data_5NI1
# 
_entry.id   5NI1 
# 
_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   5NI1         
WWPDB D_1200004172 
EMDB  EMD-3488     
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2017-04-12 
_pdbx_database_PDB_obs_spr.pdb_id           5NI1 
_pdbx_database_PDB_obs_spr.replace_pdb_id   5ME2 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          EMD-3488 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5NI1 
_pdbx_database_status.recvd_initial_deposition_date   2017-03-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Khoshouei, M.'  1 ? 
'Radjainia, M.'  2 ? 
'Bunker, R.'     3 ? 
'Baumeister, W.' 4 ? 
'Danev, R.'      5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Elife 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2050-084X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            5 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cryo-EM single particle analysis with the Volta phase plate.' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.7554/eLife.13046 
_citation.pdbx_database_id_PubMed   26949259 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Danev, R.'      1 
primary 'Baumeister, W.' 2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5NI1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.000 
_cell.length_a_esd                 ? 
_cell.length_b                     1.000 
_cell.length_b_esd                 ? 
_cell.length_c                     1.000 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5NI1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hemoglobin subunit alpha'        15150.353 2  ? ? ? ? 
2 polymer     man 'Hemoglobin subunit beta'         15890.198 2  ? ? ? ? 
3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   4  ? ? ? ? 
4 water       nat water                             18.015    24 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Alpha-globin,Hemoglobin alpha chain' 
2 'Beta-globin,Hemoglobin beta chain'   
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
;
;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
;
A,C ? 
2 'polypeptide(L)' no no 
;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
;
;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
;
B,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   LEU n 
1 3   SER n 
1 4   PRO n 
1 5   ALA n 
1 6   ASP n 
1 7   LYS n 
1 8   THR n 
1 9   ASN n 
1 10  VAL n 
1 11  LYS n 
1 12  ALA n 
1 13  ALA n 
1 14  TRP n 
1 15  GLY n 
1 16  LYS n 
1 17  VAL n 
1 18  GLY n 
1 19  ALA n 
1 20  HIS n 
1 21  ALA n 
1 22  GLY n 
1 23  GLU n 
1 24  TYR n 
1 25  GLY n 
1 26  ALA n 
1 27  GLU n 
1 28  ALA n 
1 29  LEU n 
1 30  GLU n 
1 31  ARG n 
1 32  MET n 
1 33  PHE n 
1 34  LEU n 
1 35  SER n 
1 36  PHE n 
1 37  PRO n 
1 38  THR n 
1 39  THR n 
1 40  LYS n 
1 41  THR n 
1 42  TYR n 
1 43  PHE n 
1 44  PRO n 
1 45  HIS n 
1 46  PHE n 
1 47  ASP n 
1 48  LEU n 
1 49  SER n 
1 50  HIS n 
1 51  GLY n 
1 52  SER n 
1 53  ALA n 
1 54  GLN n 
1 55  VAL n 
1 56  LYS n 
1 57  GLY n 
1 58  HIS n 
1 59  GLY n 
1 60  LYS n 
1 61  LYS n 
1 62  VAL n 
1 63  ALA n 
1 64  ASP n 
1 65  ALA n 
1 66  LEU n 
1 67  THR n 
1 68  ASN n 
1 69  ALA n 
1 70  VAL n 
1 71  ALA n 
1 72  HIS n 
1 73  VAL n 
1 74  ASP n 
1 75  ASP n 
1 76  MET n 
1 77  PRO n 
1 78  ASN n 
1 79  ALA n 
1 80  LEU n 
1 81  SER n 
1 82  ALA n 
1 83  LEU n 
1 84  SER n 
1 85  ASP n 
1 86  LEU n 
1 87  HIS n 
1 88  ALA n 
1 89  HIS n 
1 90  LYS n 
1 91  LEU n 
1 92  ARG n 
1 93  VAL n 
1 94  ASP n 
1 95  PRO n 
1 96  VAL n 
1 97  ASN n 
1 98  PHE n 
1 99  LYS n 
1 100 LEU n 
1 101 LEU n 
1 102 SER n 
1 103 HIS n 
1 104 CYS n 
1 105 LEU n 
1 106 LEU n 
1 107 VAL n 
1 108 THR n 
1 109 LEU n 
1 110 ALA n 
1 111 ALA n 
1 112 HIS n 
1 113 LEU n 
1 114 PRO n 
1 115 ALA n 
1 116 GLU n 
1 117 PHE n 
1 118 THR n 
1 119 PRO n 
1 120 ALA n 
1 121 VAL n 
1 122 HIS n 
1 123 ALA n 
1 124 SER n 
1 125 LEU n 
1 126 ASP n 
1 127 LYS n 
1 128 PHE n 
1 129 LEU n 
1 130 ALA n 
1 131 SER n 
1 132 VAL n 
1 133 SER n 
1 134 THR n 
1 135 VAL n 
1 136 LEU n 
1 137 THR n 
1 138 SER n 
1 139 LYS n 
1 140 TYR n 
1 141 ARG n 
2 1   VAL n 
2 2   HIS n 
2 3   LEU n 
2 4   THR n 
2 5   PRO n 
2 6   GLU n 
2 7   GLU n 
2 8   LYS n 
2 9   SER n 
2 10  ALA n 
2 11  VAL n 
2 12  THR n 
2 13  ALA n 
2 14  LEU n 
2 15  TRP n 
2 16  GLY n 
2 17  LYS n 
2 18  VAL n 
2 19  ASN n 
2 20  VAL n 
2 21  ASP n 
2 22  GLU n 
2 23  VAL n 
2 24  GLY n 
2 25  GLY n 
2 26  GLU n 
2 27  ALA n 
2 28  LEU n 
2 29  GLY n 
2 30  ARG n 
2 31  LEU n 
2 32  LEU n 
2 33  VAL n 
2 34  VAL n 
2 35  TYR n 
2 36  PRO n 
2 37  TRP n 
2 38  THR n 
2 39  GLN n 
2 40  ARG n 
2 41  PHE n 
2 42  PHE n 
2 43  GLU n 
2 44  SER n 
2 45  PHE n 
2 46  GLY n 
2 47  ASP n 
2 48  LEU n 
2 49  SER n 
2 50  THR n 
2 51  PRO n 
2 52  ASP n 
2 53  ALA n 
2 54  VAL n 
2 55  MET n 
2 56  GLY n 
2 57  ASN n 
2 58  PRO n 
2 59  LYS n 
2 60  VAL n 
2 61  LYS n 
2 62  ALA n 
2 63  HIS n 
2 64  GLY n 
2 65  LYS n 
2 66  LYS n 
2 67  VAL n 
2 68  LEU n 
2 69  GLY n 
2 70  ALA n 
2 71  PHE n 
2 72  SER n 
2 73  ASP n 
2 74  GLY n 
2 75  LEU n 
2 76  ALA n 
2 77  HIS n 
2 78  LEU n 
2 79  ASP n 
2 80  ASN n 
2 81  LEU n 
2 82  LYS n 
2 83  GLY n 
2 84  THR n 
2 85  PHE n 
2 86  ALA n 
2 87  THR n 
2 88  LEU n 
2 89  SER n 
2 90  GLU n 
2 91  LEU n 
2 92  HIS n 
2 93  CYS n 
2 94  ASP n 
2 95  LYS n 
2 96  LEU n 
2 97  HIS n 
2 98  VAL n 
2 99  ASP n 
2 100 PRO n 
2 101 GLU n 
2 102 ASN n 
2 103 PHE n 
2 104 ARG n 
2 105 LEU n 
2 106 LEU n 
2 107 GLY n 
2 108 ASN n 
2 109 VAL n 
2 110 LEU n 
2 111 VAL n 
2 112 CYS n 
2 113 VAL n 
2 114 LEU n 
2 115 ALA n 
2 116 HIS n 
2 117 HIS n 
2 118 PHE n 
2 119 GLY n 
2 120 LYS n 
2 121 GLU n 
2 122 PHE n 
2 123 THR n 
2 124 PRO n 
2 125 PRO n 
2 126 VAL n 
2 127 GLN n 
2 128 ALA n 
2 129 ALA n 
2 130 TYR n 
2 131 GLN n 
2 132 LYS n 
2 133 VAL n 
2 134 VAL n 
2 135 ALA n 
2 136 GLY n 
2 137 VAL n 
2 138 ALA n 
2 139 ASN n 
2 140 ALA n 
2 141 LEU n 
2 142 ALA n 
2 143 HIS n 
2 144 LYS n 
2 145 TYR n 
2 146 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 141 Human ? 'HBA1, HBA2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 146 Human ? HBB          ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP HBA_HUMAN P69905 ? 1 
;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
;
2 
2 UNP HBB_HUMAN P68871 ? 2 
;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
;
2 
# 
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 5NI1 A 1 ? 141 ? P69905 2 ? 142 ? 1 141 
2 2 5NI1 B 1 ? 146 ? P68871 2 ? 147 ? 1 146 
3 1 5NI1 C 1 ? 141 ? P69905 2 ? 142 ? 1 141 
4 2 5NI1 D 1 ? 146 ? P68871 2 ? 147 ? 1 146 
# 
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 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                         ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ?    'H2 O'             18.015  
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 
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5NI1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
loop_
_refine.aniso_B[1][1] 
_refine.aniso_B[1][2] 
_refine.aniso_B[1][3] 
_refine.aniso_B[2][2] 
_refine.aniso_B[2][3] 
_refine.aniso_B[3][3] 
_refine.B_iso_max 
_refine.B_iso_mean 
_refine.B_iso_min 
_refine.correlation_coeff_Fo_to_Fc 
_refine.correlation_coeff_Fo_to_Fc_free 
_refine.details 
_refine.diff_density_max 
_refine.diff_density_max_esd 
_refine.diff_density_min 
_refine.diff_density_min_esd 
_refine.diff_density_rms 
_refine.diff_density_rms_esd 
_refine.entry_id 
_refine.pdbx_refine_id 
_refine.ls_abs_structure_details 
_refine.ls_abs_structure_Flack 
_refine.ls_abs_structure_Flack_esd 
_refine.ls_abs_structure_Rogers 
_refine.ls_abs_structure_Rogers_esd 
_refine.ls_d_res_high 
_refine.ls_d_res_low 
_refine.ls_extinction_coef 
_refine.ls_extinction_coef_esd 
_refine.ls_extinction_expression 
_refine.ls_extinction_method 
_refine.ls_goodness_of_fit_all 
_refine.ls_goodness_of_fit_all_esd 
_refine.ls_goodness_of_fit_obs 
_refine.ls_goodness_of_fit_obs_esd 
_refine.ls_hydrogen_treatment 
_refine.ls_matrix_type 
_refine.ls_number_constraints 
_refine.ls_number_parameters 
_refine.ls_number_reflns_all 
_refine.ls_number_reflns_obs 
_refine.ls_number_reflns_R_free 
_refine.ls_number_reflns_R_work 
_refine.ls_number_restraints 
_refine.ls_percent_reflns_obs 
_refine.ls_percent_reflns_R_free 
_refine.ls_R_factor_all 
_refine.ls_R_factor_obs 
_refine.ls_R_factor_R_free 
_refine.ls_R_factor_R_free_error 
_refine.ls_R_factor_R_free_error_details 
_refine.ls_R_factor_R_work 
_refine.ls_R_Fsqd_factor_obs 
_refine.ls_R_I_factor_obs 
_refine.ls_redundancy_reflns_all 
_refine.ls_redundancy_reflns_obs 
_refine.ls_restrained_S_all 
_refine.ls_restrained_S_obs 
_refine.ls_shift_over_esd_max 
_refine.ls_shift_over_esd_mean 
_refine.ls_structure_factor_coef 
_refine.ls_weighting_details 
_refine.ls_weighting_scheme 
_refine.ls_wR_factor_all 
_refine.ls_wR_factor_obs 
_refine.ls_wR_factor_R_free 
_refine.ls_wR_factor_R_work 
_refine.occupancy_max 
_refine.occupancy_min 
_refine.solvent_model_details 
_refine.solvent_model_param_bsol 
_refine.solvent_model_param_ksol 
_refine.ls_R_factor_gt 
_refine.ls_goodness_of_fit_gt 
_refine.ls_goodness_of_fit_ref 
_refine.ls_shift_over_su_max 
_refine.ls_shift_over_su_max_lt 
_refine.ls_shift_over_su_mean 
_refine.ls_shift_over_su_mean_lt 
_refine.pdbx_ls_sigma_I 
_refine.pdbx_ls_sigma_F 
_refine.pdbx_ls_sigma_Fsqd 
_refine.pdbx_data_cutoff_high_absF 
_refine.pdbx_data_cutoff_high_rms_absF 
_refine.pdbx_data_cutoff_low_absF 
_refine.pdbx_isotropic_thermal_model 
_refine.pdbx_ls_cross_valid_method 
_refine.pdbx_method_to_determine_struct 
_refine.pdbx_starting_model 
_refine.pdbx_stereochemistry_target_values 
_refine.pdbx_R_Free_selection_details 
_refine.pdbx_stereochem_target_val_spec_case 
_refine.pdbx_overall_ESU_R 
_refine.pdbx_overall_ESU_R_Free 
_refine.pdbx_solvent_vdw_probe_radii 
_refine.pdbx_solvent_ion_probe_radii 
_refine.pdbx_solvent_shrinkage_radii 
_refine.pdbx_real_space_R 
_refine.pdbx_density_correlation 
_refine.pdbx_pd_number_of_powder_patterns 
_refine.pdbx_pd_number_of_points 
_refine.pdbx_pd_meas_number_of_points 
_refine.pdbx_pd_proc_ls_prof_R_factor 
_refine.pdbx_pd_proc_ls_prof_wR_factor 
_refine.pdbx_pd_Marquardt_correlation_coeff 
_refine.pdbx_pd_Fsqrd_R_factor 
_refine.pdbx_pd_ls_matrix_band_width 
_refine.pdbx_overall_phase_error 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI 
_refine.pdbx_overall_SU_R_free_Blow_DPI 
_refine.pdbx_overall_SU_R_Blow_DPI 
_refine.pdbx_TLS_residual_ADP_flag 
_refine.pdbx_diffrn_id 
_refine.overall_SU_B 
_refine.overall_SU_ML 
_refine.overall_SU_R_Cruickshank_DPI 
_refine.overall_SU_R_free 
_refine.overall_FOM_free_R_set 
_refine.overall_FOM_work_R_set 
_refine.pdbx_average_fsc_overall 
_refine.pdbx_average_fsc_work 
_refine.pdbx_average_fsc_free 
-1.39 -1.67 -0.01 0.67 -0.01 0.72 ? 60.032 ? 0.574 ? 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' ? ? ? ? ? ? 5NI1 1 ? ? ? 
? ? 3.20 105.00 ? ? ? ? ? ? ? ? ? ? ? ? ? 74004 ? ? ? 100.00 ? ? 0.37077 ? ? ? 0.37077 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
'PARAMETERS FOR MASK CACLULATION' ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 'MAXIMUM LIKELIHOOD WITH PHASES' ? ? 0.340 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? 18.168 0.278 ? ? ? ? ? ? ? 
?     ?     ?     ?    ?     ?    ? ?      ? ?     ? ?                                                   ? ? ? ? ? ? 5NI1 
'ELECTRON MICROSCOPY' ? ? ? ? ? .    ?      ? ? ? ? ? ? ? ? ? ? ? ? ? ?     ? ? ? ?      ? ? ?       ? ? ? ?       ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ?                                 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?                                ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?      ?     ? ? ? ? ? ? ? 
# 
_refine_hist.pdbx_refine_id                   'ELECTRON MICROSCOPY' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        ? 
_refine_hist.pdbx_number_atoms_nucleic_acid   ? 
_refine_hist.pdbx_number_atoms_ligand         ? 
_refine_hist.number_atoms_solvent             ? 
_refine_hist.number_atoms_total               4580 
_refine_hist.d_res_high                       . 
_refine_hist.d_res_low                        . 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.010  0.019  4703  ? r_bond_refined_d             ? ? 
'ELECTRON MICROSCOPY' ? 0.002  0.020  4331  ? r_bond_other_d               ? ? 
'ELECTRON MICROSCOPY' ? 1.532  2.000  6449  ? r_angle_refined_deg          ? ? 
'ELECTRON MICROSCOPY' ? 1.296  3.000  10003 ? r_angle_other_deg            ? ? 
'ELECTRON MICROSCOPY' ? 5.712  5.000  570   ? r_dihedral_angle_1_deg       ? ? 
'ELECTRON MICROSCOPY' ? 33.077 23.889 180   ? r_dihedral_angle_2_deg       ? ? 
'ELECTRON MICROSCOPY' ? 12.446 15.000 705   ? r_dihedral_angle_3_deg       ? ? 
'ELECTRON MICROSCOPY' ? 11.357 15.000 12    ? r_dihedral_angle_4_deg       ? ? 
'ELECTRON MICROSCOPY' ? 0.104  0.200  708   ? r_chiral_restr               ? ? 
'ELECTRON MICROSCOPY' ? 0.006  0.021  5272  ? r_gen_planes_refined         ? ? 
