -0.746  -13.817 1.00 13.47 ? 121  GLN D NE2 1 
ATOM   6047 N  N   . GLY D  1 122 ? 36.701  0.090   -13.230 1.00 12.92 ? 122  GLY D N   1 
ATOM   6048 C  CA  . GLY D  1 122 ? 37.576  0.035   -14.394 1.00 18.52 ? 122  GLY D CA  1 
ATOM   6049 C  C   . GLY D  1 122 ? 39.042  0.308   -14.099 1.00 15.82 ? 122  GLY D C   1 
ATOM   6050 O  O   . GLY D  1 122 ? 39.901  0.120   -14.972 1.00 18.22 ? 122  GLY D O   1 
ATOM   6051 N  N   . TYR D  1 123 ? 39.333  0.749   -12.877 1.00 13.56 ? 123  TYR D N   1 
ATOM   6052 C  CA  . TYR D  1 123 ? 40.695  1.052   -12.441 1.00 15.94 ? 123  TYR D CA  1 
ATOM   6053 C  C   . TYR D  1 123 ? 41.488  -0.215  -12.121 1.00 15.43 ? 123  TYR D C   1 
ATOM   6054 O  O   . TYR D  1 123 ? 40.909  -1.236  -11.769 1.00 14.72 ? 123  TYR D O   1 
ATOM   6055 C  CB  . TYR D  1 123 ? 40.631  1.943   -11.198 1.00 15.94 ? 123  TYR D CB  1 
ATOM   6056 C  CG  . TYR D  1 123 ? 41.948  2.463   -10.688 1.00 15.34 ? 123  TYR D CG  1 
ATOM   6057 C  CD1 . TYR D  1 123 ? 42.613  3.493   -11.347 1.00 17.40 ? 123  TYR D CD1 1 
ATOM   6058 C  CD2 . TYR D  1 123 ? 42.514  1.956   -9.523  1.00 12.49 ? 123  TYR D CD2 1 
ATOM   6059 C  CE1 . TYR D  1 123 ? 43.812  3.982   -10.876 1.00 19.77 ? 123  TYR D CE1 1 
ATOM   6060 C  CE2 . TYR D  1 123 ? 43.709  2.435   -9.043  1.00 15.13 ? 123  TYR D CE2 1 
ATOM   6061 C  CZ  . TYR D  1 123 ? 44.356  3.447   -9.719  1.00 19.87 ? 123  TYR D CZ  1 
ATOM   6062 O  OH  . TYR D  1 123 ? 45.545  3.924   -9.243  1.00 18.52 ? 123  TYR D OH  1 
ATOM   6063 N  N   . PHE D  1 124 ? 42.813  -0.147  -12.256 1.00 15.66 ? 124  PHE D N   1 
ATOM   6064 C  CA  . PHE D  1 124 ? 43.685  -1.219  -11.786 1.00 13.07 ? 124  PHE D CA  1 
ATOM   6065 C  C   . PHE D  1 124 ? 44.581  -0.694  -10.669 1.00 11.96 ? 124  PHE D C   1 
ATOM   6066 O  O   . PHE D  1 124 ? 45.255  0.329   -10.824 1.00 13.89 ? 124  PHE D O   1 
ATOM   6067 C  CB  . PHE D  1 124 ? 44.567  -1.757  -12.914 1.00 22.10 ? 124  PHE D CB  1 
ATOM   6068 C  CG  . PHE D  1 124 ? 43.803  -2.246  -14.110 1.00 27.87 ? 124  PHE D CG  1 
ATOM   6069 C  CD1 . PHE D  1 124 ? 43.342  -3.549  -14.170 1.00 42.42 ? 124  PHE D CD1 1 
ATOM   6070 C  CD2 . PHE D  1 124 ? 43.567  -1.406  -15.186 1.00 41.90 ? 124  PHE D CD2 1 
ATOM   6071 C  CE1 . PHE D  1 124 ? 42.648  -4.004  -15.275 1.00 43.19 ? 124  PHE D CE1 1 
ATOM   6072 C  CE2 . PHE D  1 124 ? 42.874  -1.854  -16.292 1.00 41.51 ? 124  PHE D CE2 1 
ATOM   6073 C  CZ  . PHE D  1 124 ? 42.413  -3.157  -16.335 1.00 49.37 ? 124  PHE D CZ  1 
ATOM   6074 N  N   . VAL D  1 125 ? 44.566  -1.377  -9.529  1.00 15.41 ? 125  VAL D N   1 
ATOM   6075 C  CA  . VAL D  1 125 ? 45.448  -1.017  -8.426  1.00 13.85 ? 125  VAL D CA  1 
ATOM   6076 C  C   . VAL D  1 125 ? 46.887  -1.308  -8.848  1.00 14.79 ? 125  VAL D C   1 
ATOM   6077 O  O   . VAL D  1 125 ? 47.201  -2.417  -9.272  1.00 14.55 ? 125  VAL D O   1 
ATOM   6078 C  CB  . VAL D  1 125 ? 45.065  -1.795  -7.160  1.00 11.39 ? 125  VAL D CB  1 
ATOM   6079 C  CG1 . VAL D  1 125 ? 46.159  -1.682  -6.095  1.00 14.64 ? 125  VAL D CG1 1 
ATOM   6080 C  CG2 . VAL D  1 125 ? 43.714  -1.296  -6.633  1.00 13.56 ? 125  VAL D CG2 1 
ATOM   6081 N  N   A GLU D  1 126 ? 47.755  -0.307  -8.739  0.57 12.80 ? 126  GLU D N   1 
ATOM   6082 N  N   B GLU D  1 126 ? 47.758  -0.311  -8.744  0.43 12.86 ? 126  GLU D N   1 
ATOM   6083 C  CA  A GLU D  1 126 ? 49.125  -0.456  -9.222  0.57 16.68 ? 126  GLU D CA  1 
ATOM   6084 C  CA  B GLU D  1 126 ? 49.105  -0.439  -9.293  0.43 16.72 ? 126  GLU D CA  1 
ATOM   6085 C  C   A GLU D  1 126 ? 49.916  -1.522  -8.482  0.57 17.37 ? 126  GLU D C   1 
ATOM   6086 C  C   B GLU D  1 126 ? 49.987  -1.396  -8.477  0.43 17.31 ? 126  GLU D C   1 
ATOM   6087 O  O   A GLU D  1 126 ? 49.616  -1.869  -7.337  0.57 13.47 ? 126  GLU D O   1 
ATOM   6088 O  O   B GLU D  1 126 ? 49.790  -1.566  -7.273  0.43 14.63 ? 126  GLU D O   1 
ATOM   6089 C  CB  A GLU D  1 126 ? 49.878  0.878   -9.194  0.57 16.11 ? 126  GLU D CB  1 
ATOM   6090 C  CB  B GLU D  1 126 ? 49.739  0.951   -9.481  0.43 17.23 ? 126  GLU D CB  1 
ATOM   6091 C  CG  A GLU D  1 126 ? 49.799  1.645   -10.506 0.57 20.71 ? 126  GLU D CG  1 
ATOM   6092 C  CG  B GLU D  1 126 ? 48.698  2.012   -9.877  0.43 16.51 ? 126  GLU D CG  1 
ATOM   6093 C  CD  A GLU D  1 126 ? 50.709  1.079   -11.594 0.57 20.80 ? 126  GLU D CD  1 
ATOM   6094 C  CD  B GLU D  1 126 ? 49.151  2.978   -10.964 0.43 28.97 ? 126  GLU D CD  1 
ATOM   6095 O  OE1 A GLU D  1 126 ? 51.251  -0.039  -11.433 0.57 28.87 ? 126  GLU D OE1 1 
ATOM   6096 O  OE1 B GLU D  1 126 ? 50.367  3.073   -11.227 0.43 25.32 ? 126  GLU D OE1 1 
ATOM   6097 O  OE2 A GLU D  1 126 ? 50.887  1.763   -12.621 0.57 31.81 ? 126  GLU D OE2 1 
ATOM   6098 O  OE2 B GLU D  1 126 ? 48.274  3.653   -11.554 0.43 29.54 ? 126  GLU D OE2 1 
ATOM   6099 N  N   . ALA D  1 127 ? 50.935  -2.039  -9.159  1.00 16.80 ? 127  ALA D N   1 
ATOM   6100 C  CA  . ALA D  1 127 ? 51.814  -3.039  -8.562  1.00 17.72 ? 127  ALA D CA  1 
ATOM   6101 C  C   . ALA D  1 127 ? 53.070  -2.436  -7.912  1.00 15.49 ? 127  ALA D C   1 
ATOM   6102 O  O   . ALA D  1 127 ? 53.217  -1.209  -7.813  1.00 15.33 ? 127  ALA D O   1 
ATOM   6103 C  CB  . ALA D  1 127 ? 52.204  -4.067  -9.609  1.00 23.40 ? 127  ALA D CB  1 
ATOM   6104 N  N   . GLN D  1 128 ? 53.964  -3.322  -7.473  1.00 15.46 ? 128  GLN D N   1 
ATOM   6105 C  CA  . GLN D  1 128 ? 55.181  -2.957  -6.742  1.00 15.00 ? 128  GLN D CA  1 
ATOM   6106 C  C   . GLN D  1 128 ? 54.898  -2.035  -5.554  1.00 15.66 ? 128  GLN D C   1 
ATOM   6107 O  O   . GLN D  1 128 ? 55.478  -0.956  -5.444  1.00 15.12 ? 128  GLN D O   1 
ATOM   6108 C  CB  . GLN D  1 128 ? 56.222  -2.335  -7.679  1.00 16.70 ? 128  GLN D CB  1 
ATOM   6109 C  CG  . GLN D  1 128 ? 56.764  -3.320  -8.715  1.00 23.48 ? 128  GLN D CG  1 
ATOM   6110 C  CD  . GLN D  1 128 ? 57.834  -2.715  -9.605  1.00 43.63 ? 128  GLN D CD  1 
ATOM   6111 O  OE1 . GLN D  1 128 ? 57.920  -1.494  -9.756  1.00 42.66 ? 128  GLN D OE1 1 
ATOM   6112 N  NE2 . GLN D  1 128 ? 58.655  -3.570  -10.203 1.00 41.68 ? 128  GLN D NE2 1 
ATOM   6113 N  N   . PRO D  1 129 ? 54.014  -2.475  -4.647  1.00 14.02 ? 129  PRO D N   1 
ATOM   6114 C  CA  . PRO D  1 129 ? 53.652  -1.626  -3.505  1.00 12.38 ? 129  PRO D CA  1 
ATOM   6115 C  C   . PRO D  1 129 ? 54.688  -1.659  -2.391  1.00 10.80 ? 129  PRO D C   1 
ATOM   6116 O  O   . PRO D  1 129 ? 55.553  -2.548  -2.342  1.00 15.48 ? 129  PRO D O   1 
ATOM   6117 C  CB  . PRO D  1 129 ? 52.371  -2.293  -2.991  1.00 11.92 ? 129  PRO D CB  1 
ATOM   6118 C  CG  . PRO D  1 129 ? 52.607  -3.747  -3.291  1.00 12.95 ? 129  PRO D CG  1 
ATOM   6119 C  CD  . PRO D  1 129 ? 53.208  -3.706  -4.685  1.00 14.24 ? 129  PRO D CD  1 
ATOM   6120 N  N   . LYS D  1 130 ? 54.614  -0.659  -1.520  1.00 11.21 ? 130  LYS D N   1 
ATOM   6121 C  CA  . LYS D  1 130 ? 55.137  -0.767  -0.170  1.00 10.36 ? 130  LYS D CA  1 
ATOM   6122 C  C   . LYS D  1 130 ? 53.900  -0.916  0.695   1.00 9.23  ? 130  LYS D C   1 
ATOM   6123 O  O   . LYS D  1 130 ? 52.954  -0.128  0.592   1.00 10.00 ? 130  LYS D O   1 
ATOM   6124 C  CB  . LYS D  1 130 ? 55.897  0.492   0.239   1.00 13.10 ? 130  LYS D CB  1 
ATOM   6125 C  CG  . LYS D  1 130 ? 57.179  0.729   -0.537  1.00 19.90 ? 130  LYS D CG  1 
ATOM   6126 C  CD  . LYS D  1 130 ? 58.234  -0.293  -0.190  1.00 22.59 ? 130  LYS D CD  1 
ATOM   6127 C  CE  . LYS D  1 130 ? 59.619  0.243   -0.554  1.00 34.22 ? 130  LYS D CE  1 
ATOM   6128 N  NZ  . LYS D  1 130 ? 60.706  -0.640  -0.051  1.00 46.65 ? 130  LYS D NZ  1 
ATOM   6129 N  N   . ILE D  1 131 ? 53.891  -1.961  1.514   1.00 11.36 ? 131  ILE D N   1 
ATOM   6130 C  CA  . ILE D  1 131 ? 52.746  -2.262  2.352   1.00 10.11 ? 131  ILE D CA  1 
ATOM   6131 C  C   . ILE D  1 131 ? 53.172  -2.152  3.809   1.00 10.24 ? 131  ILE D C   1 
ATOM   6132 O  O   . ILE D  1 131 ? 54.154  -2.769  4.227   1.00 10.50 ? 131  ILE D O   1 
ATOM   6133 C  CB  . ILE D  1 131 ? 52.216  -3.670  2.073   1.00 9.92  ? 131  ILE D CB  1 
ATOM   6134 C  CG1 . ILE D  1 131 ? 51.817  -3.805  0.597   1.00 10.54 ? 131  ILE D CG1 1 
ATOM   6135 C  CG2 . ILE D  1 131 ? 51.020  -3.961  2.970   1.00 8.39  ? 131  ILE D CG2 1 
ATOM   6136 C  CD1 . ILE D  1 131 ? 51.296  -5.201  0.236   1.00 12.60 ? 131  ILE D CD1 1 
ATOM   6137 N  N   . VAL D  1 132 ? 52.457  -1.326  4.566   1.00 7.96  ? 132  VAL D N   1 
ATOM   6138 C  CA  . VAL D  1 132 ? 52.848  -1.035  5.938   1.00 8.97  ? 132  VAL D CA  1 
ATOM   6139 C  C   . VAL D  1 132 ? 51.697  -1.267  6.913   1.00 8.41  ? 132  VAL D C   1 
ATOM   6140 O  O   . VAL D  1 132 ? 50.554  -0.867  6.653   1.00 9.54  ? 132  VAL D O   1 
ATOM   6141 C  CB  . VAL D  1 132 ? 53.352  0.429   6.081   1.00 8.77  ? 132  VAL D CB  1 
ATOM   6142 C  CG1 . VAL D  1 132 ? 53.617  0.780   7.538   1.00 9.82  ? 132  VAL D CG1 1 
ATOM   6143 C  CG2 . VAL D  1 132 ? 54.625  0.634   5.270   1.00 9.59  ? 132  VAL D CG2 1 
ATOM   6144 N  N   . LEU D  1 133 ? 52.010  -1.939  8.018   1.00 9.13  ? 133  LEU D N   1 
ATOM   6145 C  CA  . LEU D  1 133 ? 51.133  -2.003  9.183   1.00 8.10  ? 133  LEU D CA  1 
ATOM   6146 C  C   . LEU D  1 133 ? 51.702  -1.118  10.279  1.00 7.40  ? 133  LEU D C   1 
ATOM   6147 O  O   . LEU D  1 133 ? 52.925  -1.039  10.456  1.00 8.26  ? 133  LEU D O   1 
ATOM   6148 C  CB  . LEU D  1 133 ? 51.054  -3.430  9.739   1.00 9.65  ? 133  LEU D CB  1 
ATOM   6149 C  CG  . LEU D  1 133 ? 50.609  -4.544  8.795   1.00 10.73 ? 133  LEU D CG  1 
ATOM   6150 C  CD1 . LEU D  1 133 ? 50.596  -5.881  9.539   1.00 9.47  ? 133  LEU D CD1 1 
ATOM   6151 C  CD2 . LEU D  1 133 ? 49.230  -4.219  8.233   1.00 12.83 ? 133  LEU D CD2 1 
ATOM   6152 N  N   . GLY D  1 134 ? 50.811  -0.468  11.021  1.00 7.63  ? 134  GLY D N   1 
ATOM   6153 C  CA  . GLY D  1 134 ? 51.211  0.321   12.174  1.00 9.28  ? 134  GLY D CA  1 
ATOM   6154 C  C   . GLY D  1 134 ? 51.324  1.812   11.905  1.00 8.63  ? 134  GLY D C   1 
ATOM   6155 O  O   . GLY D  1 134 ? 51.249  2.628   12.825  1.00 9.53  ? 134  GLY D O   1 
ATOM   6156 N  N   . GLN D  1 135 ? 51.520  2.165   10.638  1.00 8.84  ? 135  GLN D N   1 
ATOM   6157 C  CA  . GLN D  1 135 ? 51.600  3.572   10.238  1.00 9.05  ? 135  GLN D CA  1 
ATOM   6158 C  C   . GLN D  1 135 ? 50.885  3.752   8.904   1.00 10.78 ? 135  GLN D C   1 
ATOM   6159 O  O   . GLN D  1 135 ? 50.711  2.791   8.153   1.00 10.12 ? 135  GLN D O   1 
ATOM   6160 C  CB  . GLN D  1 135 ? 53.063  4.031   10.087  1.00 9.17  ? 135  GLN D CB  1 
ATOM   6161 C  CG  . GLN D  1 135 ? 53.931  3.869   11.336  1.00 8.87  ? 135  GLN D CG  1 
ATOM   6162 C  CD  . GLN D  1 135 ? 53.558  4.829   12.455  1.00 9.14  ? 135  GLN D CD  1 
ATOM   6163 O  OE1 . GLN D  1 135 ? 52.987  5.892   12.214  1.00 11.65 ? 135  GLN D OE1 1 
ATOM   6164 N  NE2 . GLN D  1 135 ? 53.891  4.458   13.691  1.00 8.49  ? 135  GLN D NE2 1 
ATOM   6165 N  N   . GLU D  1 136 ? 50.480  4.990   8.624   1.00 10.06 ? 136  GLU D N   1 
ATOM   6166 C  CA  . GLU D  1 136 ? 49.850  5.349   7.357   1.00 7.71  ? 136  GLU D CA  1 
ATOM   6167 C  C   . GLU D  1 136 ? 50.919  6.015   6.514   1.00 8.86  ? 136  GLU D C   1 
ATOM   6168 O  O   . GLU D  1 136 ? 51.531  6.982   6.958   1.00 10.85 ? 136  GLU D O   1 
ATOM   6169 C  CB  . GLU D  1 136 ? 48.700  6.341   7.612   1.00 8.10  ? 136  GLU D CB  1 
ATOM   6170 C  CG  . GLU D  1 136 ? 47.610  6.313   6.560   1.00 10.14 ? 136  GLU D CG  1 
ATOM   6171 C  CD  . GLU D  1 136 ? 47.994  7.064   5.317   1.00 11.26 ? 136  GLU D CD  1 
ATOM   6172 O  OE1 . GLU D  1 136 ? 48.574  8.157   5.462   1.00 11.07 ? 136  GLU D OE1 1 
ATOM   6173 O  OE2 . GLU D  1 136 ? 47.719  6.588   4.201   1.00 9.88  ? 136  GLU D OE2 1 
ATOM   6174 N  N   . GLN D  1 137 ? 51.159  5.507   5.309   1.00 8.47  ? 137  GLN D N   1 
ATOM   6175 C  CA  . GLN D  1 137 ? 52.183  6.115   4.434   1.00 8.75  ? 137  GLN D CA  1 
ATOM   6176 C  C   . GLN D  1 137 ? 51.640  7.321   3.695   1.00 8.85  ? 137  GLN D C   1 
ATOM   6177 O  O   . GLN D  1 137 ? 50.527  7.266   3.216   1.00 8.63  ? 137  GLN D O   1 
ATOM   6178 C  CB  . GLN D  1 137 ? 52.599  5.136   3.357   1.00 9.12  ? 137  GLN D CB  1 
ATOM   6179 C  CG  . GLN D  1 137 ? 53.289  3.879   3.817   1.00 9.54  ? 137  GLN D CG  1 
ATOM   6180 C  CD  . GLN D  1 137 ? 53.436  2.892   2.671   1.00 11.50 ? 137  GLN D CD  1 
ATOM   6181 O  OE1 . GLN D  1 137 ? 54.379  2.978   1.874   1.00 13.83 ? 137  GLN D OE1 1 
ATOM   6182 N  NE2 . GLN D  1 137 ? 52.498  1.963   2.569   1.00 9.75  ? 137  GLN D NE2 1 
ATOM   6183 N  N   . ASP D  1 138 ? 52.452  8.376   3.546   1.00 9.09  ? 138  ASP D N   1 
ATOM   6184 C  CA  . ASP D  1 138 ? 52.156  9.452   2.588   1.00 12.25 ? 138  ASP D CA  1 
ATOM   6185 C  C   . ASP D  1 138 ? 53.199  9.513   1.481   1.00 9.56  ? 138  ASP D C   1 
ATOM   6186 O  O   . ASP D  1 138 ? 53.042  10.254  0.506   1.00 13.22 ? 138  ASP D O   1 
ATOM   6187 C  CB  . ASP D  1 138 ? 52.062  10.824  3.264   1.00 10.34 ? 138  ASP D CB  1 
ATOM   6188 C  CG  . ASP D  1 138 ? 50.769  11.018  4.009   1.00 13.73 ? 138  ASP D CG  1 
ATOM   6189 O  OD1 . ASP D  1 138 ? 49.782  10.321  3.695   1.00 10.88 ? 138  ASP D OD1 1 
ATOM   6190 O  OD2 . ASP D  1 138 ? 50.728  11.858  4.929   1.00 12.47 ? 138  ASP D OD2 1 
ATOM   6191 N  N   . SER D  1 139 ? 54.262  8.732   1.622   1.00 10.10 ? 139  SER D N   1 
ATOM   6192 C  CA  . SER D  1 139 ? 55.234  8.585   0.542   1.00 13.13 ? 139  SER D CA  1 
ATOM   6193 C  C   . SER D  1 139 ? 55.356  7.114   0.165   1.00 15.09 ? 139  SER D C   1 
ATOM   6194 O  O   . SER D  1 139 ? 54.601  6.273   0.665   1.00 13.78 ? 139  SER D O   1 
ATOM   6195 C  CB  . SER D  1 139 ? 56.591  9.141   0.973   1.00 13.32 ? 139  SER D CB  1 
ATOM   6196 O  OG  . SER D  1 139 ? 57.221  8.275   1.907   1.00 14.52 ? 139  SER D OG  1 
ATOM   6197 N  N   . TYR D  1 140 ? 56.298  6.791   -0.717  1.00 14.95 ? 140  TYR D N   1 
ATOM   6198 C  CA  . TYR D  1 140 ? 56.513  5.401   -1.085  1.00 10.29 ? 140  TYR D CA  1 
ATOM   6199 C  C   . TYR D  1 140 ? 57.348  4.748   0.004   1.00 13.64 ? 140  TYR D C   1 
ATOM   6200 O  O   . TYR D  1 140 ? 58.576  4.753   -0.046  1.00 16.11 ? 140  TYR D O   1 
ATOM   6201 C  CB  . TYR D  1 140 ? 57.154  5.287   -2.470  1.00 10.42 ? 140  TYR D CB  1 
ATOM   6202 C  CG  . TYR D  1 140 ? 57.325  3.877   -3.025  1.00 14.06 ? 140  TYR D CG  1 
ATOM   6203 C  CD1 . TYR D  1 140 ? 56.234  3.026   -3.203  1.00 11.71 ? 140  TYR D CD1 1 
ATOM   6204 C  CD2 . TYR D  1 140 ? 58.578  3.411   -3.413  1.00 16.36 ? 140  TYR D CD2 1 
ATOM   6205 C  CE1 . TYR D  1 140 ? 56.396  1.746   -3.737  1.00 11.05 ? 140  TYR D CE1 1 
ATOM   6206 C  CE2 . TYR D  1 140 ? 58.746  2.134   -3.939  1.00 18.20 ? 140  TYR D CE2 1 
ATOM   6207 C  CZ  . TYR D  1 140 ? 57.655  1.310   -4.097  1.00 15.04 ? 140  TYR D CZ  1 
ATOM   6208 O  OH  . TYR D  1 140 ? 57.825  0.047   -4.622  1.00 15.77 ? 140  TYR D OH  1 
ATOM   6209 N  N   . GLY D  1 141 ? 56.658  4.228   1.019   1.00 11.21 ? 141  GLY D N   1 
ATOM   6210 C  CA  . GLY D  1 141 ? 57.309  3.560   2.128   1.00 14.28 ? 141  GLY D CA  1 
ATOM   6211 C  C   . GLY D  1 141 ? 57.461  4.400   3.383   1.00 15.78 ? 141  GLY D C   1 
ATOM   6212 O  O   . GLY D  1 141 ? 57.973  3.914   4.386   1.00 18.47 ? 141  GLY D O   1 
ATOM   6213 N  N   . GLY D  1 142 ? 57.024  5.655   3.352   1.00 11.10 ? 142  GLY D N   1 
ATOM   6214 C  CA  . GLY D  1 142 ? 57.278  6.518   4.490   1.00 10.74 ? 142  GLY D CA  1 
ATOM   6215 C  C   . GLY D  1 142 ? 56.343  7.691   4.686   1.00 11.77 ? 142  GLY D C   1 
ATOM   6216 O  O   . GLY D  1 142 ? 55.167  7.617   4.351   1.00 11.87 ? 142  GLY D O   1 
ATOM   6217 N  N   . LYS D  1 143 ? 56.902  8.776   5.223   1.00 12.52 ? 143  LYS D N   1 
ATOM   6218 C  CA  . LYS D  1 143 ? 56.145  9.969   5.589   1.00 11.48 ? 143  LYS D CA  1 
ATOM   6219 C  C   . LYS D  1 143 ? 54.952  9.617   6.468   1.00 11.75 ? 143  LYS D C   1 
ATOM   6220 O  O   . LYS D  1 143 ? 53.804  9.895   6.120   1.00 12.99 ? 143  LYS D O   1 
ATOM   6221 C  CB  . LYS D  1 143 ? 55.702  10.755  4.351   1.00 14.98 ? 143  LYS D CB  1 
ATOM   6222 C  CG  . LYS D  1 143 ? 56.560  11.978  4.057   1.00 35.38 ? 143  LYS D CG  1 
ATOM   6223 C  CD  . LYS D  1 143 ? 55.671  13.136  3.607   1.00 34.08 ? 143  LYS D CD  1 
ATOM   6224 C  CE  . LYS D  1 143 ? 56.168  14.471  4.143   1.00 40.22 ? 143  LYS D CE  1 
ATOM   6225 N  NZ  . LYS D  1 143 ? 55.086  15.504  4.126   1.00 42.98 ? 143  LYS D NZ  1 
ATOM   6226 N  N   . PHE D  1 144 ? 55.256  9.005   7.608   1.00 11.95 ? 144  PHE D N   1 
ATOM   6227 C  CA  . PHE D  1 144 ? 54.248  8.593   8.587   1.00 10.97 ? 144  PHE D CA  1 
ATOM   6228 C  C   . PHE D  1 144 ? 53.702  9.767   9.398   1.00 15.84 ? 144  PHE D C   1 
ATOM   6229 O  O   . PHE D  1 144 ? 54.278  10.860  9.398   1.00 13.84 ? 144  PHE D O   1 
ATOM   6230 C  CB  . PHE D  1 144 ? 54.829  7.535   9.534   1.00 12.33 ? 144  PHE D CB  1 
ATOM   6231 C  CG  . PHE D  1 144 ? 55.410  6.336   8.836   1.00 11.33 ? 144  PHE D CG  1 
ATOM   6232 C  CD1 . PHE D  1 144 ? 54.804  5.811   7.711   1.00 10.45 ? 144  PHE D CD1 1 
ATOM   6233 C  CD2 . PHE D  1 144 ? 56.539  5.697   9.350   1.00 13.44 ? 144  PHE D CD2 1 
ATOM   6234 C  CE1 . PHE D  1 144 ? 55.331  4.689   7.078   1.00 10.88 ? 144  PHE D CE1 1 
ATOM   6235 C  CE2 . PHE D  1 144 ? 57.066  4.578   8.726   1.00 13.96 ? 144  PHE D CE2 1 
ATOM   6236 C  CZ  . PHE D  1 144 ? 56.458  4.076   7.585   1.00 14.01 ? 144  PHE D CZ  1 
ATOM   6237 N  N   . ASP D  1 145 ? 52.595  9.521   10.099  1.00 11.39 ? 145  ASP D N   1 
ATOM   6238 C  CA  . ASP D  1 145 ? 51.898  10.545  10.869  1.00 11.88 ? 145  ASP D CA  1 
ATOM   6239 C  C   . ASP D  1 145 ? 51.439  9.936   12.195  1.00 14.23 ? 145  ASP D C   1 
ATOM   6240 O  O   . ASP D  1 145 ? 50.595  9.047   12.221  1.00 12.59 ? 145  ASP D O   1 
ATOM   6241 C  CB  . ASP D  1 145 ? 50.709  11.090  10.057  1.00 12.25 ? 145  ASP D CB  1 
ATOM   6242 C  CG  . ASP D  1 145 ? 49.875  12.122  10.820  1.00 19.00 ? 145  ASP D CG  1 
ATOM   6243 O  OD1 . ASP D  1 145 ? 50.058  12.280  12.048  1.00 16.02 ? 145  ASP D OD1 1 
ATOM   6244 O  OD2 . ASP D  1 145 ? 49.013  12.768  10.178  1.00 17.08 ? 145  ASP D OD2 1 
ATOM   6245 N  N   . ARG D  1 146 ? 52.024  10.406  13.294  1.00 15.52 ? 146  ARG D N   1 
ATOM   6246 C  CA  . ARG D  1 146 ? 51.732  9.883   14.630  1.00 17.97 ? 146  ARG D CA  1 
ATOM   6247 C  C   . ARG D  1 146 ? 50.235  9.772   14.934  1.00 12.44 ? 146  ARG D C   1 
ATOM   6248 O  O   . ARG D  1 146 ? 49.782  8.827   15.593  1.00 13.09 ? 146  ARG D O   1 
ATOM   6249 C  CB  . ARG D  1 146 ? 52.412  10.783  15.676  1.00 19.77 ? 146  ARG D CB  1 
ATOM   6250 C  CG  . ARG D  1 146 ? 52.311  10.280  17.088  1.00 19.75 ? 146  ARG D CG  1 
ATOM   6251 C  CD  . ARG D  1 146 ? 52.896  11.295  18.066  1.00 21.55 ? 146  ARG D CD  1 
ATOM   6252 N  NE  . ARG D  1 146 ? 52.793  10.807  19.435  1.00 29.03 ? 146  ARG D NE  1 
ATOM   6253 C  CZ  . ARG D  1 146 ? 53.782  10.210  20.091  1.00 27.70 ? 146  ARG D CZ  1 
ATOM   6254 N  NH1 . ARG D  1 146 ? 54.960  10.039  19.504  1.00 28.46 ? 146  ARG D NH1 1 
ATOM   6255 N  NH2 . ARG D  1 146 ? 53.590  9.792   21.338  1.00 32.44 ? 146  ARG D NH2 1 
ATOM   6256 N  N   . SER D  1 147 ? 49.462  10.733  14.445  1.00 11.95 ? 147  SER D N   1 
ATOM   6257 C  CA  . SER D  1 147 ? 48.040  10.797  14.754  1.00 10.28 ? 147  SER D CA  1 
ATOM   6258 C  C   . SER D  1 147 ? 47.231  9.814   13.914  1.00 12.72 ? 147  SER D C   1 
ATOM   6259 O  O   . SER D  1 147 ? 46.013  9.723   14.060  1.00 12.50 ? 147  SER D O   1 
ATOM   6260 C  CB  . SER D  1 147 ? 47.504  12.218  14.564  1.00 16.42 ? 147  SER D CB  1 
ATOM   6261 O  OG  . SER D  1 147 ? 47.415  12.554  13.191  1.00 19.63 ? 147  SER D OG  1 
ATOM   6262 N  N   . GLN D  1 148 ? 47.915  9.079   13.038  1.00 12.10 ? 148  GLN D N   1 
ATOM   6263 C  CA  . GLN D  1 148 ? 47.274  8.027   12.253  1.00 10.92 ? 148  GLN D CA  1 
ATOM   6264 C  C   . GLN D  1 148 ? 47.849  6.651   12.565  1.00 8.09  ? 148  GLN D C   1 
ATOM   6265 O  O   . GLN D  1 148 ? 47.440  5.651   11.960  1.00 10.60 ? 148  GLN D O   1 
ATOM   6266 C  CB  . GLN D  1 148 ? 47.412  8.302   10.754  1.00 11.79 ? 148  GLN D CB  1 
ATOM   6267 C  CG  . GLN D  1 148 ? 46.683  9.564   10.300  1.00 9.68  ? 148  GLN D CG  1 
ATOM   6268 C  CD  . GLN D  1 148 ? 46.908  9.864   8.829   1.00 11.13 ? 148  GLN D CD  1 
ATOM   6269 O  OE1 . GLN D  1 148 ? 48.023  9.752   8.327   1.00 13.96 ? 148  GLN D OE1 1 
ATOM   6270 N  NE2 . GLN D  1 148 ? 45.851  10.242  8.136   1.00 18.46 ? 148  GLN D NE2 1 
ATOM   6271 N  N   . SER D  1 149 ? 48.775  6.597   13.519  1.00 8.73  ? 149  SER D N   1 
ATOM   6272 C  CA  . SER D  1 149 ? 49.424  5.333   13.877  1.00 8.20  ? 149  SER D CA  1 
ATOM   6273 C  C   . SER D  1 149 ? 48.432  4.359   14.504  1.00 7.81  ? 149  SER D C   1 
ATOM   6274 O  O   . SER D  1 149 ? 47.483  4.761   15.175  1.00 9.08  ? 149  SER D O   1 
ATOM   6275 C  CB  . SER D  1 149 ? 50.606  5.561   14.835  1.00 10.58 ? 149  SER D CB  1 
ATOM   6276 O  OG  . SER D  1 149 ? 50.190  6.157   16.067  1.00 10.89 ? 149  SER D OG  1 
ATOM   6277 N  N   . PHE D  1 150 ? 48.664  3.070   14.279  1.00 6.30  ? 150  PHE D N   1 
ATOM   6278 C  CA  . PHE D  1 150 ? 47.824  2.048   14.878  1.00 7.71  ? 150  PHE D CA  1 
ATOM   6279 C  C   . PHE D  1 150 ? 48.501  1.568   16.157  1.00 9.22  ? 150  PHE D C   1 
ATOM   6280 O  O   . PHE D  1 150 ? 49.662  1.173   16.139  1.00 10.40 ? 150  PHE D O   1 
ATOM   6281 C  CB  . PHE D  1 150 ? 47.642  0.868   13.922  1.00 9.09  ? 150  PHE D CB  1 
ATOM   6282 C  CG  . PHE D  1 150 ? 46.930  -0.293  14.549  1.00 8.28  ? 150  PHE D CG  1 
ATOM   6283 C  CD1 . PHE D  1 150 ? 45.548  -0.279  14.678  1.00 8.54  ? 150  PHE D CD1 1 
ATOM   6284 C  CD2 . PHE D  1 150 ? 47.642  -1.368  15.059  1.00 9.81  ? 150  PHE D CD2 1 
ATOM   6285 C  CE1 . PHE D  1 150 ? 44.878  -1.332  15.277  1.00 7.36  ? 150  PHE D CE1 1 
ATOM   6286 C  CE2 . PHE D  1 150 ? 46.990  -2.422  15.670  1.00 8.83  ? 150  PHE D CE2 1 
ATOM   6287 C  CZ  . PHE D  1 150 ? 45.600  -2.409  15.776  1.00 8.31  ? 150  PHE D CZ  1 
ATOM   6288 N  N   . VAL D  1 151 ? 47.775  1.634   17.268  1.00 8.63  ? 151  VAL D N   1 
ATOM   6289 C  CA  . VAL D  1 151 ? 48.261  1.116   18.548  1.00 6.50  ? 151  VAL D CA  1 
ATOM   6290 C  C   . VAL D  1 151 ? 47.353  -0.042  18.915  1.00 8.13  ? 151  VAL D C   1 
ATOM   6291 O  O   . VAL D  1 151 ? 46.127  0.094   18.922  1.00 10.31 ? 151  VAL D O   1 
ATOM   6292 C  CB  . VAL D  1 151 ? 48.216  2.179   19.659  1.00 8.49  ? 151  VAL D CB  1 
ATOM   6293 C  CG1 . VAL D  1 151 ? 48.789  1.597   20.960  1.00 9.34  ? 151  VAL D CG1 1 
ATOM   6294 C  CG2 . VAL D  1 151 ? 49.015  3.423   19.238  1.00 11.34 ? 151  VAL D CG2 1 
ATOM   6295 N  N   . GLY D  1 152 ? 47.936  -1.200  19.182  1.00 9.36  ? 152  GLY D N   1 
ATOM   6296 C  CA  . GLY D  1 152 ? 47.116  -2.366  19.470  1.00 7.99  ? 152  GLY D CA  1 
ATOM   6297 C  C   . GLY D  1 152 ? 47.659  -3.599  18.779  1.00 8.17  ? 152  GLY D C   1 
ATOM   6298 O  O   . GLY D  1 152 ? 48.852  -3.673  18.492  1.00 7.83  ? 152  GLY D O   1 
ATOM   6299 N  N   . GLU D  1 153 ? 46.788  -4.563  18.510  1.00 6.89  ? 153  GLU D N   1 
ATOM   6300 C  CA  . GLU D  1 153 ? 47.235  -5.854  18.023  1.00 7.22  ? 153  GLU D CA  1 
ATOM   6301 C  C   . GLU D  1 153 ? 46.575  -6.196  16.700  1.00 7.13  ? 153  GLU D C   1 
ATOM   6302 O  O   . GLU D  1 153 ? 45.390  -5.916  16.504  1.00 7.10  ? 153  GLU D O   1 
ATOM   6303 C  CB  . GLU D  1 153 ? 46.912  -6.925  19.067  1.00 8.31  ? 153  GLU D CB  1 
ATOM   6304 C  CG  . GLU D  1 153 ? 47.283  -6.475  20.471  1.00 9.02  ? 153  GLU D CG  1 
ATOM   6305 C  CD  . GLU D  1 153 ? 47.055  -7.548  21.511  1.00 9.73  ? 153  GLU D CD  1 
ATOM   6306 O  OE1 . GLU D  1 153 ? 47.184  -8.739  21.171  1.00 10.23 ? 153  GLU D OE1 1 
ATOM   6307 O  OE2 . GLU D  1 153 ? 46.749  -7.200  22.668  1.00 9.79  ? 153  GLU D OE2 1 
ATOM   6308 N  N   . ILE D  1 154 ? 47.348  -6.801  15.795  1.00 5.44  ? 154  ILE D N   1 
ATOM   6309 C  CA  . ILE D  1 154 ? 46.814  -7.265  14.516  1.00 5.55  ? 154  ILE D CA  1 
ATOM   6310 C  C   . ILE D  1 154 ? 47.283  -8.687  14.254  1.00 9.32  ? 154  ILE D C   1 
ATOM   6311 O  O   . ILE D  1 154 ? 48.453  -9.008  14.455  1.00 11.75 ? 154  ILE D O   1 
ATOM   6312 C  CB  . ILE D  1 154 ? 47.293  -6.391  13.342  1.00 11.02 ? 154  ILE D CB  1 
ATOM   6313 C  CG1 . ILE D  1 154 ? 46.666  -4.999  13.408  1.00 13.23 ? 154  ILE D CG1 1 
ATOM   6314 C  CG2 . ILE D  1 154 ? 46.967  -7.066  11.994  1.00 12.76 ? 154  ILE D CG2 1 
ATOM   6315 C  CD1 . ILE D  1 154 ? 47.251  -4.009  12.392  1.00 14.77 ? 154  ILE D CD1 1 
ATOM   6316 N  N   . GLY D  1 155 ? 46.370  -9.537  13.804  1.00 8.68  ? 155  GLY D N   1 
ATOM   6317 C  CA  . GLY D  1 155 ? 46.733  -10.898 13.454  1.00 12.31 ? 155  GLY D CA  1 
ATOM   6318 C  C   . GLY D  1 155 ? 45.918  -11.466 12.312  1.00 9.78  ? 155  GLY D C   1 
ATOM   6319 O  O   . GLY D  1 155 ? 45.048  -10.796 11.769  1.00 8.96  ? 155  GLY D O   1 
ATOM   6320 N  N   . ASP D  1 156 ? 46.220  -12.711 11.944  1.00 9.95  ? 156  ASP D N   1 
ATOM   6321 C  CA  . ASP D  1 156 ? 45.426  -13.455 10.961  1.00 8.86  ? 156  ASP D CA  1 
ATOM   6322 C  C   . ASP D  1 156 ? 45.194  -12.650 9.692   1.00 10.48 ? 156  ASP D C   1 
ATOM   6323 O  O   . ASP D  1 156 ? 44.063  -12.560 9.206   1.00 9.52  ? 156  ASP D O   1 
ATOM   6324 C  CB  . ASP D  1 156 ? 44.080  -13.899 11.547  1.00 9.10  ? 156  ASP D CB  1 
ATOM   6325 C  CG  . ASP D  1 156 ? 44.224  -14.979 12.607  1.00 20.68 ? 156  ASP D CG  1 
ATOM   6326 O  OD1 . ASP D  1 156 ? 45.309  -15.592 12.697  1.00 15.60 ? 156  ASP D OD1 1 
ATOM   6327 O  OD2 . ASP D  1 156 ? 43.248  -15.221 13.351  1.00 16.92 ? 156  ASP D OD2 1 
ATOM   6328 N  N   . LEU D  1 157 ? 46.266  -12.077 9.153   1.00 9.17  ? 157  LEU D N   1 
ATOM   6329 C  CA  . LEU D  1 157 ? 46.148  -11.258 7.952   1.00 9.01  ? 157  LEU D CA  1 
ATOM   6330 C  C   . LEU D  1 157 ? 46.380  -12.083 6.690   1.00 8.04  ? 157  LEU D C   1 
ATOM   6331 O  O   . LEU D  1 157 ? 47.374  -12.794 6.572   1.00 10.44 ? 157  LEU D O   1 
ATOM   6332 C  CB  . LEU D  1 157 ? 47.102  -10.057 8.011   1.00 9.18  ? 157  LEU D CB  1 
ATOM   6333 C  CG  . LEU D  1 157 ? 46.907  -9.020  6.909   1.00 9.84  ? 157  LEU D CG  1 
ATOM   6334 C  CD1 . LEU D  1 157 ? 47.298  -7.655  7.439   1.00 8.17  ? 157  LEU D CD1 1 
ATOM   6335 C  CD2 . LEU D  1 157 ? 47.725  -9.348  5.648   1.00 8.46  ? 157  LEU D CD2 1 
ATOM   6336 N  N   . TYR D  1 158 ? 45.433  -11.985 5.764   1.00 8.25  ? 158  TYR D N   1 
ATOM   6337 C  CA  . TYR D  1 158 ? 45.483  -12.708 4.498   1.00 8.63  ? 158  TYR D CA  1 
ATOM   6338 C  C   . TYR D  1 158 ? 45.006  -11.803 3.377   1.00 9.24  ? 158  TYR D C   1 
ATOM   6339 O  O   . TYR D  1 158 ? 44.065  -11.027 3.559   1.00 8.98  ? 158  TYR D O   1 
ATOM   6340 C  CB  . TYR D  1 158 ? 44.561  -13.919 4.572   1.00 9.94  ? 158  TYR D CB  1 
ATOM   6341 C  CG  . TYR D  1 158 ? 44.960  -14.932 5.619   1.00 11.07 ? 158  TYR D CG  1 
ATOM   6342 C  CD1 . TYR D  1 158 ? 44.464  -14.856 6.920   1.00 8.29  ? 158  TYR D CD1 1 
ATOM   6343 C  CD2 . TYR D  1 158 ? 45.844  -15.961 5.310   1.00 11.05 ? 158  TYR D CD2 1 
ATOM   6344 C  CE1 . TYR D  1 158 ? 44.829  -15.786 7.875   1.00 11.46 ? 158  TYR D CE1 1 
ATOM   6345 C  CE2 . TYR D  1 158 ? 46.217  -16.892 6.266   1.00 12.88 ? 158  TYR D CE2 1 
ATOM   6346 C  CZ  . TYR D  1 158 ? 45.709  -16.805 7.538   1.00 13.94 ? 158  TYR D CZ  1 
ATOM   6347 O  OH  . TYR D  1 158 ? 46.082  -17.740 8.478   1.00 14.24 ? 158  TYR D OH  1 
ATOM   6348 N  N   . MET D  1 159 ? 45.643  -11.899 2.210   1.00 8.73  ? 159  MET D N   1 
ATOM   6349 C  CA  . MET D  1 159 ? 45.197  -11.128 1.061   1.00 11.12 ? 159  MET D CA  1 
ATOM   6350 C  C   . MET D  1 159 ? 45.200  -11.995 -0.185  1.00 11.08 ? 159  MET D C   1 
ATOM   6351 O  O   . MET D  1 159 ? 46.207  -12.644 -0.483  1.00 10.08 ? 159  MET D O   1 
ATOM   6352 C  CB  . MET D  1 159 ? 46.084  -9.901  0.846   1.00 11.39 ? 159  MET D CB  1 
ATOM   6353 C  CG  . MET D  1 159 ? 45.518  -8.886  -0.137  1.00 9.20  ? 159  MET D CG  1 
ATOM   6354 S  SD  . MET D  1 159 ? 46.636  -7.483  -0.289  1.00 13.14 ? 159  MET D SD  1 
ATOM   6355 C  CE  . MET D  1 159 ? 45.828  -6.555  -1.611  1.00 12.78 ? 159  MET D CE  1 
ATOM   6356 N  N   . TRP D  1 160 ? 44.063  -11.982 -0.881  1.00 9.29  ? 160  TRP D N   1 
ATOM   6357 C  CA  . TRP D  1 160 ? 43.825  -12.759 -2.104  1.00 11.63 ? 160  TRP D CA  1 
ATOM   6358 C  C   . TRP D  1 160 ? 43.682  -11.831 -3.308  1.00 12.96 ? 160  TRP D C   1 
ATOM   6359 O  O   . TRP D  1 160 ? 43.197  -10.701 -3.183  1.00 11.90 ? 160  TRP D O   1 
ATOM   6360 C  CB  . TRP D  1 160 ? 42.518  -13.555 -1.998  1.00 10.20 ? 160  TRP D CB  1 
ATOM   6361 C  CG  . TRP D  1 160 ? 42.439  -14.602 -0.924  1.00 11.14 ? 160  TRP D CG  1 
ATOM   6362 C  CD1 . TRP D  1 160 ? 42.632  -15.942 -1.079  1.00 11.67 ? 160  TRP D CD1 1 
ATOM   6363 C  CD2 . TRP D  1 160 ? 42.111  -14.402 0.467   1.00 11.24 ? 160  TRP D CD2 1 
ATOM   6364 N  NE1 . TRP D  1 160 ? 42.454  -16.590 0.120   1.00 11.62 ? 160  TRP D NE1 1 
ATOM   6365 C  CE2 . TRP D  1 160 ? 42.128  -15.670 1.084   1.00 12.06 ? 160  TRP D CE2 1 
ATOM   6366 C  CE3 . TRP D  1 160 ? 41.815  -13.276 1.245   1.00 11.94 ? 160  TRP D CE3 1 
ATOM   6367 C  CZ2 . TRP D  1 160 ? 41.873  -15.845 2.446   1.00 14.00 ? 160  TRP D CZ2 1 
ATOM   6368 C  CZ3 . TRP D  1 160 ? 41.546  -13.454 2.595   1.00 12.76 ? 160  TRP D CZ3 1 
ATOM   6369 C  CH2 . TRP D  1 160 ? 41.571  -14.729 3.179   1.00 12.23 ? 160  TRP D CH2 1 
ATOM   6370 N  N   . ASP D  1 161 ? 44.072  -12.320 -4.483  1.00 12.55 ? 161  ASP D N   1 
ATOM   6371 C  CA  . ASP D  1 161 ? 43.877  -11.557 -5.719  1.00 10.41 ? 161  ASP D CA  1 
ATOM   6372 C  C   . ASP D  1 161 ? 42.531  -11.835 -6.398  1.00 17.66 ? 161  ASP D C   1 
ATOM   6373 O  O   . ASP D  1 161 ? 42.396  -11.702 -7.622  1.00 15.65 ? 161  ASP D O   1 
ATOM   6374 C  CB  . ASP D  1 161 ? 45.050  -11.766 -6.691  1.00 16.28 ? 161  ASP D CB  1 
ATOM   6375 C  CG  . ASP D  1 161 ? 45.018  -13.122 -7.382  1.00 16.40 ? 161  ASP D CG  1 
ATOM   6376 O  OD1 . ASP D  1 161 ? 44.263  -14.007 -6.958  1.00 15.06 ? 161  ASP D OD1 1 
ATOM   6377 O  OD2 . ASP D  1 161 ? 45.763  -13.293 -8.364  1.00 22.44 ? 161  ASP D OD2 1 
ATOM   6378 N  N   . SER D  1 162 ? 41.533  -12.191 -5.593  1.00 12.70 ? 162  SER D N   1 
ATOM   6379 C  CA  . SER D  1 162 ? 40.178  -12.422 -6.085  1.00 13.10 ? 162  SER D CA  1 
ATOM   6380 C  C   . SER D  1 162 ? 39.177  -11.905 -5.045  1.00 13.94 ? 162  SER D C   1 
ATOM   6381 O  O   . SER D  1 162 ? 39.562  -11.584 -3.921  1.00 12.83 ? 162  SER D O   1 
ATOM   6382 C  CB  . SER D  1 162 ? 39.945  -13.912 -6.347  1.00 15.85 ? 162  SER D CB  1 
ATOM   6383 O  OG  . SER D  1 162 ? 40.023  -14.659 -5.147  1.00 16.42 ? 162  SER D OG  1 
ATOM   6384 N  N   . VAL D  1 163 ? 37.910  -11.805 -5.432  1.00 12.74 ? 163  VAL D N   1 
ATOM   6385 C  CA  . VAL D  1 163 ? 36.848  -11.422 -4.504  1.00 11.83 ? 163  VAL D CA  1 
ATOM   6386 C  C   . VAL D  1 163 ? 36.277  -12.671 -3.850  1.00 15.39 ? 163  VAL D C   1 
ATOM   6387 O  O   . VAL D  1 163 ? 35.705  -13.523 -4.532  1.00 14.98 ? 163  VAL D O   1 
ATOM   6388 C  CB  . VAL D  1 163 ? 35.706  -10.671 -5.221  1.00 10.54 ? 163  VAL D CB  1 
ATOM   6389 C  CG1 . VAL D  1 163 ? 34.561  -10.364 -4.248  1.00 10.95 ? 163  VAL D CG1 1 
ATOM   6390 C  CG2 . VAL D  1 163 ? 36.233  -9.389  -5.867  1.00 15.41 ? 163  VAL D CG2 1 
ATOM   6391 N  N   . LEU D  1 164 ? 36.441  -12.803 -2.535  1.00 9.95  ? 164  LEU D N   1 
ATOM   6392 C  CA  . LEU D  1 164 ? 35.895  -13.972 -1.844  1.00 13.61 ? 164  LEU D CA  1 
ATOM   6393 C  C   . LEU D  1 164 ? 34.372  -13.938 -1.757  1.00 11.96 ? 164  LEU D C   1 
ATOM   6394 O  O   . LEU D  1 164 ? 33.775  -12.917 -1.419  1.00 12.24 ? 164  LEU D O   1 
ATOM   6395 C  CB  . LEU D  1 164 ? 36.468  -14.096 -0.429  1.00 11.99 ? 164  LEU D CB  1 
ATOM   6396 C  CG  . LEU D  1 164 ? 37.972  -14.305 -0.260  1.00 13.71 ? 164  LEU D CG  1 
ATOM   6397 C  CD1 . LEU D  1 164 ? 38.280  -14.591 1.213   1.00 15.00 ? 164  LEU D CD1 1 
ATOM   6398 C  CD2 . LEU D  1 164 ? 38.484  -15.416 -1.152  1.00 18.03 ? 164  LEU D CD2 1 
ATOM   6399 N  N   . PRO D  1 165 ? 33.732  -15.084 -2.024  1.00 14.61 ? 165  PRO D N   1 
ATOM   6400 C  CA  . PRO D  1 165 ? 32.299  -15.227 -1.764  1.00 14.92 ? 165  PRO D CA  1 
ATOM   6401 C  C   . PRO D  1 165 ? 32.046  -15.358 -0.264  1.00 14.29 ? 165  PRO D C   1 
ATOM   6402 O  O   . PRO D  1 165 ? 32.992  -15.624 0.491   1.00 13.01 ? 165  PRO D O   1 
ATOM   6403 C  CB  . PRO D  1 165 ? 31.964  -16.523 -2.509  1.00 15.01 ? 165  PRO D CB  1 
ATOM   6404 C  CG  . PRO D  1 165 ? 33.183  -17.334 -2.292  1.00 14.59 ? 165  PRO D CG  1 
ATOM   6405 C  CD  . PRO D  1 165 ? 34.307  -16.334 -2.551  1.00 17.22 ? 165  PRO D CD  1 
ATOM   6406 N  N   . PRO D  1 166 ? 30.795  -15.148 0.176   1.00 13.26 ? 166  PRO D N   1 
ATOM   6407 C  CA  . PRO D  1 166 ? 30.489  -15.153 1.611   1.00 11.45 ? 166  PRO D CA  1 
ATOM   6408 C  C   . PRO D  1 166 ? 31.002  -16.377 2.370   1.00 12.97 ? 166  PRO D C   1 
ATOM   6409 O  O   . PRO D  1 166 ? 31.472  -16.214 3.490   1.00 12.17 ? 166  PRO D O   1 
ATOM   6410 C  CB  . PRO D  1 166 ? 28.963  -15.094 1.645   1.00 15.77 ? 166  PRO D CB  1 
ATOM   6411 C  CG  . PRO D  1 166 ? 28.605  -14.356 0.400   1.00 13.60 ? 166  PRO D CG  1 
ATOM   6412 C  CD  . PRO D  1 166 ? 29.622  -14.757 -0.633  1.00 15.56 ? 166  PRO D CD  1 
ATOM   6413 N  N   . GLU D  1 167 ? 30.917  -17.570 1.785   1.00 12.40 ? 167  GLU D N   1 
ATOM   6414 C  CA  . GLU D  1 167 ? 31.362  -18.762 2.510   1.00 12.34 ? 167  GLU D CA  1 
ATOM   6415 C  C   . GLU D  1 167 ? 32.842  -18.689 2.860   1.00 12.58 ? 167  GLU D C   1 
ATOM   6416 O  O   . GLU D  1 167 ? 33.256  -19.159 3.929   1.00 14.61 ? 167  GLU D O   1 
ATOM   6417 C  CB  . GLU D  1 167 ? 31.099  -20.052 1.717   1.00 20.44 ? 167  GLU D CB  1 
ATOM   6418 C  CG  . GLU D  1 167 ? 29.874  -20.035 0.850   1.00 42.64 ? 167  GLU D CG  1 
ATOM   6419 C  CD  . GLU D  1 167 ? 30.121  -19.337 -0.469  1.00 32.29 ? 167  GLU D CD  1 
ATOM   6420 O  OE1 . GLU D  1 167 ? 30.877  -19.878 -1.312  1.00 35.88 ? 167  GLU D OE1 1 
ATOM   6421 O  OE2 . GLU D  1 167 ? 29.548  -18.250 -0.657  1.00 21.82 ? 167  GLU D OE2 1 
ATOM   6422 N  N   . ASN D  1 168 ? 33.643  -18.108 1.968   1.00 13.84 ? 168  ASN D N   1 
ATOM   6423 C  CA  . ASN D  1 168 ? 35.079  -18.008 2.215   1.00 12.09 ? 168  ASN D CA  1 
ATOM   6424 C  C   . ASN D  1 168 ? 35.406  -16.883 3.200   1.00 12.30 ? 168  ASN D C   1 
ATOM   6425 O  O   . ASN D  1 168 ? 36.387  -16.960 3.937   1.00 11.80 ? 168  ASN D O   1 
ATOM   6426 C  CB  . ASN D  1 168 ? 35.865  -17.801 0.925   1.00 11.23 ? 168  ASN D CB  1 
ATOM   6427 C  CG  . ASN D  1 168 ? 35.727  -18.957 -0.050  1.00 19.25 ? 168  ASN D CG  1 
ATOM   6428 O  OD1 . ASN D  1 168 ? 35.960  -18.785 -1.242  1.00 27.07 ? 168  ASN D OD1 1 
ATOM   6429 N  ND2 . ASN D  1 168 ? 35.367  -20.137 0.449   1.00 17.41 ? 168  ASN D ND2 1 
ATOM   6430 N  N   . ILE D  1 169 ? 34.586  -15.841 3.204   1.00 10.29 ? 169  ILE D N   1 
ATOM   6431 C  CA  . ILE D  1 169 ? 34.733  -14.791 4.209   1.00 11.46 ? 169  ILE D CA  1 
ATOM   6432 C  C   . ILE D  1 169 ? 34.467  -15.375 5.592   1.00 11.03 ? 169  ILE D C   1 
ATOM   6433 O  O   . ILE D  1 169 ? 35.231  -15.134 6.527   1.00 12.04 ? 169  ILE D O   1 
ATOM   6434 C  CB  . ILE D  1 169 ? 33.769  -13.614 3.963   1.00 13.09 ? 169  ILE D CB  1 
ATOM   6435 C  CG1 . ILE D  1 169 ? 34.047  -12.953 2.604   1.00 14.19 ? 169  ILE D CG1 1 
ATOM   6436 C  CG2 . ILE D  1 169 ? 33.854  -12.615 5.113   1.00 11.73 ? 169  ILE D CG2 1 
ATOM   6437 C  CD1 . ILE D  1 169 ? 35.314  -12.136 2.545   1.00 19.35 ? 169  ILE D CD1 1 
ATOM   6438 N  N   . LEU D  1 170 ? 33.392  -16.156 5.719   1.00 10.73 ? 170  LEU D N   1 
ATOM   6439 C  CA  . LEU D  1 170 ? 33.052  -16.775 6.997   1.00 11.56 ? 170  LEU D CA  1 
ATOM   6440 C  C   . LEU D  1 170 ? 34.123  -17.764 7.447   1.00 10.91 ? 170  LEU D C   1 
ATOM   6441 O  O   . LEU D  1 170 ? 34.454  -17.826 8.629   1.00 12.05 ? 170  LEU D O   1 
ATOM   6442 C  CB  . LEU D  1 170 ? 31.672  -17.445 6.950   1.00 13.79 ? 170  LEU D CB  1 
ATOM   6443 C  CG  . LEU D  1 170 ? 30.508  -16.455 6.819   1.00 20.78 ? 170  LEU D CG  1 
ATOM   6444 C  CD1 . LEU D  1 170 ? 29.185  -17.134 7.168   1.00 29.63 ? 170  LEU D CD1 1 
ATOM   6445 C  CD2 . LEU D  1 170 ? 30.728  -15.226 7.686   1.00 28.20 ? 170  LEU D CD2 1 
ATOM   6446 N  N   . SER D  1 171 ? 34.684  -18.518 6.505   1.00 10.80 ? 171  SER D N   1 
ATOM   6447 C  CA  . SER D  1 171 ? 35.793  -19.399 6.834   1.00 12.16 ? 171  SER D CA  1 
ATOM   6448 C  C   . SER D  1 171 ? 36.955  -18.610 7.441   1.00 12.41 ? 171  SER D C   1 
ATOM   6449 O  O   . SER D  1 171 ? 37.551  -19.028 8.433   1.00 14.27 ? 171  SER D O   1 
ATOM   6450 C  CB  . SER D  1 171 ? 36.259  -20.166 5.600   1.00 13.79 ? 171  SER D CB  1 
ATOM   6451 O  OG  . SER D  1 171 ? 35.253  -21.072 5.183   1.00 18.56 ? 171  SER D OG  1 
ATOM   6452 N  N   . ALA D  1 172 ? 37.280  -17.466 6.850   1.00 9.22  ? 172  ALA D N   1 
ATOM   6453 C  CA  . ALA D  1 172 ? 38.344  -16.644 7.409   1.00 10.82 ? 172  ALA D CA  1 
ATOM   6454 C  C   . ALA D  1 172 ? 37.970  -16.170 8.819   1.00 11.03 ? 172  ALA D C   1 
ATOM   6455 O  O   . ALA D  1 172 ? 38.773  -16.245 9.751   1.00 11.65 ? 172  ALA D O   1 
ATOM   6456 C  CB  . ALA D  1 172 ? 38.630  -15.458 6.494   1.00 10.09 ? 172  ALA D CB  1 
ATOM   6457 N  N   . TYR D  1 173 ? 36.745  -15.685 8.969   1.00 9.84  ? 173  TYR D N   1 
ATOM   6458 C  CA  . TYR D  1 173 ? 36.285  -15.198 10.261  1.00 9.00  ? 173  TYR D CA  1 
ATOM   6459 C  C   . TYR D  1 173 ? 36.417  -16.290 11.322  1.00 13.48 ? 173  TYR D C   1 
ATOM   6460 O  O   . TYR D  1 173 ? 36.799  -16.019 12.469  1.00 13.38 ? 173  TYR D O   1 
ATOM   6461 C  CB  . TYR D  1 173 ? 34.843  -14.695 10.146  1.00 10.05 ? 173  TYR D CB  1 
ATOM   6462 C  CG  . TYR D  1 173 ? 34.190  -14.320 11.460  1.00 11.10 ? 173  TYR D CG  1 
ATOM   6463 C  CD1 . TYR D  1 173 ? 34.801  -13.438 12.342  1.00 13.43 ? 173  TYR D CD1 1 
ATOM   6464 C  CD2 . TYR D  1 173 ? 32.957  -14.845 11.803  1.00 15.95 ? 173  TYR D CD2 1 
ATOM   6465 C  CE1 . TYR D  1 173 ? 34.195  -13.095 13.545  1.00 13.79 ? 173  TYR D CE1 1 
ATOM   6466 C  CE2 . TYR D  1 173 ? 32.345  -14.514 12.989  1.00 19.65 ? 173  TYR D CE2 1 
ATOM   6467 C  CZ  . TYR D  1 173 ? 32.964  -13.638 13.854  1.00 18.31 ? 173  TYR D CZ  1 
ATOM   6468 O  OH  . TYR D  1 173 ? 32.334  -13.321 15.034  1.00 23.62 ? 173  TYR D OH  1 
ATOM   6469 N  N   . GLN D  1 174 ? 36.134  -17.527 10.920  1.00 12.86 ? 174  GLN D N   1 
ATOM   6470 C  CA  . GLN D  1 174 ? 36.093  -18.652 11.858  1.00 13.11 ? 174  GLN D CA  1 
ATOM   6471 C  C   . GLN D  1 174 ? 37.470  -19.244 12.127  1.00 15.91 ? 174  GLN D C   1 
ATOM   6472 O  O   . GLN D  1 174 ? 37.625  -20.100 12.987  1.00 18.42 ? 174  GLN D O   1 
ATOM   6473 C  CB  . GLN D  1 174 ? 35.166  -19.753 11.341  1.00 13.24 ? 174  GLN D CB  1 
ATOM   6474 C  CG  . GLN D  1 174 ? 33.696  -19.394 11.367  1.00 18.84 ? 174  GLN D CG  1 
ATOM   6475 C  CD  . GLN D  1 174 ? 32.874  -20.296 10.460  1.00 26.16 ? 174  GLN D CD  1 
ATOM   6476 O  OE1 . GLN D  1 174 ? 33.392  -21.258 9.890   1.00 27.17 ? 174  GLN D OE1 1 
ATOM   6477 N  NE2 . GLN D  1 174 ? 31.593  -19.980 10.313  1.00 31.58 ? 174  GLN D NE2 1 
ATOM   6478 N  N   . GLY D  1 175 ? 38.470  -18.798 11.385  1.00 13.50 ? 175  GLY D N   1 
ATOM   6479 C  CA  . GLY D  1 175 ? 39.826  -19.240 11.636  1.00 14.64 ? 175  GLY D CA  1 
ATOM   6480 C  C   . GLY D  1 175 ? 40.323  -20.343 10.726  1.00 17.80 ? 175  GLY D C   1 
ATOM   6481 O  O   . GLY D  1 175 ? 41.368  -20.933 10.993  1.00 17.28 ? 175  GLY D O   1 
ATOM   6482 N  N   . THR D  1 176 ? 39.586  -20.618 9.652   1.00 14.64 ? 176  THR D N   1 
ATOM   6483 C  CA  . THR D  1 176 ? 40.035  -21.579 8.644   1.00 17.83 ? 176  THR D CA  1 
ATOM   6484 C  C   . THR D  1 176 ? 39.993  -20.971 7.243   1.00 14.76 ? 176  THR D C   1 
ATOM   6485 O  O   . THR D  1 176 ? 39.247  -21.432 6.373   1.00 14.41 ? 176  THR D O   1 
ATOM   6486 C  CB  . THR D  1 176 ? 39.191  -22.866 8.681   1.00 15.84 ? 176  THR D CB  1 
ATOM   6487 O  OG1 . THR D  1 176 ? 37.805  -22.531 8.528   1.00 18.59 ? 176  THR D OG1 1 
ATOM   6488 C  CG2 . THR D  1 176 ? 39.381  -23.579 10.002  1.00 23.13 ? 176  THR D CG2 1 
ATOM   6489 N  N   . PRO D  1 177 ? 40.795  -19.921 7.018   1.00 11.57 ? 177  PRO D N   1 
ATOM   6490 C  CA  . PRO D  1 177 ? 40.781  -19.230 5.723   1.00 12.48 ? 177  PRO D CA  1 
ATOM   6491 C  C   . PRO D  1 177 ? 41.296  -20.112 4.600   1.00 12.50 ? 177  PRO D C   1 
ATOM   6492 O  O   . PRO D  1 177 ? 42.085  -21.033 4.843   1.00 15.11 ? 177  PRO D O   1 
ATOM   6493 C  CB  . PRO D  1 177 ? 41.748  -18.060 5.930   1.00 11.44 ? 177  PRO D CB  1 
ATOM   6494 C  CG  . PRO D  1 177 ? 42.641  -18.495 7.064   1.00 13.06 ? 177  PRO D CG  1 
ATOM   6495 C  CD  . PRO D  1 177 ? 41.811  -19.380 7.941   1.00 13.48 ? 177  PRO D CD  1 
ATOM   6496 N  N   . LEU D  1 178 ? 40.857  -19.822 3.382   1.00 10.28 ? 178  LEU D N   1 
ATOM   6497 C  CA  . LEU D  1 178 ? 41.434  -20.460 2.202   1.00 11.82 ? 178  LEU D CA  1 
ATOM   6498 C  C   . LEU D  1 178 ? 42.865  -19.953 2.013   1.00 16.00 ? 178  LEU D C   1 
ATOM   6499 O  O   . LEU D  1 178 ? 43.222  -18.885 2.505   1.00 16.09 ? 178  LEU D O   1 
ATOM   6500 C  CB  . LEU D  1 178 ? 40.610  -20.139 0.959   1.00 13.64 ? 178  LEU D CB  1 
ATOM   6501 C  CG  . LEU D  1 178 ? 39.237  -20.785 0.846   1.00 18.25 ? 178  LEU D CG  1 
ATOM   6502 C  CD1 . LEU D  1 178 ? 38.537  -20.226 -0.376  1.00 24.75 ? 178  LEU D CD1 1 
ATOM   6503 C  CD2 . LEU D  1 178 ? 39.330  -22.315 0.769   1.00 15.74 ? 178  LEU D CD2 1 
ATOM   6504 N  N   . PRO D  1 179 ? 43.698  -20.727 1.301   1.00 15.22 ? 179  PRO D N   1 
ATOM   6505 C  CA  . PRO D  1 179 ? 45.072  -20.282 1.008   1.00 15.35 ? 179  PRO D CA  1 
ATOM   6506 C  C   . PRO D  1 179 ? 45.039  -18.935 0.298   1.00 13.46 ? 179  PRO D C   1 
ATOM   6507 O  O   . PRO D  1 179 ? 44.223  -18.774 -0.618  1.00 14.75 ? 179  PRO D O   1 
ATOM   6508 C  CB  . PRO D  1 179 ? 45.599  -21.328 0.015   1.00 17.61 ? 179  PRO D CB  1 
ATOM   6509 C  CG  . PRO D  1 179 ? 44.546  -22.366 -0.117  1.00 16.35 ? 179  PRO D CG  1 
ATOM   6510 C  CD  . PRO D  1 179 ? 43.316  -21.970 0.604   1.00 14.38 ? 179  PRO D CD  1 
ATOM   6511 N  N   . ALA D  1 180 ? 45.912  -18.003 0.683   1.00 10.59 ? 180  ALA D N   1 
ATOM   6512 C  CA  . ALA D  1 180 ? 45.895  -16.657 0.102   1.00 11.32 ? 180  ALA D CA  1 
ATOM   6513 C  C   . ALA D  1 180 ? 47.176  -16.403 -0.686  1.00 14.70 ? 180  ALA D C   1 
ATOM   6514 O  O   . ALA D  1 180 ? 48.269  -16.752 -0.231  1.00 17.07 ? 180  ALA D O   1 
ATOM   6515 C  CB  . ALA D  1 180 ? 45.704  -15.594 1.193   1.00 10.86 ? 180  ALA D CB  1 
ATOM   6516 N  N   . ASN D  1 181 ? 47.051  -15.800 -1.868  1.00 10.40 ? 181  ASN D N   1 
ATOM   6517 C  CA  . ASN D  1 181 ? 48.195  -15.742 -2.778  1.00 14.54 ? 181  ASN D CA  1 
ATOM   6518 C  C   . ASN D  1 181 ? 48.967  -14.429 -2.854  1.00 19.61 ? 181  ASN D C   1 
ATOM   6519 O  O   . ASN D  1 181 ? 49.964  -14.341 -3.562  1.00 19.64 ? 181  ASN D O   1 
ATOM   6520 C  CB  . ASN D  1 181 ? 47.822  -16.221 -4.188  1.00 14.27 ? 181  ASN D CB  1 
ATOM   6521 C  CG  . ASN D  1 181 ? 46.650  -15.459 -4.787  1.00 18.66 ? 181  ASN D CG  1 
ATOM   6522 O  OD1 . ASN D  1 181 ? 46.078  -14.566 -4.160  1.00 15.35 ? 181  ASN D OD1 1 
ATOM   6523 N  ND2 . ASN D  1 181 ? 46.290  -15.814 -6.016  1.00 19.11 ? 181  ASN D ND2 1 
ATOM   6524 N  N   . ILE D  1 182 ? 48.519  -13.411 -2.132  1.00 10.80 ? 182  ILE D N   1 
ATOM   6525 C  CA  . ILE D  1 182 ? 49.269  -12.156 -2.076  1.00 11.04 ? 182  ILE D CA  1 
ATOM   6526 C  C   . ILE D  1 182 ? 49.975  -12.007 -0.727  1.00 14.30 ? 182  ILE D C   1 
ATOM   6527 O  O   . ILE D  1 182 ? 51.179  -11.750 -0.673  1.00 12.67 ? 182  ILE D O   1 
ATOM   6528 C  CB  . ILE D  1 182 ? 48.370  -10.936 -2.349  1.00 12.34 ? 182  ILE D CB  1 
ATOM   6529 C  CG1 . ILE D  1 182 ? 47.728  -11.053 -3.738  1.00 13.07 ? 182  ILE D CG1 1 
ATOM   6530 C  CG2 . ILE D  1 182 ? 49.176  -9.648  -2.235  1.00 13.22 ? 182  ILE D CG2 1 
ATOM   6531 C  CD1 . ILE D  1 182 ? 46.658  -9.975  -4.008  1.00 15.29 ? 182  ILE D CD1 1 
ATOM   6532 N  N   . LEU D  1 183 ? 49.216  -12.152 0.358   1.00 11.35 ? 183  LEU D N   1 
ATOM   6533 C  CA  . LEU D  1 183 ? 49.785  -12.187 1.710   1.00 10.84 ? 183  LEU D CA  1 
ATOM   6534 C  C   . LEU D  1 183 ? 49.162  -13.338 2.477   1.00 11.90 ? 183  LEU D C   1 
ATOM   6535 O  O   . LEU D  1 183 ? 47.961  -13.549 2.418   1.00 11.28 ? 183  LEU D O   1 
ATOM   6536 C  CB  . LEU D  1 183 ? 49.510  -10.876 2.466   1.00 8.34  ? 183  LEU D CB  1 
ATOM   6537 C  CG  . LEU D  1 183 ? 50.161  -9.622  1.869   1.00 11.36 ? 183  LEU D CG  1 
ATOM   6538 C  CD1 . LEU D  1 183 ? 49.575  -8.347  2.465   1.00 12.42 ? 183  LEU D CD1 1 
ATOM   6539 C  CD2 . LEU D  1 183 ? 51.679  -9.674  2.059   1.00 12.98 ? 183  LEU D CD2 1 
ATOM   6540 N  N   . ASP D  1 184 ? 49.976  -14.085 3.209   1.00 9.68  ? 184  ASP D N   1 
ATOM   6541 C  CA  . ASP D  1 184 ? 49.431  -15.199 3.970   1.00 9.84  ? 184  ASP D CA  1 
ATOM   6542 C  C   . ASP D  1 184 ? 50.110  -15.285 5.330   1.00 10.75 ? 184  ASP D C   1 
ATOM   6543 O  O   . ASP D  1 184 ? 51.329  -15.419 5.421   1.00 11.58 ? 184  ASP D O   1 
ATOM   6544 C  CB  . ASP D  1 184 ? 49.578  -16.508 3.180   1.00 18.45 ? 184  ASP D CB  1 
ATOM   6545 C  CG  . ASP D  1 184 ? 48.783  -17.654 3.790   1.00 19.18 ? 184  ASP D CG  1 
ATOM   6546 O  OD1 . ASP D  1 184 ? 49.125  -18.070 4.912   1.00 17.05 ? 184  ASP D OD1 1 
ATOM   6547 O  OD2 . ASP D  1 184 ? 47.826  -18.154 3.146   1.00 21.92 ? 184  ASP D OD2 1 
ATOM   6548 N  N   . TRP D  1 185 ? 49.303  -15.197 6.387   1.00 12.38 ? 185  TRP D N   1 
ATOM   6549 C  CA  . TRP D  1 185 ? 49.800  -15.142 7.755   1.00 10.99 ? 185  TRP D CA  1 
ATOM   6550 C  C   . TRP D  1 185 ? 50.656  -16.354 8.120   1.00 14.16 ? 185  TRP D C   1 
ATOM   6551 O  O   . TRP D  1 185 ? 51.508  -16.271 9.005   1.00 13.19 ? 185  TRP D O   1 
ATOM   6552 C  CB  . TRP D  1 185 ? 48.603  -15.053 8.705   1.00 9.14  ? 185  TRP D CB  1 
ATOM   6553 C  CG  . TRP D  1 185 ? 48.911  -14.533 10.076  1.00 10.98 ? 185  TRP D CG  1 
ATOM   6554 C  CD1 . TRP D  1 185 ? 48.787  -15.211 11.262  1.00 10.72 ? 185  TRP D CD1 1 
ATOM   6555 C  CD2 . TRP D  1 185 ? 49.354  -13.214 10.413  1.00 8.39  ? 185  TRP D CD2 1 
ATOM   6556 N  NE1 . TRP D  1 185 ? 49.143  -14.392 12.311  1.00 10.71 ? 185  TRP D NE1 1 
ATOM   6557 C  CE2 . TRP D  1 185 ? 49.503  -13.167 11.817  1.00 8.39  ? 185  TRP D CE2 1 
ATOM   6558 C  CE3 . TRP D  1 185 ? 49.665  -12.074 9.663   1.00 10.82 ? 185  TRP D CE3 1 
ATOM   6559 C  CZ2 . TRP D  1 185 ? 49.940  -12.015 12.486  1.00 9.48  ? 185  TRP D CZ2 1 
ATOM   6560 C  CZ3 . TRP D  1 185 ? 50.092  -10.932 10.330  1.00 12.09 ? 185  TRP D CZ3 1 
ATOM   6561 C  CH2 . TRP D  1 185 ? 50.222  -10.916 11.728  1.00 10.34 ? 185  TRP D CH2 1 
ATOM   6562 N  N   . GLN D  1 186 ? 50.421  -17.473 7.441   1.00 11.66 ? 186  GLN D N   1 
ATOM   6563 C  CA  . GLN D  1 186 ? 51.156  -18.708 7.730   1.00 10.39 ? 186  GLN D CA  1 
ATOM   6564 C  C   . GLN D  1 186 ? 52.484  -18.802 6.984   1.00 13.18 ? 186  GLN D C   1 
ATOM   6565 O  O   . GLN D  1 186 ? 53.250  -19.746 7.193   1.00 13.86 ? 186  GLN D O   1 
ATOM   6566 C  CB  . GLN D  1 186 ? 50.299  -19.936 7.418   1.00 12.94 ? 186  GLN D CB  1 
ATOM   6567 C  CG  . GLN D  1 186 ? 49.109  -20.081 8.342   1.00 14.23 ? 186  GLN D CG  1 
ATOM   6568 C  CD  . GLN D  1 186 ? 48.481  -21.466 8.257   1.00 25.13 ? 186  GLN D CD  1 
ATOM   6569 O  OE1 . GLN D  1 186 ? 48.357  -22.031 7.177   1.00 26.61 ? 186  GLN D OE1 1 
ATOM   6570 N  NE2 . GLN D  1 186 ? 48.084  -22.014 9.403   1.00 30.91 ? 186  GLN D NE2 1 
ATOM   6571 N  N   . ALA D  1 187 ? 52.736  -17.837 6.103   1.00 12.36 ? 187  ALA D N   1 
ATOM   6572 C  CA  . ALA D  1 187 ? 53.977  -17.771 5.348   1.00 14.42 ? 187  ALA D CA  1 
ATOM   6573 C  C   . ALA D  1 187 ? 54.251  -16.317 5.004   1.00 12.29 ? 187  ALA D C   1 
ATOM   6574 O  O   . ALA D  1 187 ? 54.239  -15.917 3.836   1.00 14.20 ? 187  ALA D O   1 
ATOM   6575 C  CB  . ALA D  1 187 ? 53.880  -18.629 4.081   1.00 17.28 ? 187  ALA D CB  1 
ATOM   6576 N  N   . LEU D  1 188 ? 54.482  -15.523 6.046   1.00 14.20 ? 188  LEU D N   1 
ATOM   6577 C  CA  . LEU D  1 188 ? 54.564  -14.076 5.915   1.00 12.24 ? 188  LEU D CA  1 
ATOM   6578 C  C   . LEU D  1 188 ? 56.010  -13.610 5.847   1.00 15.97 ? 188  LEU D C   1 
ATOM   6579 O  O   . LEU D  1 188 ? 56.841  -14.010 6.666   1.00 15.42 ? 188  LEU D O   1 
ATOM   6580 C  CB  . LEU D  1 188 ? 53.860  -13.399 7.097   1.00 9.38  ? 188  LEU D CB  1 
ATOM   6581 C  CG  . LEU D  1 188 ? 53.521  -11.924 6.861   1.00 10.19 ? 188  LEU D CG  1 
ATOM   6582 C  CD1 . LEU D  1 188 ? 52.376  -11.826 5.871   1.00 13.96 ? 188  LEU D CD1 1 
ATOM   6583 C  CD2 . LEU D  1 188 ? 53.148  -11.242 8.191   1.00 11.80 ? 188  LEU D CD2 1 
ATOM   6584 N  N   . ASN D  1 189 ? 56.297  -12.769 4.857   1.00 12.07 ? 189  ASN D N   1 
ATOM   6585 C  CA  . ASN D  1 189 ? 57.608  -12.155 4.709   1.00 14.31 ? 189  ASN D CA  1 
ATOM   6586 C  C   . ASN D  1 189 ? 57.483  -10.724 5.178   1.00 15.56 ? 189  ASN D C   1 
ATOM   6587 O  O   . ASN D  1 189 ? 56.805  -9.925  4.540   1.00 15.92 ? 189  ASN D O   1 
ATOM   6588 C  CB  . ASN D  1 189 ? 58.040  -12.194 3.239   1.00 15.64 ? 189  ASN D CB  1 
ATOM   6589 C  CG  . ASN D  1 189 ? 59.498  -11.803 3.044   1.00 27.38 ? 189  ASN D CG  1 
ATOM   6590 O  OD1 . ASN D  1 189 ? 60.229  -11.582 4.009   1.00 32.99 ? 189  ASN D OD1 1 
ATOM   6591 N  ND2 . ASN D  1 189 ? 59.927  -11.723 1.788   1.00 27.07 ? 189  ASN D ND2 1 
ATOM   6592 N  N   . TYR D  1 190 ? 58.114  -10.397 6.303   1.00 12.47 ? 190  TYR D N   1 
ATOM   6593 C  CA  . TYR D  1 190 ? 57.921  -9.074  6.897   1.00 13.67 ? 190  TYR D CA  1 
ATOM   6594 C  C   . TYR D  1 190 ? 59.205  -8.515  7.476   1.00 19.10 ? 190  TYR D C   1 
ATOM   6595 O  O   . TYR D  1 190 ? 60.191  -9.236  7.652   1.00 15.13 ? 190  TYR D O   1 
ATOM   6596 C  CB  . TYR D  1 190 ? 56.850  -9.129  7.999   1.00 12.56 ? 190  TYR D CB  1 
ATOM   6597 C  CG  . TYR D  1 190 ? 57.240  -10.027 9.147   1.00 9.69  ? 190  TYR D CG  1 
ATOM   6598 C  CD1 . TYR D  1 190 ? 57.952  -9.537  10.234  1.00 10.94 ? 190  TYR D CD1 1 
ATOM   6599 C  CD2 . TYR D  1 190 ? 56.931  -11.382 9.121   1.00 14.60 ? 190  TYR D CD2 1 
ATOM   6600 C  CE1 . TYR D  1 190 ? 58.333  -10.376 11.271  1.00 16.49 ? 190  TYR D CE1 1 
ATOM   6601 C  CE2 . TYR D  1 190 ? 57.297  -12.217 10.148  1.00 20.75 ? 190  TYR D CE2 1 
ATOM   6602 C  CZ  . TYR D  1 190 ? 57.996  -11.716 11.215  1.00 18.91 ? 190  TYR D CZ  1 
ATOM   6603 O  OH  . TYR D  1 190 ? 58.356  -12.566 12.233  1.00 22.98 ? 190  TYR D OH  1 
ATOM   6604 N  N   . GLU D  1 191 ? 59.181  -7.220  7.765   1.00 15.85 ? 191  GLU D N   1 
ATOM   6605 C  CA  . GLU D  1 191 ? 60.269  -6.556  8.459   1.00 13.47 ? 191  GLU D CA  1 
ATOM   6606 C  C   . GLU D  1 191 ? 59.709  -5.700  9.584   1.00 14.43 ? 191  GLU D C   1 
ATOM   6607 O  O   . GLU D  1 191 ? 58.895  -4.800  9.348   1.00 13.46 ? 191  GLU D O   1 
ATOM   6608 C  CB  . GLU D  1 191 ? 61.031  -5.643  7.503   1.00 19.01 ? 191  GLU D CB  1 
ATOM   6609 C  CG  . GLU D  1 191 ? 61.553  -6.343  6.265   1.00 26.20 ? 191  GLU D CG  1 
ATOM   6610 C  CD  . GLU D  1 191 ? 62.127  -5.376  5.251   1.00 34.28 ? 191  GLU D CD  1 
ATOM   6611 O  OE1 . GLU D  1 191 ? 61.584  -4.259  5.111   1.00 25.64 ? 191  GLU D OE1 1 
ATOM   6612 O  OE2 . GLU D  1 191 ? 63.119  -5.740  4.585   1.00 37.25 ? 191  GLU D OE2 1 
ATOM   6613 N  N   . ILE D  1 192 ? 60.150  -5.971  10.805  1.00 10.52 ? 192  ILE D N   1 
ATOM   6614 C  CA  . ILE D  1 192 ? 59.772  -5.130  11.924  1.00 10.98 ? 192  ILE D CA  1 
ATOM   6615 C  C   . ILE D  1 192 ? 60.726  -3.951  12.006  1.00 14.54 ? 192  ILE D C   1 
ATOM   6616 O  O   . ILE D  1 192 ? 61.947  -4.129  11.888  1.00 14.80 ? 192  ILE D O   1 
ATOM   6617 C  CB  . ILE D  1 192 ? 59.814  -5.910  13.243  1.00 9.62  ? 192  ILE D CB  1 
ATOM   6618 C  CG1 . ILE D  1 192 ? 58.591  -6.822  13.354  1.00 11.70 ? 192  ILE D CG1 1 
ATOM   6619 C  CG2 . ILE D  1 192 ? 59.887  -4.958  14.442  1.00 10.37 ? 192  ILE D CG2 1 
ATOM   6620 C  CD1 . ILE D  1 192 ? 58.592  -7.686  14.604  1.00 14.97 ? 192  ILE D CD1 1 
ATOM   6621 N  N   . ARG D  1 193 ? 60.162  -2.758  12.174  1.00 13.01 ? 193  ARG D N   1 
ATOM   6622 C  CA  . ARG D  1 193 ? 60.930  -1.540  12.406  1.00 12.36 ? 193  ARG D CA  1 
ATOM   6623 C  C   . ARG D  1 193 ? 60.429  -0.848  13.672  1.00 13.54 ? 193  ARG D C   1 
ATOM   6624 O  O   . ARG D  1 193 ? 59.221  -0.712  13.892  1.00 14.19 ? 193  ARG D O   1 
ATOM   6625 C  CB  . ARG D  1 193 ? 60.830  -0.583  11.213  1.00 12.81 ? 193  ARG D CB  1 
ATOM   6626 C  CG  . ARG D  1 193 ? 61.378  -1.149  9.906   1.00 15.89 ? 193  ARG D CG  1 
ATOM   6627 C  CD  . ARG D  1 193 ? 62.872  -1.399  9.990   1.00 26.28 ? 193  ARG D CD  1 
ATOM   6628 N  NE  . ARG D  1 193 ? 63.392  -1.941  8.736   1.00 30.34 ? 193  ARG D NE  1 
ATOM   6629 C  CZ  . ARG D  1 193 ? 63.765  -3.207  8.559   1.00 33.32 ? 193  ARG D CZ  1 
ATOM   6630 N  NH1 . ARG D  1 193 ? 63.689  -4.078  9.562   1.00 28.96 ? 193  ARG D NH1 1 
ATOM   6631 N  NH2 . ARG D  1 193 ? 64.222  -3.601  7.378   1.00 27.18 ? 193  ARG D NH2 1 
ATOM   6632 N  N   . GLY D  1 194 ? 61.354  -0.416  14.522  1.00 13.82 ? 194  GLY D N   1 
ATOM   6633 C  CA  . GLY D  1 194 ? 60.953  0.159   15.788  1.00 16.13 ? 194  GLY D CA  1 
ATOM   6634 C  C   . GLY D  1 194 ? 60.358  -0.862  16.743  1.00 15.11 ? 194  GLY D C   1 
ATOM   6635 O  O   . GLY D  1 194 ? 60.729  -2.035  16.730  1.00 13.07 ? 194  GLY D O   1 
ATOM   6636 N  N   . TYR D  1 195 ? 59.426  -0.397  17.570  1.00 13.42 ? 195  TYR D N   1 
ATOM   6637 C  CA  . TYR D  1 195 ? 58.880  -1.175  18.676  1.00 11.64 ? 195  TYR D CA  1 
ATOM   6638 C  C   . TYR D  1 195 ? 57.617  -1.899  18.243  1.00 9.00  ? 195  TYR D C   1 
ATOM   6639 O  O   . TYR D  1 195 ? 56.514  -1.359  18.334  1.00 9.41  ? 195  TYR D O   1 
ATOM   6640 C  CB  . TYR D  1 195 ? 58.563  -0.237  19.839  1.00 12.41 ? 195  TYR D CB  1 
ATOM   6641 C  CG  . TYR D  1 195 ? 58.196  -0.889  21.159  1.00 9.68  ? 195  TYR D CG  1 
ATOM   6642 C  CD1 . TYR D  1 195 ? 58.731  -2.119  21.542  1.00 12.18 ? 195  TYR D CD1 1 
ATOM   6643 C  CD2 . TYR D  1 195 ? 57.371  -0.227  22.058  1.00 11.10 ? 195  TYR D CD2 1 
ATOM   6644 C  CE1 . TYR D  1 195 ? 58.397  -2.691  22.782  1.00 10.22 ? 195  TYR D CE1 1 
ATOM   6645 C  CE2 . TYR D  1 195 ? 57.046  -0.780  23.286  1.00 9.98  ? 195  TYR D CE2 1 
ATOM   6646 C  CZ  . TYR D  1 195 ? 57.554  -2.006  23.641  1.00 9.00  ? 195  TYR D CZ  1 
ATOM   6647 O  OH  . TYR D  1 195 ? 57.219  -2.529  24.882  1.00 10.27 ? 195  TYR D OH  1 
ATOM   6648 N  N   . VAL D  1 196 ? 57.805  -3.125  17.771  1.00 10.81 ? 196  VAL D N   1 
ATOM   6649 C  CA  . VAL D  1 196 ? 56.710  -4.035  17.472  1.00 10.78 ? 196  VAL D CA  1 
ATOM   6650 C  C   . VAL D  1 196 ? 57.104  -5.383  18.053  1.00 9.66  ? 196  VAL D C   1 
ATOM   6651 O  O   . VAL D  1 196 ? 58.244  -5.842  17.865  1.00 11.48 ? 196  VAL D O   1 
ATOM   6652 C  CB  . VAL D  1 196 ? 56.470  -4.160  15.958  1.00 8.95  ? 196  VAL D CB  1 
ATOM   6653 C  CG1 . VAL D  1 196 ? 55.209  -4.974  15.681  1.00 8.45  ? 196  VAL D CG1 1 
ATOM   6654 C  CG2 . VAL D  1 196 ? 56.347  -2.770  15.334  1.00 11.69 ? 196  VAL D CG2 1 
ATOM   6655 N  N   . ILE D  1 197 ? 56.182  -6.000  18.784  1.00 8.38  ? 197  ILE D N   1 
ATOM   6656 C  CA  . ILE D  1 197 ? 56.473  -7.252  19.478  1.00 6.48  ? 197  ILE D CA  1 
ATOM   6657 C  C   . ILE D  1 197 ? 55.514  -8.333  18.991  1.00 10.59 ? 197  ILE D C   1 
ATOM   6658 O  O   . ILE D  1 197 ? 54.316  -8.101  18.895  1.00 10.43 ? 197  ILE D O   1 
ATOM   6659 C  CB  . ILE D  1 197 ? 56.268  -7.105  21.003  1.00 8.52  ? 197  ILE D CB  1 
ATOM   6660 C  CG1 . ILE D  1 197 ? 57.162  -6.004  21.585  1.00 8.31  ? 197  ILE D CG1 1 
ATOM   6661 C  CG2 . ILE D  1 197 ? 56.502  -8.442  21.719  1.00 11.18 ? 197  ILE D CG2 1 