'ELECTRON MICROSCOPY' ? 0.003  0.020  984   ? r_gen_planes_other           ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'ELECTRON MICROSCOPY' ? 5.564  5.685  2292  ? r_mcbond_it                  ? ? 
'ELECTRON MICROSCOPY' ? 5.520  5.673  2291  ? r_mcbond_other               ? ? 
'ELECTRON MICROSCOPY' ? 9.818  8.484  2858  ? r_mcangle_it                 ? ? 
'ELECTRON MICROSCOPY' ? 9.833  8.496  2859  ? r_mcangle_other              ? ? 
'ELECTRON MICROSCOPY' ? 7.102  6.495  2411  ? r_scbond_it                  ? ? 
'ELECTRON MICROSCOPY' ? 7.091  6.492  2409  ? r_scbond_other               ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'ELECTRON MICROSCOPY' ? 12.743 9.252  3591  ? r_scangle_other              ? ? 
'ELECTRON MICROSCOPY' ? 18.717 64.935 5272  ? r_long_range_B_refined       ? ? 
'ELECTRON MICROSCOPY' ? 18.721 64.943 5273  ? r_long_range_B_other         ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_type 
'ELECTRON MICROSCOPY' 1 1 1 ? 0.34 0.50 ? ? A 1068 'tight thermal' 
'ELECTRON MICROSCOPY' 2 2 2 ? 0.12 0.50 ? ? B 1123 'tight thermal' 
# 
_refine_ls_shell.pdbx_refine_id                   'ELECTRON MICROSCOPY' 
_refine_ls_shell.d_res_high                       3.200 
_refine_ls_shell.d_res_low                        3.283 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             0 
_refine_ls_shell.number_reflns_R_work             5475 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.965 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? 1.000000  0.000000  0.000000  0.000000 1.000000  0.000000  0.000000  0.000000  1.000000 0.00000   0.00000   0.00000 
2 given ? -1.000000 -0.000463 -0.000170 0.000463 -1.000000 -0.000505 -0.000170 -0.000505 1.000000 105.04034 105.01142 0.03988 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 A 1 
2 C 1 
1 B 2 
2 D 2 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1 A 1 A 141 1 1 ? ? ? ? ? ? ? ? 1 ? 
2 C 1 C 141 1 1 ? ? ? ? ? ? ? ? 1 ? 
1 B 1 B 146 1 1 ? ? ? ? ? ? ? ? 2 ? 
2 D 1 D 146 1 1 ? ? ? ? ? ? ? ? 2 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
# 
_struct.entry_id                     5NI1 
_struct.title                        'CryoEM structure of haemoglobin at 3.2 A determined with the Volta phase plate' 
_struct.pdbx_descriptor              'Hemoglobin subunit alpha, Hemoglobin subunit beta' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5NI1 
_struct_keywords.text            'Volta phase plate, Single particle analysis, Hemoglobin, oxygen transport' 
_struct_keywords.pdbx_keywords   'OXYGEN TRANSPORT' 
# 
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 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
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  AA1 SER A 3   ? GLY A 18  ? SER A 3   GLY A 18  1 ? 16 
HELX_P HELX_P2  AA2 HIS A 20  ? PHE A 36  ? HIS A 20  PHE A 36  1 ? 17 
HELX_P HELX_P3  AA3 PRO A 37  ? PHE A 43  ? PRO A 37  PHE A 43  5 ? 7  
HELX_P HELX_P4  AA4 SER A 52  ? HIS A 72  ? SER A 52  HIS A 72  1 ? 21 
HELX_P HELX_P5  AA5 ASP A 75  ? LEU A 80  ? ASP A 75  LEU A 80  1 ? 6  
HELX_P HELX_P6  AA6 LEU A 80  ? HIS A 89  ? LEU A 80  HIS A 89  1 ? 10 
HELX_P HELX_P7  AA7 ASP A 94  ? VAL A 96  ? ASP A 94  VAL A 96  5 ? 3  
HELX_P HELX_P8  AA8 ASN A 97  ? ALA A 111 ? ASN A 97  ALA A 111 1 ? 15 
HELX_P HELX_P9  AA9 THR A 118 ? THR A 137 ? THR A 118 THR A 137 1 ? 20 
HELX_P HELX_P10 AB1 THR B 4   ? LYS B 17  ? THR B 4   LYS B 17  1 ? 14 
HELX_P HELX_P11 AB2 ASP B 21  ? TYR B 35  ? ASP B 21  TYR B 35  1 ? 15 
HELX_P HELX_P12 AB3 PRO B 36  ? GLY B 46  ? PRO B 36  GLY B 46  5 ? 11 
HELX_P HELX_P13 AB4 THR B 50  ? ASN B 57  ? THR B 50  ASN B 57  1 ? 8  
HELX_P HELX_P14 AB5 ASN B 57  ? HIS B 77  ? ASN B 57  HIS B 77  1 ? 21 
HELX_P HELX_P15 AB6 ASN B 80  ? PHE B 85  ? ASN B 80  PHE B 85  1 ? 6  
HELX_P HELX_P16 AB7 PHE B 85  ? LYS B 95  ? PHE B 85  LYS B 95  1 ? 11 
HELX_P HELX_P17 AB8 PRO B 100 ? GLY B 119 ? PRO B 100 GLY B 119 1 ? 20 
HELX_P HELX_P18 AB9 LYS B 120 ? PHE B 122 ? LYS B 120 PHE B 122 5 ? 3  
HELX_P HELX_P19 AC1 THR B 123 ? ALA B 142 ? THR B 123 ALA B 142 1 ? 20 
HELX_P HELX_P20 AC2 SER C 3   ? GLY C 18  ? SER C 3   GLY C 18  1 ? 16 
HELX_P HELX_P21 AC3 HIS C 20  ? PHE C 36  ? HIS C 20  PHE C 36  1 ? 17 
HELX_P HELX_P22 AC4 PRO C 37  ? PHE C 43  ? PRO C 37  PHE C 43  5 ? 7  
HELX_P HELX_P23 AC5 SER C 52  ? HIS C 72  ? SER C 52  HIS C 72  1 ? 21 
HELX_P HELX_P24 AC6 ASP C 75  ? LEU C 80  ? ASP C 75  LEU C 80  1 ? 6  
HELX_P HELX_P25 AC7 LEU C 80  ? HIS C 89  ? LEU C 80  HIS C 89  1 ? 10 
HELX_P HELX_P26 AC8 ASP C 94  ? VAL C 96  ? ASP C 94  VAL C 96  5 ? 3  
HELX_P HELX_P27 AC9 ASN C 97  ? ALA C 111 ? ASN C 97  ALA C 111 1 ? 15 
HELX_P HELX_P28 AD1 THR C 118 ? THR C 137 ? THR C 118 THR C 137 1 ? 20 
HELX_P HELX_P29 AD2 THR D 4   ? LYS D 17  ? THR D 4   LYS D 17  1 ? 14 
HELX_P HELX_P30 AD3 ASP D 21  ? TYR D 35  ? ASP D 21  TYR D 35  1 ? 15 
HELX_P HELX_P31 AD4 PRO D 36  ? GLY D 46  ? PRO D 36  GLY D 46  5 ? 11 
HELX_P HELX_P32 AD5 THR D 50  ? ASN D 57  ? THR D 50  ASN D 57  1 ? 8  
HELX_P HELX_P33 AD6 ASN D 57  ? HIS D 77  ? ASN D 57  HIS D 77  1 ? 21 
HELX_P HELX_P34 AD7 ASN D 80  ? PHE D 85  ? ASN D 80  PHE D 85  1 ? 6  
HELX_P HELX_P35 AD8 PHE D 85  ? LYS D 95  ? PHE D 85  LYS D 95  1 ? 11 
HELX_P HELX_P36 AD9 PRO D 100 ? GLY D 119 ? PRO D 100 GLY D 119 1 ? 20 
HELX_P HELX_P37 AE1 LYS D 120 ? PHE D 122 ? LYS D 120 PHE D 122 5 ? 3  
HELX_P HELX_P38 AE2 THR D 123 ? ALA D 142 ? THR D 123 ALA D 142 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1 metalc ? ? A HIS 87 NE2 ? ? ? 1_555 E HEM . FE ? ? A HIS 87 A HEM 201 1_555 ? ? ? ? ? ? ? 1.971 ? 
metalc2 metalc ? ? B HIS 92 NE2 ? ? ? 1_555 F HEM . FE ? ? B HIS 92 B HEM 201 1_555 ? ? ? ? ? ? ? 1.979 ? 
metalc3 metalc ? ? C HIS 87 NE2 ? ? ? 1_555 G HEM . FE ? ? C HIS 87 C HEM 201 1_555 ? ? ? ? ? ? ? 1.972 ? 
metalc4 metalc ? ? D HIS 92 NE2 ? ? ? 1_555 H HEM . FE ? ? D HIS 92 D HEM 201 1_555 ? ? ? ? ? ? ? 1.975 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 A HEM 201 ? 12 'binding site for residue HEM A 201' 
AC2 Software B HEM 201 ? 8  'binding site for residue HEM B 201' 
AC3 Software C HEM 201 ? 12 'binding site for residue HEM C 201' 
AC4 Software D HEM 201 ? 7  'binding site for residue HEM D 201' 
# 
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 12 THR A 39  ? THR A 39  . ? 1_555 ? 