ATOM   6662 C  CD1 . ILE D  1 197 ? 58.661  -6.231  21.418  1.00 10.74 ? 197  ILE D CD1 1 
ATOM   6663 N  N   . ILE D  1 198 ? 56.036  -9.515  18.694  1.00 7.70  ? 198  ILE D N   1 
ATOM   6664 C  CA  . ILE D  1 198 ? 55.173  -10.649 18.380  1.00 7.58  ? 198  ILE D CA  1 
ATOM   6665 C  C   . ILE D  1 198 ? 54.769  -11.409 19.648  1.00 10.70 ? 198  ILE D C   1 
ATOM   6666 O  O   . ILE D  1 198 ? 55.618  -11.804 20.445  1.00 10.20 ? 198  ILE D O   1 
ATOM   6667 C  CB  . ILE D  1 198 ? 55.841  -11.604 17.369  1.00 9.14  ? 198  ILE D CB  1 
ATOM   6668 C  CG1 . ILE D  1 198 ? 56.080  -10.868 16.049  1.00 11.25 ? 198  ILE D CG1 1 
ATOM   6669 C  CG2 . ILE D  1 198 ? 54.979  -12.846 17.155  1.00 12.35 ? 198  ILE D CG2 1 
ATOM   6670 C  CD1 . ILE D  1 198 ? 57.031  -11.593 15.110  1.00 14.32 ? 198  ILE D CD1 1 
ATOM   6671 N  N   . LYS D  1 199 ? 53.465  -11.579 19.842  1.00 9.70  ? 199  LYS D N   1 
ATOM   6672 C  CA  . LYS D  1 199 ? 52.939  -12.295 21.006  1.00 8.05  ? 199  LYS D CA  1 
ATOM   6673 C  C   . LYS D  1 199 ? 51.875  -13.282 20.577  1.00 7.49  ? 199  LYS D C   1 
ATOM   6674 O  O   . LYS D  1 199 ? 51.306  -13.166 19.507  1.00 8.63  ? 199  LYS D O   1 
ATOM   6675 C  CB  . LYS D  1 199 ? 52.308  -11.310 22.004  1.00 9.02  ? 199  LYS D CB  1 
ATOM   6676 C  CG  . LYS D  1 199 ? 53.305  -10.484 22.807  1.00 10.60 ? 199  LYS D CG  1 
ATOM   6677 C  CD  . LYS D  1 199 ? 54.016  -11.404 23.790  1.00 16.91 ? 199  LYS D CD  1 
ATOM   6678 C  CE  . LYS D  1 199 ? 54.881  -10.652 24.788  1.00 21.41 ? 199  LYS D CE  1 
ATOM   6679 N  NZ  . LYS D  1 199 ? 55.499  -11.636 25.733  1.00 26.88 ? 199  LYS D NZ  1 
ATOM   6680 N  N   . PRO D  1 200 ? 51.564  -14.249 21.443  1.00 11.60 ? 200  PRO D N   1 
ATOM   6681 C  CA  . PRO D  1 200 ? 50.413  -15.108 21.161  1.00 10.55 ? 200  PRO D CA  1 
ATOM   6682 C  C   . PRO D  1 200 ? 49.127  -14.290 21.111  1.00 11.60 ? 200  PRO D C   1 
ATOM   6683 O  O   . PRO D  1 200 ? 48.999  -13.293 21.824  1.00 10.10 ? 200  PRO D O   1 
ATOM   6684 C  CB  . PRO D  1 200 ? 50.376  -16.039 22.375  1.00 13.06 ? 200  PRO D CB  1 
ATOM   6685 C  CG  . PRO D  1 200 ? 51.780  -16.068 22.866  1.00 17.93 ? 200  PRO D CG  1 
ATOM   6686 C  CD  . PRO D  1 200 ? 52.312  -14.683 22.632  1.00 15.48 ? 200  PRO D CD  1 
ATOM   6687 N  N   . LEU D  1 201 ? 48.195  -14.727 20.274  1.00 8.37  ? 201  LEU D N   1 
ATOM   6688 C  CA  . LEU D  1 201 ? 46.846  -14.179 20.202  1.00 10.10 ? 201  LEU D CA  1 
ATOM   6689 C  C   . LEU D  1 201 ? 46.020  -14.719 21.360  1.00 14.33 ? 201  LEU D C   1 
ATOM   6690 O  O   . LEU D  1 201 ? 45.741  -15.921 21.414  1.00 15.74 ? 201  LEU D O   1 
ATOM   6691 C  CB  . LEU D  1 201 ? 46.212  -14.620 18.877  1.00 12.60 ? 201  LEU D CB  1 
ATOM   6692 C  CG  . LEU D  1 201 ? 44.707  -14.442 18.702  1.00 17.23 ? 201  LEU D CG  1 
ATOM   6693 C  CD1 . LEU D  1 201 ? 44.349  -12.987 18.731  1.00 11.92 ? 201  LEU D CD1 1 
ATOM   6694 C  CD2 . LEU D  1 201 ? 44.225  -15.078 17.396  1.00 21.24 ? 201  LEU D CD2 1 
ATOM   6695 N  N   . VAL D  1 202 ? 45.635  -13.858 22.298  1.00 8.38  ? 202  VAL D N   1 
ATOM   6696 C  CA  . VAL D  1 202 ? 44.910  -14.352 23.474  1.00 8.13  ? 202  VAL D CA  1 
ATOM   6697 C  C   . VAL D  1 202 ? 43.442  -13.941 23.499  1.00 9.82  ? 202  VAL D C   1 
ATOM   6698 O  O   . VAL D  1 202 ? 42.677  -14.388 24.368  1.00 12.21 ? 202  VAL D O   1 
ATOM   6699 C  CB  . VAL D  1 202 ? 45.595  -13.912 24.793  1.00 10.28 ? 202  VAL D CB  1 
ATOM   6700 C  CG1 . VAL D  1 202 ? 47.059  -14.357 24.813  1.00 15.57 ? 202  VAL D CG1 1 
ATOM   6701 C  CG2 . VAL D  1 202 ? 45.471  -12.398 24.990  1.00 10.70 ? 202  VAL D CG2 1 
ATOM   6702 N  N   . TRP D  1 203 ? 43.045  -13.112 22.540  1.00 8.79  ? 203  TRP D N   1 
ATOM   6703 C  CA  . TRP D  1 203 ? 41.722  -12.503 22.565  1.00 12.62 ? 203  TRP D CA  1 
ATOM   6704 C  C   . TRP D  1 203 ? 40.712  -13.066 21.580  1.00 16.82 ? 203  TRP D C   1 
ATOM   6705 O  O   . TRP D  1 203 ? 39.589  -12.573 21.506  1.00 25.54 ? 203  TRP D O   1 
ATOM   6706 C  CB  . TRP D  1 203 ? 41.794  -10.981 22.391  1.00 12.27 ? 203  TRP D CB  1 
ATOM   6707 C  CG  . TRP D  1 203 ? 42.807  -10.487 21.416  1.00 8.46  ? 203  TRP D CG  1 
ATOM   6708 C  CD1 . TRP D  1 203 ? 44.104  -10.150 21.682  1.00 10.09 ? 203  TRP D CD1 1 
ATOM   6709 C  CD2 . TRP D  1 203 ? 42.605  -10.224 20.022  1.00 9.59  ? 203  TRP D CD2 1 
ATOM   6710 N  NE1 . TRP D  1 203 ? 44.724  -9.706  20.544  1.00 10.42 ? 203  TRP D NE1 1 
ATOM   6711 C  CE2 . TRP D  1 203 ? 43.825  -9.739  19.508  1.00 8.01  ? 203  TRP D CE2 1 
ATOM   6712 C  CE3 . TRP D  1 203 ? 41.510  -10.359 19.156  1.00 12.95 ? 203  TRP D CE3 1 
ATOM   6713 C  CZ2 . TRP D  1 203 ? 43.992  -9.396  18.169  1.00 10.88 ? 203  TRP D CZ2 1 
ATOM   6714 C  CZ3 . TRP D  1 203 ? 41.677  -10.006 17.821  1.00 12.67 ? 203  TRP D CZ3 1 
ATOM   6715 C  CH2 . TRP D  1 203 ? 42.906  -9.525  17.345  1.00 9.55  ? 203  TRP D CH2 1 
ATOM   6716 N  N   . VAL D  1 204 ? 41.091  -14.075 20.819  1.00 16.77 ? 204  VAL D N   1 
ATOM   6717 C  CA  . VAL D  1 204 ? 40.088  -14.761 20.011  1.00 38.79 ? 204  VAL D CA  1 
ATOM   6718 C  C   . VAL D  1 204 ? 39.414  -15.902 20.773  1.00 46.44 ? 204  VAL D C   1 
ATOM   6719 O  O   . VAL D  1 204 ? 40.058  -16.670 21.489  1.00 48.48 ? 204  VAL D O   1 
ATOM   6720 C  CB  . VAL D  1 204 ? 40.663  -15.250 18.675  1.00 36.52 ? 204  VAL D CB  1 
ATOM   6721 C  CG1 . VAL D  1 204 ? 39.853  -16.424 18.136  1.00 44.21 ? 204  VAL D CG1 1 
ATOM   6722 C  CG2 . VAL D  1 204 ? 40.669  -14.102 17.689  1.00 23.44 ? 204  VAL D CG2 1 
ATOM   6723 O  OXT . VAL D  1 204 ? 38.196  -16.070 20.698  1.00 62.31 ? 204  VAL D OXT 1 
ATOM   6724 N  N   . HIS E  1 1   ? 51.642  -14.864 56.802  1.00 31.67 ? 1    HIS E N   1 
ATOM   6725 C  CA  . HIS E  1 1   ? 51.476  -14.781 58.247  1.00 36.76 ? 1    HIS E CA  1 
ATOM   6726 C  C   . HIS E  1 1   ? 50.008  -14.739 58.660  1.00 27.65 ? 1    HIS E C   1 
ATOM   6727 O  O   . HIS E  1 1   ? 49.669  -15.170 59.757  1.00 27.98 ? 1    HIS E O   1 
ATOM   6728 C  CB  . HIS E  1 1   ? 52.244  -13.585 58.798  1.00 35.57 ? 1    HIS E CB  1 
ATOM   6729 C  CG  . HIS E  1 1   ? 53.653  -13.511 58.298  1.00 31.92 ? 1    HIS E CG  1 
ATOM   6730 N  ND1 . HIS E  1 1   ? 53.975  -13.699 56.970  1.00 35.64 ? 1    HIS E ND1 1 
ATOM   6731 C  CD2 . HIS E  1 1   ? 54.822  -13.288 58.941  1.00 43.69 ? 1    HIS E CD2 1 
ATOM   6732 C  CE1 . HIS E  1 1   ? 55.282  -13.587 56.816  1.00 33.96 ? 1    HIS E CE1 1 
ATOM   6733 N  NE2 . HIS E  1 1   ? 55.819  -13.337 57.997  1.00 42.38 ? 1    HIS E NE2 1 
ATOM   6734 N  N   . THR E  1 2   ? 49.139  -14.231 57.789  1.00 15.97 ? 2    THR E N   1 
ATOM   6735 C  CA  . THR E  1 2   ? 47.700  -14.320 58.035  1.00 10.85 ? 2    THR E CA  1 
ATOM   6736 C  C   . THR E  1 2   ? 46.954  -14.896 56.836  1.00 10.79 ? 2    THR E C   1 
ATOM   6737 O  O   . THR E  1 2   ? 47.164  -14.481 55.707  1.00 9.93  ? 2    THR E O   1 
ATOM   6738 C  CB  . THR E  1 2   ? 47.096  -12.949 58.384  1.00 19.79 ? 2    THR E CB  1 
ATOM   6739 O  OG1 . THR E  1 2   ? 47.747  -12.428 59.547  1.00 23.96 ? 2    THR E OG1 1 
ATOM   6740 C  CG2 . THR E  1 2   ? 45.608  -13.071 58.658  1.00 15.92 ? 2    THR E CG2 1 
ATOM   6741 N  N   . ASP E  1 3   ? 46.074  -15.858 57.091  1.00 9.60  ? 3    ASP E N   1 
ATOM   6742 C  CA  . ASP E  1 3   ? 45.231  -16.412 56.038  1.00 10.26 ? 3    ASP E CA  1 
ATOM   6743 C  C   . ASP E  1 3   ? 43.950  -15.592 55.915  1.00 10.11 ? 3    ASP E C   1 
ATOM   6744 O  O   . ASP E  1 3   ? 43.076  -15.627 56.797  1.00 10.08 ? 3    ASP E O   1 
ATOM   6745 C  CB  . ASP E  1 3   ? 44.897  -17.876 56.361  1.00 9.60  ? 3    ASP E CB  1 
ATOM   6746 C  CG  . ASP E  1 3   ? 43.967  -18.506 55.347  1.00 13.01 ? 3    ASP E CG  1 
ATOM   6747 O  OD1 . ASP E  1 3   ? 43.769  -17.919 54.263  1.00 10.69 ? 3    ASP E OD1 1 
ATOM   6748 O  OD2 . ASP E  1 3   ? 43.449  -19.612 55.626  1.00 12.66 ? 3    ASP E OD2 1 
ATOM   6749 N  N   . LEU E  1 4   ? 43.840  -14.837 54.825  1.00 9.24  ? 4    LEU E N   1 
ATOM   6750 C  CA  . LEU E  1 4   ? 42.669  -13.997 54.604  1.00 5.67  ? 4    LEU E CA  1 
ATOM   6751 C  C   . LEU E  1 4   ? 41.659  -14.629 53.650  1.00 7.56  ? 4    LEU E C   1 
ATOM   6752 O  O   . LEU E  1 4   ? 40.788  -13.934 53.134  1.00 8.94  ? 4    LEU E O   1 
ATOM   6753 C  CB  . LEU E  1 4   ? 43.099  -12.622 54.069  1.00 8.32  ? 4    LEU E CB  1 
ATOM   6754 C  CG  . LEU E  1 4   ? 43.904  -11.790 55.066  1.00 10.78 ? 4    LEU E CG  1 
ATOM   6755 C  CD1 . LEU E  1 4   ? 44.387  -10.490 54.414  1.00 10.82 ? 4    LEU E CD1 1 
ATOM   6756 C  CD2 . LEU E  1 4   ? 43.107  -11.495 56.314  1.00 12.12 ? 4    LEU E CD2 1 
ATOM   6757 N  N   . SER E  1 5   ? 41.747  -15.943 53.441  1.00 8.42  ? 5    SER E N   1 
ATOM   6758 C  CA  . SER E  1 5   ? 40.753  -16.635 52.620  1.00 8.91  ? 5    SER E CA  1 
ATOM   6759 C  C   . SER E  1 5   ? 39.337  -16.221 52.996  1.00 9.43  ? 5    SER E C   1 
ATOM   6760 O  O   . SER E  1 5   ? 38.957  -16.267 54.164  1.00 9.83  ? 5    SER E O   1 
ATOM   6761 C  CB  . SER E  1 5   ? 40.869  -18.159 52.768  1.00 9.31  ? 5    SER E CB  1 
ATOM   6762 O  OG  . SER E  1 5   ? 42.131  -18.617 52.325  1.00 10.01 ? 5    SER E OG  1 
ATOM   6763 N  N   . GLY E  1 6   ? 38.565  -15.814 51.994  1.00 8.96  ? 6    GLY E N   1 
ATOM   6764 C  CA  . GLY E  1 6   ? 37.170  -15.482 52.196  1.00 8.60  ? 6    GLY E CA  1 
ATOM   6765 C  C   . GLY E  1 6   ? 36.921  -14.157 52.890  1.00 8.81  ? 6    GLY E C   1 
ATOM   6766 O  O   . GLY E  1 6   ? 35.796  -13.885 53.304  1.00 9.33  ? 6    GLY E O   1 
ATOM   6767 N  N   . LYS E  1 7   ? 37.968  -13.342 53.011  1.00 8.19  ? 7    LYS E N   1 
ATOM   6768 C  CA  . LYS E  1 7   ? 37.862  -12.037 53.659  1.00 7.52  ? 7    LYS E CA  1 
ATOM   6769 C  C   . LYS E  1 7   ? 38.390  -10.933 52.749  1.00 6.45  ? 7    LYS E C   1 
ATOM   6770 O  O   . LYS E  1 7   ? 39.164  -11.191 51.813  1.00 8.95  ? 7    LYS E O   1 
ATOM   6771 C  CB  . LYS E  1 7   ? 38.641  -12.026 54.973  1.00 9.18  ? 7    LYS E CB  1 
ATOM   6772 C  CG  . LYS E  1 7   ? 38.107  -13.060 55.951  1.00 9.83  ? 7    LYS E CG  1 
ATOM   6773 C  CD  . LYS E  1 7   ? 38.965  -13.185 57.181  1.00 14.09 ? 7    LYS E CD  1 
ATOM   6774 C  CE  . LYS E  1 7   ? 38.379  -14.273 58.084  1.00 19.43 ? 7    LYS E CE  1 
ATOM   6775 N  NZ  . LYS E  1 7   ? 39.203  -14.485 59.299  1.00 31.15 ? 7    LYS E NZ  1 
ATOM   6776 N  N   . VAL E  1 8   ? 37.951  -9.711  53.038  1.00 7.10  ? 8    VAL E N   1 
ATOM   6777 C  CA  . VAL E  1 8   ? 38.415  -8.515  52.340  1.00 6.74  ? 8    VAL E CA  1 
ATOM   6778 C  C   . VAL E  1 8   ? 38.918  -7.489  53.350  1.00 7.01  ? 8    VAL E C   1 
ATOM   6779 O  O   . VAL E  1 8   ? 38.526  -7.514  54.510  1.00 7.16  ? 8    VAL E O   1 
ATOM   6780 C  CB  . VAL E  1 8   ? 37.268  -7.824  51.549  1.00 7.85  ? 8    VAL E CB  1 
ATOM   6781 C  CG1 . VAL E  1 8   ? 36.843  -8.656  50.350  1.00 10.96 ? 8    VAL E CG1 1 
ATOM   6782 C  CG2 . VAL E  1 8   ? 36.059  -7.543  52.459  1.00 7.47  ? 8    VAL E CG2 1 
ATOM   6783 N  N   . PHE E  1 9   ? 39.806  -6.593  52.907  1.00 6.50  ? 9    PHE E N   1 
ATOM   6784 C  CA  . PHE E  1 9   ? 39.992  -5.323  53.617  1.00 5.82  ? 9    PHE E CA  1 
ATOM   6785 C  C   . PHE E  1 9   ? 38.889  -4.374  53.172  1.00 8.54  ? 9    PHE E C   1 
ATOM   6786 O  O   . PHE E  1 9   ? 38.656  -4.193  51.962  1.00 5.72  ? 9    PHE E O   1 
ATOM   6787 C  CB  . PHE E  1 9   ? 41.333  -4.677  53.255  1.00 5.84  ? 9    PHE E CB  1 
ATOM   6788 C  CG  . PHE E  1 9   ? 42.538  -5.414  53.758  1.00 7.73  ? 9    PHE E CG  1 
ATOM   6789 C  CD1 . PHE E  1 9   ? 42.728  -5.633  55.122  1.00 9.71  ? 9    PHE E CD1 1 
ATOM   6790 C  CD2 . PHE E  1 9   ? 43.504  -5.857  52.869  1.00 9.53  ? 9    PHE E CD2 1 
ATOM   6791 C  CE1 . PHE E  1 9   ? 43.844  -6.302  55.577  1.00 9.19  ? 9    PHE E CE1 1 
ATOM   6792 C  CE2 . PHE E  1 9   ? 44.640  -6.537  53.327  1.00 11.00 ? 9    PHE E CE2 1 
ATOM   6793 C  CZ  . PHE E  1 9   ? 44.803  -6.755  54.680  1.00 12.61 ? 9    PHE E CZ  1 
ATOM   6794 N  N   . VAL E  1 10  ? 38.194  -3.785  54.146  1.00 5.70  ? 10   VAL E N   1 
ATOM   6795 C  CA  . VAL E  1 10  ? 37.231  -2.729  53.879  1.00 6.56  ? 10   VAL E CA  1 
ATOM   6796 C  C   . VAL E  1 10  ? 37.839  -1.393  54.294  1.00 6.29  ? 10   VAL E C   1 
ATOM   6797 O  O   . VAL E  1 10  ? 38.213  -1.201  55.451  1.00 6.97  ? 10   VAL E O   1 
ATOM   6798 C  CB  . VAL E  1 10  ? 35.921  -2.927  54.668  1.00 5.66  ? 10   VAL E CB  1 
ATOM   6799 C  CG1 . VAL E  1 10  ? 34.902  -1.843  54.265  1.00 8.63  ? 10   VAL E CG1 1 
ATOM   6800 C  CG2 . VAL E  1 10  ? 35.375  -4.355  54.475  1.00 8.38  ? 10   VAL E CG2 1 
ATOM   6801 N  N   . PHE E  1 11  ? 37.962  -0.483  53.333  1.00 6.62  ? 11   PHE E N   1 
ATOM   6802 C  CA  . PHE E  1 11  ? 38.360  0.894   53.592  1.00 6.20  ? 11   PHE E CA  1 
ATOM   6803 C  C   . PHE E  1 11  ? 37.054  1.680   53.574  1.00 6.88  ? 11   PHE E C   1 
ATOM   6804 O  O   . PHE E  1 11  ? 36.552  2.036   52.505  1.00 6.23  ? 11   PHE E O   1 
ATOM   6805 C  CB  . PHE E  1 11  ? 39.326  1.380   52.491  1.00 5.26  ? 11   PHE E CB  1 
ATOM   6806 C  CG  . PHE E  1 11  ? 40.559  0.521   52.353  1.00 6.03  ? 11   PHE E CG  1 
ATOM   6807 C  CD1 . PHE E  1 11  ? 40.532  -0.646  51.597  1.00 7.69  ? 11   PHE E CD1 1 
ATOM   6808 C  CD2 . PHE E  1 11  ? 41.733  0.861   53.017  1.00 8.70  ? 11   PHE E CD2 1 
ATOM   6809 C  CE1 . PHE E  1 11  ? 41.668  -1.440  51.476  1.00 8.49  ? 11   PHE E CE1 1 
ATOM   6810 C  CE2 . PHE E  1 11  ? 42.873  0.070   52.912  1.00 7.00  ? 11   PHE E CE2 1 
ATOM   6811 C  CZ  . PHE E  1 11  ? 42.838  -1.086  52.139  1.00 9.54  ? 11   PHE E CZ  1 
ATOM   6812 N  N   . PRO E  1 12  ? 36.470  1.918   54.758  1.00 7.29  ? 12   PRO E N   1 
ATOM   6813 C  CA  . PRO E  1 12  ? 35.045  2.279   54.805  1.00 6.95  ? 12   PRO E CA  1 
ATOM   6814 C  C   . PRO E  1 12  ? 34.735  3.751   54.604  1.00 7.54  ? 12   PRO E C   1 
ATOM   6815 O  O   . PRO E  1 12  ? 33.559  4.120   54.511  1.00 8.54  ? 12   PRO E O   1 
ATOM   6816 C  CB  . PRO E  1 12  ? 34.608  1.833   56.221  1.00 6.82  ? 12   PRO E CB  1 
ATOM   6817 C  CG  . PRO E  1 12  ? 35.790  1.018   56.774  1.00 9.11  ? 12   PRO E CG  1 
ATOM   6818 C  CD  . PRO E  1 12  ? 36.996  1.614   56.099  1.00 7.96  ? 12   PRO E CD  1 
ATOM   6819 N  N   . ARG E  1 13  ? 35.768  4.581   54.540  1.00 8.17  ? 13   ARG E N   1 
ATOM   6820 C  CA  . ARG E  1 13  ? 35.564  6.007   54.356  1.00 8.21  ? 13   ARG E CA  1 
ATOM   6821 C  C   . ARG E  1 13  ? 36.761  6.606   53.641  1.00 10.81 ? 13   ARG E C   1 
ATOM   6822 O  O   . ARG E  1 13  ? 37.844  6.013   53.599  1.00 8.10  ? 13   ARG E O   1 
ATOM   6823 C  CB  . ARG E  1 13  ? 35.452  6.689   55.711  1.00 10.21 ? 13   ARG E CB  1 
ATOM   6824 C  CG  . ARG E  1 13  ? 36.727  6.452   56.493  1.00 13.84 ? 13   ARG E CG  1 
ATOM   6825 C  CD  . ARG E  1 13  ? 37.064  7.517   57.491  1.00 17.03 ? 13   ARG E CD  1 
ATOM   6826 N  NE  . ARG E  1 13  ? 38.359  7.229   58.102  1.00 13.08 ? 13   ARG E NE  1 
ATOM   6827 C  CZ  . ARG E  1 13  ? 38.745  7.692   59.284  1.00 12.77 ? 13   ARG E CZ  1 
ATOM   6828 N  NH1 . ARG E  1 13  ? 37.928  8.476   59.975  1.00 15.81 ? 13   ARG E NH1 1 
ATOM   6829 N  NH2 . ARG E  1 13  ? 39.944  7.376   59.771  1.00 14.25 ? 13   ARG E NH2 1 
ATOM   6830 N  N   . GLU E  1 14  ? 36.554  7.804   53.101  1.00 9.01  ? 14   GLU E N   1 
ATOM   6831 C  CA  . GLU E  1 14  ? 37.637  8.565   52.491  1.00 10.80 ? 14   GLU E CA  1 
ATOM   6832 C  C   . GLU E  1 14  ? 38.492  9.210   53.570  1.00 8.68  ? 14   GLU E C   1 
ATOM   6833 O  O   . GLU E  1 14  ? 37.973  9.739   54.547  1.00 10.74 ? 14   GLU E O   1 
ATOM   6834 C  CB  . GLU E  1 14  ? 37.082  9.648   51.570  1.00 8.39  ? 14   GLU E CB  1 
ATOM   6835 C  CG  . GLU E  1 14  ? 38.177  10.456  50.874  1.00 8.18  ? 14   GLU E CG  1 
ATOM   6836 C  CD  . GLU E  1 14  ? 37.647  11.317  49.753  1.00 9.26  ? 14   GLU E CD  1 
ATOM   6837 O  OE1 . GLU E  1 14  ? 36.939  10.779  48.865  1.00 11.78 ? 14   GLU E OE1 1 
ATOM   6838 O  OE2 . GLU E  1 14  ? 37.968  12.530  49.745  1.00 15.23 ? 14   GLU E OE2 1 
ATOM   6839 N  N   . SER E  1 15  ? 39.807  9.141   53.393  1.00 7.61  ? 15   SER E N   1 
ATOM   6840 C  CA  . SER E  1 15  ? 40.748  9.711   54.350  1.00 7.96  ? 15   SER E CA  1 
ATOM   6841 C  C   . SER E  1 15  ? 42.090  9.883   53.666  1.00 10.72 ? 15   SER E C   1 
ATOM   6842 O  O   . SER E  1 15  ? 42.277  9.422   52.546  1.00 8.42  ? 15   SER E O   1 
ATOM   6843 C  CB  . SER E  1 15  ? 40.949  8.756   55.524  1.00 9.21  ? 15   SER E CB  1 
ATOM   6844 O  OG  . SER E  1 15  ? 41.771  7.664   55.126  1.00 10.13 ? 15   SER E OG  1 
ATOM   6845 N  N   . VAL E  1 16  ? 43.029  10.537  54.350  1.00 9.46  ? 16   VAL E N   1 
ATOM   6846 C  CA  . VAL E  1 16  ? 44.404  10.577  53.884  1.00 10.20 ? 16   VAL E CA  1 
ATOM   6847 C  C   . VAL E  1 16  ? 45.249  9.629   54.742  1.00 12.94 ? 16   VAL E C   1 
ATOM   6848 O  O   . VAL E  1 16  ? 46.443  9.474   54.504  1.00 21.14 ? 16   VAL E O   1 
ATOM   6849 C  CB  . VAL E  1 16  ? 44.972  12.016  53.953  1.00 13.93 ? 16   VAL E CB  1 
ATOM   6850 C  CG1 . VAL E  1 16  ? 45.194  12.427  55.396  1.00 18.93 ? 16   VAL E CG1 1 
ATOM   6851 C  CG2 . VAL E  1 16  ? 46.255  12.142  53.132  1.00 17.77 ? 16   VAL E CG2 1 
ATOM   6852 N  N   . THR E  1 17  ? 44.611  8.984   55.725  1.00 11.39 ? 17   THR E N   1 
ATOM   6853 C  CA  . THR E  1 17  ? 45.315  8.205   56.755  1.00 14.37 ? 17   THR E CA  1 
ATOM   6854 C  C   . THR E  1 17  ? 45.167  6.687   56.684  1.00 11.83 ? 17   THR E C   1 
ATOM   6855 O  O   . THR E  1 17  ? 46.089  5.950   57.050  1.00 12.43 ? 17   THR E O   1 
ATOM   6856 C  CB  . THR E  1 17  ? 44.816  8.596   58.168  1.00 14.84 ? 17   THR E CB  1 
ATOM   6857 O  OG1 . THR E  1 17  ? 43.392  8.416   58.246  1.00 22.92 ? 17   THR E OG1 1 
ATOM   6858 C  CG2 . THR E  1 17  ? 45.159  10.027  58.475  1.00 21.98 ? 17   THR E CG2 1 
ATOM   6859 N  N   . ASP E  1 18  ? 43.995  6.227   56.263  1.00 10.23 ? 18   ASP E N   1 
ATOM   6860 C  CA  . ASP E  1 18  ? 43.657  4.810   56.331  1.00 8.54  ? 18   ASP E CA  1 
ATOM   6861 C  C   . ASP E  1 18  ? 44.383  4.043   55.229  1.00 7.52  ? 18   ASP E C   1 
ATOM   6862 O  O   . ASP E  1 18  ? 44.228  4.360   54.055  1.00 8.96  ? 18   ASP E O   1 
ATOM   6863 C  CB  . ASP E  1 18  ? 42.148  4.607   56.137  1.00 7.79  ? 18   ASP E CB  1 
ATOM   6864 C  CG  . ASP E  1 18  ? 41.299  5.430   57.111  1.00 9.02  ? 18   ASP E CG  1 
ATOM   6865 O  OD1 . ASP E  1 18  ? 41.767  5.764   58.232  1.00 12.28 ? 18   ASP E OD1 1 
ATOM   6866 O  OD2 . ASP E  1 18  ? 40.142  5.709   56.752  1.00 10.53 ? 18   ASP E OD2 1 
ATOM   6867 N  N   . HIS E  1 19  ? 45.151  3.022   55.603  1.00 6.85  ? 19   HIS E N   1 
ATOM   6868 C  CA  . HIS E  1 19  ? 45.868  2.212   54.614  1.00 7.75  ? 19   HIS E CA  1 
ATOM   6869 C  C   . HIS E  1 19  ? 46.318  0.875   55.173  1.00 7.04  ? 19   HIS E C   1 
ATOM   6870 O  O   . HIS E  1 19  ? 46.291  0.657   56.383  1.00 9.02  ? 19   HIS E O   1 
ATOM   6871 C  CB  . HIS E  1 19  ? 47.072  2.978   54.018  1.00 7.03  ? 19   HIS E CB  1 
ATOM   6872 C  CG  . HIS E  1 19  ? 48.163  3.287   54.996  1.00 9.35  ? 19   HIS E CG  1 
ATOM   6873 N  ND1 . HIS E  1 19  ? 48.048  4.271   55.959  1.00 11.98 ? 19   HIS E ND1 1 
ATOM   6874 C  CD2 . HIS E  1 19  ? 49.411  2.774   55.133  1.00 13.00 ? 19   HIS E CD2 1 
ATOM   6875 C  CE1 . HIS E  1 19  ? 49.170  4.339   56.654  1.00 14.37 ? 19   HIS E CE1 1 
ATOM   6876 N  NE2 . HIS E  1 19  ? 50.016  3.444   56.169  1.00 13.41 ? 19   HIS E NE2 1 
ATOM   6877 N  N   . VAL E  1 20  ? 46.720  -0.020  54.276  1.00 7.73  ? 20   VAL E N   1 
ATOM   6878 C  CA  . VAL E  1 20  ? 47.341  -1.268  54.679  1.00 7.29  ? 20   VAL E CA  1 
ATOM   6879 C  C   . VAL E  1 20  ? 48.724  -1.330  54.052  1.00 10.49 ? 20   VAL E C   1 
ATOM   6880 O  O   . VAL E  1 20  ? 48.879  -1.106  52.848  1.00 11.68 ? 20   VAL E O   1 
ATOM   6881 C  CB  . VAL E  1 20  ? 46.512  -2.494  54.235  1.00 6.92  ? 20   VAL E CB  1 
ATOM   6882 C  CG1 . VAL E  1 20  ? 47.189  -3.777  54.712  1.00 10.10 ? 20   VAL E CG1 1 
ATOM   6883 C  CG2 . VAL E  1 20  ? 45.088  -2.411  54.791  1.00 9.25  ? 20   VAL E CG2 1 
ATOM   6884 N  N   . ASN E  1 21  ? 49.736  -1.604  54.870  1.00 6.54  ? 21   ASN E N   1 
ATOM   6885 C  CA  . ASN E  1 21  ? 51.074  -1.878  54.353  1.00 8.47  ? 21   ASN E CA  1 
ATOM   6886 C  C   . ASN E  1 21  ? 51.219  -3.363  54.115  1.00 9.27  ? 21   ASN E C   1 
ATOM   6887 O  O   . ASN E  1 21  ? 50.912  -4.164  55.005  1.00 10.98 ? 21   ASN E O   1 
ATOM   6888 C  CB  . ASN E  1 21  ? 52.134  -1.458  55.369  1.00 12.14 ? 21   ASN E CB  1 
ATOM   6889 C  CG  . ASN E  1 21  ? 52.136  0.031   55.626  1.00 15.26 ? 21   ASN E CG  1 
ATOM   6890 O  OD1 . ASN E  1 21  ? 52.031  0.832   54.699  1.00 16.32 ? 21   ASN E OD1 1 
ATOM   6891 N  ND2 . ASN E  1 21  ? 52.291  0.413   56.892  1.00 20.15 ? 21   ASN E ND2 1 
ATOM   6892 N  N   . LEU E  1 22  ? 51.695  -3.731  52.929  1.00 8.41  ? 22   LEU E N   1 
ATOM   6893 C  CA  . LEU E  1 22  ? 51.953  -5.129  52.613  1.00 8.77  ? 22   LEU E CA  1 
ATOM   6894 C  C   . LEU E  1 22  ? 53.451  -5.366  52.650  1.00 11.75 ? 22   LEU E C   1 
ATOM   6895 O  O   . LEU E  1 22  ? 54.224  -4.638  52.019  1.00 12.38 ? 22   LEU E O   1 
ATOM   6896 C  CB  . LEU E  1 22  ? 51.392  -5.492  51.238  1.00 8.02  ? 22   LEU E CB  1 
ATOM   6897 C  CG  . LEU E  1 22  ? 49.895  -5.243  51.057  1.00 9.23  ? 22   LEU E CG  1 
ATOM   6898 C  CD1 . LEU E  1 22  ? 49.448  -5.667  49.666  1.00 10.22 ? 22   LEU E CD1 1 
ATOM   6899 C  CD2 . LEU E  1 22  ? 49.060  -5.963  52.135  1.00 9.77  ? 22   LEU E CD2 1 
ATOM   6900 N  N   . ILE E  1 23  ? 53.851  -6.382  53.404  1.00 10.18 ? 23   ILE E N   1 
ATOM   6901 C  CA  . ILE E  1 23  ? 55.257  -6.655  53.647  1.00 12.18 ? 23   ILE E CA  1 
ATOM   6902 C  C   . ILE E  1 23  ? 55.703  -7.868  52.848  1.00 13.02 ? 23   ILE E C   1 
ATOM   6903 O  O   . ILE E  1 23  ? 55.099  -8.930  52.923  1.00 13.97 ? 23   ILE E O   1 
ATOM   6904 C  CB  . ILE E  1 23  ? 55.518  -6.881  55.156  1.00 16.04 ? 23   ILE E CB  1 
ATOM   6905 C  CG1 . ILE E  1 23  ? 55.030  -5.667  55.955  1.00 19.61 ? 23   ILE E CG1 1 
ATOM   6906 C  CG2 . ILE E  1 23  ? 56.994  -7.182  55.410  1.00 22.44 ? 23   ILE E CG2 1 
ATOM   6907 C  CD1 . ILE E  1 23  ? 54.960  -5.890  57.450  1.00 25.80 ? 23   ILE E CD1 1 
ATOM   6908 N  N   . THR E  1 24  ? 56.753  -7.693  52.054  1.00 15.65 ? 24   THR E N   1 
ATOM   6909 C  CA  . THR E  1 24  ? 57.333  -8.813  51.324  1.00 18.23 ? 24   THR E CA  1 
ATOM   6910 C  C   . THR E  1 24  ? 58.852  -8.665  51.406  1.00 19.22 ? 24   THR E C   1 
ATOM   6911 O  O   . THR E  1 24  ? 59.373  -7.548  51.344  1.00 24.70 ? 24   THR E O   1 
ATOM   6912 C  CB  . THR E  1 24  ? 56.831  -8.857  49.852  1.00 19.02 ? 24   THR E CB  1 
ATOM   6913 O  OG1 . THR E  1 24  ? 57.473  -9.925  49.133  1.00 21.06 ? 24   THR E OG1 1 
ATOM   6914 C  CG2 . THR E  1 24  ? 57.101  -7.536  49.145  1.00 21.62 ? 24   THR E CG2 1 
ATOM   6915 N  N   . PRO E  1 25  ? 59.563  -9.785  51.579  1.00 25.60 ? 25   PRO E N   1 
ATOM   6916 C  CA  . PRO E  1 25  ? 61.028  -9.762  51.592  1.00 29.76 ? 25   PRO E CA  1 
ATOM   6917 C  C   . PRO E  1 25  ? 61.575  -9.785  50.173  1.00 34.08 ? 25   PRO E C   1 
ATOM   6918 O  O   . PRO E  1 25  ? 62.257  -10.734 49.785  1.00 38.73 ? 25   PRO E O   1 
ATOM   6919 C  CB  . PRO E  1 25  ? 61.366  -11.065 52.305  1.00 30.30 ? 25   PRO E CB  1 
ATOM   6920 C  CG  . PRO E  1 25  ? 60.299  -12.010 51.807  1.00 30.91 ? 25   PRO E CG  1 
ATOM   6921 C  CD  . PRO E  1 25  ? 59.039  -11.163 51.651  1.00 24.94 ? 25   PRO E CD  1 
ATOM   6922 N  N   . LEU E  1 26  ? 61.269  -8.750  49.401  1.00 23.14 ? 26   LEU E N   1 
ATOM   6923 C  CA  . LEU E  1 26  ? 61.700  -8.703  48.016  1.00 17.59 ? 26   LEU E CA  1 
ATOM   6924 C  C   . LEU E  1 26  ? 62.999  -7.933  47.886  1.00 24.84 ? 26   LEU E C   1 
ATOM   6925 O  O   . LEU E  1 26  ? 63.025  -6.706  48.028  1.00 26.34 ? 26   LEU E O   1 
ATOM   6926 C  CB  . LEU E  1 26  ? 60.614  -8.088  47.129  1.00 22.09 ? 26   LEU E CB  1 
ATOM   6927 C  CG  . LEU E  1 26  ? 60.962  -8.092  45.639  1.00 30.49 ? 26   LEU E CG  1 
ATOM   6928 C  CD1 . LEU E  1 26  ? 61.282  -9.511  45.153  1.00 24.21 ? 26   LEU E CD1 1 
ATOM   6929 C  CD2 . LEU E  1 26  ? 59.835  -7.475  44.834  1.00 29.12 ? 26   LEU E CD2 1 
ATOM   6930 N  N   . GLU E  1 27  ? 64.075  -8.665  47.607  1.00 21.92 ? 27   GLU E N   1 
ATOM   6931 C  CA  . GLU E  1 27  ? 65.407  -8.081  47.543  1.00 28.36 ? 27   GLU E CA  1 
ATOM   6932 C  C   . GLU E  1 27  ? 65.952  -8.016  46.121  1.00 17.92 ? 27   GLU E C   1 
ATOM   6933 O  O   . GLU E  1 27  ? 66.880  -7.257  45.845  1.00 23.79 ? 27   GLU E O   1 
ATOM   6934 C  CB  . GLU E  1 27  ? 66.363  -8.880  48.432  1.00 29.82 ? 27   GLU E CB  1 
ATOM   6935 C  CG  . GLU E  1 27  ? 65.753  -9.280  49.767  1.00 39.19 ? 27   GLU E CG  1 
ATOM   6936 C  CD  . GLU E  1 27  ? 66.711  -10.078 50.631  1.00 61.29 ? 27   GLU E CD  1 
ATOM   6937 O  OE1 . GLU E  1 27  ? 66.236  -10.883 51.462  1.00 65.37 ? 27   GLU E OE1 1 
ATOM   6938 O  OE2 . GLU E  1 27  ? 67.939  -9.902  50.473  1.00 67.40 ? 27   GLU E OE2 1 
ATOM   6939 N  N   . LYS E  1 28  ? 65.379  -8.816  45.224  1.00 18.82 ? 28   LYS E N   1 
ATOM   6940 C  CA  . LYS E  1 28  ? 65.850  -8.875  43.843  1.00 21.18 ? 28   LYS E CA  1 
ATOM   6941 C  C   . LYS E  1 28  ? 64.953  -8.017  42.956  1.00 20.05 ? 28   LYS E C   1 
ATOM   6942 O  O   . LYS E  1 28  ? 63.739  -8.174  42.977  1.00 21.51 ? 28   LYS E O   1 
ATOM   6943 C  CB  . LYS E  1 28  ? 65.857  -10.326 43.349  1.00 24.12 ? 28   LYS E CB  1 
ATOM   6944 C  CG  . LYS E  1 28  ? 66.993  -11.165 43.934  1.00 31.10 ? 28   LYS E CG  1 
ATOM   6945 C  CD  . LYS E  1 28  ? 66.609  -12.636 44.077  1.00 43.18 ? 28   LYS E CD  1 
ATOM   6946 C  CE  . LYS E  1 28  ? 66.238  -13.262 42.745  1.00 39.98 ? 28   LYS E CE  1 
ATOM   6947 N  NZ  . LYS E  1 28  ? 66.264  -14.752 42.825  1.00 27.48 ? 28   LYS E NZ  1 
ATOM   6948 N  N   . PRO E  1 29  ? 65.544  -7.093  42.189  1.00 19.75 ? 29   PRO E N   1 
ATOM   6949 C  CA  . PRO E  1 29  ? 64.701  -6.315  41.274  1.00 14.05 ? 29   PRO E CA  1 
ATOM   6950 C  C   . PRO E  1 29  ? 63.914  -7.233  40.344  1.00 14.97 ? 29   PRO E C   1 
ATOM   6951 O  O   . PRO E  1 29  ? 64.389  -8.315  39.983  1.00 18.17 ? 29   PRO E O   1 
ATOM   6952 C  CB  . PRO E  1 29  ? 65.717  -5.509  40.472  1.00 17.70 ? 29   PRO E CB  1 
ATOM   6953 C  CG  . PRO E  1 29  ? 66.878  -5.349  41.400  1.00 24.19 ? 29   PRO E CG  1 
ATOM   6954 C  CD  . PRO E  1 29  ? 66.940  -6.618  42.201  1.00 18.81 ? 29   PRO E CD  1 
ATOM   6955 N  N   . LEU E  1 30  ? 62.728  -6.788  39.947  1.00 11.95 ? 30   LEU E N   1 
ATOM   6956 C  CA  . LEU E  1 30  ? 61.805  -7.608  39.181  1.00 13.69 ? 30   LEU E CA  1 
ATOM   6957 C  C   . LEU E  1 30  ? 61.929  -7.371  37.693  1.00 12.62 ? 30   LEU E C   1 
ATOM   6958 O  O   . LEU E  1 30  ? 61.823  -6.236  37.228  1.00 11.60 ? 30   LEU E O   1 
ATOM   6959 C  CB  . LEU E  1 30  ? 60.365  -7.281  39.588  1.00 11.22 ? 30   LEU E CB  1 
ATOM   6960 C  CG  . LEU E  1 30  ? 59.909  -7.694  40.987  1.00 18.19 ? 30   LEU E CG  1 
ATOM   6961 C  CD1 . LEU E  1 30  ? 58.582  -7.041  41.297  1.00 15.15 ? 30   LEU E CD1 1 
ATOM   6962 C  CD2 . LEU E  1 30  ? 59.819  -9.209  41.101  1.00 20.52 ? 30   LEU E CD2 1 
ATOM   6963 N  N   . GLN E  1 31  ? 62.113  -8.458  36.956  1.00 10.78 ? 31   GLN E N   1 
ATOM   6964 C  CA  . GLN E  1 31  ? 62.105  -8.421  35.512  1.00 9.54  ? 31   GLN E CA  1 
ATOM   6965 C  C   . GLN E  1 31  ? 60.713  -8.770  35.002  1.00 11.06 ? 31   GLN E C   1 
ATOM   6966 O  O   . GLN E  1 31  ? 60.277  -8.268  33.961  1.00 14.00 ? 31   GLN E O   1 
ATOM   6967 C  CB  . GLN E  1 31  ? 63.154  -9.395  34.966  1.00 16.97 ? 31   GLN E CB  1 
ATOM   6968 C  CG  . GLN E  1 31  ? 63.822  -8.926  33.691  1.00 33.19 ? 31   GLN E CG  1 
ATOM   6969 C  CD  . GLN E  1 31  ? 64.915  -9.869  33.230  1.00 41.13 ? 31   GLN E CD  1 
ATOM   6970 O  OE1 . GLN E  1 31  ? 65.403  -10.698 34.003  1.00 35.29 ? 31   GLN E OE1 1 
ATOM   6971 N  NE2 . GLN E  1 31  ? 65.300  -9.752  31.966  1.00 31.77 ? 31   GLN E NE2 1 
ATOM   6972 N  N   . ASN E  1 32  ? 60.014  -9.629  35.745  1.00 9.09  ? 32   ASN E N   1 
ATOM   6973 C  CA  . ASN E  1 32  ? 58.674  -10.073 35.369  1.00 9.62  ? 32   ASN E CA  1 
ATOM   6974 C  C   . ASN E  1 32  ? 57.785  -10.058 36.597  1.00 9.40  ? 32   ASN E C   1 
ATOM   6975 O  O   . ASN E  1 32  ? 58.233  -10.399 37.691  1.00 9.83  ? 32   ASN E O   1 
ATOM   6976 C  CB  . ASN E  1 32  ? 58.676  -11.526 34.864  1.00 10.57 ? 32   ASN E CB  1 
ATOM   6977 C  CG  . ASN E  1 32  ? 59.563  -11.756 33.641  1.00 18.17 ? 32   ASN E CG  1 
ATOM   6978 O  OD1 . ASN E  1 32  ? 59.495  -11.036 32.653  1.00 17.07 ? 32   ASN E OD1 1 
ATOM   6979 N  ND2 . ASN E  1 32  ? 60.380  -12.798 33.713  1.00 26.89 ? 32   ASN E ND2 1 
ATOM   6980 N  N   . PHE E  1 33  ? 56.519  -9.696  36.439  1.00 7.48  ? 33   PHE E N   1 
ATOM   6981 C  CA  . PHE E  1 33  ? 55.585  -9.944  37.537  1.00 7.73  ? 33   PHE E CA  1 
ATOM   6982 C  C   . PHE E  1 33  ? 54.159  -10.024 37.032  1.00 8.37  ? 33   PHE E C   1 
ATOM   6983 O  O   . PHE E  1 33  ? 53.847  -9.591  35.917  1.00 7.53  ? 33   PHE E O   1 
ATOM   6984 C  CB  . PHE E  1 33  ? 55.663  -8.848  38.608  1.00 7.79  ? 33   PHE E CB  1 
ATOM   6985 C  CG  . PHE E  1 33  ? 55.042  -7.545  38.172  1.00 6.61  ? 33   PHE E CG  1 
ATOM   6986 C  CD1 . PHE E  1 33  ? 53.682  -7.309  38.340  1.00 7.57  ? 33   PHE E CD1 1 
ATOM   6987 C  CD2 . PHE E  1 33  ? 55.816  -6.573  37.574  1.00 8.50  ? 33   PHE E CD2 1 
ATOM   6988 C  CE1 . PHE E  1 33  ? 53.115  -6.115  37.905  1.00 6.90  ? 33   PHE E CE1 1 
ATOM   6989 C  CE2 . PHE E  1 33  ? 55.265  -5.374  37.143  1.00 10.50 ? 33   PHE E CE2 1 
ATOM   6990 C  CZ  . PHE E  1 33  ? 53.911  -5.144  37.313  1.00 9.16  ? 33   PHE E CZ  1 
ATOM   6991 N  N   . THR E  1 34  ? 53.305  -10.609 37.861  1.00 6.85  ? 34   THR E N   1 
ATOM   6992 C  CA  . THR E  1 34  ? 51.864  -10.564 37.658  1.00 6.03  ? 34   THR E CA  1 
ATOM   6993 C  C   . THR E  1 34  ? 51.243  -10.239 39.002  1.00 7.76  ? 34   THR E C   1 
ATOM   6994 O  O   . THR E  1 34  ? 51.695  -10.723 40.035  1.00 7.87  ? 34   THR E O   1 
ATOM   6995 C  CB  . THR E  1 34  ? 51.288  -11.916 37.170  1.00 5.84  ? 34   THR E CB  1 
ATOM   6996 O  OG1 . THR E  1 34  ? 51.975  -12.332 35.984  1.00 7.54  ? 34   THR E OG1 1 
ATOM   6997 C  CG2 . THR E  1 34  ? 49.798  -11.775 36.858  1.00 7.46  ? 34   THR E CG2 1 
ATOM   6998 N  N   . LEU E  1 35  ? 50.212  -9.407  38.977  1.00 6.93  ? 35   LEU E N   1 
ATOM   6999 C  CA  . LEU E  1 35  ? 49.476  -9.024  40.175  1.00 7.28  ? 35   LEU E CA  1 
ATOM   7000 C  C   . LEU E  1 35  ? 47.989  -9.233  39.886  1.00 6.82  ? 35   LEU E C   1 
ATOM   7001 O  O   . LEU E  1 35  ? 47.484  -8.714  38.885  1.00 7.44  ? 35   LEU E O   1 
ATOM   7002 C  CB  . LEU E  1 35  ? 49.740  -7.536  40.469  1.00 6.91  ? 35   LEU E CB  1 
ATOM   7003 C  CG  . LEU E  1 35  ? 48.873  -6.841  41.510  1.00 10.96 ? 35   LEU E CG  1 
ATOM   7004 C  CD1 . LEU E  1 35  ? 49.143  -7.385  42.915  1.00 11.24 ? 35   LEU E CD1 1 
ATOM   7005 C  CD2 . LEU E  1 35  ? 49.132  -5.325  41.456  1.00 10.78 ? 35   LEU E CD2 1 
ATOM   7006 N  N   . CYS E  1 36  ? 47.284  -9.973  40.751  1.00 6.64  ? 36   CYS E N   1 
ATOM   7007 C  CA  . CYS E  1 36  ? 45.833  -10.161 40.611  1.00 8.05  ? 36   CYS E CA  1 
ATOM   7008 C  C   . CYS E  1 36  ? 45.150  -9.793  41.922  1.00 8.18  ? 36   CYS E C   1 
ATOM   7009 O  O   . CYS E  1 36  ? 45.720  -9.992  42.998  1.00 8.37  ? 36   CYS E O   1 
ATOM   7010 C  CB  . CYS E  1 36  ? 45.484  -11.630 40.268  1.00 9.04  ? 36   CYS E CB  1 
ATOM   7011 S  SG  . CYS E  1 36  ? 46.081  -12.238 38.652  1.00 13.02 ? 36   CYS E SG  1 
ATOM   7012 N  N   . PHE E  1 37  ? 43.938  -9.248  41.847  1.00 6.74  ? 37   PHE E N   1 
ATOM   7013 C  CA  . PHE E  1 37  ? 43.144  -9.003  43.053  1.00 7.03  ? 37   PHE E CA  1 
ATOM   7014 C  C   . PHE E  1 37  ? 41.714  -8.680  42.654  1.00 6.35  ? 37   PHE E C   1 
ATOM   7015 O  O   . PHE E  1 37  ? 41.432  -8.460  41.460  1.00 7.75  ? 37   PHE E O   1 
ATOM   7016 C  CB  . PHE E  1 37  ? 43.745  -7.852  43.891  1.00 7.97  ? 37   PHE E CB  1 
ATOM   7017 C  CG  . PHE E  1 37  ? 43.938  -6.584  43.115  1.00 7.28  ? 37   PHE E CG  1 
ATOM   7018 C  CD1 . PHE E  1 37  ? 45.125  -6.352  42.435  1.00 10.57 ? 37   PHE E CD1 1 
ATOM   7019 C  CD2 . PHE E  1 37  ? 42.922  -5.639  43.037  1.00 8.88  ? 37   PHE E CD2 1 
ATOM   7020 C  CE1 . PHE E  1 37  ? 45.293  -5.200  41.686  1.00 11.28 ? 37   PHE E CE1 1 
ATOM   7021 C  CE2 . PHE E  1 37  ? 43.088  -4.487  42.299  1.00 10.75 ? 37   PHE E CE2 1 
ATOM   7022 C  CZ  . PHE E  1 37  ? 44.264  -4.263  41.628  1.00 9.52  ? 37   PHE E CZ  1 
ATOM   7023 N  N   . ARG E  1 38  ? 40.802  -8.680  43.633  1.00 6.22  ? 38   ARG E N   1 
ATOM   7024 C  CA  . ARG E  1 38  ? 39.417  -8.267  43.399  1.00 6.13  ? 38   ARG E CA  1 
ATOM   7025 C  C   . ARG E  1 38  ? 39.151  -6.976  44.115  1.00 8.25  ? 38   ARG E C   1 
ATOM   7026 O  O   . ARG E  1 38  ? 39.661  -6.761  45.215  1.00 9.09  ? 38   ARG E O   1 
ATOM   7027 C  CB  . ARG E  1 38  ? 38.430  -9.289  43.971  1.00 8.75  ? 38   ARG E CB  1 
ATOM   7028 C  CG  . ARG E  1 38  ? 38.500  -10.612 43.342  1.00 12.31 ? 38   ARG E CG  1 
ATOM   7029 C  CD  . ARG E  1 38  ? 37.512  -11.567 44.012  1.00 12.67 ? 38   ARG E CD  1 
ATOM   7030 N  NE  . ARG E  1 38  ? 37.909  -12.913 43.669  1.00 12.70 ? 38   ARG E NE  1 
ATOM   7031 C  CZ  . ARG E  1 38  ? 37.668  -13.476 42.493  1.00 13.53 ? 38   ARG E CZ  1 
ATOM   7032 N  NH1 . ARG E  1 38  ? 36.993  -12.805 41.563  1.00 13.01 ? 38   ARG E NH1 1 
ATOM   7033 N  NH2 . ARG E  1 38  ? 38.082  -14.711 42.256  1.00 18.09 ? 38   ARG E NH2 1 
ATOM   7034 N  N   . ALA E  1 39  ? 38.340  -6.114  43.512  1.00 5.81  ? 39   ALA E N   1 
ATOM   7035 C  CA  . ALA E  1 39  ? 37.997  -4.868  44.184  1.00 5.49  ? 39   ALA E CA  1 
ATOM   7036 C  C   . ALA E  1 39  ? 36.539  -4.504  43.955  1.00 6.82  ? 39   ALA E C   1 
ATOM   7037 O  O   . ALA E  1 39  ? 35.945  -4.855  42.936  1.00 6.75  ? 39   ALA E O   1 
ATOM   7038 C  CB  . ALA E  1 39  ? 38.907  -3.734  43.692  1.00 6.99  ? 39   ALA E CB  1 
ATOM   7039 N  N   . TYR E  1 40  ? 35.976  -3.767  44.900  1.00 5.33  ? 40   TYR E N   1 
ATOM   7040 C  CA  . TYR E  1 40  ? 34.599  -3.323  44.780  1.00 6.98  ? 40   TYR E CA  1 
ATOM   7041 C  C   . TYR E  1 40  ? 34.544  -1.931  45.383  1.00 6.31  ? 40   TYR E C   1 
ATOM   7042 O  O   . TYR E  1 40  ? 34.758  -1.754  46.588  1.00 8.06  ? 40   TYR E O   1 
ATOM   7043 C  CB  . TYR E  1 40  ? 33.682  -4.299  45.527  1.00 6.30  ? 40   TYR E CB  1 
ATOM   7044 C  CG  . TYR E  1 40  ? 32.190  -4.119  45.339  1.00 7.77  ? 40   TYR E CG  1 
ATOM   7045 C  CD1 . TYR E  1 40  ? 31.667  -3.428  44.246  1.00 6.04  ? 40   TYR E CD1 1 
ATOM   7046 C  CD2 . TYR E  1 40  ? 31.299  -4.686  46.246  1.00 6.08  ? 40   TYR E CD2 1 
ATOM   7047 C  CE1 . TYR E  1 40  ? 30.277  -3.282  44.089  1.00 6.57  ? 40   TYR E CE1 1 
ATOM   7048 C  CE2 . TYR E  1 40  ? 29.916  -4.558  46.096  1.00 5.66  ? 40   TYR E CE2 1 
ATOM   7049 C  CZ  . TYR E  1 40  ? 29.417  -3.857  45.020  1.00 6.49  ? 40   TYR E CZ  1 
ATOM   7050 O  OH  . TYR E  1 40  ? 28.060  -3.724  44.865  1.00 8.29  ? 40   TYR E OH  1 
ATOM   7051 N  N   . SER E  1 41  ? 34.292  -0.940  44.532  1.00 5.71  ? 41   SER E N   1 
ATOM   7052 C  CA  . SER E  1 41  ? 34.223  0.445   44.983  1.00 4.76  ? 41   SER E CA  1 
ATOM   7053 C  C   . SER E  1 41  ? 33.144  1.162   44.201  1.00 8.62  ? 41   SER E C   1 
ATOM   7054 O  O   . SER E  1 41  ? 32.936  0.846   43.033  1.00 11.99 ? 41   SER E O   1 
ATOM   7055 C  CB  . SER E  1 41  ? 35.568  1.135   44.722  1.00 6.91  ? 41   SER E CB  1 
ATOM   7056 O  OG  . SER E  1 41  ? 35.504  2.518   45.052  1.00 7.08  ? 41   SER E OG  1 
ATOM   7057 N  N   . ASP E  1 42  ? 32.459  2.123   44.817  1.00 6.04  ? 42   ASP E N   1 
ATOM   7058 C  CA  . ASP E  1 42  ? 31.544  2.971   44.046  1.00 5.95  ? 42   ASP E CA  1 
ATOM   7059 C  C   . ASP E  1 42  ? 32.038  4.415   43.881  1.00 6.39  ? 42   ASP E C   1 
ATOM   7060 O  O   . ASP E  1 42  ? 31.255  5.347   43.641  1.00 8.85  ? 42   ASP E O   1 
ATOM   7061 C  CB  . ASP E  1 42  ? 30.082  2.878   44.540  1.00 9.62  ? 42   ASP E CB  1 
ATOM   7062 C  CG  . ASP E  1 42  ? 29.906  3.266   45.998  1.00 9.91  ? 42   ASP E CG  1 
ATOM   7063 O  OD1 . ASP E  1 42  ? 30.761  3.984   46.551  1.00 10.76 ? 42   ASP E OD1 1 
ATOM   7064 O  OD2 . ASP E  1 42  ? 28.876  2.856   46.592  1.00 10.79 ? 42   ASP E OD2 1 
ATOM   7065 N  N   . LEU E  1 43  ? 33.354  4.594   43.981  1.00 8.28  ? 43   LEU E N   1 
ATOM   7066 C  CA  . LEU E  1 43  ? 33.970  5.876   43.651  1.00 7.05  ? 43   LEU E CA  1 
ATOM   7067 C  C   . LEU E  1 43  ? 33.921  6.122   42.149  1.00 7.74  ? 43   LEU E C   1 
ATOM   7068 O  O   . LEU E  1 43  ? 34.152  5.209   41.353  1.00 10.59 ? 43   LEU E O   1 
ATOM   7069 C  CB  . LEU E  1 43  ? 35.442  5.871   44.046  1.00 6.58  ? 43   LEU E CB  1 
ATOM   7070 C  CG  . LEU E  1 43  ? 35.751  5.929   45.544  1.00 7.88  ? 43   LEU E CG  1 
ATOM   7071 C  CD1 . LEU E  1 43  ? 37.249  5.788   45.749  1.00 4.99  ? 43   LEU E CD1 1 
ATOM   7072 C  CD2 . LEU E  1 43  ? 35.245  7.231   46.147  1.00 9.00  ? 43   LEU E CD2 1 
ATOM   7073 N  N   . SER E  1 44  ? 33.654  7.371   41.774  1.00 10.92 ? 44   SER E N   1 
ATOM   7074 C  CA  . SER E  1 44  ? 33.773  7.796   40.389  1.00 11.93 ? 44   SER E CA  1 
ATOM   7075 C  C   . SER E  1 44  ? 35.077  8.551   40.143  1.00 9.59  ? 44   SER E C   1 
ATOM   7076 O  O   . SER E  1 44  ? 35.562  8.587   39.008  1.00 11.22 ? 44   SER E O   1 
ATOM   7077 C  CB  . SER E  1 44  ? 32.583  8.676   40.004  1.00 14.25 ? 44   SER E CB  1 
ATOM   7078 O  OG  . SER E  1 44  ? 31.402  7.902   39.907  1.00 19.44 ? 44   SER E OG  1 
ATOM   7079 N  N   . ARG E  1 45  ? 35.640  9.167   41.188  1.00 6.69  ? 45   ARG E N   1 
ATOM   7080 C  CA  . ARG E  1 45  ? 36.899  9.876   41.014  1.00 6.91  ? 45   ARG E CA  1 
ATOM   7081 C  C   . ARG E  1 45  ? 38.042  8.883   40.850  1.00 10.16 ? 45   ARG E C   1 
ATOM   7082 O  O   . ARG E  1 45  ? 37.858  7.689   41.049  1.00 9.56  ? 45   ARG E O   1 
ATOM   7083 C  CB  . ARG E  1 45  ? 37.183  10.795  42.201  1.00 9.73  ? 45   ARG E CB  1 
ATOM   7084 C  CG  . ARG E  1 45  ? 37.291  10.068  43.538  1.00 10.66 ? 45   ARG E CG  1 
ATOM   7085 C  CD  . ARG E  1 45  ? 38.079  10.912  44.556  1.00 8.88  ? 45   ARG E CD  1 
ATOM   7086 N  NE  . ARG E  1 45  ? 37.956  10.340  45.897  1.00 7.88  ? 45   ARG E NE  1 
ATOM   7087 C  CZ  . ARG E  1 45  ? 38.678  9.307   46.324  1.00 7.35  ? 45   ARG E CZ  1 
ATOM   7088 N  NH1 . ARG E  1 45  ? 39.575  8.757   45.522  1.00 7.78  ? 45   ARG E NH1 1 
ATOM   7089 N  NH2 . ARG E  1 45  ? 38.501  8.826   47.550  1.00 8.67  ? 45   ARG E NH2 1 
ATOM   7090 N  N   . ALA E  1 46  ? 39.223  9.386   40.497  1.00 9.45  ? 46   ALA E N   1 
ATOM   7091 C  CA  . ALA E  1 46  ? 40.408  8.542   40.353  1.00 10.06 ? 46   ALA E CA  1 
ATOM   7092 C  C   . ALA E  1 46  ? 40.815  7.909   41.678  1.00 11.05 ? 46   ALA E C   1 
ATOM   7093 O  O   . ALA E  1 46  ? 40.591  8.468   42.753  1.00 9.97  ? 46   ALA E O   1 
ATOM   7094 C  CB  . ALA E  1 46  ? 41.581  9.360   39.786  1.00 12.46 ? 46   ALA E CB  1 
ATOM   7095 N  N   . TYR E  1 47  ? 41.439  6.746   41.602  1.00 7.52  ? 47   TYR E N   1 
ATOM   7096 C  CA  . TYR E  1 47  ? 41.983  6.140   42.806  1.00 6.92  ? 47   TYR E CA  1 
ATOM   7097 C  C   . TYR E  1 47  ? 43.060  5.115   42.524  1.00 7.87  ? 47   TYR E C   1 
ATOM   7098 O  O   . TYR E  1 47  ? 43.097  4.505   41.459  1.00 9.04  ? 47   TYR E O   1 
ATOM   7099 C  CB  . TYR E  1 47  ? 40.878  5.532   43.671  1.00 8.80  ? 47   TYR E CB  1 
ATOM   7100 C  CG  . TYR E  1 47  ? 39.976  4.525   42.997  1.00 7.66  ? 47   TYR E CG  1 
ATOM   7101 C  CD1 . TYR E  1 47  ? 38.744  4.909   42.487  1.00 6.62  ? 47   TYR E CD1 1 
ATOM   7102 C  CD2 . TYR E  1 47  ? 40.340  3.178   42.899  1.00 8.38  ? 47   TYR E CD2 1 
ATOM   7103 C  CE1 . TYR E  1 47  ? 37.882  3.983   41.878  1.00 7.64  ? 47   TYR E CE1 1 
ATOM   7104 C  CE2 . TYR E  1 47  ? 39.481  2.242   42.307  1.00 9.27  ? 47   TYR E CE2 1 
ATOM   7105 C  CZ  . TYR E  1 47  ? 38.254  2.653   41.811  1.00 10.27 ? 47   TYR E CZ  1 
ATOM   7106 O  OH  . TYR E  1 47  ? 37.397  1.746   41.222  1.00 10.11 ? 47   TYR E OH  1 
ATOM   7107 N  N   . SER E  1 48  ? 43.953  4.965   43.496  1.00 6.44  ? 48   SER E N   1 
ATOM   7108 C  CA  . SER E  1 48  ? 45.015  3.973   43.442  1.00 6.89  ? 48   SER E CA  1 
ATOM   7109 C  C   . SER E  1 48  ? 44.532  2.622   43.953  1.00 7.24  ? 48   SER E C   1 
ATOM   7110 O  O   . SER E  1 48  ? 43.887  2.544   44.993  1.00 9.06  ? 48   SER E O   1 
ATOM   7111 C  CB  . SER E  1 48  ? 46.202  4.426   44.297  1.00 8.16  ? 48   SER E CB  1 
ATOM   7112 O  OG  . SER E  1 48  ? 47.213  3.432   44.325  1.00 9.31  ? 48   SER E OG  1 
ATOM   7113 N  N   . LEU E  1 49  ? 44.818  1.567   43.192  1.00 5.99  ? 49   LEU E N   1 
ATOM   7114 C  CA  . LEU E  1 49  ? 44.511  0.205   43.608  1.00 7.75  ? 49   LEU E CA  1 
ATOM   7115 C  C   . LEU E  1 49  ? 45.688  -0.478  44.301  1.00 7.26  ? 49   LEU E C   1 
ATOM   7116 O  O   . LEU E  1 49  ? 45.487  -1.213  45.247  1.00 7.09  ? 49   LEU E O   1 
ATOM   7117 C  CB  . LEU E  1 49  ? 44.027  -0.635  42.414  1.00 5.40  ? 49   LEU E CB  1 
ATOM   7118 C  CG  . LEU E  1 49  ? 42.611  -0.285  41.944  1.00 8.54  ? 49   LEU E CG  1 
ATOM   7119 C  CD1 . LEU E  1 49  ? 42.359  -0.717  40.501  1.00 12.21 ? 49   LEU E CD1 1 
ATOM   7120 C  CD2 . LEU E  1 49  ? 41.566  -0.884  42.903  1.00 9.89  ? 49   LEU E CD2 1 
ATOM   7121 N  N   . PHE E  1 50  ? 46.911  -0.223  43.834  1.00 6.48  ? 50   PHE E N   1 
ATOM   7122 C  CA  . PHE E  1 50  ? 48.105  -0.909  44.353  1.00 6.24  ? 50   PHE E CA  1 
ATOM   7123 C  C   . PHE E  1 50  ? 49.276  0.019   44.119  1.00 7.92  ? 50   PHE E C   1 
ATOM   7124 O  O   . PHE E  1 50  ? 49.596  0.322   42.968  1.00 7.00  ? 50   PHE E O   1 
ATOM   7125 C  CB  . PHE E  1 50  ? 48.321  -2.227  43.597  1.00 7.19  ? 50   PHE E CB  1 
ATOM   7126 C  CG  . PHE E  1 50  ? 49.478  -3.064  44.090  1.00 5.95  ? 50   PHE E CG  1 
ATOM   7127 C  CD1 . PHE E  1 50  ? 49.277  -4.044  45.046  1.00 8.64  ? 50   PHE E CD1 1 
ATOM   7128 C  CD2 . PHE E  1 50  ? 50.754  -2.905  43.547  1.00 6.98  ? 50   PHE E CD2 1 
ATOM   7129 C  CE1 . PHE E  1 50  ? 50.318  -4.845  45.481  1.00 8.24  ? 50   PHE E CE1 1 
ATOM   7130 C  CE2 . PHE E  1 50  ? 51.818  -3.724  43.963  1.00 8.38  ? 50   PHE E CE2 1 
ATOM   7131 C  CZ  . PHE E  1 50  ? 51.593  -4.693  44.932  1.00 8.51  ? 50   PHE E CZ  1 
ATOM   7132 N  N   . SER E  1 51  ? 49.899  0.465   45.212  1.00 5.95  ? 51   SER E N   1 
ATOM   7133 C  CA  . SER E  1 51  ? 50.980  1.471   45.170  1.00 4.69  ? 51   SER E CA  1 
ATOM   7134 C  C   . SER E  1 51  ? 52.286  0.896   45.692  1.00 8.20  ? 51   SER E C   1 
ATOM   7135 O  O   . SER E  1 51  ? 52.372  0.503   46.857  1.00 7.85  ? 51   SER E O   1 
ATOM   7136 C  CB  . SER E  1 51  ? 50.572  2.678   46.025  1.00 5.91  ? 51   SER E CB  1 
ATOM   7137 O  OG  . SER E  1 51  ? 51.619  3.639   46.126  1.00 8.19  ? 51   SER E OG  1 
ATOM   7138 N  N   . TYR E  1 52  ? 53.301  0.858   44.829  1.00 6.01  ? 52   TYR E N   1 
ATOM   7139 C  CA  . TYR E  1 52  ? 54.601  0.252   45.144  1.00 7.66  ? 52   TYR E CA  1 
ATOM   7140 C  C   . TYR E  1 52  ? 55.679  1.288   44.818  1.00 7.07  ? 52   TYR E C   1 
ATOM   7141 O  O   . TYR E  1 52  ? 55.896  1.642   43.658  1.00 8.08  ? 52   TYR E O   1 
ATOM   7142 C  CB  . TYR E  1 52  ? 54.725  -1.036  44.311  1.00 7.19  ? 52   TYR E CB  1 
ATOM   7143 C  CG  . TYR E  1 52  ? 56.030  -1.815  44.241  1.00 7.32  ? 52   TYR E CG  1 
ATOM   7144 C  CD1 . TYR E  1 52  ? 57.217  -1.224  43.794  1.00 10.27 ? 52   TYR E CD1 1 
ATOM   7145 C  CD2 . TYR E  1 52  ? 56.039  -3.182  44.503  1.00 7.32  ? 52   TYR E CD2 1 
ATOM   7146 C  CE1 . TYR E  1 52  ? 58.398  -1.983  43.671  1.00 8.32  ? 52   TYR E CE1 1 
ATOM   7147 C  CE2 . TYR E  1 52  ? 57.198  -3.940  44.387  1.00 8.68  ? 52   TYR E CE2 1 
ATOM   7148 C  CZ  . TYR E  1 52  ? 58.373  -3.339  43.964  1.00 8.63  ? 52   TYR E CZ  1 
ATOM   7149 O  OH  . TYR E  1 52  ? 59.533  -4.100  43.851  1.00 11.22 ? 52   TYR E OH  1 
ATOM   7150 N  N   . ASN E  1 53  ? 56.311  1.808   45.865  1.00 7.51  ? 53   ASN E N   1 
ATOM   7151 C  CA  . ASN E  1 53  ? 57.341  2.850   45.739  1.00 9.62  ? 53   ASN E CA  1 
ATOM   7152 C  C   . ASN E  1 53  ? 58.644  2.337   46.326  1.00 11.53 ? 53   ASN E C   1 
ATOM   7153 O  O   . ASN E  1 53  ? 58.629  1.483   47.198  1.00 9.64  ? 53   ASN E O   1 
ATOM   7154 C  CB  . ASN E  1 53  ? 56.927  4.102   46.514  1.00 8.76  ? 53   ASN E CB  1 
ATOM   7155 C  CG  . ASN E  1 53  ? 56.099  5.066   45.688  1.00 9.61  ? 53   ASN E CG  1 
ATOM   7156 O  OD1 . ASN E  1 53  ? 55.531  4.698   44.665  1.00 9.47  ? 53   ASN E OD1 1 
ATOM   7157 N  ND2 . ASN E  1 53  ? 56.036  6.324   46.129  1.00 8.07  ? 53   ASN E ND2 1 
ATOM   7158 N  N   . THR E  1 54  ? 59.776  2.858   45.853  1.00 9.88  ? 54   THR E N   1 
ATOM   7159 C  CA  . THR E  1 54  ? 61.056  2.472   46.437  1.00 12.02 ? 54   THR E CA  1 
ATOM   7160 C  C   . THR E  1 54  ? 61.786  3.750   46.827  1.00 12.16 ? 54   THR E C   1 
ATOM   7161 O  O   . THR E  1 54  ? 61.311  4.854   46.542  1.00 12.35 ? 54   THR E O   1 
ATOM   7162 C  CB  . THR E  1 54  ? 61.917  1.593   45.482  1.00 10.44 ? 54   THR E CB  1 
ATOM   7163 O  OG1 . THR E  1 54  ? 62.203  2.321   44.287  1.00 14.48 ? 54   THR E OG1 1 
ATOM   7164 C  CG2 . THR E  1 54  ? 61.170  0.312   45.103  1.00 10.40 ? 54   THR E CG2 1 
ATOM   7165 N  N   . GLN E  1 55  ? 62.924  3.623   47.500  1.00 12.85 ? 55   GLN E N   1 
ATOM   7166 C  CA  . GLN E  1 55  ? 63.574  4.825   48.014  1.00 13.29 ? 55   GLN E CA  1 
ATOM   7167 C  C   . GLN E  1 55  ? 63.967  5.759   46.869  1.00 16.53 ? 55   GLN E C   1 
ATOM   7168 O  O   . GLN E  1 55  ? 64.720  5.374   45.971  1.00 17.42 ? 55   GLN E O   1 
ATOM   7169 C  CB  . GLN E  1 55  ? 64.794  4.481   48.867  1.00 20.06 ? 55   GLN E CB  1 
ATOM   7170 C  CG  . GLN E  1 55  ? 65.481  5.711   49.453  1.00 20.81 ? 55   GLN E CG  1 
ATOM   7171 C  CD  . GLN E  1 55  ? 64.555  6.533   50.339  1.00 24.16 ? 55   GLN E CD  1 
ATOM   7172 O  OE1 . GLN E  1 55  ? 63.994  6.024   51.304  1.00 26.62 ? 55   GLN E OE1 1 
ATOM   7173 N  NE2 . GLN E  1 55  ? 64.401  7.812   50.015  1.00 29.68 ? 55   GLN E NE2 1 
ATOM   7174 N  N   . GLY E  1 56  ? 63.437  6.978   46.907  1.00 12.97 ? 56   GLY E N   1 
ATOM   7175 C  CA  . GLY E  1 56  ? 63.723  7.983   45.901  1.00 16.45 ? 56   GLY E CA  1 
ATOM   7176 C  C   . GLY E  1 56  ? 62.979  7.837   44.584  1.00 14.24 ? 56   GLY E C   1 
ATOM   7177 O  O   . GLY E  1 56  ? 63.212  8.612   43.654  1.00 15.02 ? 56   GLY E O   1 
ATOM   7178 N  N   . ARG E  1 57  ? 62.066  6.868   44.510  1.00 12.27 ? 57   ARG E N   1 
ATOM   7179 C  CA  . ARG E  1 57  ? 61.359  6.575   43.264  1.00 8.03  ? 57   ARG E CA  1 
ATOM   7180 C  C   . ARG E  1 57  ? 59.858  6.461   43.475  1.00 9.27  ? 57   ARG E C   1 
ATOM   7181 O  O   . ARG E  1 57  ? 59.381  5.522   44.122  1.00 12.04 ? 57   ARG E O   1 
ATOM   7182 C  CB  . ARG E  1 57  ? 61.882  5.271   42.669  1.00 10.00 ? 57   ARG E CB  1 
ATOM   7183 C  CG  . ARG E  1 57  ? 63.378  5.311   42.362  1.00 12.32 ? 57   ARG E CG  1 
ATOM   7184 C  CD  . ARG E  1 57  ? 63.817  4.065   41.607  1.00 10.82 ? 57   ARG E CD  1 
ATOM   7185 N  NE  . ARG E  1 57  ? 63.380  4.080   40.216  1.00 10.91 ? 57   ARG E NE  1 
ATOM   7186 C  CZ  . ARG E  1 57  ? 64.006  4.737   39.244  1.00 18.08 ? 57   ARG E CZ  1 
ATOM   7187 N  NH1 . ARG E  1 57  ? 65.079  5.465   39.524  1.00 18.18 ? 57   ARG E NH1 1 
ATOM   7188 N  NH2 . ARG E  1 57  ? 63.553  4.682   37.997  1.00 14.44 ? 57   ARG E NH2 1 
ATOM   7189 N  N   . ASP E  1 58  ? 59.125  7.419   42.925  1.00 10.52 ? 58   ASP E N   1 
ATOM   7190 C  CA  . ASP E  1 58  ? 57.671  7.429   43.004  1.00 10.19 ? 58   ASP E CA  1 
ATOM   7191 C  C   . ASP E  1 58  ? 57.094  6.633   41.839  1.00 9.10  ? 58   ASP E C   1 
ATOM   7192 O  O   . ASP E  1 58  ? 57.668  6.601   40.748  1.00 10.34 ? 58   ASP E O   1 
ATOM   7193 C  CB  . ASP E  1 58  ? 57.157  8.862   42.930  1.00 9.21  ? 58   ASP E CB  1 
ATOM   7194 C  CG  . ASP E  1 58  ? 55.678  8.970   43.248  1.00 9.39  ? 58   ASP E CG  1 
ATOM   7195 O  OD1 . ASP E  1 58  ? 55.193  8.165   44.062  1.00 10.53 ? 58   ASP E OD1 1 
ATOM   7196 O  OD2 . ASP E  1 58  ? 55.007  9.856   42.685  1.00 12.15 ? 58   ASP E OD2 1 
ATOM   7197 N  N   . ASN E  1 59  ? 55.941  6.016   42.072  1.00 8.54  ? 59   ASN E N   1 
ATOM   7198 C  CA  . ASN E  1 59  ? 55.268  5.254   41.038  1.00 7.49  ? 59   ASN E CA  1 
ATOM   7199 C  C   . ASN E  1 59  ? 56.172  4.230   40.372  1.00 7.95  ? 59   ASN E C   1 
ATOM   7200 O  O   . ASN E  1 59  ? 56.168  4.090   39.143  1.00 7.71  ? 59   ASN E O   1 
ATOM   7201 C  CB  . ASN E  1 59  ? 54.643  6.183   39.996  1.00 9.49  ? 59   ASN E CB  1 
ATOM   7202 C  CG  . ASN E  1 59  ? 53.719  7.199   40.617  1.00 7.23  ? 59   ASN E CG  1 
ATOM   7203 O  OD1 . ASN E  1 59  ? 53.387  7.097   41.801  1.00 8.54  ? 59   ASN E OD1 1 
ATOM   7204 N  ND2 . ASN E  1 59  ? 53.290  8.186   39.837  1.00 7.75  ? 59   ASN E ND2 1 
ATOM   7205 N  N   . GLU E  1 60  ? 56.938  3.516   41.192  1.00 7.07  ? 60   GLU E N   1 
ATOM   7206 C  CA  . GLU E  1 60  ? 57.834  2.479   40.690  1.00 8.19  ? 60   GLU E CA  1 
ATOM   7207 C  C   . GLU E  1 60  ? 57.016  1.345   40.090  1.00 7.74  ? 60   GLU E C   1 
ATOM   7208 O  O   . GLU E  1 60  ? 57.355  0.807   39.036  1.00 7.16  ? 60   GLU E O   1 
ATOM   7209 C  CB  . GLU E  1 60  ? 58.754  1.979   41.818  1.00 9.06  ? 60   GLU E CB  1 
ATOM   7210 C  CG  . GLU E  1 60  ? 59.838  0.997   41.375  1.00 9.92  ? 60   GLU E CG  1 
ATOM   7211 C  CD  . GLU E  1 60  ? 60.795  1.560   40.340  1.00 9.90  ? 60   GLU E CD  1 
ATOM   7212 O  OE1 . GLU E  1 60  ? 60.842  2.787   40.152  1.00 11.34 ? 60   GLU E OE1 1 
ATOM   7213 O  OE2 . GLU E  1 60  ? 61.513  0.749   39.725  1.00 10.35 ? 60   GLU E OE2 1 
ATOM   7214 N  N   . LEU E  1 61  ? 55.913  1.004   40.753  1.00 8.12  ? 61   LEU E N   1 
ATOM   7215 C  CA  . LEU E  1 61  ? 54.947  0.056   40.203  1.00 6.55  ? 61   LEU E CA  1 
ATOM   7216 C  C   . LEU E  1 61  ? 53.599  0.470   40.776  1.00 9.05  ? 61   LEU E C   1 
ATOM   7217 O  O   . LEU E  1 61  ? 53.386  0.412   41.984  1.00 8.58  ? 61   LEU E O   1 
ATOM   7218 C  CB  . LEU E  1 61  ? 55.318  -1.387  40.579  1.00 5.91  ? 61   LEU E CB  1 
ATOM   7219 C  CG  . LEU E  1 61  ? 54.584  -2.557  39.903  1.00 9.03  ? 61   LEU E CG  1 
ATOM   7220 C  CD1 . LEU E  1 61  ? 55.194  -3.868  40.413  1.00 9.56  ? 61   LEU E CD1 1 
ATOM   7221 C  CD2 . LEU E  1 61  ? 53.084  -2.547  40.175  1.00 8.58  ? 61   LEU E CD2 1 
ATOM   7222 N  N   . LEU E  1 62  ? 52.713  0.967   39.917  1.00 6.88  ? 62   LEU E N   1 
ATOM   7223 C  CA  . LEU E  1 62  ? 51.428  1.503   40.384  1.00 7.87  ? 62   LEU E CA  1 
ATOM   7224 C  C   . LEU E  1 62  ? 50.299  1.061   39.464  1.00 7.01  ? 62   LEU E C   1 
ATOM   7225 O  O   . LEU E  1 62  ? 50.409  1.171   38.235  1.00 6.93  ? 62   LEU E O   1 
ATOM   7226 C  CB  . LEU E  1 62  ? 51.484  3.032   40.442  1.00 7.59  ? 62   LEU E CB  1 
ATOM   7227 C  CG  . LEU E  1 62  ? 50.180  3.824   40.643  1.00 6.54  ? 62   LEU E CG  1 
ATOM   7228 C  CD1 . LEU E  1 62  ? 49.571  3.536   42.017  1.00 7.17  ? 62   LEU E CD1 1 
ATOM   7229 C  CD2 . LEU E  1 62  ? 50.410  5.321   40.451  1.00 9.33  ? 62   LEU E CD2 1 
ATOM   7230 N  N   . VAL E  1 63  ? 49.218  0.562   40.068  1.00 6.44  ? 63   VAL E N   1 
ATOM   7231 C  CA  . VAL E  1 63  ? 48.006  0.222   39.342  1.00 4.97  ? 63   VAL E CA  1 
ATOM   7232 C  C   . VAL E  1 63  ? 46.964  1.241   39.766  1.00 7.53  ? 63   VAL E C   1 
ATOM   7233 O  O   . VAL E  1 63  ? 46.630  1.349   40.943  1.00 7.08  ? 63   VAL E O   1 
ATOM   7234 C  CB  . VAL E  1 63  ? 47.507  -1.181  39.682  1.00 6.32  ? 63   VAL E CB  1 
ATOM   7235 C  CG1 . VAL E  1 63  ? 46.245  -1.501  38.857  1.00 8.02  ? 63   VAL E CG1 1 
ATOM   7236 C  CG2 . VAL E  1 63  ? 48.613  -2.202  39.419  1.00 11.52 ? 63   VAL E CG2 1 
ATOM   7237 N  N   . TYR E  1 64  ? 46.470  2.000   38.803  1.00 5.05  ? 64   TYR E N   1 
ATOM   7238 C  CA  . TYR E  1 64  ? 45.701  3.198   39.111  1.00 7.29  ? 64   TYR E CA  1 
ATOM   7239 C  C   . TYR E  1 64  ? 44.487  3.232   38.204  1.00 9.29  ? 64   TYR E C   1 
ATOM   7240 O  O   . TYR E  1 64  ? 44.582  2.857   37.040  1.00 9.23  ? 64   TYR E O   1 
ATOM   7241 C  CB  . TYR E  1 64  ? 46.597  4.403   38.805  1.00 7.15  ? 64   TYR E CB  1 
ATOM   7242 C  CG  . TYR E  1 64  ? 46.119  5.729   39.344  1.00 9.10  ? 64   TYR E CG  1 
ATOM   7243 C  CD1 . TYR E  1 64  ? 46.251  6.039   40.699  1.00 8.03  ? 64   TYR E CD1 1 
ATOM   7244 C  CD2 . TYR E  1 64  ? 45.565  6.684   38.500  1.00 10.41 ? 64   TYR E CD2 1 
ATOM   7245 C  CE1 . TYR E  1 64  ? 45.838  7.258   41.191  1.00 7.73  ? 64   TYR E CE1 1 
ATOM   7246 C  CE2 . TYR E  1 64  ? 45.151  7.903   38.990  1.00 11.35 ? 64   TYR E CE2 1 
ATOM   7247 C  CZ  . TYR E  1 64  ? 45.295  8.182   40.335  1.00 11.26 ? 64   TYR E CZ  1 
ATOM   7248 O  OH  . TYR E  1 64  ? 44.877  9.403   40.827  1.00 13.59 ? 64   TYR E OH  1 
ATOM   7249 N  N   . LYS E  1 65  ? 43.355  3.678   38.732  1.00 9.05  ? 65   LYS E N   1 
ATOM   7250 C  CA  . LYS E  1 65  ? 42.117  3.766   37.956  1.00 8.39  ? 65   LYS E CA  1 
ATOM   7251 C  C   . LYS E  1 65  ? 41.756  5.233   37.805  1.00 8.98  ? 65   LYS E C   1 
ATOM   7252 O  O   . LYS E  1 65  ? 41.271  5.838   38.752  1.00 8.44  ? 65   LYS E O   1 
ATOM   7253 C  CB  . LYS E  1 65  ? 41.002  3.054   38.723  1.00 9.87  ? 65   LYS E CB  1 
ATOM   7254 C  CG  . LYS E  1 65  ? 39.673  2.943   37.977  1.00 16.30 ? 65   LYS E CG  1 
ATOM   7255 C  CD  . LYS E  1 65  ? 39.538  1.599   37.309  1.00 20.63 ? 65   LYS E CD  1 
ATOM   7256 C  CE  . LYS E  1 65  ? 38.229  1.484   36.536  1.00 14.30 ? 65   LYS E CE  1 
ATOM   7257 N  NZ  . LYS E  1 65  ? 37.031  1.533   37.428  1.00 17.94 ? 65   LYS E NZ  1 
ATOM   7258 N  N   A GLU E  1 66  ? 41.989  5.813   36.631  0.44 12.41 ? 66   GLU E N   1 
ATOM   7259 N  N   B GLU E  1 66  ? 41.987  5.807   36.624  0.56 12.40 ? 66   GLU E N   1 
ATOM   7260 C  CA  A GLU E  1 66  ? 41.707  7.235   36.445  0.44 15.09 ? 66   GLU E CA  1 
ATOM   7261 C  CA  B GLU E  1 66  ? 41.728  7.233   36.422  0.56 15.11 ? 66   GLU E CA  1 
ATOM   7262 C  C   A GLU E  1 66  ? 40.216  7.542   36.383  0.44 11.50 ? 66   GLU E C   1 
ATOM   7263 C  C   B GLU E  1 66  ? 40.232  7.549   36.360  0.56 11.45 ? 66   GLU E C   1 
ATOM   7264 O  O   A GLU E  1 66  ? 39.772  8.591   36.851  0.44 14.18 ? 66   GLU E O   1 
ATOM   7265 O  O   B GLU E  1 66  ? 39.799  8.612   36.806  0.56 14.17 ? 66   GLU E O   1 
ATOM   7266 C  CB  A GLU E  1 66  ? 42.412  7.789   35.207  0.44 19.08 ? 66   GLU E CB  1 
ATOM   7267 C  CB  B GLU E  1 66  ? 42.426  7.757   35.161  0.56 19.14 ? 66   GLU E CB  1 
ATOM   7268 C  CG  A GLU E  1 66  ? 43.461  8.832   35.535  0.44 21.00 ? 66   GLU E CG  1 
ATOM   7269 C  CG  B GLU E  1 66  ? 43.911  8.100   35.329  0.56 11.51 ? 66   GLU E CG  1 
ATOM   7270 C  CD  A GLU E  1 66  ? 42.853  10.069  36.170  0.44 16.28 ? 66   GLU E CD  1 
ATOM   7271 C  CD  B GLU E  1 66  ? 44.427  8.966   34.193  0.56 20.13 ? 66   GLU E CD  1 
ATOM   7272 O  OE1 A GLU E  1 66  ? 41.685  10.383  35.863  0.44 29.64 ? 66   GLU E OE1 1 
ATOM   7273 O  OE1 B GLU E  1 66  ? 43.624  9.736   33.620  0.56 27.94 ? 66   GLU E OE1 1 
ATOM   7274 O  OE2 A GLU E  1 66  ? 43.537  10.728  36.977  0.44 24.05 ? 66   GLU E OE2 1 
ATOM   7275 O  OE2 B GLU E  1 66  ? 45.632  8.887   33.873  0.56 25.83 ? 66   GLU E OE2 1 
ATOM   7276 N  N   . ARG E  1 67  ? 39.454  6.621   35.808  1.00 9.67  ? 67   ARG E N   1 
ATOM   7277 C  CA  . ARG E  1 67  ? 38.011  6.793   35.668  1.00 10.07 ? 67   ARG E CA  1 
ATOM   7278 C  C   . ARG E  1 67  ? 37.397  5.474   35.247  1.00 12.99 ? 67   ARG E C   1 
ATOM   7279 O  O   . ARG E  1 67  ? 38.114  4.541   34.900  1.00 11.07 ? 67   ARG E O   1 
ATOM   7280 C  CB  . ARG E  1 67  ? 37.700  7.869   34.631  1.00 12.52 ? 67   ARG E CB  1 
ATOM   7281 C  CG  . ARG E  1 67  ? 38.219  7.572   33.228  1.00 13.37 ? 67   ARG E CG  1 
ATOM   7282 C  CD  . ARG E  1 67  ? 38.051  8.784   32.307  1.00 15.75 ? 67   ARG E CD  1 
ATOM   7283 N  NE  . ARG E  1 67  ? 39.197  9.681   32.406  1.00 26.95 ? 67   ARG E NE  1 
ATOM   7284 C  CZ  . ARG E  1 67  ? 39.254  10.759  33.174  1.00 35.35 ? 67   ARG E CZ  1 
ATOM   7285 N  NH1 . ARG E  1 67  ? 38.213  11.110  33.921  1.00 57.76 ? 67   ARG E NH1 1 
ATOM   7286 N  NH2 . ARG E  1 67  ? 40.360  11.492  33.191  1.00 31.03 ? 67   ARG E NH2 1 
ATOM   7287 N  N   . VAL E  1 68  ? 36.072  5.391   35.280  1.00 10.25 ? 68   VAL E N   1 
ATOM   7288 C  CA  . VAL E  1 68  ? 35.405  4.158   34.900  1.00 8.12  ? 68   VAL E CA  1 
ATOM   7289 C  C   . VAL E  1 68  ? 35.893  3.712   33.523  1.00 11.55 ? 68   VAL E C   1 
ATOM   7290 O  O   . VAL E  1 68  ? 36.066  4.528   32.607  1.00 12.24 ? 68   VAL E O   1 
ATOM   7291 C  CB  . VAL E  1 68  ? 33.855  4.292   34.951  1.00 13.74 ? 68   VAL E CB  1 
ATOM   7292 C  CG1 . VAL E  1 68  ? 33.364  5.389   34.011  1.00 15.83 ? 68   VAL E CG1 1 
ATOM   7293 C  CG2 . VAL E  1 68  ? 33.187  2.961   34.632  1.00 14.49 ? 68   VAL E CG2 1 
ATOM   7294 N  N   . GLY E  1 69  ? 36.163  2.416   33.411  1.00 9.24  ? 69   GLY E N   1 
ATOM   7295 C  CA  . GLY E  1 69  ? 36.538  1.818   32.140  1.00 11.87 ? 69   GLY E CA  1 
ATOM   7296 C  C   . GLY E  1 69  ? 37.994  1.978   31.736  1.00 10.55 ? 69   GLY E C   1 
ATOM   7297 O  O   . GLY E  1 69  ? 38.350  1.591   30.641  1.00 11.66 ? 69   GLY E O   1 
ATOM   7298 N  N   . GLU E  1 70  ? 38.837  2.531   32.603  1.00 6.31  ? 70   GLU E N   1 
ATOM   7299 C  CA  . GLU E  1 70  ? 40.237  2.780   32.232  1.00 10.86 ? 70   GLU E CA  1 
ATOM   7300 C  C   . GLU E  1 70  ? 41.196  2.364   33.341  1.00 11.75 ? 70   GLU E C   1 
ATOM   7301 O  O   . GLU E  1 70  ? 41.109  2.855   34.467  1.00 14.89 ? 70   GLU E O   1 
ATOM   7302 C  CB  . GLU E  1 70  ? 40.448  4.265   31.890  1.00 11.73 ? 70   GLU E CB  1 
ATOM   7303 C  CG  . GLU E  1 70  ? 39.614  4.708   30.681  1.00 17.90 ? 70   GLU E CG  1 
ATOM   7304 C  CD  . GLU E  1 70  ? 39.860  6.151   30.253  1.00 23.40 ? 70   GLU E CD  1 
ATOM   7305 O  OE1 . GLU E  1 70  ? 40.787  6.801   30.775  1.00 16.55 ? 70   GLU E OE1 1 
ATOM   7306 O  OE2 . GLU E  1 70  ? 39.119  6.632   29.370  1.00 27.98 ? 70   GLU E OE2 1 
ATOM   7307 N  N   . TYR E  1 71  ? 42.120  1.469   33.009  1.00 7.38  ? 71   TYR E N   1 
ATOM   7308 C  CA  . TYR E  1 71  ? 43.099  0.974   33.974  1.00 7.84  ? 71   TYR E CA  1 
ATOM   7309 C  C   . TYR E  1 71  ? 44.502  1.364   33.533  1.00 6.48  ? 71   TYR E C   1 
ATOM   7310 O  O   . TYR E  1 71  ? 44.860  1.187   32.365  1.00 8.00  ? 71   TYR E O   1 
ATOM   7311 C  CB  . TYR E  1 71  ? 43.000  -0.546  34.105  1.00 8.13  ? 71   TYR E CB  1 
ATOM   7312 C  CG  . TYR E  1 71  ? 41.696  -0.968  34.731  1.00 8.08  ? 71   TYR E CG  1 
ATOM   7313 C  CD1 . TYR E  1 71  ? 40.571  -1.202  33.952  1.00 9.68  ? 71   TYR E CD1 1 
ATOM   7314 C  CD2 . TYR E  1 71  ? 41.586  -1.096  36.103  1.00 12.81 ? 71   TYR E CD2 1 
ATOM   7315 C  CE1 . TYR E  1 71  ? 39.365  -1.564  34.531  1.00 9.43  ? 71   TYR E CE1 1 
ATOM   7316 C  CE2 . TYR E  1 71  ? 40.383  -1.458  36.693  1.00 10.34 ? 71   TYR E CE2 1 
ATOM   7317 C  CZ  . TYR E  1 71  ? 39.287  -1.692  35.899  1.00 10.51 ? 71   TYR E CZ  1 
ATOM   7318 O  OH  . TYR E  1 71  ? 38.103  -2.047  36.495  1.00 11.79 ? 71   TYR E OH  1 
ATOM   7319 N  N   . SER E  1 72  ? 45.290  1.915   34.459  1.00 6.67  ? 72   SER E N   1 
ATOM   7320 C  CA  . SER E  1 72  ? 46.671  2.295   34.149  1.00 7.62  ? 72   SER E CA  1 
ATOM   7321 C  C   . SER E  1 72  ? 47.681  1.488   34.958  1.00 6.08  ? 72   SER E C   1 
ATOM   7322 O  O   . SER E  1 72  ? 47.440  1.176   36.122  1.00 6.55  ? 72   SER E O   1 
ATOM   7323 C  CB  . SER E  1 72  ? 46.905  3.783   34.431  1.00 9.03  ? 72   SER E CB  1 
ATOM   7324 O  OG  . SER E  1 72  ? 46.063  4.593   33.633  1.00 9.91  ? 72   SER E OG  1 
ATOM   7325 N  N   . LEU E  1 73  ? 48.800  1.139   34.322  1.00 5.45  ? 73   LEU E N   1 
ATOM   7326 C  CA  . LEU E  1 73  ? 49.964  0.584   35.010  1.00 7.26  ? 73   LEU E CA  1 
ATOM   7327 C  C   . LEU E  1 73  ? 51.133  1.552   34.846  1.00 8.25  ? 73   LEU E C   1 
ATOM   7328 O  O   . LEU E  1 73  ? 51.430  1.997   33.728  1.00 6.55  ? 73   LEU E O   1 
ATOM   7329 C  CB  . LEU E  1 73  ? 50.356  -0.776  34.432  1.00 6.65  ? 73   LEU E CB  1 
ATOM   7330 C  CG  . LEU E  1 73  ? 51.673  -1.334  34.966  1.00 5.87  ? 73   LEU E CG  1 
ATOM   7331 C  CD1 . LEU E  1 73  ? 51.491  -1.804  36.403  1.00 9.11  ? 73   LEU E CD1 1 
ATOM   7332 C  CD2 . LEU E  1 73  ? 52.154  -2.488  34.065  1.00 9.05  ? 73   LEU E CD2 1 
ATOM   7333 N  N   . TYR E  1 74  ? 51.767  1.899   35.964  1.00 7.50  ? 74   TYR E N   1 
ATOM   7334 C  CA  . TYR E  1 74  ? 53.040  2.619   35.949  1.00 7.01  ? 74   TYR E CA  1 
ATOM   7335 C  C   . TYR E  1 74  ? 54.201  1.680   36.258  1.00 6.36  ? 74   TYR E C   1 
ATOM   7336 O  O   . TYR E  1 74  ? 54.134  0.862   37.184  1.00 6.59  ? 74   TYR E O   1 
ATOM   7337 C  CB  . TYR E  1 74  ? 53.061  3.745   36.989  1.00 6.99  ? 74   TYR E CB  1 
ATOM   7338 C  CG  . TYR E  1 74  ? 52.019  4.823   36.783  1.00 7.68  ? 74   TYR E CG  1 
ATOM   7339 C  CD1 . TYR E  1 74  ? 50.664  4.543   36.901  1.00 8.87  ? 74   TYR E CD1 1 
ATOM   7340 C  CD2 . TYR E  1 74  ? 52.400  6.138   36.517  1.00 10.13 ? 74   TYR E CD2 1 
ATOM   7341 C  CE1 . TYR E  1 74  ? 49.710  5.542   36.731  1.00 7.95  ? 74   TYR E CE1 1 
ATOM   7342 C  CE2 . TYR E  1 74  ? 51.453  7.138   36.347  1.00 14.44 ? 74   TYR E CE2 1 
ATOM   7343 C  CZ  . TYR E  1 74  ? 50.113  6.831   36.456  1.00 13.12 ? 74   TYR E CZ  1 
ATOM   7344 O  OH  . TYR E  1 74  ? 49.162  7.815   36.283  1.00 15.24 ? 74   TYR E OH  1 
ATOM   7345 N  N   . ILE E  1 75  ? 55.278  1.828   35.497  1.00 6.04  ? 75   ILE E N   1 
ATOM   7346 C  CA  . ILE E  1 75  ? 56.537  1.141   35.782  1.00 7.66  ? 75   ILE E CA  1 
ATOM   7347 C  C   . ILE E  1 75  ? 57.632  2.201   35.770  1.00 8.55  ? 75   ILE E C   1 
ATOM   7348 O  O   . ILE E  1 75  ? 57.855  2.824   34.748  1.00 6.62  ? 75   ILE E O   1 
ATOM   7349 C  CB  . ILE E  1 75  ? 56.879  0.106   34.696  1.00 7.71  ? 75   ILE E CB  1 
ATOM   7350 C  CG1 . ILE E  1 75  ? 55.803  -0.985  34.601  1.00 7.71  ? 75   ILE E CG1 1 
ATOM   7351 C  CG2 . ILE E  1 75  ? 58.248  -0.512  34.961  1.00 8.05  ? 75   ILE E CG2 1 
ATOM   7352 C  CD1 . ILE E  1 75  ? 55.706  -1.875  35.852  1.00 8.24  ? 75   ILE E CD1 1 
ATOM   7353 N  N   . GLY E  1 76  ? 58.297  2.429   36.898  1.00 7.02  ? 76   GLY E N   1 
ATOM   7354 C  CA  . GLY E  1 76  ? 59.324  3.466   36.930  1.00 8.03  ? 76   GLY E CA  1 
ATOM   7355 C  C   . GLY E  1 76  ? 58.830  4.824   36.456  1.00 12.01 ? 76   GLY E C   1 
ATOM   7356 O  O   . GLY E  1 76  ? 59.527  5.504   35.716  1.00 8.82  ? 76   GLY E O   1 
ATOM   7357 N  N   A ARG E  1 77  ? 57.635  5.222   36.888  0.50 10.30 ? 77   ARG E N   1 
ATOM   7358 N  N   B ARG E  1 77  ? 57.624  5.201   36.881  0.50 10.29 ? 77   ARG E N   1 
ATOM   7359 C  CA  A ARG E  1 77  ? 57.055  6.532   36.542  0.50 10.50 ? 77   ARG E CA  1 
ATOM   7360 C  CA  B ARG E  1 77  ? 57.006  6.494   36.543  0.50 10.50 ? 77   ARG E CA  1 
ATOM   7361 C  C   A ARG E  1 77  ? 56.385  6.609   35.168  0.50 9.89  ? 77   ARG E C   1 
ATOM   7362 C  C   B ARG E  1 77  ? 56.292  6.525   35.198  0.50 9.98  ? 77   ARG E C   1 
ATOM   7363 O  O   A ARG E  1 77  ? 55.548  7.485   34.947  0.50 10.94 ? 77   ARG E O   1 
ATOM   7364 O  O   B ARG E  1 77  ? 55.338  7.284   35.024  0.50 11.15 ? 77   ARG E O   1 
ATOM   7365 C  CB  A ARG E  1 77  ? 58.082  7.668   36.644  0.50 15.36 ? 77   ARG E CB  1 
ATOM   7366 C  CB  B ARG E  1 77  ? 58.013  7.646   36.585  0.50 15.32 ? 77   ARG E CB  1 
ATOM   7367 C  CG  A ARG E  1 77  ? 58.261  8.264   38.023  0.50 21.38 ? 77   ARG E CG  1 
ATOM   7368 C  CG  B ARG E  1 77  ? 58.802  7.710   37.855  0.50 20.39 ? 77   ARG E CG  1 
ATOM   7369 C  CD  A ARG E  1 77  ? 59.376  9.300   37.997  0.50 28.64 ? 77   ARG E CD  1 
ATOM   7370 C  CD  B ARG E  1 77  ? 59.692  8.920   37.866  0.50 26.99 ? 77   ARG E CD  1 
ATOM   7371 N  NE  A ARG E  1 77  ? 60.674  8.678   37.764  0.50 36.87 ? 77   ARG E NE  1 
ATOM   7372 N  NE  B ARG E  1 77  ? 59.793  9.408   39.228  0.50 36.14 ? 77   ARG E NE  1 
ATOM   7373 C  CZ  A ARG E  1 77  ? 61.283  8.625   36.585  0.50 20.31 ? 77   ARG E CZ  1 
ATOM   7374 C  CZ  B ARG E  1 77  ? 60.564  8.865   40.159  0.50 30.60 ? 77   ARG E CZ  1 
ATOM   7375 N  NH1 A ARG E  1 77  ? 62.456  8.028   36.482  0.50 15.43 ? 77   ARG E NH1 1 
ATOM   7376 N  NH1 B ARG E  1 77  ? 60.558  9.393   41.376  0.50 7.10  ? 77   ARG E NH1 1 
ATOM   7377 N  NH2 A ARG E  1 77  ? 60.722  9.164   35.517  0.50 26.84 ? 77   ARG E NH2 1 
ATOM   7378 N  NH2 B ARG E  1 77  ? 61.336  7.807   39.866  0.50 14.37 ? 77   ARG E NH2 1 
ATOM   7379 N  N   . HIS E  1 78  ? 56.754  5.719   34.247  1.00 9.47  ? 78   HIS E N   1 
ATOM   7380 C  CA  . HIS E  1 78  ? 56.155  5.717   32.911  1.00 7.11  ? 78   HIS E CA  1 
ATOM   7381 C  C   . HIS E  1 78  ? 54.807  5.009   33.004  1.00 10.48 ? 78   HIS E C   1 
ATOM   7382 O  O   . HIS E  1 78  ? 54.629  4.137   33.839  1.00 8.64  ? 78   HIS E O   1 
ATOM   7383 C  CB  . HIS E  1 78  ? 57.038  4.946   31.922  1.00 8.66  ? 78   HIS E CB  1 
ATOM   7384 C  CG  . HIS E  1 78  ? 58.363  5.590   31.657  1.00 10.90 ? 78   HIS E CG  1 
ATOM   7385 N  ND1 . HIS E  1 78  ? 59.168  5.220   30.601  1.00 13.38 ? 78   HIS E ND1 1 
ATOM   7386 C  CD2 . HIS E  1 78  ? 59.020  6.585   32.301  1.00 16.14 ? 78   HIS E CD2 1 
ATOM   7387 C  CE1 . HIS E  1 78  ? 60.269  5.949   30.612  1.00 15.31 ? 78   HIS E CE1 1 
ATOM   7388 N  NE2 . HIS E  1 78  ? 60.206  6.787   31.631  1.00 16.19 ? 78   HIS E NE2 1 
ATOM   7389 N  N   . LYS E  1 79  ? 53.848  5.376   32.171  1.00 9.12  ? 79   LYS E N   1 
ATOM   7390 C  CA  . LYS E  1 79  ? 52.544  4.727   32.308  1.00 8.46  ? 79   LYS E CA  1 
ATOM   7391 C  C   . LYS E  1 79  ? 51.954  4.291   30.978  1.00 11.07 ? 79   LYS E C   1 
ATOM   7392 O  O   . LYS E  1 79  ? 52.292  4.829   29.908  1.00 9.47  ? 79   LYS E O   1 
ATOM   7393 C  CB  . LYS E  1 79  ? 51.549  5.615   33.068  1.00 13.78 ? 79   LYS E CB  1 
ATOM   7394 C  CG  . LYS E  1 79  ? 51.024  6.773   32.253  1.00 13.93 ? 79   LYS E CG  1 
ATOM   7395 C  CD  . LYS E  1 79  ? 49.834  7.466   32.914  1.00 20.68 ? 79   LYS E CD  1 
ATOM   7396 C  CE  . LYS E  1 79  ? 49.336  8.611   32.047  1.00 37.19 ? 79   LYS E CE  1 
ATOM   7397 N  NZ  . LYS E  1 79  ? 48.391  9.504   32.774  1.00 52.40 ? 79   LYS E NZ  1 
ATOM   7398 N  N   . VAL E  1 80  ? 51.088  3.291   31.066  1.00 8.27  ? 80   VAL E N   1 
ATOM   7399 C  CA  . VAL E  1 80  ? 50.248  2.862   29.956  1.00 8.32  ? 80   VAL E CA  1 
ATOM   7400 C  C   . VAL E  1 80  ? 48.830  2.729   30.494  1.00 7.15  ? 80   VAL E C   1 
ATOM   7401 O  O   . VAL E  1 80  ? 48.625  2.569   31.703  1.00 7.28  ? 80   VAL E O   1 
ATOM   7402 C  CB  . VAL E  1 80  ? 50.700  1.518   29.334  1.00 7.33  ? 80   VAL E CB  1 
ATOM   7403 C  CG1 . VAL E  1 80  ? 52.037  1.688   28.593  1.00 8.79  ? 80   VAL E CG1 1 
ATOM   7404 C  CG2 . VAL E  1 80  ? 50.778  0.410   30.393  1.00 8.45  ? 80   VAL E CG2 1 
ATOM   7405 N  N   . THR E  1 81  ? 47.852  2.844   29.604  1.00 7.17  ? 81   THR E N   1 
ATOM   7406 C  CA  . THR E  1 81  ? 46.449  2.745   30.002  1.00 6.19  ? 81   THR E CA  1 
ATOM   7407 C  C   . THR E  1 81  ? 45.707  1.944   28.958  1.00 7.38  ? 81   THR E C   1 
ATOM   7408 O  O   . THR E  1 81  ? 45.918  2.127   27.761  1.00 8.72  ? 81   THR E O   1 
ATOM   7409 C  CB  . THR E  1 81  ? 45.795  4.139   30.072  1.00 9.02  ? 81   THR E CB  1 
ATOM   7410 O  OG1 . THR E  1 81  ? 46.506  4.961   31.006  1.00 10.34 ? 81   THR E OG1 1 
ATOM   7411 C  CG2 . THR E  1 81  ? 44.338  4.033   30.511  1.00 10.02 ? 81   THR E CG2 1 
ATOM   7412 N  N   . SER E  1 82  ? 44.829  1.058   29.404  1.00 7.67  ? 82   SER E N   1 
ATOM   7413 C  CA  . SER E  1 82  ? 43.966  0.359   28.472  1.00 6.01  ? 82   SER E CA  1 
ATOM   7414 C  C   . SER E  1 82  ? 42.521  0.422   28.941  1.00 7.39  ? 82   SER E C   1 
ATOM   7415 O  O   . SER E  1 82  ? 42.243  0.582   30.131  1.00 8.20  ? 82   SER E O   1 
ATOM   7416 C  CB  . SER E  1 82  ? 44.424  -1.088  28.283  1.00 10.61 ? 82   SER E CB  1 
ATOM   7417 O  OG  . SER E  1 82  ? 45.542  -1.096  27.408  1.00 11.98 ? 82   SER E OG  1 
ATOM   7418 N  N   . LYS E  1 83  ? 41.613  0.296   27.982  1.00 6.25  ? 83   LYS E N   1 
ATOM   7419 C  CA  . LYS E  1 83  ? 40.193  0.516   28.223  1.00 8.26  ? 83   LYS E CA  1 
ATOM   7420 C  C   . LYS E  1 83  ? 39.376  -0.756  28.193  1.00 9.59  ? 83   LYS E C   1 
ATOM   7421 O  O   . LYS E  1 83  ? 39.764  -1.734  27.567  1.00 8.91  ? 83   LYS E O   1 
ATOM   7422 C  CB  . LYS E  1 83  ? 39.639  1.490   27.183  1.00 7.71  ? 83   LYS E CB  1 
ATOM   7423 C  CG  . LYS E  1 83  ? 40.325  2.832   27.248  1.00 12.83 ? 83   LYS E CG  1 
ATOM   7424 C  CD  . LYS E  1 83  ? 39.659  3.853   26.350  1.00 19.35 ? 83   LYS E CD  1 
ATOM   7425 C  CE  . LYS E  1 83  ? 40.399  5.181   26.468  1.00 23.18 ? 83   LYS E CE  1 
ATOM   7426 N  NZ  . LYS E  1 83  ? 39.633  6.308   25.881  1.00 27.69 ? 83   LYS E NZ  1 
ATOM   7427 N  N   . VAL E  1 84  ? 38.227  -0.722  28.860  1.00 7.66  ? 84   VAL E N   1 
ATOM   7428 C  CA  . VAL E  1 84  ? 37.350  -1.884  28.891  1.00 8.04  ? 84   VAL E CA  1 
ATOM   7429 C  C   . VAL E  1 84  ? 35.918  -1.438  29.089  1.00 10.76 ? 84   VAL E C   1 
ATOM   7430 O  O   . VAL E  1 84  ? 35.669  -0.398  29.690  1.00 8.79  ? 84   VAL E O   1 
ATOM   7431 C  CB  . VAL E  1 84  ? 37.768  -2.868  30.013  1.00 7.70  ? 84   VAL E CB  1 
ATOM   7432 C  CG1 . VAL E  1 84  ? 37.575  -2.240  31.384  1.00 10.83 ? 84   VAL E CG1 1 
ATOM   7433 C  CG2 . VAL E  1 84  ? 37.019  -4.209  29.886  1.00 10.89 ? 84   VAL E CG2 1 
ATOM   7434 N  N   . ILE E  1 85  ? 34.988  -2.232  28.564  1.00 10.26 ? 85   ILE E N   1 
ATOM   7435 C  CA  . ILE E  1 85  ? 33.571  -2.074  28.867  1.00 8.60  ? 85   ILE E CA  1 
ATOM   7436 C  C   . ILE E  1 85  ? 33.280  -2.671  30.239  1.00 10.25 ? 85   ILE E C   1 
ATOM   7437 O  O   . ILE E  1 85  ? 33.507  -3.866  30.469  1.00 13.38 ? 85   ILE E O   1 
ATOM   7438 C  CB  . ILE E  1 85  ? 32.714  -2.798  27.804  1.00 10.71 ? 85   ILE E CB  1 
ATOM   7439 C  CG1 . ILE E  1 85  ? 32.972  -2.174  26.425  1.00 18.11 ? 85   ILE E CG1 1 
ATOM   7440 C  CG2 . ILE E  1 85  ? 31.251  -2.722  28.159  1.00 12.69 ? 85   ILE E CG2 1 
ATOM   7441 C  CD1 . ILE E  1 85  ? 32.432  -3.002  25.263  1.00 13.89 ? 85   ILE E CD1 1 
ATOM   7442 N  N   A GLU E  1 86  ? 32.780  -1.847  31.159  0.57 14.01 ? 86   GLU E N   1 
ATOM   7443 N  N   B GLU E  1 86  ? 32.781  -1.837  31.147  0.43 13.99 ? 86   GLU E N   1 
ATOM   7444 C  CA  A GLU E  1 86  ? 32.421  -2.336  32.495  0.57 13.93 ? 86   GLU E CA  1 
ATOM   7445 C  CA  B GLU E  1 86  ? 32.392  -2.300  32.475  0.43 13.95 ? 86   GLU E CA  1 
ATOM   7446 C  C   A GLU E  1 86  ? 31.229  -1.574  33.052  0.57 11.12 ? 86   GLU E C   1 
ATOM   7447 C  C   B GLU E  1 86  ? 31.111  -1.621  32.918  0.43 11.33 ? 86   GLU E C   1 
ATOM   7448 O  O   A GLU E  1 86  ? 31.060  -0.390  32.768  0.57 12.94 ? 86   GLU E O   1 
ATOM   7449 O  O   B GLU E  1 86  ? 30.766  -0.546  32.431  0.43 12.29 ? 86   GLU E O   1 
ATOM   7450 C  CB  A GLU E  1 86  ? 33.605  -2.239  33.468  0.57 16.09 ? 86   GLU E CB  1 
ATOM   7451 C  CB  B GLU E  1 86  ? 33.489  -2.022  33.505  0.43 15.87 ? 86   GLU E CB  1 
ATOM   7452 C  CG  A GLU E  1 86  ? 34.133  -0.822  33.696  0.57 12.66 ? 86   GLU E CG  1 
ATOM   7453 C  CG  B GLU E  1 86  ? 34.403  -3.196  33.794  0.43 15.45 ? 86   GLU E CG  1 
ATOM   7454 C  CD  A GLU E  1 86  ? 35.265  -0.773  34.721  0.57 17.35 ? 86   GLU E CD  1 
ATOM   7455 C  CD  B GLU E  1 86  ? 35.271  -2.959  35.010  0.43 16.82 ? 86   GLU E CD  1 
ATOM   7456 O  OE1 A GLU E  1 86  ? 35.886  -1.829  34.972  0.57 13.28 ? 86   GLU E OE1 1 
ATOM   7457 O  OE1 B GLU E  1 86  ? 36.198  -2.128  34.930  0.43 12.36 ? 86   GLU E OE1 1 
ATOM   7458 O  OE2 A GLU E  1 86  ? 35.523  0.318   35.283  0.57 6.97  ? 86   GLU E OE2 1 
ATOM   7459 O  OE2 B GLU E  1 86  ? 35.025  -3.600  36.047  0.43 14.63 ? 86   GLU E OE2 1 
ATOM   7460 N  N   . LYS E  1 87  ? 30.407  -2.270  33.838  1.00 12.51 ? 87   LYS E N   1 
ATOM   7461 C  CA  . LYS E  1 87  ? 29.259  -1.659  34.504  1.00 16.51 ? 87   LYS E CA  1 
ATOM   7462 C  C   . LYS E  1 87  ? 29.745  -0.891  35.730  1.00 14.24 ? 87   LYS E C   1 
ATOM   7463 O  O   . LYS E  1 87  ? 30.835  -1.143  36.234  1.00 14.55 ? 87   LYS E O   1 
ATOM   7464 C  CB  . LYS E  1 87  ? 28.285  -2.739  34.955  1.00 15.16 ? 87   LYS E CB  1 
ATOM   7465 C  CG  . LYS E  1 87  ? 27.697  -3.554  33.819  1.00 24.31 ? 87   LYS E CG  1 
ATOM   7466 C  CD  . LYS E  1 87  ? 26.627  -4.504  34.345  1.00 32.98 ? 87   LYS E CD  1 
ATOM   7467 C  CE  . LYS E  1 87  ? 25.957  -5.270  33.213  1.00 43.84 ? 87   LYS E CE  1 
ATOM   7468 N  NZ  . LYS E  1 87  ? 26.913  -6.180  32.523  1.00 51.05 ? 87   LYS E NZ  1 
ATOM   7469 N  N   . PHE E  1 88  ? 28.938  0.051   36.205  1.00 11.87 ? 88   PHE E N   1 
ATOM   7470 C  CA  . PHE E  1 88  ? 29.312  0.828   37.379  1.00 12.40 ? 88   PHE E CA  1 
ATOM   7471 C  C   . PHE E  1 88  ? 28.099  1.123   38.242  1.00 11.07 ? 88   PHE E C   1 
ATOM   7472 O  O   . PHE E  1 88  ? 27.083  1.575   37.728  1.00 11.69 ? 88   PHE E O   1 
ATOM   7473 C  CB  . PHE E  1 88  ? 29.940  2.173   36.996  1.00 10.86 ? 88   PHE E CB  1 
ATOM   7474 C  CG  . PHE E  1 88  ? 30.114  3.083   38.179  1.00 9.64  ? 88   PHE E CG  1 
ATOM   7475 C  CD1 . PHE E  1 88  ? 31.197  2.926   39.027  1.00 12.53 ? 88   PHE E CD1 1 
ATOM   7476 C  CD2 . PHE E  1 88  ? 29.162  4.042   38.484  1.00 12.93 ? 88   PHE E CD2 1 
ATOM   7477 C  CE1 . PHE E  1 88  ? 31.342  3.734   40.145  1.00 14.04 ? 88   PHE E CE1 1 
ATOM   7478 C  CE2 . PHE E  1 88  ? 29.301  4.844   39.605  1.00 13.49 ? 88   PHE E CE2 1 
ATOM   7479 C  CZ  . PHE E  1 88  ? 30.390  4.689   40.432  1.00 13.30 ? 88   PHE E CZ  1 
ATOM   7480 N  N   . PRO E  1 89  ? 28.204  0.890   39.565  1.00 8.87  ? 89   PRO E N   1 
ATOM   7481 C  CA  . PRO E  1 89  ? 29.334  0.225   40.217  1.00 8.93  ? 89   PRO E CA  1 
ATOM   7482 C  C   . PRO E  1 89  ? 29.257  -1.273  40.010  1.00 11.03 ? 89   PRO E C   1 
ATOM   7483 O  O   . PRO E  1 89  ? 28.173  -1.815  39.770  1.00 11.05 ? 89   PRO E O   1 
ATOM   7484 C  CB  . PRO E  1 89  ? 29.125  0.524   41.711  1.00 10.77 ? 89   PRO E CB  1 
ATOM   7485 C  CG  . PRO E  1 89  ? 27.921  1.390   41.814  1.00 13.74 ? 89   PRO E CG  1 
ATOM   7486 C  CD  . PRO E  1 89  ? 27.175  1.325   40.528  1.00 9.39  ? 89   PRO E CD  1 
ATOM   7487 N  N   . ALA E  1 90  ? 30.397  -1.946  40.115  1.00 7.74  ? 90   ALA E N   1 
ATOM   7488 C  CA  . ALA E  1 90  ? 30.422  -3.393  39.973  1.00 9.90  ? 90   ALA E CA  1 
ATOM   7489 C  C   . ALA E  1 90  ? 31.701  -3.947  40.569  1.00 7.39  ? 90   ALA E C   1 
ATOM   7490 O  O   . ALA E  1 90  ? 32.765  -3.345  40.435  1.00 9.65  ? 90   ALA E O   1 
ATOM   7491 C  CB  . ALA E  1 90  ? 30.322  -3.790  38.493  1.00 14.58 ? 90   ALA E CB  1 
ATOM   7492 N  N   . PRO E  1 91  ? 31.610  -5.106  41.219  1.00 6.33  ? 91   PRO E N   1 
ATOM   7493 C  CA  . PRO E  1 91  ? 32.839  -5.804  41.616  1.00 7.95  ? 91   PRO E CA  1 
ATOM   7494 C  C   . PRO E  1 91  ? 33.690  -6.114  40.396  1.00 12.27 ? 91   PRO E C   1 
ATOM   7495 O  O   . PRO E  1 91  ? 33.153  -6.325  39.305  1.00 10.60 ? 91   PRO E O   1 
ATOM   7496 C  CB  . PRO E  1 91  ? 32.315  -7.121  42.189  1.00 11.59 ? 91   PRO E CB  1 
ATOM   7497 C  CG  . PRO E  1 91  ? 30.944  -6.796  42.657  1.00 9.39  ? 91   PRO E CG  1 
ATOM   7498 C  CD  . PRO E  1 91  ? 30.400  -5.832  41.640  1.00 9.60  ? 91   PRO E CD  1 
ATOM   7499 N  N   . VAL E  1 92  ? 35.004  -6.146  40.572  1.00 6.73  ? 92   VAL E N   1 
ATOM   7500 C  CA  . VAL E  1 92  ? 35.872  -6.462  39.439  1.00 6.24  ? 92   VAL E CA  1 
ATOM   7501 C  C   . VAL E  1 92  ? 37.006  -7.378  39.875  1.00 8.55  ? 92   VAL E C   1 
ATOM   7502 O  O   . VAL E  1 92  ? 37.458  -7.330  41.028  1.00 9.55  ? 92   VAL E O   1 
ATOM   7503 C  CB  . VAL E  1 92  ? 36.437  -5.170  38.804  1.00 10.09 ? 92   VAL E CB  1 
ATOM   7504 C  CG1 . VAL E  1 92  ? 37.450  -4.505  39.735  1.00 9.64  ? 92   VAL E CG1 1 
ATOM   7505 C  CG2 . VAL E  1 92  ? 37.061  -5.447  37.433  1.00 9.36  ? 92   VAL E CG2 1 
ATOM   7506 N  N   . HIS E  1 93  ? 37.445  -8.239  38.963  1.00 6.08  ? 93   HIS E N   1 
ATOM   7507 C  CA  . HIS E  1 93  ? 38.678  -8.978  39.154  1.00 6.11  ? 93   HIS E CA  1 
ATOM   7508 C  C   . HIS E  1 93  ? 39.702  -8.419  38.182  1.00 6.73  ? 93   HIS E C   1 
ATOM   7509 O  O   . HIS E  1 93  ? 39.441  -8.318  36.987  1.00 6.75  ? 93   HIS E O   1 
ATOM   7510 C  CB  . HIS E  1 93  ? 38.479  -10.478 38.907  1.00 6.10  ? 93   HIS E CB  1 
ATOM   7511 C  CG  . HIS E  1 93  ? 39.709  -11.286 39.167  1.00 5.52  ? 93   HIS E CG  1 
ATOM   7512 N  ND1 . HIS E  1 93  ? 40.577  -11.674 38.167  1.00 7.30  ? 93   HIS E ND1 1 
ATOM   7513 C  CD2 . HIS E  1 93  ? 40.243  -11.741 40.328  1.00 7.18  ? 93   HIS E CD2 1 
ATOM   7514 C  CE1 . HIS E  1 93  ? 41.584  -12.345 38.700  1.00 8.95  ? 93   HIS E CE1 1 
ATOM   7515 N  NE2 . HIS E  1 93  ? 41.405  -12.401 40.008  1.00 7.51  ? 93   HIS E NE2 1 
ATOM   7516 N  N   . ILE E  1 94  ? 40.874  -8.060  38.701  1.00 4.40  ? 94   ILE E N   1 
ATOM   7517 C  CA  . ILE E  1 94  ? 41.906  -7.424  37.891  1.00 6.35  ? 94   ILE E CA  1 
ATOM   7518 C  C   . ILE E  1 94  ? 43.187  -8.232  37.959  1.00 8.33  ? 94   ILE E C   1 
ATOM   7519 O  O   . ILE E  1 94  ? 43.654  -8.586  39.050  1.00 9.67  ? 94   ILE E O   1 
ATOM   7520 C  CB  . ILE E  1 94  ? 42.190  -6.016  38.421  1.00 6.15  ? 94   ILE E CB  1 
ATOM   7521 C  CG1 . ILE E  1 94  ? 40.930  -5.150  38.335  1.00 10.80 ? 94   ILE E CG1 1 
ATOM   7522 C  CG2 . ILE E  1 94  ? 43.383  -5.369  37.666  1.00 11.89 ? 94   ILE E CG2 1 
ATOM   7523 C  CD1 . ILE E  1 94  ? 40.942  -3.956  39.275  1.00 15.22 ? 94   ILE E CD1 1 
ATOM   7524 N  N   . CYS E  1 95  ? 43.749  -8.539  36.795  1.00 5.45  ? 95   CYS E N   1 
ATOM   7525 C  CA  . CYS E  1 95  ? 45.113  -9.058  36.737  1.00 5.82  ? 95   CYS E CA  1 
ATOM   7526 C  C   . CYS E  1 95  ? 45.925  -8.132  35.852  1.00 9.50  ? 95   CYS E C   1 
ATOM   7527 O  O   . CYS E  1 95  ? 45.435  -7.637  34.839  1.00 9.45  ? 95   CYS E O   1 
ATOM   7528 C  CB  . CYS E  1 95  ? 45.165  -10.465 36.150  1.00 14.89 ? 95   CYS E CB  1 
ATOM   7529 S  SG  . CYS E  1 95  ? 44.660  -11.796 37.268  1.00 16.79 ? 95   CYS E SG  1 
ATOM   7530 N  N   . VAL E  1 96  ? 47.167  -7.890  36.227  1.00 7.34  ? 96   VAL E N   1 
ATOM   7531 C  CA  . VAL E  1 96  ? 48.056  -7.170  35.342  1.00 6.32  ? 96   VAL E CA  1 
ATOM   7532 C  C   . VAL E  1 96  ? 49.438  -7.817  35.406  1.00 6.71  ? 96   VAL E C   1 
ATOM   7533 O  O   . VAL E  1 96  ? 49.944  -8.151  36.479  1.00 7.03  ? 96   VAL E O   1 
ATOM   7534 C  CB  . VAL E  1 96  ? 48.097  -5.657  35.661  1.00 8.85  ? 96   VAL E CB  1 
ATOM   7535 C  CG1 . VAL E  1 96  ? 48.636  -5.416  37.062  1.00 11.36 ? 96   VAL E CG1 1 
ATOM   7536 C  CG2 . VAL E  1 96  ? 48.929  -4.908  34.604  1.00 9.51  ? 96   VAL E CG2 1 
ATOM   7537 N  N   . SER E  1 97  ? 50.041  -8.032  34.244  1.00 6.53  ? 97   SER E N   1 
ATOM   7538 C  CA  . SER E  1 97  ? 51.397  -8.551  34.222  1.00 5.59  ? 97   SER E CA  1 
ATOM   7539 C  C   . SER E  1 97  ? 52.290  -7.619  33.425  1.00 7.62  ? 97   SER E C   1 
ATOM   7540 O  O   . SER E  1 97  ? 51.818  -6.854  32.573  1.00 8.68  ? 97   SER E O   1 
ATOM   7541 C  CB  . SER E  1 97  ? 51.448  -9.946  33.600  1.00 7.44  ? 97   SER E CB  1 
ATOM   7542 O  OG  . SER E  1 97  ? 51.207  -9.899  32.203  1.00 9.71  ? 97   SER E OG  1 
ATOM   7543 N  N   . TRP E  1 98  ? 53.586  -7.702  33.685  1.00 7.50  ? 98   TRP E N   1 
ATOM   7544 C  CA  . TRP E  1 98  ? 54.548  -6.927  32.898  1.00 6.22  ? 98   TRP E CA  1 
ATOM   7545 C  C   . TRP E  1 98  ? 55.829  -7.729  32.722  1.00 7.54  ? 98   TRP E C   1 
ATOM   7546 O  O   . TRP E  1 98  ? 56.261  -8.434  33.641  1.00 6.94  ? 98   TRP E O   1 
ATOM   7547 C  CB  . TRP E  1 98  ? 54.809  -5.567  33.559  1.00 6.47  ? 98   TRP E CB  1 
ATOM   7548 C  CG  . TRP E  1 98  ? 55.879  -4.746  32.881  1.00 9.06  ? 98   TRP E CG  1 
ATOM   7549 C  CD1 . TRP E  1 98  ? 55.733  -3.942  31.776  1.00 8.56  ? 98   TRP E CD1 1 
ATOM   7550 C  CD2 . TRP E  1 98  ? 57.247  -4.645  33.276  1.00 7.58  ? 98   TRP E CD2 1 
ATOM   7551 N  NE1 . TRP E  1 98  ? 56.946  -3.349  31.463  1.00 9.85  ? 98   TRP E NE1 1 
ATOM   7552 C  CE2 . TRP E  1 98  ? 57.886  -3.765  32.370  1.00 9.74  ? 98   TRP E CE2 1 
ATOM   7553 C  CE3 . TRP E  1 98  ? 57.999  -5.211  34.311  1.00 10.59 ? 98   TRP E CE3 1 
ATOM   7554 C  CZ2 . TRP E  1 98  ? 59.250  -3.445  32.468  1.00 8.99  ? 98   TRP E CZ2 1 
ATOM   7555 C  CZ3 . TRP E  1 98  ? 59.361  -4.890  34.406  1.00 10.71 ? 98   TRP E CZ3 1 
ATOM   7556 C  CH2 . TRP E  1 98  ? 59.964  -4.014  33.491  1.00 8.55  ? 98   TRP E CH2 1 
ATOM   7557 N  N   . GLU E  1 99  ? 56.426  -7.606  31.537  1.00 7.51  ? 99   GLU E N   1 
ATOM   7558 C  CA  . GLU E  1 99  ? 57.576  -8.411  31.136  1.00 8.18  ? 99   GLU E CA  1 
ATOM   7559 C  C   . GLU E  1 99  ? 58.658  -7.455  30.631  1.00 10.26 ? 99   GLU E C   1 
ATOM   7560 O  O   . GLU E  1 99  ? 58.472  -6.824  29.598  1.00 11.51 ? 99   GLU E O   1 
ATOM   7561 C  CB  . GLU E  1 99  ? 57.131  -9.322  29.989  1.00 12.23 ? 99   GLU E CB  1 
ATOM   7562 C  CG  . GLU E  1 99  ? 58.160  -10.310 29.498  1.00 16.43 ? 99   GLU E CG  1 
ATOM   7563 C  CD  . GLU E  1 99  ? 57.637  -11.112 28.330  1.00 23.37 ? 99   GLU E CD  1 
ATOM   7564 O  OE1 . GLU E  1 99  ? 57.282  -10.509 27.292  1.00 17.96 ? 99   GLU E OE1 1 
ATOM   7565 O  OE2 . GLU E  1 99  ? 57.569  -12.348 28.458  1.00 30.53 ? 99   GLU E OE2 1 
ATOM   7566 N  N   . SER E  1 100 ? 59.770  -7.347  31.356  1.00 10.28 ? 100  SER E N   1 
ATOM   7567 C  CA  . SER E  1 100 ? 60.849  -6.433  30.958  1.00 9.39  ? 100  SER E CA  1 
ATOM   7568 C  C   . SER E  1 100 ? 61.373  -6.675  29.541  1.00 10.73 ? 100  SER E C   1 
ATOM   7569 O  O   . SER E  1 100 ? 61.624  -5.724  28.786  1.00 11.36 ? 100  SER E O   1 
ATOM   7570 C  CB  . SER E  1 100 ? 62.020  -6.504  31.946  1.00 10.44 ? 100  SER E CB  1 
ATOM   7571 O  OG  . SER E  1 100 ? 63.108  -5.719  31.478  1.00 11.60 ? 100  SER E OG  1 
ATOM   7572 N  N   . SER E  1 101 ? 61.534  -7.936  29.167  1.00 8.83  ? 101  SER E N   1 
ATOM   7573 C  CA  . SER E  1 101 ? 62.203  -8.241  27.898  1.00 10.44 ? 101  SER E CA  1 
ATOM   7574 C  C   . SER E  1 101 ? 61.501  -7.614  26.694  1.00 10.23 ? 101  SER E C   1 
ATOM   7575 O  O   . SER E  1 101 ? 62.160  -7.208  25.734  1.00 12.12 ? 101  SER E O   1 
ATOM   7576 C  CB  . SER E  1 101 ? 62.361  -9.753  27.702  1.00 17.06 ? 101  SER E CB  1 
ATOM   7577 O  OG  . SER E  1 101 ? 61.102  -10.388 27.696  1.00 20.08 ? 101  SER E OG  1 
ATOM   7578 N  N   . SER E  1 102 ? 60.173  -7.523  26.760  1.00 8.65  ? 102  SER E N   1 
ATOM   7579 C  CA  . SER E  1 102 ? 59.367  -6.967  25.679  1.00 7.25  ? 102  SER E CA  1 
ATOM   7580 C  C   . SER E  1 102 ? 58.764  -5.626  26.047  1.00 10.12 ? 102  SER E C   1 
ATOM   7581 O  O   . SER E  1 102 ? 58.281  -4.900  25.180  1.00 10.88 ? 102  SER E O   1 
ATOM   7582 C  CB  . SER E  1 102 ? 58.214  -7.916  25.336  1.00 10.02 ? 102  SER E CB  1 
ATOM   7583 O  OG  . SER E  1 102 ? 57.343  -8.054  26.449  1.00 8.26  ? 102  SER E OG  1 
ATOM   7584 N  N   . GLY E  1 103 ? 58.742  -5.331  27.343  1.00 8.14  ? 103  GLY E N   1 
ATOM   7585 C  CA  . GLY E  1 103 ? 58.016  -4.181  27.865  1.00 7.95  ? 103  GLY E CA  1 
ATOM   7586 C  C   . GLY E  1 103 ? 56.501  -4.342  27.901  1.00 7.66  ? 103  GLY E C   1 
ATOM   7587 O  O   . GLY E  1 103 ? 55.794  -3.401  28.256  1.00 7.12  ? 103  GLY E O   1 
ATOM   7588 N  N   . ILE E  1 104 ? 55.991  -5.514  27.524  1.00 7.04  ? 104  ILE E N   1 
ATOM   7589 C  CA  . ILE E  1 104 ? 54.538  -5.679  27.369  1.00 8.76  ? 104  ILE E CA  1 
ATOM   7590 C  C   . ILE E  1 104 ? 53.810  -5.749  28.706  1.00 9.07  ? 104  ILE E C   1 
ATOM   7591 O  O   . ILE E  1 104 ? 54.198  -6.499  29.588  1.00 7.26  ? 104  ILE E O   1 
ATOM   7592 C  CB  . ILE E  1 104 ? 54.173  -6.924  26.522  1.00 7.64  ? 104  ILE E CB  1 
ATOM   7593 C  CG1 . ILE E  1 104 ? 54.634  -6.743  25.070  1.00 8.77  ? 104  ILE E CG1 1 
ATOM   7594 C  CG2 . ILE E  1 104 ? 52.647  -7.205  26.567  1.00 9.33  ? 104  ILE E CG2 1 
ATOM   7595 C  CD1 . ILE E  1 104 ? 53.975  -5.566  24.339  1.00 11.26 ? 104  ILE E CD1 1 
ATOM   7596 N  N   . ALA E  1 105 ? 52.756  -4.945  28.835  1.00 8.74  ? 105  ALA E N   1 
ATOM   7597 C  CA  . ALA E  1 105 ? 51.857  -4.994  29.986  1.00 8.46  ? 105  ALA E CA  1 
ATOM   7598 C  C   . ALA E  1 105 ? 50.521  -5.586  29.547  1.00 8.89  ? 105  ALA E C   1 
ATOM   7599 O  O   . ALA E  1 105 ? 49.942  -5.128  28.558  1.00 8.50  ? 105  ALA E O   1 
ATOM   7600 C  CB  . ALA E  1 105 ? 51.642  -3.577  30.535  1.00 10.27 ? 105  ALA E CB  1 
ATOM   7601 N  N   . GLU E  1 106 ? 50.034  -6.596  30.271  1.00 7.28  ? 106  GLU E N   1 
ATOM   7602 C  CA  . GLU E  1 106 ? 48.745  -7.217  29.970  1.00 6.25  ? 106  GLU E CA  1 
ATOM   7603 C  C   . GLU E  1 106 ? 47.767  -6.995  31.111  1.00 8.43  ? 106  GLU E C   1 
ATOM   7604 O  O   . GLU E  1 106 ? 47.985  -7.508  32.206  1.00 10.44 ? 106  GLU E O   1 
ATOM   7605 C  CB  . GLU E  1 106 ? 48.878  -8.737  29.832  1.00 9.91  ? 106  GLU E CB  1 
ATOM   7606 C  CG  . GLU E  1 106 ? 49.609  -9.239  28.628  1.00 16.43 ? 106  GLU E CG  1 
ATOM   7607 C  CD  . GLU E  1 106 ? 49.607  -10.762 28.573  1.00 18.13 ? 106  GLU E CD  1 
ATOM   7608 O  OE1 . GLU E  1 106 ? 48.813  -11.418 29.302  1.00 13.44 ? 106  GLU E OE1 1 
ATOM   7609 O  OE2 . GLU E  1 106 ? 50.408  -11.299 27.795  1.00 18.20 ? 106  GLU E OE2 1 
ATOM   7610 N  N   . PHE E  1 107 ? 46.696  -6.243  30.868  1.00 7.12  ? 107  PHE E N   1 
ATOM   7611 C  CA  . PHE E  1 107 ? 45.577  -6.183  31.815  1.00 6.51  ? 107  PHE E CA  1 
ATOM   7612 C  C   . PHE E  1 107 ? 44.529  -7.217  31.441  1.00 7.96  ? 107  PHE E C   1 
ATOM   7613 O  O   . PHE E  1 107 ? 44.213  -7.402  30.258  1.00 6.04  ? 107  PHE E O   1 
ATOM   7614 C  CB  . PHE E  1 107 ? 44.909  -4.805  31.788  1.00 5.49  ? 107  PHE E CB  1 
ATOM   7615 C  CG  . PHE E  1 107 ? 45.511  -3.799  32.746  1.00 8.86  ? 107  PHE E CG  1 
ATOM   7616 C  CD1 . PHE E  1 107 ? 45.272  -3.895  34.111  1.00 8.17  ? 107  PHE E CD1 1 
ATOM   7617 C  CD2 . PHE E  1 107 ? 46.264  -2.737  32.276  1.00 9.14  ? 107  PHE E CD2 1 
ATOM   7618 C  CE1 . PHE E  1 107 ? 45.803  -2.959  34.996  1.00 8.73  ? 107  PHE E CE1 1 
ATOM   7619 C  CE2 . PHE E  1 107 ? 46.799  -1.793  33.148  1.00 10.15 ? 107  PHE E CE2 1 
ATOM   7620 C  CZ  . PHE E  1 107 ? 46.569  -1.901  34.509  1.00 11.76 ? 107  PHE E CZ  1 
ATOM   7621 N  N   . TRP E  1 108 ? 43.994  -7.892  32.450  1.00 6.40  ? 108  TRP E N   1 
ATOM   7622 C  CA  . TRP E  1 108 ? 42.860  -8.787  32.270  1.00 7.94  ? 108  TRP E CA  1 
ATOM   7623 C  C   . TRP E  1 108 ? 41.804  -8.372  33.270  1.00 7.57  ? 108  TRP E C   1 
ATOM   7624 O  O   . TRP E  1 108 ? 42.073  -8.318  34.468  1.00 8.13  ? 108  TRP E O   1 
ATOM   7625 C  CB  . TRP E  1 108 ? 43.266  -10.226 32.571  1.00 7.39  ? 108  TRP E CB  1 
ATOM   7626 C  CG  . TRP E  1 108 ? 44.251  -10.788 31.593  1.00 9.19  ? 108  TRP E CG  1 
ATOM   7627 C  CD1 . TRP E  1 108 ? 45.575  -10.452 31.466  1.00 11.55 ? 108  TRP E CD1 1 
ATOM   7628 C  CD2 . TRP E  1 108 ? 43.995  -11.809 30.618  1.00 7.25  ? 108  TRP E CD2 1 
ATOM   7629 N  NE1 . TRP E  1 108 ? 46.157  -11.202 30.452  1.00 12.70 ? 108  TRP E NE1 1 
ATOM   7630 C  CE2 . TRP E  1 108 ? 45.207  -12.040 29.922  1.00 10.05 ? 108  TRP E CE2 1 
ATOM   7631 C  CE3 . TRP E  1 108 ? 42.861  -12.552 30.269  1.00 8.39  ? 108  TRP E CE3 1 
ATOM   7632 C  CZ2 . TRP E  1 108 ? 45.311  -12.981 28.893  1.00 8.58  ? 108  TRP E CZ2 1 
ATOM   7633 C  CZ3 . TRP E  1 108 ? 42.967  -13.491 29.237  1.00 9.65  ? 108  TRP E CZ3 1 
ATOM   7634 C  CH2 . TRP E  1 108 ? 44.185  -13.695 28.568  1.00 9.93  ? 108  TRP E CH2 1 
ATOM   7635 N  N   . ILE E  1 109 ? 40.594  -8.105  32.780  1.00 5.79  ? 109  ILE E N   1 
ATOM   7636 C  CA  . ILE E  1 109 ? 39.519  -7.598  33.623  1.00 4.81  ? 109  ILE E CA  1 
ATOM   7637 C  C   . ILE E  1 109 ? 38.390  -8.626  33.582  1.00 8.39  ? 109  ILE E C   1 
ATOM   7638 O  O   . ILE E  1 109 ? 37.853  -8.913  32.510  1.00 9.62  ? 109  ILE E O   1 
ATOM   7639 C  CB  . ILE E  1 109 ? 39.015  -6.233  33.099  1.00 8.94  ? 109  ILE E CB  1 
ATOM   7640 C  CG1 . ILE E  1 109 ? 40.137  -5.179  33.126  1.00 8.99  ? 109  ILE E CG1 1 
ATOM   7641 C  CG2 . ILE E  1 109 ? 37.769  -5.765  33.885  1.00 11.99 ? 109  ILE E CG2 1 
ATOM   7642 C  CD1 . ILE E  1 109 ? 40.724  -4.912  34.537  1.00 8.84  ? 109  ILE E CD1 1 
ATOM   7643 N  N   . ASN E  1 110 ? 38.048  -9.199  34.734  1.00 7.40  ? 110  ASN E N   1 
ATOM   7644 C  CA  . ASN E  1 110 ? 37.056  -10.285 34.780  1.00 6.91  ? 110  ASN E CA  1 
ATOM   7645 C  C   . ASN E  1 110 ? 37.372  -11.367 33.751  1.00 11.51 ? 110  ASN E C   1 
ATOM   7646 O  O   . ASN E  1 110 ? 36.480  -11.877 33.061  1.00 12.81 ? 110  ASN E O   1 
ATOM   7647 C  CB  . ASN E  1 110 ? 35.643  -9.749  34.571  1.00 11.78 ? 110  ASN E CB  1 
ATOM   7648 C  CG  . ASN E  1 110 ? 35.252  -8.747  35.625  1.00 13.24 ? 110  ASN E CG  1 
ATOM   7649 O  OD1 . ASN E  1 110 ? 35.649  -8.870  36.787  1.00 10.31 ? 110  ASN E OD1 1 
ATOM   7650 N  ND2 . ASN E  1 110 ? 34.466  -7.744  35.233  1.00 17.98 ? 110  ASN E ND2 1 
ATOM   7651 N  N   . GLY E  1 111 ? 38.651  -11.697 33.649  1.00 8.73  ? 111  GLY E N   1 
ATOM   7652 C  CA  . GLY E  1 111 ? 39.101  -12.788 32.806  1.00 10.29 ? 111  GLY E CA  1 
ATOM   7653 C  C   . GLY E  1 111 ? 39.135  -12.464 31.319  1.00 8.96  ? 111  GLY E C   1 
ATOM   7654 O  O   . GLY E  1 111 ? 39.378  -13.359 30.509  1.00 14.11 ? 111  GLY E O   1 
ATOM   7655 N  N   . THR E  1 112 ? 38.903  -11.205 30.964  1.00 9.75  ? 112  THR E N   1 
ATOM   7656 C  CA  . THR E  1 112 ? 38.940  -10.746 29.575  1.00 10.14 ? 112  THR E CA  1 
ATOM   7657 C  C   . THR E  1 112 ? 40.199  -9.904  29.338  1.00 7.86  ? 112  THR E C   1 
ATOM   7658 O  O   . THR E  1 112 ? 40.456  -8.962  30.091  1.00 10.01 ? 112  THR E O   1 
ATOM   7659 C  CB  . THR E  1 112 ? 37.718  -9.860  29.269  1.00 16.78 ? 112  THR E CB  1 
ATOM   7660 O  OG1 . THR E  1 112 ? 36.529  -10.662 29.336  1.00 22.01 ? 112  THR E OG1 1 
ATOM   7661 C  CG2 . THR E  1 112 ? 37.831  -9.237  27.873  1.00 23.73 ? 112  THR E CG2 1 
ATOM   7662 N  N   . PRO E  1 113 ? 40.979  -10.231 28.290  1.00 7.03  ? 113  PRO E N   1 
ATOM   7663 C  CA  . PRO E  1 113 ? 42.222  -9.488  28.047  1.00 5.45  ? 113  PRO E CA  1 
ATOM   7664 C  C   . PRO E  1 113 ? 41.957  -8.117  27.440  1.00 6.52  ? 113  PRO E C   1 
ATOM   7665 O  O   . PRO E  1 113 ? 41.160  -8.015  26.509  1.00 8.51  ? 113  PRO E O   1 
ATOM   7666 C  CB  . PRO E  1 113 ? 42.973  -10.365 27.035  1.00 9.54  ? 113  PRO E CB  1 
ATOM   7667 C  CG  . PRO E  1 113 ? 41.893  -11.149 26.334  1.00 9.84  ? 113  PRO E CG  1 
ATOM   7668 C  CD  . PRO E  1 113 ? 40.776  -11.343 27.337  1.00 9.03  ? 113  PRO E CD  1 
ATOM   7669 N  N   . LEU E  1 114 ? 42.590  -7.083  27.986  1.00 6.09  ? 114  LEU E N   1 
ATOM   7670 C  CA  . LEU E  1 114 ? 42.538  -5.764  27.363  1.00 6.93  ? 114  LEU E CA  1 
ATOM   7671 C  C   . LEU E  1 114 ? 43.607  -5.707  26.272  1.00 6.56  ? 114  LEU E C   1 
ATOM   7672 O  O   . LEU E  1 114 ? 44.430  -6.630  26.130  1.00 8.39  ? 114  LEU E O   1 
ATOM   7673 C  CB  . LEU E  1 114 ? 42.788  -4.655  28.390  1.00 7.15  ? 114  LEU E CB  1 
ATOM   7674 C  CG  . LEU E  1 114 ? 41.895  -4.634  29.633  1.00 9.54  ? 114  LEU E CG  1 
ATOM   7675 C  CD1 . LEU E  1 114 ? 41.903  -3.244  30.284  1.00 7.16  ? 114  LEU E CD1 1 
ATOM   7676 C  CD2 . LEU E  1 114 ? 40.478  -5.085  29.305  1.00 11.54 ? 114  LEU E CD2 1 
ATOM   7677 N  N   . VAL E  1 115 ? 43.604  -4.634  25.493  1.00 6.76  ? 115  VAL E N   1 
ATOM   7678 C  CA  . VAL E  1 115 ? 44.654  -4.445  24.497  1.00 6.16  ? 115  VAL E CA  1 
ATOM   7679 C  C   . VAL E  1 115 ? 46.020  -4.344  25.185  1.00 5.51  ? 115  VAL E C   1 
ATOM   7680 O  O   . VAL E  1 115 ? 46.187  -3.607  26.155  1.00 6.61  ? 115  VAL E O   1 
ATOM   7681 C  CB  . VAL E  1 115 ? 44.396  -3.176  23.661  1.00 6.37  ? 115  VAL E CB  1 
ATOM   7682 C  CG1 . VAL E  1 115 ? 45.516  -2.972  22.613  1.00 7.12  ? 115  VAL E CG1 1 
ATOM   7683 C  CG2 . VAL E  1 115 ? 43.045  -3.274  22.975  1.00 6.49  ? 115  VAL E CG2 1 
ATOM   7684 N  N   . LYS E  1 116 ? 46.995  -5.109  24.708  1.00 6.37  ? 116  LYS E N   1 
ATOM   7685 C  CA  . LYS E  1 116 ? 48.352  -5.000  25.240  1.00 8.24  ? 116  LYS E CA  1 
ATOM   7686 C  C   . LYS E  1 116 ? 48.953  -3.622  24.976  1.00 10.31 ? 116  LYS E C   1 
ATOM   7687 O  O   . LYS E  1 116 ? 48.739  -3.036  23.914  1.00 9.10  ? 116  LYS E O   1 
ATOM   7688 C  CB  . LYS E  1 116 ? 49.267  -6.065  24.612  1.00 8.47  ? 116  LYS E CB  1 
ATOM   7689 C  CG  . LYS E  1 116 ? 49.052  -7.489  25.120  1.00 9.30  ? 116  LYS E CG  1 
ATOM   7690 C  CD  . LYS E  1 116 ? 49.799  -8.474  24.209  1.00 10.20 ? 116  LYS E CD  1 
ATOM   7691 C  CE  . LYS E  1 116 ? 49.966  -9.841  24.857  1.00 12.31 ? 116  LYS E CE  1 
ATOM   7692 N  NZ  . LYS E  1 116 ? 48.686  -10.597 24.940  1.00 12.42 ? 116  LYS E NZ  1 
ATOM   7693 N  N   . LYS E  1 117 ? 49.721  -3.116  25.943  1.00 8.31  ? 117  LYS E N   1 
ATOM   7694 C  CA  . LYS E  1 117 ? 50.517  -1.909  25.728  1.00 6.14  ? 117  LYS E CA  1 
ATOM   7695 C  C   . LYS E  1 117 ? 51.942  -2.223  26.163  1.00 8.34  ? 117  LYS E C   1 
ATOM   7696 O  O   . LYS E  1 117 ? 52.212  -3.304  26.677  1.00 11.02 ? 117  LYS E O   1 
ATOM   7697 C  CB  . LYS E  1 117 ? 49.951  -0.718  26.524  1.00 9.58  ? 117  LYS E CB  1 
ATOM   7698 C  CG  . LYS E  1 117 ? 48.480  -0.393  26.212  1.00 9.06  ? 117  LYS E CG  1 
ATOM   7699 C  CD  . LYS E  1 117 ? 48.305  0.148   24.789  1.00 10.09 ? 117  LYS E CD  1 
ATOM   7700 C  CE  . LYS E  1 117 ? 46.851  0.054   24.348  1.00 10.06 ? 117  LYS E CE  1 
ATOM   7701 N  NZ  . LYS E  1 117 ? 45.952  0.952   25.149  1.00 13.33 ? 117  LYS E NZ  1 
ATOM   7702 N  N   . GLY E  1 118 ? 52.866  -1.299  25.936  1.00 7.76  ? 118  GLY E N   1 
ATOM   7703 C  CA  . GLY E  1 118 ? 54.250  -1.587  26.240  1.00 9.49  ? 118  GLY E CA  1 
ATOM   7704 C  C   . GLY E  1 118 ? 54.968  -0.384  26.799  1.00 8.66  ? 118  GLY E C   1 
ATOM   7705 O  O   . GLY E  1 118 ? 54.745  0.752   26.354  1.00 8.22  ? 118  GLY E O   1 
ATOM   7706 N  N   . LEU E  1 119 ? 55.834  -0.638  27.772  1.00 7.32  ? 119  LEU E N   1 
ATOM   7707 C  CA  . LEU E  1 119 ? 56.624  0.409   28.404  1.00 7.77  ? 119  LEU E CA  1 
ATOM   7708 C  C   . LEU E  1 119 ? 57.854  -0.171  29.084  1.00 8.06  ? 119  LEU E C   1 
ATOM   7709 O  O   . LEU E  1 119 ? 57.865  -1.340  29.480  1.00 8.85  ? 119  LEU E O   1 
ATOM   7710 C  CB  . LEU E  1 119 ? 55.779  1.179   29.436  1.00 7.96  ? 119  LEU E CB  1 
ATOM   7711 C  CG  . LEU E  1 119 ? 55.455  0.498   30.772  1.00 5.11  ? 119  LEU E CG  1 
ATOM   7712 C  CD1 . LEU E  1 119 ? 54.801  1.514   31.712  1.00 7.90  ? 119  LEU E CD1 1 
ATOM   7713 C  CD2 . LEU E  1 119 ? 54.525  -0.733  30.601  1.00 6.55  ? 119  LEU E CD2 1 
ATOM   7714 N  N   . ARG E  1 120 ? 58.892  0.655   29.212  1.00 9.01  ? 120  ARG E N   1 
ATOM   7715 C  CA  . ARG E  1 120 ? 60.053  0.288   30.018  1.00 8.29  ? 120  ARG E CA  1 
ATOM   7716 C  C   . ARG E  1 120 ? 60.717  -1.028  29.603  1.00 10.45 ? 120  ARG E C   1 
ATOM   7717 O  O   . ARG E  1 120 ? 61.207  -1.791  30.438  1.00 8.72  ? 120  ARG E O   1 
ATOM   7718 C  CB  . ARG E  1 120 ? 59.658  0.262   31.502  1.00 9.18  ? 120  ARG E CB  1 
ATOM   7719 C  CG  . ARG E  1 120 ? 59.433  1.655   32.069  1.00 8.77  ? 120  ARG E CG  1 
ATOM   7720 C  CD  . ARG E  1 120 ? 60.753  2.370   32.171  1.00 12.37 ? 120  ARG E CD  1 
ATOM   7721 N  NE  . ARG E  1 120 ? 60.760  3.470   33.133  1.00 10.70 ? 120  ARG E NE  1 
ATOM   7722 C  CZ  . ARG E  1 120 ? 61.791  4.297   33.264  1.00 17.26 ? 120  ARG E CZ  1 
ATOM   7723 N  NH1 . ARG E  1 120 ? 61.769  5.285   34.154  1.00 13.90 ? 120  ARG E NH1 1 
ATOM   7724 N  NH2 . ARG E  1 120 ? 62.860  4.128   32.489  1.00 13.89 ? 120  ARG E NH2 1 
ATOM   7725 N  N   . GLN E  1 121 ? 60.743  -1.293  28.303  1.00 8.95  ? 121  GLN E N   1 
ATOM   7726 C  CA  . GLN E  1 121 ? 61.438  -2.478  27.826  1.00 9.17  ? 121  GLN E CA  1 
ATOM   7727 C  C   . GLN E  1 121 ? 62.884  -2.458  28.335  1.00 7.83  ? 121  GLN E C   1 
ATOM   7728 O  O   . GLN E  1 121 ? 63.605  -1.464  28.161  1.00 9.04  ? 121  GLN E O   1 
ATOM   7729 C  CB  . GLN E  1 121 ? 61.427  -2.528  26.294  1.00 7.84  ? 121  GLN E CB  1 
ATOM   7730 C  CG  . GLN E  1 121 ? 62.122  -3.769  25.730  1.00 10.61 ? 121  GLN E CG  1 
ATOM   7731 C  CD  . GLN E  1 121 ? 62.039  -3.835  24.211  1.00 13.10 ? 121  GLN E CD  1 
ATOM   7732 O  OE1 . GLN E  1 121 ? 62.076  -2.807  23.533  1.00 12.79 ? 121  GLN E OE1 1 
ATOM   7733 N  NE2 . GLN E  1 121 ? 61.928  -5.045  23.672  1.00 12.27 ? 121  GLN E NE2 1 
ATOM   7734 N  N   . GLY E  1 122 ? 63.294  -3.538  28.993  1.00 8.50  ? 122  GLY E N   1 
ATOM   7735 C  CA  . GLY E  1 122 ? 64.677  -3.694  29.432  1.00 8.17  ? 122  GLY E CA  1 
ATOM   7736 C  C   . GLY E  1 122 ? 64.935  -3.224  30.855  1.00 11.40 ? 122  GLY E C   1 
ATOM   7737 O  O   . GLY E  1 122 ? 65.999  -3.475  31.425  1.00 10.84 ? 122  GLY E O   1 
ATOM   7738 N  N   . TYR E  1 123 ? 63.956  -2.525  31.420  1.00 7.05  ? 123  TYR E N   1 
ATOM   7739 C  CA  . TYR E  1 123 ? 64.034  -1.987  32.773  1.00 7.80  ? 123  TYR E CA  1 
ATOM   7740 C  C   . TYR E  1 123 ? 63.839  -3.072  33.833  1.00 11.53 ? 123  TYR E C   1 
ATOM   7741 O  O   . TYR E  1 123 ? 63.241  -4.108  33.556  1.00 11.38 ? 123  TYR E O   1 
ATOM   7742 C  CB  . TYR E  1 123 ? 62.946  -0.904  32.913  1.00 8.33  ? 123  TYR E CB  1 
ATOM   7743 C  CG  . TYR E  1 123 ? 62.884  -0.184  34.242  1.00 9.81  ? 123  TYR E CG  1 
ATOM   7744 C  CD1 . TYR E  1 123 ? 63.850  0.752   34.582  1.00 9.61  ? 123  TYR E CD1 1 
ATOM   7745 C  CD2 . TYR E  1 123 ? 61.838  -0.412  35.141  1.00 7.48  ? 123  TYR E CD2 1 
ATOM   7746 C  CE1 . TYR E  1 123 ? 63.797  1.432   35.782  1.00 11.52 ? 123  TYR E CE1 1 
ATOM   7747 C  CE2 . TYR E  1 123 ? 61.779  0.272   36.355  1.00 9.12  ? 123  TYR E CE2 1 
ATOM   7748 C  CZ  . TYR E  1 123 ? 62.767  1.195   36.661  1.00 9.55  ? 123  TYR E CZ  1 
ATOM   7749 O  OH  . TYR E  1 123 ? 62.758  1.879   37.854  1.00 11.02 ? 123  TYR E OH  1 
ATOM   7750 N  N   . PHE E  1 124 ? 64.358  -2.841  35.038  1.00 9.12  ? 124  PHE E N   1 
ATOM   7751 C  CA  . PHE E  1 124 ? 64.058  -3.715  36.176  1.00 12.46 ? 124  PHE E CA  1 
ATOM   7752 C  C   . PHE E  1 124 ? 63.362  -2.909  37.260  1.00 9.51  ? 124  PHE E C   1 
ATOM   7753 O  O   . PHE E  1 124 ? 63.854  -1.845  37.681  1.00 11.75 ? 124  PHE E O   1 
ATOM   7754 C  CB  . PHE E  1 124 ? 65.319  -4.339  36.783  1.00 13.01 ? 124  PHE E CB  1 
ATOM   7755 C  CG  . PHE E  1 124 ? 65.907  -5.472  35.982  1.00 17.17 ? 124  PHE E CG  1 
ATOM   7756 C  CD1 . PHE E  1 124 ? 66.437  -5.251  34.723  1.00 20.54 ? 124  PHE E CD1 1 
ATOM   7757 C  CD2 . PHE E  1 124 ? 65.974  -6.752  36.516  1.00 25.85 ? 124  PHE E CD2 1 
ATOM   7758 C  CE1 . PHE E  1 124 ? 66.997  -6.294  33.990  1.00 22.99 ? 124  PHE E CE1 1 
ATOM   7759 C  CE2 . PHE E  1 124 ? 66.531  -7.801  35.791  1.00 28.66 ? 124  PHE E CE2 1 
ATOM   7760 C  CZ  . PHE E  1 124 ? 67.042  -7.570  34.526  1.00 23.82 ? 124  PHE E CZ  1 
ATOM   7761 N  N   . VAL E  1 125 ? 62.221  -3.409  37.721  1.00 9.79  ? 125  VAL E N   1 
ATOM   7762 C  CA  . VAL E  1 125 ? 61.521  -2.751  38.818  1.00 9.13  ? 125  VAL E CA  1 
ATOM   7763 C  C   . VAL E  1 125 ? 62.366  -2.870  40.082  1.00 10.46 ? 125  VAL E C   1 
ATOM   7764 O  O   . VAL E  1 125 ? 62.801  -3.963  40.447  1.00 11.83 ? 125  VAL E O   1 
ATOM   7765 C  CB  . VAL E  1 125 ? 60.112  -3.341  39.031  1.00 10.00 ? 125  VAL E CB  1 
ATOM   7766 C  CG1 . VAL E  1 125 ? 59.484  -2.788  40.298  1.00 10.19 ? 125  VAL E CG1 1 
ATOM   7767 C  CG2 . VAL E  1 125 ? 59.225  -3.046  37.813  1.00 10.36 ? 125  VAL E CG2 1 
ATOM   7768 N  N   . GLU E  1 126 ? 62.601  -1.737  40.736  1.00 10.02 ? 126  GLU E N   1 
ATOM   7769 C  CA  . GLU E  1 126 ? 63.486  -1.706  41.898  1.00 11.29 ? 126  GLU E CA  1 
ATOM   7770 C  C   . GLU E  1 126 ? 62.890  -2.515  43.052  1.00 16.02 ? 126  GLU E C   1 
ATOM   7771 O  O   . GLU E  1 126 ? 61.675  -2.592  43.186  1.00 13.04 ? 126  GLU E O   1 
ATOM   7772 C  CB  . GLU E  1 126 ? 63.772  -0.266  42.323  1.00 12.60 ? 126  GLU E CB  1 
ATOM   7773 C  CG  . GLU E  1 126 ? 64.823  -0.147  43.409  1.00 17.33 ? 126  GLU E CG  1 
ATOM   7774 C  CD  . GLU E  1 126 ? 66.134  -0.838  43.020  1.00 24.01 ? 126  GLU E CD  1 
ATOM   7775 O  OE1 . GLU E  1 126 ? 66.403  -1.951  43.524  1.00 28.76 ? 126  GLU E OE1 1 
ATOM   7776 O  OE2 . GLU E  1 126 ? 66.880  -0.277  42.195  1.00 24.28 ? 126  GLU E OE2 1 
ATOM   7777 N  N   . ALA E  1 127 ? 63.756  -3.125  43.862  1.00 13.47 ? 127  ALA E N   1 
ATOM   7778 C  CA  . ALA E  1 127 ? 63.339  -3.916  45.021  1.00 16.34 ? 127  ALA E CA  1 
ATOM   7779 C  C   . ALA E  1 127 ? 63.308  -3.073  46.299  1.00 12.51 ? 127  ALA E C   1 
ATOM   7780 O  O   . ALA E  1 127 ? 63.416  -1.852  46.244  1.00 13.90 ? 127  ALA E O   1 
ATOM   7781 C  CB  . ALA E  1 127 ? 64.265  -5.126  45.202  1.00 18.01 ? 127  ALA E CB  1 
ATOM   7782 N  N   . GLN E  1 128 ? 63.176  -3.744  47.446  1.00 13.64 ? 128  GLN E N   1 
ATOM   7783 C  CA  . GLN E  1 128 ? 62.988  -3.080  48.741  1.00 14.52 ? 128  GLN E CA  1 
ATOM   7784 C  C   . GLN E  1 128 ? 61.833  -2.075  48.714  1.00 10.10 ? 128  GLN E C   1 
ATOM   7785 O  O   . GLN E  1 128 ? 61.997  -0.907  49.071  1.00 12.16 ? 128  GLN E O   1 
ATOM   7786 C  CB  . GLN E  1 128 ? 64.292  -2.423  49.218  1.00 17.62 ? 128  GLN E CB  1 
ATOM   7787 C  CG  . GLN E  1 128 ? 65.407  -3.454  49.465  1.00 18.39 ? 128  GLN E CG  1 
ATOM   7788 C  CD  . GLN E  1 128 ? 66.719  -2.823  49.894  1.00 39.70 ? 128  GLN E CD  1 
ATOM   7789 O  OE1 . GLN E  1 128 ? 66.947  -1.629  49.692  1.00 55.41 ? 128  GLN E OE1 1 
ATOM   7790 N  NE2 . GLN E  1 128 ? 67.595  -3.630  50.487  1.00 51.71 ? 128  GLN E NE2 1 
ATOM   7791 N  N   . PRO E  1 129 ? 60.651  -2.525  48.280  1.00 10.83 ? 129  PRO E N   1 
ATOM   7792 C  CA  . PRO E  1 129 ? 59.545  -1.573  48.138  1.00 9.02  ? 129  PRO E CA  1 
ATOM   7793 C  C   . PRO E  1 129 ? 58.809  -1.339  49.446  1.00 10.30 ? 129  PRO E C   1 
ATOM   7794 O  O   . PRO E  1 129 ? 58.909  -2.134  50.391  1.00 14.40 ? 129  PRO E O   1 
ATOM   7795 C  CB  . PRO E  1 129 ? 58.594  -2.310  47.203  1.00 8.56  ? 129  PRO E CB  1 
ATOM   7796 C  CG  . PRO E  1 129 ? 58.783  -3.756  47.583  1.00 10.94 ? 129  PRO E CG  1 
ATOM   7797 C  CD  . PRO E  1 129 ? 60.269  -3.886  47.865  1.00 11.63 ? 129  PRO E CD  1 
ATOM   7798 N  N   . LYS E  1 130 ? 58.075  -0.238  49.491  1.00 7.99  ? 130  LYS E N   1 
ATOM   7799 C  CA  . LYS E  1 130 ? 56.940  -0.109  50.394  1.00 10.01 ? 130  LYS E CA  1 
ATOM   7800 C  C   . LYS E  1 130 ? 55.704  -0.275  49.514  1.00 10.10 ? 130  LYS E C   1 
ATOM   7801 O  O   . LYS E  1 130 ? 55.592  0.363   48.460  1.00 8.69  ? 130  LYS E O   1 
ATOM   7802 C  CB  . LYS E  1 130 ? 56.939  1.242   51.109  1.00 13.45 ? 130  LYS E CB  1 
ATOM   7803 C  CG  . LYS E  1 130 ? 58.058  1.347   52.152  1.00 18.09 ? 130  LYS E CG  1 
ATOM   7804 C  CD  . LYS E  1 130 ? 57.804  2.446   53.164  1.00 28.50 ? 130  LYS E CD  1 
ATOM   7805 C  CE  . LYS E  1 130 ? 58.786  2.355   54.330  1.00 28.93 ? 130  LYS E CE  1 
ATOM   7806 N  NZ  . LYS E  1 130 ? 58.742  1.010   54.975  1.00 36.58 ? 130  LYS E NZ  1 
ATOM   7807 N  N   . ILE E  1 131 ? 54.805  -1.156  49.936  1.00 9.00  ? 131  ILE E N   1 
ATOM   7808 C  CA  . ILE E  1 131 ? 53.611  -1.502  49.163  1.00 9.06  ? 131  ILE E CA  1 
ATOM   7809 C  C   . ILE E  1 131 ? 52.370  -1.141  49.973  1.00 9.25  ? 131  ILE E C   1 
ATOM   7810 O  O   . ILE E  1 131 ? 52.228  -1.566  51.119  1.00 9.52  ? 131  ILE E O   1 
ATOM   7811 C  CB  . ILE E  1 131 ? 53.568  -3.012  48.851  1.00 6.12  ? 131  ILE E CB  1 
ATOM   7812 C  CG1 . ILE E  1 131 ? 54.823  -3.413  48.065  1.00 9.31  ? 131  ILE E CG1 1 
ATOM   7813 C  CG2 . ILE E  1 131 ? 52.298  -3.359  48.083  1.00 10.90 ? 131  ILE E CG2 1 
ATOM   7814 C  CD1 . ILE E  1 131 ? 54.929  -4.910  47.816  1.00 8.72  ? 131  ILE E CD1 1 
ATOM   7815 N  N   . VAL E  1 132 ? 51.489  -0.335  49.387  1.00 5.97  ? 132  VAL E N   1 
ATOM   7816 C  CA  . VAL E  1 132 ? 50.364  0.209   50.145  1.00 8.54  ? 132  VAL E CA  1 
ATOM   7817 C  C   . VAL E  1 132 ? 49.062  -0.006  49.408  1.00 7.64  ? 132  VAL E C   1 
ATOM   7818 O  O   . VAL E  1 132 ? 48.994  0.217   48.195  1.00 6.88  ? 132  VAL E O   1 
ATOM   7819 C  CB  . VAL E  1 132 ? 50.550  1.719   50.407  1.00 8.84  ? 132  VAL E CB  1 
ATOM   7820 C  CG1 . VAL E  1 132 ? 49.293  2.329   51.037  1.00 9.85  ? 132  VAL E CG1 1 
ATOM   7821 C  CG2 . VAL E  1 132 ? 51.757  1.950   51.289  1.00 10.07 ? 132  VAL E CG2 1 
ATOM   7822 N  N   . LEU E  1 133 ? 48.055  -0.485  50.143  1.00 7.11  ? 133  LEU E N   1 
ATOM   7823 C  CA  . LEU E  1 133 ? 46.669  -0.506  49.683  1.00 7.59  ? 133  LEU E CA  1 
ATOM   7824 C  C   . LEU E  1 133 ? 45.904  0.596   50.398  1.00 6.76  ? 133  LEU E C   1 
ATOM   7825 O  O   . LEU E  1 133 ? 46.129  0.836   51.584  1.00 8.40  ? 133  LEU E O   1 
ATOM   7826 C  CB  . LEU E  1 133 ? 45.999  -1.846  50.020  1.00 7.08  ? 133  LEU E CB  1 
ATOM   7827 C  CG  . LEU E  1 133 ? 46.621  -3.138  49.484  1.00 8.92  ? 133  LEU E CG  1 
ATOM   7828 C  CD1 . LEU E  1 133 ? 45.741  -4.341  49.870  1.00 7.91  ? 133  LEU E CD1 1 
ATOM   7829 C  CD2 . LEU E  1 133 ? 46.784  -3.062  47.974  1.00 10.80 ? 133  LEU E CD2 1 
ATOM   7830 N  N   . GLY E  1 134 ? 45.004  1.257   49.677  1.00 5.72  ? 134  GLY E N   1 
ATOM   7831 C  CA  . GLY E  1 134 ? 44.100  2.226   50.282  1.00 6.09  ? 134  GLY E CA  1 
ATOM   7832 C  C   . GLY E  1 134 ? 44.530  3.661   50.055  1.00 7.40  ? 134  GLY E C   1 
ATOM   7833 O  O   . GLY E  1 134 ? 43.710  4.579   50.121  1.00 7.14  ? 134  GLY E O   1 
ATOM   7834 N  N   . GLN E  1 135 ? 45.821  3.845   49.781  1.00 6.35  ? 135  GLN E N   1 
ATOM   7835 C  CA  . GLN E  1 135 ? 46.345  5.172   49.472  1.00 8.28  ? 135  GLN E CA  1 
ATOM   7836 C  C   . GLN E  1 135 ? 47.391  5.082   48.370  1.00 8.92  ? 135  GLN E C   1 
ATOM   7837 O  O   . GLN E  1 135 ? 47.983  4.026   48.133  1.00 8.17  ? 135  GLN E O   1 
ATOM   7838 C  CB  . GLN E  1 135 ? 46.965  5.834   50.715  1.00 6.07  ? 135  GLN E CB  1 
ATOM   7839 C  CG  . GLN E  1 135 ? 46.039  5.960   51.937  1.00 5.69  ? 135  GLN E CG  1 
ATOM   7840 C  CD  . GLN E  1 135 ? 44.984  7.043   51.799  1.00 7.14  ? 135  GLN E CD  1 
ATOM   7841 O  OE1 . GLN E  1 135 ? 45.114  7.960   50.990  1.00 9.66  ? 135  GLN E OE1 1 
ATOM   7842 N  NE2 . GLN E  1 135 ? 43.912  6.929   52.592  1.00 8.00  ? 135  GLN E NE2 1 
ATOM   7843 N  N   . GLU E  1 136 ? 47.613  6.207   47.703  1.00 7.04  ? 136  GLU E N   1 
ATOM   7844 C  CA  . GLU E  1 136 ? 48.654  6.314   46.698  1.00 5.84  ? 136  GLU E CA  1 
ATOM   7845 C  C   . GLU E  1 136 ? 49.850  6.997   47.357  1.00 8.32  ? 136  GLU E C   1 
ATOM   7846 O  O   . GLU E  1 136 ? 49.705  8.094   47.891  1.00 9.63  ? 136  GLU E O   1 
ATOM   7847 C  CB  . GLU E  1 136 ? 48.131  7.177   45.546  1.00 8.16  ? 136  GLU E CB  1 
ATOM   7848 C  CG  . GLU E  1 136 ? 48.793  6.890   44.188  1.00 6.70  ? 136  GLU E CG  1 
ATOM   7849 C  CD  . GLU E  1 136 ? 50.160  7.519   44.064  1.00 9.21  ? 136  GLU E CD  1 
ATOM   7850 O  OE1 . GLU E  1 136 ? 50.304  8.697   44.443  1.00 8.46  ? 136  GLU E OE1 1 
ATOM   7851 O  OE2 . GLU E  1 136 ? 51.091  6.850   43.583  1.00 7.97  ? 136  GLU E OE2 1 
ATOM   7852 N  N   . GLN E  1 137 ? 51.022  6.366   47.322  1.00 7.79  ? 137  GLN E N   1 
ATOM   7853 C  CA  . GLN E  1 137 ? 52.236  6.969   47.903  1.00 6.55  ? 137  GLN E CA  1 
ATOM   7854 C  C   . GLN E  1 137 ? 52.867  7.976   46.974  1.00 10.25 ? 137  GLN E C   1 
ATOM   7855 O  O   . GLN E  1 137 ? 52.978  7.714   45.789  1.00 8.91  ? 137  GLN E O   1 
ATOM   7856 C  CB  . GLN E  1 137 ? 53.298  5.903   48.130  1.00 8.32  ? 137  GLN E CB  1 
ATOM   7857 C  CG  . GLN E  1 137 ? 52.942  4.805   49.098  1.00 7.28  ? 137  GLN E CG  1 
ATOM   7858 C  CD  . GLN E  1 137 ? 53.988  3.721   49.066  1.00 9.21  ? 137  GLN E CD  1 
ATOM   7859 O  OE1 . GLN E  1 137 ? 55.037  3.820   49.718  1.00 12.43 ? 137  GLN E OE1 1 
ATOM   7860 N  NE2 . GLN E  1 137 ? 53.733  2.692   48.274  1.00 6.43  ? 137  GLN E NE2 1 
ATOM   7861 N  N   . ASP E  1 138 ? 53.341  9.097   47.524  1.00 7.68  ? 138  ASP E N   1 
ATOM   7862 C  CA  . ASP E  1 138 ? 54.243  9.992   46.788  1.00 10.25 ? 138  ASP E CA  1 
ATOM   7863 C  C   . ASP E  1 138 ? 55.639  10.036  47.401  1.00 12.17 ? 138  ASP E C   1 
ATOM   7864 O  O   . ASP E  1 138 ? 56.538  10.687  46.864  1.00 14.76 ? 138  ASP E O   1 
ATOM   7865 C  CB  . ASP E  1 138 ? 53.677  11.409  46.698  1.00 11.73 ? 138  ASP E CB  1 
ATOM   7866 C  CG  . ASP E  1 138 ? 52.573  11.529  45.676  1.00 9.49  ? 138  ASP E CG  1 
ATOM   7867 O  OD1 . ASP E  1 138 ? 52.503  10.678  44.771  1.00 10.21 ? 138  ASP E OD1 1 
ATOM   7868 O  OD2 . ASP E  1 138 ? 51.768  12.473  45.751  1.00 9.15  ? 138  ASP E OD2 1 
ATOM   7869 N  N   . SER E  1 139 ? 55.810  9.361   48.534  1.00 13.04 ? 139  SER E N   1 
ATOM   7870 C  CA  . SER E  1 139 ? 57.118  9.174   49.133  1.00 12.82 ? 139  SER E CA  1 
ATOM   7871 C  C   . SER E  1 139 ? 57.341  7.696   49.428  1.00 13.79 ? 139  SER E C   1 
ATOM   7872 O  O   . SER E  1 139 ? 56.533  6.840   49.051  1.00 12.50 ? 139  SER E O   1 
ATOM   7873 C  CB  . SER E  1 139 ? 57.240  9.977   50.428  1.00 14.54 ? 139  SER E CB  1 
ATOM   7874 O  OG  . SER E  1 139 ? 56.441  9.411   51.450  1.00 14.10 ? 139  SER E OG  1 
ATOM   7875 N  N   . TYR E  1 140 ? 58.446  7.382   50.090  1.00 13.16 ? 140  TYR E N   1 
ATOM   7876 C  CA  . TYR E  1 140 ? 58.714  5.995   50.429  1.00 10.56 ? 140  TYR E CA  1 
ATOM   7877 C  C   . TYR E  1 140 ? 57.896  5.652   51.662  1.00 16.97 ? 140  TYR E C   1 
ATOM   7878 O  O   . TYR E  1 140 ? 58.353  5.816   52.797  1.00 16.50 ? 140  TYR E O   1 
ATOM   7879 C  CB  . TYR E  1 140 ? 60.205  5.779   50.669  1.00 13.57 ? 140  TYR E CB  1 
ATOM   7880 C  CG  . TYR E  1 140 ? 60.630  4.337   50.871  1.00 13.00 ? 140  TYR E CG  1 
ATOM   7881 C  CD1 . TYR E  1 140 ? 60.365  3.361   49.911  1.00 10.08 ? 140  TYR E CD1 1 
ATOM   7882 C  CD2 . TYR E  1 140 ? 61.333  3.961   52.007  1.00 16.93 ? 140  TYR E CD2 1 
ATOM   7883 C  CE1 . TYR E  1 140 ? 60.779  2.047   50.089  1.00 11.66 ? 140  TYR E CE1 1 
ATOM   7884 C  CE2 . TYR E  1 140 ? 61.751  2.657   52.194  1.00 16.91 ? 140  TYR E CE2 1 
ATOM   7885 C  CZ  . TYR E  1 140 ? 61.473  1.702   51.234  1.00 15.59 ? 140  TYR E CZ  1 
ATOM   7886 O  OH  . TYR E  1 140 ? 61.887  0.406   51.435  1.00 15.84 ? 140  TYR E OH  1 
ATOM   7887 N  N   . GLY E  1 141 ? 56.666  5.210   51.427  1.00 12.15 ? 141  GLY E N   1 
ATOM   7888 C  CA  . GLY E  1 141 ? 55.784  4.814   52.510  1.00 13.16 ? 141  GLY E CA  1 
ATOM   7889 C  C   . GLY E  1 141 ? 54.730  5.827   52.907  1.00 13.77 ? 141  GLY E C   1 
ATOM   7890 O  O   . GLY E  1 141 ? 53.917  5.548   53.784  1.00 19.75 ? 141  GLY E O   1 
ATOM   7891 N  N   . GLY E  1 142 ? 54.727  6.999   52.282  1.00 11.53 ? 142  GLY E N   1 
ATOM   7892 C  CA  . GLY E  1 142 ? 53.800  8.040   52.688  1.00 13.14 ? 142  GLY E CA  1 
ATOM   7893 C  C   . GLY E  1 142 ? 53.477  9.077   51.634  1.00 13.56 ? 142  GLY E C   1 