2  AC1 12 HIS A 45  ? HIS A 45  . ? 1_555 ? 
3  AC1 12 PHE A 46  ? PHE A 46  . ? 1_555 ? 
4  AC1 12 HIS A 58  ? HIS A 58  . ? 1_555 ? 
5  AC1 12 LYS A 61  ? LYS A 61  . ? 1_555 ? 
6  AC1 12 ALA A 65  ? ALA A 65  . ? 1_555 ? 
7  AC1 12 LEU A 83  ? LEU A 83  . ? 1_555 ? 
8  AC1 12 HIS A 87  ? HIS A 87  . ? 1_555 ? 
9  AC1 12 LEU A 91  ? LEU A 91  . ? 1_555 ? 
10 AC1 12 ASN A 97  ? ASN A 97  . ? 1_555 ? 
11 AC1 12 PHE A 98  ? PHE A 98  . ? 1_555 ? 
12 AC1 12 LEU A 101 ? LEU A 101 . ? 1_555 ? 
13 AC2 8  PHE B 41  ? PHE B 41  . ? 1_555 ? 
14 AC2 8  PHE B 42  ? PHE B 42  . ? 1_555 ? 
15 AC2 8  HIS B 63  ? HIS B 63  . ? 1_555 ? 
16 AC2 8  LEU B 88  ? LEU B 88  . ? 1_555 ? 
17 AC2 8  HIS B 92  ? HIS B 92  . ? 1_555 ? 
18 AC2 8  ASN B 102 ? ASN B 102 . ? 1_555 ? 
19 AC2 8  PHE B 103 ? PHE B 103 . ? 1_555 ? 
20 AC2 8  LEU B 106 ? LEU B 106 . ? 1_555 ? 
21 AC3 12 THR C 39  ? THR C 39  . ? 1_555 ? 
22 AC3 12 HIS C 45  ? HIS C 45  . ? 1_555 ? 
23 AC3 12 PHE C 46  ? PHE C 46  . ? 1_555 ? 
24 AC3 12 HIS C 58  ? HIS C 58  . ? 1_555 ? 
25 AC3 12 LYS C 61  ? LYS C 61  . ? 1_555 ? 
26 AC3 12 ALA C 65  ? ALA C 65  . ? 1_555 ? 
27 AC3 12 LEU C 83  ? LEU C 83  . ? 1_555 ? 
28 AC3 12 HIS C 87  ? HIS C 87  . ? 1_555 ? 
29 AC3 12 LEU C 91  ? LEU C 91  . ? 1_555 ? 
30 AC3 12 ASN C 97  ? ASN C 97  . ? 1_555 ? 
31 AC3 12 PHE C 98  ? PHE C 98  . ? 1_555 ? 
32 AC3 12 LEU C 101 ? LEU C 101 . ? 1_555 ? 
33 AC4 7  PHE D 41  ? PHE D 41  . ? 1_555 ? 
34 AC4 7  PHE D 42  ? PHE D 42  . ? 1_555 ? 
35 AC4 7  HIS D 63  ? HIS D 63  . ? 1_555 ? 
36 AC4 7  LEU D 88  ? LEU D 88  . ? 1_555 ? 
37 AC4 7  HIS D 92  ? HIS D 92  . ? 1_555 ? 
38 AC4 7  ASN D 102 ? ASN D 102 . ? 1_555 ? 
39 AC4 7  PHE D 103 ? PHE D 103 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5NI1 
_atom_sites.fract_transf_matrix[1][1]   0.009524 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009524 
_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]   0.009524 
_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  
FE 
N  
O  
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   . VAL A 1 1   ? 45.716 55.727 67.167 1.00 80.64  ? 1   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 1   ? 46.415 54.489 67.609 1.00 80.57  ? 1   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 1   ? 45.428 53.308 67.689 1.00 75.67  ? 1   VAL A C   1 
ATOM   4    O  O   . VAL A 1 1   ? 45.466 52.422 66.838 1.00 78.47  ? 1   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 1   ? 47.147 54.718 68.953 1.00 88.38  ? 1   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 1   ? 47.894 53.450 69.374 1.00 103.03 ? 1   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 1   ? 48.084 55.917 68.846 1.00 83.92  ? 1   VAL A CG2 1 
ATOM   8    N  N   . LEU A 1 2   ? 44.553 53.319 68.697 1.00 68.83  ? 2   LEU A N   1 
ATOM   9    C  CA  . LEU A 1 2   ? 43.478 52.333 68.873 1.00 61.97  ? 2   LEU A CA  1 
ATOM   10   C  C   . LEU A 1 2   ? 42.517 52.889 69.911 1.00 62.94  ? 2   LEU A C   1 
ATOM   11   O  O   . LEU A 1 2   ? 42.877 52.986 71.088 1.00 64.40  ? 2   LEU A O   1 
ATOM   12   C  CB  . LEU A 1 2   ? 44.028 50.997 69.377 1.00 60.27  ? 2   LEU A CB  1 
ATOM   13   C  CG  . LEU A 1 2   ? 44.273 49.854 68.392 1.00 60.54  ? 2   LEU A CG  1 
ATOM   14   C  CD1 . LEU A 1 2   ? 44.992 48.724 69.110 1.00 62.94  ? 2   LEU A CD1 1 
ATOM   15   C  CD2 . LEU A 1 2   ? 42.981 49.347 67.765 1.00 57.86  ? 2   LEU A CD2 1 
ATOM   16   N  N   . SER A 1 3   ? 41.312 53.271 69.493 1.00 64.75  ? 3   SER A N   1 
ATOM   17   C  CA  . SER A 1 3   ? 40.336 53.821 70.438 1.00 70.19  ? 3   SER A CA  1 
ATOM   18   C  C   . SER A 1 3   ? 39.834 52.739 71.395 1.00 78.69  ? 3   SER A C   1 
ATOM   19   O  O   . SER A 1 3   ? 39.930 51.547 71.078 1.00 82.88  ? 3   SER A O   1 
ATOM   20   C  CB  . SER A 1 3   ? 39.159 54.488 69.712 1.00 70.97  ? 3   SER A CB  1 
ATOM   21   O  OG  . SER A 1 3   ? 38.630 53.665 68.692 1.00 71.13  ? 3   SER A OG  1 
ATOM   22   N  N   . PRO A 1 4   ? 39.315 53.143 72.576 1.00 81.70  ? 4   PRO A N   1 
ATOM   23   C  CA  . PRO A 1 4   ? 38.761 52.149 73.505 1.00 83.79  ? 4   PRO A CA  1 
ATOM   24   C  C   . PRO A 1 4   ? 37.525 51.406 72.970 1.00 81.12  ? 4   PRO A C   1 
ATOM   25   O  O   . PRO A 1 4   ? 37.280 50.264 73.379 1.00 80.87  ? 4   PRO A O   1 
ATOM   26   C  CB  . PRO A 1 4   ? 38.415 52.982 74.746 1.00 85.54  ? 4   PRO A CB  1 
ATOM   27   C  CG  . PRO A 1 4   ? 38.259 54.370 74.242 1.00 83.34  ? 4   PRO A CG  1 
ATOM   28   C  CD  . PRO A 1 4   ? 39.272 54.499 73.152 1.00 80.76  ? 4   PRO A CD  1 
ATOM   29   N  N   . ALA A 1 5   ? 36.769 52.044 72.073 1.00 76.67  ? 5   ALA A N   1 
ATOM   30   C  CA  . ALA A 1 5   ? 35.700 51.368 71.327 1.00 78.76  ? 5   ALA A CA  1 
ATOM   31   C  C   . ALA A 1 5   ? 36.228 50.285 70.360 1.00 79.37  ? 5   ALA A C   1 
ATOM   32   O  O   . ALA A 1 5   ? 35.617 49.219 70.226 1.00 82.71  ? 5   ALA A O   1 
ATOM   33   C  CB  . ALA A 1 5   ? 34.859 52.386 70.574 1.00 77.33  ? 5   ALA A CB  1 
ATOM   34   N  N   . ASP A 1 6   ? 37.350 50.562 69.693 1.00 74.36  ? 6   ASP A N   1 
ATOM   35   C  CA  . ASP A 1 6   ? 37.996 49.582 68.818 1.00 70.42  ? 6   ASP A CA  1 
ATOM   36   C  C   . ASP A 1 6   ? 38.572 48.403 69.584 1.00 63.92  ? 6   ASP A C   1 
ATOM   37   O  O   . ASP A 1 6   ? 38.526 47.285 69.084 1.00 67.42  ? 6   ASP A O   1 
ATOM   38   C  CB  . ASP A 1 6   ? 39.105 50.227 67.970 1.00 83.63  ? 6   ASP A CB  1 
ATOM   39   C  CG  . ASP A 1 6   ? 38.563 51.149 66.864 1.00 96.98  ? 6   ASP A CG  1 
ATOM   40   O  OD1 . ASP A 1 6   ? 37.335 51.174 66.615 1.00 106.83 ? 6   ASP A OD1 1 
ATOM   41   O  OD2 . ASP A 1 6   ? 39.382 51.859 66.237 1.00 94.49  ? 6   ASP A OD2 1 
ATOM   42   N  N   . LYS A 1 7   ? 39.116 48.635 70.777 1.00 63.04  ? 7   LYS A N   1 
ATOM   43   C  CA  . LYS A 1 7   ? 39.633 47.534 71.604 1.00 65.61  ? 7   LYS A CA  1 
ATOM   44   C  C   . LYS A 1 7   ? 38.530 46.576 72.012 1.00 64.36  ? 7   LYS A C   1 
ATOM   45   O  O   . LYS A 1 7   ? 38.739 45.366 72.032 1.00 70.21  ? 7   LYS A O   1 
ATOM   46   C  CB  . LYS A 1 7   ? 40.312 48.045 72.863 1.00 74.19  ? 7   LYS A CB  1 
ATOM   47   C  CG  . LYS A 1 7   ? 41.605 48.796 72.615 1.00 85.58  ? 7   LYS A CG  1 
ATOM   48   C  CD  . LYS A 1 7   ? 42.089 49.482 73.888 1.00 94.54  ? 7   LYS A CD  1 
ATOM   49   C  CE  . LYS A 1 7   ? 43.264 50.416 73.627 1.00 99.12  ? 7   LYS A CE  1 
ATOM   50   N  NZ  . LYS A 1 7   ? 44.526 49.690 73.291 1.00 101.21 ? 7   LYS A NZ  1 
ATOM   51   N  N   . THR A 1 8   ? 37.362 47.114 72.345 1.00 62.38  ? 8   THR A N   1 
ATOM   52   C  CA  . THR A 1 8   ? 36.198 46.286 72.647 1.00 62.56  ? 8   THR A CA  1 
ATOM   53   C  C   . THR A 1 8   ? 35.808 45.439 71.442 1.00 58.75  ? 8   THR A C   1 
ATOM   54   O  O   . THR A 1 8   ? 35.738 44.214 71.541 1.00 58.08  ? 8   THR A O   1 
ATOM   55   C  CB  . THR A 1 8   ? 34.999 47.147 73.069 1.00 67.97  ? 8   THR A CB  1 
ATOM   56   O  OG1 . THR A 1 8   ? 35.339 47.887 74.250 1.00 70.77  ? 8   THR A OG1 1 
ATOM   57   C  CG2 . THR A 1 8   ? 33.761 46.278 73.339 1.00 71.45  ? 8   THR A CG2 1 
ATOM   58   N  N   . ASN A 1 9   ? 35.566 46.107 70.315 1.00 54.24  ? 9   ASN A N   1 
ATOM   59   C  CA  . ASN A 1 9   ? 35.198 45.440 69.065 1.00 51.81  ? 9   ASN A CA  1 
ATOM   60   C  C   . ASN A 1 9   ? 36.126 44.302 68.679 1.00 47.04  ? 9   ASN A C   1 
ATOM   61   O  O   . ASN A 1 9   ? 35.659 43.253 68.243 1.00 48.57  ? 9   ASN A O   1 
ATOM   62   C  CB  . ASN A 1 9   ? 35.160 46.436 67.898 1.00 55.50  ? 9   ASN A CB  1 
ATOM   63   C  CG  . ASN A 1 9   ? 33.888 47.254 67.857 1.00 58.88  ? 9   ASN A CG  1 
ATOM   64   O  OD1 . ASN A 1 9   ? 33.882 48.383 67.358 1.00 59.98  ? 9   ASN A OD1 1 
ATOM   65   N  ND2 . ASN A 1 9   ? 32.798 46.688 68.360 1.00 65.17  ? 9   ASN A ND2 1 
ATOM   66   N  N   . VAL A 1 10  ? 37.428 44.512 68.815 1.00 44.20  ? 10  VAL A N   1 
ATOM   67   C  CA  . VAL A 1 10  ? 38.386 43.470 68.488 1.00 45.87  ? 10  VAL A CA  1 
ATOM   68   C  C   . VAL A 1 10  ? 38.190 42.292 69.428 1.00 49.15  ? 10  VAL A C   1 
ATOM   69   O  O   . VAL A 1 10  ? 38.124 41.154 68.971 1.00 51.15  ? 10  VAL A O   1 
ATOM   70   C  CB  . VAL A 1 10  ? 39.841 43.984 68.527 1.00 46.42  ? 10  VAL A CB  1 
ATOM   71   C  CG1 . VAL A 1 10  ? 40.862 42.843 68.487 1.00 46.19  ? 10  VAL A CG1 1 
ATOM   72   C  CG2 . VAL A 1 10  ? 40.070 44.920 67.356 1.00 47.57  ? 10  VAL A CG2 1 
ATOM   73   N  N   . LYS A 1 11  ? 38.077 42.557 70.726 1.00 53.23  ? 11  LYS A N   1 
ATOM   74   C  CA  . LYS A 1 11  ? 37.895 41.476 71.700 1.00 59.49  ? 11  LYS A CA  1 
ATOM   75   C  C   . LYS A 1 11  ? 36.635 40.660 71.436 1.00 61.09  ? 11  LYS A C   1 
ATOM   76   O  O   . LYS A 1 11  ? 36.681 39.424 71.399 1.00 60.51  ? 11  LYS A O   1 
ATOM   77   C  CB  . LYS A 1 11  ? 37.885 42.021 73.127 1.00 65.01  ? 11  LYS A CB  1 
ATOM   78   C  CG  . LYS A 1 11  ? 39.273 42.388 73.598 1.00 70.72  ? 11  LYS A CG  1 
ATOM   79   C  CD  . LYS A 1 11  ? 39.282 43.013 74.978 1.00 76.25  ? 11  LYS A CD  1 
ATOM   80   C  CE  . LYS A 1 11  ? 40.676 43.528 75.310 1.00 83.51  ? 11  LYS A CE  1 
ATOM   81   N  NZ  . LYS A 1 11  ? 41.737 42.476 75.226 1.00 85.70  ? 11  LYS A NZ  1 
ATOM   82   N  N   . ALA A 1 12  ? 35.526 41.368 71.234 1.00 60.17  ? 12  ALA A N   1 
ATOM   83   C  CA  . ALA A 1 12  ? 34.231 40.752 70.957 1.00 59.25  ? 12  ALA A CA  1 
ATOM   84   C  C   . ALA A 1 12  ? 34.237 39.936 69.668 1.00 57.12  ? 12  ALA A C   1 
ATOM   85   O  O   . ALA A 1 12  ? 33.878 38.760 69.680 1.00 58.56  ? 12  ALA A O   1 
ATOM   86   C  CB  . ALA A 1 12  ? 33.155 41.823 70.884 1.00 62.36  ? 12  ALA A CB  1 
ATOM   87   N  N   . ALA A 1 13  ? 34.653 40.562 68.571 1.00 53.33  ? 13  ALA A N   1 
ATOM   88   C  CA  . ALA A 1 13  ? 34.648 39.914 67.261 1.00 52.11  ? 13  ALA A CA  1 
ATOM   89   C  C   . ALA A 1 13  ? 35.646 38.770 67.148 1.00 50.79  ? 13  ALA A C   1 
ATOM   90   O  O   . ALA A 1 13  ? 35.360 37.788 66.472 1.00 53.89  ? 13  ALA A O   1 
ATOM   91   C  CB  . ALA A 1 13  ? 34.901 40.925 66.160 1.00 54.01  ? 13  ALA A CB  1 
ATOM   92   N  N   . TRP A 1 14  ? 36.808 38.888 67.788 1.00 51.22  ? 14  TRP A N   1 
ATOM   93   C  CA  . TRP A 1 14  ? 37.775 37.785 67.809 1.00 52.04  ? 14  TRP A CA  1 
ATOM   94   C  C   . TRP A 1 14  ? 37.346 36.681 68.775 1.00 57.40  ? 14  TRP A C   1 
ATOM   95   O  O   . TRP A 1 14  ? 37.745 35.525 68.615 1.00 57.49  ? 14  TRP A O   1 
ATOM   96   C  CB  . TRP A 1 14  ? 39.177 38.271 68.153 1.00 50.49  ? 14  TRP A CB  1 
ATOM   97   C  CG  . TRP A 1 14  ? 40.194 37.247 67.865 1.00 49.19  ? 14  TRP A CG  1 
ATOM   98   C  CD1 . TRP A 1 14  ? 40.796 36.412 68.760 1.00 53.59  ? 14  TRP A CD1 1 
ATOM   99   C  CD2 . TRP A 1 14  ? 40.706 36.905 66.589 1.00 48.17  ? 14  TRP A CD2 1 
ATOM   100  N  NE1 . TRP A 1 14  ? 41.675 35.575 68.117 1.00 50.60  ? 14  TRP A NE1 1 
ATOM   101  C  CE2 . TRP A 1 14  ? 41.638 35.854 66.781 1.00 48.39  ? 14  TRP A CE2 1 
ATOM   102  C  CE3 . TRP A 1 14  ? 40.477 37.385 65.297 1.00 49.26  ? 14  TRP A CE3 1 
ATOM   103  C  CZ2 . TRP A 1 14  ? 42.331 35.269 65.731 1.00 50.79  ? 14  TRP A CZ2 1 
ATOM   104  C  CZ3 . TRP A 1 14  ? 41.162 36.801 64.242 1.00 52.93  ? 14  TRP A CZ3 1 
ATOM   105  C  CH2 . TRP A 1 14  ? 42.086 35.751 64.468 1.00 54.82  ? 14  TRP A CH2 1 
ATOM   106  N  N   . GLY A 1 15  ? 36.543 37.035 69.778 1.00 65.48  ? 15  GLY A N   1 