ATOM   7894 O  O   . GLY E  1 142 ? 53.456  8.783   50.438  1.00 11.49 ? 142  GLY E O   1 
ATOM   7895 N  N   . LYS E  1 143 ? 53.236  10.299  52.105  1.00 12.39 ? 143  LYS E N   1 
ATOM   7896 C  CA  . LYS E  1 143 ? 52.766  11.412  51.287  1.00 10.97 ? 143  LYS E CA  1 
ATOM   7897 C  C   . LYS E  1 143 ? 51.538  11.031  50.482  1.00 11.36 ? 143  LYS E C   1 
ATOM   7898 O  O   . LYS E  1 143 ? 51.525  11.102  49.254  1.00 12.25 ? 143  LYS E O   1 
ATOM   7899 C  CB  . LYS E  1 143 ? 53.874  11.982  50.395  1.00 11.39 ? 143  LYS E CB  1 
ATOM   7900 C  CG  . LYS E  1 143 ? 55.087  12.439  51.173  1.00 27.17 ? 143  LYS E CG  1 
ATOM   7901 C  CD  . LYS E  1 143 ? 55.896  13.435  50.375  1.00 32.85 ? 143  LYS E CD  1 
ATOM   7902 C  CE  . LYS E  1 143 ? 55.464  14.853  50.695  1.00 57.25 ? 143  LYS E CE  1 
ATOM   7903 N  NZ  . LYS E  1 143 ? 55.663  15.155  52.144  1.00 53.11 ? 143  LYS E NZ  1 
ATOM   7904 N  N   . PHE E  1 144 ? 50.493  10.651  51.213  1.00 9.09  ? 144  PHE E N   1 
ATOM   7905 C  CA  . PHE E  1 144 ? 49.229  10.240  50.628  1.00 9.39  ? 144  PHE E CA  1 
ATOM   7906 C  C   . PHE E  1 144 ? 48.371  11.433  50.176  1.00 9.85  ? 144  PHE E C   1 
ATOM   7907 O  O   . PHE E  1 144 ? 48.669  12.595  50.487  1.00 10.80 ? 144  PHE E O   1 
ATOM   7908 C  CB  . PHE E  1 144 ? 48.460  9.407   51.650  1.00 8.78  ? 144  PHE E CB  1 
ATOM   7909 C  CG  . PHE E  1 144 ? 49.205  8.192   52.143  1.00 11.75 ? 144  PHE E CG  1 
ATOM   7910 C  CD1 . PHE E  1 144 ? 49.935  7.396   51.267  1.00 10.15 ? 144  PHE E CD1 1 
ATOM   7911 C  CD2 . PHE E  1 144 ? 49.120  7.810   53.478  1.00 12.49 ? 144  PHE E CD2 1 
ATOM   7912 C  CE1 . PHE E  1 144 ? 50.593  6.263   51.715  1.00 10.65 ? 144  PHE E CE1 1 
ATOM   7913 C  CE2 . PHE E  1 144 ? 49.777  6.674   53.931  1.00 11.88 ? 144  PHE E CE2 1 
ATOM   7914 C  CZ  . PHE E  1 144 ? 50.513  5.903   53.047  1.00 11.42 ? 144  PHE E CZ  1 
ATOM   7915 N  N   . ASP E  1 145 ? 47.290  11.134  49.463  1.00 8.54  ? 145  ASP E N   1 
ATOM   7916 C  CA  . ASP E  1 145 ? 46.418  12.144  48.864  1.00 8.24  ? 145  ASP E CA  1 
ATOM   7917 C  C   . ASP E  1 145 ? 44.995  11.599  48.912  1.00 9.86  ? 145  ASP E C   1 
ATOM   7918 O  O   . ASP E  1 145 ? 44.685  10.611  48.255  1.00 9.14  ? 145  ASP E O   1 
ATOM   7919 C  CB  . ASP E  1 145 ? 46.866  12.385  47.413  1.00 6.89  ? 145  ASP E CB  1 
ATOM   7920 C  CG  . ASP E  1 145 ? 45.957  13.339  46.641  1.00 12.03 ? 145  ASP E CG  1 
ATOM   7921 O  OD1 . ASP E  1 145 ? 44.893  13.754  47.148  1.00 10.43 ? 145  ASP E OD1 1 
ATOM   7922 O  OD2 . ASP E  1 145 ? 46.318  13.670  45.488  1.00 13.02 ? 145  ASP E OD2 1 
ATOM   7923 N  N   . ARG E  1 146 ? 44.126  12.198  49.720  1.00 8.71  ? 146  ARG E N   1 
ATOM   7924 C  CA  . ARG E  1 146 ? 42.802  11.600  49.883  1.00 6.26  ? 146  ARG E CA  1 
ATOM   7925 C  C   . ARG E  1 146 ? 42.002  11.566  48.575  1.00 6.92  ? 146  ARG E C   1 
ATOM   7926 O  O   . ARG E  1 146 ? 41.082  10.768  48.438  1.00 9.02  ? 146  ARG E O   1 
ATOM   7927 C  CB  . ARG E  1 146 ? 42.003  12.295  51.004  1.00 11.93 ? 146  ARG E CB  1 
ATOM   7928 C  CG  . ARG E  1 146 ? 41.541  13.699  50.689  1.00 12.46 ? 146  ARG E CG  1 
ATOM   7929 C  CD  . ARG E  1 146 ? 40.716  14.242  51.860  1.00 12.52 ? 146  ARG E CD  1 
ATOM   7930 N  NE  . ARG E  1 146 ? 39.369  13.670  51.932  1.00 9.96  ? 146  ARG E NE  1 
ATOM   7931 C  CZ  . ARG E  1 146 ? 38.626  13.616  53.042  1.00 13.56 ? 146  ARG E CZ  1 
ATOM   7932 N  NH1 . ARG E  1 146 ? 37.404  13.094  53.012  1.00 11.38 ? 146  ARG E NH1 1 
ATOM   7933 N  NH2 . ARG E  1 146 ? 39.100  14.088  54.187  1.00 14.94 ? 146  ARG E NH2 1 
ATOM   7934 N  N   A SER E  1 147 ? 42.355  12.428  47.622  0.63 8.08  ? 147  SER E N   1 
ATOM   7935 N  N   B SER E  1 147 ? 42.355  12.427  47.621  0.37 8.10  ? 147  SER E N   1 
ATOM   7936 C  CA  A SER E  1 147 ? 41.659  12.439  46.335  0.63 9.15  ? 147  SER E CA  1 
ATOM   7937 C  CA  B SER E  1 147 ? 41.679  12.438  46.321  0.37 9.14  ? 147  SER E CA  1 
ATOM   7938 C  C   A SER E  1 147 ? 42.078  11.251  45.467  0.63 7.36  ? 147  SER E C   1 
ATOM   7939 C  C   B SER E  1 147 ? 42.040  11.212  45.492  0.37 7.42  ? 147  SER E C   1 
ATOM   7940 O  O   A SER E  1 147 ? 41.546  11.061  44.375  0.63 8.38  ? 147  SER E O   1 
ATOM   7941 O  O   B SER E  1 147 ? 41.446  10.967  44.443  0.37 8.40  ? 147  SER E O   1 
ATOM   7942 C  CB  A SER E  1 147 ? 41.879  13.760  45.582  0.63 10.37 ? 147  SER E CB  1 
ATOM   7943 C  CB  B SER E  1 147 ? 42.022  13.700  45.526  0.37 10.54 ? 147  SER E CB  1 
ATOM   7944 O  OG  A SER E  1 147 ? 43.189  13.833  45.032  0.63 11.92 ? 147  SER E OG  1 
ATOM   7945 O  OG  B SER E  1 147 ? 41.384  14.838  46.062  0.37 10.56 ? 147  SER E OG  1 
ATOM   7946 N  N   . GLN E  1 148 ? 43.018  10.450  45.970  1.00 8.22  ? 148  GLN E N   1 
ATOM   7947 C  CA  . GLN E  1 148 ? 43.476  9.249   45.277  1.00 6.65  ? 148  GLN E CA  1 
ATOM   7948 C  C   . GLN E  1 148 ? 43.263  8.005   46.134  1.00 5.63  ? 148  GLN E C   1 
ATOM   7949 O  O   . GLN E  1 148 ? 43.664  6.907   45.758  1.00 7.43  ? 148  GLN E O   1 
ATOM   7950 C  CB  . GLN E  1 148 ? 44.955  9.371   44.923  1.00 8.42  ? 148  GLN E CB  1 
ATOM   7951 C  CG  . GLN E  1 148 ? 45.257  10.510  43.956  1.00 9.14  ? 148  GLN E CG  1 
ATOM   7952 C  CD  . GLN E  1 148 ? 46.739  10.664  43.697  1.00 11.45 ? 148  GLN E CD  1 
ATOM   7953 O  OE1 . GLN E  1 148 ? 47.554  10.467  44.588  1.00 10.15 ? 148  GLN E OE1 1 
ATOM   7954 N  NE2 . GLN E  1 148 ? 47.091  11.015  42.467  1.00 14.12 ? 148  GLN E NE2 1 
ATOM   7955 N  N   . SER E  1 149 ? 42.630  8.186   47.287  1.00 7.17  ? 149  SER E N   1 
ATOM   7956 C  CA  . SER E  1 149 ? 42.435  7.092   48.228  1.00 6.08  ? 149  SER E CA  1 
ATOM   7957 C  C   . SER E  1 149 ? 41.416  6.099   47.687  1.00 7.84  ? 149  SER E C   1 
ATOM   7958 O  O   . SER E  1 149 ? 40.513  6.459   46.940  1.00 7.05  ? 149  SER E O   1 
ATOM   7959 C  CB  . SER E  1 149 ? 41.969  7.621   49.590  1.00 6.90  ? 149  SER E CB  1 
ATOM   7960 O  OG  . SER E  1 149 ? 40.678  8.208   49.505  1.00 9.13  ? 149  SER E OG  1 
ATOM   7961 N  N   . PHE E  1 150 ? 41.562  4.848   48.087  1.00 6.43  ? 150  PHE E N   1 
ATOM   7962 C  CA  . PHE E  1 150 ? 40.617  3.818   47.677  1.00 7.21  ? 150  PHE E CA  1 
ATOM   7963 C  C   . PHE E  1 150 ? 39.616  3.605   48.801  1.00 8.36  ? 150  PHE E C   1 
ATOM   7964 O  O   . PHE E  1 150 ? 39.999  3.295   49.935  1.00 9.05  ? 150  PHE E O   1 
ATOM   7965 C  CB  . PHE E  1 150 ? 41.349  2.506   47.337  1.00 8.51  ? 150  PHE E CB  1 
ATOM   7966 C  CG  . PHE E  1 150 ? 40.417  1.363   47.047  1.00 6.61  ? 150  PHE E CG  1 
ATOM   7967 C  CD1 . PHE E  1 150 ? 39.872  1.197   45.784  1.00 6.60  ? 150  PHE E CD1 1 
ATOM   7968 C  CD2 . PHE E  1 150 ? 40.057  0.486   48.053  1.00 8.45  ? 150  PHE E CD2 1 
ATOM   7969 C  CE1 . PHE E  1 150 ? 38.991  0.148   45.524  1.00 7.44  ? 150  PHE E CE1 1 
ATOM   7970 C  CE2 . PHE E  1 150 ? 39.165  -0.566  47.806  1.00 8.96  ? 150  PHE E CE2 1 
ATOM   7971 C  CZ  . PHE E  1 150 ? 38.640  -0.731  46.537  1.00 8.49  ? 150  PHE E CZ  1 
ATOM   7972 N  N   . VAL E  1 151 ? 38.342  3.821   48.485  1.00 6.22  ? 151  VAL E N   1 
ATOM   7973 C  CA  . VAL E  1 151 ? 37.241  3.581   49.418  1.00 4.36  ? 151  VAL E CA  1 
ATOM   7974 C  C   . VAL E  1 151 ? 36.476  2.400   48.859  1.00 6.59  ? 151  VAL E C   1 
ATOM   7975 O  O   . VAL E  1 151 ? 36.063  2.410   47.703  1.00 8.13  ? 151  VAL E O   1 
ATOM   7976 C  CB  . VAL E  1 151 ? 36.326  4.813   49.556  1.00 6.14  ? 151  VAL E CB  1 
ATOM   7977 C  CG1 . VAL E  1 151 ? 35.204  4.550   50.581  1.00 6.97  ? 151  VAL E CG1 1 
ATOM   7978 C  CG2 . VAL E  1 151 ? 37.156  6.026   50.009  1.00 8.83  ? 151  VAL E CG2 1 
ATOM   7979 N  N   . GLY E  1 152 ? 36.328  1.361   49.666  1.00 8.85  ? 152  GLY E N   1 
ATOM   7980 C  CA  . GLY E  1 152 ? 35.688  0.154   49.186  1.00 7.47  ? 152  GLY E CA  1 
ATOM   7981 C  C   . GLY E  1 152 ? 36.402  -1.077  49.700  1.00 6.25  ? 152  GLY E C   1 
ATOM   7982 O  O   . GLY E  1 152 ? 37.022  -1.049  50.759  1.00 8.31  ? 152  GLY E O   1 
ATOM   7983 N  N   . GLU E  1 153 ? 36.312  -2.162  48.945  1.00 6.67  ? 153  GLU E N   1 
ATOM   7984 C  CA  . GLU E  1 153 ? 36.770  -3.463  49.435  1.00 5.62  ? 153  GLU E CA  1 
ATOM   7985 C  C   . GLU E  1 153 ? 37.781  -4.098  48.485  1.00 6.06  ? 153  GLU E C   1 
ATOM   7986 O  O   . GLU E  1 153 ? 37.618  -4.026  47.266  1.00 6.93  ? 153  GLU E O   1 
ATOM   7987 C  CB  . GLU E  1 153 ? 35.561  -4.382  49.586  1.00 7.68  ? 153  GLU E CB  1 
ATOM   7988 C  CG  . GLU E  1 153 ? 34.436  -3.732  50.399  1.00 6.23  ? 153  GLU E CG  1 
ATOM   7989 C  CD  . GLU E  1 153 ? 33.265  -4.660  50.621  1.00 9.31  ? 153  GLU E CD  1 
ATOM   7990 O  OE1 . GLU E  1 153 ? 33.487  -5.879  50.786  1.00 9.37  ? 153  GLU E OE1 1 
ATOM   7991 O  OE2 . GLU E  1 153 ? 32.121  -4.170  50.637  1.00 8.99  ? 153  GLU E OE2 1 
ATOM   7992 N  N   . ILE E  1 154 ? 38.820  -4.722  49.043  1.00 5.91  ? 154  ILE E N   1 
ATOM   7993 C  CA  . ILE E  1 154 ? 39.807  -5.435  48.230  1.00 5.90  ? 154  ILE E CA  1 
ATOM   7994 C  C   . ILE E  1 154 ? 40.058  -6.821  48.805  1.00 8.10  ? 154  ILE E C   1 
ATOM   7995 O  O   . ILE E  1 154 ? 40.226  -6.976  50.008  1.00 7.76  ? 154  ILE E O   1 
ATOM   7996 C  CB  . ILE E  1 154 ? 41.143  -4.695  48.186  1.00 8.54  ? 154  ILE E CB  1 
ATOM   7997 C  CG1 . ILE E  1 154 ? 41.009  -3.406  47.377  1.00 12.22 ? 154  ILE E CG1 1 
ATOM   7998 C  CG2 . ILE E  1 154 ? 42.242  -5.594  47.583  1.00 11.99 ? 154  ILE E CG2 1 
ATOM   7999 C  CD1 . ILE E  1 154 ? 42.276  -2.526  47.415  1.00 14.44 ? 154  ILE E CD1 1 
ATOM   8000 N  N   . GLY E  1 155 ? 40.098  -7.828  47.945  1.00 8.20  ? 155  GLY E N   1 
ATOM   8001 C  CA  . GLY E  1 155 ? 40.372  -9.172  48.417  1.00 9.97  ? 155  GLY E CA  1 
ATOM   8002 C  C   . GLY E  1 155 ? 41.127  -9.992  47.390  1.00 8.55  ? 155  GLY E C   1 
ATOM   8003 O  O   . GLY E  1 155 ? 41.405  -9.511  46.290  1.00 7.43  ? 155  GLY E O   1 
ATOM   8004 N  N   . ASP E  1 156 ? 41.449  -11.227 47.764  1.00 7.27  ? 156  ASP E N   1 
ATOM   8005 C  CA  . ASP E  1 156 ? 42.088  -12.193 46.862  1.00 8.46  ? 156  ASP E CA  1 
ATOM   8006 C  C   . ASP E  1 156 ? 43.280  -11.629 46.084  1.00 6.79  ? 156  ASP E C   1 
ATOM   8007 O  O   . ASP E  1 156 ? 43.372  -11.784 44.856  1.00 6.54  ? 156  ASP E O   1 
ATOM   8008 C  CB  . ASP E  1 156 ? 41.052  -12.768 45.893  1.00 9.37  ? 156  ASP E CB  1 
ATOM   8009 C  CG  . ASP E  1 156 ? 40.043  -13.648 46.585  1.00 14.22 ? 156  ASP E CG  1 
ATOM   8010 O  OD1 . ASP E  1 156 ? 40.306  -14.084 47.732  1.00 13.26 ? 156  ASP E OD1 1 
ATOM   8011 O  OD2 . ASP E  1 156 ? 38.992  -13.912 45.976  1.00 12.65 ? 156  ASP E OD2 1 
ATOM   8012 N  N   . LEU E  1 157 ? 44.202  -11.003 46.808  1.00 6.03  ? 157  LEU E N   1 
ATOM   8013 C  CA  . LEU E  1 157 ? 45.383  -10.406 46.197  1.00 6.09  ? 157  LEU E CA  1 
ATOM   8014 C  C   . LEU E  1 157 ? 46.582  -11.348 46.170  1.00 7.82  ? 157  LEU E C   1 
ATOM   8015 O  O   . LEU E  1 157 ? 46.929  -11.962 47.183  1.00 7.50  ? 157  LEU E O   1 
ATOM   8016 C  CB  . LEU E  1 157 ? 45.739  -9.099  46.910  1.00 6.79  ? 157  LEU E CB  1 
ATOM   8017 C  CG  . LEU E  1 157 ? 46.813  -8.244  46.238  1.00 8.04  ? 157  LEU E CG  1 
ATOM   8018 C  CD1 . LEU E  1 157 ? 46.526  -6.769  46.479  1.00 9.58  ? 157  LEU E CD1 1 
ATOM   8019 C  CD2 . LEU E  1 157 ? 48.189  -8.626  46.776  1.00 11.70 ? 157  LEU E CD2 1 
ATOM   8020 N  N   . TYR E  1 158 ? 47.205  -11.435 44.997  1.00 5.11  ? 158  TYR E N   1 
ATOM   8021 C  CA  . TYR E  1 158 ? 48.364  -12.296 44.763  1.00 6.61  ? 158  TYR E CA  1 
ATOM   8022 C  C   . TYR E  1 158 ? 49.344  -11.570 43.873  1.00 8.85  ? 158  TYR E C   1 
ATOM   8023 O  O   . TYR E  1 158 ? 48.941  -10.861 42.954  1.00 8.64  ? 158  TYR E O   1 
ATOM   8024 C  CB  . TYR E  1 158 ? 47.941  -13.566 44.026  1.00 4.51  ? 158  TYR E CB  1 
ATOM   8025 C  CG  . TYR E  1 158 ? 46.964  -14.405 44.812  1.00 8.26  ? 158  TYR E CG  1 
ATOM   8026 C  CD1 . TYR E  1 158 ? 47.413  -15.367 45.708  1.00 9.90  ? 158  TYR E CD1 1 
ATOM   8027 C  CD2 . TYR E  1 158 ? 45.600  -14.194 44.696  1.00 7.62  ? 158  TYR E CD2 1 
ATOM   8028 C  CE1 . TYR E  1 158 ? 46.519  -16.125 46.449  1.00 12.11 ? 158  TYR E CE1 1 
ATOM   8029 C  CE2 . TYR E  1 158 ? 44.690  -14.940 45.439  1.00 8.41  ? 158  TYR E CE2 1 
ATOM   8030 C  CZ  . TYR E  1 158 ? 45.160  -15.904 46.311  1.00 8.41  ? 158  TYR E CZ  1 
ATOM   8031 O  OH  . TYR E  1 158 ? 44.242  -16.630 47.032  1.00 9.65  ? 158  TYR E OH  1 
ATOM   8032 N  N   . MET E  1 159 ? 50.629  -11.764 44.131  1.00 6.52  ? 159  MET E N   1 
ATOM   8033 C  CA  . MET E  1 159 ? 51.661  -11.232 43.246  1.00 7.39  ? 159  MET E CA  1 
ATOM   8034 C  C   . MET E  1 159 ? 52.730  -12.290 43.021  1.00 8.27  ? 159  MET E C   1 
ATOM   8035 O  O   . MET E  1 159 ? 53.248  -12.860 43.977  1.00 8.08  ? 159  MET E O   1 
ATOM   8036 C  CB  . MET E  1 159 ? 52.262  -9.945  43.808  1.00 8.29  ? 159  MET E CB  1 
ATOM   8037 C  CG  . MET E  1 159 ? 53.175  -9.216  42.812  1.00 8.05  ? 159  MET E CG  1 
ATOM   8038 S  SD  . MET E  1 159 ? 53.784  -7.679  43.543  1.00 10.76 ? 159  MET E SD  1 
ATOM   8039 C  CE  . MET E  1 159 ? 54.792  -7.048  42.206  1.00 11.97 ? 159  MET E CE  1 
ATOM   8040 N  N   . TRP E  1 160 ? 53.015  -12.556 41.747  1.00 6.73  ? 160  TRP E N   1 
ATOM   8041 C  CA  . TRP E  1 160 ? 53.994  -13.563 41.332  1.00 9.82  ? 160  TRP E CA  1 
ATOM   8042 C  C   . TRP E  1 160 ? 55.170  -12.897 40.629  1.00 8.85  ? 160  TRP E C   1 
ATOM   8043 O  O   . TRP E  1 160 ? 55.007  -11.875 39.964  1.00 9.40  ? 160  TRP E O   1 
ATOM   8044 C  CB  . TRP E  1 160 ? 53.373  -14.533 40.327  1.00 7.59  ? 160  TRP E CB  1 
ATOM   8045 C  CG  . TRP E  1 160 ? 52.189  -15.336 40.786  1.00 8.20  ? 160  TRP E CG  1 
ATOM   8046 C  CD1 . TRP E  1 160 ? 52.204  -16.622 41.233  1.00 11.28 ? 160  TRP E CD1 1 
ATOM   8047 C  CD2 . TRP E  1 160 ? 50.813  -14.932 40.771  1.00 8.11  ? 160  TRP E CD2 1 
ATOM   8048 N  NE1 . TRP E  1 160 ? 50.927  -17.045 41.514  1.00 8.82  ? 160  TRP E NE1 1 
ATOM   8049 C  CE2 . TRP E  1 160 ? 50.052  -16.027 41.237  1.00 7.83  ? 160  TRP E CE2 1 
ATOM   8050 C  CE3 . TRP E  1 160 ? 50.152  -13.751 40.420  1.00 6.66  ? 160  TRP E CE3 1 
ATOM   8051 C  CZ2 . TRP E  1 160 ? 48.664  -15.978 41.360  1.00 7.75  ? 160  TRP E CZ2 1 
ATOM   8052 C  CZ3 . TRP E  1 160 ? 48.769  -13.705 40.535  1.00 8.83  ? 160  TRP E CZ3 1 
ATOM   8053 C  CH2 . TRP E  1 160 ? 48.039  -14.812 41.007  1.00 9.39  ? 160  TRP E CH2 1 
ATOM   8054 N  N   . ASP E  1 161 ? 56.348  -13.503 40.729  1.00 9.09  ? 161  ASP E N   1 
ATOM   8055 C  CA  . ASP E  1 161 ? 57.519  -12.980 40.021  1.00 8.53  ? 161  ASP E CA  1 
ATOM   8056 C  C   . ASP E  1 161 ? 57.666  -13.562 38.610  1.00 9.49  ? 161  ASP E C   1 
ATOM   8057 O  O   . ASP E  1 161 ? 58.778  -13.701 38.103  1.00 13.29 ? 161  ASP E O   1 
ATOM   8058 C  CB  . ASP E  1 161 ? 58.794  -13.216 40.838  1.00 10.73 ? 161  ASP E CB  1 
ATOM   8059 C  CG  . ASP E  1 161 ? 59.241  -14.669 40.838  1.00 14.68 ? 161  ASP E CG  1 
ATOM   8060 O  OD1 . ASP E  1 161 ? 58.461  -15.560 40.434  1.00 14.88 ? 161  ASP E OD1 1 
ATOM   8061 O  OD2 . ASP E  1 161 ? 60.398  -14.912 41.250  1.00 19.94 ? 161  ASP E OD2 1 
ATOM   8062 N  N   . SER E  1 162 ? 56.543  -13.874 37.973  1.00 8.37  ? 162  SER E N   1 
ATOM   8063 C  CA  . SER E  1 162 ? 56.530  -14.321 36.584  1.00 9.52  ? 162  SER E CA  1 
ATOM   8064 C  C   . SER E  1 162 ? 55.306  -13.759 35.865  1.00 11.71 ? 162  SER E C   1 
ATOM   8065 O  O   . SER E  1 162 ? 54.413  -13.201 36.506  1.00 10.81 ? 162  SER E O   1 
ATOM   8066 C  CB  . SER E  1 162 ? 56.523  -15.850 36.509  1.00 10.51 ? 162  SER E CB  1 
ATOM   8067 O  OG  . SER E  1 162 ? 55.359  -16.379 37.122  1.00 14.64 ? 162  SER E OG  1 
ATOM   8068 N  N   . VAL E  1 163 ? 55.276  -13.894 34.541  1.00 9.08  ? 163  VAL E N   1 
ATOM   8069 C  CA  . VAL E  1 163 ? 54.135  -13.473 33.750  1.00 10.39 ? 163  VAL E CA  1 
ATOM   8070 C  C   . VAL E  1 163 ? 53.223  -14.680 33.596  1.00 10.90 ? 163  VAL E C   1 
ATOM   8071 O  O   . VAL E  1 163 ? 53.596  -15.666 32.940  1.00 12.99 ? 163  VAL E O   1 
ATOM   8072 C  CB  . VAL E  1 163 ? 54.561  -12.993 32.355  1.00 13.85 ? 163  VAL E CB  1 
ATOM   8073 C  CG1 . VAL E  1 163 ? 53.337  -12.723 31.481  1.00 12.10 ? 163  VAL E CG1 1 
ATOM   8074 C  CG2 . VAL E  1 163 ? 55.442  -11.750 32.469  1.00 15.30 ? 163  VAL E CG2 1 
ATOM   8075 N  N   . LEU E  1 164 ? 52.046  -14.616 34.211  1.00 9.25  ? 164  LEU E N   1 
ATOM   8076 C  CA  . LEU E  1 164 ? 51.091  -15.724 34.123  1.00 10.75 ? 164  LEU E CA  1 
ATOM   8077 C  C   . LEU E  1 164 ? 50.503  -15.860 32.721  1.00 11.44 ? 164  LEU E C   1 
ATOM   8078 O  O   . LEU E  1 164 ? 50.097  -14.872 32.102  1.00 10.39 ? 164  LEU E O   1 
ATOM   8079 C  CB  . LEU E  1 164 ? 49.958  -15.541 35.145  1.00 9.39  ? 164  LEU E CB  1 
ATOM   8080 C  CG  . LEU E  1 164 ? 50.336  -15.591 36.625  1.00 13.70 ? 164  LEU E CG  1 
ATOM   8081 C  CD1 . LEU E  1 164 ? 49.088  -15.468 37.480  1.00 15.82 ? 164  LEU E CD1 1 
ATOM   8082 C  CD2 . LEU E  1 164 ? 51.075  -16.863 36.957  1.00 18.19 ? 164  LEU E CD2 1 
ATOM   8083 N  N   . PRO E  1 165 ? 50.450  -17.095 32.208  1.00 10.54 ? 165  PRO E N   1 
ATOM   8084 C  CA  . PRO E  1 165 ? 49.728  -17.348 30.959  1.00 12.29 ? 165  PRO E CA  1 
ATOM   8085 C  C   . PRO E  1 165 ? 48.216  -17.278 31.183  1.00 10.00 ? 165  PRO E C   1 
ATOM   8086 O  O   . PRO E  1 165 ? 47.757  -17.297 32.330  1.00 9.86  ? 165  PRO E O   1 
ATOM   8087 C  CB  . PRO E  1 165 ? 50.172  -18.769 30.614  1.00 12.06 ? 165  PRO E CB  1 
ATOM   8088 C  CG  . PRO E  1 165 ? 50.269  -19.410 31.957  1.00 12.88 ? 165  PRO E CG  1 
ATOM   8089 C  CD  . PRO E  1 165 ? 51.025  -18.339 32.755  1.00 11.55 ? 165  PRO E CD  1 
ATOM   8090 N  N   . PRO E  1 166 ? 47.432  -17.189 30.099  1.00 10.77 ? 166  PRO E N   1 
ATOM   8091 C  CA  . PRO E  1 166 ? 45.984  -17.009 30.238  1.00 10.09 ? 166  PRO E CA  1 
ATOM   8092 C  C   . PRO E  1 166 ? 45.292  -18.029 31.146  1.00 9.36  ? 166  PRO E C   1 
ATOM   8093 O  O   . PRO E  1 166 ? 44.405  -17.657 31.899  1.00 10.70 ? 166  PRO E O   1 
ATOM   8094 C  CB  . PRO E  1 166 ? 45.487  -17.127 28.800  1.00 11.08 ? 166  PRO E CB  1 
ATOM   8095 C  CG  . PRO E  1 166 ? 46.613  -16.514 28.010  1.00 9.14  ? 166  PRO E CG  1 
ATOM   8096 C  CD  . PRO E  1 166 ? 47.864  -17.064 28.694  1.00 12.72 ? 166  PRO E CD  1 
ATOM   8097 N  N   A GLU E  1 167 ? 45.689  -19.297 31.082  0.53 9.09  ? 167  GLU E N   1 
ATOM   8098 N  N   B GLU E  1 167 ? 45.710  -19.288 31.068  0.47 9.09  ? 167  GLU E N   1 
ATOM   8099 C  CA  A GLU E  1 167 ? 45.033  -20.304 31.919  0.53 11.92 ? 167  GLU E CA  1 
ATOM   8100 C  CA  B GLU E  1 167 ? 45.102  -20.341 31.876  0.47 11.95 ? 167  GLU E CA  1 
ATOM   8101 C  C   A GLU E  1 167 ? 45.162  -19.962 33.396  0.53 9.41  ? 167  GLU E C   1 
ATOM   8102 C  C   B GLU E  1 167 ? 45.210  -20.049 33.377  0.47 9.42  ? 167  GLU E C   1 
ATOM   8103 O  O   A GLU E  1 167 ? 44.216  -20.146 34.155  0.53 9.15  ? 167  GLU E O   1 
ATOM   8104 O  O   B GLU E  1 167 ? 44.288  -20.338 34.133  0.47 9.17  ? 167  GLU E O   1 
ATOM   8105 C  CB  A GLU E  1 167 ? 45.582  -21.712 31.669  0.53 15.53 ? 167  GLU E CB  1 
ATOM   8106 C  CB  B GLU E  1 167 ? 45.716  -21.706 31.534  0.47 15.24 ? 167  GLU E CB  1 
ATOM   8107 C  CG  A GLU E  1 167 ? 46.015  -21.957 30.261  0.53 20.57 ? 167  GLU E CG  1 
ATOM   8108 C  CG  B GLU E  1 167 ? 47.173  -21.830 31.925  0.47 11.87 ? 167  GLU E CG  1 
ATOM   8109 C  CD  A GLU E  1 167 ? 47.339  -21.292 29.965  0.53 11.76 ? 167  GLU E CD  1 
ATOM   8110 C  CD  B GLU E  1 167 ? 47.899  -22.937 31.195  0.47 22.35 ? 167  GLU E CD  1 
ATOM   8111 O  OE1 A GLU E  1 167 ? 48.322  -21.574 30.678  0.53 24.17 ? 167  GLU E OE1 1 
ATOM   8112 O  OE1 B GLU E  1 167 ? 48.855  -22.628 30.444  0.47 17.51 ? 167  GLU E OE1 1 
ATOM   8113 O  OE2 A GLU E  1 167 ? 47.390  -20.494 29.023  0.53 10.36 ? 167  GLU E OE2 1 
ATOM   8114 O  OE2 B GLU E  1 167 ? 47.519  -24.115 31.376  0.47 29.19 ? 167  GLU E OE2 1 
ATOM   8115 N  N   . ASN E  1 168 ? 46.329  -19.461 33.799  1.00 11.10 ? 168  ASN E N   1 
ATOM   8116 C  CA  . ASN E  1 168 ? 46.550  -19.140 35.210  1.00 9.84  ? 168  ASN E CA  1 
ATOM   8117 C  C   . ASN E  1 168 ? 45.798  -17.880 35.613  1.00 9.09  ? 168  ASN E C   1 
ATOM   8118 O  O   . ASN E  1 168 ? 45.397  -17.735 36.761  1.00 10.12 ? 168  ASN E O   1 
ATOM   8119 C  CB  . ASN E  1 168 ? 48.037  -18.938 35.531  1.00 10.18 ? 168  ASN E CB  1 
ATOM   8120 C  CG  . ASN E  1 168 ? 48.886  -20.202 35.344  1.00 15.44 ? 168  ASN E CG  1 
ATOM   8121 O  OD1 . ASN E  1 168 ? 50.097  -20.099 35.211  1.00 15.16 ? 168  ASN E OD1 1 
ATOM   8122 N  ND2 . ASN E  1 168 ? 48.263  -21.376 35.344  1.00 16.35 ? 168  ASN E ND2 1 
ATOM   8123 N  N   . ILE E  1 169 ? 45.653  -16.947 34.677  1.00 8.70  ? 169  ILE E N   1 
ATOM   8124 C  CA  . ILE E  1 169 ? 44.849  -15.754 34.933  1.00 9.30  ? 169  ILE E CA  1 
ATOM   8125 C  C   . ILE E  1 169 ? 43.392  -16.167 35.166  1.00 8.69  ? 169  ILE E C   1 
ATOM   8126 O  O   . ILE E  1 169 ? 42.749  -15.720 36.125  1.00 9.03  ? 169  ILE E O   1 
ATOM   8127 C  CB  . ILE E  1 169 ? 44.935  -14.765 33.753  1.00 8.87  ? 169  ILE E CB  1 
ATOM   8128 C  CG1 . ILE E  1 169 ? 46.362  -14.224 33.590  1.00 14.74 ? 169  ILE E CG1 1 
ATOM   8129 C  CG2 . ILE E  1 169 ? 43.895  -13.637 33.911  1.00 10.61 ? 169  ILE E CG2 1 
ATOM   8130 C  CD1 . ILE E  1 169 ? 46.840  -13.371 34.750  1.00 19.53 ? 169  ILE E CD1 1 
ATOM   8131 N  N   . LEU E  1 170 ? 42.860  -17.010 34.281  1.00 8.69  ? 170  LEU E N   1 
ATOM   8132 C  CA  . LEU E  1 170 ? 41.483  -17.465 34.419  1.00 10.06 ? 170  LEU E CA  1 
ATOM   8133 C  C   . LEU E  1 170 ? 41.296  -18.254 35.715  1.00 9.54  ? 170  LEU E C   1 
ATOM   8134 O  O   . LEU E  1 170 ? 40.269  -18.131 36.376  1.00 10.92 ? 170  LEU E O   1 
ATOM   8135 C  CB  . LEU E  1 170 ? 41.048  -18.287 33.198  1.00 15.00 ? 170  LEU E CB  1 
ATOM   8136 C  CG  . LEU E  1 170 ? 40.486  -17.468 32.028  1.00 28.48 ? 170  LEU E CG  1 
ATOM   8137 C  CD1 . LEU E  1 170 ? 39.136  -16.858 32.413  1.00 34.95 ? 170  LEU E CD1 1 
ATOM   8138 C  CD2 . LEU E  1 170 ? 41.441  -16.382 31.555  1.00 30.51 ? 170  LEU E CD2 1 
ATOM   8139 N  N   . SER E  1 171 ? 42.299  -19.037 36.094  1.00 11.72 ? 171  SER E N   1 
ATOM   8140 C  CA  . SER E  1 171 ? 42.233  -19.778 37.358  1.00 11.53 ? 171  SER E CA  1 
ATOM   8141 C  C   . SER E  1 171 ? 42.115  -18.828 38.552  1.00 9.97  ? 171  SER E C   1 
ATOM   8142 O  O   . SER E  1 171 ? 41.327  -19.072 39.466  1.00 10.05 ? 171  SER E O   1 
ATOM   8143 C  CB  . SER E  1 171 ? 43.444  -20.697 37.525  1.00 13.31 ? 171  SER E CB  1 
ATOM   8144 O  OG  . SER E  1 171 ? 43.368  -21.787 36.632  1.00 16.05 ? 171  SER E OG  1 
ATOM   8145 N  N   . ALA E  1 172 ? 42.884  -17.743 38.539  1.00 9.36  ? 172  ALA E N   1 
ATOM   8146 C  CA  . ALA E  1 172 ? 42.782  -16.752 39.602  1.00 9.51  ? 172  ALA E CA  1 
ATOM   8147 C  C   . ALA E  1 172 ? 41.375  -16.149 39.626  1.00 9.16  ? 172  ALA E C   1 
ATOM   8148 O  O   . ALA E  1 172 ? 40.758  -16.033 40.683  1.00 9.01  ? 172  ALA E O   1 
ATOM   8149 C  CB  . ALA E  1 172 ? 43.842  -15.665 39.429  1.00 8.85  ? 172  ALA E CB  1 
ATOM   8150 N  N   . TYR E  1 173 ? 40.863  -15.797 38.450  1.00 9.15  ? 173  TYR E N   1 
ATOM   8151 C  CA  . TYR E  1 173 ? 39.565  -15.149 38.334  1.00 9.32  ? 173  TYR E CA  1 
ATOM   8152 C  C   . TYR E  1 173 ? 38.456  -16.063 38.866  1.00 11.93 ? 173  TYR E C   1 
ATOM   8153 O  O   . TYR E  1 173 ? 37.569  -15.632 39.605  1.00 10.75 ? 173  TYR E O   1 
ATOM   8154 C  CB  . TYR E  1 173 ? 39.317  -14.769 36.863  1.00 8.30  ? 173  TYR E CB  1 
ATOM   8155 C  CG  . TYR E  1 173 ? 37.919  -14.290 36.563  1.00 8.99  ? 173  TYR E CG  1 
ATOM   8156 C  CD1 . TYR E  1 173 ? 37.330  -13.297 37.326  1.00 10.60 ? 173  TYR E CD1 1 
ATOM   8157 C  CD2 . TYR E  1 173 ? 37.196  -14.818 35.496  1.00 14.16 ? 173  TYR E CD2 1 
ATOM   8158 C  CE1 . TYR E  1 173 ? 36.048  -12.843 37.054  1.00 12.63 ? 173  TYR E CE1 1 
ATOM   8159 C  CE2 . TYR E  1 173 ? 35.910  -14.366 35.215  1.00 14.91 ? 173  TYR E CE2 1 
ATOM   8160 C  CZ  . TYR E  1 173 ? 35.351  -13.383 35.995  1.00 16.57 ? 173  TYR E CZ  1 
ATOM   8161 O  OH  . TYR E  1 173 ? 34.078  -12.937 35.723  1.00 21.28 ? 173  TYR E OH  1 
ATOM   8162 N  N   . GLN E  1 174 ? 38.537  -17.338 38.513  1.00 12.38 ? 174  GLN E N   1 
ATOM   8163 C  CA  . GLN E  1 174 ? 37.544  -18.321 38.945  1.00 12.45 ? 174  GLN E CA  1 
ATOM   8164 C  C   . GLN E  1 174 ? 37.720  -18.779 40.393  1.00 26.27 ? 174  GLN E C   1 
ATOM   8165 O  O   . GLN E  1 174 ? 36.929  -19.585 40.884  1.00 28.49 ? 174  GLN E O   1 
ATOM   8166 C  CB  . GLN E  1 174 ? 37.575  -19.539 38.018  1.00 26.15 ? 174  GLN E CB  1 
ATOM   8167 C  CG  . GLN E  1 174 ? 37.211  -19.212 36.568  1.00 23.72 ? 174  GLN E CG  1 
ATOM   8168 C  CD  . GLN E  1 174 ? 37.720  -20.258 35.582  1.00 39.36 ? 174  GLN E CD  1 
ATOM   8169 O  OE1 . GLN E  1 174 ? 38.467  -21.169 35.952  1.00 39.62 ? 174  GLN E OE1 1 
ATOM   8170 N  NE2 . GLN E  1 174 ? 37.323  -20.126 34.320  1.00 41.41 ? 174  GLN E NE2 1 
ATOM   8171 N  N   . GLY E  1 175 ? 38.745  -18.275 41.077  1.00 16.54 ? 175  GLY E N   1 
ATOM   8172 C  CA  . GLY E  1 175 ? 38.972  -18.633 42.467  1.00 21.95 ? 175  GLY E CA  1 
ATOM   8173 C  C   . GLY E  1 175 ? 39.900  -19.808 42.755  1.00 19.85 ? 175  GLY E C   1 
ATOM   8174 O  O   . GLY E  1 175 ? 39.911  -20.326 43.880  1.00 20.62 ? 175  GLY E O   1 
ATOM   8175 N  N   . THR E  1 176 ? 40.675  -20.223 41.755  1.00 15.81 ? 176  THR E N   1 
ATOM   8176 C  CA  . THR E  1 176 ? 41.735  -21.239 41.930  1.00 12.88 ? 176  THR E CA  1 
ATOM   8177 C  C   . THR E  1 176 ? 43.144  -20.725 41.576  1.00 10.78 ? 176  THR E C   1 
ATOM   8178 O  O   . THR E  1 176 ? 43.845  -21.305 40.728  1.00 11.58 ? 176  THR E O   1 
ATOM   8179 C  CB  . THR E  1 176 ? 41.456  -22.457 41.076  1.00 16.05 ? 176  THR E CB  1 
ATOM   8180 O  OG1 . THR E  1 176 ? 40.397  -22.157 40.159  1.00 47.11 ? 176  THR E OG1 1 
ATOM   8181 C  CG2 . THR E  1 176 ? 41.040  -23.633 41.975  1.00 28.92 ? 176  THR E CG2 1 
ATOM   8182 N  N   . PRO E  1 177 ? 43.584  -19.658 42.253  1.00 11.04 ? 177  PRO E N   1 
ATOM   8183 C  CA  . PRO E  1 177 ? 44.869  -19.054 41.882  1.00 8.89  ? 177  PRO E CA  1 
ATOM   8184 C  C   . PRO E  1 177 ? 46.056  -19.955 42.199  1.00 8.73  ? 177  PRO E C   1 
ATOM   8185 O  O   . PRO E  1 177 ? 46.048  -20.686 43.188  1.00 9.93  ? 177  PRO E O   1 
ATOM   8186 C  CB  . PRO E  1 177 ? 44.931  -17.803 42.771  1.00 8.61  ? 177  PRO E CB  1 
ATOM   8187 C  CG  . PRO E  1 177 ? 44.048  -18.151 43.954  1.00 14.82 ? 177  PRO E CG  1 
ATOM   8188 C  CD  . PRO E  1 177 ? 42.907  -18.904 43.329  1.00 11.03 ? 177  PRO E CD  1 
ATOM   8189 N  N   . LEU E  1 178 ? 47.088  -19.896 41.368  1.00 9.52  ? 178  LEU E N   1 
ATOM   8190 C  CA  . LEU E  1 178 ? 48.347  -20.544 41.714  1.00 11.41 ? 178  LEU E CA  1 
ATOM   8191 C  C   . LEU E  1 178 ? 48.918  -19.860 42.944  1.00 11.33 ? 178  LEU E C   1 
ATOM   8192 O  O   . LEU E  1 178 ? 48.859  -18.634 43.054  1.00 11.96 ? 178  LEU E O   1 
ATOM   8193 C  CB  . LEU E  1 178 ? 49.348  -20.385 40.572  1.00 11.06 ? 178  LEU E CB  1 
ATOM   8194 C  CG  . LEU E  1 178 ? 49.144  -21.220 39.317  1.00 19.01 ? 178  LEU E CG  1 
ATOM   8195 C  CD1 . LEU E  1 178 ? 50.265  -20.896 38.346  1.00 18.08 ? 178  LEU E CD1 1 
ATOM   8196 C  CD2 . LEU E  1 178 ? 49.134  -22.705 39.660  1.00 25.17 ? 178  LEU E CD2 1 
ATOM   8197 N  N   . PRO E  1 179 ? 49.487  -20.641 43.875  1.00 10.89 ? 179  PRO E N   1 
ATOM   8198 C  CA  . PRO E  1 179 ? 50.208  -20.025 44.993  1.00 8.65  ? 179  PRO E CA  1 
ATOM   8199 C  C   . PRO E  1 179 ? 51.218  -19.014 44.463  1.00 6.70  ? 179  PRO E C   1 
ATOM   8200 O  O   . PRO E  1 179 ? 51.834  -19.241 43.415  1.00 11.31 ? 179  PRO E O   1 
ATOM   8201 C  CB  . PRO E  1 179 ? 50.923  -21.210 45.643  1.00 14.00 ? 179  PRO E CB  1 
ATOM   8202 C  CG  . PRO E  1 179 ? 50.064  -22.382 45.318  1.00 15.48 ? 179  PRO E CG  1 
ATOM   8203 C  CD  . PRO E  1 179 ? 49.510  -22.115 43.939  1.00 13.08 ? 179  PRO E CD  1 
ATOM   8204 N  N   . ALA E  1 180 ? 51.354  -17.902 45.176  1.00 10.37 ? 180  ALA E N   1 
ATOM   8205 C  CA  . ALA E  1 180 ? 52.115  -16.758 44.693  1.00 9.19  ? 180  ALA E CA  1 
ATOM   8206 C  C   . ALA E  1 180 ? 53.306  -16.473 45.597  1.00 9.08  ? 180  ALA E C   1 
ATOM   8207 O  O   . ALA E  1 180 ? 53.214  -16.599 46.820  1.00 12.15 ? 180  ALA E O   1 
ATOM   8208 C  CB  . ALA E  1 180 ? 51.190  -15.515 44.588  1.00 9.81  ? 180  ALA E CB  1 
ATOM   8209 N  N   . ASN E  1 181 ? 54.430  -16.089 45.000  1.00 8.68  ? 181  ASN E N   1 
ATOM   8210 C  CA  . ASN E  1 181 ? 55.664  -16.000 45.766  1.00 13.14 ? 181  ASN E CA  1 
ATOM   8211 C  C   . ASN E  1 181 ? 56.095  -14.614 46.233  1.00 15.87 ? 181  ASN E C   1 
ATOM   8212 O  O   . ASN E  1 181 ? 57.067  -14.486 46.979  1.00 18.03 ? 181  ASN E O   1 
ATOM   8213 C  CB  . ASN E  1 181 ? 56.812  -16.734 45.048  1.00 11.87 ? 181  ASN E CB  1 
ATOM   8214 C  CG  . ASN E  1 181 ? 57.062  -16.225 43.635  1.00 16.85 ? 181  ASN E CG  1 
ATOM   8215 O  OD1 . ASN E  1 181 ? 56.443  -15.259 43.173  1.00 11.28 ? 181  ASN E OD1 1 
ATOM   8216 N  ND2 . ASN E  1 181 ? 57.978  -16.888 42.934  1.00 16.01 ? 181  ASN E ND2 1 
ATOM   8217 N  N   . ILE E  1 182 ? 55.388  -13.572 45.814  1.00 9.60  ? 182  ILE E N   1 
ATOM   8218 C  CA  . ILE E  1 182 ? 55.713  -12.240 46.314  1.00 8.45  ? 182  ILE E CA  1 
ATOM   8219 C  C   . ILE E  1 182 ? 54.688  -11.791 47.357  1.00 11.04 ? 182  ILE E C   1 
ATOM   8220 O  O   . ILE E  1 182 ? 55.048  -11.378 48.460  1.00 11.10 ? 182  ILE E O   1 
ATOM   8221 C  CB  . ILE E  1 182 ? 55.820  -11.206 45.173  1.00 10.57 ? 182  ILE E CB  1 
ATOM   8222 C  CG1 . ILE E  1 182 ? 56.910  -11.630 44.182  1.00 10.71 ? 182  ILE E CG1 1 
ATOM   8223 C  CG2 . ILE E  1 182 ? 56.114  -9.822  45.739  1.00 14.18 ? 182  ILE E CG2 1 
ATOM   8224 C  CD1 . ILE E  1 182 ? 56.982  -10.741 42.931  1.00 12.87 ? 182  ILE E CD1 1 
ATOM   8225 N  N   . LEU E  1 183 ? 53.408  -11.872 46.995  1.00 8.84  ? 183  LEU E N   1 
ATOM   8226 C  CA  . LEU E  1 183 ? 52.305  -11.630 47.913  1.00 9.00  ? 183  LEU E CA  1 
ATOM   8227 C  C   . LEU E  1 183 ? 51.254  -12.720 47.717  1.00 7.62  ? 183  LEU E C   1 
ATOM   8228 O  O   . LEU E  1 183 ? 50.922  -13.092 46.594  1.00 7.45  ? 183  LEU E O   1 
ATOM   8229 C  CB  . LEU E  1 183 ? 51.657  -10.259 47.663  1.00 8.04  ? 183  LEU E CB  1 
ATOM   8230 C  CG  . LEU E  1 183 ? 52.551  -9.038  47.881  1.00 9.13  ? 183  LEU E CG  1 
ATOM   8231 C  CD1 . LEU E  1 183 ? 51.869  -7.780  47.355  1.00 11.01 ? 183  LEU E CD1 1 
ATOM   8232 C  CD2 . LEU E  1 183 ? 52.932  -8.885  49.358  1.00 9.80  ? 183  LEU E CD2 1 
ATOM   8233 N  N   . ASP E  1 184 ? 50.727  -13.242 48.814  1.00 9.05  ? 184  ASP E N   1 
ATOM   8234 C  CA  . ASP E  1 184 ? 49.748  -14.323 48.711  1.00 8.66  ? 184  ASP E CA  1 
ATOM   8235 C  C   . ASP E  1 184 ? 48.688  -14.177 49.805  1.00 8.01  ? 184  ASP E C   1 
ATOM   8236 O  O   . ASP E  1 184 ? 49.014  -14.068 50.991  1.00 9.48  ? 184  ASP E O   1 
ATOM   8237 C  CB  . ASP E  1 184 ? 50.467  -15.684 48.770  1.00 9.15  ? 184  ASP E CB  1 
ATOM   8238 C  CG  . ASP E  1 184 ? 49.525  -16.861 48.580  1.00 12.47 ? 184  ASP E CG  1 
ATOM   8239 O  OD1 . ASP E  1 184 ? 49.710  -17.630 47.619  1.00 11.62 ? 184  ASP E OD1 1 
ATOM   8240 O  OD2 . ASP E  1 184 ? 48.605  -17.028 49.395  1.00 12.82 ? 184  ASP E OD2 1 
ATOM   8241 N  N   . TRP E  1 185 ? 47.420  -14.141 49.385  1.00 7.66  ? 185  TRP E N   1 
ATOM   8242 C  CA  . TRP E  1 185 ? 46.282  -13.875 50.273  1.00 6.35  ? 185  TRP E CA  1 
ATOM   8243 C  C   . TRP E  1 185 ? 46.147  -14.885 51.403  1.00 6.62  ? 185  TRP E C   1 
ATOM   8244 O  O   . TRP E  1 185 ? 45.607  -14.565 52.466  1.00 8.73  ? 185  TRP E O   1 
ATOM   8245 C  CB  . TRP E  1 185 ? 44.975  -13.828 49.457  1.00 8.27  ? 185  TRP E CB  1 
ATOM   8246 C  CG  . TRP E  1 185 ? 43.854  -13.012 50.067  1.00 7.50  ? 185  TRP E CG  1 
ATOM   8247 C  CD1 . TRP E  1 185 ? 42.619  -13.469 50.442  1.00 7.03  ? 185  TRP E CD1 1 
ATOM   8248 C  CD2 . TRP E  1 185 ? 43.856  -11.604 50.347  1.00 6.60  ? 185  TRP E CD2 1 
ATOM   8249 N  NE1 . TRP E  1 185 ? 41.855  -12.436 50.934  1.00 8.45  ? 185  TRP E NE1 1 
ATOM   8250 C  CE2 . TRP E  1 185 ? 42.590  -11.281 50.889  1.00 7.03  ? 185  TRP E CE2 1 
ATOM   8251 C  CE3 . TRP E  1 185 ? 44.802  -10.585 50.189  1.00 6.66  ? 185  TRP E CE3 1 
ATOM   8252 C  CZ2 . TRP E  1 185 ? 42.251  -9.985  51.283  1.00 8.70  ? 185  TRP E CZ2 1 
ATOM   8253 C  CZ3 . TRP E  1 185 ? 44.454  -9.286  50.574  1.00 7.14  ? 185  TRP E CZ3 1 
ATOM   8254 C  CH2 . TRP E  1 185 ? 43.201  -9.004  51.120  1.00 8.08  ? 185  TRP E CH2 1 
ATOM   8255 N  N   . GLN E  1 186 ? 46.636  -16.103 51.173  1.00 8.12  ? 186  GLN E N   1 
ATOM   8256 C  CA  . GLN E  1 186 ? 46.571  -17.163 52.188  1.00 9.93  ? 186  GLN E CA  1 
ATOM   8257 C  C   . GLN E  1 186 ? 47.680  -17.060 53.244  1.00 10.95 ? 186  GLN E C   1 
ATOM   8258 O  O   . GLN E  1 186 ? 47.668  -17.776 54.258  1.00 10.02 ? 186  GLN E O   1 
ATOM   8259 C  CB  . GLN E  1 186 ? 46.612  -18.547 51.519  1.00 6.85  ? 186  GLN E CB  1 
ATOM   8260 C  CG  . GLN E  1 186 ? 45.259  -19.047 51.031  1.00 8.45  ? 186  GLN E CG  1 
ATOM   8261 C  CD  . GLN E  1 186 ? 44.721  -18.222 49.880  1.00 8.53  ? 186  GLN E CD  1 
ATOM   8262 O  OE1 . GLN E  1 186 ? 45.354  -18.129 48.823  1.00 8.98  ? 186  GLN E OE1 1 
ATOM   8263 N  NE2 . GLN E  1 186 ? 43.553  -17.619 50.076  1.00 10.82 ? 186  GLN E NE2 1 
ATOM   8264 N  N   . ALA E  1 187 ? 48.641  -16.173 53.013  1.00 9.45  ? 187  ALA E N   1 
ATOM   8265 C  CA  . ALA E  1 187 ? 49.748  -15.985 53.945  1.00 8.30  ? 187  ALA E CA  1 
ATOM   8266 C  C   . ALA E  1 187 ? 50.292  -14.582 53.800  1.00 10.99 ? 187  ALA E C   1 
ATOM   8267 O  O   . ALA E  1 187 ? 51.438  -14.368 53.370  1.00 11.06 ? 187  ALA E O   1 
ATOM   8268 C  CB  . ALA E  1 187 ? 50.842  -17.016 53.684  1.00 12.17 ? 187  ALA E CB  1 
ATOM   8269 N  N   . LEU E  1 188 ? 49.446  -13.625 54.147  1.00 9.49  ? 188  LEU E N   1 
ATOM   8270 C  CA  . LEU E  1 188 ? 49.752  -12.229 53.916  1.00 9.24  ? 188  LEU E CA  1 
ATOM   8271 C  C   . LEU E  1 188 ? 50.300  -11.583 55.179  1.00 11.21 ? 188  LEU E C   1 
ATOM   8272 O  O   . LEU E  1 188 ? 49.707  -11.688 56.259  1.00 12.39 ? 188  LEU E O   1 
ATOM   8273 C  CB  . LEU E  1 188 ? 48.483  -11.491 53.487  1.00 12.06 ? 188  LEU E CB  1 
ATOM   8274 C  CG  . LEU E  1 188 ? 48.736  -10.135 52.830  1.00 11.01 ? 188  LEU E CG  1 
ATOM   8275 C  CD1 . LEU E  1 188 ? 49.389  -10.333 51.475  1.00 10.66 ? 188  LEU E CD1 1 
ATOM   8276 C  CD2 . LEU E  1 188 ? 47.415  -9.387  52.689  1.00 10.48 ? 188  LEU E CD2 1 
ATOM   8277 N  N   . ASN E  1 189 ? 51.431  -10.906 55.026  1.00 8.83  ? 189  ASN E N   1 
ATOM   8278 C  CA  . ASN E  1 189 ? 52.041  -10.157 56.115  1.00 9.48  ? 189  ASN E CA  1 
ATOM   8279 C  C   . ASN E  1 189 ? 51.667  -8.695  55.927  1.00 12.76 ? 189  ASN E C   1 
ATOM   8280 O  O   . ASN E  1 189 ? 52.135  -8.055  54.990  1.00 15.30 ? 189  ASN E O   1 
ATOM   8281 C  CB  . ASN E  1 189 ? 53.556  -10.309 56.037  1.00 11.77 ? 189  ASN E CB  1 
ATOM   8282 C  CG  . ASN E  1 189 ? 54.265  -9.813  57.280  1.00 16.87 ? 189  ASN E CG  1 
ATOM   8283 O  OD1 . ASN E  1 189 ? 53.634  -9.478  58.283  1.00 20.85 ? 189  ASN E OD1 1 
ATOM   8284 N  ND2 . ASN E  1 189 ? 55.594  -9.756  57.214  1.00 16.06 ? 189  ASN E ND2 1 
ATOM   8285 N  N   . TYR E  1 190 ? 50.804  -8.176  56.791  1.00 11.14 ? 190  TYR E N   1 
ATOM   8286 C  CA  . TYR E  1 190 ? 50.268  -6.832  56.575  1.00 9.76  ? 190  TYR E CA  1 
ATOM   8287 C  C   . TYR E  1 190 ? 50.208  -6.041  57.864  1.00 11.69 ? 190  TYR E C   1 
ATOM   8288 O  O   . TYR E  1 190 ? 50.265  -6.600  58.959  1.00 12.25 ? 190  TYR E O   1 
ATOM   8289 C  CB  . TYR E  1 190 ? 48.870  -6.895  55.956  1.00 11.78 ? 190  TYR E CB  1 
ATOM   8290 C  CG  . TYR E  1 190 ? 47.841  -7.543  56.845  1.00 10.64 ? 190  TYR E CG  1 
ATOM   8291 C  CD1 . TYR E  1 190 ? 47.107  -6.793  57.750  1.00 13.60 ? 190  TYR E CD1 1 
ATOM   8292 C  CD2 . TYR E  1 190 ? 47.601  -8.912  56.779  1.00 13.61 ? 190  TYR E CD2 1 
ATOM   8293 C  CE1 . TYR E  1 190 ? 46.168  -7.386  58.571  1.00 16.26 ? 190  TYR E CE1 1 
ATOM   8294 C  CE2 . TYR E  1 190 ? 46.670  -9.511  57.589  1.00 19.06 ? 190  TYR E CE2 1 
ATOM   8295 C  CZ  . TYR E  1 190 ? 45.957  -8.751  58.484  1.00 18.36 ? 190  TYR E CZ  1 
ATOM   8296 O  OH  . TYR E  1 190 ? 45.025  -9.354  59.293  1.00 22.58 ? 190  TYR E OH  1 
ATOM   8297 N  N   . GLU E  1 191 ? 50.079  -4.728  57.717  1.00 10.72 ? 191  GLU E N   1 
ATOM   8298 C  CA  . GLU E  1 191 ? 49.882  -3.843  58.848  1.00 9.99  ? 191  GLU E CA  1 
ATOM   8299 C  C   . GLU E  1 191 ? 48.730  -2.909  58.517  1.00 9.77  ? 191  GLU E C   1 
ATOM   8300 O  O   . GLU E  1 191 ? 48.804  -2.168  57.539  1.00 12.02 ? 191  GLU E O   1 
ATOM   8301 C  CB  . GLU E  1 191 ? 51.134  -2.995  59.081  1.00 15.21 ? 191  GLU E CB  1 
ATOM   8302 C  CG  . GLU E  1 191 ? 52.384  -3.804  59.376  1.00 23.94 ? 191  GLU E CG  1 
ATOM   8303 C  CD  . GLU E  1 191 ? 53.637  -2.948  59.434  1.00 29.15 ? 191  GLU E CD  1 
ATOM   8304 O  OE1 . GLU E  1 191 ? 53.686  -1.905  58.742  1.00 24.99 ? 191  GLU E OE1 1 
ATOM   8305 O  OE2 . GLU E  1 191 ? 54.575  -3.328  60.169  1.00 32.52 ? 191  GLU E OE2 1 
ATOM   8306 N  N   . ILE E  1 192 ? 47.670  -2.956  59.319  1.00 10.25 ? 192  ILE E N   1 
ATOM   8307 C  CA  . ILE E  1 192 ? 46.581  -1.996  59.188  1.00 7.32  ? 192  ILE E CA  1 
ATOM   8308 C  C   . ILE E  1 192 ? 46.947  -0.704  59.900  1.00 11.43 ? 192  ILE E C   1 
ATOM   8309 O  O   . ILE E  1 192 ? 47.432  -0.725  61.037  1.00 14.12 ? 192  ILE E O   1 
ATOM   8310 C  CB  . ILE E  1 192 ? 45.266  -2.572  59.754  1.00 9.30  ? 192  ILE E CB  1 
ATOM   8311 C  CG1 . ILE E  1 192 ? 44.685  -3.607  58.781  1.00 12.33 ? 192  ILE E CG1 1 
ATOM   8312 C  CG2 . ILE E  1 192 ? 44.259  -1.470  60.036  1.00 12.62 ? 192  ILE E CG2 1 
ATOM   8313 C  CD1 . ILE E  1 192 ? 43.456  -4.343  59.320  1.00 11.76 ? 192  ILE E CD1 1 
ATOM   8314 N  N   . ARG E  1 193 ? 46.726  0.417   59.224  1.00 9.65  ? 193  ARG E N   1 
ATOM   8315 C  CA  . ARG E  1 193 ? 46.909  1.738   59.814  1.00 11.21 ? 193  ARG E CA  1 
ATOM   8316 C  C   . ARG E  1 193 ? 45.623  2.541   59.632  1.00 11.35 ? 193  ARG E C   1 
ATOM   8317 O  O   . ARG E  1 193 ? 45.060  2.612   58.536  1.00 11.42 ? 193  ARG E O   1 
ATOM   8318 C  CB  . ARG E  1 193 ? 48.109  2.456   59.179  1.00 12.10 ? 193  ARG E CB  1 
ATOM   8319 C  CG  . ARG E  1 193 ? 49.447  1.727   59.390  1.00 13.90 ? 193  ARG E CG  1 
ATOM   8320 C  CD  . ARG E  1 193 ? 49.911  1.820   60.838  1.00 22.59 ? 193  ARG E CD  1 
ATOM   8321 N  NE  . ARG E  1 193 ? 51.186  1.130   61.049  1.00 30.01 ? 193  ARG E NE  1 
ATOM   8322 C  CZ  . ARG E  1 193 ? 51.306  -0.071  61.607  1.00 25.38 ? 193  ARG E CZ  1 
ATOM   8323 N  NH1 . ARG E  1 193 ? 50.226  -0.721  62.017  1.00 29.06 ? 193  ARG E NH1 1 
ATOM   8324 N  NH2 . ARG E  1 193 ? 52.504  -0.621  61.758  1.00 28.58 ? 193  ARG E NH2 1 
ATOM   8325 N  N   . GLY E  1 194 ? 45.121  3.116   60.717  1.00 9.90  ? 194  GLY E N   1 
ATOM   8326 C  CA  . GLY E  1 194 ? 43.878  3.856   60.645  1.00 8.10  ? 194  GLY E CA  1 
ATOM   8327 C  C   . GLY E  1 194 ? 42.656  2.950   60.545  1.00 10.19 ? 194  GLY E C   1 
ATOM   8328 O  O   . GLY E  1 194 ? 42.650  1.827   61.060  1.00 11.27 ? 194  GLY E O   1 
ATOM   8329 N  N   . TYR E  1 195 ? 41.624  3.440   59.865  1.00 9.42  ? 195  TYR E N   1 
ATOM   8330 C  CA  . TYR E  1 195 ? 40.323  2.767   59.820  1.00 9.09  ? 195  TYR E CA  1 
ATOM   8331 C  C   . TYR E  1 195 ? 40.241  1.805   58.646  1.00 6.84  ? 195  TYR E C   1 
ATOM   8332 O  O   . TYR E  1 195 ? 39.799  2.183   57.559  1.00 7.91  ? 195  TYR E O   1 
ATOM   8333 C  CB  . TYR E  1 195 ? 39.227  3.824   59.695  1.00 7.81  ? 195  TYR E CB  1 
ATOM   8334 C  CG  . TYR E  1 195 ? 37.798  3.345   59.863  1.00 8.02  ? 195  TYR E CG  1 
ATOM   8335 C  CD1 . TYR E  1 195 ? 37.486  2.264   60.683  1.00 6.96  ? 195  TYR E CD1 1 
ATOM   8336 C  CD2 . TYR E  1 195 ? 36.762  4.018   59.242  1.00 9.20  ? 195  TYR E CD2 1 
ATOM   8337 C  CE1 . TYR E  1 195 ? 36.156  1.851   60.855  1.00 11.03 ? 195  TYR E CE1 1 
ATOM   8338 C  CE2 . TYR E  1 195 ? 35.445  3.622   59.398  1.00 10.89 ? 195  TYR E CE2 1 
ATOM   8339 C  CZ  . TYR E  1 195 ? 35.144  2.543   60.195  1.00 8.67  ? 195  TYR E CZ  1 
ATOM   8340 O  OH  . TYR E  1 195 ? 33.809  2.187   60.340  1.00 9.43  ? 195  TYR E OH  1 
ATOM   8341 N  N   . VAL E  1 196 ? 40.685  0.571   58.867  1.00 6.98  ? 196  VAL E N   1 
ATOM   8342 C  CA  . VAL E  1 196 ? 40.526  -0.498  57.886  1.00 8.68  ? 196  VAL E CA  1 
ATOM   8343 C  C   . VAL E  1 196 ? 39.973  -1.701  58.650  1.00 8.83  ? 196  VAL E C   1 
ATOM   8344 O  O   . VAL E  1 196 ? 40.457  -2.056  59.731  1.00 10.38 ? 196  VAL E O   1 
ATOM   8345 C  CB  . VAL E  1 196 ? 41.852  -0.874  57.178  1.00 6.79  ? 196  VAL E CB  1 
ATOM   8346 C  CG1 . VAL E  1 196 ? 41.591  -1.885  56.042  1.00 8.23  ? 196  VAL E CG1 1 
ATOM   8347 C  CG2 . VAL E  1 196 ? 42.536  0.372   56.632  1.00 9.44  ? 196  VAL E CG2 1 
ATOM   8348 N  N   . ILE E  1 197 ? 38.920  -2.294  58.111  1.00 7.65  ? 197  ILE E N   1 
ATOM   8349 C  CA  . ILE E  1 197 ? 38.238  -3.378  58.803  1.00 6.49  ? 197  ILE E CA  1 
ATOM   8350 C  C   . ILE E  1 197 ? 38.281  -4.637  57.941  1.00 10.39 ? 197  ILE E C   1 
ATOM   8351 O  O   . ILE E  1 197 ? 38.013  -4.596  56.737  1.00 9.73  ? 197  ILE E O   1 
ATOM   8352 C  CB  . ILE E  1 197 ? 36.757  -3.028  59.070  1.00 8.13  ? 197  ILE E CB  1 
ATOM   8353 C  CG1 . ILE E  1 197 ? 36.614  -1.707  59.839  1.00 8.28  ? 197  ILE E CG1 1 
ATOM   8354 C  CG2 . ILE E  1 197 ? 36.046  -4.204  59.790  1.00 9.04  ? 197  ILE E CG2 1 
ATOM   8355 C  CD1 . ILE E  1 197 ? 37.129  -1.752  61.286  1.00 9.56  ? 197  ILE E CD1 1 
ATOM   8356 N  N   . ILE E  1 198 ? 38.619  -5.765  58.552  1.00 8.80  ? 198  ILE E N   1 
ATOM   8357 C  CA  . ILE E  1 198 ? 38.556  -7.024  57.824  1.00 6.54  ? 198  ILE E CA  1 
ATOM   8358 C  C   . ILE E  1 198 ? 37.158  -7.626  57.969  1.00 6.50  ? 198  ILE E C   1 
ATOM   8359 O  O   . ILE E  1 198 ? 36.636  -7.743  59.084  1.00 9.42  ? 198  ILE E O   1 
ATOM   8360 C  CB  . ILE E  1 198 ? 39.623  -8.012  58.315  1.00 7.44  ? 198  ILE E CB  1 
ATOM   8361 C  CG1 . ILE E  1 198 ? 41.023  -7.440  58.057  1.00 10.74 ? 198  ILE E CG1 1 
ATOM   8362 C  CG2 . ILE E  1 198 ? 39.436  -9.368  57.622  1.00 9.99  ? 198  ILE E CG2 1 
ATOM   8363 C  CD1 . ILE E  1 198 ? 42.146  -8.242  58.719  1.00 17.48 ? 198  ILE E CD1 1 
ATOM   8364 N  N   . LYS E  1 199 ? 36.539  -7.974  56.840  1.00 7.42  ? 199  LYS E N   1 
ATOM   8365 C  CA  . LYS E  1 199 ? 35.189  -8.536  56.827  1.00 9.64  ? 199  LYS E CA  1 
ATOM   8366 C  C   . LYS E  1 199 ? 35.125  -9.696  55.849  1.00 7.26  ? 199  LYS E C   1 
ATOM   8367 O  O   . LYS E  1 199 ? 35.964  -9.821  54.966  1.00 9.59  ? 199  LYS E O   1 
ATOM   8368 C  CB  . LYS E  1 199 ? 34.158  -7.482  56.407  1.00 10.27 ? 199  LYS E CB  1 
ATOM   8369 C  CG  . LYS E  1 199 ? 33.815  -6.483  57.492  1.00 9.19  ? 199  LYS E CG  1 
ATOM   8370 C  CD  . LYS E  1 199 ? 32.921  -7.157  58.534  1.00 12.77 ? 199  LYS E CD  1 
ATOM   8371 C  CE  . LYS E  1 199 ? 32.477  -6.190  59.622  1.00 17.72 ? 199  LYS E CE  1 
ATOM   8372 N  NZ  . LYS E  1 199 ? 31.700  -6.918  60.669  1.00 22.35 ? 199  LYS E NZ  1 
ATOM   8373 N  N   . PRO E  1 200 ? 34.115  -10.555 55.998  1.00 7.74  ? 200  PRO E N   1 
ATOM   8374 C  CA  . PRO E  1 200 ? 33.916  -11.609 55.001  1.00 8.14  ? 200  PRO E CA  1 
ATOM   8375 C  C   . PRO E  1 200 ? 33.659  -11.020 53.630  1.00 7.59  ? 200  PRO E C   1 
ATOM   8376 O  O   . PRO E  1 200 ? 33.043  -9.950  53.517  1.00 8.90  ? 200  PRO E O   1 
ATOM   8377 C  CB  . PRO E  1 200 ? 32.642  -12.311 55.490  1.00 9.96  ? 200  PRO E CB  1 
ATOM   8378 C  CG  . PRO E  1 200 ? 32.602  -12.043 56.933  1.00 12.09 ? 200  PRO E CG  1 
ATOM   8379 C  CD  . PRO E  1 200 ? 33.138  -10.645 57.094  1.00 13.34 ? 200  PRO E CD  1 
ATOM   8380 N  N   . LEU E  1 201 ? 34.123  -11.717 52.599  1.00 6.45  ? 201  LEU E N   1 
ATOM   8381 C  CA  . LEU E  1 201 ? 33.823  -11.359 51.212  1.00 6.65  ? 201  LEU E CA  1 
ATOM   8382 C  C   . LEU E  1 201 ? 32.424  -11.859 50.879  1.00 14.30 ? 201  LEU E C   1 
ATOM   8383 O  O   . LEU E  1 201 ? 32.187  -13.073 50.891  1.00 16.56 ? 201  LEU E O   1 
ATOM   8384 C  CB  . LEU E  1 201 ? 34.858  -12.016 50.291  1.00 10.51 ? 201  LEU E CB  1 
ATOM   8385 C  CG  . LEU E  1 201 ? 34.574  -12.064 48.792  1.00 13.92 ? 201  LEU E CG  1 
ATOM   8386 C  CD1 . LEU E  1 201 ? 34.610  -10.666 48.192  1.00 10.26 ? 201  LEU E CD1 1 
ATOM   8387 C  CD2 . LEU E  1 201 ? 35.597  -12.956 48.114  1.00 16.46 ? 201  LEU E CD2 1 
ATOM   8388 N  N   . VAL E  1 202 ? 31.492  -10.946 50.599  1.00 9.54  ? 202  VAL E N   1 
ATOM   8389 C  CA  . VAL E  1 202 ? 30.109  -11.361 50.361  1.00 8.19  ? 202  VAL E CA  1 
ATOM   8390 C  C   . VAL E  1 202 ? 29.647  -11.142 48.921  1.00 9.69  ? 202  VAL E C   1 
ATOM   8391 O  O   . VAL E  1 202 ? 28.526  -11.526 48.566  1.00 11.25 ? 202  VAL E O   1 
ATOM   8392 C  CB  . VAL E  1 202 ? 29.097  -10.655 51.313  1.00 8.65  ? 202  VAL E CB  1 
ATOM   8393 C  CG1 . VAL E  1 202 ? 29.491  -10.872 52.762  1.00 12.06 ? 202  VAL E CG1 1 
ATOM   8394 C  CG2 . VAL E  1 202 ? 29.000  -9.165  50.985  1.00 8.02  ? 202  VAL E CG2 1 
ATOM   8395 N  N   . TRP E  1 203 ? 30.505  -10.538 48.102  1.00 8.17  ? 203  TRP E N   1 
ATOM   8396 C  CA  . TRP E  1 203 ? 30.130  -10.173 46.737  1.00 9.77  ? 203  TRP E CA  1 
ATOM   8397 C  C   . TRP E  1 203 ? 30.735  -11.013 45.618  1.00 17.89 ? 203  TRP E C   1 
ATOM   8398 O  O   . TRP E  1 203 ? 30.322  -10.878 44.473  1.00 23.98 ? 203  TRP E O   1 
ATOM   8399 C  CB  . TRP E  1 203 ? 30.426  -8.693  46.462  1.00 12.60 ? 203  TRP E CB  1 
ATOM   8400 C  CG  . TRP E  1 203 ? 31.713  -8.159  47.042  1.00 9.80  ? 203  TRP E CG  1 
ATOM   8401 C  CD1 . TRP E  1 203 ? 31.882  -7.588  48.269  1.00 9.54  ? 203  TRP E CD1 1 
ATOM   8402 C  CD2 . TRP E  1 203 ? 32.999  -8.102  46.397  1.00 8.14  ? 203  TRP E CD2 1 
ATOM   8403 N  NE1 . TRP E  1 203 ? 33.183  -7.202  48.439  1.00 8.79  ? 203  TRP E NE1 1 
ATOM   8404 C  CE2 . TRP E  1 203 ? 33.891  -7.502  47.303  1.00 9.39  ? 203  TRP E CE2 1 
ATOM   8405 C  CE3 . TRP E  1 203 ? 33.481  -8.518  45.148  1.00 11.61 ? 203  TRP E CE3 1 
ATOM   8406 C  CZ2 . TRP E  1 203 ? 35.239  -7.294  47.003  1.00 9.06  ? 203  TRP E CZ2 1 
ATOM   8407 C  CZ3 . TRP E  1 203 ? 34.820  -8.314  44.850  1.00 11.40 ? 203  TRP E CZ3 1 
ATOM   8408 C  CH2 . TRP E  1 203 ? 35.684  -7.699  45.773  1.00 8.67  ? 203  TRP E CH2 1 
ATOM   8409 N  N   . VAL E  1 204 ? 31.721  -11.847 45.918  1.00 18.19 ? 204  VAL E N   1 
ATOM   8410 C  CA  . VAL E  1 204 ? 32.322  -12.662 44.850  1.00 49.65 ? 204  VAL E CA  1 
ATOM   8411 C  C   . VAL E  1 204 ? 33.246  -13.751 45.386  1.00 49.87 ? 204  VAL E C   1 
ATOM   8412 O  O   . VAL E  1 204 ? 34.400  -13.494 45.720  1.00 52.89 ? 204  VAL E O   1 
ATOM   8413 C  CB  . VAL E  1 204 ? 33.098  -11.800 43.792  1.00 45.92 ? 204  VAL E CB  1 
ATOM   8414 C  CG1 . VAL E  1 204 ? 34.226  -12.601 43.164  1.00 45.70 ? 204  VAL E CG1 1 
ATOM   8415 C  CG2 . VAL E  1 204 ? 32.167  -11.272 42.692  1.00 33.79 ? 204  VAL E CG2 1 
ATOM   8416 O  OXT . VAL E  1 204 ? 32.864  -14.920 45.483  1.00 63.30 ? 204  VAL E OXT 1 
HETATM 8417 CA CA  . CA  F  2 .   ? 15.350  14.687  59.947  1.00 15.07 ? 205  CA  A CA  1 
HETATM 8418 CA CA  . CA  G  2 .   ? 13.450  16.768  57.245  1.00 15.13 ? 206  CA  A CA  1 
HETATM 8419 C  C1  . NAG H  3 .   ? 26.996  -6.741  68.331  1.00 37.23 ? 207  NAG A C1  1 
HETATM 8420 C  C2  . NAG H  3 .   ? 27.543  -7.878  68.450  1.00 46.48 ? 207  NAG A C2  1 
HETATM 8421 C  C3  . NAG H  3 .   ? 28.319  -7.956  69.450  1.00 54.30 ? 207  NAG A C3  1 
HETATM 8422 C  C4  . NAG H  3 .   ? 27.510  -7.946  70.632  1.00 48.82 ? 207  NAG A C4  1 
HETATM 8423 C  C5  . NAG H  3 .   ? 27.017  -6.687  70.783  1.00 47.49 ? 207  NAG A C5  1 
HETATM 8424 C  C6  . NAG H  3 .   ? 25.652  -6.684  71.326  1.00 36.54 ? 207  NAG A C6  1 
HETATM 8425 C  C7  . NAG H  3 .   ? 29.488  -8.093  67.047  1.00 46.08 ? 207  NAG A C7  1 
HETATM 8426 C  C8  . NAG H  3 .   ? 30.183  -9.099  66.105  1.00 54.89 ? 207  NAG A C8  1 
HETATM 8427 N  N2  . NAG H  3 .   ? 28.061  -8.302  67.395  1.00 51.26 ? 207  NAG A N2  1 
HETATM 8428 O  O3  . NAG H  3 .   ? 29.026  -9.174  69.431  1.00 51.69 ? 207  NAG A O3  1 
HETATM 8429 O  O4  . NAG H  3 .   ? 26.520  -8.907  70.552  1.00 64.96 ? 207  NAG A O4  1 
HETATM 8430 O  O5  . NAG H  3 .   ? 27.186  -5.959  69.590  1.00 55.46 ? 207  NAG A O5  1 
HETATM 8431 O  O6  . NAG H  3 .   ? 24.759  -7.432  70.541  1.00 44.12 ? 207  NAG A O6  1 
HETATM 8432 O  O7  . NAG H  3 .   ? 30.066  -7.111  67.369  1.00 45.69 ? 207  NAG A O7  1 
HETATM 8433 N  N   . TPO I  4 .   ? 20.260  15.281  54.562  1.00 21.36 ? 500  TPO A N   1 
HETATM 8434 C  CA  . TPO I  4 .   ? 18.886  15.325  54.040  1.00 20.14 ? 500  TPO A CA  1 
HETATM 8435 C  CB  . TPO I  4 .   ? 17.896  15.161  55.195  1.00 20.39 ? 500  TPO A CB  1 
HETATM 8436 C  CG2 . TPO I  4 .   ? 17.931  13.735  55.749  1.00 16.00 ? 500  TPO A CG2 1 
HETATM 8437 O  OG1 . TPO I  4 .   ? 18.193  16.116  56.218  1.00 15.71 ? 500  TPO A OG1 1 
HETATM 8438 P  P   . TPO I  4 .   ? 17.029  16.621  57.210  1.00 18.75 ? 500  TPO A P   1 
HETATM 8439 O  O1P . TPO I  4 .   ? 16.919  15.526  58.397  1.00 15.86 ? 500  TPO A O1P 1 
HETATM 8440 O  O2P . TPO I  4 .   ? 15.724  16.844  56.538  1.00 16.12 ? 500  TPO A O2P 1 
HETATM 8441 O  O3P . TPO I  4 .   ? 17.578  17.965  57.926  1.00 19.74 ? 500  TPO A O3P 1 
HETATM 8442 C  C   . TPO I  4 .   ? 18.645  16.668  53.348  1.00 25.27 ? 500  TPO A C   1 
HETATM 8443 O  O   . TPO I  4 .   ? 19.449  17.591  53.604  1.00 21.04 ? 500  TPO A O   1 
HETATM 8444 O  OXT . TPO I  4 .   ? 17.688  16.750  52.589  1.00 21.03 ? 500  TPO A OXT 1 
HETATM 8445 CA CA  . CA  J  2 .   ? -9.848  19.091  26.720  1.00 8.85  ? 205  CA  B CA  1 
HETATM 8446 CA CA  . CA  K  2 .   ? -11.876 17.522  29.609  1.00 8.35  ? 206  CA  B CA  1 
HETATM 8447 C  C1  . NAG L  3 .   ? -17.404 -1.595  46.139  1.00 33.47 ? 207  NAG B C1  1 
HETATM 8448 C  C2  . NAG L  3 .   ? -18.409 -1.631  46.921  1.00 38.29 ? 207  NAG B C2  1 
HETATM 8449 C  C3  . NAG L  3 .   ? -18.786 -2.795  47.255  1.00 54.18 ? 207  NAG B C3  1 
HETATM 8450 C  C4  . NAG L  3 .   ? -17.746 -3.448  47.994  1.00 50.23 ? 207  NAG B C4  1 
HETATM 8451 C  C5  . NAG L  3 .   ? -16.723 -3.630  47.123  1.00 53.58 ? 207  NAG B C5  1 
HETATM 8452 C  C6  . NAG L  3 .   ? -15.675 -4.440  47.743  1.00 47.02 ? 207  NAG B C6  1 
HETATM 8453 C  C7  . NAG L  3 .   ? -20.515 -1.257  45.718  1.00 44.32 ? 207  NAG B C7  1 
HETATM 8454 C  C8  . NAG L  3 .   ? -20.625 -2.584  44.927  1.00 38.84 ? 207  NAG B C8  1 
HETATM 8455 N  N2  . NAG L  3 .   ? -19.346 -0.881  46.555  1.00 42.44 ? 207  NAG B N2  1 
HETATM 8456 O  O3  . NAG L  3 .   ? -19.930 -2.719  48.075  1.00 52.05 ? 207  NAG B O3  1 
HETATM 8457 O  O4  . NAG L  3 .   ? -17.374 -2.699  49.095  1.00 56.42 ? 207  NAG B O4  1 
HETATM 8458 O  O5  . NAG L  3 .   ? -16.279 -2.355  46.756  1.00 40.35 ? 207  NAG B O5  1 
HETATM 8459 O  O6  . NAG L  3 .   ? -14.538 -3.648  47.962  1.00 61.14 ? 207  NAG B O6  1 
HETATM 8460 O  O7  . NAG L  3 .   ? -21.332 -0.431  45.519  1.00 51.48 ? 207  NAG B O7  1 
HETATM 8461 N  N   . TPO M  4 .   ? -5.159  18.065  32.384  1.00 24.57 ? 500  TPO B N   1 
HETATM 8462 C  CA  . TPO M  4 .   ? -5.110  18.016  30.915  1.00 23.46 ? 500  TPO B CA  1 
HETATM 8463 C  CB  . TPO M  4 .   ? -6.524  17.827  30.363  1.00 13.81 ? 500  TPO B CB  1 
HETATM 8464 C  CG2 . TPO M  4 .   ? -7.076  16.448  30.729  1.00 16.04 ? 500  TPO B CG2 1 
HETATM 8465 O  OG1 . TPO M  4 .   ? -7.373  18.866  30.857  1.00 14.79 ? 500  TPO B OG1 1 
HETATM 8466 P  P   . TPO M  4 .   ? -8.664  19.322  30.009  1.00 14.74 ? 500  TPO B P   1 
HETATM 8467 O  O1P . TPO M  4 .   ? -9.867  18.317  30.413  1.00 11.30 ? 500  TPO B O1P 1 
HETATM 8468 O  O2P . TPO M  4 .   ? -8.437  19.354  28.543  1.00 13.07 ? 500  TPO B O2P 1 
HETATM 8469 O  O3P . TPO M  4 .   ? -9.113  20.768  30.583  1.00 18.25 ? 500  TPO B O3P 1 
HETATM 8470 C  C   . TPO M  4 .   ? -4.524  19.324  30.380  1.00 26.13 ? 500  TPO B C   1 
HETATM 8471 O  O   . TPO M  4 .   ? -4.465  20.287  31.176  1.00 29.31 ? 500  TPO B O   1 
HETATM 8472 O  OXT . TPO M  4 .   ? -4.142  19.346  29.233  1.00 20.82 ? 500  TPO B OXT 1 
HETATM 8473 CA CA  . CA  N  2 .   ? 8.551   14.234  -5.673  1.00 9.55  ? 205  CA  C CA  1 
HETATM 8474 CA CA  . CA  O  2 .   ? 12.085  15.670  -4.895  1.00 12.06 ? 206  CA  C CA  1 
HETATM 8475 C  C1  . NAG P  3 .   ? -10.225 -3.309  -3.494  1.00 26.30 ? 207  NAG C C1  1 
HETATM 8476 C  C2  . NAG P  3 .   ? -11.207 -3.436  -4.290  1.00 34.83 ? 207  NAG C C2  1 
HETATM 8477 C  C3  . NAG P  3 .   ? -11.855 -4.518  -4.141  1.00 41.05 ? 207  NAG C C3  1 
HETATM 8478 C  C4  . NAG P  3 .   ? -12.499 -4.535  -2.852  1.00 38.84 ? 207  NAG C C4  1 
HETATM 8479 C  C5  . NAG P  3 .   ? -11.578 -4.436  -1.854  1.00 49.97 ? 207  NAG C C5  1 
HETATM 8480 C  C6  . NAG P  3 .   ? -12.281 -4.256  -0.583  1.00 44.00 ? 207  NAG C C6  1 
HETATM 8481 C  C7  . NAG P  3 .   ? -10.447 -3.902  -6.618  1.00 37.97 ? 207  NAG C C7  1 
HETATM 8482 C  C8  . NAG P  3 .   ? -10.120 -5.411  -6.533  1.00 28.51 ? 207  NAG C C8  1 
HETATM 8483 N  N2  . NAG P  3 .   ? -10.939 -3.088  -5.475  1.00 27.74 ? 207  NAG C N2  1 
HETATM 8484 O  O3  . NAG P  3 .   ? -12.880 -4.631  -5.106  1.00 34.36 ? 207  NAG C O3  1 
HETATM 8485 O  O4  . NAG P  3 .   ? -13.476 -3.559  -2.739  1.00 53.84 ? 207  NAG C O4  1 
HETATM 8486 O  O5  . NAG P  3 .   ? -10.715 -3.360  -2.088  1.00 30.79 ? 207  NAG C O5  1 
HETATM 8487 O  O6  . NAG P  3 .   ? -11.469 -4.693  0.474   1.00 49.51 ? 207  NAG C O6  1 
HETATM 8488 O  O7  . NAG P  3 .   ? -10.253 -3.351  -7.647  1.00 43.90 ? 207  NAG C O7  1 
HETATM 8489 N  N   . TPO Q  4 .   ? 8.122   15.810  1.413   1.00 20.25 ? 500  TPO C N   1 
HETATM 8490 C  CA  . TPO Q  4 .   ? 9.512   15.576  0.995   1.00 25.30 ? 500  TPO C CA  1 
HETATM 8491 C  CB  . TPO Q  4 .   ? 9.541   15.181  -0.483  1.00 23.82 ? 500  TPO C CB  1 
HETATM 8492 C  CG2 . TPO Q  4 .   ? 8.898   13.809  -0.696  1.00 17.40 ? 500  TPO C CG2 1 
HETATM 8493 O  OG1 . TPO Q  4 .   ? 8.879   16.183  -1.258  1.00 16.31 ? 500  TPO C OG1 1 
HETATM 8494 P  P   . TPO Q  4 .   ? 9.333   16.454  -2.779  1.00 15.75 ? 500  TPO C P   1 
HETATM 8495 O  O1P . TPO Q  4 .   ? 8.462   15.456  -3.711  1.00 12.73 ? 500  TPO C O1P 1 
HETATM 8496 O  O2P . TPO Q  4 .   ? 10.791  16.294  -3.007  1.00 13.37 ? 500  TPO C O2P 1 
HETATM 8497 O  O3P . TPO Q  4 .   ? 8.821   17.941  -3.162  1.00 16.64 ? 500  TPO C O3P 1 
HETATM 8498 C  C   . TPO Q  4 .   ? 10.328  16.854  1.198   1.00 26.17 ? 500  TPO C C   1 
HETATM 8499 O  O   . TPO Q  4 .   ? 9.690   17.918  1.343   1.00 29.46 ? 500  TPO C O   1 
HETATM 8500 O  OXT . TPO Q  4 .   ? 11.550  16.766  1.225   1.00 26.26 ? 500  TPO C OXT 1 
HETATM 8501 CA CA  . CA  R  2 .   ? 48.971  10.423  6.199   1.00 11.48 ? 205  CA  D CA  1 
HETATM 8502 CA CA  . CA  S  2 .   ? 48.436  8.523   2.837   1.00 9.99  ? 206  CA  D CA  1 
HETATM 8503 C  C1  . NAG T  3 .   ? 38.715  -10.165 -11.677 1.00 23.96 ? 207  NAG D C1  1 
HETATM 8504 C  C2  . NAG T  3 .   ? 39.115  -10.609 -12.803 1.00 26.76 ? 207  NAG D C2  1 
HETATM 8505 C  C3  . NAG T  3 .   ? 38.629  -11.735 -13.132 1.00 41.13 ? 207  NAG D C3  1 
HETATM 8506 C  C4  . NAG T  3 .   ? 37.221  -11.566 -13.377 1.00 34.80 ? 207  NAG D C4  1 
HETATM 8507 C  C5  . NAG T  3 .   ? 36.589  -11.186 -12.229 1.00 46.77 ? 207  NAG D C5  1 
HETATM 8508 C  C6  . NAG T  3 .   ? 35.193  -10.866 -12.525 1.00 41.04 ? 207  NAG D C6  1 
HETATM 8509 C  C7  . NAG T  3 .   ? 41.435  -11.442 -12.741 1.00 32.09 ? 207  NAG D C7  1 
HETATM 8510 C  C8  . NAG T  3 .   ? 42.888  -11.027 -13.052 1.00 35.27 ? 207  NAG D C8  1 
HETATM 8511 N  N2  . NAG T  3 .   ? 40.353  -10.463 -12.991 1.00 24.48 ? 207  NAG D N2  1 
HETATM 8512 O  O3  . NAG T  3 .   ? 39.194  -12.202 -14.345 1.00 33.70 ? 207  NAG D O3  1 
HETATM 8513 O  O4  . NAG T  3 .   ? 36.986  -10.687 -14.419 1.00 46.46 ? 207  NAG D O4  1 
HETATM 8514 O  O5  . NAG T  3 .   ? 37.225  -10.087 -11.635 1.00 24.39 ? 207  NAG D O5  1 
HETATM 8515 O  O6  . NAG T  3 .   ? 34.365  -11.526 -11.605 1.00 47.34 ? 207  NAG D O6  1 
HETATM 8516 O  O7  . NAG T  3 .   ? 41.240  -12.482 -12.221 1.00 37.79 ? 207  NAG D O7  1 
HETATM 8517 N  N   . TPO U  4 .   ? 41.728  11.135  4.445   1.00 32.86 ? 500  TPO D N   1 
HETATM 8518 C  CA  . TPO U  4 .   ? 42.495  10.955  5.686   1.00 30.42 ? 500  TPO D CA  1 
HETATM 8519 C  CB  . TPO U  4 .   ? 43.848  10.318  5.362   1.00 22.14 ? 500  TPO D CB  1 
HETATM 8520 C  CG2 . TPO U  4 .   ? 43.679  8.861   4.927   1.00 23.59 ? 500  TPO D CG2 1 
HETATM 8521 O  OG1 . TPO U  4 .   ? 44.505  11.082  4.348   1.00 25.02 ? 500  TPO D OG1 1 
HETATM 8522 P  P   . TPO U  4 .   ? 46.112  11.075  4.248   1.00 28.41 ? 500  TPO D P   1 
HETATM 8523 O  O1P . TPO U  4 .   ? 46.517  9.804   3.330   1.00 13.64 ? 500  TPO D O1P 1 
HETATM 8524 O  O2P . TPO U  4 .   ? 46.794  11.047  5.566   1.00 19.30 ? 500  TPO D O2P 1 
HETATM 8525 O  O3P . TPO U  4 .   ? 46.532  12.373  3.377   1.00 33.74 ? 500  TPO D O3P 1 
HETATM 8526 C  C   . TPO U  4 .   ? 42.716  12.315  6.351   1.00 40.89 ? 500  TPO D C   1 
HETATM 8527 O  O   . TPO U  4 .   ? 42.495  13.329  5.655   1.00 41.45 ? 500  TPO D O   1 
HETATM 8528 O  OXT . TPO U  4 .   ? 43.091  12.329  7.528   1.00 37.67 ? 500  TPO D OXT 1 
HETATM 8529 CA CA  . CA  V  2 .   ? 52.752  8.691   43.504  1.00 8.18  ? 205  CA  E CA  1 
HETATM 8530 CA CA  . CA  W  2 .   ? 49.924  11.054  44.675  1.00 8.91  ? 206  CA  E CA  1 
HETATM 8531 C  C1  . NAG X  3 .   ? 60.487  -13.531 32.471  1.00 40.72 ? 207  NAG E C1  1 
HETATM 8532 C  C2  . NAG X  3 .   ? 61.511  -13.818 31.800  1.00 42.06 ? 207  NAG E C2  1 
HETATM 8533 C  C3  . NAG X  3 .   ? 61.426  -14.988 31.332  1.00 48.01 ? 207  NAG E C3  1 
HETATM 8534 C  C4  . NAG X  3 .   ? 60.416  -14.982 30.300  1.00 48.47 ? 207  NAG E C4  1 
HETATM 8535 C  C5  . NAG X  3 .   ? 59.210  -14.755 30.893  1.00 55.55 ? 207  NAG E C5  1 
HETATM 8536 C  C6  . NAG X  3 .   ? 58.123  -14.771 29.907  1.00 40.64 ? 207  NAG E C6  1 
HETATM 8537 C  C7  . NAG X  3 .   ? 62.809  -14.130 33.799  1.00 45.25 ? 207  NAG E C7  1 
HETATM 8538 C  C8  . NAG X  3 .   ? 63.920  -13.499 34.662  1.00 31.33 ? 207  NAG E C8  1 
HETATM 8539 N  N2  . NAG X  3 .   ? 62.567  -13.607 32.435  1.00 43.28 ? 207  NAG E N2  1 
HETATM 8540 O  O3  . NAG X  3 .   ? 62.670  -15.362 30.789  1.00 49.70 ? 207  NAG E O3  1 
HETATM 8541 O  O4  . NAG X  3 .   ? 60.673  -14.030 29.327  1.00 60.48 ? 207  NAG E O4  1 
HETATM 8542 O  O5  . NAG X  3 .   ? 59.282  -13.534 31.583  1.00 37.62 ? 207  NAG E O5  1 
HETATM 8543 O  O6  . NAG X  3 .   ? 57.035  -15.526 30.383  1.00 52.48 ? 207  NAG E O6  1 
HETATM 8544 O  O7  . NAG X  3 .   ? 62.186  -15.037 34.232  1.00 45.38 ? 207  NAG E O7  1 
HETATM 8545 N  N   . TPO Y  4 .   ? 49.198  10.300  37.334  1.00 20.96 ? 500  TPO E N   1 
HETATM 8546 C  CA  . TPO Y  4 .   ? 48.342  10.519  38.509  1.00 24.27 ? 500  TPO E CA  1 
HETATM 8547 C  CB  . TPO Y  4 .   ? 49.091  10.091  39.773  1.00 18.02 ? 500  TPO E CB  1 
HETATM 8548 C  CG2 . TPO Y  4 .   ? 49.353  8.584   39.770  1.00 18.78 ? 500  TPO E CG2 1 
HETATM 8549 O  OG1 . TPO Y  4 .   ? 50.314  10.824  39.875  1.00 14.24 ? 500  TPO E OG1 1 
HETATM 8550 P  P   . TPO Y  4 .   ? 50.962  11.112  41.320  1.00 15.56 ? 500  TPO E P   1 
HETATM 8551 O  O1P . TPO Y  4 .   ? 51.858  9.817   41.698  1.00 11.16 ? 500  TPO E O1P 1 
HETATM 8552 O  O2P . TPO Y  4 .   ? 49.963  11.421  42.374  1.00 12.32 ? 500  TPO E O2P 1 
HETATM 8553 O  O3P . TPO Y  4 .   ? 52.026  12.317  41.124  1.00 17.54 ? 500  TPO E O3P 1 
HETATM 8554 C  C   . TPO Y  4 .   ? 47.980  12.003  38.608  1.00 27.05 ? 500  TPO E C   1 
HETATM 8555 O  O   . TPO Y  4 .   ? 48.721  12.809  38.004  1.00 24.87 ? 500  TPO E O   1 
HETATM 8556 O  OXT . TPO Y  4 .   ? 46.986  12.306  39.267  1.00 29.34 ? 500  TPO E OXT 1 
HETATM 8557 O  O   . HOH Z  5 .   ? -4.883  -5.877  57.905  1.00 38.24 ? 2001 HOH A O   1 
HETATM 8558 O  O   . HOH Z  5 .   ? -1.842  -14.842 60.776  1.00 19.64 ? 2002 HOH A O   1 
HETATM 8559 O  O   . HOH Z  5 .   ? -3.425  -10.408 62.442  1.00 23.49 ? 2003 HOH A O   1 
HETATM 8560 O  O   . HOH Z  5 .   ? -4.288  -8.507  58.701  1.00 38.62 ? 2004 HOH A O   1 
HETATM 8561 O  O   . HOH Z  5 .   ? 2.537   -15.356 60.015  1.00 14.07 ? 2005 HOH A O   1 
HETATM 8562 O  O   . HOH Z  5 .   ? -3.682  14.145  46.749  1.00 28.93 ? 2006 HOH A O   1 
HETATM 8563 O  O   . HOH Z  5 .   ? 4.978   -12.953 55.269  1.00 31.29 ? 2007 HOH A O   1 
HETATM 8564 O  O   . HOH Z  5 .   ? 2.830   -15.815 56.606  1.00 32.25 ? 2008 HOH A O   1 
HETATM 8565 O  O   . HOH Z  5 .   ? -2.102  -11.061 56.601  1.00 17.64 ? 2009 HOH A O   1 
HETATM 8566 O  O   . HOH Z  5 .   ? -2.836  -11.371 53.117  1.00 32.78 ? 2010 HOH A O   1 
HETATM 8567 O  O   . HOH Z  5 .   ? 3.176   11.824  44.185  1.00 15.83 ? 2011 HOH A O   1 
HETATM 8568 O  O   . HOH Z  5 .   ? 8.972   18.579  46.155  1.00 36.18 ? 2012 HOH A O   1 
HETATM 8569 O  O   . HOH Z  5 .   ? -1.406  19.687  55.811  1.00 36.64 ? 2013 HOH A O   1 
HETATM 8570 O  O   . HOH Z  5 .   ? -1.524  -10.865 48.792  1.00 37.15 ? 2014 HOH A O   1 
HETATM 8571 O  O   . HOH Z  5 .   ? -6.415  -5.621  55.328  1.00 32.83 ? 2015 HOH A O   1 
HETATM 8572 O  O   . HOH Z  5 .   ? -5.809  -5.860  52.465  1.00 32.27 ? 2016 HOH A O   1 
HETATM 8573 O  O   . HOH Z  5 .   ? -1.334  10.651  44.345  1.00 15.78 ? 2017 HOH A O   1 
HETATM 8574 O  O   . HOH Z  5 .   ? 19.488  -2.453  34.800  1.00 36.67 ? 2018 HOH A O   1 
HETATM 8575 O  O   . HOH Z  5 .   ? 8.030   -5.902  35.695  1.00 47.98 ? 2019 HOH A O   1 
HETATM 8576 O  O   . HOH Z  5 .   ? -5.424  13.651  56.559  1.00 37.06 ? 2020 HOH A O   1 
HETATM 8577 O  O   . HOH Z  5 .   ? -5.691  14.459  48.426  1.00 31.04 ? 2021 HOH A O   1 
HETATM 8578 O  O   . HOH Z  5 .   ? -1.910  16.168  50.658  1.00 31.81 ? 2022 HOH A O   1 
HETATM 8579 O  O   . HOH Z  5 .   ? 7.305   16.601  44.824  1.00 35.60 ? 2023 HOH A O   1 
HETATM 8580 O  O   . HOH Z  5 .   ? 6.804   19.458  47.988  1.00 47.57 ? 2024 HOH A O   1 
HETATM 8581 O  O   . HOH Z  5 .   ? 0.677   12.726  45.093  1.00 19.79 ? 2025 HOH A O   1 
HETATM 8582 O  O   . HOH Z  5 .   ? 4.737   14.018  43.863  1.00 28.96 ? 2026 HOH A O   1 
HETATM 8583 O  O   . HOH Z  5 .   ? -1.142  15.347  47.165  1.00 29.42 ? 2027 HOH A O   1 
HETATM 8584 O  O   . HOH Z  5 .   ? 25.019  -8.622  41.068  1.00 37.03 ? 2028 HOH A O   1 
HETATM 8585 O  O   . HOH Z  5 .   ? 2.307   11.644  52.091  1.00 14.33 ? 2029 HOH A O   1 
HETATM 8586 O  O   . HOH Z  5 .   ? 6.772   12.545  40.869  1.00 29.31 ? 2030 HOH A O   1 
HETATM 8587 O  O   . HOH Z  5 .   ? -0.542  17.626  53.569  1.00 23.27 ? 2031 HOH A O   1 
HETATM 8588 O  O   . HOH Z  5 .   ? 2.217   17.105  59.677  1.00 33.09 ? 2032 HOH A O   1 
HETATM 8589 O  O   . HOH Z  5 .   ? -1.897  13.122  60.372  1.00 27.00 ? 2033 HOH A O   1 
HETATM 8590 O  O   . HOH Z  5 .   ? -2.674  16.132  53.277  1.00 31.26 ? 2034 HOH A O   1 
HETATM 8591 O  O   . HOH Z  5 .   ? -0.201  9.092   51.511  1.00 15.72 ? 2035 HOH A O   1 
HETATM 8592 O  O   . HOH Z  5 .   ? 1.936   10.823  65.039  1.00 20.75 ? 2036 HOH A O   1 
HETATM 8593 O  O   . HOH Z  5 .   ? 20.156  11.763  74.370  1.00 42.24 ? 2037 HOH A O   1 
HETATM 8594 O  O   . HOH Z  5 .   ? 28.271  8.870   72.051  1.00 35.27 ? 2038 HOH A O   1 
HETATM 8595 O  O   . HOH Z  5 .   ? 25.270  14.693  66.724  1.00 43.11 ? 2039 HOH A O   1 
HETATM 8596 O  O   . HOH Z  5 .   ? 5.952   7.370   66.170  1.00 36.64 ? 2040 HOH A O   1 
HETATM 8597 O  O   . HOH Z  5 .   ? 5.174   10.030  65.369  1.00 30.75 ? 2041 HOH A O   1 
HETATM 8598 O  O   . HOH Z  5 .   ? 6.938   5.088   67.051  1.00 21.44 ? 2042 HOH A O   1 
HETATM 8599 O  O   . HOH Z  5 .   ? 5.646   -3.507  65.952  1.00 22.52 ? 2043 HOH A O   1 
HETATM 8600 O  O   . HOH Z  5 .   ? 5.414   -3.769  69.683  1.00 33.19 ? 2044 HOH A O   1 
HETATM 8601 O  O   . HOH Z  5 .   ? 10.351  2.536   72.525  1.00 43.77 ? 2045 HOH A O   1 
HETATM 8602 O  O   . HOH Z  5 .   ? 6.798   1.648   72.946  1.00 45.20 ? 2046 HOH A O   1 
HETATM 8603 O  O   . HOH Z  5 .   ? 7.874   2.435   69.955  1.00 40.69 ? 2047 HOH A O   1 
HETATM 8604 O  O   . HOH Z  5 .   ? 22.442  -3.537  71.614  1.00 29.82 ? 2048 HOH A O   1 
HETATM 8605 O  O   . HOH Z  5 .   ? 33.231  8.932   63.967  1.00 33.71 ? 2049 HOH A O   1 
HETATM 8606 O  O   . HOH Z  5 .   ? 33.049  9.222   59.384  1.00 29.35 ? 2050 HOH A O   1 
HETATM 8607 O  O   . HOH Z  5 .   ? 32.004  8.456   54.971  1.00 22.12 ? 2051 HOH A O   1 
HETATM 8608 O  O   . HOH Z  5 .   ? 30.725  11.577  52.594  1.00 32.47 ? 2052 HOH A O   1 
HETATM 8609 O  O   . HOH Z  5 .   ? 22.950  -1.654  74.827  1.00 41.03 ? 2053 HOH A O   1 
HETATM 8610 O  O   . HOH Z  5 .   ? 27.734  9.574   47.101  1.00 24.64 ? 2054 HOH A O   1 
HETATM 8611 O  O   . HOH Z  5 .   ? 28.977  9.627   49.425  1.00 34.59 ? 2055 HOH A O   1 
HETATM 8612 O  O   . HOH Z  5 .   ? 17.815  -4.020  39.320  1.00 30.86 ? 2056 HOH A O   1 
HETATM 8613 O  O   . HOH Z  5 .   ? 19.081  -3.520  37.102  1.00 37.06 ? 2057 HOH A O   1 
HETATM 8614 O  O   . HOH Z  5 .   ? 29.046  -3.915  70.321  1.00 35.06 ? 2058 HOH A O   1 
HETATM 8615 O  O   . HOH Z  5 .   ? 28.708  -4.107  74.668  1.00 50.44 ? 2059 HOH A O   1 
HETATM 8616 O  O   . HOH Z  5 .   ? 12.580  7.613   33.398  1.00 29.65 ? 2060 HOH A O   1 
HETATM 8617 O  O   . HOH Z  5 .   ? 7.547   -3.563  37.731  1.00 35.74 ? 2061 HOH A O   1 
HETATM 8618 O  O   . HOH Z  5 .   ? 28.900  -4.048  67.615  1.00 14.53 ? 2062 HOH A O   1 
HETATM 8619 O  O   . HOH Z  5 .   ? 21.953  -4.558  69.249  1.00 20.32 ? 2063 HOH A O   1 
HETATM 8620 O  O   . HOH Z  5 .   ? 10.124  -6.359  40.323  1.00 39.08 ? 2064 HOH A O   1 
HETATM 8621 O  O   . HOH Z  5 .   ? 35.312  2.189   68.925  1.00 34.79 ? 2065 HOH A O   1 
HETATM 8622 O  O   . HOH Z  5 .   ? 10.396  -6.579  45.812  1.00 32.11 ? 2066 HOH A O   1 
HETATM 8623 O  O   . HOH Z  5 .   ? 28.889  -11.270 56.356  1.00 26.59 ? 2067 HOH A O   1 
HETATM 8624 O  O   . HOH Z  5 .   ? 24.751  -14.216 49.008  1.00 33.99 ? 2068 HOH A O   1 
HETATM 8625 O  O   . HOH Z  5 .   ? 6.311   0.871   37.240  1.00 12.99 ? 2069 HOH A O   1 
HETATM 8626 O  O   . HOH Z  5 .   ? 26.938  -6.086  41.962  1.00 31.33 ? 2070 HOH A O   1 
HETATM 8627 O  O   . HOH Z  5 .   ? 11.366  2.951   41.816  1.00 13.60 ? 2071 HOH A O   1 
HETATM 8628 O  O   . HOH Z  5 .   ? 33.317  7.654   49.684  1.00 24.01 ? 2072 HOH A O   1 
HETATM 8629 O  O   . HOH Z  5 .   ? 4.539   9.300   43.448  1.00 16.29 ? 2073 HOH A O   1 
HETATM 8630 O  O   . HOH Z  5 .   ? 5.541   10.206  40.867  1.00 17.11 ? 2074 HOH A O   1 
HETATM 8631 O  O   . HOH Z  5 .   ? 30.679  7.102   70.621  1.00 41.08 ? 2075 HOH A O   1 
HETATM 8632 O  O   . HOH Z  5 .   ? 11.509  5.908   43.504  1.00 16.02 ? 2076 HOH A O   1 
HETATM 8633 O  O   . HOH Z  5 .   ? 9.231   13.171  41.992  1.00 14.76 ? 2077 HOH A O   1 
HETATM 8634 O  O   . HOH Z  5 .   ? 16.029  10.299  40.953  1.00 18.06 ? 2078 HOH A O   1 
HETATM 8635 O  O   . HOH Z  5 .   ? 14.213  8.793   39.215  1.00 27.70 ? 2079 HOH A O   1 
HETATM 8636 O  O   . HOH Z  5 .   ? 14.903  9.474   45.246  1.00 15.30 ? 2080 HOH A O   1 
HETATM 8637 O  O   . HOH Z  5 .   ? 15.014  15.814  45.621  1.00 27.62 ? 2081 HOH A O   1 
HETATM 8638 O  O   . HOH Z  5 .   ? 11.854  2.835   46.586  1.00 18.60 ? 2082 HOH A O   1 
HETATM 8639 O  O   . HOH Z  5 .   ? 10.244  7.639   56.713  1.00 11.61 ? 2083 HOH A O   1 
HETATM 8640 O  O   . HOH Z  5 .   ? 8.740   5.883   54.432  1.00 12.99 ? 2084 HOH A O   1 
HETATM 8641 O  O   . HOH Z  5 .   ? 14.711  10.707  60.702  1.00 13.09 ? 2085 HOH A O   1 
HETATM 8642 O  O   . HOH Z  5 .   ? 11.620  18.255  45.805  1.00 32.60 ? 2086 HOH A O   1 
HETATM 8643 O  O   . HOH Z  5 .   ? 14.019  14.274  67.434  1.00 23.14 ? 2087 HOH A O   1 
HETATM 8644 O  O   . HOH Z  5 .   ? 13.938  9.337   73.137  1.00 26.47 ? 2088 HOH A O   1 
HETATM 8645 O  O   . HOH Z  5 .   ? 17.791  10.908  72.731  1.00 38.49 ? 2089 HOH A O   1 
HETATM 8646 O  O   . HOH Z  5 .   ? 21.255  16.472  68.421  1.00 24.20 ? 2090 HOH A O   1 
HETATM 8647 O  O   . HOH Z  5 .   ? 13.482  16.012  69.421  1.00 32.71 ? 2091 HOH A O   1 
HETATM 8648 O  O   . HOH Z  5 .   ? 25.840  11.147  71.557  1.00 35.24 ? 2092 HOH A O   1 
HETATM 8649 O  O   . HOH Z  5 .   ? 26.424  12.316  69.019  1.00 25.24 ? 2093 HOH A O   1 
HETATM 8650 O  O   . HOH Z  5 .   ? 24.917  15.894  69.931  1.00 43.29 ? 2094 HOH A O   1 
HETATM 8651 O  O   . HOH Z  5 .   ? 22.098  -18.484 50.687  1.00 32.37 ? 2095 HOH A O   1 
HETATM 8652 O  O   . HOH Z  5 .   ? 19.677  -20.309 54.672  1.00 36.33 ? 2096 HOH A O   1 
HETATM 8653 O  O   . HOH Z  5 .   ? 29.486  -14.018 55.157  1.00 31.72 ? 2097 HOH A O   1 
HETATM 8654 O  O   . HOH Z  5 .   ? 18.092  -14.366 64.202  1.00 40.99 ? 2098 HOH A O   1 
HETATM 8655 O  O   . HOH Z  5 .   ? 21.153  12.070  66.043  1.00 15.61 ? 2099 HOH A O   1 
HETATM 8656 O  O   . HOH Z  5 .   ? 19.091  16.805  66.515  1.00 28.12 ? 2100 HOH A O   1 
HETATM 8657 O  O   . HOH Z  5 .   ? 18.602  17.486  60.247  1.00 21.82 ? 2101 HOH A O   1 
HETATM 8658 O  O   . HOH Z  5 .   ? 16.473  18.852  62.395  1.00 39.65 ? 2102 HOH A O   1 
HETATM 8659 O  O   . HOH Z  5 .   ? 14.645  7.194   43.944  1.00 27.43 ? 2103 HOH A O   1 
HETATM 8660 O  O   . HOH Z  5 .   ? 13.892  4.894   42.589  1.00 33.75 ? 2104 HOH A O   1 
HETATM 8661 O  O   . HOH Z  5 .   ? 16.296  13.232  43.441  1.00 18.13 ? 2105 HOH A O   1 
HETATM 8662 O  O   . HOH Z  5 .   ? 16.900  15.715  50.203  1.00 25.67 ? 2106 HOH A O   1 
HETATM 8663 O  O   . HOH Z  5 .   ? -0.903  -11.252 43.727  1.00 41.48 ? 2107 HOH A O   1 
HETATM 8664 O  O   . HOH Z  5 .   ? -4.612  -9.744  45.641  1.00 32.28 ? 2108 HOH A O   1 
HETATM 8665 O  O   . HOH Z  5 .   ? 20.876  9.077   40.043  1.00 28.91 ? 2109 HOH A O   1 
HETATM 8666 O  O   . HOH Z  5 .   ? -0.192  -11.035 38.963  1.00 36.80 ? 2110 HOH A O   1 
HETATM 8667 O  O   . HOH Z  5 .   ? 24.790  7.052   41.223  1.00 35.21 ? 2111 HOH A O   1 
HETATM 8668 O  O   . HOH Z  5 .   ? 22.731  10.039  47.620  1.00 24.99 ? 2112 HOH A O   1 
HETATM 8669 O  O   . HOH Z  5 .   ? 14.093  2.418   45.286  1.00 23.78 ? 2113 HOH A O   1 
HETATM 8670 O  O   . HOH Z  5 .   ? 20.771  8.662   49.025  1.00 14.42 ? 2114 HOH A O   1 
HETATM 8671 O  O   . HOH Z  5 .   ? 21.147  11.333  51.867  1.00 22.42 ? 2115 HOH A O   1 
HETATM 8672 O  O   . HOH Z  5 .   ? 21.959  14.568  59.392  1.00 17.76 ? 2116 HOH A O   1 
HETATM 8673 O  O   . HOH Z  5 .   ? 26.356  15.259  60.630  1.00 25.48 ? 2117 HOH A O   1 
HETATM 8674 O  O   . HOH Z  5 .   ? 23.118  17.692  67.037  1.00 26.61 ? 2118 HOH A O   1 
HETATM 8675 O  O   . HOH Z  5 .   ? 31.350  8.651   62.013  1.00 15.90 ? 2119 HOH A O   1 
HETATM 8676 O  O   . HOH Z  5 .   ? 30.789  10.870  59.829  1.00 29.83 ? 2120 HOH A O   1 
HETATM 8677 O  O   . HOH Z  5 .   ? 28.230  12.353  57.468  1.00 24.66 ? 2121 HOH A O   1 
HETATM 8678 O  O   . HOH Z  5 .   ? 29.816  9.516   57.951  1.00 23.16 ? 2122 HOH A O   1 
HETATM 8679 O  O   . HOH Z  5 .   ? 23.380  15.197  54.514  1.00 32.87 ? 2123 HOH A O   1 
HETATM 8680 O  O   . HOH Z  5 .   ? 29.705  9.558   53.983  1.00 20.12 ? 2124 HOH A O   1 
HETATM 8681 O  O   . HOH Z  5 .   ? 29.736  7.037   52.405  1.00 19.25 ? 2125 HOH A O   1 
HETATM 8682 O  O   . HOH Z  5 .   ? 28.349  6.924   47.430  1.00 19.53 ? 2126 HOH A O   1 
HETATM 8683 O  O   . HOH Z  5 .   ? 24.594  11.205  49.452  1.00 38.43 ? 2127 HOH A O   1 
HETATM 8684 O  O   . HOH Z  5 .   ? 27.115  10.351  52.013  1.00 29.25 ? 2128 HOH A O   1 
HETATM 8685 O  O   . HOH Z  5 .   ? 26.424  -1.689  43.529  1.00 11.96 ? 2129 HOH A O   1 
HETATM 8686 O  O   . HOH Z  5 .   ? 26.914  7.921   40.009  1.00 32.09 ? 2130 HOH A O   1 
HETATM 8687 O  O   . HOH Z  5 .   ? 27.860  0.298   46.254  1.00 8.74  ? 2131 HOH A O   1 
HETATM 8688 O  O   . HOH Z  5 .   ? 24.285  4.404   40.936  1.00 22.74 ? 2132 HOH A O   1 
HETATM 8689 O  O   . HOH Z  5 .   ? 20.930  2.929   39.191  1.00 23.17 ? 2133 HOH A O   1 
HETATM 8690 O  O   . HOH Z  5 .   ? 25.295  -2.095  41.127  1.00 21.91 ? 2134 HOH A O   1 
HETATM 8691 O  O   . HOH Z  5 .   ? 19.107  -3.258  41.473  1.00 24.56 ? 2135 HOH A O   1 
HETATM 8692 O  O   . HOH Z  5 .   ? 21.904  -4.360  38.897  1.00 37.22 ? 2136 HOH A O   1 
HETATM 8693 O  O   . HOH Z  5 .   ? 17.602  3.813   36.248  1.00 36.11 ? 2137 HOH A O   1 
HETATM 8694 O  O   . HOH Z  5 .   ? 15.698  -2.655  39.537  1.00 18.89 ? 2138 HOH A O   1 
HETATM 8695 O  O   . HOH Z  5 .   ? 14.500  2.803   41.183  1.00 22.18 ? 2139 HOH A O   1 
HETATM 8696 O  O   . HOH Z  5 .   ? 15.377  2.359   34.421  1.00 26.54 ? 2140 HOH A O   1 
HETATM 8697 O  O   . HOH Z  5 .   ? 11.219  5.263   33.519  1.00 25.92 ? 2141 HOH A O   1 
HETATM 8698 O  O   . HOH Z  5 .   ? 9.606   -1.892  36.718  1.00 30.26 ? 2142 HOH A O   1 
HETATM 8699 O  O   . HOH Z  5 .   ? 13.858  0.848   42.863  1.00 20.98 ? 2143 HOH A O   1 
HETATM 8700 O  O   . HOH Z  5 .   ? 10.673  1.622   44.295  1.00 10.08 ? 2144 HOH A O   1 
HETATM 8701 O  O   . HOH Z  5 .   ? 12.330  -4.959  40.629  1.00 24.59 ? 2145 HOH A O   1 
HETATM 8702 O  O   . HOH Z  5 .   ? 14.665  -2.461  42.018  1.00 17.12 ? 2146 HOH A O   1 
HETATM 8703 O  O   . HOH Z  5 .   ? 17.928  -7.084  49.473  1.00 8.27  ? 2147 HOH A O   1 
HETATM 8704 O  O   . HOH Z  5 .   ? 26.934  -4.303  59.225  1.00 12.41 ? 2148 HOH A O   1 
HETATM 8705 O  O   . HOH Z  5 .   ? 24.133  -7.544  57.017  1.00 14.68 ? 2149 HOH A O   1 
HETATM 8706 O  O   . HOH Z  5 .   ? 27.859  -8.746  64.421  1.00 38.38 ? 2150 HOH A O   1 
HETATM 8707 O  O   . HOH Z  5 .   ? 32.281  -8.560  63.794  1.00 36.11 ? 2151 HOH A O   1 
HETATM 8708 O  O   . HOH Z  5 .   ? 30.508  -0.901  70.141  1.00 21.54 ? 2152 HOH A O   1 
HETATM 8709 O  O   . HOH Z  5 .   ? 34.974  -0.660  68.501  1.00 34.14 ? 2153 HOH A O   1 
HETATM 8710 O  O   . HOH Z  5 .   ? 34.014  -5.655  65.130  1.00 26.84 ? 2154 HOH A O   1 
HETATM 8711 O  O   . HOH Z  5 .   ? 36.260  -3.659  64.327  1.00 26.42 ? 2155 HOH A O   1 
HETATM 8712 O  O   . HOH Z  5 .   ? 28.912  -6.137  58.839  1.00 16.70 ? 2156 HOH A O   1 
HETATM 8713 O  O   . HOH Z  5 .   ? 26.172  -10.025 55.979  1.00 22.68 ? 2157 HOH A O   1 
HETATM 8714 O  O   . HOH Z  5 .   ? 21.899  -5.690  55.488  1.00 24.89 ? 2158 HOH A O   1 
HETATM 8715 O  O   . HOH Z  5 .   ? 12.599  -6.578  44.272  1.00 25.46 ? 2159 HOH A O   1 
HETATM 8716 O  O   . HOH Z  5 .   ? 18.775  -5.742  41.065  1.00 33.14 ? 2160 HOH A O   1 
HETATM 8717 O  O   . HOH Z  5 .   ? 23.982  -12.200 46.688  1.00 31.69 ? 2161 HOH A O   1 
HETATM 8718 O  O   . HOH Z  5 .   ? 20.549  -4.890  42.903  1.00 27.88 ? 2162 HOH A O   1 
HETATM 8719 O  O   . HOH Z  5 .   ? 27.553  -7.056  44.340  1.00 21.90 ? 2163 HOH A O   1 
HETATM 8720 O  O   . HOH Z  5 .   ? 26.883  -3.998  51.700  1.00 21.11 ? 2164 HOH A O   1 
HETATM 8721 O  O   . HOH Z  5 .   ? 26.616  -0.299  52.292  1.00 18.15 ? 2165 HOH A O   1 
HETATM 8722 O  O   . HOH Z  5 .   ? 28.225  -6.225  52.154  1.00 23.70 ? 2166 HOH A O   1 
HETATM 8723 O  O   . HOH Z  5 .   ? 30.522  -8.988  55.555  1.00 25.20 ? 2167 HOH A O   1 
HETATM 8724 O  O   . HOH Z  5 .   ? 30.724  6.848   49.998  1.00 18.22 ? 2168 HOH A O   1 
HETATM 8725 O  O   . HOH Z  5 .   ? 31.801  7.834   57.337  1.00 24.41 ? 2169 HOH A O   1 
HETATM 8726 O  O   . HOH Z  5 .   ? 30.646  7.893   67.249  1.00 27.21 ? 2170 HOH A O   1 
HETATM 8727 O  O   . HOH Z  5 .   ? 32.822  6.090   69.584  1.00 40.93 ? 2171 HOH A O   1 
HETATM 8728 O  O   . HOH Z  5 .   ? 36.390  5.267   63.325  1.00 34.61 ? 2172 HOH A O   1 
HETATM 8729 O  O   . HOH Z  5 .   ? 34.313  6.584   65.928  1.00 32.23 ? 2173 HOH A O   1 
HETATM 8730 O  O   . HOH Z  5 .   ? 39.245  2.214   63.919  1.00 27.81 ? 2174 HOH A O   1 
HETATM 8731 O  O   . HOH Z  5 .   ? 31.617  1.793   72.570  1.00 40.10 ? 2175 HOH A O   1 
HETATM 8732 O  O   . HOH Z  5 .   ? 29.670  5.254   72.698  1.00 40.59 ? 2176 HOH A O   1 
HETATM 8733 O  O   . HOH Z  5 .   ? 23.664  9.654   71.533  1.00 22.47 ? 2177 HOH A O   1 
HETATM 8734 O  O   . HOH Z  5 .   ? 27.095  6.393   72.107  1.00 22.84 ? 2178 HOH A O   1 
HETATM 8735 O  O   . HOH Z  5 .   ? 24.495  6.875   72.373  1.00 25.04 ? 2179 HOH A O   1 
HETATM 8736 O  O   . HOH Z  5 .   ? 21.144  9.286   77.138  1.00 52.46 ? 2180 HOH A O   1 
HETATM 8737 O  O   . HOH Z  5 .   ? 16.611  8.399   73.954  1.00 32.83 ? 2181 HOH A O   1 
HETATM 8738 O  O   . HOH Z  5 .   ? 7.418   4.937   69.597  1.00 33.34 ? 2182 HOH A O   1 
HETATM 8739 O  O   . HOH Z  5 .   ? 8.275   14.098  55.520  1.00 12.83 ? 2183 HOH A O   1 
HETATM 8740 O  O   . HOH Z  5 .   ? 11.041  16.536  57.970  1.00 15.54 ? 2184 HOH A O   1 
HETATM 8741 O  O   . HOH Z  5 .   ? 15.102  16.338  66.137  1.00 33.20 ? 2185 HOH A O   1 
HETATM 8742 O  O   . HOH Z  5 .   ? 11.333  20.646  59.176  1.00 29.30 ? 2186 HOH A O   1 
HETATM 8743 O  O   . HOH Z  5 .   ? 6.833   18.065  66.508  1.00 37.34 ? 2187 HOH A O   1 
HETATM 8744 O  O   . HOH Z  5 .   ? 10.759  17.179  69.601  1.00 29.27 ? 2188 HOH A O   1 
HETATM 8745 O  O   . HOH Z  5 .   ? 11.763  25.379  66.442  1.00 39.90 ? 2189 HOH A O   1 
HETATM 8746 O  O   . HOH Z  5 .   ? 5.263   18.932  63.978  1.00 30.73 ? 2190 HOH A O   1 
HETATM 8747 O  O   . HOH Z  5 .   ? 4.679   18.025  60.736  1.00 24.08 ? 2191 HOH A O   1 
HETATM 8748 O  O   . HOH Z  5 .   ? 13.110  18.890  56.054  1.00 18.60 ? 2192 HOH A O   1 
HETATM 8749 O  O   . HOH Z  5 .   ? 6.333   20.528  54.042  1.00 25.77 ? 2193 HOH A O   1 
HETATM 8750 O  O   . HOH Z  5 .   ? 1.682   20.285  52.522  1.00 46.37 ? 2194 HOH A O   1 
HETATM 8751 O  O   . HOH Z  5 .   ? 13.032  16.535  47.858  1.00 23.66 ? 2195 HOH A O   1 
HETATM 8752 O  O   . HOH Z  5 .   ? 3.403   9.517   52.965  1.00 11.87 ? 2196 HOH A O   1 
HETATM 8753 O  O   . HOH Z  5 .   ? 5.148   6.678   44.105  1.00 10.79 ? 2197 HOH A O   1 
HETATM 8754 O  O   . HOH Z  5 .   ? -0.066  -3.766  46.181  1.00 14.65 ? 2198 HOH A O   1 
HETATM 8755 O  O   . HOH Z  5 .   ? 0.794   -1.833  43.030  1.00 10.54 ? 2199 HOH A O   1 
HETATM 8756 O  O   . HOH Z  5 .   ? 11.884  -8.354  53.957  1.00 10.02 ? 2200 HOH A O   1 
HETATM 8757 O  O   . HOH Z  5 .   ? 6.670   -11.439 50.459  1.00 30.65 ? 2201 HOH A O   1 
HETATM 8758 O  O   . HOH Z  5 .   ? 4.397   -7.097  52.284  1.00 24.71 ? 2202 HOH A O   1 
HETATM 8759 O  O   . HOH Z  5 .   ? 4.164   -10.172 52.503  1.00 25.54 ? 2203 HOH A O   1 
HETATM 8760 O  O   . HOH Z  5 .   ? 6.443   -10.771 55.079  1.00 27.83 ? 2204 HOH A O   1 
HETATM 8761 O  O   . HOH Z  5 .   ? 20.589  -10.639 69.382  1.00 30.11 ? 2205 HOH A O   1 
HETATM 8762 O  O   . HOH Z  5 .   ? 22.005  -12.218 63.208  1.00 30.46 ? 2206 HOH A O   1 
HETATM 8763 O  O   . HOH Z  5 .   ? 18.470  -10.474 66.195  1.00 17.91 ? 2207 HOH A O   1 
HETATM 8764 O  O   . HOH Z  5 .   ? 25.174  -9.073  65.199  1.00 21.61 ? 2208 HOH A O   1 
HETATM 8765 O  O   . HOH Z  5 .   ? 26.530  -11.523 60.477  1.00 26.96 ? 2209 HOH A O   1 
HETATM 8766 O  O   . HOH Z  5 .   ? 24.350  -12.683 63.745  1.00 41.99 ? 2210 HOH A O   1 
HETATM 8767 O  O   . HOH Z  5 .   ? 19.275  -18.234 52.083  1.00 22.60 ? 2211 HOH A O   1 
HETATM 8768 O  O   . HOH Z  5 .   ? 27.957  -16.115 56.366  1.00 35.41 ? 2212 HOH A O   1 
HETATM 8769 O  O   . HOH Z  5 .   ? 20.220  -19.058 59.921  1.00 35.40 ? 2213 HOH A O   1 
HETATM 8770 O  O   . HOH Z  5 .   ? 15.798  -12.882 57.543  1.00 11.89 ? 2214 HOH A O   1 
HETATM 8771 O  O   . HOH Z  5 .   ? 20.356  -14.590 62.712  1.00 45.27 ? 2215 HOH A O   1 
HETATM 8772 O  O   . HOH Z  5 .   ? 18.470  -18.100 56.087  1.00 21.14 ? 2216 HOH A O   1 
HETATM 8773 O  O   . HOH Z  5 .   ? 14.862  -19.218 53.896  1.00 29.34 ? 2217 HOH A O   1 
HETATM 8774 O  O   . HOH Z  5 .   ? 10.466  -10.519 53.263  1.00 20.27 ? 2218 HOH A O   1 
HETATM 8775 O  O   . HOH Z  5 .   ? 9.838   -12.526 46.964  1.00 33.82 ? 2219 HOH A O   1 
HETATM 8776 O  O   . HOH Z  5 .   ? 13.592  -8.178  42.352  1.00 44.72 ? 2220 HOH A O   1 
HETATM 8777 O  O   . HOH Z  5 .   ? 16.834  -11.680 41.841  1.00 38.06 ? 2221 HOH A O   1 
HETATM 8778 O  O   . HOH Z  5 .   ? 10.828  -16.244 45.942  1.00 41.79 ? 2222 HOH A O   1 
HETATM 8779 O  O   . HOH Z  5 .   ? 8.201   -11.884 53.365  1.00 29.10 ? 2223 HOH A O   1 
HETATM 8780 O  O   . HOH Z  5 .   ? 13.973  -18.783 56.969  1.00 41.42 ? 2224 HOH A O   1 
HETATM 8781 O  O   . HOH Z  5 .   ? 13.370  -18.959 50.615  1.00 30.89 ? 2225 HOH A O   1 
HETATM 8782 O  O   . HOH Z  5 .   ? 8.755   -15.996 57.115  1.00 25.84 ? 2226 HOH A O   1 
HETATM 8783 O  O   . HOH Z  5 .   ? 15.541  -15.050 64.281  1.00 30.95 ? 2227 HOH A O   1 
HETATM 8784 O  O   . HOH Z  5 .   ? 11.305  -12.037 67.426  1.00 22.39 ? 2228 HOH A O   1 
HETATM 8785 O  O   . HOH Z  5 .   ? 9.159   -7.851  66.998  1.00 23.29 ? 2229 HOH A O   1 
HETATM 8786 O  O   . HOH Z  5 .   ? 15.535  -11.448 65.976  1.00 24.76 ? 2230 HOH A O   1 
HETATM 8787 O  O   . HOH Z  5 .   ? 11.098  -8.954  70.861  1.00 33.47 ? 2231 HOH A O   1 
HETATM 8788 O  O   . HOH Z  5 .   ? 14.495  -6.139  71.483  1.00 45.41 ? 2232 HOH A O   1 
HETATM 8789 O  O   . HOH Z  5 .   ? 8.976   -12.038 65.818  1.00 21.12 ? 2233 HOH A O   1 
HETATM 8790 O  O   . HOH Z  5 .   ? 0.558   -11.959 64.442  1.00 28.70 ? 2234 HOH A O   1 
HETATM 8791 O  O   . HOH Z  5 .   ? 5.262   -17.308 59.100  1.00 19.93 ? 2235 HOH A O   1 
HETATM 8792 O  O   . HOH Z  5 .   ? 6.762   -6.057  65.678  1.00 15.72 ? 2236 HOH A O   1 
HETATM 8793 O  O   . HOH Z  5 .   ? 4.896   -8.226  68.148  1.00 34.71 ? 2237 HOH A O   1 
HETATM 8794 O  O   . HOH Z  5 .   ? -1.374  -2.547  65.553  1.00 26.22 ? 2238 HOH A O   1 
HETATM 8795 O  O   . HOH Z  5 .   ? -5.395  -0.876  60.466  1.00 31.63 ? 2239 HOH A O   1 
HETATM 8796 O  O   . HOH Z  5 .   ? -3.887  0.050   64.792  1.00 35.32 ? 2240 HOH A O   1 
HETATM 8797 O  O   . HOH Z  5 .   ? 3.357   6.181   69.064  1.00 39.82 ? 2241 HOH A O   1 
HETATM 8798 O  O   . HOH Z  5 .   ? -4.156  2.688   63.221  1.00 21.59 ? 2242 HOH A O   1 
HETATM 8799 O  O   . HOH Z  5 .   ? -6.477  6.127   61.428  1.00 42.53 ? 2243 HOH A O   1 
HETATM 8800 O  O   . HOH Z  5 .   ? -5.346  10.478  61.565  1.00 25.51 ? 2244 HOH A O   1 
HETATM 8801 O  O   . HOH Z  5 .   ? -6.958  6.302   56.122  1.00 32.25 ? 2245 HOH A O   1 
HETATM 8802 O  O   . HOH Z  5 .   ? -6.445  7.933   59.519  1.00 30.06 ? 2246 HOH A O   1 
HETATM 8803 O  O   . HOH Z  5 .   ? -7.101  11.296  56.073  1.00 38.48 ? 2247 HOH A O   1 
HETATM 8804 O  O   . HOH Z  5 .   ? -8.553  9.917   48.335  1.00 19.00 ? 2248 HOH A O   1 
HETATM 8805 O  O   . HOH Z  5 .   ? -6.517  2.795   56.661  1.00 19.90 ? 2249 HOH A O   1 
HETATM 8806 O  O   . HOH Z  5 .   ? -6.670  0.322   55.411  1.00 19.38 ? 2250 HOH A O   1 
HETATM 8807 O  O   . HOH Z  5 .   ? -8.373  -1.479  52.400  1.00 36.44 ? 2251 HOH A O   1 
HETATM 8808 O  O   . HOH Z  5 .   ? 1.577   -11.062 48.299  1.00 37.13 ? 2252 HOH A O   1 
HETATM 8809 O  O   . HOH Z  5 .   ? -1.851  -10.386 46.059  1.00 39.59 ? 2253 HOH A O   1 
HETATM 8810 O  O   . HOH Z  5 .   ? -0.247  -9.812  41.552  1.00 22.15 ? 2254 HOH A O   1 
HETATM 8811 O  O   . HOH Z  5 .   ? 3.058   -8.811  39.682  1.00 30.64 ? 2255 HOH A O   1 
HETATM 8812 O  O   . HOH Z  5 .   ? 5.490   -6.793  39.681  1.00 28.10 ? 2256 HOH A O   1 
HETATM 8813 O  O   . HOH Z  5 .   ? 8.789   -7.581  42.865  1.00 31.92 ? 2257 HOH A O   1 
HETATM 8814 O  O   . HOH Z  5 .   ? 23.435  -8.389  68.346  1.00 24.08 ? 2258 HOH A O   1 
HETATM 8815 O  O   . HOH Z  5 .   ? 21.249  16.868  56.599  1.00 37.61 ? 2259 HOH A O   1 
HETATM 8816 O  O   . HOH Z  5 .   ? 15.961  19.247  54.772  1.00 32.17 ? 2260 HOH A O   1 
HETATM 8817 O  O   . HOH Z  5 .   ? 21.423  15.261  51.712  1.00 31.59 ? 2261 HOH A O   1 
HETATM 8818 O  O   . HOH AA 5 .   ? -25.276 -2.547  25.906  1.00 41.16 ? 2001 HOH B O   1 
HETATM 8819 O  O   . HOH AA 5 .   ? -16.748 -12.660 15.507  1.00 36.58 ? 2002 HOH B O   1 
HETATM 8820 O  O   . HOH AA 5 .   ? -24.967 -2.724  18.057  1.00 42.38 ? 2003 HOH B O   1 
HETATM 8821 O  O   . HOH AA 5 .   ? -20.730 -13.173 17.722  1.00 31.04 ? 2004 HOH B O   1 
HETATM 8822 O  O   . HOH AA 5 .   ? -16.975 -13.787 17.803  1.00 40.25 ? 2005 HOH B O   1 
HETATM 8823 O  O   . HOH AA 5 .   ? -21.984 -8.969  16.127  1.00 22.93 ? 2006 HOH B O   1 
HETATM 8824 O  O   . HOH AA 5 .   ? -12.806 -10.980 13.986  1.00 27.68 ? 2007 HOH B O   1 
HETATM 8825 O  O   . HOH AA 5 .   ? -11.920 -11.895 21.787  1.00 35.26 ? 2008 HOH B O   1 
HETATM 8826 O  O   . HOH AA 5 .   ? -15.968 -10.102 15.635  1.00 19.60 ? 2009 HOH B O   1 
HETATM 8827 O  O   . HOH AA 5 .   ? -0.812  11.583  13.883  1.00 15.94 ? 2010 HOH B O   1 
HETATM 8828 O  O   . HOH AA 5 .   ? 1.423   14.610  12.525  1.00 26.29 ? 2011 HOH B O   1 
HETATM 8829 O  O   . HOH AA 5 .   ? 2.958   12.618  15.956  1.00 26.10 ? 2012 HOH B O   1 
HETATM 8830 O  O   . HOH AA 5 .   ? -0.444  19.335  18.753  1.00 30.00 ? 2013 HOH B O   1 
HETATM 8831 O  O   . HOH AA 5 .   ? -1.034  14.540  11.248  1.00 30.73 ? 2014 HOH B O   1 
HETATM 8832 O  O   . HOH AA 5 .   ? -8.941  -10.868 13.893  1.00 36.04 ? 2015 HOH B O   1 
HETATM 8833 O  O   . HOH AA 5 .   ? -18.770 -7.998  10.430  1.00 48.43 ? 2016 HOH B O   1 
HETATM 8834 O  O   . HOH AA 5 .   ? -18.350 -7.592  14.057  1.00 35.10 ? 2017 HOH B O   1 
HETATM 8835 O  O   . HOH AA 5 .   ? -17.741 -4.971  12.566  1.00 36.77 ? 2018 HOH B O   1 
HETATM 8836 O  O   . HOH AA 5 .   ? -27.960 8.612   29.884  1.00 32.80 ? 2019 HOH B O   1 
HETATM 8837 O  O   . HOH AA 5 .   ? -2.646  10.060  9.950   1.00 16.02 ? 2020 HOH B O   1 
HETATM 8838 O  O   . HOH AA 5 .   ? -11.641 15.838  6.320   1.00 52.19 ? 2021 HOH B O   1 
HETATM 8839 O  O   . HOH AA 5 .   ? -17.703 -5.578  44.181  1.00 31.07 ? 2022 HOH B O   1 
HETATM 8840 O  O   . HOH AA 5 .   ? -3.664  18.250  12.128  1.00 33.24 ? 2023 HOH B O   1 
HETATM 8841 O  O   . HOH AA 5 .   ? 0.506   13.744  14.797  1.00 23.33 ? 2024 HOH B O   1 
HETATM 8842 O  O   . HOH AA 5 .   ? 0.396   15.773  16.754  1.00 30.37 ? 2025 HOH B O   1 
HETATM 8843 O  O   . HOH AA 5 .   ? -2.419  18.515  17.386  1.00 26.61 ? 2026 HOH B O   1 
HETATM 8844 O  O   . HOH AA 5 .   ? -2.534  12.434  11.760  1.00 15.37 ? 2027 HOH B O   1 
HETATM 8845 O  O   . HOH AA 5 .   ? -8.829  12.214  15.293  1.00 13.05 ? 2028 HOH B O   1 
HETATM 8846 O  O   . HOH AA 5 .   ? -15.756 18.600  17.270  1.00 25.44 ? 2029 HOH B O   1 
HETATM 8847 O  O   . HOH AA 5 .   ? 9.634   8.794   23.338  1.00 23.47 ? 2030 HOH B O   1 
HETATM 8848 O  O   . HOH AA 5 .   ? 8.101   12.710  25.725  1.00 29.79 ? 2031 HOH B O   1 
HETATM 8849 O  O   . HOH AA 5 .   ? -17.899 14.359  15.488  1.00 32.23 ? 2032 HOH B O   1 
HETATM 8850 O  O   . HOH AA 5 .   ? -9.217  9.493   13.065  1.00 14.86 ? 2033 HOH B O   1 
HETATM 8851 O  O   . HOH AA 5 .   ? 2.855   18.777  20.902  1.00 29.19 ? 2034 HOH B O   1 
HETATM 8852 O  O   . HOH AA 5 .   ? -21.089 12.540  18.803  1.00 29.39 ? 2035 HOH B O   1 
HETATM 8853 O  O   . HOH AA 5 .   ? -27.735 13.783  31.891  1.00 26.93 ? 2036 HOH B O   1 
HETATM 8854 O  O   . HOH AA 5 .   ? -20.654 22.241  30.850  1.00 31.39 ? 2037 HOH B O   1 
HETATM 8855 O  O   . HOH AA 5 .   ? -19.841 23.728  33.471  1.00 28.62 ? 2038 HOH B O   1 
HETATM 8856 O  O   . HOH AA 5 .   ? -15.462 22.838  32.477  1.00 35.70 ? 2039 HOH B O   1 
HETATM 8857 O  O   . HOH AA 5 .   ? -14.069 21.330  34.951  1.00 25.25 ? 2040 HOH B O   1 
HETATM 8858 O  O   . HOH AA 5 .   ? -21.775 7.663   25.430  1.00 16.94 ? 2041 HOH B O   1 
HETATM 8859 O  O   . HOH AA 5 .   ? -20.365 12.407  21.873  1.00 26.00 ? 2042 HOH B O   1 
HETATM 8860 O  O   . HOH AA 5 .   ? -21.752 -1.003  24.994  1.00 22.80 ? 2043 HOH B O   1 
HETATM 8861 O  O   . HOH AA 5 .   ? -25.726 5.005   31.593  1.00 19.68 ? 2044 HOH B O   1 
HETATM 8862 O  O   . HOH AA 5 .   ? -23.143 5.515   28.003  1.00 31.61 ? 2045 HOH B O   1 
HETATM 8863 O  O   . HOH AA 5 .   ? -30.695 1.889   30.818  1.00 19.14 ? 2046 HOH B O   1 
HETATM 8864 O  O   . HOH AA 5 .   ? 10.576  9.630   34.996  1.00 31.76 ? 2047 HOH B O   1 
HETATM 8865 O  O   . HOH AA 5 .   ? -29.326 1.939   38.932  1.00 23.76 ? 2048 HOH B O   1 
HETATM 8866 O  O   . HOH AA 5 .   ? -28.155 6.215   31.153  1.00 25.19 ? 2049 HOH B O   1 
HETATM 8867 O  O   . HOH AA 5 .   ? -32.154 8.011   32.240  1.00 24.12 ? 2050 HOH B O   1 
HETATM 8868 O  O   . HOH AA 5 .   ? -28.867 7.616   37.388  1.00 27.63 ? 2051 HOH B O   1 
HETATM 8869 O  O   . HOH AA 5 .   ? -12.722 18.853  46.933  1.00 35.56 ? 2052 HOH B O   1 
HETATM 8870 O  O   . HOH AA 5 .   ? -11.197 14.155  47.836  1.00 28.97 ? 2053 HOH B O   1 
HETATM 8871 O  O   . HOH AA 5 .   ? 2.157   12.975  39.810  1.00 27.63 ? 2054 HOH B O   1 
HETATM 8872 O  O   . HOH AA 5 .   ? 10.782  6.875   24.695  1.00 36.16 ? 2055 HOH B O   1 
HETATM 8873 O  O   . HOH AA 5 .   ? 6.941   -3.776  24.059  1.00 33.14 ? 2056 HOH B O   1 
HETATM 8874 O  O   . HOH AA 5 .   ? 11.905  7.410   19.698  1.00 33.46 ? 2057 HOH B O   1 
HETATM 8875 O  O   . HOH AA 5 .   ? -15.811 1.336   47.285  1.00 15.31 ? 2058 HOH B O   1 
HETATM 8876 O  O   . HOH AA 5 .   ? -18.540 -3.345  43.159  1.00 28.73 ? 2059 HOH B O   1 
HETATM 8877 O  O   . HOH AA 5 .   ? -19.787 0.670   41.083  1.00 19.83 ? 2060 HOH B O   1 
HETATM 8878 O  O   . HOH AA 5 .   ? 4.976   -5.626  20.606  1.00 36.25 ? 2061 HOH B O   1 
HETATM 8879 O  O   . HOH AA 5 .   ? -16.904 5.056   51.930  1.00 40.93 ? 2062 HOH B O   1 
HETATM 8880 O  O   . HOH AA 5 .   ? -1.814  -5.469  23.828  1.00 29.01 ? 2063 HOH B O   1 
HETATM 8881 O  O   . HOH AA 5 .   ? -5.697  -6.728  44.954  1.00 34.44 ? 2064 HOH B O   1 
HETATM 8882 O  O   . HOH AA 5 .   ? 6.090   0.387   15.998  1.00 11.96 ? 2065 HOH B O   1 
HETATM 8883 O  O   . HOH AA 5 .   ? 3.345   3.438   21.819  1.00 14.45 ? 2066 HOH B O   1 
HETATM 8884 O  O   . HOH AA 5 .   ? 3.796   2.858   14.401  1.00 8.73  ? 2067 HOH B O   1 
HETATM 8885 O  O   . HOH AA 5 .   ? 0.090   9.218   15.256  1.00 12.97 ? 2068 HOH B O   1 
HETATM 8886 O  O   . HOH AA 5 .   ? 2.938   9.951   15.248  1.00 12.53 ? 2069 HOH B O   1 
HETATM 8887 O  O   . HOH AA 5 .   ? 4.603   8.329   23.450  1.00 17.41 ? 2070 HOH B O   1 
HETATM 8888 O  O   . HOH AA 5 .   ? 1.915   6.707   22.106  1.00 11.82 ? 2071 HOH B O   1 
HETATM 8889 O  O   . HOH AA 5 .   ? -23.736 10.190  42.370  1.00 32.44 ? 2072 HOH B O   1 
HETATM 8890 O  O   . HOH AA 5 .   ? 3.204   13.372  18.638  1.00 11.44 ? 2073 HOH B O   1 
HETATM 8891 O  O   . HOH AA 5 .   ? 6.070   11.295  24.932  1.00 12.54 ? 2074 HOH B O   1 
HETATM 8892 O  O   . HOH AA 5 .   ? 7.025   9.532   22.969  1.00 21.19 ? 2075 HOH B O   1 
HETATM 8893 O  O   . HOH AA 5 .   ? 1.456   10.865  25.411  1.00 11.75 ? 2076 HOH B O   1 
HETATM 8894 O  O   . HOH AA 5 .   ? -26.797 15.384  24.584  1.00 41.00 ? 2077 HOH B O   1 
HETATM 8895 O  O   . HOH AA 5 .   ? 1.481   17.271  24.649  1.00 22.53 ? 2078 HOH B O   1 
HETATM 8896 O  O   . HOH AA 5 .   ? -1.085  3.896   23.917  1.00 19.16 ? 2079 HOH B O   1 
HETATM 8897 O  O   . HOH AA 5 .   ? -8.562  11.330  22.659  1.00 19.09 ? 2080 HOH B O   1 
HETATM 8898 O  O   . HOH AA 5 .   ? -9.210  7.463   22.977  1.00 10.63 ? 2081 HOH B O   1 
HETATM 8899 O  O   . HOH AA 5 .   ? -12.997 13.505  29.828  1.00 8.97  ? 2082 HOH B O   1 
HETATM 8900 O  O   . HOH AA 5 .   ? 0.338   19.404  21.333  1.00 25.49 ? 2083 HOH B O   1 
HETATM 8901 O  O   . HOH AA 5 .   ? -22.201 4.927   35.030  1.00 20.00 ? 2084 HOH B O   1 
HETATM 8902 O  O   . HOH AA 5 .   ? -19.354 17.635  30.679  1.00 14.43 ? 2085 HOH B O   1 
HETATM 8903 O  O   . HOH AA 5 .   ? -25.734 20.920  33.822  1.00 31.51 ? 2086 HOH B O   1 
HETATM 8904 O  O   . HOH AA 5 .   ? -28.096 16.090  29.753  1.00 36.55 ? 2087 HOH B O   1 
HETATM 8905 O  O   . HOH AA 5 .   ? -25.189 19.594  27.741  1.00 34.09 ? 2088 HOH B O   1 
HETATM 8906 O  O   . HOH AA 5 .   ? -17.710 21.784  33.124  1.00 19.34 ? 2089 HOH B O   1 
HETATM 8907 O  O   . HOH AA 5 .   ? -21.420 19.552  30.345  1.00 17.82 ? 2090 HOH B O   1 
HETATM 8908 O  O   . HOH AA 5 .   ? -18.998 21.198  37.449  1.00 34.45 ? 2091 HOH B O   1 
HETATM 8909 O  O   . HOH AA 5 .   ? -22.235 21.753  41.004  1.00 23.23 ? 2092 HOH B O   1 
HETATM 8910 O  O   . HOH AA 5 .   ? -16.582 20.496  35.287  1.00 14.92 ? 2093 HOH B O   1 
HETATM 8911 O  O   . HOH AA 5 .   ? -11.787 20.043  34.040  1.00 25.41 ? 2094 HOH B O   1 
HETATM 8912 O  O   . HOH AA 5 .   ? -9.639  18.079  35.713  1.00 14.16 ? 2095 HOH B O   1 
HETATM 8913 O  O   . HOH AA 5 .   ? 0.060   -13.052 27.078  1.00 48.99 ? 2096 HOH B O   1 
HETATM 8914 O  O   . HOH AA 5 .   ? -17.917 -14.531 35.069  1.00 40.49 ? 2097 HOH B O   1 
HETATM 8915 O  O   . HOH AA 5 .   ? -21.903 -10.001 33.873  1.00 40.06 ? 2098 HOH B O   1 
HETATM 8916 O  O   . HOH AA 5 .   ? -24.393 -8.170  32.456  1.00 36.92 ? 2099 HOH B O   1 
HETATM 8917 O  O   . HOH AA 5 .   ? -19.791 -12.161 26.460  1.00 36.55 ? 2100 HOH B O   1 
HETATM 8918 O  O   . HOH AA 5 .   ? -2.230  17.792  28.015  1.00 21.85 ? 2101 HOH B O   1 
HETATM 8919 O  O   . HOH AA 5 .   ? 3.566   5.711   24.229  1.00 24.75 ? 2102 HOH B O   1 
HETATM 8920 O  O   . HOH AA 5 .   ? 2.590   8.425   25.171  1.00 18.26 ? 2103 HOH B O   1 
HETATM 8921 O  O   . HOH AA 5 .   ? -20.628 1.927   11.992  1.00 31.31 ? 2104 HOH B O   1 
HETATM 8922 O  O   . HOH AA 5 .   ? 3.786   14.484  25.649  1.00 14.56 ? 2105 HOH B O   1 
HETATM 8923 O  O   . HOH AA 5 .   ? -19.056 3.209   10.084  1.00 37.78 ? 2106 HOH B O   1 
HETATM 8924 O  O   . HOH AA 5 .   ? 4.267   17.636  27.863  1.00 44.84 ? 2107 HOH B O   1 
HETATM 8925 O  O   . HOH AA 5 .   ? 7.108   15.621  28.018  1.00 38.20 ? 2108 HOH B O   1 
HETATM 8926 O  O   . HOH AA 5 .   ? 1.669   15.816  32.823  1.00 39.74 ? 2109 HOH B O   1 
HETATM 8927 O  O   . HOH AA 5 .   ? -15.007 -4.457  6.458   1.00 43.63 ? 2110 HOH B O   1 
HETATM 8928 O  O   . HOH AA 5 .   ? -6.291  -10.364 9.832   1.00 23.96 ? 2111 HOH B O   1 
HETATM 8929 O  O   . HOH AA 5 .   ? -4.206  -12.784 10.566  1.00 32.86 ? 2112 HOH B O   1 
HETATM 8930 O  O   . HOH AA 5 .   ? 8.383   10.486  29.687  1.00 32.68 ? 2113 HOH B O   1 
HETATM 8931 O  O   . HOH AA 5 .   ? 8.394   6.514   33.321  1.00 25.52 ? 2114 HOH B O   1 
HETATM 8932 O  O   . HOH AA 5 .   ? 8.495   9.306   33.297  1.00 32.75 ? 2115 HOH B O   1 
HETATM 8933 O  O   . HOH AA 5 .   ? 7.537   13.660  34.241  1.00 40.27 ? 2116 HOH B O   1 
HETATM 8934 O  O   . HOH AA 5 .   ? 0.863   3.501   25.805  1.00 18.08 ? 2117 HOH B O   1 
HETATM 8935 O  O   . HOH AA 5 .   ? -6.808  17.835  38.609  1.00 26.32 ? 2118 HOH B O   1 
HETATM 8936 O  O   . HOH AA 5 .   ? -8.780  13.731  45.915  1.00 19.26 ? 2119 HOH B O   1 
HETATM 8937 O  O   . HOH AA 5 .   ? -12.713 19.306  44.203  1.00 22.28 ? 2120 HOH B O   1 
HETATM 8938 O  O   . HOH AA 5 .   ? -5.513  13.760  43.337  1.00 23.61 ? 2121 HOH B O   1 
HETATM 8939 O  O   . HOH AA 5 .   ? -1.393  13.699  41.424  1.00 31.65 ? 2122 HOH B O   1 
HETATM 8940 O  O   . HOH AA 5 .   ? -5.769  16.634  41.204  1.00 20.46 ? 2123 HOH B O   1 
HETATM 8941 O  O   . HOH AA 5 .   ? 3.771   9.915   38.891  1.00 22.07 ? 2124 HOH B O   1 
HETATM 8942 O  O   . HOH AA 5 .   ? -0.458  10.924  41.776  1.00 15.59 ? 2125 HOH B O   1 
HETATM 8943 O  O   . HOH AA 5 .   ? -0.360  13.768  38.950  1.00 32.38 ? 2126 HOH B O   1 
HETATM 8944 O  O   . HOH AA 5 .   ? 0.832   14.149  35.958  1.00 34.85 ? 2127 HOH B O   1 
HETATM 8945 O  O   . HOH AA 5 .   ? -2.081  6.162   39.292  1.00 31.66 ? 2128 HOH B O   1 
HETATM 8946 O  O   . HOH AA 5 .   ? 4.263   3.318   38.986  1.00 10.80 ? 2129 HOH B O   1 
HETATM 8947 O  O   . HOH AA 5 .   ? 8.917   4.416   29.807  1.00 24.83 ? 2130 HOH B O   1 
HETATM 8948 O  O   . HOH AA 5 .   ? 8.145   0.049   35.391  1.00 17.07 ? 2131 HOH B O   1 
HETATM 8949 O  O   . HOH AA 5 .   ? 7.478   -3.018  28.423  1.00 37.09 ? 2132 HOH B O   1 
HETATM 8950 O  O   . HOH AA 5 .   ? 2.957   1.897   24.920  1.00 20.77 ? 2133 HOH B O   1 
HETATM 8951 O  O   . HOH AA 5 .   ? 3.802   -1.545  25.956  1.00 16.83 ? 2134 HOH B O   1 
HETATM 8952 O  O   . HOH AA 5 .   ? 10.586  4.374   25.778  1.00 39.56 ? 2135 HOH B O   1 
HETATM 8953 O  O   . HOH AA 5 .   ? 6.668   -1.803  26.007  1.00 20.22 ? 2136 HOH B O   1 
HETATM 8954 O  O   . HOH AA 5 .   ? 5.078   3.555   24.834  1.00 19.58 ? 2137 HOH B O   1 
HETATM 8955 O  O   . HOH AA 5 .   ? 11.425  4.807   18.845  1.00 23.53 ? 2138 HOH B O   1 
HETATM 8956 O  O   . HOH AA 5 .   ? 11.876  2.432   23.249  1.00 22.00 ? 2139 HOH B O   1 
HETATM 8957 O  O   . HOH AA 5 .   ? 0.694   2.373   22.185  1.00 12.55 ? 2140 HOH B O   1 
HETATM 8958 O  O   . HOH AA 5 .   ? 4.094   -4.297  23.461  1.00 23.80 ? 2141 HOH B O   1 
HETATM 8959 O  O   . HOH AA 5 .   ? -7.589  -3.742  40.067  1.00 16.85 ? 2142 HOH B O   1 
HETATM 8960 O  O   . HOH AA 5 .   ? -11.506 -2.400  50.119  1.00 41.19 ? 2143 HOH B O   1 
HETATM 8961 O  O   . HOH AA 5 .   ? -17.485 5.068   49.255  1.00 26.19 ? 2144 HOH B O   1 
HETATM 8962 O  O   . HOH AA 5 .   ? -11.868 0.302   51.620  1.00 28.94 ? 2145 HOH B O   1 
HETATM 8963 O  O   . HOH AA 5 .   ? -10.284 2.244   53.196  1.00 34.16 ? 2146 HOH B O   1 
HETATM 8964 O  O   . HOH AA 5 .   ? -14.546 5.670   52.951  1.00 34.00 ? 2147 HOH B O   1 
HETATM 8965 O  O   . HOH AA 5 .   ? -8.596  0.069   42.913  1.00 11.96 ? 2148 HOH B O   1 
HETATM 8966 O  O   . HOH AA 5 .   ? -6.846  -2.526  37.378  1.00 27.56 ? 2149 HOH B O   1 
HETATM 8967 O  O   . HOH AA 5 .   ? -5.969  -6.029  42.019  1.00 22.45 ? 2150 HOH B O   1 
HETATM 8968 O  O   . HOH AA 5 .   ? -7.588  -1.548  45.003  1.00 17.48 ? 2151 HOH B O   1 
HETATM 8969 O  O   . HOH AA 5 .   ? -1.592  -0.508  40.346  1.00 16.95 ? 2152 HOH B O   1 
HETATM 8970 O  O   . HOH AA 5 .   ? 2.415   -10.197 32.829  1.00 40.67 ? 2153 HOH B O   1 
HETATM 8971 O  O   . HOH AA 5 .   ? 4.358   -7.834  30.377  1.00 32.06 ? 2154 HOH B O   1 
HETATM 8972 O  O   . HOH AA 5 .   ? 0.612   -5.659  25.243  1.00 24.38 ? 2155 HOH B O   1 
HETATM 8973 O  O   . HOH AA 5 .   ? 1.601   -9.362  37.390  1.00 35.01 ? 2156 HOH B O   1 
HETATM 8974 O  O   . HOH AA 5 .   ? -2.518  -4.918  31.971  1.00 10.33 ? 2157 HOH B O   1 
HETATM 8975 O  O   . HOH AA 5 .   ? 5.454   -4.005  39.229  1.00 30.37 ? 2158 HOH B O   1 
HETATM 8976 O  O   . HOH AA 5 .   ? -1.894  3.149   39.940  1.00 15.65 ? 2159 HOH B O   1 
HETATM 8977 O  O   . HOH AA 5 .   ? -1.767  -2.507  42.265  1.00 17.26 ? 2160 HOH B O   1 
HETATM 8978 O  O   . HOH AA 5 .   ? -4.329  -4.488  45.840  1.00 22.70 ? 2161 HOH B O   1 
HETATM 8979 O  O   . HOH AA 5 .   ? 2.165   10.562  41.837  1.00 17.26 ? 2162 HOH B O   1 
HETATM 8980 O  O   . HOH AA 5 .   ? -3.798  12.089  45.062  1.00 27.07 ? 2163 HOH B O   1 
HETATM 8981 O  O   . HOH AA 5 .   ? -14.148 13.996  47.382  1.00 30.29 ? 2164 HOH B O   1 
HETATM 8982 O  O   . HOH AA 5 .   ? -17.363 17.153  44.805  1.00 33.39 ? 2165 HOH B O   1 
HETATM 8983 O  O   . HOH AA 5 .   ? -8.471  10.972  51.447  1.00 35.71 ? 2166 HOH B O   1 
HETATM 8984 O  O   . HOH AA 5 .   ? -11.946 12.405  49.713  1.00 31.94 ? 2167 HOH B O   1 
HETATM 8985 O  O   . HOH AA 5 .   ? -9.271  5.076   55.168  1.00 36.37 ? 2168 HOH B O   1 
HETATM 8986 O  O   . HOH AA 5 .   ? -8.568  8.453   54.977  1.00 32.31 ? 2169 HOH B O   1 
HETATM 8987 O  O   . HOH AA 5 .   ? -19.306 8.396   50.644  1.00 29.85 ? 2170 HOH B O   1 
HETATM 8988 O  O   . HOH AA 5 .   ? -20.238 11.836  45.462  1.00 26.23 ? 2171 HOH B O   1 
HETATM 8989 O  O   . HOH AA 5 .   ? -21.524 11.771  42.873  1.00 23.08 ? 2172 HOH B O   1 
HETATM 8990 O  O   . HOH AA 5 .   ? -20.374 14.678  41.583  1.00 31.33 ? 2173 HOH B O   1 
HETATM 8991 O  O   . HOH AA 5 .   ? -24.301 16.228  41.165  1.00 38.75 ? 2174 HOH B O   1 
HETATM 8992 O  O   . HOH AA 5 .   ? -25.049 10.254  39.582  1.00 24.49 ? 2175 HOH B O   1 
HETATM 8993 O  O   . HOH AA 5 .   ? -25.411 13.021  35.801  1.00 30.00 ? 2176 HOH B O   1 
HETATM 8994 O  O   . HOH AA 5 .   ? -24.697 5.527   34.078  1.00 15.95 ? 2177 HOH B O   1 
HETATM 8995 O  O   . HOH AA 5 .   ? -25.195 13.234  32.885  1.00 13.85 ? 2178 HOH B O   1 
HETATM 8996 O  O   . HOH AA 5 .   ? -24.201 7.739   26.681  1.00 28.55 ? 2179 HOH B O   1 
HETATM 8997 O  O   . HOH AA 5 .   ? -25.329 7.129   29.787  1.00 34.99 ? 2180 HOH B O   1 
HETATM 8998 O  O   . HOH AA 5 .   ? -27.824 12.334  23.174  1.00 46.21 ? 2181 HOH B O   1 
HETATM 8999 O  O   . HOH AA 5 .   ? -22.992 12.154  21.752  1.00 38.51 ? 2182 HOH B O   1 
HETATM 9000 O  O   . HOH AA 5 .   ? -25.378 8.638   23.742  1.00 36.75 ? 2183 HOH B O   1 
HETATM 9001 O  O   . HOH AA 5 .   ? -10.840 9.476   24.858  1.00 9.08  ? 2184 HOH B O   1 
HETATM 9002 O  O   . HOH AA 5 .   ? -9.912  15.700  21.775  1.00 7.57  ? 2185 HOH B O   1 
HETATM 9003 O  O   . HOH AA 5 .   ? -11.298 18.634  24.736  1.00 11.48 ? 2186 HOH B O   1 
HETATM 9004 O  O   . HOH AA 5 .   ? -17.895 20.036  31.023  1.00 19.79 ? 2187 HOH B O   1 
HETATM 9005 O  O   . HOH AA 5 .   ? -18.635 22.741  28.924  1.00 40.35 ? 2188 HOH B O   1 
HETATM 9006 O  O   . HOH AA 5 .   ? -15.607 22.990  29.628  1.00 33.07 ? 2189 HOH B O   1 
HETATM 9007 O  O   . HOH AA 5 .   ? -20.930 20.373  23.306  1.00 35.13 ? 2190 HOH B O   1 
HETATM 9008 O  O   . HOH AA 5 .   ? -28.551 12.267  29.538  1.00 42.30 ? 2191 HOH B O   1 
HETATM 9009 O  O   . HOH AA 5 .   ? -22.341 20.168  27.845  1.00 18.27 ? 2192 HOH B O   1 
HETATM 9010 O  O   . HOH AA 5 .   ? -24.857 17.817  25.299  1.00 38.14 ? 2193 HOH B O   1 
HETATM 9011 O  O   . HOH AA 5 .   ? -19.833 16.425  19.554  1.00 32.08 ? 2194 HOH B O   1 
HETATM 9012 O  O   . HOH AA 5 .   ? -18.971 20.144  20.721  1.00 23.84 ? 2195 HOH B O   1 
HETATM 9013 O  O   . HOH AA 5 .   ? -10.529 22.556  20.286  1.00 15.44 ? 2196 HOH B O   1 
HETATM 9014 O  O   . HOH AA 5 .   ? -15.927 19.604  19.537  1.00 18.45 ? 2197 HOH B O   1 
HETATM 9015 O  O   . HOH AA 5 .   ? -6.002  22.844  20.035  1.00 40.22 ? 2198 HOH B O   1 
HETATM 9016 O  O   . HOH AA 5 .   ? -4.692  20.783  25.230  1.00 38.54 ? 2199 HOH B O   1 
HETATM 9017 O  O   . HOH AA 5 .   ? -8.660  21.012  25.772  1.00 10.99 ? 2200 HOH B O   1 
HETATM 9018 O  O   . HOH AA 5 .   ? -5.478  23.216  23.533  1.00 40.73 ? 2201 HOH B O   1 
HETATM 9019 O  O   . HOH AA 5 .   ? -4.142  20.703  16.799  1.00 23.88 ? 2202 HOH B O   1 
HETATM 9020 O  O   . HOH AA 5 .   ? -8.764  21.582  18.313  1.00 13.71 ? 2203 HOH B O   1 
HETATM 9021 O  O   . HOH AA 5 .   ? -0.951  17.977  23.235  1.00 21.34 ? 2204 HOH B O   1 
HETATM 9022 O  O   . HOH AA 5 .   ? -2.742  22.812  22.728  1.00 34.04 ? 2205 HOH B O   1 
HETATM 9023 O  O   . HOH AA 5 .   ? -9.336  10.397  16.953  1.00 8.26  ? 2206 HOH B O   1 
HETATM 9024 O  O   . HOH AA 5 .   ? -0.487  6.791   16.283  1.00 10.09 ? 2207 HOH B O   1 
HETATM 9025 O  O   . HOH AA 5 .   ? -1.417  -2.262  13.156  1.00 10.69 ? 2208 HOH B O   1 
HETATM 9026 O  O   . HOH AA 5 .   ? -4.852  -3.892  13.512  1.00 12.39 ? 2209 HOH B O   1 
HETATM 9027 O  O   . HOH AA 5 .   ? -9.973  -8.108  19.398  1.00 28.83 ? 2210 HOH B O   1 
HETATM 9028 O  O   . HOH AA 5 .   ? -8.780  -6.272  27.758  1.00 11.65 ? 2211 HOH B O   1 
HETATM 9029 O  O   . HOH AA 5 .   ? -7.309  -10.449 22.138  1.00 31.20 ? 2212 HOH B O   1 
HETATM 9030 O  O   . HOH AA 5 .   ? -12.201 -9.359  22.369  1.00 27.43 ? 2213 HOH B O   1 
HETATM 9031 O  O   . HOH AA 5 .   ? -10.202 -10.140 25.011  1.00 27.77 ? 2214 HOH B O   1 
HETATM 9032 O  O   . HOH AA 5 .   ? -20.771 -6.315  40.609  1.00 35.06 ? 2215 HOH B O   1 
HETATM 9033 O  O   . HOH AA 5 .   ? -18.345 -6.299  38.060  1.00 16.74 ? 2216 HOH B O   1 
HETATM 9034 O  O   . HOH AA 5 .   ? -23.903 -5.322  39.070  1.00 35.43 ? 2217 HOH B O   1 
HETATM 9035 O  O   . HOH AA 5 .   ? -14.397 -8.144  40.732  1.00 34.07 ? 2218 HOH B O   1 
HETATM 9036 O  O   . HOH AA 5 .   ? -15.130 -4.354  43.915  1.00 21.52 ? 2219 HOH B O   1 
HETATM 9037 O  O   . HOH AA 5 .   ? -10.422 -7.076  44.080  1.00 31.41 ? 2220 HOH B O   1 
HETATM 9038 O  O   . HOH AA 5 .   ? -8.220  -12.479 44.932  1.00 46.23 ? 2221 HOH B O   1 
HETATM 9039 O  O   . HOH AA 5 .   ? -5.355  -15.456 35.765  1.00 22.15 ? 2222 HOH B O   1 
HETATM 9040 O  O   . HOH AA 5 .   ? -5.622  -12.262 44.657  1.00 39.12 ? 2223 HOH B O   1 
HETATM 9041 O  O   . HOH AA 5 .   ? -11.132 -9.901  33.320  1.00 17.80 ? 2224 HOH B O   1 
HETATM 9042 O  O   . HOH AA 5 .   ? -12.825 -14.887 39.083  1.00 27.77 ? 2225 HOH B O   1 
HETATM 9043 O  O   . HOH AA 5 .   ? -8.361  -16.694 32.341  1.00 37.51 ? 2226 HOH B O   1 
HETATM 9044 O  O   . HOH AA 5 .   ? -9.355  -14.868 36.230  1.00 25.42 ? 2227 HOH B O   1 
HETATM 9045 O  O   . HOH AA 5 .   ? -8.630  -8.781  26.605  1.00 24.65 ? 2228 HOH B O   1 
HETATM 9046 O  O   . HOH AA 5 .   ? 0.551   -10.421 25.411  1.00 45.20 ? 2229 HOH B O   1 
HETATM 9047 O  O   . HOH AA 5 .   ? 3.021   -11.935 28.314  1.00 46.27 ? 2230 HOH B O   1 
HETATM 9048 O  O   . HOH AA 5 .   ? -9.581  -12.014 23.138  1.00 39.10 ? 2231 HOH B O   1 
HETATM 9049 O  O   . HOH AA 5 .   ? -12.199 -15.623 31.783  1.00 32.67 ? 2232 HOH B O   1 
HETATM 9050 O  O   . HOH AA 5 .   ? -5.812  -16.887 29.405  1.00 33.28 ? 2233 HOH B O   1 
HETATM 9051 O  O   . HOH AA 5 .   ? -15.953 -12.945 28.324  1.00 38.06 ? 2234 HOH B O   1 
HETATM 9052 O  O   . HOH AA 5 .   ? -12.981 -14.822 28.139  1.00 29.32 ? 2235 HOH B O   1 
HETATM 9053 O  O   . HOH AA 5 .   ? -18.710 -11.884 34.308  1.00 33.49 ? 2236 HOH B O   1 
HETATM 9054 O  O   . HOH AA 5 .   ? -19.823 -8.669  34.631  1.00 24.80 ? 2237 HOH B O   1 
HETATM 9055 O  O   . HOH AA 5 .   ? -21.891 -10.106 31.302  1.00 42.94 ? 2238 HOH B O   1 
HETATM 9056 O  O   . HOH AA 5 .   ? -21.243 -9.064  29.068  1.00 32.25 ? 2239 HOH B O   1 
HETATM 9057 O  O   . HOH AA 5 .   ? -23.913 -7.753  36.739  1.00 33.09 ? 2240 HOH B O   1 
HETATM 9058 O  O   . HOH AA 5 .   ? -24.681 -5.817  31.622  1.00 28.90 ? 2241 HOH B O   1 
HETATM 9059 O  O   . HOH AA 5 .   ? -21.647 -8.631  38.327  1.00 36.82 ? 2242 HOH B O   1 
HETATM 9060 O  O   . HOH AA 5 .   ? -22.014 -4.319  28.843  1.00 29.81 ? 2243 HOH B O   1 
HETATM 9061 O  O   . HOH AA 5 .   ? -17.247 -10.985 27.092  1.00 23.79 ? 2244 HOH B O   1 
HETATM 9062 O  O   . HOH AA 5 .   ? -22.962 -9.339  20.563  1.00 27.48 ? 2245 HOH B O   1 
HETATM 9063 O  O   . HOH AA 5 .   ? -13.320 -13.408 25.422  1.00 39.76 ? 2246 HOH B O   1 
HETATM 9064 O  O   . HOH AA 5 .   ? -24.440 -5.440  25.601  1.00 36.43 ? 2247 HOH B O   1 
HETATM 9065 O  O   . HOH AA 5 .   ? -21.391 -3.460  26.316  1.00 15.22 ? 2248 HOH B O   1 
HETATM 9066 O  O   . HOH AA 5 .   ? -19.826 -0.405  12.535  1.00 27.85 ? 2249 HOH B O   1 
HETATM 9067 O  O   . HOH AA 5 .   ? -23.510 -0.807  17.982  1.00 29.13 ? 2250 HOH B O   1 
HETATM 9068 O  O   . HOH AA 5 .   ? -23.382 1.621   15.187  1.00 34.93 ? 2251 HOH B O   1 
HETATM 9069 O  O   . HOH AA 5 .   ? -21.808 3.526   13.960  1.00 19.43 ? 2252 HOH B O   1 
HETATM 9070 O  O   . HOH AA 5 .   ? -20.280 10.696  11.251  1.00 30.13 ? 2253 HOH B O   1 
HETATM 9071 O  O   . HOH AA 5 .   ? -18.615 8.025   9.818   1.00 27.02 ? 2254 HOH B O   1 
HETATM 9072 O  O   . HOH AA 5 .   ? -15.279 10.882  7.763   1.00 34.47 ? 2255 HOH B O   1 
HETATM 9073 O  O   . HOH AA 5 .   ? -16.370 2.960   9.730   1.00 23.12 ? 2256 HOH B O   1 
HETATM 9074 O  O   . HOH AA 5 .   ? -12.772 -2.280  7.079   1.00 41.08 ? 2257 HOH B O   1 
HETATM 9075 O  O   . HOH AA 5 .   ? -15.501 0.443   9.549   1.00 16.73 ? 2258 HOH B O   1 
HETATM 9076 O  O   . HOH AA 5 .   ? -10.980 -4.691  6.424   1.00 41.97 ? 2259 HOH B O   1 
HETATM 9077 O  O   . HOH AA 5 .   ? -5.780  -10.570 12.613  1.00 33.50 ? 2260 HOH B O   1 
HETATM 9078 O  O   . HOH AA 5 .   ? 2.008   -9.052  15.539  1.00 32.95 ? 2261 HOH B O   1 
HETATM 9079 O  O   . HOH AA 5 .   ? -0.943  -10.450 12.660  1.00 21.08 ? 2262 HOH B O   1 
HETATM 9080 O  O   . HOH AA 5 .   ? 2.832   -6.921  17.143  1.00 29.47 ? 2263 HOH B O   1 
HETATM 9081 O  O   . HOH AA 5 .   ? 1.315   -7.097  21.141  1.00 27.47 ? 2264 HOH B O   1 
HETATM 9082 O  O   . HOH AA 5 .   ? -0.075  -11.018 18.969  1.00 42.08 ? 2265 HOH B O   1 
HETATM 9083 O  O   . HOH AA 5 .   ? -18.337 -2.671  52.354  1.00 48.11 ? 2266 HOH B O   1 
HETATM 9084 O  O   . HOH AA 5 .   ? -6.447  21.417  27.831  1.00 35.47 ? 2267 HOH B O   1 
HETATM 9085 O  O   . HOH AA 5 .   ? -11.750 21.678  30.697  1.00 35.11 ? 2268 HOH B O   1 
HETATM 9086 O  O   . HOH AA 5 .   ? -8.835  21.050  33.152  1.00 32.92 ? 2269 HOH B O   1 
HETATM 9087 O  O   . HOH AA 5 .   ? -7.234  19.106  34.206  1.00 36.02 ? 2270 HOH B O   1 
HETATM 9088 O  O   . HOH BA 5 .   ? 8.736   -6.584  -22.543 1.00 45.29 ? 2001 HOH C O   1 
HETATM 9089 O  O   . HOH BA 5 .   ? 14.029  -12.801 -20.299 1.00 19.77 ? 2002 HOH C O   1 
HETATM 9090 O  O   . HOH BA 5 .   ? 19.564  -13.709 -15.621 1.00 36.45 ? 2003 HOH C O   1 
HETATM 9091 O  O   . HOH BA 5 .   ? 23.797  -10.916 -12.053 1.00 29.25 ? 2004 HOH C O   1 
HETATM 9092 O  O   . HOH BA 5 .   ? 13.155  -18.338 -9.337  1.00 29.96 ? 2005 HOH C O   1 
HETATM 9093 O  O   . HOH BA 5 .   ? 17.434  -17.422 -10.828 1.00 34.36 ? 2006 HOH C O   1 
HETATM 9094 O  O   . HOH BA 5 .   ? 16.496  -14.232 -15.550 1.00 15.89 ? 2007 HOH C O   1 
HETATM 9095 O  O   . HOH BA 5 .   ? 19.432  -12.851 -12.848 1.00 22.66 ? 2008 HOH C O   1 
HETATM 9096 O  O   . HOH BA 5 .   ? 31.136  8.695   -5.794  1.00 28.65 ? 2009 HOH C O   1 
HETATM 9097 O  O   . HOH BA 5 .   ? 20.885  -15.688 -7.444  1.00 31.05 ? 2010 HOH C O   1 
HETATM 9098 O  O   . HOH BA 5 .   ? 18.418  -14.887 -10.025 1.00 17.42 ? 2011 HOH C O   1 
HETATM 9099 O  O   . HOH BA 5 .   ? 13.210  -15.576 -4.227  1.00 36.41 ? 2012 HOH C O   1 
HETATM 9100 O  O   . HOH BA 5 .   ? 26.786  7.795   0.544   1.00 16.19 ? 2013 HOH C O   1 
HETATM 9101 O  O   . HOH BA 5 .   ? 25.606  14.484  -12.235 1.00 31.35 ? 2014 HOH C O   1 
HETATM 9102 O  O   . HOH BA 5 .   ? 18.942  11.546  -15.136 1.00 36.12 ? 2015 HOH C O   1 
HETATM 9103 O  O   . HOH BA 5 .   ? 21.363  15.236  -14.146 1.00 33.20 ? 2016 HOH C O   1 
HETATM 9104 O  O   . HOH BA 5 .   ? 22.288  -15.234 -3.273  1.00 36.25 ? 2017 HOH C O   1 
HETATM 9105 O  O   . HOH BA 5 .   ? 23.221  -14.775 -6.507  1.00 37.93 ? 2018 HOH C O   1 
HETATM 9106 O  O   . HOH BA 5 .   ? 24.846  -10.954 -9.732  1.00 29.09 ? 2019 HOH C O   1 
HETATM 9107 O  O   . HOH BA 5 .   ? 22.860  -15.693 -11.553 1.00 35.91 ? 2020 HOH C O   1 
HETATM 9108 O  O   . HOH BA 5 .   ? 16.817  -9.971  -3.270  1.00 19.64 ? 2021 HOH C O   1 
HETATM 9109 O  O   . HOH BA 5 .   ? 4.915   -3.549  -19.812 1.00 35.12 ? 2022 HOH C O   1 
HETATM 9110 O  O   . HOH BA 5 .   ? 29.787  5.613   -2.126  1.00 16.36 ? 2023 HOH C O   1 
HETATM 9111 O  O   . HOH BA 5 .   ? 15.074  -3.766  17.338  1.00 38.11 ? 2024 HOH C O   1 
HETATM 9112 O  O   . HOH BA 5 .   ? 23.772  -8.753  11.690  1.00 44.58 ? 2025 HOH C O   1 
HETATM 9113 O  O   . HOH BA 5 .   ? 31.958  8.103   -8.507  1.00 40.42 ? 2026 HOH C O   1 
HETATM 9114 O  O   . HOH BA 5 .   ? 28.353  8.094   -1.791  1.00 17.31 ? 2027 HOH C O   1 
HETATM 9115 O  O   . HOH BA 5 .   ? 29.081  10.299  -4.868  1.00 26.36 ? 2028 HOH C O   1 
HETATM 9116 O  O   . HOH BA 5 .   ? 26.223  10.221  1.320   1.00 26.70 ? 2029 HOH C O   1 
HETATM 9117 O  O   . HOH BA 5 .   ? 27.850  10.825  -8.206  1.00 30.90 ? 2030 HOH C O   1 
HETATM 9118 O  O   . HOH BA 5 .   ? 23.217  15.353  -0.423  1.00 37.12 ? 2031 HOH C O   1 
HETATM 9119 O  O   . HOH BA 5 .   ? 24.231  13.723  1.395   1.00 30.97 ? 2032 HOH C O   1 
HETATM 9120 O  O   . HOH BA 5 .   ? 22.721  7.728   -6.397  1.00 12.95 ? 2033 HOH C O   1 
HETATM 9121 O  O   . HOH BA 5 .   ? 26.069  9.277   5.015   1.00 31.10 ? 2034 HOH C O   1 
HETATM 9122 O  O   . HOH BA 5 .   ? 25.381  12.936  -9.866  1.00 18.92 ? 2035 HOH C O   1 
HETATM 9123 O  O   . HOH BA 5 .   ? 19.426  13.294  -13.233 1.00 25.08 ? 2036 HOH C O   1 
HETATM 9124 O  O   . HOH BA 5 .   ? 20.780  7.197   13.940  1.00 30.03 ? 2037 HOH C O   1 
HETATM 9125 O  O   . HOH BA 5 .   ? 18.371  11.330  12.298  1.00 33.48 ? 2038 HOH C O   1 