ATOM   107  C  CA  . GLY A 1 15  ? 35.847 36.041 70.601 1.00 74.03  ? 15  GLY A CA  1 
ATOM   108  C  C   . GLY A 1 15  ? 34.911 35.119 69.819 1.00 77.79  ? 15  GLY A C   1 
ATOM   109  O  O   . GLY A 1 15  ? 34.854 33.918 70.092 1.00 77.28  ? 15  GLY A O   1 
ATOM   110  N  N   . LYS A 1 16  ? 34.190 35.679 68.846 1.00 82.03  ? 16  LYS A N   1 
ATOM   111  C  CA  . LYS A 1 16  ? 33.236 34.912 68.030 1.00 84.89  ? 16  LYS A CA  1 
ATOM   112  C  C   . LYS A 1 16  ? 33.919 33.960 67.056 1.00 75.38  ? 16  LYS A C   1 
ATOM   113  O  O   . LYS A 1 16  ? 33.332 32.953 66.669 1.00 73.51  ? 16  LYS A O   1 
ATOM   114  C  CB  . LYS A 1 16  ? 32.296 35.842 67.254 1.00 98.56  ? 16  LYS A CB  1 
ATOM   115  C  CG  . LYS A 1 16  ? 31.444 36.758 68.124 1.00 119.10 ? 16  LYS A CG  1 
ATOM   116  C  CD  . LYS A 1 16  ? 30.386 36.009 68.925 1.00 133.19 ? 16  LYS A CD  1 
ATOM   117  C  CE  . LYS A 1 16  ? 29.544 36.967 69.761 1.00 145.33 ? 16  LYS A CE  1 
ATOM   118  N  NZ  . LYS A 1 16  ? 30.339 37.687 70.799 1.00 150.38 ? 16  LYS A NZ  1 
ATOM   119  N  N   . VAL A 1 17  ? 35.144 34.287 66.649 1.00 74.84  ? 17  VAL A N   1 
ATOM   120  C  CA  . VAL A 1 17  ? 35.971 33.363 65.875 1.00 77.49  ? 17  VAL A CA  1 
ATOM   121  C  C   . VAL A 1 17  ? 36.195 32.137 66.742 1.00 80.00  ? 17  VAL A C   1 
ATOM   122  O  O   . VAL A 1 17  ? 35.830 31.023 66.363 1.00 77.45  ? 17  VAL A O   1 
ATOM   123  C  CB  . VAL A 1 17  ? 37.332 33.990 65.478 1.00 77.99  ? 17  VAL A CB  1 
ATOM   124  C  CG1 . VAL A 1 17  ? 38.307 32.936 64.957 1.00 77.44  ? 17  VAL A CG1 1 
ATOM   125  C  CG2 . VAL A 1 17  ? 37.131 35.090 64.445 1.00 78.39  ? 17  VAL A CG2 1 
ATOM   126  N  N   . GLY A 1 18  ? 36.784 32.371 67.913 1.00 86.35  ? 18  GLY A N   1 
ATOM   127  C  CA  . GLY A 1 18  ? 36.932 31.355 68.946 1.00 91.60  ? 18  GLY A CA  1 
ATOM   128  C  C   . GLY A 1 18  ? 37.794 30.169 68.561 1.00 90.02  ? 18  GLY A C   1 
ATOM   129  O  O   . GLY A 1 18  ? 39.005 30.306 68.370 1.00 93.62  ? 18  GLY A O   1 
ATOM   130  N  N   . ALA A 1 19  ? 37.152 29.011 68.428 1.00 88.51  ? 19  ALA A N   1 
ATOM   131  C  CA  . ALA A 1 19  ? 37.843 27.727 68.319 1.00 92.09  ? 19  ALA A CA  1 
ATOM   132  C  C   . ALA A 1 19  ? 38.090 27.230 66.890 1.00 92.83  ? 19  ALA A C   1 
ATOM   133  O  O   . ALA A 1 19  ? 38.674 26.161 66.712 1.00 93.81  ? 19  ALA A O   1 
ATOM   134  C  CB  . ALA A 1 19  ? 37.074 26.676 69.102 1.00 95.42  ? 19  ALA A CB  1 
ATOM   135  N  N   . HIS A 1 20  ? 37.658 27.988 65.882 1.00 97.20  ? 20  HIS A N   1 
ATOM   136  C  CA  . HIS A 1 20  ? 37.994 27.685 64.486 1.00 101.42 ? 20  HIS A CA  1 
ATOM   137  C  C   . HIS A 1 20  ? 39.222 28.478 64.031 1.00 91.15  ? 20  HIS A C   1 
ATOM   138  O  O   . HIS A 1 20  ? 39.434 28.672 62.829 1.00 91.14  ? 20  HIS A O   1 
ATOM   139  C  CB  . HIS A 1 20  ? 36.800 27.990 63.576 1.00 116.73 ? 20  HIS A CB  1 
ATOM   140  C  CG  . HIS A 1 20  ? 35.581 27.186 63.896 1.00 132.56 ? 20  HIS A CG  1 
ATOM   141  N  ND1 . HIS A 1 20  ? 34.563 27.664 64.692 1.00 141.29 ? 20  HIS A ND1 1 
ATOM   142  C  CD2 . HIS A 1 20  ? 35.221 25.933 63.534 1.00 144.72 ? 20  HIS A CD2 1 
ATOM   143  C  CE1 . HIS A 1 20  ? 33.625 26.740 64.804 1.00 150.83 ? 20  HIS A CE1 1 
ATOM   144  N  NE2 . HIS A 1 20  ? 34.000 25.680 64.110 1.00 153.31 ? 20  HIS A NE2 1 
ATOM   145  N  N   . ALA A 1 21  ? 40.045 28.909 64.987 1.00 80.35  ? 21  ALA A N   1 
ATOM   146  C  CA  . ALA A 1 21  ? 41.169 29.779 64.697 1.00 74.52  ? 21  ALA A CA  1 
ATOM   147  C  C   . ALA A 1 21  ? 42.185 29.056 63.830 1.00 69.23  ? 21  ALA A C   1 
ATOM   148  O  O   . ALA A 1 21  ? 42.708 29.635 62.885 1.00 76.78  ? 21  ALA A O   1 
ATOM   149  C  CB  . ALA A 1 21  ? 41.807 30.270 65.986 1.00 75.37  ? 21  ALA A CB  1 
ATOM   150  N  N   . GLY A 1 22  ? 42.440 27.789 64.135 1.00 65.34  ? 22  GLY A N   1 
ATOM   151  C  CA  . GLY A 1 22  ? 43.311 26.969 63.310 1.00 66.62  ? 22  GLY A CA  1 
ATOM   152  C  C   . GLY A 1 22  ? 42.907 26.974 61.851 1.00 66.14  ? 22  GLY A C   1 
ATOM   153  O  O   . GLY A 1 22  ? 43.726 27.237 60.972 1.00 65.68  ? 22  GLY A O   1 
ATOM   154  N  N   . GLU A 1 23  ? 41.632 26.713 61.599 1.00 71.61  ? 23  GLU A N   1 
ATOM   155  C  CA  . GLU A 1 23  ? 41.138 26.586 60.236 1.00 78.39  ? 23  GLU A CA  1 
ATOM   156  C  C   . GLU A 1 23  ? 41.163 27.913 59.491 1.00 64.25  ? 23  GLU A C   1 
ATOM   157  O  O   . GLU A 1 23  ? 41.548 27.947 58.323 1.00 66.15  ? 23  GLU A O   1 
ATOM   158  C  CB  . GLU A 1 23  ? 39.725 26.008 60.231 1.00 101.26 ? 23  GLU A CB  1 
ATOM   159  C  CG  . GLU A 1 23  ? 39.228 25.567 58.859 1.00 121.69 ? 23  GLU A CG  1 
ATOM   160  C  CD  . GLU A 1 23  ? 37.806 25.019 58.883 1.00 148.12 ? 23  GLU A CD  1 
ATOM   161  O  OE1 . GLU A 1 23  ? 37.201 24.913 59.976 1.00 161.99 ? 23  GLU A OE1 1 
ATOM   162  O  OE2 . GLU A 1 23  ? 37.285 24.691 57.794 1.00 165.06 ? 23  GLU A OE2 1 
ATOM   163  N  N   . TYR A 1 24  ? 40.754 28.992 60.154 1.00 52.40  ? 24  TYR A N   1 
ATOM   164  C  CA  . TYR A 1 24  ? 40.773 30.309 59.522 1.00 47.39  ? 24  TYR A CA  1 
ATOM   165  C  C   . TYR A 1 24  ? 42.188 30.752 59.217 1.00 43.28  ? 24  TYR A C   1 
ATOM   166  O  O   . TYR A 1 24  ? 42.428 31.334 58.160 1.00 48.14  ? 24  TYR A O   1 
ATOM   167  C  CB  . TYR A 1 24  ? 40.061 31.369 60.363 1.00 48.04  ? 24  TYR A CB  1 
ATOM   168  C  CG  . TYR A 1 24  ? 38.569 31.141 60.556 1.00 53.85  ? 24  TYR A CG  1 
ATOM   169  C  CD1 . TYR A 1 24  ? 37.823 30.281 59.713 1.00 56.35  ? 24  TYR A CD1 1 
ATOM   170  C  CD2 . TYR A 1 24  ? 37.883 31.807 61.579 1.00 56.20  ? 24  TYR A CD2 1 
ATOM   171  C  CE1 . TYR A 1 24  ? 36.459 30.086 59.911 1.00 58.56  ? 24  TYR A CE1 1 
ATOM   172  C  CE2 . TYR A 1 24  ? 36.518 31.622 61.779 1.00 56.88  ? 24  TYR A CE2 1 
ATOM   173  C  CZ  . TYR A 1 24  ? 35.811 30.762 60.949 1.00 60.55  ? 24  TYR A CZ  1 
ATOM   174  O  OH  . TYR A 1 24  ? 34.460 30.575 61.153 1.00 64.58  ? 24  TYR A OH  1 
ATOM   175  N  N   . GLY A 1 25  ? 43.120 30.469 60.122 1.00 36.14  ? 25  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 25  ? 44.528 30.765 59.900 1.00 31.31  ? 25  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 25  ? 45.079 30.057 58.683 1.00 28.87  ? 25  GLY A C   1 
ATOM   178  O  O   . GLY A 1 25  ? 45.867 30.627 57.938 1.00 29.21  ? 25  GLY A O   1 
ATOM   179  N  N   . ALA A 1 26  ? 44.657 28.818 58.479 1.00 28.33  ? 26  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 26  ? 45.135 28.023 57.364 1.00 29.86  ? 26  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 26  ? 44.620 28.558 56.052 1.00 31.92  ? 26  ALA A C   1 
ATOM   182  O  O   . ALA A 1 26  ? 45.371 28.702 55.095 1.00 33.51  ? 26  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 26  ? 44.695 26.581 57.528 1.00 30.77  ? 26  ALA A CB  1 
ATOM   184  N  N   . GLU A 1 27  ? 43.325 28.832 56.012 1.00 36.92  ? 27  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 27  ? 42.672 29.333 54.811 1.00 41.46  ? 27  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 27  ? 43.231 30.692 54.399 1.00 37.39  ? 27  GLU A C   1 
ATOM   187  O  O   . GLU A 1 27  ? 43.397 30.948 53.211 1.00 38.13  ? 27  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 27  ? 41.173 29.441 55.054 1.00 52.95  ? 27  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 27  ? 40.346 29.775 53.821 1.00 66.28  ? 27  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 27  ? 38.873 30.028 54.138 1.00 79.29  ? 27  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 27  ? 38.415 29.677 55.253 1.00 86.92  ? 27  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 27  ? 38.169 30.579 53.260 1.00 84.86  ? 27  GLU A OE2 1 
ATOM   193  N  N   . ALA A 1 28  ? 43.517 31.551 55.379 1.00 32.65  ? 28  ALA A N   1 
ATOM   194  C  CA  . ALA A 1 28  ? 44.200 32.825 55.134 1.00 28.74  ? 28  ALA A CA  1 
ATOM   195  C  C   . ALA A 1 28  ? 45.540 32.628 54.417 1.00 27.38  ? 28  ALA A C   1 
ATOM   196  O  O   . ALA A 1 28  ? 45.737 33.177 53.331 1.00 26.89  ? 28  ALA A O   1 
ATOM   197  C  CB  . ALA A 1 28  ? 44.389 33.599 56.431 1.00 27.10  ? 28  ALA A CB  1 
ATOM   198  N  N   . LEU A 1 29  ? 46.442 31.836 54.993 1.00 27.86  ? 29  LEU A N   1 
ATOM   199  C  CA  . LEU A 1 29  ? 47.696 31.505 54.309 1.00 30.11  ? 29  LEU A CA  1 
ATOM   200  C  C   . LEU A 1 29  ? 47.485 30.963 52.913 1.00 32.20  ? 29  LEU A C   1 
ATOM   201  O  O   . LEU A 1 29  ? 48.247 31.299 52.016 1.00 36.76  ? 29  LEU A O   1 
ATOM   202  C  CB  . LEU A 1 29  ? 48.531 30.489 55.078 1.00 31.07  ? 29  LEU A CB  1 
ATOM   203  C  CG  . LEU A 1 29  ? 49.182 31.018 56.348 1.00 34.32  ? 29  LEU A CG  1 
ATOM   204  C  CD1 . LEU A 1 29  ? 49.968 29.919 57.040 1.00 34.40  ? 29  LEU A CD1 1 
ATOM   205  C  CD2 . LEU A 1 29  ? 50.085 32.207 56.054 1.00 37.51  ? 29  LEU A CD2 1 
ATOM   206  N  N   . GLU A 1 30  ? 46.466 30.137 52.721 1.00 33.82  ? 30  GLU A N   1 
ATOM   207  C  CA  . GLU A 1 30  ? 46.237 29.517 51.427 1.00 36.27  ? 30  GLU A CA  1 
ATOM   208  C  C   . GLU A 1 30  ? 45.795 30.511 50.349 1.00 29.82  ? 30  GLU A C   1 
ATOM   209  O  O   . GLU A 1 30  ? 46.249 30.417 49.211 1.00 29.13  ? 30  GLU A O   1 
ATOM   210  C  CB  . GLU A 1 30  ? 45.216 28.403 51.569 1.00 49.43  ? 30  GLU A CB  1 
ATOM   211  C  CG  . GLU A 1 30  ? 45.160 27.464 50.373 1.00 65.28  ? 30  GLU A CG  1 
ATOM   212  C  CD  . GLU A 1 30  ? 44.080 26.394 50.510 1.00 82.77  ? 30  GLU A CD  1 
ATOM   213  O  OE1 . GLU A 1 30  ? 43.801 25.946 51.651 1.00 95.08  ? 30  GLU A OE1 1 
ATOM   214  O  OE2 . GLU A 1 30  ? 43.510 25.995 49.466 1.00 92.83  ? 30  GLU A OE2 1 
ATOM   215  N  N   . ARG A 1 31  ? 44.905 31.435 50.704 1.00 25.17  ? 31  ARG A N   1 
ATOM   216  C  CA  . ARG A 1 31  ? 44.485 32.503 49.797 1.00 22.50  ? 31  ARG A CA  1 
ATOM   217  C  C   . ARG A 1 31  ? 45.662 33.356 49.437 1.00 22.60  ? 31  ARG A C   1 
ATOM   218  O  O   . ARG A 1 31  ? 45.851 33.661 48.266 1.00 23.18  ? 31  ARG A O   1 
ATOM   219  C  CB  . ARG A 1 31  ? 43.441 33.414 50.432 1.00 21.82  ? 31  ARG A CB  1 
ATOM   220  C  CG  . ARG A 1 31  ? 42.060 32.815 50.491 1.00 22.02  ? 31  ARG A CG  1 
ATOM   221  C  CD  . ARG A 1 31  ? 41.134 33.608 51.395 1.00 22.28  ? 31  ARG A CD  1 
ATOM   222  N  NE  . ARG A 1 31  ? 39.846 32.929 51.513 1.00 22.95  ? 31  ARG A NE  1 
ATOM   223  C  CZ  . ARG A 1 31  ? 38.890 32.920 50.582 1.00 23.82  ? 31  ARG A CZ  1 
ATOM   224  N  NH1 . ARG A 1 31  ? 37.762 32.250 50.809 1.00 24.70  ? 31  ARG A NH1 1 
ATOM   225  N  NH2 . ARG A 1 31  ? 39.032 33.580 49.429 1.00 23.81  ? 31  ARG A NH2 1 
ATOM   226  N  N   . MET A 1 32  ? 46.439 33.759 50.445 1.00 23.02  ? 32  MET A N   1 
ATOM   227  C  CA  . MET A 1 32  ? 47.616 34.586 50.224 1.00 23.94  ? 32  MET A CA  1 
ATOM   228  C  C   . MET A 1 32  ? 48.609 33.951 49.234 1.00 23.95  ? 32  MET A C   1 
ATOM   229  O  O   . MET A 1 32  ? 48.965 34.603 48.264 1.00 24.85  ? 32  MET A O   1 
ATOM   230  C  CB  . MET A 1 32  ? 48.306 34.923 51.537 1.00 27.10  ? 32  MET A CB  1 
ATOM   231  C  CG  . MET A 1 32  ? 49.475 35.902 51.375 1.00 31.65  ? 32  MET A CG  1 
ATOM   232  S  SD  . MET A 1 32  ? 50.456 36.331 52.846 1.00 37.56  ? 32  MET A SD  1 
ATOM   233  C  CE  . MET A 1 32  ? 50.990 34.727 53.499 1.00 36.28  ? 32  MET A CE  1 
ATOM   234  N  N   . PHE A 1 33  ? 49.039 32.704 49.438 1.00 24.62  ? 33  PHE A N   1 
ATOM   235  C  CA  . PHE A 1 33  ? 49.940 32.048 48.471 1.00 25.99  ? 33  PHE A CA  1 