HETATM 9126 O  O   . HOH BA 5 .   ? 21.339  8.662   -15.533 1.00 24.89 ? 2039 HOH C O   1 
HETATM 9127 O  O   . HOH BA 5 .   ? 26.878  10.901  -10.890 1.00 29.52 ? 2040 HOH C O   1 
HETATM 9128 O  O   . HOH BA 5 .   ? 24.446  4.642   -7.052  1.00 13.77 ? 2041 HOH C O   1 
HETATM 9129 O  O   . HOH BA 5 .   ? 15.337  7.247   -17.026 1.00 19.24 ? 2042 HOH C O   1 
HETATM 9130 O  O   . HOH BA 5 .   ? -3.731  18.049  -11.637 1.00 30.21 ? 2043 HOH C O   1 
HETATM 9131 O  O   . HOH BA 5 .   ? 12.152  7.129   -15.443 1.00 25.23 ? 2044 HOH C O   1 
HETATM 9132 O  O   . HOH BA 5 .   ? 10.474  5.223   -14.576 1.00 32.62 ? 2045 HOH C O   1 
HETATM 9133 O  O   . HOH BA 5 .   ? 8.797   3.192   -15.058 1.00 17.81 ? 2046 HOH C O   1 
HETATM 9134 O  O   . HOH BA 5 .   ? 15.705  16.547  1.556   1.00 33.00 ? 2047 HOH C O   1 
HETATM 9135 O  O   . HOH BA 5 .   ? 8.383   -5.333  -13.906 1.00 16.85 ? 2048 HOH C O   1 
HETATM 9136 O  O   . HOH BA 5 .   ? 6.316   -4.901  -17.770 1.00 27.71 ? 2049 HOH C O   1 
HETATM 9137 O  O   . HOH BA 5 .   ? 1.864   1.434   -17.866 1.00 37.32 ? 2050 HOH C O   1 
HETATM 9138 O  O   . HOH BA 5 .   ? 5.835   1.241   -15.004 1.00 28.25 ? 2051 HOH C O   1 
HETATM 9139 O  O   . HOH BA 5 .   ? 5.339   11.825  12.559  1.00 24.31 ? 2052 HOH C O   1 
HETATM 9140 O  O   . HOH BA 5 .   ? 3.605   17.888  1.852   1.00 37.06 ? 2053 HOH C O   1 
HETATM 9141 O  O   . HOH BA 5 .   ? -7.660  -1.297  -8.951  1.00 31.41 ? 2054 HOH C O   1 
HETATM 9142 O  O   . HOH BA 5 .   ? -9.625  1.122   -11.224 1.00 36.41 ? 2055 HOH C O   1 
HETATM 9143 O  O   . HOH BA 5 .   ? 2.943   12.333  11.450  1.00 24.61 ? 2056 HOH C O   1 
HETATM 9144 O  O   . HOH BA 5 .   ? 9.152   -2.977  16.988  1.00 49.60 ? 2057 HOH C O   1 
HETATM 9145 O  O   . HOH BA 5 .   ? 19.520  5.406   15.705  1.00 35.16 ? 2058 HOH C O   1 
HETATM 9146 O  O   . HOH BA 5 .   ? 18.332  -5.434  12.994  1.00 27.92 ? 2059 HOH C O   1 
HETATM 9147 O  O   . HOH BA 5 .   ? 14.739  -4.015  14.855  1.00 35.42 ? 2060 HOH C O   1 
HETATM 9148 O  O   . HOH BA 5 .   ? 25.193  5.746   14.471  1.00 37.16 ? 2061 HOH C O   1 
HETATM 9149 O  O   . HOH BA 5 .   ? 23.534  -6.208  9.886   1.00 36.03 ? 2062 HOH C O   1 
HETATM 9150 O  O   . HOH BA 5 .   ? -10.724 -0.267  -1.614  1.00 18.18 ? 2063 HOH C O   1 
HETATM 9151 O  O   . HOH BA 5 .   ? -6.335  -2.393  -7.068  1.00 19.82 ? 2064 HOH C O   1 
HETATM 9152 O  O   . HOH BA 5 .   ? -15.053 7.443   0.161   1.00 34.82 ? 2065 HOH C O   1 
HETATM 9153 O  O   . HOH BA 5 .   ? 15.898  -8.148  5.270   1.00 30.24 ? 2066 HOH C O   1 
HETATM 9154 O  O   . HOH BA 5 .   ? -5.915  -7.729  8.377   1.00 31.54 ? 2067 HOH C O   1 
HETATM 9155 O  O   . HOH BA 5 .   ? 25.999  -2.312  9.156   1.00 12.30 ? 2068 HOH C O   1 
HETATM 9156 O  O   . HOH BA 5 .   ? 19.871  1.094   8.111   1.00 12.40 ? 2069 HOH C O   1 
HETATM 9157 O  O   . HOH BA 5 .   ? 26.475  6.700   4.758   1.00 17.27 ? 2070 HOH C O   1 
HETATM 9158 O  O   . HOH BA 5 .   ? 25.600  5.742   2.235   1.00 15.64 ? 2071 HOH C O   1 
HETATM 9159 O  O   . HOH BA 5 .   ? 19.032  6.116   9.195   1.00 22.85 ? 2072 HOH C O   1 
HETATM 9160 O  O   . HOH BA 5 .   ? 19.393  4.119   6.345   1.00 15.15 ? 2073 HOH C O   1 
HETATM 9161 O  O   . HOH BA 5 .   ? 24.737  7.840   8.185   1.00 18.49 ? 2074 HOH C O   1 
HETATM 9162 O  O   . HOH BA 5 .   ? 23.594  10.563  5.597   1.00 11.74 ? 2075 HOH C O   1 
HETATM 9163 O  O   . HOH BA 5 .   ? 20.386  7.483   11.042  1.00 20.46 ? 2076 HOH C O   1 
HETATM 9164 O  O   . HOH BA 5 .   ? 18.318  9.382   10.581  1.00 13.30 ? 2077 HOH C O   1 
HETATM 9165 O  O   . HOH BA 5 .   ? -7.575  13.966  -8.341  1.00 26.63 ? 2078 HOH C O   1 
HETATM 9166 O  O   . HOH BA 5 .   ? 16.353  8.604   6.500   1.00 14.93 ? 2079 HOH C O   1 
HETATM 9167 O  O   . HOH BA 5 .   ? 17.426  14.704  5.373   1.00 23.86 ? 2080 HOH C O   1 
HETATM 9168 O  O   . HOH BA 5 .   ? 16.546  1.387   4.478   1.00 14.72 ? 2081 HOH C O   1 
HETATM 9169 O  O   . HOH BA 5 .   ? 15.778  7.729   -3.955  1.00 20.87 ? 2082 HOH C O   1 
HETATM 9170 O  O   . HOH BA 5 .   ? 12.831  5.931   -5.151  1.00 9.23  ? 2083 HOH C O   1 
HETATM 9171 O  O   . HOH BA 5 .   ? 16.897  19.633  -7.907  1.00 38.71 ? 2084 HOH C O   1 
HETATM 9172 O  O   . HOH BA 5 .   ? 7.660   10.187  -6.184  1.00 11.44 ? 2085 HOH C O   1 
HETATM 9173 O  O   . HOH BA 5 .   ? 16.918  21.044  -5.048  1.00 47.83 ? 2086 HOH C O   1 
HETATM 9174 O  O   . HOH BA 5 .   ? 23.281  17.431  -7.882  1.00 37.24 ? 2087 HOH C O   1 
HETATM 9175 O  O   . HOH BA 5 .   ? 20.481  16.287  3.003   1.00 35.64 ? 2088 HOH C O   1 
HETATM 9176 O  O   . HOH BA 5 .   ? 5.016   13.915  -12.397 1.00 15.45 ? 2089 HOH C O   1 
HETATM 9177 O  O   . HOH BA 5 .   ? -1.690  11.266  -14.121 1.00 18.93 ? 2090 HOH C O   1 
HETATM 9178 O  O   . HOH BA 5 .   ? 17.384  -14.762 -1.467  1.00 29.04 ? 2091 HOH C O   1 
HETATM 9179 O  O   . HOH BA 5 .   ? 2.679   11.398  -20.563 1.00 37.07 ? 2092 HOH C O   1 
HETATM 9180 O  O   . HOH BA 5 .   ? -2.614  15.058  -14.693 1.00 37.63 ? 2093 HOH C O   1 
HETATM 9181 O  O   . HOH BA 5 .   ? 6.066   14.705  -18.996 1.00 37.71 ? 2094 HOH C O   1 
HETATM 9182 O  O   . HOH BA 5 .   ? 0.432   16.873  -17.844 1.00 40.52 ? 2095 HOH C O   1 
HETATM 9183 O  O   . HOH BA 5 .   ? -8.736  -7.505  -3.100  1.00 29.65 ? 2096 HOH C O   1 
HETATM 9184 O  O   . HOH BA 5 .   ? -1.560  17.196  -10.298 1.00 22.62 ? 2097 HOH C O   1 
HETATM 9185 O  O   . HOH BA 5 .   ? 4.551   15.348  -14.777 1.00 21.84 ? 2098 HOH C O   1 
HETATM 9186 O  O   . HOH BA 5 .   ? -3.981  15.369  -12.560 1.00 23.33 ? 2099 HOH C O   1 
HETATM 9187 O  O   . HOH BA 5 .   ? -0.057  13.341  -6.927  1.00 10.87 ? 2100 HOH C O   1 
HETATM 9188 O  O   . HOH BA 5 .   ? 13.052  15.312  3.119   1.00 23.02 ? 2101 HOH C O   1 
HETATM 9189 O  O   . HOH BA 5 .   ? 16.729  6.397   7.735   1.00 21.29 ? 2102 HOH C O   1 
HETATM 9190 O  O   . HOH BA 5 .   ? 17.899  3.698   8.752   1.00 24.35 ? 2103 HOH C O   1 
HETATM 9191 O  O   . HOH BA 5 .   ? 9.480   15.171  4.346   1.00 33.76 ? 2104 HOH C O   1 
HETATM 9192 O  O   . HOH BA 5 .   ? 17.103  12.337  8.257   1.00 17.88 ? 2105 HOH C O   1 
HETATM 9193 O  O   . HOH BA 5 .   ? 16.232  13.761  12.063  1.00 33.66 ? 2106 HOH C O   1 
HETATM 9194 O  O   . HOH BA 5 .   ? 25.161  -15.687 0.874   1.00 30.46 ? 2107 HOH C O   1 
HETATM 9195 O  O   . HOH BA 5 .   ? 27.336  -14.807 -3.050  1.00 35.29 ? 2108 HOH C O   1 
HETATM 9196 O  O   . HOH BA 5 .   ? 14.509  9.351   14.373  1.00 27.13 ? 2109 HOH C O   1 
HETATM 9197 O  O   . HOH BA 5 .   ? 10.726  5.918   15.912  1.00 26.29 ? 2110 HOH C O   1 
HETATM 9198 O  O   . HOH BA 5 .   ? 9.006   10.977  9.292   1.00 31.26 ? 2111 HOH C O   1 
HETATM 9199 O  O   . HOH BA 5 .   ? 11.061  8.822   15.598  1.00 31.76 ? 2112 HOH C O   1 
HETATM 9200 O  O   . HOH BA 5 .   ? 7.646   12.499  11.399  1.00 26.03 ? 2113 HOH C O   1 
HETATM 9201 O  O   . HOH BA 5 .   ? 9.535   8.754   7.103   1.00 24.86 ? 2114 HOH C O   1 
HETATM 9202 O  O   . HOH BA 5 .   ? -17.539 -6.563  -1.549  1.00 51.66 ? 2115 HOH C O   1 
HETATM 9203 O  O   . HOH BA 5 .   ? 15.343  1.341   7.010   1.00 19.01 ? 2116 HOH C O   1 
HETATM 9204 O  O   . HOH BA 5 .   ? 6.926   18.069  -4.802  1.00 24.58 ? 2117 HOH C O   1 
HETATM 9205 O  O   . HOH BA 5 .   ? 3.559   15.664  -1.507  1.00 14.21 ? 2118 HOH C O   1 
HETATM 9206 O  O   . HOH BA 5 .   ? 2.109   15.697  2.127   1.00 17.74 ? 2119 HOH C O   1 
HETATM 9207 O  O   . HOH BA 5 .   ? -3.015  15.210  4.353   1.00 15.14 ? 2120 HOH C O   1 
HETATM 9208 O  O   . HOH BA 5 .   ? -0.258  15.161  4.192   1.00 14.68 ? 2121 HOH C O   1 
HETATM 9209 O  O   . HOH BA 5 .   ? -2.668  12.578  5.005   1.00 14.02 ? 2122 HOH C O   1 
HETATM 9210 O  O   . HOH BA 5 .   ? 0.222   12.626  8.353   1.00 22.31 ? 2123 HOH C O   1 
HETATM 9211 O  O   . HOH BA 5 .   ? 6.830   12.743  8.462   1.00 30.87 ? 2124 HOH C O   1 
HETATM 9212 O  O   . HOH BA 5 .   ? 3.019   12.564  8.444   1.00 29.53 ? 2125 HOH C O   1 
HETATM 9213 O  O   . HOH BA 5 .   ? 0.148   10.057  9.668   1.00 16.57 ? 2126 HOH C O   1 
HETATM 9214 O  O   . HOH BA 5 .   ? 4.266   9.376   13.006  1.00 18.56 ? 2127 HOH C O   1 
HETATM 9215 O  O   . HOH BA 5 .   ? 5.700   10.520  17.848  1.00 20.23 ? 2128 HOH C O   1 
HETATM 9216 O  O   . HOH BA 5 .   ? 5.655   13.151  14.918  1.00 31.90 ? 2129 HOH C O   1 
HETATM 9217 O  O   . HOH BA 5 .   ? 10.237  9.888   17.861  1.00 36.05 ? 2130 HOH C O   1 
HETATM 9218 O  O   . HOH BA 5 .   ? 14.118  3.540   15.503  1.00 23.14 ? 2131 HOH C O   1 
HETATM 9219 O  O   . HOH BA 5 .   ? 8.263   -0.213  17.440  1.00 18.41 ? 2132 HOH C O   1 
HETATM 9220 O  O   . HOH BA 5 .   ? 17.073  4.007   15.882  1.00 39.07 ? 2133 HOH C O   1 
HETATM 9221 O  O   . HOH BA 5 .   ? 15.746  -3.387  10.528  1.00 16.08 ? 2134 HOH C O   1 
HETATM 9222 O  O   . HOH BA 5 .   ? 16.682  -0.157  8.868   1.00 20.25 ? 2135 HOH C O   1 
HETATM 9223 O  O   . HOH BA 5 .   ? 17.667  1.681   10.604  1.00 19.77 ? 2136 HOH C O   1 
HETATM 9224 O  O   . HOH BA 5 .   ? 16.516  -3.406  13.116  1.00 19.17 ? 2137 HOH C O   1 
HETATM 9225 O  O   . HOH BA 5 .   ? 21.181  1.046   16.583  1.00 22.53 ? 2138 HOH C O   1 
HETATM 9226 O  O   . HOH BA 5 .   ? 25.363  2.865   14.555  1.00 23.99 ? 2139 HOH C O   1 
HETATM 9227 O  O   . HOH BA 5 .   ? 22.930  -4.199  11.772  1.00 31.43 ? 2140 HOH C O   1 
HETATM 9228 O  O   . HOH BA 5 .   ? 18.620  -0.124  5.862   1.00 10.95 ? 2141 HOH C O   1 
HETATM 9229 O  O   . HOH BA 5 .   ? 17.879  -6.572  10.336  1.00 26.50 ? 2142 HOH C O   1 
HETATM 9230 O  O   . HOH BA 5 .   ? 9.581   -9.151  -0.035  1.00 11.99 ? 2143 HOH C O   1 
HETATM 9231 O  O   . HOH BA 5 .   ? -1.400  -5.146  4.543   1.00 14.41 ? 2144 HOH C O   1 
HETATM 9232 O  O   . HOH BA 5 .   ? -8.235  -6.150  3.558   1.00 43.14 ? 2145 HOH C O   1 
HETATM 9233 O  O   . HOH BA 5 .   ? -11.656 -4.091  3.783   1.00 38.19 ? 2146 HOH C O   1 
HETATM 9234 O  O   . HOH BA 5 .   ? -12.792 3.456   -3.032  1.00 22.44 ? 2147 HOH C O   1 
HETATM 9235 O  O   . HOH BA 5 .   ? -13.676 -0.691  3.318   1.00 33.99 ? 2148 HOH C O   1 
HETATM 9236 O  O   . HOH BA 5 .   ? -15.326 4.591   0.856   1.00 28.85 ? 2149 HOH C O   1 
HETATM 9237 O  O   . HOH BA 5 .   ? -14.204 1.721   5.234   1.00 27.64 ? 2150 HOH C O   1 
HETATM 9238 O  O   . HOH BA 5 .   ? -4.279  -1.285  3.984   1.00 11.47 ? 2151 HOH C O   1 
HETATM 9239 O  O   . HOH BA 5 .   ? -5.972  -2.559  5.677   1.00 14.97 ? 2152 HOH C O   1 
HETATM 9240 O  O   . HOH BA 5 .   ? -3.126  -7.014  6.856   1.00 22.61 ? 2153 HOH C O   1 
HETATM 9241 O  O   . HOH BA 5 .   ? 1.591   -4.104  4.247   1.00 25.78 ? 2154 HOH C O   1 
HETATM 9242 O  O   . HOH BA 5 .   ? 8.811   -10.578 13.008  1.00 35.88 ? 2155 HOH C O   1 
HETATM 9243 O  O   . HOH BA 5 .   ? 15.147  -7.814  7.802   1.00 25.79 ? 2156 HOH C O   1 
HETATM 9244 O  O   . HOH BA 5 .   ? 12.216  -5.180  13.726  1.00 32.78 ? 2157 HOH C O   1 
HETATM 9245 O  O   . HOH BA 5 .   ? 7.760   -6.694  7.004   1.00 10.02 ? 2158 HOH C O   1 
HETATM 9246 O  O   . HOH BA 5 .   ? 3.766   -10.101 13.237  1.00 27.24 ? 2159 HOH C O   1 
HETATM 9247 O  O   . HOH BA 5 .   ? 0.299   -1.347  9.946   1.00 15.91 ? 2160 HOH C O   1 
HETATM 9248 O  O   . HOH BA 5 .   ? 0.923   2.155   9.018   1.00 17.09 ? 2161 HOH C O   1 
HETATM 9249 O  O   . HOH BA 5 .   ? -5.800  -5.044  9.382   1.00 23.22 ? 2162 HOH C O   1 
HETATM 9250 O  O   . HOH BA 5 .   ? -1.553  -3.216  10.519  1.00 15.53 ? 2163 HOH C O   1 
HETATM 9251 O  O   . HOH BA 5 .   ? 0.853   10.187  12.236  1.00 19.64 ? 2164 HOH C O   1 
HETATM 9252 O  O   . HOH BA 5 .   ? -4.108  11.563  7.055   1.00 21.23 ? 2165 HOH C O   1 
HETATM 9253 O  O   . HOH BA 5 .   ? -9.001  11.791  -1.469  1.00 21.29 ? 2166 HOH C O   1 
HETATM 9254 O  O   . HOH BA 5 .   ? -6.122  12.694  2.903   1.00 32.72 ? 2167 HOH C O   1 
HETATM 9255 O  O   . HOH BA 5 .   ? -10.464 14.612  -4.929  1.00 32.73 ? 2168 HOH C O   1 
HETATM 9256 O  O   . HOH BA 5 .   ? -8.173  15.613  -4.445  1.00 19.86 ? 2169 HOH C O   1 
HETATM 9257 O  O   . HOH BA 5 .   ? -11.737 10.834  -2.376  1.00 36.61 ? 2170 HOH C O   1 
HETATM 9258 O  O   . HOH BA 5 .   ? -11.813 10.270  5.127   1.00 31.41 ? 2171 HOH C O   1 
HETATM 9259 O  O   . HOH BA 5 .   ? -15.058 8.263   6.724   1.00 28.65 ? 2172 HOH C O   1 
HETATM 9260 O  O   . HOH BA 5 .   ? -8.711  9.116   4.429   1.00 17.44 ? 2173 HOH C O   1 
HETATM 9261 O  O   . HOH BA 5 .   ? -14.391 6.471   -4.670  1.00 35.68 ? 2174 HOH C O   1 
HETATM 9262 O  O   . HOH BA 5 .   ? -12.078 8.607   -6.727  1.00 38.12 ? 2175 HOH C O   1 
HETATM 9263 O  O   . HOH BA 5 .   ? -7.540  9.484   -9.275  1.00 20.43 ? 2176 HOH C O   1 
HETATM 9264 O  O   . HOH BA 5 .   ? -9.675  9.405   -7.536  1.00 21.77 ? 2177 HOH C O   1 
HETATM 9265 O  O   . HOH BA 5 .   ? -4.095  12.737  -14.267 1.00 29.75 ? 2178 HOH C O   1 
HETATM 9266 O  O   . HOH BA 5 .   ? -6.002  11.682  -9.477  1.00 22.22 ? 2179 HOH C O   1 
HETATM 9267 O  O   . HOH BA 5 .   ? -7.959  7.801   -11.618 1.00 34.31 ? 2180 HOH C O   1 
HETATM 9268 O  O   . HOH BA 5 .   ? -1.946  9.155   -15.876 1.00 29.52 ? 2181 HOH C O   1 
HETATM 9269 O  O   . HOH BA 5 .   ? 0.988   9.100   -19.493 1.00 34.41 ? 2182 HOH C O   1 
HETATM 9270 O  O   . HOH BA 5 .   ? 0.738   8.922   -16.730 1.00 18.30 ? 2183 HOH C O   1 
HETATM 9271 O  O   . HOH BA 5 .   ? 6.732   3.105   -16.840 1.00 29.93 ? 2184 HOH C O   1 
HETATM 9272 O  O   . HOH BA 5 .   ? 9.033   7.267   -21.949 1.00 44.06 ? 2185 HOH C O   1 
HETATM 9273 O  O   . HOH BA 5 .   ? 7.021   4.462   -19.026 1.00 42.72 ? 2186 HOH C O   1 
HETATM 9274 O  O   . HOH BA 5 .   ? 11.683  7.059   -17.967 1.00 36.91 ? 2187 HOH C O   1 
HETATM 9275 O  O   . HOH BA 5 .   ? 14.974  3.836   -3.928  1.00 12.42 ? 2188 HOH C O   1 
HETATM 9276 O  O   . HOH BA 5 .   ? 16.501  11.776  -6.004  1.00 10.46 ? 2189 HOH C O   1 
HETATM 9277 O  O   . HOH BA 5 .   ? 13.316  14.913  -6.789  1.00 9.71  ? 2190 HOH C O   1 
HETATM 9278 O  O   . HOH BA 5 .   ? 6.795   18.774  -8.561  1.00 41.54 ? 2191 HOH C O   1 
HETATM 9279 O  O   . HOH BA 5 .   ? 13.323  18.970  -8.217  1.00 22.80 ? 2192 HOH C O   1 
HETATM 9280 O  O   . HOH BA 5 .   ? 7.225   18.389  -12.015 1.00 35.15 ? 2193 HOH C O   1 
HETATM 9281 O  O   . HOH BA 5 .   ? 11.750  15.752  -16.387 1.00 32.70 ? 2194 HOH C O   1 
HETATM 9282 O  O   . HOH BA 5 .   ? 6.798   15.636  -16.312 1.00 22.60 ? 2195 HOH C O   1 
HETATM 9283 O  O   . HOH BA 5 .   ? 15.229  11.234  -16.043 1.00 30.68 ? 2196 HOH C O   1 
HETATM 9284 O  O   . HOH BA 5 .   ? 15.245  15.040  -15.182 1.00 33.43 ? 2197 HOH C O   1 
HETATM 9285 O  O   . HOH BA 5 .   ? 16.963  14.717  -12.928 1.00 20.03 ? 2198 HOH C O   1 
HETATM 9286 O  O   . HOH BA 5 .   ? 13.484  17.576  -4.316  1.00 15.17 ? 2199 HOH C O   1 
HETATM 9287 O  O   . HOH BA 5 .   ? 20.029  18.614  -4.303  1.00 36.94 ? 2200 HOH C O   1 
HETATM 9288 O  O   . HOH BA 5 .   ? 17.090  19.478  -2.226  1.00 37.69 ? 2201 HOH C O   1 
HETATM 9289 O  O   . HOH BA 5 .   ? 14.940  17.625  -0.860  1.00 34.45 ? 2202 HOH C O   1 
HETATM 9290 O  O   . HOH BA 5 .   ? 25.388  15.454  -7.980  1.00 39.31 ? 2203 HOH C O   1 
HETATM 9291 O  O   . HOH BA 5 .   ? 20.501  17.372  -6.804  1.00 20.76 ? 2204 HOH C O   1 
HETATM 9292 O  O   . HOH BA 5 .   ? 18.031  15.075  2.530   1.00 24.20 ? 2205 HOH C O   1 
HETATM 9293 O  O   . HOH BA 5 .   ? 20.841  5.992   -6.245  1.00 11.61 ? 2206 HOH C O   1 
HETATM 9294 O  O   . HOH BA 5 .   ? 24.102  3.366   2.186   1.00 10.73 ? 2207 HOH C O   1 
HETATM 9295 O  O   . HOH BA 5 .   ? 26.107  -6.053  1.598   1.00 10.86 ? 2208 HOH C O   1 
HETATM 9296 O  O   . HOH BA 5 .   ? 24.439  -7.986  -1.164  1.00 12.84 ? 2209 HOH C O   1 
HETATM 9297 O  O   . HOH BA 5 .   ? 16.129  -12.960 -2.982  1.00 23.22 ? 2210 HOH C O   1 
HETATM 9298 O  O   . HOH BA 5 .   ? 14.857  -13.615 0.156   1.00 26.22 ? 2211 HOH C O   1 
HETATM 9299 O  O   . HOH BA 5 .   ? 13.079  -12.936 -4.523  1.00 27.98 ? 2212 HOH C O   1 
HETATM 9300 O  O   . HOH BA 5 .   ? -6.155  -8.548  -10.720 1.00 36.33 ? 2213 HOH C O   1 
HETATM 9301 O  O   . HOH BA 5 .   ? -7.784  -5.626  -4.896  1.00 25.03 ? 2214 HOH C O   1 
HETATM 9302 O  O   . HOH BA 5 .   ? -4.142  -4.889  -11.717 1.00 42.98 ? 2215 HOH C O   1 
HETATM 9303 O  O   . HOH BA 5 .   ? -6.830  -8.968  -6.537  1.00 39.85 ? 2216 HOH C O   1 
HETATM 9304 O  O   . HOH BA 5 .   ? -4.575  -9.950  -0.814  1.00 25.47 ? 2217 HOH C O   1 
HETATM 9305 O  O   . HOH BA 5 .   ? -3.150  -9.139  -5.707  1.00 13.73 ? 2218 HOH C O   1 
HETATM 9306 O  O   . HOH BA 5 .   ? -7.513  -5.944  -1.282  1.00 18.63 ? 2219 HOH C O   1 
HETATM 9307 O  O   . HOH BA 5 .   ? -6.269  -8.467  3.452   1.00 26.12 ? 2220 HOH C O   1 
HETATM 9308 O  O   . HOH BA 5 .   ? -2.581  -15.148 11.955  1.00 35.37 ? 2221 HOH C O   1 
HETATM 9309 O  O   . HOH BA 5 .   ? -3.530  -13.571 7.817   1.00 17.70 ? 2222 HOH C O   1 
HETATM 9310 O  O   . HOH BA 5 .   ? -4.373  -18.040 11.730  1.00 20.93 ? 2223 HOH C O   1 
HETATM 9311 O  O   . HOH BA 5 .   ? 2.776   -17.238 6.771   1.00 13.54 ? 2224 HOH C O   1 
HETATM 9312 O  O   . HOH BA 5 .   ? 0.830   -18.849 8.019   1.00 14.47 ? 2225 HOH C O   1 
HETATM 9313 O  O   . HOH BA 5 .   ? 3.266   -12.359 0.085   1.00 10.53 ? 2226 HOH C O   1 
HETATM 9314 O  O   . HOH BA 5 .   ? -3.231  -12.266 -0.634  1.00 27.48 ? 2227 HOH C O   1 
HETATM 9315 O  O   . HOH BA 5 .   ? -3.924  -16.255 0.611   1.00 17.23 ? 2228 HOH C O   1 
HETATM 9316 O  O   . HOH BA 5 .   ? 3.474   -18.697 4.579   1.00 21.50 ? 2229 HOH C O   1 
HETATM 9317 O  O   . HOH BA 5 .   ? 10.607  -11.656 0.036   1.00 22.20 ? 2230 HOH C O   1 
HETATM 9318 O  O   . HOH BA 5 .   ? 15.147  -9.218  9.916   1.00 39.71 ? 2231 HOH C O   1 
HETATM 9319 O  O   . HOH BA 5 .   ? 9.941   -15.365 9.979   1.00 37.67 ? 2232 HOH C O   1 
HETATM 9320 O  O   . HOH BA 5 .   ? 4.852   -17.533 8.280   1.00 33.18 ? 2233 HOH C O   1 
HETATM 9321 O  O   . HOH BA 5 .   ? 6.252   -19.632 6.364   1.00 24.16 ? 2234 HOH C O   1 
HETATM 9322 O  O   . HOH BA 5 .   ? 12.645  -18.858 2.984   1.00 42.05 ? 2235 HOH C O   1 
HETATM 9323 O  O   . HOH BA 5 .   ? 11.574  -13.331 -1.795  1.00 20.51 ? 2236 HOH C O   1 
HETATM 9324 O  O   . HOH BA 5 .   ? 7.523   -17.466 -3.080  1.00 28.11 ? 2237 HOH C O   1 
HETATM 9325 O  O   . HOH BA 5 .   ? -1.206  -13.985 -4.620  1.00 22.67 ? 2238 HOH C O   1 
HETATM 9326 O  O   . HOH BA 5 .   ? -1.095  -11.177 -7.289  1.00 21.99 ? 2239 HOH C O   1 
HETATM 9327 O  O   . HOH BA 5 .   ? 3.779   -10.586 -12.125 1.00 18.71 ? 2240 HOH C O   1 
HETATM 9328 O  O   . HOH BA 5 .   ? 2.256   -13.989 -10.754 1.00 31.72 ? 2241 HOH C O   1 
HETATM 9329 O  O   . HOH BA 5 .   ? -3.848  -10.678 -11.860 1.00 33.28 ? 2242 HOH C O   1 
HETATM 9330 O  O   . HOH BA 5 .   ? 0.180   -9.224  -14.012 1.00 32.87 ? 2243 HOH C O   1 
HETATM 9331 O  O   . HOH BA 5 .   ? 4.807   -8.351  -13.166 1.00 34.38 ? 2244 HOH C O   1 
HETATM 9332 O  O   . HOH BA 5 .   ? 11.065  -17.948 -10.325 1.00 31.65 ? 2245 HOH C O   1 
HETATM 9333 O  O   . HOH BA 5 .   ? 8.643   -18.122 -5.367  1.00 36.78 ? 2246 HOH C O   1 
HETATM 9334 O  O   . HOH BA 5 .   ? 10.523  -16.538 -12.558 1.00 14.54 ? 2247 HOH C O   1 
HETATM 9335 O  O   . HOH BA 5 .   ? 7.348   -7.662  -12.748 1.00 12.05 ? 2248 HOH C O   1 
HETATM 9336 O  O   . HOH BA 5 .   ? 8.991   -3.571  -22.024 1.00 40.43 ? 2249 HOH C O   1 
HETATM 9337 O  O   . HOH BA 5 .   ? 13.363  -3.375  -19.792 1.00 37.41 ? 2250 HOH C O   1 
HETATM 9338 O  O   . HOH BA 5 .   ? 21.052  -5.836  -16.170 1.00 34.30 ? 2251 HOH C O   1 
HETATM 9339 O  O   . HOH BA 5 .   ? 17.252  -4.663  -18.486 1.00 37.02 ? 2252 HOH C O   1 
HETATM 9340 O  O   . HOH BA 5 .   ? 14.387  -6.398  -17.620 1.00 27.62 ? 2253 HOH C O   1 
HETATM 9341 O  O   . HOH BA 5 .   ? 19.131  -2.111  -18.065 1.00 21.55 ? 2254 HOH C O   1 
HETATM 9342 O  O   . HOH BA 5 .   ? 23.069  5.017   -18.299 1.00 33.92 ? 2255 HOH C O   1 
HETATM 9343 O  O   . HOH BA 5 .   ? 26.320  0.576   -14.084 1.00 31.81 ? 2256 HOH C O   1 
HETATM 9344 O  O   . HOH BA 5 .   ? 24.497  2.381   -16.837 1.00 27.77 ? 2257 HOH C O   1 
HETATM 9345 O  O   . HOH BA 5 .   ? 24.671  -2.811  -14.102 1.00 21.74 ? 2258 HOH C O   1 
HETATM 9346 O  O   . HOH BA 5 .   ? 25.223  -5.326  -12.955 1.00 15.87 ? 2259 HOH C O   1 
HETATM 9347 O  O   . HOH BA 5 .   ? 27.905  -7.736  -10.909 1.00 29.62 ? 2260 HOH C O   1 
HETATM 9348 O  O   . HOH BA 5 .   ? 31.647  -10.046 -6.558  1.00 35.32 ? 2261 HOH C O   1 
HETATM 9349 O  O   . HOH BA 5 .   ? 20.646  -14.591 -0.554  1.00 31.80 ? 2262 HOH C O   1 
HETATM 9350 O  O   . HOH BA 5 .   ? 24.755  -14.818 -1.529  1.00 30.95 ? 2263 HOH C O   1 
HETATM 9351 O  O   . HOH BA 5 .   ? 24.679  -12.400 6.310   1.00 29.83 ? 2264 HOH C O   1 
HETATM 9352 O  O   . HOH BA 5 .   ? 25.991  -14.224 3.054   1.00 19.39 ? 2265 HOH C O   1 
HETATM 9353 O  O   . HOH BA 5 .   ? 18.682  -9.537  6.993   1.00 29.74 ? 2266 HOH C O   1 
HETATM 9354 O  O   . HOH BA 5 .   ? 23.177  -9.719  7.638   1.00 31.08 ? 2267 HOH C O   1 
HETATM 9355 O  O   . HOH BA 5 .   ? -14.965 -6.563  -2.691  1.00 41.84 ? 2268 HOH C O   1 
HETATM 9356 O  O   . HOH BA 5 .   ? -8.915  -3.990  -0.104  1.00 27.99 ? 2269 HOH C O   1 
HETATM 9357 O  O   . HOH BA 5 .   ? -16.159 -4.202  -1.137  1.00 42.77 ? 2270 HOH C O   1 
HETATM 9358 O  O   . HOH BA 5 .   ? 12.144  18.193  -1.478  1.00 26.36 ? 2271 HOH C O   1 
HETATM 9359 O  O   . HOH BA 5 .   ? 10.594  19.351  -4.890  1.00 32.78 ? 2272 HOH C O   1 
HETATM 9360 O  O   . HOH BA 5 .   ? 7.042   18.870  -0.995  1.00 33.81 ? 2273 HOH C O   1 
HETATM 9361 O  O   . HOH CA 5 .   ? 55.305  -14.551 -0.547  1.00 38.47 ? 2001 HOH D O   1 
HETATM 9362 O  O   . HOH CA 5 .   ? 51.194  -19.423 23.634  1.00 42.28 ? 2002 HOH D O   1 
HETATM 9363 O  O   . HOH CA 5 .   ? 51.772  -18.756 20.250  1.00 36.71 ? 2003 HOH D O   1 
HETATM 9364 O  O   . HOH CA 5 .   ? 48.514  -19.560 22.662  1.00 38.61 ? 2004 HOH D O   1 
HETATM 9365 O  O   . HOH CA 5 .   ? 50.689  -23.617 11.784  1.00 28.99 ? 2005 HOH D O   1 
HETATM 9366 O  O   . HOH CA 5 .   ? 56.457  -18.351 14.218  1.00 29.15 ? 2006 HOH D O   1 
HETATM 9367 O  O   . HOH CA 5 .   ? 52.362  -23.805 7.984   1.00 31.71 ? 2007 HOH D O   1 
HETATM 9368 O  O   . HOH CA 5 .   ? 54.459  -24.069 10.561  1.00 23.36 ? 2008 HOH D O   1 
HETATM 9369 O  O   . HOH CA 5 .   ? 57.850  -20.262 10.800  1.00 19.54 ? 2009 HOH D O   1 
HETATM 9370 O  O   . HOH CA 5 .   ? 51.451  -20.033 17.928  1.00 27.07 ? 2010 HOH D O   1 
HETATM 9371 O  O   . HOH CA 5 .   ? 53.153  -19.737 14.723  1.00 19.19 ? 2011 HOH D O   1 
HETATM 9372 O  O   . HOH CA 5 .   ? 47.922  4.900   22.753  1.00 17.45 ? 2012 HOH D O   1 
HETATM 9373 O  O   . HOH CA 5 .   ? 46.695  12.542  17.748  1.00 30.21 ? 2013 HOH D O   1 
HETATM 9374 O  O   . HOH CA 5 .   ? 47.954  -18.540 20.251  1.00 34.90 ? 2014 HOH D O   1 
HETATM 9375 O  O   . HOH CA 5 .   ? 56.159  -20.610 18.083  1.00 39.41 ? 2015 HOH D O   1 
HETATM 9376 O  O   . HOH CA 5 .   ? 57.399  -15.856 15.420  1.00 41.39 ? 2016 HOH D O   1 
HETATM 9377 O  O   . HOH CA 5 .   ? 57.156  -15.632 18.486  1.00 35.03 ? 2017 HOH D O   1 
HETATM 9378 O  O   . HOH CA 5 .   ? 46.568  -14.181 14.824  1.00 24.91 ? 2018 HOH D O   1 
HETATM 9379 O  O   . HOH CA 5 .   ? 51.251  2.689   25.111  1.00 13.45 ? 2019 HOH D O   1 
HETATM 9380 O  O   . HOH CA 5 .   ? 62.224  3.661   21.614  1.00 38.79 ? 2020 HOH D O   1 
HETATM 9381 O  O   . HOH CA 5 .   ? 61.751  2.887   18.377  1.00 43.26 ? 2021 HOH D O   1 
HETATM 9382 O  O   . HOH CA 5 .   ? 58.001  4.238   24.746  1.00 32.54 ? 2022 HOH D O   1 
HETATM 9383 O  O   . HOH CA 5 .   ? 47.115  7.338   22.242  1.00 24.50 ? 2023 HOH D O   1 
HETATM 9384 O  O   . HOH CA 5 .   ? 46.732  10.515  19.935  1.00 31.61 ? 2024 HOH D O   1 
HETATM 9385 O  O   . HOH CA 5 .   ? 56.841  6.798   20.847  1.00 29.60 ? 2025 HOH D O   1 
HETATM 9386 O  O   . HOH CA 5 .   ? 50.583  4.948   23.469  1.00 16.90 ? 2026 HOH D O   1 
HETATM 9387 O  O   . HOH CA 5 .   ? 53.919  6.790   23.059  1.00 29.18 ? 2027 HOH D O   1 
HETATM 9388 O  O   . HOH CA 5 .   ? 53.084  3.471   16.832  1.00 11.91 ? 2028 HOH D O   1 
HETATM 9389 O  O   . HOH CA 5 .   ? 43.332  6.849   23.298  1.00 31.82 ? 2029 HOH D O   1 
HETATM 9390 O  O   . HOH CA 5 .   ? 57.714  8.500   17.656  1.00 17.91 ? 2030 HOH D O   1 
HETATM 9391 O  O   . HOH CA 5 .   ? 59.004  7.966   10.926  1.00 27.68 ? 2031 HOH D O   1 
HETATM 9392 O  O   . HOH CA 5 .   ? 33.505  5.306   21.528  1.00 26.32 ? 2032 HOH D O   1 
HETATM 9393 O  O   . HOH CA 5 .   ? 41.147  10.359  21.501  1.00 30.44 ? 2033 HOH D O   1 
HETATM 9394 O  O   . HOH CA 5 .   ? 61.372  3.130   12.570  1.00 28.10 ? 2034 HOH D O   1 
HETATM 9395 O  O   . HOH CA 5 .   ? 59.174  6.340   18.940  1.00 28.15 ? 2035 HOH D O   1 
HETATM 9396 O  O   . HOH CA 5 .   ? 54.115  0.492   18.727  1.00 10.85 ? 2036 HOH D O   1 
HETATM 9397 O  O   . HOH CA 5 .   ? 60.706  0.953   6.680   1.00 16.53 ? 2037 HOH D O   1 
HETATM 9398 O  O   . HOH CA 5 .   ? 58.317  1.025   4.246   1.00 27.92 ? 2038 HOH D O   1 
HETATM 9399 O  O   . HOH CA 5 .   ? 56.938  -1.318  3.104   1.00 27.22 ? 2039 HOH D O   1 
HETATM 9400 O  O   . HOH CA 5 .   ? 56.328  -3.530  1.539   1.00 21.13 ? 2040 HOH D O   1 
HETATM 9401 O  O   . HOH CA 5 .   ? 54.510  -11.765 2.802   1.00 20.45 ? 2041 HOH D O   1 
HETATM 9402 O  O   . HOH CA 5 .   ? 57.121  -12.184 -0.171  1.00 29.57 ? 2042 HOH D O   1 
HETATM 9403 O  O   . HOH CA 5 .   ? 52.621  -11.436 -5.095  1.00 44.23 ? 2043 HOH D O   1 
HETATM 9404 O  O   . HOH CA 5 .   ? 52.209  -10.391 -9.737  1.00 35.87 ? 2044 HOH D O   1 
HETATM 9405 O  O   . HOH CA 5 .   ? 41.760  13.220  -1.515  1.00 43.62 ? 2045 HOH D O   1 
HETATM 9406 O  O   . HOH CA 5 .   ? 35.748  6.593   -10.936 1.00 37.04 ? 2046 HOH D O   1 
HETATM 9407 O  O   . HOH CA 5 .   ? 46.390  -6.979  -14.278 1.00 34.70 ? 2047 HOH D O   1 
HETATM 9408 O  O   . HOH CA 5 .   ? 30.220  8.372   6.013   1.00 26.23 ? 2048 HOH D O   1 
HETATM 9409 O  O   . HOH CA 5 .   ? 29.596  -6.211  17.508  1.00 35.07 ? 2049 HOH D O   1 
HETATM 9410 O  O   . HOH CA 5 .   ? 44.720  -8.542  -11.565 1.00 30.77 ? 2050 HOH D O   1 
HETATM 9411 O  O   . HOH CA 5 .   ? 38.627  -6.758  -14.271 1.00 29.01 ? 2051 HOH D O   1 
HETATM 9412 O  O   . HOH CA 5 .   ? 32.238  -7.332  20.621  1.00 26.57 ? 2052 HOH D O   1 
HETATM 9413 O  O   . HOH CA 5 .   ? 36.798  -7.889  24.631  1.00 29.58 ? 2053 HOH D O   1 
HETATM 9414 O  O   . HOH CA 5 .   ? 43.379  -9.396  -9.404  1.00 18.06 ? 2054 HOH D O   1 
HETATM 9415 O  O   . HOH CA 5 .   ? 37.083  -7.028  -11.992 1.00 16.83 ? 2055 HOH D O   1 
HETATM 9416 O  O   . HOH CA 5 .   ? 35.443  -10.438 21.791  1.00 37.33 ? 2056 HOH D O   1 
HETATM 9417 O  O   . HOH CA 5 .   ? 38.456  -11.433 15.999  1.00 31.44 ? 2057 HOH D O   1 
HETATM 9418 O  O   . HOH CA 5 .   ? 28.723  -12.505 -3.303  1.00 32.58 ? 2058 HOH D O   1 
HETATM 9419 O  O   . HOH CA 5 .   ? 30.134  -9.996  17.008  1.00 46.72 ? 2059 HOH D O   1 
HETATM 9420 O  O   . HOH CA 5 .   ? 38.631  -4.098  26.161  1.00 12.88 ? 2060 HOH D O   1 
HETATM 9421 O  O   . HOH CA 5 .   ? 37.913  -1.423  19.542  1.00 13.61 ? 2061 HOH D O   1 
HETATM 9422 O  O   . HOH CA 5 .   ? 43.776  4.338   23.903  1.00 15.65 ? 2062 HOH D O   1 
HETATM 9423 O  O   . HOH CA 5 .   ? 45.939  2.962   22.451  1.00 15.28 ? 2063 HOH D O   1 
HETATM 9424 O  O   . HOH CA 5 .   ? 35.881  6.899   17.807  1.00 16.49 ? 2064 HOH D O   1 
HETATM 9425 O  O   . HOH CA 5 .   ? 42.361  7.850   20.953  1.00 10.33 ? 2065 HOH D O   1 
HETATM 9426 O  O   . HOH CA 5 .   ? 36.021  5.470   20.163  1.00 24.50 ? 2066 HOH D O   1 
HETATM 9427 O  O   . HOH CA 5 .   ? 40.117  5.660   23.304  1.00 23.10 ? 2067 HOH D O   1 
HETATM 9428 O  O   . HOH CA 5 .   ? 39.068  5.303   14.801  1.00 16.63 ? 2068 HOH D O   1 
HETATM 9429 O  O   . HOH CA 5 .   ? 41.099  11.453  14.615  1.00 25.20 ? 2069 HOH D O   1 
HETATM 9430 O  O   . HOH CA 5 .   ? 39.623  1.173   18.101  1.00 15.88 ? 2070 HOH D O   1 
HETATM 9431 O  O   . HOH CA 5 .   ? 40.217  -2.049  15.268  1.00 16.82 ? 2071 HOH D O   1 
HETATM 9432 O  O   . HOH CA 5 .   ? 48.715  3.053   11.137  1.00 19.52 ? 2072 HOH D O   1 
HETATM 9433 O  O   . HOH CA 5 .   ? 48.652  0.910   8.262   1.00 9.75  ? 2073 HOH D O   1 
HETATM 9434 O  O   . HOH CA 5 .   ? 59.136  10.858  -1.451  1.00 31.23 ? 2074 HOH D O   1 
HETATM 9435 O  O   . HOH CA 5 .   ? 47.988  -0.760  10.812  1.00 12.57 ? 2075 HOH D O   1 
HETATM 9436 O  O   . HOH CA 5 .   ? 48.258  4.407   2.455   1.00 9.04  ? 2076 HOH D O   1 
HETATM 9437 O  O   . HOH CA 5 .   ? 55.530  12.987  15.419  1.00 38.68 ? 2077 HOH D O   1 
HETATM 9438 O  O   . HOH CA 5 .   ? 44.250  12.842  16.498  1.00 28.51 ? 2078 HOH D O   1 
HETATM 9439 O  O   . HOH CA 5 .   ? 53.631  6.803   -2.544  1.00 14.72 ? 2079 HOH D O   1 
HETATM 9440 O  O   . HOH CA 5 .   ? 52.718  3.648   -9.024  1.00 21.93 ? 2080 HOH D O   1 
HETATM 9441 O  O   . HOH CA 5 .   ? 59.987  7.480   -3.644  1.00 27.78 ? 2081 HOH D O   1 
HETATM 9442 O  O   . HOH CA 5 .   ? 55.598  7.268   -10.729 1.00 41.46 ? 2082 HOH D O   1 
HETATM 9443 O  O   . HOH CA 5 .   ? 57.682  9.010   -7.055  1.00 38.93 ? 2083 HOH D O   1 
HETATM 9444 O  O   . HOH CA 5 .   ? 51.486  9.499   -9.882  1.00 32.90 ? 2084 HOH D O   1 
HETATM 9445 O  O   . HOH CA 5 .   ? 55.578  8.272   -3.945  1.00 18.67 ? 2085 HOH D O   1 
HETATM 9446 O  O   . HOH CA 5 .   ? 43.123  -17.999 -4.768  1.00 31.91 ? 2086 HOH D O   1 
HETATM 9447 O  O   . HOH CA 5 .   ? 34.809  -18.246 -5.761  1.00 41.00 ? 2087 HOH D O   1 
HETATM 9448 O  O   . HOH CA 5 .   ? 32.606  -16.591 -6.345  1.00 36.66 ? 2088 HOH D O   1 
HETATM 9449 O  O   . HOH CA 5 .   ? 47.234  8.844   -7.011  1.00 24.64 ? 2089 HOH D O   1 
HETATM 9450 O  O   . HOH CA 5 .   ? 50.730  7.609   -11.438 1.00 31.26 ? 2090 HOH D O   1 
HETATM 9451 O  O   . HOH CA 5 .   ? 44.583  8.842   -10.152 1.00 30.41 ? 2091 HOH D O   1 
HETATM 9452 O  O   . HOH CA 5 .   ? 28.969  -20.287 5.011   1.00 37.41 ? 2092 HOH D O   1 
HETATM 9453 O  O   . HOH CA 5 .   ? 49.148  10.386  -5.030  1.00 18.33 ? 2093 HOH D O   1 
HETATM 9454 O  O   . HOH CA 5 .   ? 46.065  11.421  -0.252  1.00 29.32 ? 2094 HOH D O   1 
HETATM 9455 O  O   . HOH CA 5 .   ? 46.720  6.597   -5.537  1.00 13.22 ? 2095 HOH D O   1 
HETATM 9456 O  O   . HOH CA 5 .   ? 51.922  -18.573 0.931   1.00 35.45 ? 2096 HOH D O   1 
HETATM 9457 O  O   . HOH CA 5 .   ? 37.696  3.330   16.102  1.00 22.69 ? 2097 HOH D O   1 
HETATM 9458 O  O   . HOH CA 5 .   ? 37.065  0.937   17.726  1.00 32.03 ? 2098 HOH D O   1 
HETATM 9459 O  O   . HOH CA 5 .   ? 62.949  -5.883  16.406  1.00 46.21 ? 2099 HOH D O   1 
HETATM 9460 O  O   . HOH CA 5 .   ? 38.343  10.406  10.534  1.00 25.82 ? 2100 HOH D O   1 
HETATM 9461 O  O   . HOH CA 5 .   ? 37.916  9.437   15.573  1.00 17.08 ? 2101 HOH D O   1 
HETATM 9462 O  O   . HOH CA 5 .   ? 39.238  10.876  6.843   1.00 39.19 ? 2102 HOH D O   1 
HETATM 9463 O  O   . HOH CA 5 .   ? 32.987  11.874  7.907   1.00 50.93 ? 2103 HOH D O   1 
HETATM 9464 O  O   . HOH CA 5 .   ? 36.758  12.692  13.738  1.00 42.19 ? 2104 HOH D O   1 
HETATM 9465 O  O   . HOH CA 5 .   ? 31.041  7.121   15.286  1.00 33.60 ? 2105 HOH D O   1 
HETATM 9466 O  O   . HOH CA 5 .   ? 41.529  -17.275 27.812  1.00 30.80 ? 2106 HOH D O   1 
HETATM 9467 O  O   . HOH CA 5 .   ? 45.065  -18.353 25.097  1.00 29.58 ? 2107 HOH D O   1 
HETATM 9468 O  O   . HOH CA 5 .   ? 36.854  -17.281 24.079  1.00 42.73 ? 2108 HOH D O   1 
HETATM 9469 O  O   . HOH CA 5 .   ? 30.051  10.502  11.153  1.00 39.22 ? 2109 HOH D O   1 
HETATM 9470 O  O   . HOH CA 5 .   ? 37.613  -1.751  15.093  1.00 21.50 ? 2110 HOH D O   1 
HETATM 9471 O  O   . HOH CA 5 .   ? 39.379  10.710  -1.464  1.00 33.75 ? 2111 HOH D O   1 
HETATM 9472 O  O   . HOH CA 5 .   ? 43.075  10.225  -0.459  1.00 18.87 ? 2112 HOH D O   1 
HETATM 9473 O  O   . HOH CA 5 .   ? 45.494  15.111  0.024   1.00 35.41 ? 2113 HOH D O   1 
HETATM 9474 O  O   . HOH CA 5 .   ? 35.737  6.555   -8.144  1.00 16.16 ? 2114 HOH D O   1 
HETATM 9475 O  O   . HOH CA 5 .   ? 32.455  8.080   -0.253  1.00 29.14 ? 2115 HOH D O   1 
HETATM 9476 O  O   . HOH CA 5 .   ? 34.579  7.534   -4.062  1.00 24.95 ? 2116 HOH D O   1 
HETATM 9477 O  O   . HOH CA 5 .   ? 36.797  10.065  -2.725  1.00 18.66 ? 2117 HOH D O   1 
HETATM 9478 O  O   . HOH CA 5 .   ? 29.040  6.010   5.317   1.00 22.60 ? 2118 HOH D O   1 
HETATM 9479 O  O   . HOH CA 5 .   ? 31.005  5.852   0.416   1.00 15.35 ? 2119 HOH D O   1 
HETATM 9480 O  O   . HOH CA 5 .   ? 33.454  8.529   2.333   1.00 33.35 ? 2120 HOH D O   1 
HETATM 9481 O  O   . HOH CA 5 .   ? 34.227  9.009   5.856   1.00 36.79 ? 2121 HOH D O   1 
HETATM 9482 O  O   . HOH CA 5 .   ? 27.043  -0.349  6.221   1.00 9.25  ? 2122 HOH D O   1 
HETATM 9483 O  O   . HOH CA 5 .   ? 26.321  7.402   12.316  1.00 32.67 ? 2123 HOH D O   1 
HETATM 9484 O  O   . HOH CA 5 .   ? 27.894  3.298   12.880  1.00 23.66 ? 2124 HOH D O   1 
HETATM 9485 O  O   . HOH CA 5 .   ? 25.357  -2.603  11.782  1.00 18.83 ? 2125 HOH D O   1 
HETATM 9486 O  O   . HOH CA 5 .   ? 30.063  -5.396  14.965  1.00 27.30 ? 2126 HOH D O   1 
HETATM 9487 O  O   . HOH CA 5 .   ? 29.283  1.157   16.158  1.00 20.65 ? 2127 HOH D O   1 
HETATM 9488 O  O   . HOH CA 5 .   ? 35.085  -0.722  18.155  1.00 19.95 ? 2128 HOH D O   1 
HETATM 9489 O  O   . HOH CA 5 .   ? 31.762  -5.493  18.581  1.00 19.05 ? 2129 HOH D O   1 
HETATM 9490 O  O   . HOH CA 5 .   ? 30.446  -0.112  23.364  1.00 23.44 ? 2130 HOH D O   1 
HETATM 9491 O  O   . HOH CA 5 .   ? 33.925  1.823   26.428  1.00 20.92 ? 2131 HOH D O   1 
HETATM 9492 O  O   . HOH CA 5 .   ? 34.936  -5.924  24.486  1.00 27.60 ? 2132 HOH D O   1 
HETATM 9493 O  O   . HOH CA 5 .   ? 36.066  -2.910  17.117  1.00 20.70 ? 2133 HOH D O   1 
HETATM 9494 O  O   . HOH CA 5 .   ? 39.529  -3.172  17.854  1.00 10.81 ? 2134 HOH D O   1 
HETATM 9495 O  O   . HOH CA 5 .   ? 34.464  -8.732  19.504  1.00 22.02 ? 2135 HOH D O   1 
HETATM 9496 O  O   . HOH CA 5 .   ? 34.025  -5.834  17.143  1.00 18.06 ? 2136 HOH D O   1 
HETATM 9497 O  O   . HOH CA 5 .   ? 34.474  -10.449 8.959   1.00 10.33 ? 2137 HOH D O   1 
HETATM 9498 O  O   . HOH CA 5 .   ? 33.925  -10.209 -0.688  1.00 16.02 ? 2138 HOH D O   1 
HETATM 9499 O  O   . HOH CA 5 .   ? 31.610  -10.367 -10.397 1.00 37.55 ? 2139 HOH D O   1 
HETATM 9500 O  O   . HOH CA 5 .   ? 35.211  -10.914 -9.031  1.00 28.33 ? 2140 HOH D O   1 
HETATM 9501 O  O   . HOH CA 5 .   ? 38.226  -3.893  -14.853 1.00 22.39 ? 2141 HOH D O   1 
HETATM 9502 O  O   . HOH CA 5 .   ? 31.270  -6.718  -13.112 1.00 32.03 ? 2142 HOH D O   1 
HETATM 9503 O  O   . HOH CA 5 .   ? 33.744  -2.373  -16.290 1.00 29.87 ? 2143 HOH D O   1 
HETATM 9504 O  O   . HOH CA 5 .   ? 29.786  -4.327  -13.474 1.00 35.71 ? 2144 HOH D O   1 
HETATM 9505 O  O   . HOH CA 5 .   ? 33.910  -6.618  -4.056  1.00 11.41 ? 2145 HOH D O   1 
HETATM 9506 O  O   . HOH CA 5 .   ? 31.494  -7.868  -4.965  1.00 19.26 ? 2146 HOH D O   1 
HETATM 9507 O  O   . HOH CA 5 .   ? 30.939  -11.898 -1.160  1.00 20.75 ? 2147 HOH D O   1 
HETATM 9508 O  O   . HOH CA 5 .   ? 28.023  -9.788  -3.227  1.00 26.44 ? 2148 HOH D O   1 
HETATM 9509 O  O   . HOH CA 5 .   ? 35.860  -10.753 16.190  1.00 25.93 ? 2149 HOH D O   1 
HETATM 9510 O  O   . HOH CA 5 .   ? 29.645  -7.904  15.403  1.00 37.78 ? 2150 HOH D O   1 
HETATM 9511 O  O   . HOH CA 5 .   ? 26.980  -13.545 7.518   1.00 29.44 ? 2151 HOH D O   1 
HETATM 9512 O  O   . HOH CA 5 .   ? 29.006  -6.809  13.108  1.00 33.05 ? 2152 HOH D O   1 
HETATM 9513 O  O   . HOH CA 5 .   ? 24.225  -7.204  7.599   1.00 25.15 ? 2153 HOH D O   1 
HETATM 9514 O  O   . HOH CA 5 .   ? 29.803  -5.477  2.191   1.00 20.20 ? 2154 HOH D O   1 
HETATM 9515 O  O   . HOH CA 5 .   ? 31.181  -2.085  1.916   1.00 17.21 ? 2155 HOH D O   1 
HETATM 9516 O  O   . HOH CA 5 .   ? 28.510  -7.306  0.785   1.00 24.18 ? 2156 HOH D O   1 
HETATM 9517 O  O   . HOH CA 5 .   ? 28.765  6.338   1.946   1.00 17.93 ? 2157 HOH D O   1 
HETATM 9518 O  O   . HOH CA 5 .   ? 31.779  6.459   -4.295  1.00 27.98 ? 2158 HOH D O   1 
HETATM 9519 O  O   . HOH CA 5 .   ? 39.000  5.468   -12.312 1.00 30.81 ? 2159 HOH D O   1 
HETATM 9520 O  O   . HOH CA 5 .   ? 31.351  4.254   -12.137 1.00 33.50 ? 2160 HOH D O   1 
HETATM 9521 O  O   . HOH CA 5 .   ? 28.675  2.191   -14.515 1.00 26.98 ? 2161 HOH D O   1 
HETATM 9522 O  O   . HOH CA 5 .   ? 33.031  3.304   -9.412  1.00 20.92 ? 2162 HOH D O   1 
HETATM 9523 O  O   . HOH CA 5 .   ? 35.293  4.773   -12.664 1.00 31.12 ? 2163 HOH D O   1 
HETATM 9524 O  O   . HOH CA 5 .   ? 28.177  -1.566  -14.910 1.00 37.15 ? 2164 HOH D O   1 
HETATM 9525 O  O   . HOH CA 5 .   ? 39.013  -1.120  -17.447 1.00 43.14 ? 2165 HOH D O   1 
HETATM 9526 O  O   . HOH CA 5 .   ? 46.433  1.689   -12.804 1.00 24.99 ? 2166 HOH D O   1 
HETATM 9527 O  O   . HOH CA 5 .   ? 44.010  1.756   -14.218 1.00 23.80 ? 2167 HOH D O   1 
HETATM 9528 O  O   . HOH CA 5 .   ? 48.233  -0.282  -13.468 1.00 28.75 ? 2168 HOH D O   1 
HETATM 9529 O  O   . HOH CA 5 .   ? 52.033  4.997   -11.598 1.00 31.16 ? 2169 HOH D O   1 
HETATM 9530 O  O   . HOH CA 5 .   ? 53.940  1.108   -9.534  1.00 30.09 ? 2170 HOH D O   1 
HETATM 9531 O  O   . HOH CA 5 .   ? 58.319  0.876   -8.009  1.00 29.18 ? 2171 HOH D O   1 
HETATM 9532 O  O   . HOH CA 5 .   ? 55.738  1.191   -7.209  1.00 16.74 ? 2172 HOH D O   1 
HETATM 9533 O  O   . HOH CA 5 .   ? 57.426  -3.795  -4.168  1.00 38.85 ? 2173 HOH D O   1 
HETATM 9534 O  O   . HOH CA 5 .   ? 57.885  -3.677  -0.870  1.00 40.97 ? 2174 HOH D O   1 
HETATM 9535 O  O   . HOH CA 5 .   ? 51.193  6.882   10.571  1.00 8.95  ? 2175 HOH D O   1 
HETATM 9536 O  O   . HOH CA 5 .   ? 51.111  9.556   7.011   1.00 13.11 ? 2176 HOH D O   1 
HETATM 9537 O  O   . HOH CA 5 .   ? 52.639  9.392   -2.025  1.00 19.30 ? 2177 HOH D O   1 
HETATM 9538 O  O   . HOH CA 5 .   ? 52.710  13.267  5.835   1.00 30.64 ? 2178 HOH D O   1 
HETATM 9539 O  O   . HOH CA 5 .   ? 59.726  8.796   2.346   1.00 29.66 ? 2179 HOH D O   1 
HETATM 9540 O  O   . HOH CA 5 .   ? 58.134  8.574   -2.278  1.00 20.26 ? 2180 HOH D O   1 
HETATM 9541 O  O   . HOH CA 5 .   ? 60.678  6.395   -1.313  1.00 35.88 ? 2181 HOH D O   1 
HETATM 9542 O  O   . HOH CA 5 .   ? 60.072  4.790   6.269   1.00 27.38 ? 2182 HOH D O   1 
HETATM 9543 O  O   . HOH CA 5 .   ? 52.884  15.014  2.247   1.00 28.68 ? 2183 HOH D O   1 
HETATM 9544 O  O   . HOH CA 5 .   ? 59.679  9.449   5.567   1.00 31.17 ? 2184 HOH D O   1 
HETATM 9545 O  O   . HOH CA 5 .   ? 54.657  13.428  10.800  1.00 41.35 ? 2185 HOH D O   1 
HETATM 9546 O  O   . HOH CA 5 .   ? 58.008  9.037   8.583   1.00 17.98 ? 2186 HOH D O   1 
HETATM 9547 O  O   . HOH CA 5 .   ? 56.845  11.903  8.979   1.00 38.09 ? 2187 HOH D O   1 
HETATM 9548 O  O   . HOH CA 5 .   ? 52.557  13.856  8.722   1.00 41.49 ? 2188 HOH D O   1 
HETATM 9549 O  O   . HOH CA 5 .   ? 51.340  14.179  13.939  1.00 40.13 ? 2189 HOH D O   1 
HETATM 9550 O  O   . HOH CA 5 .   ? 49.024  12.580  7.457   1.00 14.83 ? 2190 HOH D O   1 
HETATM 9551 O  O   . HOH CA 5 .   ? 57.020  9.280   21.423  1.00 38.56 ? 2191 HOH D O   1 
HETATM 9552 O  O   . HOH CA 5 .   ? 56.750  11.797  17.464  1.00 38.83 ? 2192 HOH D O   1 
HETATM 9553 O  O   . HOH CA 5 .   ? 53.773  12.688  13.256  1.00 19.11 ? 2193 HOH D O   1 
HETATM 9554 O  O   . HOH CA 5 .   ? 44.791  12.814  11.272  1.00 41.02 ? 2194 HOH D O   1 
HETATM 9555 O  O   . HOH CA 5 .   ? 43.816  11.330  14.193  1.00 26.47 ? 2195 HOH D O   1 
HETATM 9556 O  O   . HOH CA 5 .   ? 52.304  1.593   15.333  1.00 11.97 ? 2196 HOH D O   1 
HETATM 9557 O  O   . HOH CA 5 .   ? 44.999  0.400   21.452  1.00 10.64 ? 2197 HOH D O   1 
HETATM 9558 O  O   . HOH CA 5 .   ? 45.367  -8.671  24.539  1.00 9.23  ? 2198 HOH D O   1 
HETATM 9559 O  O   . HOH CA 5 .   ? 47.358  -11.121 22.336  1.00 10.96 ? 2199 HOH D O   1 
HETATM 9560 O  O   . HOH CA 5 .   ? 42.633  -17.425 14.553  1.00 25.87 ? 2200 HOH D O   1 
HETATM 9561 O  O   . HOH CA 5 .   ? 46.160  -17.100 14.493  1.00 29.87 ? 2201 HOH D O   1 
HETATM 9562 O  O   . HOH CA 5 .   ? 41.453  -13.547 8.742   1.00 10.89 ? 2202 HOH D O   1 
HETATM 9563 O  O   . HOH CA 5 .   ? 46.121  -20.121 7.190   1.00 27.16 ? 2203 HOH D O   1 
HETATM 9564 O  O   . HOH CA 5 .   ? 46.314  -17.627 11.115  1.00 30.50 ? 2204 HOH D O   1 
HETATM 9565 O  O   . HOH CA 5 .   ? 43.158  -15.521 -8.794  1.00 29.78 ? 2205 HOH D O   1 
HETATM 9566 O  O   . HOH CA 5 .   ? 46.582  -15.566 -9.627  1.00 37.04 ? 2206 HOH D O   1 
HETATM 9567 O  O   . HOH CA 5 .   ? 42.710  -15.445 -5.039  1.00 18.03 ? 2207 HOH D O   1 
HETATM 9568 O  O   . HOH CA 5 .   ? 37.329  -12.250 -8.133  1.00 18.31 ? 2208 HOH D O   1 
HETATM 9569 O  O   . HOH CA 5 .   ? 33.119  -13.983 -5.522  1.00 30.20 ? 2209 HOH D O   1 
HETATM 9570 O  O   . HOH CA 5 .   ? 37.269  -15.891 -4.903  1.00 34.64 ? 2210 HOH D O   1 
HETATM 9571 O  O   . HOH CA 5 .   ? 31.989  -21.137 5.345   1.00 25.28 ? 2211 HOH D O   1 
HETATM 9572 O  O   . HOH CA 5 .   ? 28.206  -18.014 3.786   1.00 23.80 ? 2212 HOH D O   1 
HETATM 9573 O  O   . HOH CA 5 .   ? 30.494  -19.213 -4.284  1.00 39.54 ? 2213 HOH D O   1 
HETATM 9574 O  O   . HOH CA 5 .   ? 26.844  -18.193 0.886   1.00 34.21 ? 2214 HOH D O   1 
HETATM 9575 O  O   . HOH CA 5 .   ? 28.286  -17.941 -3.018  1.00 42.00 ? 2215 HOH D O   1 
HETATM 9576 O  O   . HOH CA 5 .   ? 39.080  -17.502 3.273   1.00 13.07 ? 2216 HOH D O   1 
HETATM 9577 O  O   . HOH CA 5 .   ? 35.447  -20.223 -3.608  1.00 40.77 ? 2217 HOH D O   1 
HETATM 9578 O  O   . HOH CA 5 .   ? 34.593  -21.652 2.549   1.00 25.43 ? 2218 HOH D O   1 
HETATM 9579 O  O   . HOH CA 5 .   ? 35.148  -22.820 -1.075  1.00 32.14 ? 2219 HOH D O   1 
HETATM 9580 O  O   . HOH CA 5 .   ? 37.140  -21.456 2.740   1.00 35.69 ? 2220 HOH D O   1 
HETATM 9581 O  O   . HOH CA 5 .   ? 35.984  -23.280 6.562   1.00 35.48 ? 2221 HOH D O   1 
HETATM 9582 O  O   . HOH CA 5 .   ? 41.475  -16.064 9.804   1.00 18.37 ? 2222 HOH D O   1 
HETATM 9583 O  O   . HOH CA 5 .   ? 36.944  -16.550 15.641  1.00 45.10 ? 2223 HOH D O   1 
HETATM 9584 O  O   . HOH CA 5 .   ? 29.830  -13.952 15.447  1.00 37.78 ? 2224 HOH D O   1 
HETATM 9585 O  O   . HOH CA 5 .   ? 32.523  -22.627 7.574   1.00 41.44 ? 2225 HOH D O   1 
HETATM 9586 O  O   . HOH CA 5 .   ? 43.196  -17.814 10.747  1.00 21.77 ? 2226 HOH D O   1 
HETATM 9587 O  O   . HOH CA 5 .   ? 43.130  -22.956 11.082  1.00 34.56 ? 2227 HOH D O   1 
HETATM 9588 O  O   . HOH CA 5 .   ? 39.958  -23.661 4.617   1.00 35.26 ? 2228 HOH D O   1 
HETATM 9589 O  O   . HOH CA 5 .   ? 35.620  -23.142 10.216  1.00 27.24 ? 2229 HOH D O   1 
HETATM 9590 O  O   . HOH CA 5 .   ? 42.749  -23.704 3.942   1.00 25.53 ? 2230 HOH D O   1 
HETATM 9591 O  O   . HOH CA 5 .   ? 42.490  -22.669 6.958   1.00 21.47 ? 2231 HOH D O   1 
HETATM 9592 O  O   . HOH CA 5 .   ? 45.239  -18.421 -3.083  1.00 28.50 ? 2232 HOH D O   1 
HETATM 9593 O  O   . HOH CA 5 .   ? 45.331  -22.262 3.838   1.00 30.68 ? 2233 HOH D O   1 
HETATM 9594 O  O   . HOH CA 5 .   ? 47.716  -18.224 -7.077  1.00 34.55 ? 2234 HOH D O   1 
HETATM 9595 O  O   . HOH CA 5 .   ? 51.356  -16.382 -4.534  1.00 38.19 ? 2235 HOH D O   1 
HETATM 9596 O  O   . HOH CA 5 .   ? 52.766  -14.423 -0.029  1.00 35.45 ? 2236 HOH D O   1 
HETATM 9597 O  O   . HOH CA 5 .   ? 45.522  -19.743 4.411   1.00 20.33 ? 2237 HOH D O   1 
HETATM 9598 O  O   . HOH CA 5 .   ? 44.689  -22.225 8.276   1.00 31.35 ? 2238 HOH D O   1 
HETATM 9599 O  O   . HOH CA 5 .   ? 53.191  -22.293 6.139   1.00 30.24 ? 2239 HOH D O   1 
HETATM 9600 O  O   . HOH CA 5 .   ? 56.112  -20.358 6.802   1.00 28.39 ? 2240 HOH D O   1 
HETATM 9601 O  O   . HOH CA 5 .   ? 45.419  -21.004 11.181  1.00 46.82 ? 2241 HOH D O   1 
HETATM 9602 O  O   . HOH CA 5 .   ? 52.709  -14.009 2.429   1.00 17.30 ? 2242 HOH D O   1 
HETATM 9603 O  O   . HOH CA 5 .   ? 55.023  -16.915 1.387   1.00 30.62 ? 2243 HOH D O   1 
HETATM 9604 O  O   . HOH CA 5 .   ? 61.911  -10.208 5.526   1.00 37.08 ? 2244 HOH D O   1 
HETATM 9605 O  O   . HOH CA 5 .   ? 61.756  -11.478 9.580   1.00 44.07 ? 2245 HOH D O   1 
HETATM 9606 O  O   . HOH CA 5 .   ? 60.229  -11.770 13.759  1.00 31.28 ? 2246 HOH D O   1 
HETATM 9607 O  O   . HOH CA 5 .   ? 60.037  -12.662 7.735   1.00 29.39 ? 2247 HOH D O   1 
HETATM 9608 O  O   . HOH CA 5 .   ? 63.535  -8.608  3.948   1.00 41.35 ? 2248 HOH D O   1 
HETATM 9609 O  O   . HOH CA 5 .   ? 63.778  -5.215  13.604  1.00 39.80 ? 2249 HOH D O   1 
HETATM 9610 O  O   . HOH CA 5 .   ? 62.072  -8.100  11.254  1.00 21.16 ? 2250 HOH D O   1 
HETATM 9611 O  O   . HOH CA 5 .   ? 63.058  -3.259  15.943  1.00 24.32 ? 2251 HOH D O   1 
HETATM 9612 O  O   . HOH CA 5 .   ? 64.177  -0.818  13.749  1.00 30.88 ? 2252 HOH D O   1 
HETATM 9613 O  O   . HOH CA 5 .   ? 61.116  -4.232  18.640  1.00 33.86 ? 2253 HOH D O   1 
HETATM 9614 O  O   . HOH CA 5 .   ? 60.138  -7.864  17.883  1.00 23.57 ? 2254 HOH D O   1 
HETATM 9615 O  O   . HOH CA 5 .   ? 58.932  -10.016 18.961  1.00 18.57 ? 2255 HOH D O   1 
HETATM 9616 O  O   . HOH CA 5 .   ? 54.946  -15.147 20.324  1.00 28.80 ? 2256 HOH D O   1 
HETATM 9617 O  O   . HOH CA 5 .   ? 57.499  -11.929 22.694  1.00 35.57 ? 2257 HOH D O   1 
HETATM 9618 O  O   . HOH CA 5 .   ? 43.456  -16.526 26.136  1.00 18.49 ? 2258 HOH D O   1 
HETATM 9619 O  O   . HOH CA 5 .   ? 39.878  -14.437 25.453  1.00 31.22 ? 2259 HOH D O   1 
HETATM 9620 O  O   . HOH CA 5 .   ? 38.440  -11.879 24.374  1.00 26.11 ? 2260 HOH D O   1 
HETATM 9621 O  O   . HOH CA 5 .   ? 37.338  -12.229 20.157  1.00 29.82 ? 2261 HOH D O   1 
HETATM 9622 O  O   . HOH CA 5 .   ? 41.651  -18.091 23.415  1.00 45.43 ? 2262 HOH D O   1 
HETATM 9623 O  O   . HOH CA 5 .   ? 39.347  -17.336 24.936  1.00 46.42 ? 2263 HOH D O   1 
HETATM 9624 O  O   . HOH CA 5 .   ? 42.605  -16.770 20.998  1.00 39.15 ? 2264 HOH D O   1 
HETATM 9625 O  O   . HOH CA 5 .   ? 40.488  -12.468 -9.611  1.00 20.73 ? 2265 HOH D O   1 
HETATM 9626 O  O   . HOH CA 5 .   ? 41.696  11.321  9.658   1.00 22.42 ? 2266 HOH D O   1 
HETATM 9627 O  O   . HOH CA 5 .   ? 48.574  13.772  4.074   1.00 27.65 ? 2267 HOH D O   1 
HETATM 9628 O  O   . HOH DA 5 .   ? 51.512  -13.048 61.685  1.00 46.63 ? 2001 HOH E O   1 
HETATM 9629 O  O   . HOH DA 5 .   ? 45.528  -19.954 59.374  1.00 21.25 ? 2002 HOH E O   1 
HETATM 9630 O  O   . HOH DA 5 .   ? 45.665  -16.947 59.767  1.00 19.55 ? 2003 HOH E O   1 
HETATM 9631 O  O   . HOH DA 5 .   ? 43.205  -20.421 58.208  1.00 17.93 ? 2004 HOH E O   1 
HETATM 9632 O  O   . HOH DA 5 .   ? 42.913  -16.020 59.547  1.00 35.27 ? 2005 HOH E O   1 
HETATM 9633 O  O   . HOH DA 5 .   ? 36.072  10.355  63.201  1.00 30.69 ? 2006 HOH E O   1 
HETATM 9634 O  O   . HOH DA 5 .   ? 36.726  -16.531 55.854  1.00 23.19 ? 2007 HOH E O   1 
HETATM 9635 O  O   . HOH DA 5 .   ? 40.408  -16.647 56.563  1.00 19.30 ? 2008 HOH E O   1 
HETATM 9636 O  O   . HOH DA 5 .   ? 33.470  10.904  52.759  1.00 30.18 ? 2009 HOH E O   1 
HETATM 9637 O  O   . HOH DA 5 .   ? 34.235  10.640  45.978  1.00 30.95 ? 2010 HOH E O   1 
HETATM 9638 O  O   . HOH DA 5 .   ? 34.588  -15.187 56.294  1.00 32.70 ? 2011 HOH E O   1 
HETATM 9639 O  O   . HOH DA 5 .   ? 33.723  -15.615 53.689  1.00 25.73 ? 2012 HOH E O   1 
HETATM 9640 O  O   . HOH DA 5 .   ? 49.921  5.662   59.976  1.00 37.73 ? 2013 HOH E O   1 
HETATM 9641 O  O   . HOH DA 5 .   ? 37.976  -16.491 60.604  1.00 39.74 ? 2014 HOH E O   1 
HETATM 9642 O  O   . HOH DA 5 .   ? 38.706  -11.946 49.147  1.00 22.40 ? 2015 HOH E O   1 
HETATM 9643 O  O   . HOH DA 5 .   ? 38.534  -11.714 60.640  1.00 30.29 ? 2016 HOH E O   1 
HETATM 9644 O  O   . HOH DA 5 .   ? 56.886  12.526  36.489  1.00 32.88 ? 2017 HOH E O   1 
HETATM 9645 O  O   . HOH DA 5 .   ? 31.995  6.330   53.627  1.00 16.01 ? 2018 HOH E O   1 
HETATM 9646 O  O   . HOH DA 5 .   ? 35.485  10.355  58.612  1.00 24.48 ? 2019 HOH E O   1 
HETATM 9647 O  O   . HOH DA 5 .   ? 38.630  9.281   62.556  1.00 29.66 ? 2020 HOH E O   1 
HETATM 9648 O  O   . HOH DA 5 .   ? 37.602  13.153  47.167  1.00 15.05 ? 2021 HOH E O   1 
HETATM 9649 O  O   . HOH DA 5 .   ? 35.590  10.827  55.435  1.00 14.90 ? 2022 HOH E O   1 
HETATM 9650 O  O   . HOH DA 5 .   ? 34.281  9.975   48.574  1.00 26.29 ? 2023 HOH E O   1 
HETATM 9651 O  O   . HOH DA 5 .   ? 33.691  8.211   52.348  1.00 20.08 ? 2024 HOH E O   1 
HETATM 9652 O  O   . HOH DA 5 .   ? 40.562  6.291   53.197  1.00 11.73 ? 2025 HOH E O   1 
HETATM 9653 O  O   . HOH DA 5 .   ? 48.644  10.504  55.940  1.00 27.71 ? 2026 HOH E O   1 
HETATM 9654 O  O   . HOH DA 5 .   ? 30.076  6.344   35.789  1.00 24.56 ? 2027 HOH E O   1 
HETATM 9655 O  O   . HOH DA 5 .   ? 33.302  12.048  42.293  1.00 24.73 ? 2028 HOH E O   1 
HETATM 9656 O  O   . HOH DA 5 .   ? 34.259  9.565   35.080  1.00 36.71 ? 2029 HOH E O   1 
HETATM 9657 O  O   . HOH DA 5 .   ? 36.797  13.530  39.632  1.00 20.81 ? 2030 HOH E O   1 
HETATM 9658 O  O   . HOH DA 5 .   ? 47.214  6.254   59.480  1.00 26.25 ? 2031 HOH E O   1 
HETATM 9659 O  O   . HOH DA 5 .   ? 38.864  3.728   55.187  1.00 11.98 ? 2032 HOH E O   1 
HETATM 9660 O  O   . HOH DA 5 .   ? 52.451  3.276   57.425  1.00 19.85 ? 2033 HOH E O   1 
HETATM 9661 O  O   . HOH DA 5 .   ? 67.155  3.786   43.406  1.00 25.49 ? 2034 HOH E O   1 
HETATM 9662 O  O   . HOH DA 5 .   ? 58.047  12.605  42.728  1.00 38.15 ? 2035 HOH E O   1 
HETATM 9663 O  O   . HOH DA 5 .   ? 56.207  10.749  38.438  1.00 26.35 ? 2036 HOH E O   1 
HETATM 9664 O  O   . HOH DA 5 .   ? 54.280  0.061   53.244  1.00 31.65 ? 2037 HOH E O   1 
HETATM 9665 O  O   . HOH DA 5 .   ? 53.942  2.658   54.390  1.00 25.82 ? 2038 HOH E O   1 
HETATM 9666 O  O   . HOH DA 5 .   ? 55.398  -2.262  52.568  1.00 15.13 ? 2039 HOH E O   1 
HETATM 9667 O  O   . HOH DA 5 .   ? 52.760  -10.397 52.626  1.00 16.60 ? 2040 HOH E O   1 
HETATM 9668 O  O   . HOH DA 5 .   ? 56.468  -11.030 54.291  1.00 25.76 ? 2041 HOH E O   1 
HETATM 9669 O  O   . HOH DA 5 .   ? 43.008  13.238  40.867  1.00 29.29 ? 2042 HOH E O   1 
HETATM 9670 O  O   . HOH DA 5 .   ? 58.154  -5.311  52.256  1.00 34.01 ? 2043 HOH E O   1 
HETATM 9671 O  O   . HOH DA 5 .   ? 34.225  9.079   32.501  1.00 39.77 ? 2044 HOH E O   1 
HETATM 9672 O  O   . HOH DA 5 .   ? 37.499  10.701  29.239  1.00 45.78 ? 2045 HOH E O   1 
HETATM 9673 O  O   . HOH DA 5 .   ? 64.263  -11.414 46.543  1.00 32.05 ? 2046 HOH E O   1 
HETATM 9674 O  O   . HOH DA 5 .   ? 68.020  -4.651  46.621  1.00 42.17 ? 2047 HOH E O   1 
HETATM 9675 O  O   . HOH DA 5 .   ? 56.458  10.966  34.244  1.00 43.82 ? 2048 HOH E O   1 
HETATM 9676 O  O   . HOH DA 5 .   ? 51.995  10.542  34.146  1.00 34.06 ? 2049 HOH E O   1 
HETATM 9677 O  O   . HOH DA 5 .   ? 67.049  -9.046  39.432  1.00 26.90 ? 2050 HOH E O   1 
HETATM 9678 O  O   . HOH DA 5 .   ? 43.928  6.543   27.512  1.00 29.65 ? 2051 HOH E O   1 
HETATM 9679 O  O   . HOH DA 5 .   ? 31.497  -6.343  32.888  1.00 30.73 ? 2052 HOH E O   1 
HETATM 9680 O  O   . HOH DA 5 .   ? 29.597  4.508   33.827  1.00 35.78 ? 2053 HOH E O   1 
HETATM 9681 O  O   . HOH DA 5 .   ? 27.293  3.191   34.202  1.00 42.68 ? 2054 HOH E O   1 
HETATM 9682 O  O   . HOH DA 5 .   ? 63.610  -10.665 38.099  1.00 32.43 ? 2055 HOH E O   1 
HETATM 9683 O  O   . HOH DA 5 .   ? 63.805  -11.604 30.760  1.00 36.95 ? 2056 HOH E O   1 
HETATM 9684 O  O   . HOH DA 5 .   ? 28.003  -3.606  29.949  1.00 34.40 ? 2057 HOH E O   1 
HETATM 9685 O  O   . HOH DA 5 .   ? 29.406  -6.447  36.434  1.00 28.66 ? 2058 HOH E O   1 
HETATM 9686 O  O   . HOH DA 5 .   ? 61.490  -10.268 30.881  1.00 12.28 ? 2059 HOH E O   1 
HETATM 9687 O  O   . HOH DA 5 .   ? 60.981  -11.232 38.108  1.00 20.38 ? 2060 HOH E O   1 
HETATM 9688 O  O   . HOH DA 5 .   ? 28.313  -8.297  39.909  1.00 38.94 ? 2061 HOH E O   1 
HETATM 9689 O  O   . HOH DA 5 .   ? 66.154  -4.115  26.210  1.00 26.82 ? 2062 HOH E O   1 
HETATM 9690 O  O   . HOH DA 5 .   ? 34.763  -16.181 41.969  1.00 37.92 ? 2063 HOH E O   1 
HETATM 9691 O  O   . HOH DA 5 .   ? 35.573  -10.072 41.725  1.00 18.82 ? 2064 HOH E O   1 
HETATM 9692 O  O   . HOH DA 5 .   ? 32.664  -0.087  40.454  1.00 10.96 ? 2065 HOH E O   1 
HETATM 9693 O  O   . HOH DA 5 .   ? 50.216  -15.455 26.115  1.00 27.10 ? 2066 HOH E O   1 
HETATM 9694 O  O   . HOH DA 5 .   ? 32.805  5.587   47.970  1.00 15.00 ? 2067 HOH E O   1 
HETATM 9695 O  O   . HOH DA 5 .   ? 30.521  7.661   42.508  1.00 21.95 ? 2068 HOH E O   1 
HETATM 9696 O  O   . HOH DA 5 .   ? 30.883  6.843   46.359  1.00 18.51 ? 2069 HOH E O   1 
HETATM 9697 O  O   . HOH DA 5 .   ? 33.911  4.584   38.571  1.00 26.82 ? 2070 HOH E O   1 
HETATM 9698 O  O   . HOH DA 5 .   ? 34.524  7.498   36.573  1.00 13.67 ? 2071 HOH E O   1 
HETATM 9699 O  O   . HOH DA 5 .   ? 33.672  9.664   43.557  1.00 12.39 ? 2072 HOH E O   1 
HETATM 9700 O  O   . HOH DA 5 .   ? 32.042  6.222   37.570  1.00 21.21 ? 2073 HOH E O   1 
HETATM 9701 O  O   . HOH DA 5 .   ? 34.253  11.911  39.608  1.00 26.49 ? 2074 HOH E O   1 
HETATM 9702 O  O   . HOH DA 5 .   ? 38.211  5.948   38.932  1.00 12.50 ? 2075 HOH E O   1 
HETATM 9703 O  O   . HOH DA 5 .   ? 39.340  12.177  39.573  1.00 17.17 ? 2076 HOH E O   1 
HETATM 9704 O  O   . HOH DA 5 .   ? 34.789  2.457   41.219  1.00 13.59 ? 2077 HOH E O   1 
HETATM 9705 O  O   . HOH DA 5 .   ? 37.448  -1.034  41.334  1.00 16.29 ? 2078 HOH E O   1 
HETATM 9706 O  O   . HOH DA 5 .   ? 44.506  4.414   47.157  1.00 18.13 ? 2079 HOH E O   1 
HETATM 9707 O  O   . HOH DA 5 .   ? 47.039  1.924   46.567  1.00 8.74  ? 2080 HOH E O   1 
HETATM 9708 O  O   . HOH DA 5 .   ? 58.845  13.890  49.679  1.00 35.28 ? 2081 HOH E O   1 
HETATM 9709 O  O   . HOH DA 5 .   ? 52.687  4.557   43.913  1.00 8.65  ? 2082 HOH E O   1 
HETATM 9710 O  O   . HOH DA 5 .   ? 47.762  16.518  48.121  1.00 24.83 ? 2083 HOH E O   1 
HETATM 9711 O  O   . HOH DA 5 .   ? 43.437  16.433  52.564  1.00 19.02 ? 2084 HOH E O   1 
HETATM 9712 O  O   . HOH DA 5 .   ? 59.269  6.893   47.068  1.00 15.98 ? 2085 HOH E O   1 
HETATM 9713 O  O   . HOH DA 5 .   ? 36.391  -16.275 48.530  1.00 32.14 ? 2086 HOH E O   1 
HETATM 9714 O  O   . HOH DA 5 .   ? 64.969  2.902   44.836  1.00 16.92 ? 2087 HOH E O   1 
HETATM 9715 O  O   . HOH DA 5 .   ? 65.096  3.914   52.488  1.00 37.22 ? 2088 HOH E O   1 
HETATM 9716 O  O   . HOH DA 5 .   ? 62.501  7.971   52.800  1.00 32.55 ? 2089 HOH E O   1 
HETATM 9717 O  O   . HOH DA 5 .   ? 66.582  6.410   44.112  1.00 33.86 ? 2090 HOH E O   1 
HETATM 9718 O  O   . HOH DA 5 .   ? 66.364  9.216   48.037  1.00 37.41 ? 2091 HOH E O   1 
HETATM 9719 O  O   . HOH DA 5 .   ? 61.293  8.359   48.272  1.00 20.00 ? 2092 HOH E O   1 
HETATM 9720 O  O   . HOH DA 5 .   ? 65.125  10.382  43.753  1.00 36.68 ? 2093 HOH E O   1 
HETATM 9721 O  O   . HOH DA 5 .   ? 66.166  6.877   41.696  1.00 25.84 ? 2094 HOH E O   1 
HETATM 9722 O  O   . HOH DA 5 .   ? 48.904  -17.782 25.317  1.00 31.29 ? 2095 HOH E O   1 
HETATM 9723 O  O   . HOH DA 5 .   ? 41.749  -21.633 30.813  1.00 30.70 ? 2096 HOH E O   1 
HETATM 9724 O  O   . HOH DA 5 .   ? 54.569  11.369  40.612  1.00 23.41 ? 2097 HOH E O   1 
HETATM 9725 O  O   . HOH DA 5 .   ? 55.315  12.382  43.786  1.00 33.76 ? 2098 HOH E O   1 
HETATM 9726 O  O   . HOH DA 5 .   ? 31.181  -10.302 34.891  1.00 47.96 ? 2099 HOH E O   1 
HETATM 9727 O  O   . HOH DA 5 .   ? 59.950  5.362   39.660  1.00 10.29 ? 2100 HOH E O   1 
HETATM 9728 O  O   . HOH DA 5 .   ? 51.500  -21.042 54.761  1.00 40.99 ? 2101 HOH E O   1 
HETATM 9729 O  O   . HOH DA 5 .   ? 47.452  -20.735 57.636  1.00 24.54 ? 2102 HOH E O   1 
HETATM 9730 O  O   . HOH DA 5 .   ? 51.417  -19.340 56.684  1.00 32.76 ? 2103 HOH E O   1 
HETATM 9731 O  O   . HOH DA 5 .   ? 36.545  4.008   38.312  1.00 18.63 ? 2104 HOH E O   1 
HETATM 9732 O  O   . HOH DA 5 .   ? 34.398  1.855   38.519  1.00 23.54 ? 2105 HOH E O   1 
HETATM 9733 O  O   . HOH DA 5 .   ? 41.268  -7.670  62.153  1.00 31.24 ? 2106 HOH E O   1 
HETATM 9734 O  O   . HOH DA 5 .   ? 44.160  -1.620  64.029  1.00 38.97 ? 2107 HOH E O   1 
HETATM 9735 O  O   . HOH DA 5 .   ? 37.476  9.976   37.477  1.00 16.23 ? 2108 HOH E O   1 
HETATM 9736 O  O   . HOH DA 5 .   ? 44.287  11.374  39.195  1.00 19.91 ? 2109 HOH E O   1 
HETATM 9737 O  O   . HOH DA 5 .   ? 43.336  4.780   34.377  1.00 15.73 ? 2110 HOH E O   1 
HETATM 9738 O  O   . HOH DA 5 .   ? 46.141  10.325  36.000  1.00 33.54 ? 2111 HOH E O   1 
HETATM 9739 O  O   . HOH DA 5 .   ? 46.500  6.938   35.094  1.00 17.10 ? 2112 HOH E O   1 
HETATM 9740 O  O   . HOH DA 5 .   ? 43.086  -3.951  63.117  1.00 34.54 ? 2113 HOH E O   1 