ATOM   236  C  C   . PHE A 1 33  ? 49.382 31.998 47.049 1.00 29.47  ? 33  PHE A C   1 
ATOM   237  O  O   . PHE A 1 33  ? 50.140 32.188 46.107 1.00 32.73  ? 33  PHE A O   1 
ATOM   238  C  CB  . PHE A 1 33  ? 50.307 30.618 48.864 1.00 26.44  ? 33  PHE A CB  1 
ATOM   239  C  CG  . PHE A 1 33  ? 51.119 30.515 50.114 1.00 27.51  ? 33  PHE A CG  1 
ATOM   240  C  CD1 . PHE A 1 33  ? 52.301 31.203 50.247 1.00 30.31  ? 33  PHE A CD1 1 
ATOM   241  C  CD2 . PHE A 1 33  ? 50.711 29.706 51.161 1.00 28.73  ? 33  PHE A CD2 1 
ATOM   242  C  CE1 . PHE A 1 33  ? 53.047 31.115 51.419 1.00 31.72  ? 33  PHE A CE1 1 
ATOM   243  C  CE2 . PHE A 1 33  ? 51.443 29.614 52.337 1.00 29.49  ? 33  PHE A CE2 1 
ATOM   244  C  CZ  . PHE A 1 33  ? 52.617 30.314 52.467 1.00 30.34  ? 33  PHE A CZ  1 
ATOM   245  N  N   . LEU A 1 34  ? 48.086 31.731 46.875 1.00 32.91  ? 34  LEU A N   1 
ATOM   246  C  CA  . LEU A 1 34  ? 47.464 31.744 45.521 1.00 34.10  ? 34  LEU A CA  1 
ATOM   247  C  C   . LEU A 1 34  ? 47.389 33.111 44.891 1.00 31.40  ? 34  LEU A C   1 
ATOM   248  O  O   . LEU A 1 34  ? 47.698 33.256 43.717 1.00 32.13  ? 34  LEU A O   1 
ATOM   249  C  CB  . LEU A 1 34  ? 46.042 31.200 45.538 1.00 37.81  ? 34  LEU A CB  1 
ATOM   250  C  CG  . LEU A 1 34  ? 45.950 29.691 45.448 1.00 44.22  ? 34  LEU A CG  1 
ATOM   251  C  CD1 . LEU A 1 34  ? 44.583 29.226 45.936 1.00 48.82  ? 34  LEU A CD1 1 
ATOM   252  C  CD2 . LEU A 1 34  ? 46.216 29.240 44.015 1.00 46.89  ? 34  LEU A CD2 1 
ATOM   253  N  N   . SER A 1 35  ? 46.942 34.092 45.669 1.00 30.22  ? 35  SER A N   1 
ATOM   254  C  CA  . SER A 1 35  ? 46.689 35.437 45.159 1.00 30.82  ? 35  SER A CA  1 
ATOM   255  C  C   . SER A 1 35  ? 47.974 36.190 44.825 1.00 32.00  ? 35  SER A C   1 
ATOM   256  O  O   . SER A 1 35  ? 48.051 36.844 43.781 1.00 35.01  ? 35  SER A O   1 
ATOM   257  C  CB  . SER A 1 35  ? 45.861 36.255 46.156 1.00 30.60  ? 35  SER A CB  1 
ATOM   258  O  OG  . SER A 1 35  ? 44.565 35.706 46.314 1.00 31.27  ? 35  SER A OG  1 
ATOM   259  N  N   . PHE A 1 36  ? 48.971 36.098 45.703 1.00 30.51  ? 36  PHE A N   1 
ATOM   260  C  CA  . PHE A 1 36  ? 50.204 36.875 45.585 1.00 30.15  ? 36  PHE A CA  1 
ATOM   261  C  C   . PHE A 1 36  ? 51.402 35.940 45.654 1.00 32.33  ? 36  PHE A C   1 
ATOM   262  O  O   . PHE A 1 36  ? 52.112 35.889 46.657 1.00 34.82  ? 36  PHE A O   1 
ATOM   263  C  CB  . PHE A 1 36  ? 50.287 37.888 46.713 1.00 29.05  ? 36  PHE A CB  1 
ATOM   264  C  CG  . PHE A 1 36  ? 49.029 38.628 46.935 1.00 28.76  ? 36  PHE A CG  1 
ATOM   265  C  CD1 . PHE A 1 36  ? 48.669 39.643 46.071 1.00 29.16  ? 36  PHE A CD1 1 
ATOM   266  C  CD2 . PHE A 1 36  ? 48.196 38.307 48.009 1.00 29.28  ? 36  PHE A CD2 1 
ATOM   267  C  CE1 . PHE A 1 36  ? 47.492 40.343 46.268 1.00 30.86  ? 36  PHE A CE1 1 
ATOM   268  C  CE2 . PHE A 1 36  ? 47.016 38.997 48.216 1.00 30.33  ? 36  PHE A CE2 1 
ATOM   269  C  CZ  . PHE A 1 36  ? 46.663 40.021 47.344 1.00 31.73  ? 36  PHE A CZ  1 
ATOM   270  N  N   . PRO A 1 37  ? 51.654 35.206 44.581 1.00 33.15  ? 37  PRO A N   1 
ATOM   271  C  CA  . PRO A 1 37  ? 52.598 34.089 44.645 1.00 33.61  ? 37  PRO A CA  1 
ATOM   272  C  C   . PRO A 1 37  ? 54.068 34.416 44.930 1.00 33.23  ? 37  PRO A C   1 
ATOM   273  O  O   . PRO A 1 37  ? 54.822 33.510 45.281 1.00 32.75  ? 37  PRO A O   1 
ATOM   274  C  CB  . PRO A 1 37  ? 52.439 33.433 43.282 1.00 36.32  ? 37  PRO A CB  1 
ATOM   275  C  CG  . PRO A 1 37  ? 51.977 34.546 42.395 1.00 37.51  ? 37  PRO A CG  1 
ATOM   276  C  CD  . PRO A 1 37  ? 51.097 35.400 43.237 1.00 34.61  ? 37  PRO A CD  1 
ATOM   277  N  N   . THR A 1 38  ? 54.474 35.674 44.810 1.00 35.63  ? 38  THR A N   1 
ATOM   278  C  CA  . THR A 1 38  ? 55.819 36.081 45.250 1.00 40.01  ? 38  THR A CA  1 
ATOM   279  C  C   . THR A 1 38  ? 56.030 36.036 46.765 1.00 37.34  ? 38  THR A C   1 
ATOM   280  O  O   . THR A 1 38  ? 57.164 36.141 47.233 1.00 36.98  ? 38  THR A O   1 
ATOM   281  C  CB  . THR A 1 38  ? 56.148 37.506 44.793 1.00 47.12  ? 38  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 38  ? 55.078 38.387 45.170 1.00 49.49  ? 38  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 38  ? 56.337 37.535 43.284 1.00 53.50  ? 38  THR A CG2 1 
ATOM   284  N  N   . THR A 1 39  ? 54.939 35.919 47.521 1.00 33.43  ? 39  THR A N   1 
ATOM   285  C  CA  . THR A 1 39  ? 55.005 35.708 48.957 1.00 30.77  ? 39  THR A CA  1 
ATOM   286  C  C   . THR A 1 39  ? 55.545 34.315 49.337 1.00 31.52  ? 39  THR A C   1 
ATOM   287  O  O   . THR A 1 39  ? 55.942 34.106 50.478 1.00 31.77  ? 39  THR A O   1 
ATOM   288  C  CB  . THR A 1 39  ? 53.622 35.925 49.603 1.00 28.46  ? 39  THR A CB  1 
ATOM   289  O  OG1 . THR A 1 39  ? 53.776 36.167 51.003 1.00 29.43  ? 39  THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 39  ? 52.719 34.719 49.402 1.00 27.89  ? 39  THR A CG2 1 
ATOM   291  N  N   . LYS A 1 40  ? 55.536 33.364 48.400 1.00 32.67  ? 40  LYS A N   1 
ATOM   292  C  CA  . LYS A 1 40  ? 56.011 32.009 48.676 1.00 33.27  ? 40  LYS A CA  1 
ATOM   293  C  C   . LYS A 1 40  ? 57.475 31.970 49.025 1.00 32.19  ? 40  LYS A C   1 
ATOM   294  O  O   . LYS A 1 40  ? 57.891 31.167 49.857 1.00 32.13  ? 40  LYS A O   1 
ATOM   295  C  CB  . LYS A 1 40  ? 55.789 31.095 47.480 1.00 37.38  ? 40  LYS A CB  1 
ATOM   296  C  CG  . LYS A 1 40  ? 54.343 30.728 47.245 1.00 41.45  ? 40  LYS A CG  1 
ATOM   297  C  CD  . LYS A 1 40  ? 54.210 29.871 45.999 1.00 46.95  ? 40  LYS A CD  1 
ATOM   298  C  CE  . LYS A 1 40  ? 52.749 29.682 45.622 1.00 54.12  ? 40  LYS A CE  1 
ATOM   299  N  NZ  . LYS A 1 40  ? 52.567 29.189 44.227 1.00 58.27  ? 40  LYS A NZ  1 
ATOM   300  N  N   . THR A 1 41  ? 58.251 32.856 48.417 1.00 31.69  ? 41  THR A N   1 
ATOM   301  C  CA  . THR A 1 41  ? 59.708 32.820 48.547 1.00 32.36  ? 41  THR A CA  1 
ATOM   302  C  C   . THR A 1 41  ? 60.259 32.849 49.984 1.00 29.63  ? 41  THR A C   1 
ATOM   303  O  O   . THR A 1 41  ? 61.404 32.454 50.208 1.00 29.46  ? 41  THR A O   1 
ATOM   304  C  CB  . THR A 1 41  ? 60.368 33.962 47.748 1.00 35.10  ? 41  THR A CB  1 
ATOM   305  O  OG1 . THR A 1 41  ? 59.966 35.231 48.277 1.00 35.64  ? 41  THR A OG1 1 
ATOM   306  C  CG2 . THR A 1 41  ? 59.985 33.875 46.269 1.00 37.17  ? 41  THR A CG2 1 
ATOM   307  N  N   . TYR A 1 42  ? 59.464 33.324 50.939 1.00 26.86  ? 42  TYR A N   1 
ATOM   308  C  CA  . TYR A 1 42  ? 59.844 33.256 52.347 1.00 25.23  ? 42  TYR A CA  1 
ATOM   309  C  C   . TYR A 1 42  ? 59.750 31.846 52.880 1.00 25.90  ? 42  TYR A C   1 
ATOM   310  O  O   . TYR A 1 42  ? 60.440 31.527 53.839 1.00 27.08  ? 42  TYR A O   1 
ATOM   311  C  CB  . TYR A 1 42  ? 58.998 34.203 53.200 1.00 23.47  ? 42  TYR A CB  1 
ATOM   312  C  CG  . TYR A 1 42  ? 59.285 35.632 52.864 1.00 22.17  ? 42  TYR A CG  1 
ATOM   313  C  CD1 . TYR A 1 42  ? 60.342 36.306 53.453 1.00 21.77  ? 42  TYR A CD1 1 
ATOM   314  C  CD2 . TYR A 1 42  ? 58.535 36.293 51.924 1.00 22.16  ? 42  TYR A CD2 1 
ATOM   315  C  CE1 . TYR A 1 42  ? 60.627 37.617 53.134 1.00 22.05  ? 42  TYR A CE1 1 
ATOM   316  C  CE2 . TYR A 1 42  ? 58.811 37.600 51.585 1.00 23.27  ? 42  TYR A CE2 1 
ATOM   317  C  CZ  . TYR A 1 42  ? 59.859 38.267 52.190 1.00 23.42  ? 42  TYR A CZ  1 
ATOM   318  O  OH  . TYR A 1 42  ? 60.123 39.583 51.843 1.00 24.03  ? 42  TYR A OH  1 
ATOM   319  N  N   . PHE A 1 43  ? 58.903 31.015 52.273 1.00 26.46  ? 43  PHE A N   1 
ATOM   320  C  CA  . PHE A 1 43  ? 58.767 29.615 52.641 1.00 28.81  ? 43  PHE A CA  1 
ATOM   321  C  C   . PHE A 1 43  ? 59.357 28.718 51.552 1.00 37.80  ? 43  PHE A C   1 
ATOM   322  O  O   . PHE A 1 43  ? 58.616 28.115 50.770 1.00 40.51  ? 43  PHE A O   1 
ATOM   323  C  CB  . PHE A 1 43  ? 57.302 29.258 52.791 1.00 25.53  ? 43  PHE A CB  1 
ATOM   324  C  CG  . PHE A 1 43  ? 56.562 30.088 53.775 1.00 23.67  ? 43  PHE A CG  1 
ATOM   325  C  CD1 . PHE A 1 43  ? 56.371 29.643 55.070 1.00 23.38  ? 43  PHE A CD1 1 
ATOM   326  C  CD2 . PHE A 1 43  ? 56.000 31.290 53.395 1.00 23.22  ? 43  PHE A CD2 1 
ATOM   327  C  CE1 . PHE A 1 43  ? 55.659 30.394 55.984 1.00 22.31  ? 43  PHE A CE1 1 
ATOM   328  C  CE2 . PHE A 1 43  ? 55.285 32.052 54.300 1.00 22.86  ? 43  PHE A CE2 1 
ATOM   329  C  CZ  . PHE A 1 43  ? 55.115 31.601 55.597 1.00 22.60  ? 43  PHE A CZ  1 
ATOM   330  N  N   . PRO A 1 44  ? 60.691 28.603 51.487 1.00 47.53  ? 44  PRO A N   1 
ATOM   331  C  CA  . PRO A 1 44  ? 61.284 27.795 50.418 1.00 52.89  ? 44  PRO A CA  1 
ATOM   332  C  C   . PRO A 1 44  ? 61.133 26.281 50.625 1.00 60.73  ? 44  PRO A C   1 
ATOM   333  O  O   . PRO A 1 44  ? 61.034 25.530 49.654 1.00 61.55  ? 44  PRO A O   1 
ATOM   334  C  CB  . PRO A 1 44  ? 62.753 28.184 50.498 1.00 53.13  ? 44  PRO A CB  1 
ATOM   335  C  CG  . PRO A 1 44  ? 62.969 28.405 51.958 1.00 51.89  ? 44  PRO A CG  1 
ATOM   336  C  CD  . PRO A 1 44  ? 61.715 29.075 52.437 1.00 48.84  ? 44  PRO A CD  1 
ATOM   337  N  N   . HIS A 1 45  ? 61.088 25.860 51.884 1.00 72.84  ? 45  HIS A N   1 
ATOM   338  C  CA  . HIS A 1 45  ? 61.195 24.454 52.264 1.00 86.74  ? 45  HIS A CA  1 
ATOM   339  C  C   . HIS A 1 45  ? 59.837 23.802 52.575 1.00 84.59  ? 45  HIS A C   1 
ATOM   340  O  O   . HIS A 1 45  ? 59.772 22.591 52.794 1.00 86.55  ? 45  HIS A O   1 
ATOM   341  C  CB  . HIS A 1 45  ? 62.142 24.316 53.466 1.00 102.69 ? 45  HIS A CB  1 
ATOM   342  C  CG  . HIS A 1 45  ? 61.677 25.046 54.689 1.00 118.26 ? 45  HIS A CG  1 
ATOM   343  N  ND1 . HIS A 1 45  ? 61.936 26.384 54.899 1.00 125.52 ? 45  HIS A ND1 1 
ATOM   344  C  CD2 . HIS A 1 45  ? 60.952 24.631 55.754 1.00 129.87 ? 45  HIS A CD2 1 
ATOM   345  C  CE1 . HIS A 1 45  ? 61.394 26.761 56.043 1.00 134.26 ? 45  HIS A CE1 1 
ATOM   346  N  NE2 . HIS A 1 45  ? 60.793 25.716 56.583 1.00 134.94 ? 45  HIS A NE2 1 
ATOM   347  N  N   . PHE A 1 46  ? 58.766 24.593 52.606 1.00 80.87  ? 46  PHE A N   1 
ATOM   348  C  CA  . PHE A 1 46  ? 57.422 24.056 52.798 1.00 82.28  ? 46  PHE A CA  1 
ATOM   349  C  C   . PHE A 1 46  ? 56.939 23.383 51.522 1.00 97.05  ? 46  PHE A C   1 
ATOM   350  O  O   . PHE A 1 46  ? 57.440 23.657 50.427 1.00 99.78  ? 46  PHE A O   1 
ATOM   351  C  CB  . PHE A 1 46  ? 56.429 25.168 53.171 1.00 77.47  ? 46  PHE A CB  1 
ATOM   352  C  CG  . PHE A 1 46  ? 56.385 25.516 54.642 1.00 71.96  ? 46  PHE A CG  1 
ATOM   353  C  CD1 . PHE A 1 46  ? 57.456 25.249 55.504 1.00 69.34  ? 46  PHE A CD1 1 
ATOM   354  C  CD2 . PHE A 1 46  ? 55.257 26.162 55.162 1.00 66.54  ? 46  PHE A CD2 1 
ATOM   355  C  CE1 . PHE A 1 46  ? 57.387 25.600 56.845 1.00 67.58  ? 46  PHE A CE1 1 
ATOM   356  C  CE2 . PHE A 1 46  ? 55.185 26.512 56.503 1.00 63.93  ? 46  PHE A CE2 1 
ATOM   357  C  CZ  . PHE A 1 46  ? 56.252 26.233 57.345 1.00 65.63  ? 46  PHE A CZ  1 
ATOM   358  N  N   . ASP A 1 47  ? 55.948 22.513 51.689 1.00 115.19 ? 47  ASP A N   1 
ATOM   359  C  CA  . ASP A 1 47  ? 55.228 21.880 50.575 1.00 124.60 ? 47  ASP A CA  1 
ATOM   360  C  C   . ASP A 1 47  ? 53.915 22.635 50.371 1.00 107.30 ? 47  ASP A C   1 
ATOM   361  O  O   . ASP A 1 47  ? 52.917 22.365 51.039 1.00 101.07 ? 47  ASP A O   1 
ATOM   362  C  CB  . ASP A 1 47  ? 54.997 20.367 50.810 1.00 148.20 ? 47  ASP A CB  1 
ATOM   363  C  CG  . ASP A 1 47  ? 54.537 20.023 52.240 1.00 165.41 ? 47  ASP A CG  1 
ATOM   364  O  OD1 . ASP A 1 47  ? 54.528 20.914 53.116 1.00 169.96 ? 47  ASP A OD1 1 
ATOM   365  O  OD2 . ASP A 1 47  ? 54.192 18.846 52.484 1.00 177.69 ? 47  ASP A OD2 1 