HETATM 9741 O  O   . HOH DA 5 .   ? 28.618  -15.351 51.442  1.00 36.13 ? 2114 HOH E O   1 
HETATM 9742 O  O   . HOH DA 5 .   ? 35.252  6.666   31.341  1.00 32.40 ? 2115 HOH E O   1 
HETATM 9743 O  O   . HOH DA 5 .   ? 42.707  6.485   32.291  1.00 25.16 ? 2116 HOH E O   1 
HETATM 9744 O  O   . HOH DA 5 .   ? 36.840  5.046   28.449  1.00 36.77 ? 2117 HOH E O   1 
HETATM 9745 O  O   . HOH DA 5 .   ? 39.879  8.922   28.147  1.00 44.18 ? 2118 HOH E O   1 
HETATM 9746 O  O   . HOH DA 5 .   ? 36.887  -1.199  38.698  1.00 16.94 ? 2119 HOH E O   1 
HETATM 9747 O  O   . HOH DA 5 .   ? 54.474  8.949   37.171  1.00 11.34 ? 2120 HOH E O   1 
HETATM 9748 O  O   . HOH DA 5 .   ? 58.402  11.215  40.170  1.00 22.15 ? 2121 HOH E O   1 
HETATM 9749 O  O   . HOH DA 5 .   ? 54.112  9.171   33.477  1.00 26.11 ? 2122 HOH E O   1 
HETATM 9750 O  O   . HOH DA 5 .   ? 59.268  10.096  33.445  1.00 36.34 ? 2123 HOH E O   1 
HETATM 9751 O  O   . HOH DA 5 .   ? 58.642  3.415   28.552  1.00 12.98 ? 2124 HOH E O   1 
HETATM 9752 O  O   . HOH DA 5 .   ? 54.319  7.902   30.687  1.00 18.17 ? 2125 HOH E O   1 
HETATM 9753 O  O   . HOH DA 5 .   ? 54.863  4.770   28.662  1.00 23.30 ? 2126 HOH E O   1 
HETATM 9754 O  O   . HOH DA 5 .   ? 50.904  5.629   27.811  1.00 28.25 ? 2127 HOH E O   1 
HETATM 9755 O  O   . HOH DA 5 .   ? 48.192  11.337  34.882  1.00 36.49 ? 2128 HOH E O   1 
HETATM 9756 O  O   . HOH DA 5 .   ? 49.095  3.367   26.849  1.00 11.66 ? 2129 HOH E O   1 
HETATM 9757 O  O   . HOH DA 5 .   ? 43.948  3.847   26.610  1.00 22.65 ? 2130 HOH E O   1 
HETATM 9758 O  O   . HOH DA 5 .   ? 48.244  6.602   29.509  1.00 32.19 ? 2131 HOH E O   1 
HETATM 9759 O  O   . HOH DA 5 .   ? 45.844  7.659   30.814  1.00 35.29 ? 2132 HOH E O   1 
HETATM 9760 O  O   . HOH DA 5 .   ? 41.817  -2.383  25.929  1.00 9.43  ? 2133 HOH E O   1 
HETATM 9761 O  O   . HOH DA 5 .   ? 36.676  6.165   25.813  1.00 33.49 ? 2134 HOH E O   1 
HETATM 9762 O  O   . HOH DA 5 .   ? 36.253  2.277   28.240  1.00 22.06 ? 2135 HOH E O   1 
HETATM 9763 O  O   . HOH DA 5 .   ? 33.320  1.042   30.660  1.00 23.27 ? 2136 HOH E O   1 
HETATM 9764 O  O   . HOH DA 5 .   ? 35.864  -3.912  26.409  1.00 17.30 ? 2137 HOH E O   1 
HETATM 9765 O  O   . HOH DA 5 .   ? 34.403  -5.788  32.279  1.00 30.46 ? 2138 HOH E O   1 
HETATM 9766 O  O   . HOH DA 5 .   ? 34.309  -2.178  38.223  1.00 16.29 ? 2139 HOH E O   1 
HETATM 9767 O  O   . HOH DA 5 .   ? 33.330  -5.385  36.693  1.00 16.59 ? 2140 HOH E O   1 
HETATM 9768 O  O   . HOH DA 5 .   ? 29.308  1.866   32.862  1.00 39.92 ? 2141 HOH E O   1 
HETATM 9769 O  O   . HOH DA 5 .   ? 33.139  0.035   37.188  1.00 17.25 ? 2142 HOH E O   1 
HETATM 9770 O  O   . HOH DA 5 .   ? 31.188  -5.007  35.045  1.00 18.17 ? 2143 HOH E O   1 
HETATM 9771 O  O   . HOH DA 5 .   ? 29.844  -5.229  30.925  1.00 36.77 ? 2144 HOH E O   1 
HETATM 9772 O  O   . HOH DA 5 .   ? 26.809  0.554   34.253  1.00 23.18 ? 2145 HOH E O   1 
HETATM 9773 O  O   . HOH DA 5 .   ? 25.192  3.394   38.142  1.00 25.04 ? 2146 HOH E O   1 
HETATM 9774 O  O   . HOH DA 5 .   ? 26.747  -4.016  39.895  1.00 26.03 ? 2147 HOH E O   1 
HETATM 9775 O  O   . HOH DA 5 .   ? 34.655  -1.807  41.700  1.00 8.11  ? 2148 HOH E O   1 
HETATM 9776 O  O   . HOH DA 5 .   ? 31.006  -7.749  38.316  1.00 22.82 ? 2149 HOH E O   1 
HETATM 9777 O  O   . HOH DA 5 .   ? 40.764  -10.968 35.419  1.00 9.65  ? 2150 HOH E O   1 
HETATM 9778 O  O   . HOH DA 5 .   ? 49.702  -12.056 31.808  1.00 13.71 ? 2151 HOH E O   1 
HETATM 9779 O  O   . HOH DA 5 .   ? 53.147  -9.187  30.233  1.00 10.22 ? 2152 HOH E O   1 
HETATM 9780 O  O   . HOH DA 5 .   ? 57.904  -13.811 26.079  1.00 40.25 ? 2153 HOH E O   1 
HETATM 9781 O  O   . HOH DA 5 .   ? 65.146  -7.297  30.565  1.00 21.03 ? 2154 HOH E O   1 
HETATM 9782 O  O   . HOH DA 5 .   ? 64.823  -6.804  25.505  1.00 30.56 ? 2155 HOH E O   1 
HETATM 9783 O  O   . HOH DA 5 .   ? 61.110  -8.769  22.932  1.00 31.41 ? 2156 HOH E O   1 
HETATM 9784 O  O   . HOH DA 5 .   ? 60.741  -10.779 25.095  1.00 33.50 ? 2157 HOH E O   1 
HETATM 9785 O  O   . HOH DA 5 .   ? 53.160  -10.746 27.966  1.00 16.39 ? 2158 HOH E O   1 
HETATM 9786 O  O   . HOH DA 5 .   ? 49.133  -14.127 29.412  1.00 24.33 ? 2159 HOH E O   1 
HETATM 9787 O  O   . HOH DA 5 .   ? 47.044  -4.245  28.877  1.00 13.67 ? 2160 HOH E O   1 
HETATM 9788 O  O   . HOH DA 5 .   ? 35.373  -7.785  30.799  1.00 29.38 ? 2161 HOH E O   1 
HETATM 9789 O  O   . HOH DA 5 .   ? 34.338  -9.799  39.078  1.00 24.00 ? 2162 HOH E O   1 
HETATM 9790 O  O   . HOH DA 5 .   ? 33.485  -8.348  32.392  1.00 36.98 ? 2163 HOH E O   1 
HETATM 9791 O  O   . HOH DA 5 .   ? 39.565  -15.020 28.392  1.00 30.45 ? 2164 HOH E O   1 
HETATM 9792 O  O   . HOH DA 5 .   ? 39.087  -9.351  24.687  1.00 24.40 ? 2165 HOH E O   1 
HETATM 9793 O  O   . HOH DA 5 .   ? 46.116  -7.608  28.087  1.00 13.34 ? 2166 HOH E O   1 
HETATM 9794 O  O   . HOH DA 5 .   ? 50.183  -12.905 24.784  1.00 24.02 ? 2167 HOH E O   1 
HETATM 9795 O  O   . HOH DA 5 .   ? 46.814  -9.770  26.581  1.00 13.55 ? 2168 HOH E O   1 
HETATM 9796 O  O   . HOH DA 5 .   ? 46.992  3.795   25.205  1.00 15.14 ? 2169 HOH E O   1 
HETATM 9797 O  O   . HOH DA 5 .   ? 54.859  3.337   26.378  1.00 26.29 ? 2170 HOH E O   1 
HETATM 9798 O  O   . HOH DA 5 .   ? 59.141  0.129   25.984  1.00 24.66 ? 2171 HOH E O   1 
HETATM 9799 O  O   . HOH DA 5 .   ? 62.288  -2.755  20.666  1.00 30.85 ? 2172 HOH E O   1 
HETATM 9800 O  O   . HOH DA 5 .   ? 61.942  0.015   24.099  1.00 27.82 ? 2173 HOH E O   1 
HETATM 9801 O  O   . HOH DA 5 .   ? 62.174  -5.918  20.920  1.00 33.93 ? 2174 HOH E O   1 
HETATM 9802 O  O   . HOH DA 5 .   ? 67.765  -5.179  30.512  1.00 20.91 ? 2175 HOH E O   1 
HETATM 9803 O  O   . HOH DA 5 .   ? 68.040  -2.710  33.353  1.00 24.59 ? 2176 HOH E O   1 
HETATM 9804 O  O   . HOH DA 5 .   ? 66.541  -0.885  35.529  1.00 18.50 ? 2177 HOH E O   1 
HETATM 9805 O  O   . HOH DA 5 .   ? 66.126  -0.782  38.852  1.00 22.97 ? 2178 HOH E O   1 
HETATM 9806 O  O   . HOH DA 5 .   ? 66.615  2.109   41.398  1.00 30.18 ? 2179 HOH E O   1 
HETATM 9807 O  O   . HOH DA 5 .   ? 68.589  -3.362  44.106  1.00 40.43 ? 2180 HOH E O   1 
HETATM 9808 O  O   . HOH DA 5 .   ? 63.875  0.994   48.486  1.00 17.06 ? 2181 HOH E O   1 
HETATM 9809 O  O   . HOH DA 5 .   ? 60.736  -3.938  51.274  1.00 30.98 ? 2182 HOH E O   1 
HETATM 9810 O  O   . HOH DA 5 .   ? 57.978  -2.966  53.068  1.00 33.08 ? 2183 HOH E O   1 
HETATM 9811 O  O   . HOH DA 5 .   ? 57.385  -2.285  55.801  1.00 40.02 ? 2184 HOH E O   1 
HETATM 9812 O  O   . HOH DA 5 .   ? 55.867  1.993   56.240  1.00 40.98 ? 2185 HOH E O   1 
HETATM 9813 O  O   . HOH DA 5 .   ? 44.241  0.601   47.046  1.00 10.73 ? 2186 HOH E O   1 
HETATM 9814 O  O   . HOH DA 5 .   ? 46.248  8.462   48.656  1.00 7.42  ? 2187 HOH E O   1 
HETATM 9815 O  O   . HOH DA 5 .   ? 49.751  10.526  47.078  1.00 10.35 ? 2188 HOH E O   1 
HETATM 9816 O  O   . HOH DA 5 .   ? 52.020  14.474  47.472  1.00 20.21 ? 2189 HOH E O   1 
HETATM 9817 O  O   . HOH DA 5 .   ? 58.770  9.350   45.834  1.00 23.08 ? 2190 HOH E O   1 
HETATM 9818 O  O   . HOH DA 5 .   ? 57.558  13.451  47.108  1.00 42.87 ? 2191 HOH E O   1 
HETATM 9819 O  O   . HOH DA 5 .   ? 57.036  10.300  53.785  1.00 29.25 ? 2192 HOH E O   1 
HETATM 9820 O  O   . HOH DA 5 .   ? 60.666  9.132   50.884  1.00 19.93 ? 2193 HOH E O   1 
HETATM 9821 O  O   . HOH DA 5 .   ? 65.294  1.345   51.047  1.00 30.53 ? 2194 HOH E O   1 
HETATM 9822 O  O   . HOH DA 5 .   ? 52.820  7.067   56.178  1.00 30.60 ? 2195 HOH E O   1 
HETATM 9823 O  O   . HOH DA 5 .   ? 53.763  11.058  54.889  1.00 32.35 ? 2196 HOH E O   1 
HETATM 9824 O  O   . HOH DA 5 .   ? 50.543  11.315  54.100  1.00 16.69 ? 2197 HOH E O   1 
HETATM 9825 O  O   . HOH DA 5 .   ? 47.372  15.400  52.237  1.00 29.95 ? 2198 HOH E O   1 
HETATM 9826 O  O   . HOH DA 5 .   ? 50.109  13.857  52.521  1.00 28.46 ? 2199 HOH E O   1 
HETATM 9827 O  O   . HOH DA 5 .   ? 50.994  14.107  50.085  1.00 34.67 ? 2200 HOH E O   1 
HETATM 9828 O  O   . HOH DA 5 .   ? 48.932  13.259  44.766  1.00 10.20 ? 2201 HOH E O   1 
HETATM 9829 O  O   . HOH DA 5 .   ? 45.173  15.991  48.584  1.00 18.38 ? 2202 HOH E O   1 
HETATM 9830 O  O   . HOH DA 5 .   ? 45.223  14.075  42.789  1.00 33.17 ? 2203 HOH E O   1 
HETATM 9831 O  O   . HOH DA 5 .   ? 45.803  15.911  44.341  1.00 32.33 ? 2204 HOH E O   1 
HETATM 9832 O  O   . HOH DA 5 .   ? 44.863  14.812  50.921  1.00 12.03 ? 2205 HOH E O   1 
HETATM 9833 O  O   . HOH DA 5 .   ? 34.901  12.876  51.560  1.00 20.84 ? 2206 HOH E O   1 
HETATM 9834 O  O   . HOH DA 5 .   ? 38.479  12.875  56.688  1.00 21.98 ? 2207 HOH E O   1 
HETATM 9835 O  O   . HOH DA 5 .   ? 40.672  12.478  42.157  1.00 15.00 ? 2208 HOH E O   1 
HETATM 9836 O  O   . HOH DA 5 .   ? 42.799  16.294  43.207  1.00 25.46 ? 2209 HOH E O   1 
HETATM 9837 O  O   . HOH DA 5 .   ? 41.558  4.222   51.956  1.00 9.24  ? 2210 HOH E O   1 
HETATM 9838 O  O   . HOH DA 5 .   ? 33.340  2.904   47.405  1.00 10.45 ? 2211 HOH E O   1 
HETATM 9839 O  O   . HOH DA 5 .   ? 29.886  -5.577  50.236  1.00 8.79  ? 2212 HOH E O   1 
HETATM 9840 O  O   . HOH DA 5 .   ? 32.299  -8.074  51.692  1.00 10.26 ? 2213 HOH E O   1 
HETATM 9841 O  O   . HOH DA 5 .   ? 42.818  -13.133 42.433  1.00 9.84  ? 2214 HOH E O   1 
HETATM 9842 O  O   . HOH DA 5 .   ? 40.966  -16.472 49.091  1.00 18.95 ? 2215 HOH E O   1 
HETATM 9843 O  O   . HOH DA 5 .   ? 38.463  -14.842 49.252  1.00 27.97 ? 2216 HOH E O   1 
HETATM 9844 O  O   . HOH DA 5 .   ? 36.969  -15.678 45.958  1.00 25.93 ? 2217 HOH E O   1 
HETATM 9845 O  O   . HOH DA 5 .   ? 39.300  -16.460 44.395  1.00 34.86 ? 2218 HOH E O   1 
HETATM 9846 O  O   . HOH DA 5 .   ? 41.437  -16.628 45.770  1.00 17.39 ? 2219 HOH E O   1 
HETATM 9847 O  O   . HOH DA 5 .   ? 56.205  -16.831 39.787  1.00 16.47 ? 2220 HOH E O   1 
HETATM 9848 O  O   . HOH DA 5 .   ? 61.164  -17.703 41.670  1.00 27.96 ? 2221 HOH E O   1 
HETATM 9849 O  O   . HOH DA 5 .   ? 53.703  -16.598 30.452  1.00 28.89 ? 2222 HOH E O   1 
HETATM 9850 O  O   . HOH DA 5 .   ? 42.190  -22.117 33.568  1.00 18.22 ? 2223 HOH E O   1 
HETATM 9851 O  O   . HOH DA 5 .   ? 42.938  -19.836 29.017  1.00 25.38 ? 2224 HOH E O   1 
HETATM 9852 O  O   . HOH DA 5 .   ? 49.547  -20.282 27.005  1.00 40.04 ? 2225 HOH E O   1 
HETATM 9853 O  O   . HOH DA 5 .   ? 52.743  -20.462 35.345  1.00 25.81 ? 2226 HOH E O   1 
HETATM 9854 O  O   . HOH DA 5 .   ? 46.858  -17.910 39.167  1.00 11.31 ? 2227 HOH E O   1 
HETATM 9855 O  O   . HOH DA 5 .   ? 45.750  -22.686 35.633  1.00 20.33 ? 2228 HOH E O   1 
HETATM 9856 O  O   . HOH DA 5 .   ? 41.803  -23.648 37.998  1.00 24.39 ? 2229 HOH E O   1 
HETATM 9857 O  O   . HOH DA 5 .   ? 41.375  -15.355 43.304  1.00 19.51 ? 2230 HOH E O   1 
HETATM 9858 O  O   . HOH DA 5 .   ? 32.855  -14.058 33.423  1.00 32.61 ? 2231 HOH E O   1 
HETATM 9859 O  O   . HOH DA 5 .   ? 35.040  -14.783 39.900  1.00 29.08 ? 2232 HOH E O   1 
HETATM 9860 O  O   . HOH DA 5 .   ? 32.800  -11.048 37.297  1.00 40.52 ? 2233 HOH E O   1 
HETATM 9861 O  O   . HOH DA 5 .   ? 36.456  -17.781 33.714  1.00 35.73 ? 2234 HOH E O   1 
HETATM 9862 O  O   . HOH DA 5 .   ? 34.111  -19.533 40.248  1.00 40.64 ? 2235 HOH E O   1 
HETATM 9863 O  O   . HOH DA 5 .   ? 40.464  -18.973 46.413  1.00 19.02 ? 2236 HOH E O   1 
HETATM 9864 O  O   . HOH DA 5 .   ? 39.861  -22.913 44.533  1.00 18.00 ? 2237 HOH E O   1 
HETATM 9865 O  O   . HOH DA 5 .   ? 45.897  -23.155 40.414  1.00 22.58 ? 2238 HOH E O   1 
HETATM 9866 O  O   . HOH DA 5 .   ? 46.408  -20.990 45.876  1.00 12.44 ? 2239 HOH E O   1 
HETATM 9867 O  O   . HOH DA 5 .   ? 52.568  -21.336 41.948  1.00 23.00 ? 2240 HOH E O   1 
HETATM 9868 O  O   . HOH DA 5 .   ? 54.688  -18.537 42.894  1.00 25.27 ? 2241 HOH E O   1 
HETATM 9869 O  O   . HOH DA 5 .   ? 54.096  -14.687 49.370  1.00 27.23 ? 2242 HOH E O   1 
HETATM 9870 O  O   . HOH DA 5 .   ? 58.543  -19.497 44.335  1.00 29.36 ? 2243 HOH E O   1 
HETATM 9871 O  O   . HOH DA 5 .   ? 58.290  -16.472 48.278  1.00 32.38 ? 2244 HOH E O   1 
HETATM 9872 O  O   . HOH DA 5 .   ? 47.638  -19.423 47.801  1.00 11.77 ? 2245 HOH E O   1 
HETATM 9873 O  O   . HOH DA 5 .   ? 50.334  -19.236 50.920  1.00 29.73 ? 2246 HOH E O   1 
HETATM 9874 O  O   . HOH DA 5 .   ? 52.189  -19.154 48.550  1.00 28.30 ? 2247 HOH E O   1 
HETATM 9875 O  O   . HOH DA 5 .   ? 48.904  -18.019 56.789  1.00 20.17 ? 2248 HOH E O   1 
HETATM 9876 O  O   . HOH DA 5 .   ? 47.115  -20.464 54.823  1.00 29.13 ? 2249 HOH E O   1 
HETATM 9877 O  O   . HOH DA 5 .   ? 49.077  -20.725 53.235  1.00 39.98 ? 2250 HOH E O   1 
HETATM 9878 O  O   . HOH DA 5 .   ? 52.424  -12.922 51.191  1.00 12.15 ? 2251 HOH E O   1 
HETATM 9879 O  O   . HOH DA 5 .   ? 54.032  -15.405 53.639  1.00 30.09 ? 2252 HOH E O   1 
HETATM 9880 O  O   . HOH DA 5 .   ? 57.367  -8.303  59.677  1.00 43.33 ? 2253 HOH E O   1 
HETATM 9881 O  O   . HOH DA 5 .   ? 49.914  -10.126 59.102  1.00 25.56 ? 2254 HOH E O   1 
HETATM 9882 O  O   . HOH DA 5 .   ? 44.256  -7.855  61.496  1.00 28.04 ? 2255 HOH E O   1 
HETATM 9883 O  O   . HOH DA 5 .   ? 48.860  -8.519  61.101  1.00 37.08 ? 2256 HOH E O   1 
HETATM 9884 O  O   . HOH DA 5 .   ? 54.824  -5.846  61.070  1.00 46.94 ? 2257 HOH E O   1 
HETATM 9885 O  O   . HOH DA 5 .   ? 47.719  -4.722  61.651  1.00 18.51 ? 2258 HOH E O   1 
HETATM 9886 O  O   . HOH DA 5 .   ? 47.159  -2.161  63.316  1.00 33.78 ? 2259 HOH E O   1 
HETATM 9887 O  O   . HOH DA 5 .   ? 50.036  -3.557  62.854  1.00 40.94 ? 2260 HOH E O   1 
HETATM 9888 O  O   . HOH DA 5 .   ? 44.111  0.902   63.189  1.00 25.76 ? 2261 HOH E O   1 
HETATM 9889 O  O   . HOH DA 5 .   ? 46.658  3.146   63.119  1.00 29.93 ? 2262 HOH E O   1 
HETATM 9890 O  O   . HOH DA 5 .   ? 40.595  -0.009  62.431  1.00 31.74 ? 2263 HOH E O   1 
HETATM 9891 O  O   . HOH DA 5 .   ? 33.193  4.585   61.862  1.00 15.60 ? 2264 HOH E O   1 
HETATM 9892 O  O   . HOH DA 5 .   ? 40.816  -3.482  61.893  1.00 18.82 ? 2265 HOH E O   1 
HETATM 9893 O  O   . HOH DA 5 .   ? 39.337  -5.910  61.386  1.00 15.07 ? 2266 HOH E O   1 
HETATM 9894 O  O   . HOH DA 5 .   ? 36.009  -11.337 59.080  1.00 27.80 ? 2267 HOH E O   1 
HETATM 9895 O  O   . HOH DA 5 .   ? 29.310  -8.062  60.393  1.00 31.83 ? 2268 HOH E O   1 
HETATM 9896 O  O   . HOH DA 5 .   ? 30.931  -14.925 53.135  1.00 35.28 ? 2269 HOH E O   1 
HETATM 9897 O  O   . HOH DA 5 .   ? 33.439  -15.281 49.863  1.00 40.06 ? 2270 HOH E O   1 
HETATM 9898 O  O   . HOH DA 5 .   ? 27.089  -13.574 49.872  1.00 20.44 ? 2271 HOH E O   1 
HETATM 9899 O  O   . HOH DA 5 .   ? 26.707  -11.860 46.388  1.00 27.10 ? 2272 HOH E O   1 
HETATM 9900 O  O   . HOH DA 5 .   ? 27.730  -9.644  44.150  1.00 24.45 ? 2273 HOH E O   1 
HETATM 9901 O  O   . HOH DA 5 .   ? 29.666  -13.949 43.814  1.00 38.43 ? 2274 HOH E O   1 
HETATM 9902 O  O   . HOH DA 5 .   ? 29.586  -10.142 41.722  1.00 48.54 ? 2275 HOH E O   1 
HETATM 9903 O  O   . HOH DA 5 .   ? 31.111  -14.135 48.008  1.00 34.72 ? 2276 HOH E O   1 
HETATM 9904 O  O   . HOH DA 5 .   ? 57.621  -14.959 33.236  1.00 25.43 ? 2277 HOH E O   1 
HETATM 9905 O  O   . HOH DA 5 .   ? 60.087  -14.829 35.773  1.00 22.04 ? 2278 HOH E O   1 
HETATM 9906 O  O   . HOH DA 5 .   ? 60.904  -14.617 26.488  1.00 45.81 ? 2279 HOH E O   1 
HETATM 9907 O  O   . HOH DA 5 .   ? 52.017  10.672  36.908  1.00 26.15 ? 2280 HOH E O   1 
HETATM 9908 O  O   . HOH DA 5 .   ? 52.095  14.144  43.265  1.00 31.13 ? 2281 HOH E O   1 
HETATM 9909 O  O   . HOH DA 5 .   ? 48.959  13.976  41.968  1.00 30.19 ? 2282 HOH E O   1 
HETATM 9910 O  O   . HOH DA 5 .   ? 46.295  14.362  36.438  1.00 42.64 ? 2283 HOH E O   1 
# 
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   HIS 1   1   1   HIS HIS A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  CYS 36  36  36  CYS CYS A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ARG 120 120 120 ARG ARG A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 ILE 154 154 154 ILE ILE A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 TYR 158 158 158 TYR TYR A . n 
A 1 159 MET 159 159 159 MET MET A . n 
A 1 160 TRP 160 160 160 TRP TRP A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 PRO 177 177 177 PRO PRO A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 TRP 185 185 185 TRP TRP A . n 
A 1 186 GLN 186 186 186 GLN GLN A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
B 1 1   HIS 1   1   1   HIS HIS B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   LYS 7   7   7   LYS LYS B . n 
B 1 8   VAL 8   8   8   VAL VAL B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  ARG 13  13  13  ARG ARG B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  THR 17  17  17  THR THR B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  HIS 19  19  19  HIS HIS B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  GLN 31  31  31  GLN GLN B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  THR 34  34  34  THR THR B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  CYS 36  36  36  CYS CYS B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  ARG 38  38  38  ARG ARG B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  TYR 47  47  47  TYR TYR B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  SER 51  51  51  SER SER B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  ASP 58  58  58  ASP ASP B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  LYS 65  65  65  LYS LYS B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  GLU 70  70  70  GLU GLU B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  TYR 74  74  74  TYR TYR B . n 
B 1 75  ILE 75  75  75  ILE ILE B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  ARG 77  77  77  ARG ARG B . n 
B 1 78  HIS 78  78  78  HIS HIS B . n 
B 1 79  LYS 79  79  79  LYS LYS B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  THR 81  81  81  THR THR B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  LYS 83  83  83  LYS LYS B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  PHE 88  88  88  PHE PHE B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  CYS 95  95  95  CYS CYS B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  SER 97  97  97  SER SER B . n 
B 1 98  TRP 98  98  98  TRP TRP B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 TRP 108 108 108 TRP TRP B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ARG 120 120 120 ARG ARG B . n 
B 1 121 GLN 121 121 121 GLN GLN B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 TYR 123 123 123 TYR TYR B . n 
B 1 124 PHE 124 124 124 PHE PHE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 LYS 130 130 130 LYS LYS B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 GLY 134 134 134 GLY GLY B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 GLN 137 137 137 GLN GLN B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 GLY 142 142 142 GLY GLY B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 ARG 146 146 146 ARG ARG B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 GLN 148 148 148 GLN GLN B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 ILE 154 154 154 ILE ILE B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 TYR 158 158 158 TYR TYR B . n 
B 1 159 MET 159 159 159 MET MET B . n 
B 1 160 TRP 160 160 160 TRP TRP B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 VAL 163 163 163 VAL VAL B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 PRO 166 166 166 PRO PRO B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 ASN 168 168 168 ASN ASN B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 TYR 173 173 173 TYR TYR B . n 
B 1 174 GLN 174 174 174 GLN GLN B . n 
B 1 175 GLY 175 175 175 GLY GLY B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 PRO 177 177 177 PRO PRO B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 PRO 179 179 179 PRO PRO B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 ASN 181 181 181 ASN ASN B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 TRP 185 185 185 TRP TRP B . n 
B 1 186 GLN 186 186 186 GLN GLN B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 ASN 189 189 189 ASN ASN B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 GLU 191 191 191 GLU GLU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 TYR 195 195 195 TYR TYR B . n 
B 1 196 VAL 196 196 196 VAL VAL B . n 
B 1 197 ILE 197 197 197 ILE ILE B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 LYS 199 199 199 LYS LYS B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 TRP 203 203 203 TRP TRP B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
C 1 1   HIS 1   1   1   HIS HIS C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   ASP 3   3   3   ASP ASP C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   SER 5   5   5   SER SER C . n 
C 1 6   GLY 6   6   6   GLY GLY C . n 
C 1 7   LYS 7   7   7   LYS LYS C . n 
C 1 8   VAL 8   8   8   VAL VAL C . n 
C 1 9   PHE 9   9   9   PHE PHE C . n 
C 1 10  VAL 10  10  10  VAL VAL C . n 
C 1 11  PHE 11  11  11  PHE PHE C . n 
C 1 12  PRO 12  12  12  PRO PRO C . n 
C 1 13  ARG 13  13  13  ARG ARG C . n 
C 1 14  GLU 14  14  14  GLU GLU C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  VAL 16  16  16  VAL VAL C . n 
C 1 17  THR 17  17  17  THR THR C . n 
C 1 18  ASP 18  18  18  ASP ASP C . n 
C 1 19  HIS 19  19  19  HIS HIS C . n 
C 1 20  VAL 20  20  20  VAL VAL C . n 
C 1 21  ASN 21  21  21  ASN ASN C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  ILE 23  23  23  ILE ILE C . n 
C 1 24  THR 24  24  24  THR THR C . n 
C 1 25  PRO 25  25  25  PRO PRO C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  LYS 28  28  28  LYS LYS C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  LEU 30  30  30  LEU LEU C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  ASN 32  32  32  ASN ASN C . n 
C 1 33  PHE 33  33  33  PHE PHE C . n 
C 1 34  THR 34  34  34  THR THR C . n 
C 1 35  LEU 35  35  35  LEU LEU C . n 
C 1 36  CYS 36  36  36  CYS CYS C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  ARG 38  38  38  ARG ARG C . n 
C 1 39  ALA 39  39  39  ALA ALA C . n 
C 1 40  TYR 40  40  40  TYR TYR C . n 
C 1 41  SER 41  41  41  SER SER C . n 
C 1 42  ASP 42  42  42  ASP ASP C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  SER 44  44  44  SER SER C . n 
C 1 45  ARG 45  45  45  ARG ARG C . n 
C 1 46  ALA 46  46  46  ALA ALA C . n 
C 1 47  TYR 47  47  47  TYR TYR C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  SER 51  51  51  SER SER C . n 
C 1 52  TYR 52  52  52  TYR TYR C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  GLN 55  55  55  GLN GLN C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  ARG 57  57  57  ARG ARG C . n 
C 1 58  ASP 58  58  58  ASP ASP C . n 
C 1 59  ASN 59  59  59  ASN ASN C . n 
C 1 60  GLU 60  60  60  GLU GLU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  LEU 62  62  62  LEU LEU C . n 
C 1 63  VAL 63  63  63  VAL VAL C . n 
C 1 64  TYR 64  64  64  TYR TYR C . n 
C 1 65  LYS 65  65  65  LYS LYS C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  ARG 67  67  67  ARG ARG C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  GLY 69  69  69  GLY GLY C . n 
C 1 70  GLU 70  70  70  GLU GLU C . n 
C 1 71  TYR 71  71  71  TYR TYR C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  LEU 73  73  73  LEU LEU C . n 
C 1 74  TYR 74  74  74  TYR TYR C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  GLY 76  76  76  GLY GLY C . n 
C 1 77  ARG 77  77  77  ARG ARG C . n 
C 1 78  HIS 78  78  78  HIS HIS C . n 
C 1 79  LYS 79  79  79  LYS LYS C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  THR 81  81  81  THR THR C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  LYS 83  83  83  LYS LYS C . n 
C 1 84  VAL 84  84  84  VAL VAL C . n 
C 1 85  ILE 85  85  85  ILE ILE C . n 
C 1 86  GLU 86  86  86  GLU GLU C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  PHE 88  88  88  PHE PHE C . n 
C 1 89  PRO 89  89  89  PRO PRO C . n 
C 1 90  ALA 90  90  90  ALA ALA C . n 
C 1 91  PRO 91  91  91  PRO PRO C . n 
C 1 92  VAL 92  92  92  VAL VAL C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  ILE 94  94  94  ILE ILE C . n 
C 1 95  CYS 95  95  95  CYS CYS C . n 
C 1 96  VAL 96  96  96  VAL VAL C . n 
C 1 97  SER 97  97  97  SER SER C . n 
C 1 98  TRP 98  98  98  TRP TRP C . n 
C 1 99  GLU 99  99  99  GLU GLU C . n 
C 1 100 SER 100 100 100 SER SER C . n 
C 1 101 SER 101 101 101 SER SER C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 ALA 105 105 105 ALA ALA C . n 
C 1 106 GLU 106 106 106 GLU GLU C . n 
C 1 107 PHE 107 107 107 PHE PHE C . n 
C 1 108 TRP 108 108 108 TRP TRP C . n 
C 1 109 ILE 109 109 109 ILE ILE C . n 
C 1 110 ASN 110 110 110 ASN ASN C . n 
C 1 111 GLY 111 111 111 GLY GLY C . n 
C 1 112 THR 112 112 112 THR THR C . n 
C 1 113 PRO 113 113 113 PRO PRO C . n 
C 1 114 LEU 114 114 114 LEU LEU C . n 
C 1 115 VAL 115 115 115 VAL VAL C . n 
C 1 116 LYS 116 116 116 LYS LYS C . n 
C 1 117 LYS 117 117 117 LYS LYS C . n 
C 1 118 GLY 118 118 118 GLY GLY C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 ARG 120 120 120 ARG ARG C . n 
C 1 121 GLN 121 121 121 GLN GLN C . n 
C 1 122 GLY 122 122 122 GLY GLY C . n 
C 1 123 TYR 123 123 123 TYR TYR C . n 
C 1 124 PHE 124 124 124 PHE PHE C . n 
C 1 125 VAL 125 125 125 VAL VAL C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 ALA 127 127 127 ALA ALA C . n 
C 1 128 GLN 128 128 128 GLN GLN C . n 
C 1 129 PRO 129 129 129 PRO PRO C . n 
C 1 130 LYS 130 130 130 LYS LYS C . n 
C 1 131 ILE 131 131 131 ILE ILE C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 GLN 135 135 135 GLN GLN C . n 
C 1 136 GLU 136 136 136 GLU GLU C . n 
C 1 137 GLN 137 137 137 GLN GLN C . n 
C 1 138 ASP 138 138 138 ASP ASP C . n 
C 1 139 SER 139 139 139 SER SER C . n 
C 1 140 TYR 140 140 140 TYR TYR C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 GLY 142 142 142 GLY GLY C . n 
C 1 143 LYS 143 143 143 LYS LYS C . n 
C 1 144 PHE 144 144 144 PHE PHE C . n 
C 1 145 ASP 145 145 145 ASP ASP C . n 
C 1 146 ARG 146 146 146 ARG ARG C . n 
C 1 147 SER 147 147 147 SER SER C . n 
C 1 148 GLN 148 148 148 GLN GLN C . n 
C 1 149 SER 149 149 149 SER SER C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 VAL 151 151 151 VAL VAL C . n 
C 1 152 GLY 152 152 152 GLY GLY C . n 
C 1 153 GLU 153 153 153 GLU GLU C . n 
C 1 154 ILE 154 154 154 ILE ILE C . n 
C 1 155 GLY 155 155 155 GLY GLY C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LEU 157 157 157 LEU LEU C . n 
C 1 158 TYR 158 158 158 TYR TYR C . n 
C 1 159 MET 159 159 159 MET MET C . n 
C 1 160 TRP 160 160 160 TRP TRP C . n 
C 1 161 ASP 161 161 161 ASP ASP C . n 
C 1 162 SER 162 162 162 SER SER C . n 
C 1 163 VAL 163 163 163 VAL VAL C . n 
C 1 164 LEU 164 164 164 LEU LEU C . n 
C 1 165 PRO 165 165 165 PRO PRO C . n 
C 1 166 PRO 166 166 166 PRO PRO C . n 
C 1 167 GLU 167 167 167 GLU GLU C . n 
C 1 168 ASN 168 168 168 ASN ASN C . n 
C 1 169 ILE 169 169 169 ILE ILE C . n 
C 1 170 LEU 170 170 170 LEU LEU C . n 
C 1 171 SER 171 171 171 SER SER C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 TYR 173 173 173 TYR TYR C . n 
C 1 174 GLN 174 174 174 GLN GLN C . n 
C 1 175 GLY 175 175 175 GLY GLY C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 PRO 177 177 177 PRO PRO C . n 
C 1 178 LEU 178 178 178 LEU LEU C . n 
C 1 179 PRO 179 179 179 PRO PRO C . n 
C 1 180 ALA 180 180 180 ALA ALA C . n 
C 1 181 ASN 181 181 181 ASN ASN C . n 
C 1 182 ILE 182 182 182 ILE ILE C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 ASP 184 184 184 ASP ASP C . n 
C 1 185 TRP 185 185 185 TRP TRP C . n 
C 1 186 GLN 186 186 186 GLN GLN C . n 
C 1 187 ALA 187 187 187 ALA ALA C . n 
C 1 188 LEU 188 188 188 LEU LEU C . n 
C 1 189 ASN 189 189 189 ASN ASN C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 GLU 191 191 191 GLU GLU C . n 
C 1 192 ILE 192 192 192 ILE ILE C . n 
C 1 193 ARG 193 193 193 ARG ARG C . n 
C 1 194 GLY 194 194 194 GLY GLY C . n 
C 1 195 TYR 195 195 195 TYR TYR C . n 
C 1 196 VAL 196 196 196 VAL VAL C . n 
C 1 197 ILE 197 197 197 ILE ILE C . n 
C 1 198 ILE 198 198 198 ILE ILE C . n 
C 1 199 LYS 199 199 199 LYS LYS C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 LEU 201 201 201 LEU LEU C . n 
C 1 202 VAL 202 202 202 VAL VAL C . n 
C 1 203 TRP 203 203 203 TRP TRP C . n 
C 1 204 VAL 204 204 204 VAL VAL C . n 
D 1 1   HIS 1   1   1   HIS HIS D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   ASP 3   3   3   ASP ASP D . n 
D 1 4   LEU 4   4   4   LEU LEU D . n 
D 1 5   SER 5   5   5   SER SER D . n 
D 1 6   GLY 6   6   6   GLY GLY D . n 
D 1 7   LYS 7   7   7   LYS LYS D . n 
D 1 8   VAL 8   8   8   VAL VAL D . n 
D 1 9   PHE 9   9   9   PHE PHE D . n 
D 1 10  VAL 10  10  10  VAL VAL D . n 
D 1 11  PHE 11  11  11  PHE PHE D . n 
D 1 12  PRO 12  12  12  PRO PRO D . n 
D 1 13  ARG 13  13  13  ARG ARG D . n 
D 1 14  GLU 14  14  14  GLU GLU D . n 
D 1 15  SER 15  15  15  SER SER D . n 
D 1 16  VAL 16  16  16  VAL VAL D . n 
D 1 17  THR 17  17  17  THR THR D . n 
D 1 18  ASP 18  18  18  ASP ASP D . n 
D 1 19  HIS 19  19  19  HIS HIS D . n 
D 1 20  VAL 20  20  20  VAL VAL D . n 
D 1 21  ASN 21  21  21  ASN ASN D . n 
D 1 22  LEU 22  22  22  LEU LEU D . n 
D 1 23  ILE 23  23  23  ILE ILE D . n 
D 1 24  THR 24  24  24  THR THR D . n 
D 1 25  PRO 25  25  25  PRO PRO D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLU 27  27  27  GLU GLU D . n 
D 1 28  LYS 28  28  28  LYS LYS D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  LEU 30  30  30  LEU LEU D . n 
D 1 31  GLN 31  31  31  GLN GLN D . n 
D 1 32  ASN 32  32  32  ASN ASN D . n 
D 1 33  PHE 33  33  33  PHE PHE D . n 
D 1 34  THR 34  34  34  THR THR D . n 
D 1 35  LEU 35  35  35  LEU LEU D . n 
D 1 36  CYS 36  36  36  CYS CYS D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  ARG 38  38  38  ARG ARG D . n 
D 1 39  ALA 39  39  39  ALA ALA D . n 
D 1 40  TYR 40  40  40  TYR TYR D . n 
D 1 41  SER 41  41  41  SER SER D . n 
D 1 42  ASP 42  42  42  ASP ASP D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  SER 44  44  44  SER SER D . n 
D 1 45  ARG 45  45  45  ARG ARG D . n 
D 1 46  ALA 46  46  46  ALA ALA D . n 
D 1 47  TYR 47  47  47  TYR TYR D . n 
D 1 48  SER 48  48  48  SER SER D . n 
D 1 49  LEU 49  49  49  LEU LEU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  SER 51  51  51  SER SER D . n 
D 1 52  TYR 52  52  52  TYR TYR D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  GLN 55  55  55  GLN GLN D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  ARG 57  57  57  ARG ARG D . n 
D 1 58  ASP 58  58  58  ASP ASP D . n 
D 1 59  ASN 59  59  59  ASN ASN D . n 
D 1 60  GLU 60  60  60  GLU GLU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  LEU 62  62  62  LEU LEU D . n 
D 1 63  VAL 63  63  63  VAL VAL D . n 
D 1 64  TYR 64  64  64  TYR TYR D . n 
D 1 65  LYS 65  65  65  LYS LYS D . n 
D 1 66  GLU 66  66  66  GLU GLU D . n 
D 1 67  ARG 67  67  67  ARG ARG D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  GLY 69  69  69  GLY GLY D . n 
D 1 70  GLU 70  70  70  GLU GLU D . n 
D 1 71  TYR 71  71  71  TYR TYR D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  LEU 73  73  73  LEU LEU D . n 
D 1 74  TYR 74  74  74  TYR TYR D . n 
D 1 75  ILE 75  75  75  ILE ILE D . n 
D 1 76  GLY 76  76  76  GLY GLY D . n 
D 1 77  ARG 77  77  77  ARG ARG D . n 
D 1 78  HIS 78  78  78  HIS HIS D . n 
D 1 79  LYS 79  79  79  LYS LYS D . n 
D 1 80  VAL 80  80  80  VAL VAL D . n 
D 1 81  THR 81  81  81  THR THR D . n 
D 1 82  SER 82  82  82  SER SER D . n 
D 1 83  LYS 83  83  83  LYS LYS D . n 
D 1 84  VAL 84  84  84  VAL VAL D . n 
D 1 85  ILE 85  85  85  ILE ILE D . n 
D 1 86  GLU 86  86  86  GLU GLU D . n 
D 1 87  LYS 87  87  87  LYS LYS D . n 
D 1 88  PHE 88  88  88  PHE PHE D . n 
D 1 89  PRO 89  89  89  PRO PRO D . n 
D 1 90  ALA 90  90  90  ALA ALA D . n 
D 1 91  PRO 91  91  91  PRO PRO D . n 
D 1 92  VAL 92  92  92  VAL VAL D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  ILE 94  94  94  ILE ILE D . n 
D 1 95  CYS 95  95  95  CYS CYS D . n 
D 1 96  VAL 96  96  96  VAL VAL D . n 
D 1 97  SER 97  97  97  SER SER D . n 
D 1 98  TRP 98  98  98  TRP TRP D . n 
D 1 99  GLU 99  99  99  GLU GLU D . n 
D 1 100 SER 100 100 100 SER SER D . n 
D 1 101 SER 101 101 101 SER SER D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 GLY 103 103 103 GLY GLY D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 ALA 105 105 105 ALA ALA D . n 
D 1 106 GLU 106 106 106 GLU GLU D . n 
D 1 107 PHE 107 107 107 PHE PHE D . n 
D 1 108 TRP 108 108 108 TRP TRP D . n 
D 1 109 ILE 109 109 109 ILE ILE D . n 
D 1 110 ASN 110 110 110 ASN ASN D . n 
D 1 111 GLY 111 111 111 GLY GLY D . n 
D 1 112 THR 112 112 112 THR THR D . n 
D 1 113 PRO 113 113 113 PRO PRO D . n 
D 1 114 LEU 114 114 114 LEU LEU D . n 
D 1 115 VAL 115 115 115 VAL VAL D . n 
D 1 116 LYS 116 116 116 LYS LYS D . n 
D 1 117 LYS 117 117 117 LYS LYS D . n 
D 1 118 GLY 118 118 118 GLY GLY D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 ARG 120 120 120 ARG ARG D . n 
D 1 121 GLN 121 121 121 GLN GLN D . n 
D 1 122 GLY 122 122 122 GLY GLY D . n 
D 1 123 TYR 123 123 123 TYR TYR D . n 
D 1 124 PHE 124 124 124 PHE PHE D . n 
D 1 125 VAL 125 125 125 VAL VAL D . n 
D 1 126 GLU 126 126 126 GLU GLU D . n 
D 1 127 ALA 127 127 127 ALA ALA D . n 
D 1 128 GLN 128 128 128 GLN GLN D . n 
D 1 129 PRO 129 129 129 PRO PRO D . n 
D 1 130 LYS 130 130 130 LYS LYS D . n 
D 1 131 ILE 131 131 131 ILE ILE D . n 
D 1 132 VAL 132 132 132 VAL VAL D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 GLY 134 134 134 GLY GLY D . n 
D 1 135 GLN 135 135 135 GLN GLN D . n 
D 1 136 GLU 136 136 136 GLU GLU D . n 
D 1 137 GLN 137 137 137 GLN GLN D . n 
D 1 138 ASP 138 138 138 ASP ASP D . n 
D 1 139 SER 139 139 139 SER SER D . n 
D 1 140 TYR 140 140 140 TYR TYR D . n 
D 1 141 GLY 141 141 141 GLY GLY D . n 
D 1 142 GLY 142 142 142 GLY GLY D . n 
D 1 143 LYS 143 143 143 LYS LYS D . n 
D 1 144 PHE 144 144 144 PHE PHE D . n 
D 1 145 ASP 145 145 145 ASP ASP D . n 
D 1 146 ARG 146 146 146 ARG ARG D . n 
D 1 147 SER 147 147 147 SER SER D . n 
D 1 148 GLN 148 148 148 GLN GLN D . n 
D 1 149 SER 149 149 149 SER SER D . n 
D 1 150 PHE 150 150 150 PHE PHE D . n 
D 1 151 VAL 151 151 151 VAL VAL D . n 
D 1 152 GLY 152 152 152 GLY GLY D . n 
D 1 153 GLU 153 153 153 GLU GLU D . n 
D 1 154 ILE 154 154 154 ILE ILE D . n 
D 1 155 GLY 155 155 155 GLY GLY D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LEU 157 157 157 LEU LEU D . n 
D 1 158 TYR 158 158 158 TYR TYR D . n 
D 1 159 MET 159 159 159 MET MET D . n 
D 1 160 TRP 160 160 160 TRP TRP D . n 
D 1 161 ASP 161 161 161 ASP ASP D . n 
D 1 162 SER 162 162 162 SER SER D . n 
D 1 163 VAL 163 163 163 VAL VAL D . n 
D 1 164 LEU 164 164 164 LEU LEU D . n 
D 1 165 PRO 165 165 165 PRO PRO D . n 
D 1 166 PRO 166 166 166 PRO PRO D . n 
D 1 167 GLU 167 167 167 GLU GLU D . n 
D 1 168 ASN 168 168 168 ASN ASN D . n 
D 1 169 ILE 169 169 169 ILE ILE D . n 
D 1 170 LEU 170 170 170 LEU LEU D . n 
D 1 171 SER 171 171 171 SER SER D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 TYR 173 173 173 TYR TYR D . n 
D 1 174 GLN 174 174 174 GLN GLN D . n 
D 1 175 GLY 175 175 175 GLY GLY D . n 
D 1 176 THR 176 176 176 THR THR D . n 
D 1 177 PRO 177 177 177 PRO PRO D . n 
D 1 178 LEU 178 178 178 LEU LEU D . n 
D 1 179 PRO 179 179 179 PRO PRO D . n 
D 1 180 ALA 180 180 180 ALA ALA D . n 
D 1 181 ASN 181 181 181 ASN ASN D . n 
D 1 182 ILE 182 182 182 ILE ILE D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 ASP 184 184 184 ASP ASP D . n 
D 1 185 TRP 185 185 185 TRP TRP D . n 
D 1 186 GLN 186 186 186 GLN GLN D . n 
D 1 187 ALA 187 187 187 ALA ALA D . n 
D 1 188 LEU 188 188 188 LEU LEU D . n 
D 1 189 ASN 189 189 189 ASN ASN D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 GLU 191 191 191 GLU GLU D . n 
D 1 192 ILE 192 192 192 ILE ILE D . n 
D 1 193 ARG 193 193 193 ARG ARG D . n 
D 1 194 GLY 194 194 194 GLY GLY D . n 
D 1 195 TYR 195 195 195 TYR TYR D . n 
D 1 196 VAL 196 196 196 VAL VAL D . n 
D 1 197 ILE 197 197 197 ILE ILE D . n 
D 1 198 ILE 198 198 198 ILE ILE D . n 
D 1 199 LYS 199 199 199 LYS LYS D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 LEU 201 201 201 LEU LEU D . n 
D 1 202 VAL 202 202 202 VAL VAL D . n 
D 1 203 TRP 203 203 203 TRP TRP D . n 
D 1 204 VAL 204 204 204 VAL VAL D . n 
E 1 1   HIS 1   1   1   HIS HIS E . n 
E 1 2   THR 2   2   2   THR THR E . n 
E 1 3   ASP 3   3   3   ASP ASP E . n 
E 1 4   LEU 4   4   4   LEU LEU E . n 
E 1 5   SER 5   5   5   SER SER E . n 
E 1 6   GLY 6   6   6   GLY GLY E . n 
E 1 7   LYS 7   7   7   LYS LYS E . n 
E 1 8   VAL 8   8   8   VAL VAL E . n 
E 1 9   PHE 9   9   9   PHE PHE E . n 
E 1 10  VAL 10  10  10  VAL VAL E . n 
E 1 11  PHE 11  11  11  PHE PHE E . n 
E 1 12  PRO 12  12  12  PRO PRO E . n 
E 1 13  ARG 13  13  13  ARG ARG E . n 
E 1 14  GLU 14  14  14  GLU GLU E . n 
E 1 15  SER 15  15  15  SER SER E . n 
E 1 16  VAL 16  16  16  VAL VAL E . n 
E 1 17  THR 17  17  17  THR THR E . n 
E 1 18  ASP 18  18  18  ASP ASP E . n 
E 1 19  HIS 19  19  19  HIS HIS E . n 
E 1 20  VAL 20  20  20  VAL VAL E . n 
E 1 21  ASN 21  21  21  ASN ASN E . n 
E 1 22  LEU 22  22  22  LEU LEU E . n 
E 1 23  ILE 23  23  23  ILE ILE E . n 
E 1 24  THR 24  24  24  THR THR E . n 
E 1 25  PRO 25  25  25  PRO PRO E . n 
E 1 26  LEU 26  26  26  LEU LEU E . n 
E 1 27  GLU 27  27  27  GLU GLU E . n 
E 1 28  LYS 28  28  28  LYS LYS E . n 
E 1 29  PRO 29  29  29  PRO PRO E . n 
E 1 30  LEU 30  30  30  LEU LEU E . n 
E 1 31  GLN 31  31  31  GLN GLN E . n 
E 1 32  ASN 32  32  32  ASN ASN E . n 
E 1 33  PHE 33  33  33  PHE PHE E . n 
E 1 34  THR 34  34  34  THR THR E . n 
E 1 35  LEU 35  35  35  LEU LEU E . n 
E 1 36  CYS 36  36  36  CYS CYS E . n 
E 1 37  PHE 37  37  37  PHE PHE E . n 
E 1 38  ARG 38  38  38  ARG ARG E . n 
E 1 39  ALA 39  39  39  ALA ALA E . n 
E 1 40  TYR 40  40  40  TYR TYR E . n 
E 1 41  SER 41  41  41  SER SER E . n 
E 1 42  ASP 42  42  42  ASP ASP E . n 
E 1 43  LEU 43  43  43  LEU LEU E . n 
E 1 44  SER 44  44  44  SER SER E . n 
E 1 45  ARG 45  45  45  ARG ARG E . n 
E 1 46  ALA 46  46  46  ALA ALA E . n 
E 1 47  TYR 47  47  47  TYR TYR E . n 
E 1 48  SER 48  48  48  SER SER E . n 
E 1 49  LEU 49  49  49  LEU LEU E . n 
E 1 50  PHE 50  50  50  PHE PHE E . n 
E 1 51  SER 51  51  51  SER SER E . n 
E 1 52  TYR 52  52  52  TYR TYR E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  THR 54  54  54  THR THR E . n 
E 1 55  GLN 55  55  55  GLN GLN E . n 
E 1 56  GLY 56  56  56  GLY GLY E . n 
E 1 57  ARG 57  57  57  ARG ARG E . n 
E 1 58  ASP 58  58  58  ASP ASP E . n 
E 1 59  ASN 59  59  59  ASN ASN E . n 
E 1 60  GLU 60  60  60  GLU GLU E . n 
E 1 61  LEU 61  61  61  LEU LEU E . n 
E 1 62  LEU 62  62  62  LEU LEU E . n 
E 1 63  VAL 63  63  63  VAL VAL E . n 
E 1 64  TYR 64  64  64  TYR TYR E . n 
E 1 65  LYS 65  65  65  LYS LYS E . n 
E 1 66  GLU 66  66  66  GLU GLU E . n 
E 1 67  ARG 67  67  67  ARG ARG E . n 
E 1 68  VAL 68  68  68  VAL VAL E . n 
E 1 69  GLY 69  69  69  GLY GLY E . n 
E 1 70  GLU 70  70  70  GLU GLU E . n 
E 1 71  TYR 71  71  71  TYR TYR E . n 
E 1 72  SER 72  72  72  SER SER E . n 
E 1 73  LEU 73  73  73  LEU LEU E . n 
E 1 74  TYR 74  74  74  TYR TYR E . n 
E 1 75  ILE 75  75  75  ILE ILE E . n 
E 1 76  GLY 76  76  76  GLY GLY E . n 
E 1 77  ARG 77  77  77  ARG ARG E . n 
E 1 78  HIS 78  78  78  HIS HIS E . n 
E 1 79  LYS 79  79  79  LYS LYS E . n 
E 1 80  VAL 80  80  80  VAL VAL E . n 
E 1 81  THR 81  81  81  THR THR E . n 
E 1 82  SER 82  82  82  SER SER E . n 
E 1 83  LYS 83  83  83  LYS LYS E . n 
E 1 84  VAL 84  84  84  VAL VAL E . n 
E 1 85  ILE 85  85  85  ILE ILE E . n 
E 1 86  GLU 86  86  86  GLU GLU E . n 
E 1 87  LYS 87  87  87  LYS LYS E . n 
E 1 88  PHE 88  88  88  PHE PHE E . n 
E 1 89  PRO 89  89  89  PRO PRO E . n 
E 1 90  ALA 90  90  90  ALA ALA E . n 
E 1 91  PRO 91  91  91  PRO PRO E . n 
E 1 92  VAL 92  92  92  VAL VAL E . n 
E 1 93  HIS 93  93  93  HIS HIS E . n 
E 1 94  ILE 94  94  94  ILE ILE E . n 
E 1 95  CYS 95  95  95  CYS CYS E . n 
E 1 96  VAL 96  96  96  VAL VAL E . n 
E 1 97  SER 97  97  97  SER SER E . n 
E 1 98  TRP 98  98  98  TRP TRP E . n 
E 1 99  GLU 99  99  99  GLU GLU E . n 
E 1 100 SER 100 100 100 SER SER E . n 
E 1 101 SER 101 101 101 SER SER E . n 
E 1 102 SER 102 102 102 SER SER E . n 
E 1 103 GLY 103 103 103 GLY GLY E . n 
E 1 104 ILE 104 104 104 ILE ILE E . n 
E 1 105 ALA 105 105 105 ALA ALA E . n 
E 1 106 GLU 106 106 106 GLU GLU E . n 
E 1 107 PHE 107 107 107 PHE PHE E . n 
E 1 108 TRP 108 108 108 TRP TRP E . n 
E 1 109 ILE 109 109 109 ILE ILE E . n 
E 1 110 ASN 110 110 110 ASN ASN E . n 
E 1 111 GLY 111 111 111 GLY GLY E . n 
E 1 112 THR 112 112 112 THR THR E . n 
E 1 113 PRO 113 113 113 PRO PRO E . n 
E 1 114 LEU 114 114 114 LEU LEU E . n 
E 1 115 VAL 115 115 115 VAL VAL E . n 
E 1 116 LYS 116 116 116 LYS LYS E . n 
E 1 117 LYS 117 117 117 LYS LYS E . n 
E 1 118 GLY 118 118 118 GLY GLY E . n 
E 1 119 LEU 119 119 119 LEU LEU E . n 
E 1 120 ARG 120 120 120 ARG ARG E . n 
E 1 121 GLN 121 121 121 GLN GLN E . n 
E 1 122 GLY 122 122 122 GLY GLY E . n 
E 1 123 TYR 123 123 123 TYR TYR E . n 
E 1 124 PHE 124 124 124 PHE PHE E . n 
E 1 125 VAL 125 125 125 VAL VAL E . n 
E 1 126 GLU 126 126 126 GLU GLU E . n 
E 1 127 ALA 127 127 127 ALA ALA E . n 
E 1 128 GLN 128 128 128 GLN GLN E . n 
E 1 129 PRO 129 129 129 PRO PRO E . n 
E 1 130 LYS 130 130 130 LYS LYS E . n 
E 1 131 ILE 131 131 131 ILE ILE E . n 
E 1 132 VAL 132 132 132 VAL VAL E . n 
E 1 133 LEU 133 133 133 LEU LEU E . n 
E 1 134 GLY 134 134 134 GLY GLY E . n 
E 1 135 GLN 135 135 135 GLN GLN E . n 
E 1 136 GLU 136 136 136 GLU GLU E . n 
E 1 137 GLN 137 137 137 GLN GLN E . n 
E 1 138 ASP 138 138 138 ASP ASP E . n 
E 1 139 SER 139 139 139 SER SER E . n 
E 1 140 TYR 140 140 140 TYR TYR E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 GLY 142 142 142 GLY GLY E . n 
E 1 143 LYS 143 143 143 LYS LYS E . n 
E 1 144 PHE 144 144 144 PHE PHE E . n 
E 1 145 ASP 145 145 145 ASP ASP E . n 
E 1 146 ARG 146 146 146 ARG ARG E . n 
E 1 147 SER 147 147 147 SER SER E . n 
E 1 148 GLN 148 148 148 GLN GLN E . n 
E 1 149 SER 149 149 149 SER SER E . n 
E 1 150 PHE 150 150 150 PHE PHE E . n 
E 1 151 VAL 151 151 151 VAL VAL E . n 
E 1 152 GLY 152 152 152 GLY GLY E . n 
E 1 153 GLU 153 153 153 GLU GLU E . n 
E 1 154 ILE 154 154 154 ILE ILE E . n 
E 1 155 GLY 155 155 155 GLY GLY E . n 
E 1 156 ASP 156 156 156 ASP ASP E . n 
E 1 157 LEU 157 157 157 LEU LEU E . n 
E 1 158 TYR 158 158 158 TYR TYR E . n 
E 1 159 MET 159 159 159 MET MET E . n 
E 1 160 TRP 160 160 160 TRP TRP E . n 
E 1 161 ASP 161 161 161 ASP ASP E . n 
E 1 162 SER 162 162 162 SER SER E . n 
E 1 163 VAL 163 163 163 VAL VAL E . n 
E 1 164 LEU 164 164 164 LEU LEU E . n 
E 1 165 PRO 165 165 165 PRO PRO E . n 
E 1 166 PRO 166 166 166 PRO PRO E . n 
E 1 167 GLU 167 167 167 GLU GLU E . n 
E 1 168 ASN 168 168 168 ASN ASN E . n 
E 1 169 ILE 169 169 169 ILE ILE E . n 
E 1 170 LEU 170 170 170 LEU LEU E . n 
E 1 171 SER 171 171 171 SER SER E . n 
E 1 172 ALA 172 172 172 ALA ALA E . n 
E 1 173 TYR 173 173 173 TYR TYR E . n 
E 1 174 GLN 174 174 174 GLN GLN E . n 
E 1 175 GLY 175 175 175 GLY GLY E . n 
E 1 176 THR 176 176 176 THR THR E . n 
E 1 177 PRO 177 177 177 PRO PRO E . n 
E 1 178 LEU 178 178 178 LEU LEU E . n 
E 1 179 PRO 179 179 179 PRO PRO E . n 
E 1 180 ALA 180 180 180 ALA ALA E . n 
E 1 181 ASN 181 181 181 ASN ASN E . n 
E 1 182 ILE 182 182 182 ILE ILE E . n 
E 1 183 LEU 183 183 183 LEU LEU E . n 
E 1 184 ASP 184 184 184 ASP ASP E . n 
E 1 185 TRP 185 185 185 TRP TRP E . n 
E 1 186 GLN 186 186 186 GLN GLN E . n 
E 1 187 ALA 187 187 187 ALA ALA E . n 
E 1 188 LEU 188 188 188 LEU LEU E . n 
E 1 189 ASN 189 189 189 ASN ASN E . n 
E 1 190 TYR 190 190 190 TYR TYR E . n 
E 1 191 GLU 191 191 191 GLU GLU E . n 
E 1 192 ILE 192 192 192 ILE ILE E . n 
E 1 193 ARG 193 193 193 ARG ARG E . n 
E 1 194 GLY 194 194 194 GLY GLY E . n 
E 1 195 TYR 195 195 195 TYR TYR E . n 
E 1 196 VAL 196 196 196 VAL VAL E . n 
E 1 197 ILE 197 197 197 ILE ILE E . n 
E 1 198 ILE 198 198 198 ILE ILE E . n 
E 1 199 LYS 199 199 199 LYS LYS E . n 
E 1 200 PRO 200 200 200 PRO PRO E . n 
E 1 201 LEU 201 201 201 LEU LEU E . n 
E 1 202 VAL 202 202 202 VAL VAL E . n 
E 1 203 TRP 203 203 203 TRP TRP E . n 
E 1 204 VAL 204 204 204 VAL VAL E . 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 
F  2 CA  1   205  205  CA  CA  A . 
G  2 CA  1   206  206  CA  CA  A . 
H  3 NAG 1   207  207  NAG NAG A . 
I  4 TPO 1   500  500  TPO TPO A . 
J  2 CA  1   205  205  CA  CA  B . 
K  2 CA  1   206  206  CA  CA  B . 
L  3 NAG 1   207  207  NAG NAG B . 
M  4 TPO 1   500  500  TPO TPO B . 
N  2 CA  1   205  205  CA  CA  C . 
O  2 CA  1   206  206  CA  CA  C . 
P  3 NAG 1   207  207  NAG NAG C . 
Q  4 TPO 1   500  500  TPO TPO C . 
R  2 CA  1   205  205  CA  CA  D . 
S  2 CA  1   206  206  CA  CA  D . 
T  3 NAG 1   207  207  NAG NAG D . 
U  4 TPO 1   500  500  TPO TPO D . 
V  2 CA  1   205  205  CA  CA  E . 
W  2 CA  1   206  206  CA  CA  E . 
X  3 NAG 1   207  207  NAG NAG E . 
Y  4 TPO 1   500  500  TPO TPO E . 
Z  5 HOH 1   2001 2001 HOH HOH A . 
Z  5 HOH 2   2002 2002 HOH HOH A . 
Z  5 HOH 3   2003 2003 HOH HOH A . 
Z  5 HOH 4   2004 2004 HOH HOH A . 
Z  5 HOH 5   2005 2005 HOH HOH A . 
Z  5 HOH 6   2006 2006 HOH HOH A . 
Z  5 HOH 7   2007 2007 HOH HOH A . 
Z  5 HOH 8   2008 2008 HOH HOH A . 
Z  5 HOH 9   2009 2009 HOH HOH A . 
Z  5 HOH 10  2010 2010 HOH HOH A . 
Z  5 HOH 11  2011 2011 HOH HOH A . 
Z  5 HOH 12  2012 2012 HOH HOH A . 
Z  5 HOH 13  2013 2013 HOH HOH A . 
Z  5 HOH 14  2014 2014 HOH HOH A . 
Z  5 HOH 15  2015 2015 HOH HOH A . 
Z  5 HOH 16  2016 2016 HOH HOH A . 
Z  5 HOH 17  2017 2017 HOH HOH A . 
Z  5 HOH 18  2018 2018 HOH HOH A . 
Z  5 HOH 19  2019 2019 HOH HOH A . 
Z  5 HOH 20  2020 2020 HOH HOH A . 
Z  5 HOH 21  2021 2021 HOH HOH A . 
Z  5 HOH 22  2022 2022 HOH HOH A . 
Z  5 HOH 23  2023 2023 HOH HOH A . 
Z  5 HOH 24  2024 2024 HOH HOH A . 
Z  5 HOH 25  2025 2025 HOH HOH A . 
Z  5 HOH 26  2026 2026 HOH HOH A . 
Z  5 HOH 27  2027 2027 HOH HOH A . 
Z  5 HOH 28  2028 2028 HOH HOH A . 
Z  5 HOH 29  2029 2029 HOH HOH A . 
Z  5 HOH 30  2030 2030 HOH HOH A . 
Z  5 HOH 31  2031 2031 HOH HOH A . 
Z  5 HOH 32  2032 2032 HOH HOH A . 
Z  5 HOH 33  2033 2033 HOH HOH A . 
Z  5 HOH 34  2034 2034 HOH HOH A . 
Z  5 HOH 35  2035 2035 HOH HOH A . 
Z  5 HOH 36  2036 2036 HOH HOH A . 
Z  5 HOH 37  2037 2037 HOH HOH A . 
Z  5 HOH 38  2038 2038 HOH HOH A . 
Z  5 HOH 39  2039 2039 HOH HOH A . 
Z  5 HOH 40  2040 2040 HOH HOH A . 
Z  5 HOH 41  2041 2041 HOH HOH A . 
Z  5 HOH 42  2042 2042 HOH HOH A . 
Z  5 HOH 43  2043 2043 HOH HOH A . 
Z  5 HOH 44  2044 2044 HOH HOH A . 
Z  5 HOH 45  2045 2045 HOH HOH A . 
Z  5 HOH 46  2046 2046 HOH HOH A . 
Z  5 HOH 47  2047 2047 HOH HOH A . 
Z  5 HOH 48  2048 2048 HOH HOH A . 
Z  5 HOH 49  2049 2049 HOH HOH A . 
Z  5 HOH 50  2050 2050 HOH HOH A . 
Z  5 HOH 51  2051 2051 HOH HOH A . 
Z  5 HOH 52  2052 2052 HOH HOH A . 
Z  5 HOH 53  2053 2053 HOH HOH A . 
Z  5 HOH 54  2054 2054 HOH HOH A . 
Z  5 HOH 55  2055 2055 HOH HOH A . 
Z  5 HOH 56  2056 2056 HOH HOH A . 
Z  5 HOH 57  2057 2057 HOH HOH A . 
Z  5 HOH 58  2058 2058 HOH HOH A . 
Z  5 HOH 59  2059 2059 HOH HOH A . 
Z  5 HOH 60  2060 2060 HOH HOH A . 
Z  5 HOH 61  2061 2061 HOH HOH A . 
Z  5 HOH 62  2062 2062 HOH HOH A . 
Z  5 HOH 63  2063 2063 HOH HOH A . 
Z  5 HOH 64  2064 2064 HOH HOH A . 
Z  5 HOH 65  2065 2065 HOH HOH A . 
Z  5 HOH 66  2066 2066 HOH HOH A . 
Z  5 HOH 67  2067 2067 HOH HOH A . 
Z  5 HOH 68  2068 2068 HOH HOH A . 
Z  5 HOH 69  2069 2069 HOH HOH A . 
Z  5 HOH 70  2070 2070 HOH HOH A . 
Z  5 HOH 71  2071 2071 HOH HOH A . 
Z  5 HOH 72  2072 2072 HOH HOH A . 
Z  5 HOH 73  2073 2073 HOH HOH A . 
Z  5 HOH 74  2074 2074 HOH HOH A . 
Z  5 HOH 75  2075 2075 HOH HOH A . 
Z  5 HOH 76  2076 2076 HOH HOH A . 
Z  5 HOH 77  2077 2077 HOH HOH A . 
Z  5 HOH 78  2078 2078 HOH HOH A . 
Z  5 HOH 79  2079 2079 HOH HOH A . 
Z  5 HOH 80  2080 2080 HOH HOH A . 
Z  5 HOH 81  2081 2081 HOH HOH A . 
Z  5 HOH 82  2082 2082 HOH HOH A . 
Z  5 HOH 83  2083 2083 HOH HOH A . 
Z  5 HOH 84  2084 2084 HOH HOH A . 
Z  5 HOH 85  2085 2085 HOH HOH A . 
Z  5 HOH 86  2086 2086 HOH HOH A . 
Z  5 HOH 87  2087 2087 HOH HOH A . 
Z  5 HOH 88  2088 2088 HOH HOH A . 
Z  5 HOH 89  2089 2089 HOH HOH A . 
Z  5 HOH 90  2090 2090 HOH HOH A . 
Z  5 HOH 91  2091 2091 HOH HOH A . 
Z  5 HOH 92  2092 2092 HOH HOH A . 
Z  5 HOH 93  2093 2093 HOH HOH A . 
Z  5 HOH 94  2094 2094 HOH HOH A . 
Z  5 HOH 95  2095 2095 HOH HOH A . 
Z  5 HOH 96  2096 2096 HOH HOH A . 
Z  5 HOH 97  2097 2097 HOH HOH A . 
Z  5 HOH 98  2098 2098 HOH HOH A . 
Z  5 HOH 99  2099 2099 HOH HOH A . 
Z  5 HOH 100 2100 2100 HOH HOH A . 
Z  5 HOH 101 2101 2101 HOH HOH A . 
Z  5 HOH 102 2102 2102 HOH HOH A . 
Z  5 HOH 103 2103 2103 HOH HOH A . 
Z  5 HOH 104 2104 2104 HOH HOH A . 
Z  5 HOH 105 2105 2105 HOH HOH A . 
Z  5 HOH 106 2106 2106 HOH HOH A . 
Z  5 HOH 107 2107 2107 HOH HOH A . 
Z  5 HOH 108 2108 2108 HOH HOH A . 
Z  5 HOH 109 2109 2109 HOH HOH A . 
Z  5 HOH 110 2110 2110 HOH HOH A . 
Z  5 HOH 111 2111 2111 HOH HOH A . 
Z  5 HOH 112 2112 2112 HOH HOH A . 
Z  5 HOH 113 2113 2113 HOH HOH A . 
Z  5 HOH 114 2114 2114 HOH HOH A . 
Z  5 HOH 115 2115 2115 HOH HOH A . 
Z  5 HOH 116 2116 2116 HOH HOH A . 
Z  5 HOH 117 2117 2117 HOH HOH A . 
Z  5 HOH 118 2118 2118 HOH HOH A . 
Z  5 HOH 119 2119 2119 HOH HOH A . 
Z  5 HOH 120 2120 2120 HOH HOH A . 
Z  5 HOH 121 2121 2121 HOH HOH A . 
Z  5 HOH 122 2122 2122 HOH HOH A . 
Z  5 HOH 123 2123 2123 HOH HOH A . 
Z  5 HOH 124 2124 2124 HOH HOH A . 
Z  5 HOH 125 2125 2125 HOH HOH A . 
Z  5 HOH 126 2126 2126 HOH HOH A . 
Z  5 HOH 127 2127 2127 HOH HOH A . 
Z  5 HOH 128 2128 2128 HOH HOH A . 
Z  5 HOH 129 2129 2129 HOH HOH A . 
Z  5 HOH 130 2130 2130 HOH HOH A . 
Z  5 HOH 131 2131 2131 HOH HOH A . 
Z  5 HOH 132 2132 2132 HOH HOH A . 
Z  5 HOH 133 2133 2133 HOH HOH A . 
Z  5 HOH 134 2134 2134 HOH HOH A . 
Z  5 HOH 135 2135 2135 HOH HOH A . 
Z  5 HOH 136 2136 2136 HOH HOH A . 
Z  5 HOH 137 2137 2137 HOH HOH A . 
Z  5 HOH 138 2138 2138 HOH HOH A . 
Z  5 HOH 139 2139 2139 HOH HOH A . 
Z  5 HOH 140 2140 2140 HOH HOH A . 
Z  5 HOH 141 2141 2141 HOH HOH A . 
Z  5 HOH 142 2142 2142 HOH HOH A . 
Z  5 HOH 143 2143 2143 HOH HOH A . 
Z  5 HOH 144 2144 2144 HOH HOH A . 
Z  5 HOH 145 2145 2145 HOH HOH A . 
Z  5 HOH 146 2146 2146 HOH HOH A . 
Z  5 HOH 147 2147 2147 HOH HOH A . 
Z  5 HOH 148 2148 2148 HOH HOH A . 
Z  5 HOH 149 2149 2149 HOH HOH A . 
Z  5 HOH 150 2150 2150 HOH HOH A . 
Z  5 HOH 151 2151 2151 HOH HOH A . 
Z  5 HOH 152 2152 2152 HOH HOH A . 
Z  5 HOH 153 2153 2153 HOH HOH A . 
Z  5 HOH 154 2154 2154 HOH HOH A . 
Z  5 HOH 155 2155 2155 HOH HOH A . 
Z  5 HOH 156 2156 2156 HOH HOH A . 
Z  5 HOH 157 2157 2157 HOH HOH A . 
Z  5 HOH 158 2158 2158 HOH HOH A . 
Z  5 HOH 159 2159 2159 HOH HOH A . 
Z  5 HOH 160 2160 2160 HOH HOH A . 
Z  5 HOH 161 2161 2161 HOH HOH A . 
Z  5 HOH 162 2162 2162 HOH HOH A . 
Z  5 HOH 163 2163 2163 HOH HOH A . 
Z  5 HOH 164 2164 2164 HOH HOH A . 
Z  5 HOH 165 2165 2165 HOH HOH A . 
Z  5 HOH 166 2166 2166 HOH HOH A . 
Z  5 HOH 167 2167 2167 HOH HOH A . 
Z  5 HOH 168 2168 2168 HOH HOH A . 
Z  5 HOH 169 2169 2169 HOH HOH A . 
Z  5 HOH 170 2170 2170 HOH HOH A . 
Z  5 HOH 171 2171 2171 HOH HOH A . 
Z  5 HOH 172 2172 2172 HOH HOH A . 
Z  5 HOH 173 2173 2173 HOH HOH A . 
Z  5 HOH 174 2174 2174 HOH HOH A . 
Z  5 HOH 175 2175 2175 HOH HOH A . 
Z  5 HOH 176 2176 2176 HOH HOH A . 
Z  5 HOH 177 2177 2177 HOH HOH A . 
Z  5 HOH 178 2178 2178 HOH HOH A . 
Z  5 HOH 179 2179 2179 HOH HOH A . 
Z  5 HOH 180 2180 2180 HOH HOH A . 
Z  5 HOH 181 2181 2181 HOH HOH A . 
Z  5 HOH 182 2182 2182 HOH HOH A . 
Z  5 HOH 183 2183 2183 HOH HOH A . 
Z  5 HOH 184 2184 2184 HOH HOH A . 
Z  5 HOH 185 2185 2185 HOH HOH A . 
Z  5 HOH 186 2186 2186 HOH HOH A . 
Z  5 HOH 187 2187 2187 HOH HOH A . 
Z  5 HOH 188 2188 2188 HOH HOH A . 
Z  5 HOH 189 2189 2189 HOH HOH A . 
Z  5 HOH 190 2190 2190 HOH HOH A . 
Z  5 HOH 191 2191 2191 HOH HOH A . 
Z  5 HOH 192 2192 2192 HOH HOH A . 
Z  5 HOH 193 2193 2193 HOH HOH A . 
Z  5 HOH 194 2194 2194 HOH HOH A . 
Z  5 HOH 195 2195 2195 HOH HOH A . 
Z  5 HOH 196 2196 2196 HOH HOH A . 
Z  5 HOH 197 2197 2197 HOH HOH A . 
Z  5 HOH 198 2198 2198 HOH HOH A . 
Z  5 HOH 199 2199 2199 HOH HOH A . 
Z  5 HOH 200 2200 2200 HOH HOH A . 
Z  5 HOH 201 2201 2201 HOH HOH A . 
Z  5 HOH 202 2202 2202 HOH HOH A . 
Z  5 HOH 203 2203 2203 HOH HOH A . 
Z  5 HOH 204 2204 2204 HOH HOH A . 
Z  5 HOH 205 2205 2205 HOH HOH A . 
Z  5 HOH 206 2206 2206 HOH HOH A . 
Z  5 HOH 207 2207 2207 HOH HOH A . 
Z  5 HOH 208 2208 2208 HOH HOH A . 
Z  5 HOH 209 2209 2209 HOH HOH A . 
Z  5 HOH 210 2210 2210 HOH HOH A . 
Z  5 HOH 211 2211 2211 HOH HOH A . 
Z  5 HOH 212 2212 2212 HOH HOH A . 
Z  5 HOH 213 2213 2213 HOH HOH A . 
Z  5 HOH 214 2214 2214 HOH HOH A . 
Z  5 HOH 215 2215 2215 HOH HOH A . 
Z  5 HOH 216 2216 2216 HOH HOH A . 
Z  5 HOH 217 2217 2217 HOH HOH A . 
Z  5 HOH 218 2218 2218 HOH HOH A . 
Z  5 HOH 219 2219 2219 HOH HOH A . 
Z  5 HOH 220 2220 2220 HOH HOH A . 
Z  5 HOH 221 2221 2221 HOH HOH A . 
Z  5 HOH 222 2222 2222 HOH HOH A . 
Z  5 HOH 223 2223 2223 HOH HOH A . 
Z  5 HOH 224 2224 2224 HOH HOH A . 
Z  5 HOH 225 2225 2225 HOH HOH A . 
Z  5 HOH 226 2226 2226 HOH HOH A . 
Z  5 HOH 227 2227 2227 HOH HOH A . 
Z  5 HOH 228 2228 2228 HOH HOH A . 
Z  5 HOH 229 2229 2229 HOH HOH A . 
Z  5 HOH 230 2230 2230 HOH HOH A . 
Z  5 HOH 231 2231 2231 HOH HOH A . 
Z  5 HOH 232 2232 2232 HOH HOH A . 
Z  5 HOH 233 2233 2233 HOH HOH A . 
Z  5 HOH 234 2234 2234 HOH HOH A . 
Z  5 HOH 235 2235 2235 HOH HOH A . 
Z  5 HOH 236 2236 2236 HOH HOH A . 
Z  5 HOH 237 2237 2237 HOH HOH A . 
Z  5 HOH 238 2238 2238 HOH HOH A . 
Z  5 HOH 239 2239 2239 HOH HOH A . 
Z  5 HOH 240 2240 2240 HOH HOH A . 
Z  5 HOH 241 2241 2241 HOH HOH A . 
Z  5 HOH 242 2242 2242 HOH HOH A . 
Z  5 HOH 243 2243 2243 HOH HOH A . 
Z  5 HOH 244 2244 2244 HOH HOH A . 
Z  5 HOH 245 2245 2245 HOH HOH A . 
Z  5 HOH 246 2246 2246 HOH HOH A . 
Z  5 HOH 247 2247 2247 HOH HOH A . 
Z  5 HOH 248 2248 2248 HOH HOH A . 
Z  5 HOH 249 2249 2249 HOH HOH A . 
Z  5 HOH 250 2250 2250 HOH HOH A . 
Z  5 HOH 251 2251 2251 HOH HOH A . 
Z  5 HOH 252 2252 2252 HOH HOH A . 
Z  5 HOH 253 2253 2253 HOH HOH A . 
Z  5 HOH 254 2254 2254 HOH HOH A . 
Z  5 HOH 255 2255 2255 HOH HOH A . 
Z  5 HOH 256 2256 2256 HOH HOH A . 
Z  5 HOH 257 2257 2257 HOH HOH A . 
Z  5 HOH 258 2258 2258 HOH HOH A . 
Z  5 HOH 259 2259 2259 HOH HOH A . 
Z  5 HOH 260 2260 2260 HOH HOH A . 
Z  5 HOH 261 2261 2261 HOH HOH A . 
AA 5 HOH 1   2001 2001 HOH HOH B . 
AA 5 HOH 2   2002 2002 HOH HOH B . 
AA 5 HOH 3   2003 2003 HOH HOH B . 
AA 5 HOH 4   2004 2004 HOH HOH B . 
AA 5 HOH 5   2005 2005 HOH HOH B . 
AA 5 HOH 6   2006 2006 HOH HOH B . 
AA 5 HOH 7   2007 2007 HOH HOH B . 
AA 5 HOH 8   2008 2008 HOH HOH B . 
AA 5 HOH 9   2009 2009 HOH HOH B . 
AA 5 HOH 10  2010 2010 HOH HOH B . 
AA 5 HOH 11  2011 2011 HOH HOH B . 
AA 5 HOH 12  2012 2012 HOH HOH B . 
AA 5 HOH 13  2013 2013 HOH HOH B . 
AA 5 HOH 14  2014 2014 HOH HOH B . 
AA 5 HOH 15  2015 2015 HOH HOH B . 
AA 5 HOH 16  2016 2016 HOH HOH B . 
AA 5 HOH 17  2017 2017 HOH HOH B . 
AA 5 HOH 18  2018 2018 HOH HOH B . 
AA 5 HOH 19  2019 2019 HOH HOH B . 
AA 5 HOH 20  2020 2020 HOH HOH B . 
AA 5 HOH 21  2021 2021 HOH HOH B . 
AA 5 HOH 22  2022 2022 HOH HOH B . 
AA 5 HOH 23  2023 2023 HOH HOH B . 
AA 5 HOH 24  2024 2024 HOH HOH B . 
AA 5 HOH 25  2025 2025 HOH HOH B . 
AA 5 HOH 26  2026 2026 HOH HOH B . 
AA 5 HOH 27  2027 2027 HOH HOH B . 
AA 5 HOH 28  2028 2028 HOH HOH B . 
AA 5 HOH 29  2029 2029 HOH HOH B . 
AA 5 HOH 30  2030 2030 HOH HOH B . 
AA 5 HOH 31  2031 2031 HOH HOH B . 
AA 5 HOH 32  2032 2032 HOH HOH B . 
AA 5 HOH 33  2033 2033 HOH HOH B . 
AA 5 HOH 34  2034 2034 HOH HOH B . 
AA 5 HOH 35  2035 2035 HOH HOH B . 
AA 5 HOH 36  2036 2036 HOH HOH B . 
AA 5 HOH 37  2037 2037 HOH HOH B . 
AA 5 HOH 38  2038 2038 HOH HOH B . 
AA 5 HOH 39  2039 2039 HOH HOH B . 
AA 5 HOH 40  2040 2040 HOH HOH B . 
AA 5 HOH 41  2041 2041 HOH HOH B . 
AA 5 HOH 42  2042 2042 HOH HOH B . 
AA 5 HOH 43  2043 2043 HOH HOH B . 
AA 5 HOH 44  2044 2044 HOH HOH B . 
AA 5 HOH 45  2045 2045 HOH HOH B . 
AA 5 HOH 46  2046 2046 HOH HOH B . 
AA 5 HOH 47  2047 2047 HOH HOH B . 
AA 5 HOH 48  2048 2048 HOH HOH B . 
AA 5 HOH 49  2049 2049 HOH HOH B . 
AA 5 HOH 50  2050 2050 HOH HOH B . 
AA 5 HOH 51  2051 2051 HOH HOH B . 
AA 5 HOH 52  2052 2052 HOH HOH B . 
AA 5 HOH 53  2053 2053 HOH HOH B . 
AA 5 HOH 54  2054 2054 HOH HOH B . 
AA 5 HOH 55  2055 2055 HOH HOH B . 