ATOM   366  N  N   . LEU A 1 48  ? 53.924 23.586 49.442 1.00 98.28  ? 48  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 48  ? 52.812 24.518 49.284 1.00 99.89  ? 48  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 48  ? 51.793 24.047 48.252 1.00 108.97 ? 48  LEU A C   1 
ATOM   369  O  O   . LEU A 1 48  ? 51.374 24.816 47.380 1.00 113.19 ? 48  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 48  ? 53.347 25.894 48.900 1.00 98.23  ? 48  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 48  ? 54.369 26.499 49.853 1.00 95.93  ? 48  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 48  ? 54.858 27.803 49.254 1.00 98.76  ? 48  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 48  ? 53.773 26.727 51.235 1.00 92.61  ? 48  LEU A CD2 1 
ATOM   374  N  N   . SER A 1 49  ? 51.383 22.786 48.366 1.00 118.74 ? 49  SER A N   1 
ATOM   375  C  CA  . SER A 1 49  ? 50.312 22.232 47.545 1.00 126.37 ? 49  SER A CA  1 
ATOM   376  C  C   . SER A 1 49  ? 48.980 22.464 48.258 1.00 130.64 ? 49  SER A C   1 
ATOM   377  O  O   . SER A 1 49  ? 48.931 23.125 49.301 1.00 130.20 ? 49  SER A O   1 
ATOM   378  C  CB  . SER A 1 49  ? 50.557 20.736 47.300 1.00 127.17 ? 49  SER A CB  1 
ATOM   379  O  OG  . SER A 1 49  ? 50.435 19.979 48.493 1.00 123.85 ? 49  SER A OG  1 
ATOM   380  N  N   . HIS A 1 50  ? 47.903 21.934 47.690 1.00 138.91 ? 50  HIS A N   1 
ATOM   381  C  CA  . HIS A 1 50  ? 46.594 22.006 48.324 1.00 147.43 ? 50  HIS A CA  1 
ATOM   382  C  C   . HIS A 1 50  ? 46.483 20.979 49.455 1.00 145.68 ? 50  HIS A C   1 
ATOM   383  O  O   . HIS A 1 50  ? 46.647 19.775 49.232 1.00 142.42 ? 50  HIS A O   1 
ATOM   384  C  CB  . HIS A 1 50  ? 45.495 21.773 47.288 1.00 160.05 ? 50  HIS A CB  1 
ATOM   385  C  CG  . HIS A 1 50  ? 44.112 21.949 47.829 1.00 168.79 ? 50  HIS A CG  1 
ATOM   386  N  ND1 . HIS A 1 50  ? 43.600 23.180 48.176 1.00 171.50 ? 50  HIS A ND1 1 
ATOM   387  C  CD2 . HIS A 1 50  ? 43.135 21.048 48.085 1.00 179.99 ? 50  HIS A CD2 1 
ATOM   388  C  CE1 . HIS A 1 50  ? 42.366 23.030 48.623 1.00 176.58 ? 50  HIS A CE1 1 
ATOM   389  N  NE2 . HIS A 1 50  ? 42.059 21.746 48.577 1.00 181.41 ? 50  HIS A NE2 1 
ATOM   390  N  N   . GLY A 1 51  ? 46.085 21.454 50.636 1.00 142.97 ? 51  GLY A N   1 
ATOM   391  C  CA  . GLY A 1 51  ? 45.898 20.618 51.815 1.00 142.60 ? 51  GLY A CA  1 
ATOM   392  C  C   . GLY A 1 51  ? 47.070 19.968 52.533 1.00 136.77 ? 51  GLY A C   1 
ATOM   393  O  O   . GLY A 1 51  ? 46.920 18.886 53.097 1.00 146.22 ? 51  GLY A O   1 
ATOM   394  N  N   . SER A 1 52  ? 48.231 20.614 52.519 1.00 125.48 ? 52  SER A N   1 
ATOM   395  C  CA  . SER A 1 52  ? 49.426 20.085 53.181 1.00 120.19 ? 52  SER A CA  1 
ATOM   396  C  C   . SER A 1 52  ? 49.312 20.237 54.683 1.00 109.94 ? 52  SER A C   1 
ATOM   397  O  O   . SER A 1 52  ? 48.785 21.239 55.172 1.00 113.29 ? 52  SER A O   1 
ATOM   398  C  CB  . SER A 1 52  ? 50.676 20.818 52.708 1.00 128.89 ? 52  SER A CB  1 
ATOM   399  O  OG  . SER A 1 52  ? 50.841 20.674 51.310 1.00 144.23 ? 52  SER A OG  1 
ATOM   400  N  N   . ALA A 1 53  ? 49.823 19.248 55.409 1.00 101.62 ? 53  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 53  ? 49.829 19.286 56.869 1.00 101.05 ? 53  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 53  ? 50.766 20.362 57.419 1.00 93.74  ? 53  ALA A C   1 
ATOM   403  O  O   . ALA A 1 53  ? 50.565 20.848 58.534 1.00 96.21  ? 53  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 53  ? 50.213 17.926 57.428 1.00 109.91 ? 53  ALA A CB  1 
ATOM   405  N  N   . GLN A 1 54  ? 51.786 20.720 56.640 1.00 84.16  ? 54  GLN A N   1 
ATOM   406  C  CA  . GLN A 1 54  ? 52.725 21.774 57.011 1.00 77.28  ? 54  GLN A CA  1 
ATOM   407  C  C   . GLN A 1 54  ? 52.026 23.128 57.127 1.00 66.04  ? 54  GLN A C   1 
ATOM   408  O  O   . GLN A 1 54  ? 52.152 23.815 58.144 1.00 64.70  ? 54  GLN A O   1 
ATOM   409  C  CB  . GLN A 1 54  ? 53.853 21.852 55.978 1.00 83.98  ? 54  GLN A CB  1 
ATOM   410  C  CG  . GLN A 1 54  ? 55.059 22.669 56.405 1.00 94.67  ? 54  GLN A CG  1 
ATOM   411  C  CD  . GLN A 1 54  ? 55.845 22.007 57.518 1.00 105.35 ? 54  GLN A CD  1 
ATOM   412  O  OE1 . GLN A 1 54  ? 55.651 22.308 58.698 1.00 119.71 ? 54  GLN A OE1 1 
ATOM   413  N  NE2 . GLN A 1 54  ? 56.729 21.089 57.149 1.00 109.68 ? 54  GLN A NE2 1 
ATOM   414  N  N   . VAL A 1 55  ? 51.281 23.488 56.089 1.00 56.86  ? 55  VAL A N   1 
ATOM   415  C  CA  . VAL A 1 55  ? 50.559 24.751 56.060 1.00 52.84  ? 55  VAL A CA  1 
ATOM   416  C  C   . VAL A 1 55  ? 49.472 24.768 57.114 1.00 57.31  ? 55  VAL A C   1 
ATOM   417  O  O   . VAL A 1 55  ? 49.368 25.732 57.869 1.00 61.42  ? 55  VAL A O   1 
ATOM   418  C  CB  . VAL A 1 55  ? 49.967 25.032 54.668 1.00 49.94  ? 55  VAL A CB  1 
ATOM   419  C  CG1 . VAL A 1 55  ? 48.998 26.211 54.685 1.00 48.11  ? 55  VAL A CG1 1 
ATOM   420  C  CG2 . VAL A 1 55  ? 51.097 25.306 53.689 1.00 50.99  ? 55  VAL A CG2 1 
ATOM   421  N  N   . LYS A 1 56  ? 48.671 23.710 57.179 1.00 64.94  ? 56  LYS A N   1 
ATOM   422  C  CA  . LYS A 1 56  ? 47.602 23.631 58.186 1.00 74.70  ? 56  LYS A CA  1 
ATOM   423  C  C   . LYS A 1 56  ? 48.119 23.782 59.618 1.00 67.55  ? 56  LYS A C   1 
ATOM   424  O  O   . LYS A 1 56  ? 47.438 24.356 60.473 1.00 62.44  ? 56  LYS A O   1 
ATOM   425  C  CB  . LYS A 1 56  ? 46.814 22.328 58.047 1.00 89.95  ? 56  LYS A CB  1 
ATOM   426  C  CG  . LYS A 1 56  ? 45.940 22.288 56.803 1.00 107.77 ? 56  LYS A CG  1 
ATOM   427  C  CD  . LYS A 1 56  ? 45.118 21.007 56.716 1.00 125.06 ? 56  LYS A CD  1 
ATOM   428  C  CE  . LYS A 1 56  ? 43.902 21.024 57.638 1.00 137.05 ? 56  LYS A CE  1 
ATOM   429  N  NZ  . LYS A 1 56  ? 42.906 22.083 57.296 1.00 139.04 ? 56  LYS A NZ  1 
ATOM   430  N  N   . GLY A 1 57  ? 49.323 23.264 59.859 1.00 66.58  ? 57  GLY A N   1 
ATOM   431  C  CA  . GLY A 1 57  ? 49.994 23.389 61.146 1.00 65.39  ? 57  GLY A CA  1 
ATOM   432  C  C   . GLY A 1 57  ? 50.453 24.805 61.402 1.00 62.04  ? 57  GLY A C   1 
ATOM   433  O  O   . GLY A 1 57  ? 50.232 25.347 62.487 1.00 67.37  ? 57  GLY A O   1 
ATOM   434  N  N   . HIS A 1 58  ? 51.081 25.408 60.397 1.00 53.18  ? 58  HIS A N   1 
ATOM   435  C  CA  . HIS A 1 58  ? 51.566 26.783 60.513 1.00 47.05  ? 58  HIS A CA  1 
ATOM   436  C  C   . HIS A 1 58  ? 50.445 27.772 60.843 1.00 41.65  ? 58  HIS A C   1 
ATOM   437  O  O   . HIS A 1 58  ? 50.597 28.626 61.717 1.00 39.47  ? 58  HIS A O   1 
ATOM   438  C  CB  . HIS A 1 58  ? 52.262 27.207 59.229 1.00 45.13  ? 58  HIS A CB  1 
ATOM   439  C  CG  . HIS A 1 58  ? 52.974 28.506 59.355 1.00 44.76  ? 58  HIS A CG  1 
ATOM   440  N  ND1 . HIS A 1 58  ? 52.364 29.715 59.106 1.00 44.17  ? 58  HIS A ND1 1 
ATOM   441  C  CD2 . HIS A 1 58  ? 54.235 28.792 59.748 1.00 47.79  ? 58  HIS A CD2 1 
ATOM   442  C  CE1 . HIS A 1 58  ? 53.227 30.691 59.317 1.00 46.25  ? 58  HIS A CE1 1 
ATOM   443  N  NE2 . HIS A 1 58  ? 54.370 30.158 59.711 1.00 48.38  ? 58  HIS A NE2 1 
ATOM   444  N  N   . GLY A 1 59  ? 49.326 27.629 60.141 1.00 37.09  ? 59  GLY A N   1 
ATOM   445  C  CA  . GLY A 1 59  ? 48.162 28.453 60.360 1.00 35.37  ? 59  GLY A CA  1 
ATOM   446  C  C   . GLY A 1 59  ? 47.644 28.385 61.776 1.00 35.71  ? 59  GLY A C   1 
ATOM   447  O  O   . GLY A 1 59  ? 47.086 29.358 62.277 1.00 36.82  ? 59  GLY A O   1 
ATOM   448  N  N   . LYS A 1 60  ? 47.804 27.241 62.424 1.00 38.75  ? 60  LYS A N   1 
ATOM   449  C  CA  . LYS A 1 60  ? 47.412 27.117 63.812 1.00 43.36  ? 60  LYS A CA  1 
ATOM   450  C  C   . LYS A 1 60  ? 48.227 28.068 64.638 1.00 39.86  ? 60  LYS A C   1 
ATOM   451  O  O   . LYS A 1 60  ? 47.676 28.800 65.456 1.00 39.26  ? 60  LYS A O   1 
ATOM   452  C  CB  . LYS A 1 60  ? 47.622 25.690 64.312 1.00 55.69  ? 60  LYS A CB  1 
ATOM   453  C  CG  . LYS A 1 60  ? 47.128 25.415 65.724 1.00 67.59  ? 60  LYS A CG  1 
ATOM   454  C  CD  . LYS A 1 60  ? 45.655 25.762 65.897 1.00 79.84  ? 60  LYS A CD  1 
ATOM   455  C  CE  . LYS A 1 60  ? 45.065 25.135 67.156 1.00 94.10  ? 60  LYS A CE  1 
ATOM   456  N  NZ  . LYS A 1 60  ? 45.555 25.753 68.426 1.00 98.93  ? 60  LYS A NZ  1 
ATOM   457  N  N   . LYS A 1 61  ? 49.537 28.070 64.404 1.00 38.99  ? 61  LYS A N   1 
ATOM   458  C  CA  . LYS A 1 61  ? 50.457 28.903 65.177 1.00 39.26  ? 61  LYS A CA  1 
ATOM   459  C  C   . LYS A 1 61  ? 50.150 30.399 65.046 1.00 33.08  ? 61  LYS A C   1 
ATOM   460  O  O   . LYS A 1 61  ? 49.935 31.079 66.057 1.00 31.31  ? 61  LYS A O   1 
ATOM   461  C  CB  . LYS A 1 61  ? 51.906 28.601 64.797 1.00 46.20  ? 61  LYS A CB  1 
ATOM   462  C  CG  . LYS A 1 61  ? 52.371 27.235 65.266 1.00 54.48  ? 61  LYS A CG  1 
ATOM   463  C  CD  . LYS A 1 61  ? 53.800 26.955 64.831 1.00 63.48  ? 61  LYS A CD  1 
ATOM   464  C  CE  . LYS A 1 61  ? 54.184 25.495 65.020 1.00 76.71  ? 61  LYS A CE  1 
ATOM   465  N  NZ  . LYS A 1 61  ? 53.438 24.546 64.137 1.00 81.68  ? 61  LYS A NZ  1 
ATOM   466  N  N   . VAL A 1 62  ? 50.092 30.879 63.802 1.00 26.86  ? 62  VAL A N   1 
ATOM   467  C  CA  . VAL A 1 62  ? 49.716 32.262 63.499 1.00 23.00  ? 62  VAL A CA  1 
ATOM   468  C  C   . VAL A 1 62  ? 48.457 32.634 64.232 1.00 24.02  ? 62  VAL A C   1 
ATOM   469  O  O   . VAL A 1 62  ? 48.425 33.605 64.973 1.00 24.39  ? 62  VAL A O   1 
ATOM   470  C  CB  . VAL A 1 62  ? 49.419 32.472 62.017 1.00 20.72  ? 62  VAL A CB  1 
ATOM   471  C  CG1 . VAL A 1 62  ? 48.835 33.853 61.757 1.00 20.17  ? 62  VAL A CG1 1 
ATOM   472  C  CG2 . VAL A 1 62  ? 50.675 32.289 61.210 1.00 21.57  ? 62  VAL A CG2 1 
ATOM   473  N  N   . ALA A 1 63  ? 47.411 31.856 64.024 1.00 26.71  ? 63  ALA A N   1 
ATOM   474  C  CA  . ALA A 1 63  ? 46.137 32.158 64.635 1.00 30.31  ? 63  ALA A CA  1 
ATOM   475  C  C   . ALA A 1 63  ? 46.236 32.240 66.160 1.00 34.43  ? 63  ALA A C   1 
ATOM   476  O  O   . ALA A 1 63  ? 45.561 33.060 66.776 1.00 34.52  ? 63  ALA A O   1 
ATOM   477  C  CB  . ALA A 1 63  ? 45.100 31.139 64.219 1.00 30.35  ? 63  ALA A CB  1 
ATOM   478  N  N   . ASP A 1 64  ? 47.085 31.417 66.762 1.00 41.49  ? 64  ASP A N   1 
ATOM   479  C  CA  . ASP A 1 64  ? 47.284 31.482 68.200 1.00 51.26  ? 64  ASP A CA  1 
ATOM   480  C  C   . ASP A 1 64  ? 48.068 32.701 68.657 1.00 48.86  ? 64  ASP A C   1 
ATOM   481  O  O   . ASP A 1 64  ? 47.721 33.307 69.678 1.00 49.74  ? 64  ASP A O   1 
ATOM   482  C  CB  . ASP A 1 64  ? 47.936 30.202 68.706 1.00 68.85  ? 64  ASP A CB  1 
ATOM   483  C  CG  . ASP A 1 64  ? 46.975 29.005 68.676 1.00 91.11  ? 64  ASP A CG  1 
ATOM   484  O  OD1 . ASP A 1 64  ? 45.762 29.184 68.382 1.00 95.56  ? 64  ASP A OD1 1 
ATOM   485  O  OD2 . ASP A 1 64  ? 47.437 27.874 68.958 1.00 106.73 ? 64  ASP A OD2 1 
ATOM   486  N  N   . ALA A 1 65  ? 49.103 33.076 67.905 1.00 43.23  ? 65  ALA A N   1 
ATOM   487  C  CA  . ALA A 1 65  ? 49.863 34.307 68.188 1.00 37.69  ? 65  ALA A CA  1 
ATOM   488  C  C   . ALA A 1 65  ? 48.984 35.552 68.160 1.00 32.48  ? 65  ALA A C   1 
ATOM   489  O  O   . ALA A 1 65  ? 49.168 36.450 68.968 1.00 31.35  ? 65  ALA A O   1 
ATOM   490  C  CB  . ALA A 1 65  ? 51.010 34.466 67.203 1.00 37.48  ? 65  ALA A CB  1 
ATOM   491  N  N   . LEU A 1 66  ? 48.051 35.598 67.215 1.00 29.91  ? 66  LEU A N   1 
ATOM   492  C  CA  . LEU A 1 66  ? 47.073 36.668 67.156 1.00 30.23  ? 66  LEU A CA  1 
ATOM   493  C  C   . LEU A 1 66  ? 46.103 36.647 68.328 1.00 35.48  ? 66  LEU A C   1 
ATOM   494  O  O   . LEU A 1 66  ? 45.637 37.707 68.754 1.00 36.08  ? 66  LEU A O   1 