AA 5 HOH 56  2056 2056 HOH HOH B . 
AA 5 HOH 57  2057 2057 HOH HOH B . 
AA 5 HOH 58  2058 2058 HOH HOH B . 
AA 5 HOH 59  2059 2059 HOH HOH B . 
AA 5 HOH 60  2060 2060 HOH HOH B . 
AA 5 HOH 61  2061 2061 HOH HOH B . 
AA 5 HOH 62  2062 2062 HOH HOH B . 
AA 5 HOH 63  2063 2063 HOH HOH B . 
AA 5 HOH 64  2064 2064 HOH HOH B . 
AA 5 HOH 65  2065 2065 HOH HOH B . 
AA 5 HOH 66  2066 2066 HOH HOH B . 
AA 5 HOH 67  2067 2067 HOH HOH B . 
AA 5 HOH 68  2068 2068 HOH HOH B . 
AA 5 HOH 69  2069 2069 HOH HOH B . 
AA 5 HOH 70  2070 2070 HOH HOH B . 
AA 5 HOH 71  2071 2071 HOH HOH B . 
AA 5 HOH 72  2072 2072 HOH HOH B . 
AA 5 HOH 73  2073 2073 HOH HOH B . 
AA 5 HOH 74  2074 2074 HOH HOH B . 
AA 5 HOH 75  2075 2075 HOH HOH B . 
AA 5 HOH 76  2076 2076 HOH HOH B . 
AA 5 HOH 77  2077 2077 HOH HOH B . 
AA 5 HOH 78  2078 2078 HOH HOH B . 
AA 5 HOH 79  2079 2079 HOH HOH B . 
AA 5 HOH 80  2080 2080 HOH HOH B . 
AA 5 HOH 81  2081 2081 HOH HOH B . 
AA 5 HOH 82  2082 2082 HOH HOH B . 
AA 5 HOH 83  2083 2083 HOH HOH B . 
AA 5 HOH 84  2084 2084 HOH HOH B . 
AA 5 HOH 85  2085 2085 HOH HOH B . 
AA 5 HOH 86  2086 2086 HOH HOH B . 
AA 5 HOH 87  2087 2087 HOH HOH B . 
AA 5 HOH 88  2088 2088 HOH HOH B . 
AA 5 HOH 89  2089 2089 HOH HOH B . 
AA 5 HOH 90  2090 2090 HOH HOH B . 
AA 5 HOH 91  2091 2091 HOH HOH B . 
AA 5 HOH 92  2092 2092 HOH HOH B . 
AA 5 HOH 93  2093 2093 HOH HOH B . 
AA 5 HOH 94  2094 2094 HOH HOH B . 
AA 5 HOH 95  2095 2095 HOH HOH B . 
AA 5 HOH 96  2096 2096 HOH HOH B . 
AA 5 HOH 97  2097 2097 HOH HOH B . 
AA 5 HOH 98  2098 2098 HOH HOH B . 
AA 5 HOH 99  2099 2099 HOH HOH B . 
AA 5 HOH 100 2100 2100 HOH HOH B . 
AA 5 HOH 101 2101 2101 HOH HOH B . 
AA 5 HOH 102 2102 2102 HOH HOH B . 
AA 5 HOH 103 2103 2103 HOH HOH B . 
AA 5 HOH 104 2104 2104 HOH HOH B . 
AA 5 HOH 105 2105 2105 HOH HOH B . 
AA 5 HOH 106 2106 2106 HOH HOH B . 
AA 5 HOH 107 2107 2107 HOH HOH B . 
AA 5 HOH 108 2108 2108 HOH HOH B . 
AA 5 HOH 109 2109 2109 HOH HOH B . 
AA 5 HOH 110 2110 2110 HOH HOH B . 
AA 5 HOH 111 2111 2111 HOH HOH B . 
AA 5 HOH 112 2112 2112 HOH HOH B . 
AA 5 HOH 113 2113 2113 HOH HOH B . 
AA 5 HOH 114 2114 2114 HOH HOH B . 
AA 5 HOH 115 2115 2115 HOH HOH B . 
AA 5 HOH 116 2116 2116 HOH HOH B . 
AA 5 HOH 117 2117 2117 HOH HOH B . 
AA 5 HOH 118 2118 2118 HOH HOH B . 
AA 5 HOH 119 2119 2119 HOH HOH B . 
AA 5 HOH 120 2120 2120 HOH HOH B . 
AA 5 HOH 121 2121 2121 HOH HOH B . 
AA 5 HOH 122 2122 2122 HOH HOH B . 
AA 5 HOH 123 2123 2123 HOH HOH B . 
AA 5 HOH 124 2124 2124 HOH HOH B . 
AA 5 HOH 125 2125 2125 HOH HOH B . 
AA 5 HOH 126 2126 2126 HOH HOH B . 
AA 5 HOH 127 2127 2127 HOH HOH B . 
AA 5 HOH 128 2128 2128 HOH HOH B . 
AA 5 HOH 129 2129 2129 HOH HOH B . 
AA 5 HOH 130 2130 2130 HOH HOH B . 
AA 5 HOH 131 2131 2131 HOH HOH B . 
AA 5 HOH 132 2132 2132 HOH HOH B . 
AA 5 HOH 133 2133 2133 HOH HOH B . 
AA 5 HOH 134 2134 2134 HOH HOH B . 
AA 5 HOH 135 2135 2135 HOH HOH B . 
AA 5 HOH 136 2136 2136 HOH HOH B . 
AA 5 HOH 137 2137 2137 HOH HOH B . 
AA 5 HOH 138 2138 2138 HOH HOH B . 
AA 5 HOH 139 2139 2139 HOH HOH B . 
AA 5 HOH 140 2140 2140 HOH HOH B . 
AA 5 HOH 141 2141 2141 HOH HOH B . 
AA 5 HOH 142 2142 2142 HOH HOH B . 
AA 5 HOH 143 2143 2143 HOH HOH B . 
AA 5 HOH 144 2144 2144 HOH HOH B . 
AA 5 HOH 145 2145 2145 HOH HOH B . 
AA 5 HOH 146 2146 2146 HOH HOH B . 
AA 5 HOH 147 2147 2147 HOH HOH B . 
AA 5 HOH 148 2148 2148 HOH HOH B . 
AA 5 HOH 149 2149 2149 HOH HOH B . 
AA 5 HOH 150 2150 2150 HOH HOH B . 
AA 5 HOH 151 2151 2151 HOH HOH B . 
AA 5 HOH 152 2152 2152 HOH HOH B . 
AA 5 HOH 153 2153 2153 HOH HOH B . 
AA 5 HOH 154 2154 2154 HOH HOH B . 
AA 5 HOH 155 2155 2155 HOH HOH B . 
AA 5 HOH 156 2156 2156 HOH HOH B . 
AA 5 HOH 157 2157 2157 HOH HOH B . 
AA 5 HOH 158 2158 2158 HOH HOH B . 
AA 5 HOH 159 2159 2159 HOH HOH B . 
AA 5 HOH 160 2160 2160 HOH HOH B . 
AA 5 HOH 161 2161 2161 HOH HOH B . 
AA 5 HOH 162 2162 2162 HOH HOH B . 
AA 5 HOH 163 2163 2163 HOH HOH B . 
AA 5 HOH 164 2164 2164 HOH HOH B . 
AA 5 HOH 165 2165 2165 HOH HOH B . 
AA 5 HOH 166 2166 2166 HOH HOH B . 
AA 5 HOH 167 2167 2167 HOH HOH B . 
AA 5 HOH 168 2168 2168 HOH HOH B . 
AA 5 HOH 169 2169 2169 HOH HOH B . 
AA 5 HOH 170 2170 2170 HOH HOH B . 
AA 5 HOH 171 2171 2171 HOH HOH B . 
AA 5 HOH 172 2172 2172 HOH HOH B . 
AA 5 HOH 173 2173 2173 HOH HOH B . 
AA 5 HOH 174 2174 2174 HOH HOH B . 
AA 5 HOH 175 2175 2175 HOH HOH B . 
AA 5 HOH 176 2176 2176 HOH HOH B . 
AA 5 HOH 177 2177 2177 HOH HOH B . 
AA 5 HOH 178 2178 2178 HOH HOH B . 
AA 5 HOH 179 2179 2179 HOH HOH B . 
AA 5 HOH 180 2180 2180 HOH HOH B . 
AA 5 HOH 181 2181 2181 HOH HOH B . 
AA 5 HOH 182 2182 2182 HOH HOH B . 
AA 5 HOH 183 2183 2183 HOH HOH B . 
AA 5 HOH 184 2184 2184 HOH HOH B . 
AA 5 HOH 185 2185 2185 HOH HOH B . 
AA 5 HOH 186 2186 2186 HOH HOH B . 
AA 5 HOH 187 2187 2187 HOH HOH B . 
AA 5 HOH 188 2188 2188 HOH HOH B . 
AA 5 HOH 189 2189 2189 HOH HOH B . 
AA 5 HOH 190 2190 2190 HOH HOH B . 
AA 5 HOH 191 2191 2191 HOH HOH B . 
AA 5 HOH 192 2192 2192 HOH HOH B . 
AA 5 HOH 193 2193 2193 HOH HOH B . 
AA 5 HOH 194 2194 2194 HOH HOH B . 
AA 5 HOH 195 2195 2195 HOH HOH B . 
AA 5 HOH 196 2196 2196 HOH HOH B . 
AA 5 HOH 197 2197 2197 HOH HOH B . 
AA 5 HOH 198 2198 2198 HOH HOH B . 
AA 5 HOH 199 2199 2199 HOH HOH B . 
AA 5 HOH 200 2200 2200 HOH HOH B . 
AA 5 HOH 201 2201 2201 HOH HOH B . 
AA 5 HOH 202 2202 2202 HOH HOH B . 
AA 5 HOH 203 2203 2203 HOH HOH B . 
AA 5 HOH 204 2204 2204 HOH HOH B . 
AA 5 HOH 205 2205 2205 HOH HOH B . 
AA 5 HOH 206 2206 2206 HOH HOH B . 
AA 5 HOH 207 2207 2207 HOH HOH B . 
AA 5 HOH 208 2208 2208 HOH HOH B . 
AA 5 HOH 209 2209 2209 HOH HOH B . 
AA 5 HOH 210 2210 2210 HOH HOH B . 
AA 5 HOH 211 2211 2211 HOH HOH B . 
AA 5 HOH 212 2212 2212 HOH HOH B . 
AA 5 HOH 213 2213 2213 HOH HOH B . 
AA 5 HOH 214 2214 2214 HOH HOH B . 
AA 5 HOH 215 2215 2215 HOH HOH B . 
AA 5 HOH 216 2216 2216 HOH HOH B . 
AA 5 HOH 217 2217 2217 HOH HOH B . 
AA 5 HOH 218 2218 2218 HOH HOH B . 
AA 5 HOH 219 2219 2219 HOH HOH B . 
AA 5 HOH 220 2220 2220 HOH HOH B . 
AA 5 HOH 221 2221 2221 HOH HOH B . 
AA 5 HOH 222 2222 2222 HOH HOH B . 
AA 5 HOH 223 2223 2223 HOH HOH B . 
AA 5 HOH 224 2224 2224 HOH HOH B . 
AA 5 HOH 225 2225 2225 HOH HOH B . 
AA 5 HOH 226 2226 2226 HOH HOH B . 
AA 5 HOH 227 2227 2227 HOH HOH B . 
AA 5 HOH 228 2228 2228 HOH HOH B . 
AA 5 HOH 229 2229 2229 HOH HOH B . 
AA 5 HOH 230 2230 2230 HOH HOH B . 
AA 5 HOH 231 2231 2231 HOH HOH B . 
AA 5 HOH 232 2232 2232 HOH HOH B . 
AA 5 HOH 233 2233 2233 HOH HOH B . 
AA 5 HOH 234 2234 2234 HOH HOH B . 
AA 5 HOH 235 2235 2235 HOH HOH B . 
AA 5 HOH 236 2236 2236 HOH HOH B . 
AA 5 HOH 237 2237 2237 HOH HOH B . 
AA 5 HOH 238 2238 2238 HOH HOH B . 
AA 5 HOH 239 2239 2239 HOH HOH B . 
AA 5 HOH 240 2240 2240 HOH HOH B . 
AA 5 HOH 241 2241 2241 HOH HOH B . 
AA 5 HOH 242 2242 2242 HOH HOH B . 
AA 5 HOH 243 2243 2243 HOH HOH B . 
AA 5 HOH 244 2244 2244 HOH HOH B . 
AA 5 HOH 245 2245 2245 HOH HOH B . 
AA 5 HOH 246 2246 2246 HOH HOH B . 
AA 5 HOH 247 2247 2247 HOH HOH B . 
AA 5 HOH 248 2248 2248 HOH HOH B . 
AA 5 HOH 249 2249 2249 HOH HOH B . 
AA 5 HOH 250 2250 2250 HOH HOH B . 
AA 5 HOH 251 2251 2251 HOH HOH B . 
AA 5 HOH 252 2252 2252 HOH HOH B . 
AA 5 HOH 253 2253 2253 HOH HOH B . 
AA 5 HOH 254 2254 2254 HOH HOH B . 
AA 5 HOH 255 2255 2255 HOH HOH B . 
AA 5 HOH 256 2256 2256 HOH HOH B . 
AA 5 HOH 257 2257 2257 HOH HOH B . 
AA 5 HOH 258 2258 2258 HOH HOH B . 
AA 5 HOH 259 2259 2259 HOH HOH B . 
AA 5 HOH 260 2260 2260 HOH HOH B . 
AA 5 HOH 261 2261 2261 HOH HOH B . 
AA 5 HOH 262 2262 2262 HOH HOH B . 
AA 5 HOH 263 2263 2263 HOH HOH B . 
AA 5 HOH 264 2264 2264 HOH HOH B . 
AA 5 HOH 265 2265 2265 HOH HOH B . 
AA 5 HOH 266 2266 2266 HOH HOH B . 
AA 5 HOH 267 2267 2267 HOH HOH B . 
AA 5 HOH 268 2268 2268 HOH HOH B . 
AA 5 HOH 269 2269 2269 HOH HOH B . 
AA 5 HOH 270 2270 2270 HOH HOH B . 
BA 5 HOH 1   2001 2001 HOH HOH C . 
BA 5 HOH 2   2002 2002 HOH HOH C . 
BA 5 HOH 3   2003 2003 HOH HOH C . 
BA 5 HOH 4   2004 2004 HOH HOH C . 
BA 5 HOH 5   2005 2005 HOH HOH C . 
BA 5 HOH 6   2006 2006 HOH HOH C . 
BA 5 HOH 7   2007 2007 HOH HOH C . 
BA 5 HOH 8   2008 2008 HOH HOH C . 
BA 5 HOH 9   2009 2009 HOH HOH C . 
BA 5 HOH 10  2010 2010 HOH HOH C . 
BA 5 HOH 11  2011 2011 HOH HOH C . 
BA 5 HOH 12  2012 2012 HOH HOH C . 
BA 5 HOH 13  2013 2013 HOH HOH C . 
BA 5 HOH 14  2014 2014 HOH HOH C . 
BA 5 HOH 15  2015 2015 HOH HOH C . 
BA 5 HOH 16  2016 2016 HOH HOH C . 
BA 5 HOH 17  2017 2017 HOH HOH C . 
BA 5 HOH 18  2018 2018 HOH HOH C . 
BA 5 HOH 19  2019 2019 HOH HOH C . 
BA 5 HOH 20  2020 2020 HOH HOH C . 
BA 5 HOH 21  2021 2021 HOH HOH C . 
BA 5 HOH 22  2022 2022 HOH HOH C . 
BA 5 HOH 23  2023 2023 HOH HOH C . 
BA 5 HOH 24  2024 2024 HOH HOH C . 
BA 5 HOH 25  2025 2025 HOH HOH C . 
BA 5 HOH 26  2026 2026 HOH HOH C . 
BA 5 HOH 27  2027 2027 HOH HOH C . 
BA 5 HOH 28  2028 2028 HOH HOH C . 
BA 5 HOH 29  2029 2029 HOH HOH C . 
BA 5 HOH 30  2030 2030 HOH HOH C . 
BA 5 HOH 31  2031 2031 HOH HOH C . 
BA 5 HOH 32  2032 2032 HOH HOH C . 
BA 5 HOH 33  2033 2033 HOH HOH C . 
BA 5 HOH 34  2034 2034 HOH HOH C . 
BA 5 HOH 35  2035 2035 HOH HOH C . 
BA 5 HOH 36  2036 2036 HOH HOH C . 
BA 5 HOH 37  2037 2037 HOH HOH C . 
BA 5 HOH 38  2038 2038 HOH HOH C . 
BA 5 HOH 39  2039 2039 HOH HOH C . 
BA 5 HOH 40  2040 2040 HOH HOH C . 
BA 5 HOH 41  2041 2041 HOH HOH C . 
BA 5 HOH 42  2042 2042 HOH HOH C . 
BA 5 HOH 43  2043 2043 HOH HOH C . 
BA 5 HOH 44  2044 2044 HOH HOH C . 
BA 5 HOH 45  2045 2045 HOH HOH C . 
BA 5 HOH 46  2046 2046 HOH HOH C . 
BA 5 HOH 47  2047 2047 HOH HOH C . 
BA 5 HOH 48  2048 2048 HOH HOH C . 
BA 5 HOH 49  2049 2049 HOH HOH C . 
BA 5 HOH 50  2050 2050 HOH HOH C . 
BA 5 HOH 51  2051 2051 HOH HOH C . 
BA 5 HOH 52  2052 2052 HOH HOH C . 
BA 5 HOH 53  2053 2053 HOH HOH C . 
BA 5 HOH 54  2054 2054 HOH HOH C . 
BA 5 HOH 55  2055 2055 HOH HOH C . 
BA 5 HOH 56  2056 2056 HOH HOH C . 
BA 5 HOH 57  2057 2057 HOH HOH C . 
BA 5 HOH 58  2058 2058 HOH HOH C . 
BA 5 HOH 59  2059 2059 HOH HOH C . 
BA 5 HOH 60  2060 2060 HOH HOH C . 
BA 5 HOH 61  2061 2061 HOH HOH C . 
BA 5 HOH 62  2062 2062 HOH HOH C . 
BA 5 HOH 63  2063 2063 HOH HOH C . 
BA 5 HOH 64  2064 2064 HOH HOH C . 
BA 5 HOH 65  2065 2065 HOH HOH C . 
BA 5 HOH 66  2066 2066 HOH HOH C . 
BA 5 HOH 67  2067 2067 HOH HOH C . 
BA 5 HOH 68  2068 2068 HOH HOH C . 
BA 5 HOH 69  2069 2069 HOH HOH C . 
BA 5 HOH 70  2070 2070 HOH HOH C . 
BA 5 HOH 71  2071 2071 HOH HOH C . 
BA 5 HOH 72  2072 2072 HOH HOH C . 
BA 5 HOH 73  2073 2073 HOH HOH C . 
BA 5 HOH 74  2074 2074 HOH HOH C . 
BA 5 HOH 75  2075 2075 HOH HOH C . 
BA 5 HOH 76  2076 2076 HOH HOH C . 
BA 5 HOH 77  2077 2077 HOH HOH C . 
BA 5 HOH 78  2078 2078 HOH HOH C . 
BA 5 HOH 79  2079 2079 HOH HOH C . 
BA 5 HOH 80  2080 2080 HOH HOH C . 
BA 5 HOH 81  2081 2081 HOH HOH C . 
BA 5 HOH 82  2082 2082 HOH HOH C . 
BA 5 HOH 83  2083 2083 HOH HOH C . 
BA 5 HOH 84  2084 2084 HOH HOH C . 
BA 5 HOH 85  2085 2085 HOH HOH C . 
BA 5 HOH 86  2086 2086 HOH HOH C . 
BA 5 HOH 87  2087 2087 HOH HOH C . 
BA 5 HOH 88  2088 2088 HOH HOH C . 
BA 5 HOH 89  2089 2089 HOH HOH C . 
BA 5 HOH 90  2090 2090 HOH HOH C . 
BA 5 HOH 91  2091 2091 HOH HOH C . 
BA 5 HOH 92  2092 2092 HOH HOH C . 
BA 5 HOH 93  2093 2093 HOH HOH C . 
BA 5 HOH 94  2094 2094 HOH HOH C . 
BA 5 HOH 95  2095 2095 HOH HOH C . 
BA 5 HOH 96  2096 2096 HOH HOH C . 
BA 5 HOH 97  2097 2097 HOH HOH C . 
BA 5 HOH 98  2098 2098 HOH HOH C . 
BA 5 HOH 99  2099 2099 HOH HOH C . 
BA 5 HOH 100 2100 2100 HOH HOH C . 
BA 5 HOH 101 2101 2101 HOH HOH C . 
BA 5 HOH 102 2102 2102 HOH HOH C . 
BA 5 HOH 103 2103 2103 HOH HOH C . 
BA 5 HOH 104 2104 2104 HOH HOH C . 
BA 5 HOH 105 2105 2105 HOH HOH C . 
BA 5 HOH 106 2106 2106 HOH HOH C . 
BA 5 HOH 107 2107 2107 HOH HOH C . 
BA 5 HOH 108 2108 2108 HOH HOH C . 
BA 5 HOH 109 2109 2109 HOH HOH C . 
BA 5 HOH 110 2110 2110 HOH HOH C . 
BA 5 HOH 111 2111 2111 HOH HOH C . 
BA 5 HOH 112 2112 2112 HOH HOH C . 
BA 5 HOH 113 2113 2113 HOH HOH C . 
BA 5 HOH 114 2114 2114 HOH HOH C . 
BA 5 HOH 115 2115 2115 HOH HOH C . 
BA 5 HOH 116 2116 2116 HOH HOH C . 
BA 5 HOH 117 2117 2117 HOH HOH C . 
BA 5 HOH 118 2118 2118 HOH HOH C . 
BA 5 HOH 119 2119 2119 HOH HOH C . 
BA 5 HOH 120 2120 2120 HOH HOH C . 
BA 5 HOH 121 2121 2121 HOH HOH C . 
BA 5 HOH 122 2122 2122 HOH HOH C . 
BA 5 HOH 123 2123 2123 HOH HOH C . 
BA 5 HOH 124 2124 2124 HOH HOH C . 
BA 5 HOH 125 2125 2125 HOH HOH C . 
BA 5 HOH 126 2126 2126 HOH HOH C . 
BA 5 HOH 127 2127 2127 HOH HOH C . 
BA 5 HOH 128 2128 2128 HOH HOH C . 
BA 5 HOH 129 2129 2129 HOH HOH C . 
BA 5 HOH 130 2130 2130 HOH HOH C . 
BA 5 HOH 131 2131 2131 HOH HOH C . 
BA 5 HOH 132 2132 2132 HOH HOH C . 
BA 5 HOH 133 2133 2133 HOH HOH C . 
BA 5 HOH 134 2134 2134 HOH HOH C . 
BA 5 HOH 135 2135 2135 HOH HOH C . 
BA 5 HOH 136 2136 2136 HOH HOH C . 
BA 5 HOH 137 2137 2137 HOH HOH C . 
BA 5 HOH 138 2138 2138 HOH HOH C . 
BA 5 HOH 139 2139 2139 HOH HOH C . 
BA 5 HOH 140 2140 2140 HOH HOH C . 
BA 5 HOH 141 2141 2141 HOH HOH C . 
BA 5 HOH 142 2142 2142 HOH HOH C . 
BA 5 HOH 143 2143 2143 HOH HOH C . 
BA 5 HOH 144 2144 2144 HOH HOH C . 
BA 5 HOH 145 2145 2145 HOH HOH C . 
BA 5 HOH 146 2146 2146 HOH HOH C . 
BA 5 HOH 147 2147 2147 HOH HOH C . 
BA 5 HOH 148 2148 2148 HOH HOH C . 
BA 5 HOH 149 2149 2149 HOH HOH C . 
BA 5 HOH 150 2150 2150 HOH HOH C . 
BA 5 HOH 151 2151 2151 HOH HOH C . 
BA 5 HOH 152 2152 2152 HOH HOH C . 
BA 5 HOH 153 2153 2153 HOH HOH C . 
BA 5 HOH 154 2154 2154 HOH HOH C . 
BA 5 HOH 155 2155 2155 HOH HOH C . 
BA 5 HOH 156 2156 2156 HOH HOH C . 
BA 5 HOH 157 2157 2157 HOH HOH C . 
BA 5 HOH 158 2158 2158 HOH HOH C . 
BA 5 HOH 159 2159 2159 HOH HOH C . 
BA 5 HOH 160 2160 2160 HOH HOH C . 
BA 5 HOH 161 2161 2161 HOH HOH C . 
BA 5 HOH 162 2162 2162 HOH HOH C . 
BA 5 HOH 163 2163 2163 HOH HOH C . 
BA 5 HOH 164 2164 2164 HOH HOH C . 
BA 5 HOH 165 2165 2165 HOH HOH C . 
BA 5 HOH 166 2166 2166 HOH HOH C . 
BA 5 HOH 167 2167 2167 HOH HOH C . 
BA 5 HOH 168 2168 2168 HOH HOH C . 
BA 5 HOH 169 2169 2169 HOH HOH C . 
BA 5 HOH 170 2170 2170 HOH HOH C . 
BA 5 HOH 171 2171 2171 HOH HOH C . 
BA 5 HOH 172 2172 2172 HOH HOH C . 
BA 5 HOH 173 2173 2173 HOH HOH C . 
BA 5 HOH 174 2174 2174 HOH HOH C . 
BA 5 HOH 175 2175 2175 HOH HOH C . 
BA 5 HOH 176 2176 2176 HOH HOH C . 
BA 5 HOH 177 2177 2177 HOH HOH C . 
BA 5 HOH 178 2178 2178 HOH HOH C . 
BA 5 HOH 179 2179 2179 HOH HOH C . 
BA 5 HOH 180 2180 2180 HOH HOH C . 
BA 5 HOH 181 2181 2181 HOH HOH C . 
BA 5 HOH 182 2182 2182 HOH HOH C . 
BA 5 HOH 183 2183 2183 HOH HOH C . 
BA 5 HOH 184 2184 2184 HOH HOH C . 
BA 5 HOH 185 2185 2185 HOH HOH C . 
BA 5 HOH 186 2186 2186 HOH HOH C . 
BA 5 HOH 187 2187 2187 HOH HOH C . 
BA 5 HOH 188 2188 2188 HOH HOH C . 
BA 5 HOH 189 2189 2189 HOH HOH C . 
BA 5 HOH 190 2190 2190 HOH HOH C . 
BA 5 HOH 191 2191 2191 HOH HOH C . 
BA 5 HOH 192 2192 2192 HOH HOH C . 
BA 5 HOH 193 2193 2193 HOH HOH C . 
BA 5 HOH 194 2194 2194 HOH HOH C . 
BA 5 HOH 195 2195 2195 HOH HOH C . 
BA 5 HOH 196 2196 2196 HOH HOH C . 
BA 5 HOH 197 2197 2197 HOH HOH C . 
BA 5 HOH 198 2198 2198 HOH HOH C . 
BA 5 HOH 199 2199 2199 HOH HOH C . 
BA 5 HOH 200 2200 2200 HOH HOH C . 
BA 5 HOH 201 2201 2201 HOH HOH C . 
BA 5 HOH 202 2202 2202 HOH HOH C . 
BA 5 HOH 203 2203 2203 HOH HOH C . 
BA 5 HOH 204 2204 2204 HOH HOH C . 
BA 5 HOH 205 2205 2205 HOH HOH C . 
BA 5 HOH 206 2206 2206 HOH HOH C . 
BA 5 HOH 207 2207 2207 HOH HOH C . 
BA 5 HOH 208 2208 2208 HOH HOH C . 
BA 5 HOH 209 2209 2209 HOH HOH C . 
BA 5 HOH 210 2210 2210 HOH HOH C . 
BA 5 HOH 211 2211 2211 HOH HOH C . 
BA 5 HOH 212 2212 2212 HOH HOH C . 
BA 5 HOH 213 2213 2213 HOH HOH C . 
BA 5 HOH 214 2214 2214 HOH HOH C . 
BA 5 HOH 215 2215 2215 HOH HOH C . 
BA 5 HOH 216 2216 2216 HOH HOH C . 
BA 5 HOH 217 2217 2217 HOH HOH C . 
BA 5 HOH 218 2218 2218 HOH HOH C . 
BA 5 HOH 219 2219 2219 HOH HOH C . 
BA 5 HOH 220 2220 2220 HOH HOH C . 
BA 5 HOH 221 2221 2221 HOH HOH C . 
BA 5 HOH 222 2222 2222 HOH HOH C . 
BA 5 HOH 223 2223 2223 HOH HOH C . 
BA 5 HOH 224 2224 2224 HOH HOH C . 
BA 5 HOH 225 2225 2225 HOH HOH C . 
BA 5 HOH 226 2226 2226 HOH HOH C . 
BA 5 HOH 227 2227 2227 HOH HOH C . 
BA 5 HOH 228 2228 2228 HOH HOH C . 
BA 5 HOH 229 2229 2229 HOH HOH C . 
BA 5 HOH 230 2230 2230 HOH HOH C . 
BA 5 HOH 231 2231 2231 HOH HOH C . 
BA 5 HOH 232 2232 2232 HOH HOH C . 
BA 5 HOH 233 2233 2233 HOH HOH C . 
BA 5 HOH 234 2234 2234 HOH HOH C . 
BA 5 HOH 235 2235 2235 HOH HOH C . 
BA 5 HOH 236 2236 2236 HOH HOH C . 
BA 5 HOH 237 2237 2237 HOH HOH C . 
BA 5 HOH 238 2238 2238 HOH HOH C . 
BA 5 HOH 239 2239 2239 HOH HOH C . 
BA 5 HOH 240 2240 2240 HOH HOH C . 
BA 5 HOH 241 2241 2241 HOH HOH C . 
BA 5 HOH 242 2242 2242 HOH HOH C . 
BA 5 HOH 243 2243 2243 HOH HOH C . 
BA 5 HOH 244 2244 2244 HOH HOH C . 
BA 5 HOH 245 2245 2245 HOH HOH C . 
BA 5 HOH 246 2246 2246 HOH HOH C . 
BA 5 HOH 247 2247 2247 HOH HOH C . 
BA 5 HOH 248 2248 2248 HOH HOH C . 
BA 5 HOH 249 2249 2249 HOH HOH C . 
BA 5 HOH 250 2250 2250 HOH HOH C . 
BA 5 HOH 251 2251 2251 HOH HOH C . 
BA 5 HOH 252 2252 2252 HOH HOH C . 
BA 5 HOH 253 2253 2253 HOH HOH C . 
BA 5 HOH 254 2254 2254 HOH HOH C . 
BA 5 HOH 255 2255 2255 HOH HOH C . 
BA 5 HOH 256 2256 2256 HOH HOH C . 
BA 5 HOH 257 2257 2257 HOH HOH C . 
BA 5 HOH 258 2258 2258 HOH HOH C . 
BA 5 HOH 259 2259 2259 HOH HOH C . 
BA 5 HOH 260 2260 2260 HOH HOH C . 
BA 5 HOH 261 2261 2261 HOH HOH C . 
BA 5 HOH 262 2262 2262 HOH HOH C . 
BA 5 HOH 263 2263 2263 HOH HOH C . 
BA 5 HOH 264 2264 2264 HOH HOH C . 
BA 5 HOH 265 2265 2265 HOH HOH C . 
BA 5 HOH 266 2266 2266 HOH HOH C . 
BA 5 HOH 267 2267 2267 HOH HOH C . 
BA 5 HOH 268 2268 2268 HOH HOH C . 
BA 5 HOH 269 2269 2269 HOH HOH C . 
BA 5 HOH 270 2270 2270 HOH HOH C . 
BA 5 HOH 271 2271 2271 HOH HOH C . 
BA 5 HOH 272 2272 2272 HOH HOH C . 
BA 5 HOH 273 2273 2273 HOH HOH C . 
CA 5 HOH 1   2001 2001 HOH HOH D . 
CA 5 HOH 2   2002 2002 HOH HOH D . 
CA 5 HOH 3   2003 2003 HOH HOH D . 
CA 5 HOH 4   2004 2004 HOH HOH D . 
CA 5 HOH 5   2005 2005 HOH HOH D . 
CA 5 HOH 6   2006 2006 HOH HOH D . 
CA 5 HOH 7   2007 2007 HOH HOH D . 
CA 5 HOH 8   2008 2008 HOH HOH D . 
CA 5 HOH 9   2009 2009 HOH HOH D . 
CA 5 HOH 10  2010 2010 HOH HOH D . 
CA 5 HOH 11  2011 2011 HOH HOH D . 
CA 5 HOH 12  2012 2012 HOH HOH D . 
CA 5 HOH 13  2013 2013 HOH HOH D . 
CA 5 HOH 14  2014 2014 HOH HOH D . 
CA 5 HOH 15  2015 2015 HOH HOH D . 
CA 5 HOH 16  2016 2016 HOH HOH D . 
CA 5 HOH 17  2017 2017 HOH HOH D . 
CA 5 HOH 18  2018 2018 HOH HOH D . 
CA 5 HOH 19  2019 2019 HOH HOH D . 
CA 5 HOH 20  2020 2020 HOH HOH D . 
CA 5 HOH 21  2021 2021 HOH HOH D . 
CA 5 HOH 22  2022 2022 HOH HOH D . 
CA 5 HOH 23  2023 2023 HOH HOH D . 
CA 5 HOH 24  2024 2024 HOH HOH D . 
CA 5 HOH 25  2025 2025 HOH HOH D . 
CA 5 HOH 26  2026 2026 HOH HOH D . 
CA 5 HOH 27  2027 2027 HOH HOH D . 
CA 5 HOH 28  2028 2028 HOH HOH D . 
CA 5 HOH 29  2029 2029 HOH HOH D . 
CA 5 HOH 30  2030 2030 HOH HOH D . 
CA 5 HOH 31  2031 2031 HOH HOH D . 
CA 5 HOH 32  2032 2032 HOH HOH D . 
CA 5 HOH 33  2033 2033 HOH HOH D . 
CA 5 HOH 34  2034 2034 HOH HOH D . 
CA 5 HOH 35  2035 2035 HOH HOH D . 
CA 5 HOH 36  2036 2036 HOH HOH D . 
CA 5 HOH 37  2037 2037 HOH HOH D . 
CA 5 HOH 38  2038 2038 HOH HOH D . 
CA 5 HOH 39  2039 2039 HOH HOH D . 
CA 5 HOH 40  2040 2040 HOH HOH D . 
CA 5 HOH 41  2041 2041 HOH HOH D . 
CA 5 HOH 42  2042 2042 HOH HOH D . 
CA 5 HOH 43  2043 2043 HOH HOH D . 
CA 5 HOH 44  2044 2044 HOH HOH D . 
CA 5 HOH 45  2045 2045 HOH HOH D . 
CA 5 HOH 46  2046 2046 HOH HOH D . 
CA 5 HOH 47  2047 2047 HOH HOH D . 
CA 5 HOH 48  2048 2048 HOH HOH D . 
CA 5 HOH 49  2049 2049 HOH HOH D . 
CA 5 HOH 50  2050 2050 HOH HOH D . 
CA 5 HOH 51  2051 2051 HOH HOH D . 
CA 5 HOH 52  2052 2052 HOH HOH D . 
CA 5 HOH 53  2053 2053 HOH HOH D . 
CA 5 HOH 54  2054 2054 HOH HOH D . 
CA 5 HOH 55  2055 2055 HOH HOH D . 
CA 5 HOH 56  2056 2056 HOH HOH D . 
CA 5 HOH 57  2057 2057 HOH HOH D . 
CA 5 HOH 58  2058 2058 HOH HOH D . 
CA 5 HOH 59  2059 2059 HOH HOH D . 
CA 5 HOH 60  2060 2060 HOH HOH D . 
CA 5 HOH 61  2061 2061 HOH HOH D . 
CA 5 HOH 62  2062 2062 HOH HOH D . 
CA 5 HOH 63  2063 2063 HOH HOH D . 
CA 5 HOH 64  2064 2064 HOH HOH D . 
CA 5 HOH 65  2065 2065 HOH HOH D . 
CA 5 HOH 66  2066 2066 HOH HOH D . 
CA 5 HOH 67  2067 2067 HOH HOH D . 
CA 5 HOH 68  2068 2068 HOH HOH D . 
CA 5 HOH 69  2069 2069 HOH HOH D . 
CA 5 HOH 70  2070 2070 HOH HOH D . 
CA 5 HOH 71  2071 2071 HOH HOH D . 
CA 5 HOH 72  2072 2072 HOH HOH D . 
CA 5 HOH 73  2073 2073 HOH HOH D . 
CA 5 HOH 74  2074 2074 HOH HOH D . 
CA 5 HOH 75  2075 2075 HOH HOH D . 
CA 5 HOH 76  2076 2076 HOH HOH D . 
CA 5 HOH 77  2077 2077 HOH HOH D . 
CA 5 HOH 78  2078 2078 HOH HOH D . 
CA 5 HOH 79  2079 2079 HOH HOH D . 
CA 5 HOH 80  2080 2080 HOH HOH D . 
CA 5 HOH 81  2081 2081 HOH HOH D . 
CA 5 HOH 82  2082 2082 HOH HOH D . 
CA 5 HOH 83  2083 2083 HOH HOH D . 
CA 5 HOH 84  2084 2084 HOH HOH D . 
CA 5 HOH 85  2085 2085 HOH HOH D . 
CA 5 HOH 86  2086 2086 HOH HOH D . 
CA 5 HOH 87  2087 2087 HOH HOH D . 
CA 5 HOH 88  2088 2088 HOH HOH D . 
CA 5 HOH 89  2089 2089 HOH HOH D . 
CA 5 HOH 90  2090 2090 HOH HOH D . 
CA 5 HOH 91  2091 2091 HOH HOH D . 
CA 5 HOH 92  2092 2092 HOH HOH D . 
CA 5 HOH 93  2093 2093 HOH HOH D . 
CA 5 HOH 94  2094 2094 HOH HOH D . 
CA 5 HOH 95  2095 2095 HOH HOH D . 
CA 5 HOH 96  2096 2096 HOH HOH D . 
CA 5 HOH 97  2097 2097 HOH HOH D . 
CA 5 HOH 98  2098 2098 HOH HOH D . 
CA 5 HOH 99  2099 2099 HOH HOH D . 
CA 5 HOH 100 2100 2100 HOH HOH D . 
CA 5 HOH 101 2101 2101 HOH HOH D . 
CA 5 HOH 102 2102 2102 HOH HOH D . 
CA 5 HOH 103 2103 2103 HOH HOH D . 
CA 5 HOH 104 2104 2104 HOH HOH D . 
CA 5 HOH 105 2105 2105 HOH HOH D . 
CA 5 HOH 106 2106 2106 HOH HOH D . 
CA 5 HOH 107 2107 2107 HOH HOH D . 
CA 5 HOH 108 2108 2108 HOH HOH D . 
CA 5 HOH 109 2109 2109 HOH HOH D . 
CA 5 HOH 110 2110 2110 HOH HOH D . 
CA 5 HOH 111 2111 2111 HOH HOH D . 
CA 5 HOH 112 2112 2112 HOH HOH D . 
CA 5 HOH 113 2113 2113 HOH HOH D . 
CA 5 HOH 114 2114 2114 HOH HOH D . 
CA 5 HOH 115 2115 2115 HOH HOH D . 
CA 5 HOH 116 2116 2116 HOH HOH D . 
CA 5 HOH 117 2117 2117 HOH HOH D . 
CA 5 HOH 118 2118 2118 HOH HOH D . 
CA 5 HOH 119 2119 2119 HOH HOH D . 
CA 5 HOH 120 2120 2120 HOH HOH D . 
CA 5 HOH 121 2121 2121 HOH HOH D . 
CA 5 HOH 122 2122 2122 HOH HOH D . 
CA 5 HOH 123 2123 2123 HOH HOH D . 
CA 5 HOH 124 2124 2124 HOH HOH D . 
CA 5 HOH 125 2125 2125 HOH HOH D . 
CA 5 HOH 126 2126 2126 HOH HOH D . 
CA 5 HOH 127 2127 2127 HOH HOH D . 
CA 5 HOH 128 2128 2128 HOH HOH D . 
CA 5 HOH 129 2129 2129 HOH HOH D . 
CA 5 HOH 130 2130 2130 HOH HOH D . 
CA 5 HOH 131 2131 2131 HOH HOH D . 
CA 5 HOH 132 2132 2132 HOH HOH D . 
CA 5 HOH 133 2133 2133 HOH HOH D . 
CA 5 HOH 134 2134 2134 HOH HOH D . 
CA 5 HOH 135 2135 2135 HOH HOH D . 
CA 5 HOH 136 2136 2136 HOH HOH D . 
CA 5 HOH 137 2137 2137 HOH HOH D . 
CA 5 HOH 138 2138 2138 HOH HOH D . 
CA 5 HOH 139 2139 2139 HOH HOH D . 
CA 5 HOH 140 2140 2140 HOH HOH D . 
CA 5 HOH 141 2141 2141 HOH HOH D . 
CA 5 HOH 142 2142 2142 HOH HOH D . 
CA 5 HOH 143 2143 2143 HOH HOH D . 
CA 5 HOH 144 2144 2144 HOH HOH D . 
CA 5 HOH 145 2145 2145 HOH HOH D . 
CA 5 HOH 146 2146 2146 HOH HOH D . 
CA 5 HOH 147 2147 2147 HOH HOH D . 
CA 5 HOH 148 2148 2148 HOH HOH D . 
CA 5 HOH 149 2149 2149 HOH HOH D . 
CA 5 HOH 150 2150 2150 HOH HOH D . 
CA 5 HOH 151 2151 2151 HOH HOH D . 
CA 5 HOH 152 2152 2152 HOH HOH D . 
CA 5 HOH 153 2153 2153 HOH HOH D . 
CA 5 HOH 154 2154 2154 HOH HOH D . 
CA 5 HOH 155 2155 2155 HOH HOH D . 
CA 5 HOH 156 2156 2156 HOH HOH D . 
CA 5 HOH 157 2157 2157 HOH HOH D . 
CA 5 HOH 158 2158 2158 HOH HOH D . 
CA 5 HOH 159 2159 2159 HOH HOH D . 
CA 5 HOH 160 2160 2160 HOH HOH D . 
CA 5 HOH 161 2161 2161 HOH HOH D . 
CA 5 HOH 162 2162 2162 HOH HOH D . 
CA 5 HOH 163 2163 2163 HOH HOH D . 
CA 5 HOH 164 2164 2164 HOH HOH D . 
CA 5 HOH 165 2165 2165 HOH HOH D . 
CA 5 HOH 166 2166 2166 HOH HOH D . 
CA 5 HOH 167 2167 2167 HOH HOH D . 
CA 5 HOH 168 2168 2168 HOH HOH D . 
CA 5 HOH 169 2169 2169 HOH HOH D . 
CA 5 HOH 170 2170 2170 HOH HOH D . 
CA 5 HOH 171 2171 2171 HOH HOH D . 
CA 5 HOH 172 2172 2172 HOH HOH D . 
CA 5 HOH 173 2173 2173 HOH HOH D . 
CA 5 HOH 174 2174 2174 HOH HOH D . 
CA 5 HOH 175 2175 2175 HOH HOH D . 
CA 5 HOH 176 2176 2176 HOH HOH D . 
CA 5 HOH 177 2177 2177 HOH HOH D . 
CA 5 HOH 178 2178 2178 HOH HOH D . 
CA 5 HOH 179 2179 2179 HOH HOH D . 
CA 5 HOH 180 2180 2180 HOH HOH D . 
CA 5 HOH 181 2181 2181 HOH HOH D . 
CA 5 HOH 182 2182 2182 HOH HOH D . 
CA 5 HOH 183 2183 2183 HOH HOH D . 
CA 5 HOH 184 2184 2184 HOH HOH D . 
CA 5 HOH 185 2185 2185 HOH HOH D . 
CA 5 HOH 186 2186 2186 HOH HOH D . 
CA 5 HOH 187 2187 2187 HOH HOH D . 
CA 5 HOH 188 2188 2188 HOH HOH D . 
CA 5 HOH 189 2189 2189 HOH HOH D . 
CA 5 HOH 190 2190 2190 HOH HOH D . 
CA 5 HOH 191 2191 2191 HOH HOH D . 
CA 5 HOH 192 2192 2192 HOH HOH D . 
CA 5 HOH 193 2193 2193 HOH HOH D . 
CA 5 HOH 194 2194 2194 HOH HOH D . 
CA 5 HOH 195 2195 2195 HOH HOH D . 
CA 5 HOH 196 2196 2196 HOH HOH D . 
CA 5 HOH 197 2197 2197 HOH HOH D . 
CA 5 HOH 198 2198 2198 HOH HOH D . 
CA 5 HOH 199 2199 2199 HOH HOH D . 
CA 5 HOH 200 2200 2200 HOH HOH D . 
CA 5 HOH 201 2201 2201 HOH HOH D . 
CA 5 HOH 202 2202 2202 HOH HOH D . 
CA 5 HOH 203 2203 2203 HOH HOH D . 
CA 5 HOH 204 2204 2204 HOH HOH D . 
CA 5 HOH 205 2205 2205 HOH HOH D . 
CA 5 HOH 206 2206 2206 HOH HOH D . 
CA 5 HOH 207 2207 2207 HOH HOH D . 
CA 5 HOH 208 2208 2208 HOH HOH D . 
CA 5 HOH 209 2209 2209 HOH HOH D . 
CA 5 HOH 210 2210 2210 HOH HOH D . 
CA 5 HOH 211 2211 2211 HOH HOH D . 
CA 5 HOH 212 2212 2212 HOH HOH D . 
CA 5 HOH 213 2213 2213 HOH HOH D . 
CA 5 HOH 214 2214 2214 HOH HOH D . 
CA 5 HOH 215 2215 2215 HOH HOH D . 
CA 5 HOH 216 2216 2216 HOH HOH D . 
CA 5 HOH 217 2217 2217 HOH HOH D . 
CA 5 HOH 218 2218 2218 HOH HOH D . 
CA 5 HOH 219 2219 2219 HOH HOH D . 
CA 5 HOH 220 2220 2220 HOH HOH D . 
CA 5 HOH 221 2221 2221 HOH HOH D . 
CA 5 HOH 222 2222 2222 HOH HOH D . 
CA 5 HOH 223 2223 2223 HOH HOH D . 
CA 5 HOH 224 2224 2224 HOH HOH D . 
CA 5 HOH 225 2225 2225 HOH HOH D . 
CA 5 HOH 226 2226 2226 HOH HOH D . 
CA 5 HOH 227 2227 2227 HOH HOH D . 
CA 5 HOH 228 2228 2228 HOH HOH D . 
CA 5 HOH 229 2229 2229 HOH HOH D . 
CA 5 HOH 230 2230 2230 HOH HOH D . 
CA 5 HOH 231 2231 2231 HOH HOH D . 
CA 5 HOH 232 2232 2232 HOH HOH D . 
CA 5 HOH 233 2233 2233 HOH HOH D . 
CA 5 HOH 234 2234 2234 HOH HOH D . 
CA 5 HOH 235 2235 2235 HOH HOH D . 
CA 5 HOH 236 2236 2236 HOH HOH D . 
CA 5 HOH 237 2237 2237 HOH HOH D . 
CA 5 HOH 238 2238 2238 HOH HOH D . 
CA 5 HOH 239 2239 2239 HOH HOH D . 
CA 5 HOH 240 2240 2240 HOH HOH D . 
CA 5 HOH 241 2241 2241 HOH HOH D . 
CA 5 HOH 242 2242 2242 HOH HOH D . 
CA 5 HOH 243 2243 2243 HOH HOH D . 
CA 5 HOH 244 2244 2244 HOH HOH D . 
CA 5 HOH 245 2245 2245 HOH HOH D . 
CA 5 HOH 246 2246 2246 HOH HOH D . 
CA 5 HOH 247 2247 2247 HOH HOH D . 
CA 5 HOH 248 2248 2248 HOH HOH D . 
CA 5 HOH 249 2249 2249 HOH HOH D . 
CA 5 HOH 250 2250 2250 HOH HOH D . 
CA 5 HOH 251 2251 2251 HOH HOH D . 
CA 5 HOH 252 2252 2252 HOH HOH D . 
CA 5 HOH 253 2253 2253 HOH HOH D . 
CA 5 HOH 254 2254 2254 HOH HOH D . 
CA 5 HOH 255 2255 2255 HOH HOH D . 
CA 5 HOH 256 2256 2256 HOH HOH D . 
CA 5 HOH 257 2257 2257 HOH HOH D . 
CA 5 HOH 258 2258 2258 HOH HOH D . 
CA 5 HOH 259 2259 2259 HOH HOH D . 
CA 5 HOH 260 2260 2260 HOH HOH D . 
CA 5 HOH 261 2261 2261 HOH HOH D . 
CA 5 HOH 262 2262 2262 HOH HOH D . 
CA 5 HOH 263 2263 2263 HOH HOH D . 
CA 5 HOH 264 2264 2264 HOH HOH D . 
CA 5 HOH 265 2265 2265 HOH HOH D . 
CA 5 HOH 266 2266 2266 HOH HOH D . 
CA 5 HOH 267 2267 2267 HOH HOH D . 
DA 5 HOH 1   2001 2001 HOH HOH E . 
DA 5 HOH 2   2002 2002 HOH HOH E . 
DA 5 HOH 3   2003 2003 HOH HOH E . 
DA 5 HOH 4   2004 2004 HOH HOH E . 
DA 5 HOH 5   2005 2005 HOH HOH E . 
DA 5 HOH 6   2006 2006 HOH HOH E . 
DA 5 HOH 7   2007 2007 HOH HOH E . 
DA 5 HOH 8   2008 2008 HOH HOH E . 
DA 5 HOH 9   2009 2009 HOH HOH E . 
DA 5 HOH 10  2010 2010 HOH HOH E . 
DA 5 HOH 11  2011 2011 HOH HOH E . 
DA 5 HOH 12  2012 2012 HOH HOH E . 
DA 5 HOH 13  2013 2013 HOH HOH E . 
DA 5 HOH 14  2014 2014 HOH HOH E . 
DA 5 HOH 15  2015 2015 HOH HOH E . 
DA 5 HOH 16  2016 2016 HOH HOH E . 
DA 5 HOH 17  2017 2017 HOH HOH E . 
DA 5 HOH 18  2018 2018 HOH HOH E . 
DA 5 HOH 19  2019 2019 HOH HOH E . 
DA 5 HOH 20  2020 2020 HOH HOH E . 
DA 5 HOH 21  2021 2021 HOH HOH E . 
DA 5 HOH 22  2022 2022 HOH HOH E . 
DA 5 HOH 23  2023 2023 HOH HOH E . 
DA 5 HOH 24  2024 2024 HOH HOH E . 
DA 5 HOH 25  2025 2025 HOH HOH E . 
DA 5 HOH 26  2026 2026 HOH HOH E . 
DA 5 HOH 27  2027 2027 HOH HOH E . 
DA 5 HOH 28  2028 2028 HOH HOH E . 
DA 5 HOH 29  2029 2029 HOH HOH E . 
DA 5 HOH 30  2030 2030 HOH HOH E . 
DA 5 HOH 31  2031 2031 HOH HOH E . 
DA 5 HOH 32  2032 2032 HOH HOH E . 
DA 5 HOH 33  2033 2033 HOH HOH E . 
DA 5 HOH 34  2034 2034 HOH HOH E . 
DA 5 HOH 35  2035 2035 HOH HOH E . 
DA 5 HOH 36  2036 2036 HOH HOH E . 
DA 5 HOH 37  2037 2037 HOH HOH E . 
DA 5 HOH 38  2038 2038 HOH HOH E . 
DA 5 HOH 39  2039 2039 HOH HOH E . 
DA 5 HOH 40  2040 2040 HOH HOH E . 
DA 5 HOH 41  2041 2041 HOH HOH E . 
DA 5 HOH 42  2042 2042 HOH HOH E . 
DA 5 HOH 43  2043 2043 HOH HOH E . 
DA 5 HOH 44  2044 2044 HOH HOH E . 
DA 5 HOH 45  2045 2045 HOH HOH E . 
DA 5 HOH 46  2046 2046 HOH HOH E . 
DA 5 HOH 47  2047 2047 HOH HOH E . 
DA 5 HOH 48  2048 2048 HOH HOH E . 
DA 5 HOH 49  2049 2049 HOH HOH E . 
DA 5 HOH 50  2050 2050 HOH HOH E . 
DA 5 HOH 51  2051 2051 HOH HOH E . 
DA 5 HOH 52  2052 2052 HOH HOH E . 
DA 5 HOH 53  2053 2053 HOH HOH E . 
DA 5 HOH 54  2054 2054 HOH HOH E . 
DA 5 HOH 55  2055 2055 HOH HOH E . 
DA 5 HOH 56  2056 2056 HOH HOH E . 
DA 5 HOH 57  2057 2057 HOH HOH E . 
DA 5 HOH 58  2058 2058 HOH HOH E . 
DA 5 HOH 59  2059 2059 HOH HOH E . 
DA 5 HOH 60  2060 2060 HOH HOH E . 
DA 5 HOH 61  2061 2061 HOH HOH E . 
DA 5 HOH 62  2062 2062 HOH HOH E . 
DA 5 HOH 63  2063 2063 HOH HOH E . 
DA 5 HOH 64  2064 2064 HOH HOH E . 
DA 5 HOH 65  2065 2065 HOH HOH E . 
DA 5 HOH 66  2066 2066 HOH HOH E . 
DA 5 HOH 67  2067 2067 HOH HOH E . 
DA 5 HOH 68  2068 2068 HOH HOH E . 
DA 5 HOH 69  2069 2069 HOH HOH E . 
DA 5 HOH 70  2070 2070 HOH HOH E . 
DA 5 HOH 71  2071 2071 HOH HOH E . 
DA 5 HOH 72  2072 2072 HOH HOH E . 
DA 5 HOH 73  2073 2073 HOH HOH E . 
DA 5 HOH 74  2074 2074 HOH HOH E . 
DA 5 HOH 75  2075 2075 HOH HOH E . 
DA 5 HOH 76  2076 2076 HOH HOH E . 
DA 5 HOH 77  2077 2077 HOH HOH E . 
DA 5 HOH 78  2078 2078 HOH HOH E . 
DA 5 HOH 79  2079 2079 HOH HOH E . 
DA 5 HOH 80  2080 2080 HOH HOH E . 
DA 5 HOH 81  2081 2081 HOH HOH E . 
DA 5 HOH 82  2082 2082 HOH HOH E . 
DA 5 HOH 83  2083 2083 HOH HOH E . 
DA 5 HOH 84  2084 2084 HOH HOH E . 
DA 5 HOH 85  2085 2085 HOH HOH E . 
DA 5 HOH 86  2086 2086 HOH HOH E . 
DA 5 HOH 87  2087 2087 HOH HOH E . 
DA 5 HOH 88  2088 2088 HOH HOH E . 
DA 5 HOH 89  2089 2089 HOH HOH E . 
DA 5 HOH 90  2090 2090 HOH HOH E . 
DA 5 HOH 91  2091 2091 HOH HOH E . 
DA 5 HOH 92  2092 2092 HOH HOH E . 
DA 5 HOH 93  2093 2093 HOH HOH E . 
DA 5 HOH 94  2094 2094 HOH HOH E . 
DA 5 HOH 95  2095 2095 HOH HOH E . 
DA 5 HOH 96  2096 2096 HOH HOH E . 
DA 5 HOH 97  2097 2097 HOH HOH E . 
DA 5 HOH 98  2098 2098 HOH HOH E . 
DA 5 HOH 99  2099 2099 HOH HOH E . 
DA 5 HOH 100 2100 2100 HOH HOH E . 
DA 5 HOH 101 2101 2101 HOH HOH E . 
DA 5 HOH 102 2102 2102 HOH HOH E . 
DA 5 HOH 103 2103 2103 HOH HOH E . 
DA 5 HOH 104 2104 2104 HOH HOH E . 
DA 5 HOH 105 2105 2105 HOH HOH E . 
DA 5 HOH 106 2106 2106 HOH HOH E . 
DA 5 HOH 107 2107 2107 HOH HOH E . 
DA 5 HOH 108 2108 2108 HOH HOH E . 
DA 5 HOH 109 2109 2109 HOH HOH E . 
DA 5 HOH 110 2110 2110 HOH HOH E . 
DA 5 HOH 111 2111 2111 HOH HOH E . 
DA 5 HOH 112 2112 2112 HOH HOH E . 
DA 5 HOH 113 2113 2113 HOH HOH E . 
DA 5 HOH 114 2114 2114 HOH HOH E . 
DA 5 HOH 115 2115 2115 HOH HOH E . 
DA 5 HOH 116 2116 2116 HOH HOH E . 
DA 5 HOH 117 2117 2117 HOH HOH E . 
DA 5 HOH 118 2118 2118 HOH HOH E . 
DA 5 HOH 119 2119 2119 HOH HOH E . 
DA 5 HOH 120 2120 2120 HOH HOH E . 
DA 5 HOH 121 2121 2121 HOH HOH E . 
DA 5 HOH 122 2122 2122 HOH HOH E . 
DA 5 HOH 123 2123 2123 HOH HOH E . 
DA 5 HOH 124 2124 2124 HOH HOH E . 
DA 5 HOH 125 2125 2125 HOH HOH E . 
DA 5 HOH 126 2126 2126 HOH HOH E . 
DA 5 HOH 127 2127 2127 HOH HOH E . 
DA 5 HOH 128 2128 2128 HOH HOH E . 
DA 5 HOH 129 2129 2129 HOH HOH E . 
DA 5 HOH 130 2130 2130 HOH HOH E . 
DA 5 HOH 131 2131 2131 HOH HOH E . 
DA 5 HOH 132 2132 2132 HOH HOH E . 
DA 5 HOH 133 2133 2133 HOH HOH E . 
DA 5 HOH 134 2134 2134 HOH HOH E . 
DA 5 HOH 135 2135 2135 HOH HOH E . 
DA 5 HOH 136 2136 2136 HOH HOH E . 
DA 5 HOH 137 2137 2137 HOH HOH E . 
DA 5 HOH 138 2138 2138 HOH HOH E . 
DA 5 HOH 139 2139 2139 HOH HOH E . 
DA 5 HOH 140 2140 2140 HOH HOH E . 
DA 5 HOH 141 2141 2141 HOH HOH E . 
DA 5 HOH 142 2142 2142 HOH HOH E . 
DA 5 HOH 143 2143 2143 HOH HOH E . 
DA 5 HOH 144 2144 2144 HOH HOH E . 
DA 5 HOH 145 2145 2145 HOH HOH E . 
DA 5 HOH 146 2146 2146 HOH HOH E . 
DA 5 HOH 147 2147 2147 HOH HOH E . 
DA 5 HOH 148 2148 2148 HOH HOH E . 
DA 5 HOH 149 2149 2149 HOH HOH E . 
DA 5 HOH 150 2150 2150 HOH HOH E . 
DA 5 HOH 151 2151 2151 HOH HOH E . 
DA 5 HOH 152 2152 2152 HOH HOH E . 
DA 5 HOH 153 2153 2153 HOH HOH E . 
DA 5 HOH 154 2154 2154 HOH HOH E . 
DA 5 HOH 155 2155 2155 HOH HOH E . 
DA 5 HOH 156 2156 2156 HOH HOH E . 
DA 5 HOH 157 2157 2157 HOH HOH E . 
DA 5 HOH 158 2158 2158 HOH HOH E . 
DA 5 HOH 159 2159 2159 HOH HOH E . 
DA 5 HOH 160 2160 2160 HOH HOH E . 
DA 5 HOH 161 2161 2161 HOH HOH E . 
DA 5 HOH 162 2162 2162 HOH HOH E . 
DA 5 HOH 163 2163 2163 HOH HOH E . 
DA 5 HOH 164 2164 2164 HOH HOH E . 
DA 5 HOH 165 2165 2165 HOH HOH E . 
DA 5 HOH 166 2166 2166 HOH HOH E . 
DA 5 HOH 167 2167 2167 HOH HOH E . 
DA 5 HOH 168 2168 2168 HOH HOH E . 
DA 5 HOH 169 2169 2169 HOH HOH E . 
DA 5 HOH 170 2170 2170 HOH HOH E . 
DA 5 HOH 171 2171 2171 HOH HOH E . 
DA 5 HOH 172 2172 2172 HOH HOH E . 
DA 5 HOH 173 2173 2173 HOH HOH E . 
DA 5 HOH 174 2174 2174 HOH HOH E . 
DA 5 HOH 175 2175 2175 HOH HOH E . 
DA 5 HOH 176 2176 2176 HOH HOH E . 
DA 5 HOH 177 2177 2177 HOH HOH E . 
DA 5 HOH 178 2178 2178 HOH HOH E . 
DA 5 HOH 179 2179 2179 HOH HOH E . 
DA 5 HOH 180 2180 2180 HOH HOH E . 
DA 5 HOH 181 2181 2181 HOH HOH E . 
DA 5 HOH 182 2182 2182 HOH HOH E . 
DA 5 HOH 183 2183 2183 HOH HOH E . 
DA 5 HOH 184 2184 2184 HOH HOH E . 
DA 5 HOH 185 2185 2185 HOH HOH E . 
DA 5 HOH 186 2186 2186 HOH HOH E . 
DA 5 HOH 187 2187 2187 HOH HOH E . 
DA 5 HOH 188 2188 2188 HOH HOH E . 
DA 5 HOH 189 2189 2189 HOH HOH E . 
DA 5 HOH 190 2190 2190 HOH HOH E . 
DA 5 HOH 191 2191 2191 HOH HOH E . 
DA 5 HOH 192 2192 2192 HOH HOH E . 
DA 5 HOH 193 2193 2193 HOH HOH E . 
DA 5 HOH 194 2194 2194 HOH HOH E . 
DA 5 HOH 195 2195 2195 HOH HOH E . 
DA 5 HOH 196 2196 2196 HOH HOH E . 
DA 5 HOH 197 2197 2197 HOH HOH E . 
DA 5 HOH 198 2198 2198 HOH HOH E . 
DA 5 HOH 199 2199 2199 HOH HOH E . 
DA 5 HOH 200 2200 2200 HOH HOH E . 
DA 5 HOH 201 2201 2201 HOH HOH E . 
DA 5 HOH 202 2202 2202 HOH HOH E . 
DA 5 HOH 203 2203 2203 HOH HOH E . 
DA 5 HOH 204 2204 2204 HOH HOH E . 
DA 5 HOH 205 2205 2205 HOH HOH E . 
DA 5 HOH 206 2206 2206 HOH HOH E . 
DA 5 HOH 207 2207 2207 HOH HOH E . 
DA 5 HOH 208 2208 2208 HOH HOH E . 
DA 5 HOH 209 2209 2209 HOH HOH E . 
DA 5 HOH 210 2210 2210 HOH HOH E . 
DA 5 HOH 211 2211 2211 HOH HOH E . 
DA 5 HOH 212 2212 2212 HOH HOH E . 
DA 5 HOH 213 2213 2213 HOH HOH E . 
DA 5 HOH 214 2214 2214 HOH HOH E . 
DA 5 HOH 215 2215 2215 HOH HOH E . 
DA 5 HOH 216 2216 2216 HOH HOH E . 
DA 5 HOH 217 2217 2217 HOH HOH E . 
DA 5 HOH 218 2218 2218 HOH HOH E . 
DA 5 HOH 219 2219 2219 HOH HOH E . 
DA 5 HOH 220 2220 2220 HOH HOH E . 
DA 5 HOH 221 2221 2221 HOH HOH E . 
DA 5 HOH 222 2222 2222 HOH HOH E . 
DA 5 HOH 223 2223 2223 HOH HOH E . 
DA 5 HOH 224 2224 2224 HOH HOH E . 
DA 5 HOH 225 2225 2225 HOH HOH E . 
DA 5 HOH 226 2226 2226 HOH HOH E . 
DA 5 HOH 227 2227 2227 HOH HOH E . 
DA 5 HOH 228 2228 2228 HOH HOH E . 
DA 5 HOH 229 2229 2229 HOH HOH E . 
DA 5 HOH 230 2230 2230 HOH HOH E . 
DA 5 HOH 231 2231 2231 HOH HOH E . 
DA 5 HOH 232 2232 2232 HOH HOH E . 
DA 5 HOH 233 2233 2233 HOH HOH E . 
DA 5 HOH 234 2234 2234 HOH HOH E . 
DA 5 HOH 235 2235 2235 HOH HOH E . 
DA 5 HOH 236 2236 2236 HOH HOH E . 
DA 5 HOH 237 2237 2237 HOH HOH E . 
DA 5 HOH 238 2238 2238 HOH HOH E . 
DA 5 HOH 239 2239 2239 HOH HOH E . 
DA 5 HOH 240 2240 2240 HOH HOH E . 
DA 5 HOH 241 2241 2241 HOH HOH E . 
DA 5 HOH 242 2242 2242 HOH HOH E . 
DA 5 HOH 243 2243 2243 HOH HOH E . 
DA 5 HOH 244 2244 2244 HOH HOH E . 
DA 5 HOH 245 2245 2245 HOH HOH E . 
DA 5 HOH 246 2246 2246 HOH HOH E . 
DA 5 HOH 247 2247 2247 HOH HOH E . 
DA 5 HOH 248 2248 2248 HOH HOH E . 
DA 5 HOH 249 2249 2249 HOH HOH E . 
DA 5 HOH 250 2250 2250 HOH HOH E . 
DA 5 HOH 251 2251 2251 HOH HOH E . 
DA 5 HOH 252 2252 2252 HOH HOH E . 
DA 5 HOH 253 2253 2253 HOH HOH E . 
DA 5 HOH 254 2254 2254 HOH HOH E . 
DA 5 HOH 255 2255 2255 HOH HOH E . 
DA 5 HOH 256 2256 2256 HOH HOH E . 
DA 5 HOH 257 2257 2257 HOH HOH E . 
DA 5 HOH 258 2258 2258 HOH HOH E . 
DA 5 HOH 259 2259 2259 HOH HOH E . 
DA 5 HOH 260 2260 2260 HOH HOH E . 
DA 5 HOH 261 2261 2261 HOH HOH E . 
DA 5 HOH 262 2262 2262 HOH HOH E . 
DA 5 HOH 263 2263 2263 HOH HOH E . 
DA 5 HOH 264 2264 2264 HOH HOH E . 
DA 5 HOH 265 2265 2265 HOH HOH E . 
DA 5 HOH 266 2266 2266 HOH HOH E . 
DA 5 HOH 267 2267 2267 HOH HOH E . 
DA 5 HOH 268 2268 2268 HOH HOH E . 
DA 5 HOH 269 2269 2269 HOH HOH E . 
DA 5 HOH 270 2270 2270 HOH HOH E . 
DA 5 HOH 271 2271 2271 HOH HOH E . 
DA 5 HOH 272 2272 2272 HOH HOH E . 
DA 5 HOH 273 2273 2273 HOH HOH E . 
DA 5 HOH 274 2274 2274 HOH HOH E . 
DA 5 HOH 275 2275 2275 HOH HOH E . 
DA 5 HOH 276 2276 2276 HOH HOH E . 
DA 5 HOH 277 2277 2277 HOH HOH E . 
DA 5 HOH 278 2278 2278 HOH HOH E . 
DA 5 HOH 279 2279 2279 HOH HOH E . 
DA 5 HOH 280 2280 2280 HOH HOH E . 
DA 5 HOH 281 2281 2281 HOH HOH E . 
DA 5 HOH 282 2282 2282 HOH HOH E . 
DA 5 HOH 283 2283 2283 HOH HOH E . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 32 A ASN 32 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 32 B ASN 32 ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 32 C ASN 32 ? ASN 'GLYCOSYLATION SITE' 
4 D ASN 32 D ASN 32 ? ASN 'GLYCOSYLATION SITE' 
5 E ASN 32 E ASN 32 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 8480  ? 
1 MORE         -56.8 ? 
1 'SSA (A^2)'  46250 ? 
# 
_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   OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 75.7  ? 
2   OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 120.0 ? 
3   OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 74.3  ? 
4   OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O   ? A  GLN 137 ? A GLN 137  ? 1_555 69.5  ? 
5   OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O   ? A  GLN 137 ? A GLN 137  ? 1_555 112.8 ? 
6   OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O   ? A  GLN 137 ? A GLN 137  ? 1_555 76.3  ? 
7   OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 49.6  ? 
8   OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 82.4  ? 
9   OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 156.6 ? 
10  O   ? A  GLN 137 ? A GLN 137  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 111.6 ? 
11  OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 100.1 ? 
12  OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 162.1 ? 
13  OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 121.6 ? 
14  O   ? A  GLN 137 ? A GLN 137  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 81.0  ? 
15  OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 81.8  ? 
16  OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O1P ? I  TPO .   ? A TPO 500  ? 1_555 126.6 ? 
17  OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O1P ? I  TPO .   ? A TPO 500  ? 1_555 81.6  ? 
18  OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O1P ? I  TPO .   ? A TPO 500  ? 1_555 98.4  ? 
19  O   ? A  GLN 137 ? A GLN 137  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O1P ? I  TPO .   ? A TPO 500  ? 1_555 162.0 ? 
20  OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O1P ? I  TPO .   ? A TPO 500  ? 1_555 80.2  ? 
21  OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 O1P ? I  TPO .   ? A TPO 500  ? 1_555 87.5  ? 
22  OD1 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 146.0 ? 
23  OD1 ? A  ASN 59  ? A ASN 59   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 120.5 ? 
24  OE2 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 50.0  ? 
25  O   ? A  GLN 137 ? A GLN 137  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 76.5  ? 
26  OD2 ? A  ASP 58  ? A ASP 58   ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 151.8 ? 
27  OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 72.7  ? 
28  O1P ? I  TPO .   ? A TPO 500  ? 1_555 CA ? F CA . ? A CA 205 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 86.9  ? 
29  O   ? Z  HOH .   ? A HOH 2184 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 85.1  ? 
30  O   ? Z  HOH .   ? A HOH 2184 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 O2P ? I  TPO .   ? A TPO 500  ? 1_555 176.5 ? 
31  OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 O2P ? I  TPO .   ? A TPO 500  ? 1_555 91.7  ? 
32  O   ? Z  HOH .   ? A HOH 2184 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 O   ? Z  HOH .   ? A HOH 2192 ? 1_555 95.0  ? 
33  OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 O   ? Z  HOH .   ? A HOH 2192 ? 1_555 166.5 ? 
34  O2P ? I  TPO .   ? A TPO 500  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 O   ? Z  HOH .   ? A HOH 2192 ? 1_555 87.7  ? 
35  O   ? Z  HOH .   ? A HOH 2184 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 89.5  ? 
36  OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 74.8  ? 
37  O2P ? I  TPO .   ? A TPO 500  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 91.1  ? 
38  O   ? Z  HOH .   ? A HOH 2192 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 118.7 ? 
39  O   ? Z  HOH .   ? A HOH 2184 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD2 ? A  ASP 138 ? A ASP 138  ? 1_555 76.2  ? 
40  OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD2 ? A  ASP 138 ? A ASP 138  ? 1_555 120.7 ? 
41  O2P ? I  TPO .   ? A TPO 500  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD2 ? A  ASP 138 ? A ASP 138  ? 1_555 106.8 ? 
42  O   ? Z  HOH .   ? A HOH 2192 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD2 ? A  ASP 138 ? A ASP 138  ? 1_555 72.2  ? 
43  OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OD2 ? A  ASP 138 ? A ASP 138  ? 1_555 49.7  ? 
44  O   ? Z  HOH .   ? A HOH 2184 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLN 148 ? A GLN 148  ? 1_555 86.3  ? 
45  OE1 ? A  GLU 136 ? A GLU 136  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLN 148 ? A GLN 148  ? 1_555 84.4  ? 
46  O2P ? I  TPO .   ? A TPO 500  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLN 148 ? A GLN 148  ? 1_555 91.9  ? 
47  O   ? Z  HOH .   ? A HOH 2192 ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLN 148 ? A GLN 148  ? 1_555 82.1  ? 
48  OD1 ? A  ASP 138 ? A ASP 138  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLN 148 ? A GLN 148  ? 1_555 159.1 ? 
49  OD2 ? A  ASP 138 ? A ASP 138  ? 1_555 CA ? G CA . ? A CA 206 ? 1_555 OE1 ? A  GLN 148 ? A GLN 148  ? 1_555 147.2 ? 
50  OD2 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 119.6 ? 
51  OD2 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OE1 ? B  GLN 148 ? B GLN 148  ? 1_555 146.2 ? 
52  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OE1 ? B  GLN 148 ? B GLN 148  ? 1_555 86.1  ? 
53  OD2 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O2P ? M  TPO .   ? B TPO 500  ? 1_555 109.6 ? 
54  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O2P ? M  TPO .   ? B TPO 500  ? 1_555 91.5  ? 
55  OE1 ? B  GLN 148 ? B GLN 148  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O2P ? M  TPO .   ? B TPO 500  ? 1_555 89.6  ? 
56  OD2 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2200 ? 1_555 75.5  ? 
57  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2200 ? 1_555 164.6 ? 
58  OE1 ? B  GLN 148 ? B GLN 148  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2200 ? 1_555 78.8  ? 
59  O2P ? M  TPO .   ? B TPO 500  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2200 ? 1_555 85.4  ? 
60  OD2 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2186 ? 1_555 74.6  ? 
61  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2186 ? 1_555 85.4  ? 
62  OE1 ? B  GLN 148 ? B GLN 148  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2186 ? 1_555 87.2  ? 
63  O2P ? M  TPO .   ? B TPO 500  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2186 ? 1_555 175.7 ? 
64  O   ? AA HOH .   ? B HOH 2200 ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 O   ? AA HOH .   ? B HOH 2186 ? 1_555 96.8  ? 
65  OD2 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 50.6  ? 
66  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 73.4  ? 
67  OE1 ? B  GLN 148 ? B GLN 148  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 159.5 ? 
68  O2P ? M  TPO .   ? B TPO 500  ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 92.5  ? 
69  O   ? AA HOH .   ? B HOH 2200 ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 121.7 ? 
70  O   ? AA HOH .   ? B HOH 2186 ? 1_555 CA ? J CA . ? B CA 205 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 89.5  ? 
71  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 49.2  ? 
72  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 77.3  ? 
73  OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 76.5  ? 
74  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 145.6 ? 
75  OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 155.1 ? 
76  OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 121.3 ? 
77  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 122.1 ? 
78  OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 151.0 ? 
79  OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 74.5  ? 
80  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 50.4  ? 
81  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O1P ? M  TPO .   ? B TPO 500  ? 1_555 129.0 ? 
82  OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O1P ? M  TPO .   ? B TPO 500  ? 1_555 80.9  ? 
83  OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O1P ? M  TPO .   ? B TPO 500  ? 1_555 82.4  ? 
84  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O1P ? M  TPO .   ? B TPO 500  ? 1_555 84.3  ? 
85  OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O1P ? M  TPO .   ? B TPO 500  ? 1_555 95.8  ? 
86  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 98.0  ? 
87  OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 88.0  ? 
88  OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 162.9 ? 
89  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 71.6  ? 
90  OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 120.9 ? 
91  O1P ? M  TPO .   ? B TPO 500  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 88.2  ? 
92  OD1 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 69.8  ? 
93  OD2 ? B  ASP 58  ? B ASP 58   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 115.4 ? 
94  OD1 ? B  ASN 59  ? B ASN 59   ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 112.1 ? 
95  OE1 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 76.1  ? 
96  OE2 ? B  GLU 136 ? B GLU 136  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 75.8  ? 
97  O1P ? M  TPO .   ? B TPO 500  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 159.7 ? 
98  OD1 ? B  ASP 138 ? B ASP 138  ? 1_555 CA ? K CA . ? B CA 206 ? 1_555 O   ? B  GLN 137 ? B GLN 137  ? 1_555 80.8  ? 
99  OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 50.3  ? 
100 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 O   ? C  GLN 137 ? C GLN 137  ? 1_555 75.3  ? 
101 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 O   ? C  GLN 137 ? C GLN 137  ? 1_555 74.6  ? 
102 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 74.1  ? 
103 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 123.0 ? 
104 O   ? C  GLN 137 ? C GLN 137  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 81.0  ? 
105 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 86.1  ? 
106 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 100.3 ? 
107 O   ? C  GLN 137 ? C GLN 137  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 159.5 ? 
108 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 85.6  ? 
109 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 143.4 ? 
110 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 119.7 ? 
111 O   ? C  GLN 137 ? C GLN 137  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 68.2  ? 
112 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 96.2  ? 
113 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 129.1 ? 
114 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 158.6 ? 
115 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 149.4 ? 
116 O   ? C  GLN 137 ? C GLN 137  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 113.3 ? 
117 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 87.6  ? 
118 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 81.4  ? 
119 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 48.0  ? 
120 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 122.4 ? 
121 OE2 ? C  GLU 136 ? C GLU 136  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 76.7  ? 
122 O   ? C  GLN 137 ? C GLN 137  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 114.8 ? 
123 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 158.7 ? 
124 O1P ? Q  TPO .   ? C TPO 500  ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 82.4  ? 
125 OD1 ? C  ASP 58  ? C ASP 58   ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 78.0  ? 
126 OD2 ? C  ASP 58  ? C ASP 58   ? 1_555 CA ? N CA . ? C CA 205 ? 1_555 OD1 ? C  ASN 59  ? C ASN 59   ? 1_555 73.2  ? 
127 OE1 ? C  GLN 148 ? C GLN 148  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 O   ? BA HOH .   ? C HOH 2190 ? 1_555 88.9  ? 
128 OE1 ? C  GLN 148 ? C GLN 148  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 O   ? BA HOH .   ? C HOH 2199 ? 1_555 78.3  ? 
129 O   ? BA HOH .   ? C HOH 2190 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 O   ? BA HOH .   ? C HOH 2199 ? 1_555 98.1  ? 
130 OE1 ? C  GLN 148 ? C GLN 148  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 O2P ? Q  TPO .   ? C TPO 500  ? 1_555 90.9  ? 
131 O   ? BA HOH .   ? C HOH 2190 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 O2P ? Q  TPO .   ? C TPO 500  ? 1_555 176.5 ? 
132 O   ? BA HOH .   ? C HOH 2199 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 O2P ? Q  TPO .   ? C TPO 500  ? 1_555 85.3  ? 
133 OE1 ? C  GLN 148 ? C GLN 148  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD2 ? C  ASP 138 ? C ASP 138  ? 1_555 145.3 ? 
134 O   ? BA HOH .   ? C HOH 2190 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD2 ? C  ASP 138 ? C ASP 138  ? 1_555 73.6  ? 
135 O   ? BA HOH .   ? C HOH 2199 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD2 ? C  ASP 138 ? C ASP 138  ? 1_555 75.1  ? 
136 O2P ? Q  TPO .   ? C TPO 500  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD2 ? C  ASP 138 ? C ASP 138  ? 1_555 108.3 ? 
137 OE1 ? C  GLN 148 ? C GLN 148  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 161.7 ? 
138 O   ? BA HOH .   ? C HOH 2190 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 88.3  ? 
139 O   ? BA HOH .   ? C HOH 2199 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 120.1 ? 
140 O2P ? Q  TPO .   ? C TPO 500  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 90.8  ? 
141 OD2 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 49.8  ? 
142 OE1 ? C  GLN 148 ? C GLN 148  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 86.5  ? 
143 O   ? BA HOH .   ? C HOH 2190 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 86.4  ? 
144 O   ? BA HOH .   ? C HOH 2199 ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 164.0 ? 
145 O2P ? Q  TPO .   ? C TPO 500  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 90.0  ? 
146 OD2 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 120.9 ? 
147 OD1 ? C  ASP 138 ? C ASP 138  ? 1_555 CA ? O CA . ? C CA 206 ? 1_555 OE1 ? C  GLU 136 ? C GLU 136  ? 1_555 75.3  ? 
148 O   ? CA HOH .   ? D HOH 2176 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 O   ? CA HOH .   ? D HOH 2190 ? 1_555 96.9  ? 
149 O   ? CA HOH .   ? D HOH 2176 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OD2 ? D  ASP 138 ? D ASP 138  ? 1_555 76.5  ? 
150 O   ? CA HOH .   ? D HOH 2190 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OD2 ? D  ASP 138 ? D ASP 138  ? 1_555 75.8  ? 
151 O   ? CA HOH .   ? D HOH 2176 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 91.9  ? 
152 O   ? CA HOH .   ? D HOH 2190 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 120.4 ? 
153 OD2 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 49.4  ? 
154 O   ? CA HOH .   ? D HOH 2176 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 O2P ? U  TPO .   ? D TPO 500  ? 1_555 173.1 ? 
155 O   ? CA HOH .   ? D HOH 2190 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 O2P ? U  TPO .   ? D TPO 500  ? 1_555 85.8  ? 
156 OD2 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 O2P ? U  TPO .   ? D TPO 500  ? 1_555 110.3 ? 
157 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 O2P ? U  TPO .   ? D TPO 500  ? 1_555 92.3  ? 
158 O   ? CA HOH .   ? D HOH 2176 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLN 148 ? D GLN 148  ? 1_555 87.3  ? 
159 O   ? CA HOH .   ? D HOH 2190 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLN 148 ? D GLN 148  ? 1_555 78.8  ? 
160 OD2 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLN 148 ? D GLN 148  ? 1_555 147.8 ? 
161 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLN 148 ? D GLN 148  ? 1_555 160.8 ? 
162 O2P ? U  TPO .   ? D TPO 500  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLN 148 ? D GLN 148  ? 1_555 87.0  ? 
163 O   ? CA HOH .   ? D HOH 2176 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 85.0  ? 
164 O   ? CA HOH .   ? D HOH 2190 ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 165.3 ? 
165 OD2 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 118.7 ? 
166 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 74.0  ? 
167 O2P ? U  TPO .   ? D TPO 500  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 90.8  ? 
168 OE1 ? D  GLN 148 ? D GLN 148  ? 1_555 CA ? R CA . ? D CA 205 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 86.8  ? 
169 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 O   ? D  GLN 137 ? D GLN 137  ? 1_555 70.1  ? 
170 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 95.2  ? 
171 O   ? D  GLN 137 ? D GLN 137  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 81.5  ? 
172 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 O1P ? U  TPO .   ? D TPO 500  ? 1_555 129.7 ? 
173 O   ? D  GLN 137 ? D GLN 137  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 O1P ? U  TPO .   ? D TPO 500  ? 1_555 158.9 ? 
174 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 O1P ? U  TPO .   ? D TPO 500  ? 1_555 88.6  ? 
175 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 50.4  ? 
176 O   ? D  GLN 137 ? D GLN 137  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 118.8 ? 
177 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 90.1  ? 
178 O1P ? U  TPO .   ? D TPO 500  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 79.5  ? 
179 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 144.2 ? 
180 O   ? D  GLN 137 ? D GLN 137  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 74.6  ? 
181 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 73.8  ? 
182 O1P ? U  TPO .   ? D TPO 500  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 84.9  ? 
183 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 157.8 ? 
184 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 123.4 ? 
185 O   ? D  GLN 137 ? D GLN 137  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 76.3  ? 
186 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 123.4 ? 
187 O1P ? U  TPO .   ? D TPO 500  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 94.2  ? 
188 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 146.0 ? 
189 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 50.3  ? 
190 OD1 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 81.2  ? 
191 O   ? D  GLN 137 ? D GLN 137  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 112.4 ? 
192 OD1 ? D  ASP 138 ? D ASP 138  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 163.0 ? 
193 O1P ? U  TPO .   ? D TPO 500  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 81.2  ? 
194 OD2 ? D  ASP 58  ? D ASP 58   ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 74.8  ? 
195 OE1 ? D  GLU 136 ? D GLU 136  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 118.3 ? 
196 OE2 ? D  GLU 136 ? D GLU 136  ? 1_555 CA ? S CA . ? D CA 206 ? 1_555 OD1 ? D  ASN 59  ? D ASN 59   ? 1_555 71.2  ? 
197 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 49.5  ? 
198 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 129.8 ? 
199 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 82.8  ? 
200 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 99.0  ? 
201 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 83.5  ? 
202 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 88.2  ? 
203 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 O   ? E  GLN 137 ? E GLN 137  ? 1_555 68.5  ? 
204 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 O   ? E  GLN 137 ? E GLN 137  ? 1_555 112.1 ? 
205 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 O   ? E  GLN 137 ? E GLN 137  ? 1_555 160.5 ? 
206 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 O   ? E  GLN 137 ? E GLN 137  ? 1_555 81.3  ? 
207 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 118.6 ? 
208 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 154.2 ? 
209 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 97.3  ? 
210 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 122.3 ? 
211 O   ? E  GLN 137 ? E GLN 137  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 75.0  ? 
212 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 144.4 ? 
213 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 153.9 ? 
214 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 85.3  ? 
215 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 73.1  ? 
216 O   ? E  GLN 137 ? E GLN 137  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 76.0  ? 
217 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 50.6  ? 
218 OD1 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 76.6  ? 
219 OD2 ? E  ASP 58  ? E ASP 58   ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 81.4  ? 
220 O1P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 82.7  ? 
221 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 163.2 ? 
222 O   ? E  GLN 137 ? E GLN 137  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 111.3 ? 
223 OE2 ? E  GLU 136 ? E GLU 136  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 73.1  ? 
224 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 CA ? V CA . ? E CA 205 ? 1_555 OD1 ? E  ASN 59  ? E ASN 59   ? 1_555 119.9 ? 
225 O   ? DA HOH .   ? E HOH 2188 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 O   ? DA HOH .   ? E HOH 2201 ? 1_555 97.5  ? 
226 O   ? DA HOH .   ? E HOH 2188 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 O2P ? Y  TPO .   ? E TPO 500  ? 1_555 175.5 ? 
227 O   ? DA HOH .   ? E HOH 2201 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 O2P ? Y  TPO .   ? E TPO 500  ? 1_555 84.3  ? 
228 O   ? DA HOH .   ? E HOH 2188 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD2 ? E  ASP 138 ? E ASP 138  ? 1_555 76.1  ? 
229 O   ? DA HOH .   ? E HOH 2201 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD2 ? E  ASP 138 ? E ASP 138  ? 1_555 77.0  ? 
230 O2P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD2 ? E  ASP 138 ? E ASP 138  ? 1_555 108.4 ? 
231 O   ? DA HOH .   ? E HOH 2188 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 90.2  ? 
232 O   ? DA HOH .   ? E HOH 2201 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 122.4 ? 
233 O2P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 92.4  ? 
234 OD2 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 49.7  ? 
235 O   ? DA HOH .   ? E HOH 2188 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 84.0  ? 
236 O   ? DA HOH .   ? E HOH 2201 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 164.6 ? 
237 O2P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 93.2  ? 
238 OD2 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 118.1 ? 
239 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 72.9  ? 
240 O   ? DA HOH .   ? E HOH 2188 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLN 148 ? E GLN 148  ? 1_555 85.1  ? 
241 O   ? DA HOH .   ? E HOH 2201 ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLN 148 ? E GLN 148  ? 1_555 79.8  ? 
242 O2P ? Y  TPO .   ? E TPO 500  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLN 148 ? E GLN 148  ? 1_555 91.1  ? 
243 OD2 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLN 148 ? E GLN 148  ? 1_555 147.7 ? 
244 OD1 ? E  ASP 138 ? E ASP 138  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLN 148 ? E GLN 148  ? 1_555 157.8 ? 
245 OE1 ? E  GLU 136 ? E GLU 136  ? 1_555 CA ? W CA . ? E CA 206 ? 1_555 OE1 ? E  GLN 148 ? E GLN 148  ? 1_555 85.1  ? 
# 
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 2009-04-14 
2 'Structure model' 1 1 2011-05-07 
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 
PHENIX refinement       '(PHENIX.REFINE)' ? 1 
MOSFLM 'data reduction' .                 ? 2 
SCALA  'data scaling'   .                 ? 3 
MOLREP phasing          .                 ? 4 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;
SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.
;
# 
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 ARG A 77  ? ? 82.31   -17.74 
2  1 ALA A 187 ? ? -157.23 64.54  
3  1 ARG B 77  ? ? 74.36   -18.07 
4  1 ASP B 161 ? ? -89.52  30.68  
5  1 ALA B 187 ? ? -154.66 65.23  
6  1 ARG C 77  ? ? 81.17   -21.70 
7  1 ALA C 187 ? ? -155.06 71.72  
8  1 ARG D 77  ? ? 76.91   -16.66 
9  1 ALA D 187 ? ? -152.37 64.83  
10 1 ARG E 77  ? A 81.25   -22.45 
11 1 ARG E 77  ? B 83.68   -29.39 
12 1 ASP E 161 ? ? -89.44  31.68  
13 1 THR E 176 ? ? -119.92 58.15  
14 1 ALA E 187 ? ? -154.17 65.04  
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1  1 C1 ? A NAG 207 ? 'WRONG HAND' . 
2  1 C2 ? A NAG 207 ? 'WRONG HAND' . 
3  1 C3 ? A NAG 207 ? 'WRONG HAND' . 
4  1 C5 ? A NAG 207 ? 'WRONG HAND' . 
5  1 C2 ? B NAG 207 ? 'WRONG HAND' . 
6  1 C3 ? B NAG 207 ? 'WRONG HAND' . 
7  1 C5 ? B NAG 207 ? 'WRONG HAND' . 
8  1 C1 ? C NAG 207 ? PLANAR       . 
9  1 C2 ? C NAG 207 ? 'WRONG HAND' . 
10 1 C3 ? C NAG 207 ? 'WRONG HAND' . 
11 1 C5 ? C NAG 207 ? 'WRONG HAND' . 
12 1 C1 ? D NAG 207 ? PLANAR       . 
13 1 C2 ? D NAG 207 ? 'WRONG HAND' . 
14 1 C3 ? D NAG 207 ? 'WRONG HAND' . 
15 1 C5 ? D NAG 207 ? 'WRONG HAND' . 
16 1 C1 ? E NAG 207 ? 'WRONG HAND' . 
17 1 C2 ? E NAG 207 ? 'WRONG HAND' . 
18 1 C3 ? E NAG 207 ? 'WRONG HAND' . 
19 1 C5 ? E NAG 207 ? 'WRONG HAND' . 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'          CA  
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 PHOSPHOTHREONINE       TPO 
5 water                  HOH 
# 