ATOM   495  C  CB  . LEU A 1 66  ? 46.251 36.578 65.889 1.00 28.10  ? 66  LEU A CB  1 
ATOM   496  C  CG  . LEU A 1 66  ? 46.905 37.032 64.610 1.00 26.43  ? 66  LEU A CG  1 
ATOM   497  C  CD1 . LEU A 1 66  ? 46.004 36.637 63.457 1.00 25.77  ? 66  LEU A CD1 1 
ATOM   498  C  CD2 . LEU A 1 66  ? 47.138 38.533 64.636 1.00 26.79  ? 66  LEU A CD2 1 
ATOM   499  N  N   . THR A 1 67  ? 45.759 35.452 68.819 1.00 40.30  ? 67  THR A N   1 
ATOM   500  C  CA  . THR A 1 67  ? 44.897 35.323 70.005 1.00 43.08  ? 67  THR A CA  1 
ATOM   501  C  C   . THR A 1 67  ? 45.578 35.907 71.240 1.00 44.94  ? 67  THR A C   1 
ATOM   502  O  O   . THR A 1 67  ? 44.962 36.666 72.001 1.00 44.85  ? 67  THR A O   1 
ATOM   503  C  CB  . THR A 1 67  ? 44.511 33.863 70.299 1.00 43.65  ? 67  THR A CB  1 
ATOM   504  O  OG1 . THR A 1 67  ? 44.198 33.186 69.078 1.00 45.07  ? 67  THR A OG1 1 
ATOM   505  C  CG2 . THR A 1 67  ? 43.297 33.818 71.217 1.00 45.19  ? 67  THR A CG2 1 
ATOM   506  N  N   . ASN A 1 68  ? 46.850 35.550 71.415 1.00 45.55  ? 68  ASN A N   1 
ATOM   507  C  CA  . ASN A 1 68  ? 47.690 36.144 72.449 1.00 46.95  ? 68  ASN A CA  1 
ATOM   508  C  C   . ASN A 1 68  ? 47.749 37.674 72.350 1.00 43.73  ? 68  ASN A C   1 
ATOM   509  O  O   . ASN A 1 68  ? 47.604 38.362 73.356 1.00 45.13  ? 68  ASN A O   1 
ATOM   510  C  CB  . ASN A 1 68  ? 49.107 35.575 72.381 1.00 51.54  ? 68  ASN A CB  1 
ATOM   511  C  CG  . ASN A 1 68  ? 49.980 36.041 73.532 1.00 57.55  ? 68  ASN A CG  1 
ATOM   512  O  OD1 . ASN A 1 68  ? 49.510 36.198 74.664 1.00 61.11  ? 68  ASN A OD1 1 
ATOM   513  N  ND2 . ASN A 1 68  ? 51.262 36.262 73.250 1.00 63.72  ? 68  ASN A ND2 1 
ATOM   514  N  N   . ALA A 1 69  ? 47.954 38.201 71.148 1.00 40.57  ? 69  ALA A N   1 
ATOM   515  C  CA  . ALA A 1 69  ? 47.995 39.648 70.949 1.00 38.75  ? 69  ALA A CA  1 
ATOM   516  C  C   . ALA A 1 69  ? 46.731 40.310 71.437 1.00 39.51  ? 69  ALA A C   1 
ATOM   517  O  O   . ALA A 1 69  ? 46.808 41.357 72.073 1.00 42.34  ? 69  ALA A O   1 
ATOM   518  C  CB  . ALA A 1 69  ? 48.217 40.001 69.490 1.00 38.31  ? 69  ALA A CB  1 
ATOM   519  N  N   . VAL A 1 70  ? 45.574 39.713 71.152 1.00 40.57  ? 70  VAL A N   1 
ATOM   520  C  CA  . VAL A 1 70  ? 44.296 40.321 71.545 1.00 43.07  ? 70  VAL A CA  1 
ATOM   521  C  C   . VAL A 1 70  ? 44.123 40.338 73.063 1.00 47.75  ? 70  VAL A C   1 
ATOM   522  O  O   . VAL A 1 70  ? 43.500 41.258 73.603 1.00 46.22  ? 70  VAL A O   1 
ATOM   523  C  CB  . VAL A 1 70  ? 43.094 39.652 70.854 1.00 41.18  ? 70  VAL A CB  1 
ATOM   524  C  CG1 . VAL A 1 70  ? 41.771 40.190 71.386 1.00 41.35  ? 70  VAL A CG1 1 
ATOM   525  C  CG2 . VAL A 1 70  ? 43.152 39.919 69.365 1.00 41.67  ? 70  VAL A CG2 1 
ATOM   526  N  N   . ALA A 1 71  ? 44.687 39.337 73.739 1.00 53.90  ? 71  ALA A N   1 
ATOM   527  C  CA  . ALA A 1 71  ? 44.701 39.293 75.208 1.00 59.59  ? 71  ALA A CA  1 
ATOM   528  C  C   . ALA A 1 71  ? 45.392 40.506 75.843 1.00 61.39  ? 71  ALA A C   1 
ATOM   529  O  O   . ALA A 1 71  ? 44.883 41.069 76.814 1.00 63.37  ? 71  ALA A O   1 
ATOM   530  C  CB  . ALA A 1 71  ? 45.363 38.010 75.697 1.00 61.91  ? 71  ALA A CB  1 
ATOM   531  N  N   . HIS A 1 72  ? 46.540 40.895 75.288 1.00 62.65  ? 72  HIS A N   1 
ATOM   532  C  CA  . HIS A 1 72  ? 47.328 42.024 75.788 1.00 63.35  ? 72  HIS A CA  1 
ATOM   533  C  C   . HIS A 1 72  ? 47.275 43.199 74.805 1.00 57.74  ? 72  HIS A C   1 
ATOM   534  O  O   . HIS A 1 72  ? 48.311 43.780 74.476 1.00 56.74  ? 72  HIS A O   1 
ATOM   535  C  CB  . HIS A 1 72  ? 48.803 41.609 75.991 1.00 69.93  ? 72  HIS A CB  1 
ATOM   536  C  CG  . HIS A 1 72  ? 48.993 40.332 76.748 1.00 76.06  ? 72  HIS A CG  1 
ATOM   537  N  ND1 . HIS A 1 72  ? 48.807 40.239 78.110 1.00 88.28  ? 72  HIS A ND1 1 
ATOM   538  C  CD2 . HIS A 1 72  ? 49.391 39.104 76.338 1.00 77.98  ? 72  HIS A CD2 1 
ATOM   539  C  CE1 . HIS A 1 72  ? 49.060 39.003 78.504 1.00 93.28  ? 72  HIS A CE1 1 
ATOM   540  N  NE2 . HIS A 1 72  ? 49.416 38.294 77.447 1.00 86.47  ? 72  HIS A NE2 1 
ATOM   541  N  N   . VAL A 1 73  ? 46.086 43.584 74.352 1.00 57.27  ? 73  VAL A N   1 
ATOM   542  C  CA  . VAL A 1 73  ? 45.981 44.638 73.324 1.00 62.90  ? 73  VAL A CA  1 
ATOM   543  C  C   . VAL A 1 73  ? 46.490 46.023 73.787 1.00 69.54  ? 73  VAL A C   1 
ATOM   544  O  O   . VAL A 1 73  ? 46.621 46.942 72.978 1.00 64.83  ? 73  VAL A O   1 
ATOM   545  C  CB  . VAL A 1 73  ? 44.536 44.739 72.766 1.00 64.94  ? 73  VAL A CB  1 
ATOM   546  C  CG1 . VAL A 1 73  ? 43.622 45.527 73.700 1.00 69.89  ? 73  VAL A CG1 1 
ATOM   547  C  CG2 . VAL A 1 73  ? 44.517 45.346 71.370 1.00 64.38  ? 73  VAL A CG2 1 
ATOM   548  N  N   . ASP A 1 74  ? 46.782 46.155 75.083 1.00 87.11  ? 74  ASP A N   1 
ATOM   549  C  CA  . ASP A 1 74  ? 47.250 47.404 75.687 1.00 100.13 ? 74  ASP A CA  1 
ATOM   550  C  C   . ASP A 1 74  ? 48.784 47.523 75.769 1.00 95.55  ? 74  ASP A C   1 
ATOM   551  O  O   . ASP A 1 74  ? 49.321 48.625 75.640 1.00 94.18  ? 74  ASP A O   1 
ATOM   552  C  CB  . ASP A 1 74  ? 46.642 47.540 77.092 1.00 118.15 ? 74  ASP A CB  1 
ATOM   553  C  CG  . ASP A 1 74  ? 45.115 47.373 77.100 1.00 130.13 ? 74  ASP A CG  1 
ATOM   554  O  OD1 . ASP A 1 74  ? 44.447 47.831 76.145 1.00 134.62 ? 74  ASP A OD1 1 
ATOM   555  O  OD2 . ASP A 1 74  ? 44.585 46.783 78.068 1.00 137.41 ? 74  ASP A OD2 1 
ATOM   556  N  N   . ASP A 1 75  ? 49.475 46.403 75.993 1.00 96.60  ? 75  ASP A N   1 
ATOM   557  C  CA  . ASP A 1 75  ? 50.942 46.375 76.115 1.00 101.35 ? 75  ASP A CA  1 
ATOM   558  C  C   . ASP A 1 75  ? 51.535 45.353 75.132 1.00 90.14  ? 75  ASP A C   1 
ATOM   559  O  O   . ASP A 1 75  ? 52.150 44.345 75.510 1.00 90.46  ? 75  ASP A O   1 
ATOM   560  C  CB  . ASP A 1 75  ? 51.333 46.056 77.562 1.00 124.67 ? 75  ASP A CB  1 
ATOM   561  C  CG  . ASP A 1 75  ? 52.833 46.152 77.803 1.00 144.15 ? 75  ASP A CG  1 
ATOM   562  O  OD1 . ASP A 1 75  ? 53.430 47.203 77.478 1.00 156.73 ? 75  ASP A OD1 1 
ATOM   563  O  OD2 . ASP A 1 75  ? 53.413 45.169 78.317 1.00 154.84 ? 75  ASP A OD2 1 
ATOM   564  N  N   . MET A 1 76  ? 51.354 45.649 73.855 1.00 75.87  ? 76  MET A N   1 
ATOM   565  C  CA  . MET A 1 76  ? 51.579 44.681 72.791 1.00 65.94  ? 76  MET A CA  1 
ATOM   566  C  C   . MET A 1 76  ? 53.045 44.398 72.453 1.00 57.24  ? 76  MET A C   1 
ATOM   567  O  O   . MET A 1 76  ? 53.373 43.255 72.154 1.00 57.12  ? 76  MET A O   1 
ATOM   568  C  CB  . MET A 1 76  ? 50.818 45.123 71.545 1.00 68.37  ? 76  MET A CB  1 
ATOM   569  C  CG  . MET A 1 76  ? 50.506 44.013 70.568 1.00 71.83  ? 76  MET A CG  1 
ATOM   570  S  SD  . MET A 1 76  ? 49.624 44.709 69.157 1.00 77.86  ? 76  MET A SD  1 
ATOM   571  C  CE  . MET A 1 76  ? 47.991 44.901 69.863 1.00 76.72  ? 76  MET A CE  1 
ATOM   572  N  N   . PRO A 1 77  ? 53.920 45.427 72.462 1.00 54.15  ? 77  PRO A N   1 
ATOM   573  C  CA  . PRO A 1 77  ? 55.344 45.217 72.173 1.00 55.35  ? 77  PRO A CA  1 
ATOM   574  C  C   . PRO A 1 77  ? 56.111 44.290 73.100 1.00 62.79  ? 77  PRO A C   1 
ATOM   575  O  O   . PRO A 1 77  ? 57.134 43.744 72.688 1.00 66.39  ? 77  PRO A O   1 
ATOM   576  C  CB  . PRO A 1 77  ? 55.926 46.617 72.281 1.00 52.36  ? 77  PRO A CB  1 
ATOM   577  C  CG  . PRO A 1 77  ? 54.821 47.468 71.808 1.00 53.68  ? 77  PRO A CG  1 
ATOM   578  C  CD  . PRO A 1 77  ? 53.604 46.864 72.435 1.00 54.62  ? 77  PRO A CD  1 
ATOM   579  N  N   . ASN A 1 78  ? 55.653 44.115 74.331 1.00 70.75  ? 78  ASN A N   1 
ATOM   580  C  CA  . ASN A 1 78  ? 56.280 43.134 75.209 1.00 80.26  ? 78  ASN A CA  1 
ATOM   581  C  C   . ASN A 1 78  ? 55.820 41.719 74.866 1.00 77.09  ? 78  ASN A C   1 
ATOM   582  O  O   . ASN A 1 78  ? 56.650 40.810 74.734 1.00 74.77  ? 78  ASN A O   1 
ATOM   583  C  CB  . ASN A 1 78  ? 56.016 43.475 76.671 1.00 93.73  ? 78  ASN A CB  1 
ATOM   584  C  CG  . ASN A 1 78  ? 56.742 44.737 77.103 1.00 107.00 ? 78  ASN A CG  1 
ATOM   585  O  OD1 . ASN A 1 78  ? 57.922 44.929 76.792 1.00 112.39 ? 78  ASN A OD1 1 
ATOM   586  N  ND2 . ASN A 1 78  ? 56.042 45.605 77.821 1.00 120.02 ? 78  ASN A ND2 1 
ATOM   587  N  N   . ALA A 1 79  ? 54.506 41.547 74.707 1.00 68.25  ? 79  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 79  ? 53.911 40.245 74.370 1.00 61.77  ? 79  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 79  ? 54.500 39.640 73.101 1.00 54.13  ? 79  ALA A C   1 
ATOM   590  O  O   . ALA A 1 79  ? 54.927 38.491 73.102 1.00 55.73  ? 79  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 79  ? 52.401 40.373 74.228 1.00 63.04  ? 79  ALA A CB  1 
ATOM   592  N  N   . LEU A 1 80  ? 54.550 40.437 72.039 1.00 49.05  ? 80  LEU A N   1 
ATOM   593  C  CA  . LEU A 1 80  ? 55.017 39.990 70.726 1.00 45.88  ? 80  LEU A CA  1 
ATOM   594  C  C   . LEU A 1 80  ? 56.536 40.124 70.508 1.00 46.65  ? 80  LEU A C   1 
ATOM   595  O  O   . LEU A 1 80  ? 56.994 40.262 69.371 1.00 47.06  ? 80  LEU A O   1 
ATOM   596  C  CB  . LEU A 1 80  ? 54.278 40.783 69.643 1.00 42.41  ? 80  LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 80  ? 52.769 40.643 69.550 1.00 40.20  ? 80  LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 80  ? 52.278 41.506 68.403 1.00 38.51  ? 80  LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 80  ? 52.386 39.188 69.325 1.00 40.52  ? 80  LEU A CD2 1 
ATOM   600  N  N   . SER A 1 81  ? 57.327 40.047 71.573 1.00 48.05  ? 81  SER A N   1 
ATOM   601  C  CA  . SER A 1 81  ? 58.742 40.381 71.471 1.00 48.51  ? 81  SER A CA  1 
ATOM   602  C  C   . SER A 1 81  ? 59.581 39.302 70.796 1.00 44.12  ? 81  SER A C   1 
ATOM   603  O  O   . SER A 1 81  ? 60.546 39.624 70.116 1.00 42.80  ? 81  SER A O   1 
ATOM   604  C  CB  . SER A 1 81  ? 59.316 40.685 72.843 1.00 54.86  ? 81  SER A CB  1 
ATOM   605  O  OG  . SER A 1 81  ? 60.696 40.996 72.736 1.00 60.43  ? 81  SER A OG  1 
ATOM   606  N  N   . ALA A 1 82  ? 59.228 38.038 71.000 1.00 41.87  ? 82  ALA A N   1 
ATOM   607  C  CA  . ALA A 1 82  ? 59.913 36.931 70.323 1.00 42.63  ? 82  ALA A CA  1 
ATOM   608  C  C   . ALA A 1 82  ? 59.614 36.871 68.833 1.00 37.73  ? 82  ALA A C   1 
ATOM   609  O  O   . ALA A 1 82  ? 60.449 36.404 68.049 1.00 35.29  ? 82  ALA A O   1 
ATOM   610  C  CB  . ALA A 1 82  ? 59.530 35.604 70.956 1.00 47.81  ? 82  ALA A CB  1 
ATOM   611  N  N   . LEU A 1 83  ? 58.410 37.302 68.460 1.00 32.58  ? 83  LEU A N   1 
ATOM   612  C  CA  . LEU A 1 83  ? 58.006 37.292 67.068 1.00 29.86  ? 83  LEU A CA  1 
ATOM   613  C  C   . LEU A 1 83  ? 58.680 38.381 66.303 1.00 28.35  ? 83  LEU A C   1 
ATOM   614  O  O   . LEU A 1 83  ? 59.151 38.155 65.188 1.00 28.93  ? 83  LEU A O   1 
ATOM   615  C  CB  . LEU A 1 83  ? 56.507 37.442 66.935 1.00 28.86  ? 83  LEU A CB  1 
ATOM   616  C  CG  . LEU A 1 83  ? 55.694 36.283 67.470 1.00 28.93  ? 83  LEU A CG  1 
ATOM   617  C  CD1 . LEU A 1 83  ? 54.254 36.485 67.037 1.00 30.05  ? 83  LEU A CD1 1 
ATOM   618  C  CD2 . LEU A 1 83  ? 56.200 34.940 66.965 1.00 28.65  ? 83  LEU A CD2 1 
ATOM   619  N  N   . SER A 1 84  ? 58.726 39.564 66.890 1.00 27.07  ? 84  SER A N   1 
ATOM   620  C  CA  . SER A 1 84  ? 59.487 40.622 66.298 1.00 28.20  ? 84  SER A CA  1 
ATOM   621  C  C   . SER A 1 84  ? 60.912 40.173 66.055 1.00 30.39  ? 84  SER A C   1 
ATOM   622  O  O   . SER A 1 84  ? 61.450 40.390 64.985 1.00 30.28  ? 84  SER A O   1 
ATOM   623  C  CB  . SER A 1 84  ? 59.495 41.842 67.180 1.00 29.13  ? 84  SER A CB  1 
ATOM   624  O  OG  . SER A 1 84  ? 60.522 42.724 66.754 1.00 30.93  ? 84  SER A OG  1 
ATOM   625  N  N   . ASP A 1 85  ? 61.516 39.527 67.040 1.00 37.66  ? 85  ASP A N   1 
ATOM   626  C  CA  . ASP A 1 85  ? 62.888 39.050 66.893 1.00 44.85  ? 85  ASP A CA  1 
ATOM   627  C  C   . ASP A 1 85  ? 63.055 38.089 65.736 1.00 38.59  ? 85  ASP A C   1 
ATOM   628  O  O   . ASP A 1 85  ? 64.122 38.029 65.145 1.00 38.77  ? 85  ASP A O   1 
ATOM   629  C  CB  . ASP A 1 85  ? 63.392 38.393 68.186 1.00 61.44  ? 85  ASP A CB  1 
ATOM   630  C  CG  . ASP A 1 85  ? 63.557 39.401 69.344 1.00 84.59  ? 85  ASP A CG  1 
ATOM   631  O  OD1 . ASP A 1 85  ? 63.374 40.626 69.125 1.00 98.99  ? 85  ASP A OD1 1 
ATOM   632  O  OD2 . ASP A 1 85  ? 63.863 38.966 70.483 1.00 93.95  ? 85  ASP A OD2 1 
ATOM   633  N  N   . LEU A 1 86  ? 62.001 37.346 65.416 1.00 35.50  ? 86  LEU A N   1 
ATOM   634  C  CA  . LEU A 1 86  ? 62.023 36.363 64.330 1.00 32.15  ? 86  LEU A CA  1 
ATOM   635  C  C   . LEU A 1 86  ? 61.731 36.993 62.979 1.00 27.68  ? 86  LEU A C   1 
ATOM   636  O  O   . LEU A 1 86  ? 62.544 36.856 62.061 1.00 28.64  ? 86  LEU A O   1 
ATOM   637  C  CB  . LEU A 1 86  ? 61.007 35.258 64.606 1.00 33.75  ? 86  LEU A CB  1 
ATOM   638  C  CG  . LEU A 1 86  ? 61.275 33.920 63.936 1.00 35.32  ? 86  LEU A CG  1 
ATOM   639  C  CD1 . LEU A 1 86  ? 60.426 32.875 64.639 1.00 41.05  ? 86  LEU A CD1 1 
ATOM   640  C  CD2 . LEU A 1 86  ? 60.950 33.926 62.460 1.00 35.43  ? 86  LEU A CD2 1 
ATOM   641  N  N   . HIS A 1 87  ? 60.572 37.648 62.840 1.00 21.13  ? 87  HIS A N   1 
ATOM   642  C  CA  . HIS A 1 87  ? 60.194 38.203 61.556 1.00 17.30  ? 87  HIS A CA  1 
ATOM   643  C  C   . HIS A 1 87  ? 61.102 39.379 61.175 1.00 17.17  ? 87  HIS A C   1 
ATOM   644  O  O   . HIS A 1 87  ? 61.316 39.599 60.000 1.00 17.57  ? 87  HIS A O   1 
ATOM   645  C  CB  . HIS A 1 87  ? 58.714 38.586 61.493 1.00 14.94  ? 87  HIS A CB  1 
ATOM   646  C  CG  . HIS A 1 87  ? 57.755 37.427 61.530 1.00 13.53  ? 87  HIS A CG  1 
ATOM   647  N  ND1 . HIS A 1 87  ? 57.173 37.012 62.695 1.00 12.97  ? 87  HIS A ND1 1 
ATOM   648  C  CD2 . HIS A 1 87  ? 57.218 36.643 60.551 1.00 13.22  ? 87  HIS A CD2 1 
ATOM   649  C  CE1 . HIS A 1 87  ? 56.334 36.020 62.446 1.00 13.13  ? 87  HIS A CE1 1 
ATOM   650  N  NE2 . HIS A 1 87  ? 56.317 35.774 61.144 1.00 12.77  ? 87  HIS A NE2 1 
ATOM   651  N  N   . ALA A 1 88  ? 61.679 40.103 62.133 1.00 18.91  ? 88  ALA A N   1 
ATOM   652  C  CA  . ALA A 1 88  ? 62.427 41.342 61.815 1.00 21.66  ? 88  ALA A CA  1 
ATOM   653  C  C   . ALA A 1 88  ? 63.933 41.203 61.723 1.00 24.20  ? 88  ALA A C   1 
ATOM   654  O  O   . ALA A 1 88  ? 64.517 41.744 60.793 1.00 24.67  ? 88  ALA A O   1 
ATOM   655  C  CB  . ALA A 1 88  ? 62.084 42.461 62.795 1.00 22.03  ? 88  ALA A CB  1 
ATOM   656  N  N   . HIS A 1 89  ? 64.565 40.542 62.692 1.00 29.54  ? 89  HIS A N   1 
ATOM   657  C  CA  . HIS A 1 89  ? 66.023 40.390 62.680 1.00 35.29  ? 89  HIS A CA  1 
ATOM   658  C  C   . HIS A 1 89  ? 66.455 39.280 61.758 1.00 37.17  ? 89  HIS A C   1 
ATOM   659  O  O   . HIS A 1 89  ? 67.285 39.497 60.883 1.00 40.43  ? 89  HIS A O   1 
ATOM   660  C  CB  . HIS A 1 89  ? 66.586 40.111 64.061 1.00 42.08  ? 89  HIS A CB  1 
ATOM   661  C  CG  . HIS A 1 89  ? 66.335 41.205 65.044 1.00 54.17  ? 89  HIS A CG  1 
ATOM   662  N  ND1 . HIS A 1 89  ? 65.109 41.403 65.645 1.00 58.03  ? 89  HIS A ND1 1 
ATOM   663  C  CD2 . HIS A 1 89  ? 67.157 42.161 65.542 1.00 65.02  ? 89  HIS A CD2 1 
ATOM   664  C  CE1 . HIS A 1 89  ? 65.184 42.435 66.469 1.00 61.73  ? 89  HIS A CE1 1 
ATOM   665  N  NE2 . HIS A 1 89  ? 66.416 42.914 66.424 1.00 64.58  ? 89  HIS A NE2 1 
ATOM   666  N  N   . LYS A 1 90  ? 65.896 38.092 61.956 1.00 39.93  ? 90  LYS A N   1 
ATOM   667  C  CA  . LYS A 1 90  ? 66.361 36.900 61.264 1.00 42.72  ? 90  LYS A CA  1 
ATOM   668  C  C   . LYS A 1 90  ? 65.811 36.808 59.844 1.00 38.14  ? 90  LYS A C   1 
ATOM   669  O  O   . LYS A 1 90  ? 66.579 36.793 58.885 1.00 39.52  ? 90  LYS A O   1 
ATOM   670  C  CB  . LYS A 1 90  ? 65.987 35.662 62.065 1.00 53.66  ? 90  LYS A CB  1 
ATOM   671  C  CG  . LYS A 1 90  ? 66.575 34.374 61.516 1.00 68.42  ? 90  LYS A CG  1 
ATOM   672  C  CD  . LYS A 1 90  ? 66.378 33.206 62.481 1.00 83.38  ? 90  LYS A CD  1 
ATOM   673  C  CE  . LYS A 1 90  ? 64.984 32.586 62.384 1.00 91.14  ? 90  LYS A CE  1 
ATOM   674  N  NZ  . LYS A 1 90  ? 64.812 31.704 61.189 1.00 91.68  ? 90  LYS A NZ  1 
ATOM   675  N  N   . LEU A 1 91  ? 64.489 36.755 59.714 1.00 33.76  ? 91  LEU A N   1 
ATOM   676  C  CA  . LEU A 1 91  ? 63.841 36.563 58.409 1.00 31.22  ? 91  LEU A CA  1 
ATOM   677  C  C   . LEU A 1 91  ? 63.842 37.768 57.494 1.00 29.56  ? 91  LEU A C   1 
ATOM   678  O  O   . LEU A 1 91  ? 63.894 37.600 56.280 1.00 31.33  ? 91  LEU A O   1 
ATOM   679  C  CB  . LEU A 1 91  ? 62.393 36.128 58.584 1.00 30.02  ? 91  LEU A CB  1 
ATOM   680  C  CG  . LEU A 1 91  ? 62.222 34.713 59.088 1.00 29.52  ? 91  LEU A CG  1 
ATOM   681  C  CD1 . LEU A 1 91  ? 60.741 34.428 59.266 1.00 28.99  ? 91  LEU A CD1 1 
ATOM   682  C  CD2 . LEU A 1 91  ? 62.861 33.739 58.109 1.00 30.70  ? 91  LEU A CD2 1 
ATOM   683  N  N   . ARG A 1 92  ? 63.733 38.963 58.067 1.00 27.60  ? 92  ARG A N   1 
ATOM   684  C  CA  . ARG A 1 92  ? 63.693 40.207 57.309 1.00 26.38  ? 92  ARG A CA  1 
ATOM   685  C  C   . ARG A 1 92  ? 62.584 40.177 56.261 1.00 21.66  ? 92  ARG A C   1 
ATOM   686  O  O   . ARG A 1 92  ? 62.823 40.256 55.061 1.00 20.91  ? 92  ARG A O   1 
ATOM   687  C  CB  . ARG A 1 92  ? 65.067 40.517 56.716 1.00 31.12  ? 92  ARG A CB  1 
ATOM   688  C  CG  . ARG A 1 92  ? 66.133 40.674 57.793 1.00 39.60  ? 92  ARG A CG  1 
ATOM   689  C  CD  . ARG A 1 92  ? 67.502 41.062 57.252 1.00 49.45  ? 92  ARG A CD  1 
ATOM   690  N  NE  . ARG A 1 92  ? 68.047 40.002 56.391 1.00 61.50  ? 92  ARG A NE  1 
ATOM   691  C  CZ  . ARG A 1 92  ? 68.911 39.044 56.751 1.00 69.23  ? 92  ARG A CZ  1 
ATOM   692  N  NH1 . ARG A 1 92  ? 69.399 38.964 57.993 1.00 74.87  ? 92  ARG A NH1 1 
ATOM   693  N  NH2 . ARG A 1 92  ? 69.300 38.145 55.842 1.00 66.49  ? 92  ARG A NH2 1 
ATOM   694  N  N   . VAL A 1 93  ? 61.364 40.026 56.749 1.00 18.64  ? 93  VAL A N   1 
ATOM   695  C  CA  . VAL A 1 93  ? 60.184 40.116 55.915 1.00 17.43  ? 93  VAL A CA  1 
ATOM   696  C  C   . VAL A 1 93  ? 59.986 41.596 55.780 1.00 17.07  ? 93  VAL A C   1 
ATOM   697  O  O   . VAL A 1 93  ? 60.154 42.321 56.771 1.00 16.38  ? 93  VAL A O   1 
ATOM   698  C  CB  . VAL A 1 93  ? 58.935 39.484 56.580 1.00 16.72  ? 93  VAL A CB  1 
ATOM   699  C  CG1 . VAL A 1 93  ? 57.708 39.588 55.677 1.00 16.07  ? 93  VAL A CG1 1 
ATOM   700  C  CG2 . VAL A 1 93  ? 59.203 38.028 56.916 1.00 16.65  ? 93  VAL A CG2 1 
ATOM   701  N  N   . ASP A 1 94  ? 59.650 42.051 54.571 1.00 17.38  ? 94  ASP A N   1 
ATOM   702  C  CA  . ASP A 1 94  ? 59.417 43.479 54.349 1.00 18.05  ? 94  ASP A CA  1 
ATOM   703  C  C   . ASP A 1 94  ? 57.969 43.779 54.508 1.00 16.62  ? 94  ASP A C   1 
ATOM   704  O  O   . ASP A 1 94  ? 57.130 42.914 54.257 1.00 16.48  ? 94  ASP A O   1 
ATOM   705  C  CB  . ASP A 1 94  ? 59.887 43.950 52.982 1.00 20.39  ? 94  ASP A CB  1 
ATOM   706  C  CG  . ASP A 1 94  ? 58.975 43.545 51.887 1.00 22.53  ? 94  ASP A CG  1 
ATOM   707  O  OD1 . ASP A 1 94  ? 58.661 42.324 51.850 1.00 23.55  ? 94  ASP A OD1 1 
ATOM   708  O  OD2 . ASP A 1 94  ? 58.599 44.443 51.078 1.00 22.86  ? 94  ASP A OD2 1 
ATOM   709  N  N   . PRO A 1 95  ? 57.661 45.018 54.884 1.00 15.78  ? 95  PRO A N   1 
ATOM   710  C  CA  . PRO A 1 95  ? 56.391 45.207 55.539 1.00 16.80  ? 95  PRO A CA  1 
ATOM   711  C  C   . PRO A 1 95  ? 55.170 45.185 54.589 1.00 17.56  ? 95  PRO A C   1 
ATOM   712  O  O   . PRO A 1 95  ? 54.033 45.045 55.060 1.00 17.87  ? 95  PRO A O   1 
ATOM   713  C  CB  . PRO A 1 95  ? 56.580 46.554 56.254 1.00 16.19  ? 95  PRO A CB  1 
ATOM   714  C  CG  . PRO A 1 95  ? 58.034 46.858 56.122 1.00 15.41  ? 95  PRO A CG  1 
ATOM   715  C  CD  . PRO A 1 95  ? 58.382 46.283 54.808 1.00 14.90  ? 95  PRO A CD  1 
ATOM   716  N  N   . VAL A 1 96  ? 55.420 45.298 53.283 1.00 17.11  ? 96  VAL A N   1 
ATOM   717  C  CA  . VAL A 1 96  ? 54.416 45.036 52.248 1.00 16.90  ? 96  VAL A CA  1 
ATOM   718  C  C   . VAL A 1 96  ? 53.709 43.706 52.378 1.00 15.78  ? 96  VAL A C   1 
ATOM   719  O  O   . VAL A 1 96  ? 52.511 43.624 52.103 1.00 16.79  ? 96  VAL A O   1 
ATOM   720  C  CB  . VAL A 1 96  ? 55.077 45.069 50.861 1.00 18.75  ? 96  VAL A CB  1 
ATOM   721  C  CG1 . VAL A 1 96  ? 54.272 44.349 49.772 1.00 18.63  ? 96  VAL A CG1 1 
ATOM   722  C  CG2 . VAL A 1 96  ? 55.303 46.521 50.493 1.00 21.18  ? 96  VAL A CG2 1 
ATOM   723  N  N   . ASN A 1 97  ? 54.432 42.664 52.761 1.00 13.55  ? 97  ASN A N   1 
ATOM   724  C  CA  . ASN A 1 97  ? 53.835 41.349 52.798 1.00 12.42  ? 97  ASN A CA  1 
ATOM   725  C  C   . ASN A 1 97  ? 52.927 41.192 53.976 1.00 11.93  ? 97  ASN A C   1 
ATOM   726  O  O   . ASN A 1 97  ? 52.114 40.283 53.979 1.00 12.02  ? 97  ASN A O   1 
ATOM   727  C  CB  . ASN A 1 97  ? 54.889 40.275 52.850 1.00 12.74  ? 97  ASN A CB  1 
ATOM   728  C  CG  . ASN A 1 97  ? 55.876 40.366 51.707 1.00 13.20  ? 97  ASN A CG  1 
ATOM   729  O  OD1 . ASN A 1 97  ? 57.013 39.925 51.843 1.00 13.32  ? 97  ASN A OD1 1 
ATOM   730  N  ND2 . ASN A 1 97  ? 55.459 40.957 50.580 1.00 13.50  ? 97  ASN A ND2 1 
ATOM   731  N  N   . PHE A 1 98  ? 53.059 42.052 54.986 1.00 11.79  ? 98  PHE A N   1 
ATOM   732  C  CA  . PHE A 1 98  ? 52.088 42.085 56.077 1.00 11.82  ? 98  PHE A CA  1 
ATOM   733  C  C   . PHE A 1 98  ? 50.752 42.591 55.631 1.00 13.74  ? 98  PHE A C   1 
ATOM   734  O  O   . PHE A 1 98  ? 49.734 42.073 56.051 1.00 14.40  ? 98  PHE A O   1 
ATOM   735  C  CB  . PHE A 1 98  ? 52.598 42.891 57.238 1.00 10.58  ? 98  PHE A CB  1 
ATOM   736  C  CG  . PHE A 1 98  ? 53.569 42.144 58.024 1.00 9.83   ? 98  PHE A CG  1 
ATOM   737  C  CD1 . PHE A 1 98  ? 53.132 41.276 58.997 1.00 9.54   ? 98  PHE A CD1 1 
ATOM   738  C  CD2 . PHE A 1 98  ? 54.913 42.209 57.719 1.00 9.54   ? 98  PHE A CD2 1 
ATOM   739  C  CE1 . PHE A 1 98  ? 54.026 40.507 59.708 1.00 9.65   ? 98  PHE A CE1 1 
ATOM   740  C  CE2 . PHE A 1 98  ? 55.821 41.431 58.412 1.00 9.70   ? 98  PHE A CE2 1 
ATOM   741  C  CZ  . PHE A 1 98  ? 55.380 40.583 59.420 1.00 9.74   ? 98  PHE A CZ  1 
ATOM   742  N  N   . LYS A 1 99  ? 50.756 43.570 54.744 1.00 16.62  ? 99  LYS A N   1 
ATOM   743  C  CA  . LYS A 1 99  ? 49.527 44.074 54.192 1.00 19.38  ? 99  LYS A CA  1 
ATOM   744  C  C   . LYS A 1 99  ? 48.740 43.089 53.355 1.00 17.45  ? 99  LYS A C   1 
ATOM   745  O  O   . LYS A 1 99  ? 47.561 43.324 53.123 1.00 18.43  ? 99  LYS A O   1 
ATOM   746  C  CB  . LYS A 1 99  ? 49.791 45.314 53.380 1.00 25.71  ? 99  LYS A CB  1 
ATOM   747  C  CG  . LYS A 1 99  ? 50.084 46.507 54.267 1.00 34.95  ? 99  LYS A CG  1 
ATOM   748  C  CD  . LYS A 1 99  ? 50.695 47.672 53.494 1.00 46.49  ? 99  LYS A CD  1 
ATOM   749  C  CE  . LYS A 1 99  ? 49.767 48.213 52.401 1.00 55.78  ? 99  LYS A CE  1 
ATOM   750  N  NZ  . LYS A 1 99  ? 50.410 49.320 51.633 1.00 61.59  ? 99  LYS A NZ  1 
ATOM   751  N  N   . LEU A 1 100 ? 49.353 42.006 52.896 1.00 15.22  ? 100 LEU A N   1 
ATOM   752  C  CA  . LEU A 1 100 ? 48.632 41.017 52.103 1.00 14.02  ? 100 LEU A CA  1 
ATOM   753  C  C   . LEU A 1 100 ? 48.088 39.915 52.993 1.00 13.27  ? 100 LEU A C   1 
ATOM   754  O  O   . LEU A 1 100 ? 46.989 39.425 52.751 1.00 13.35  ? 100 LEU A O   1 
ATOM   755  C  CB  . LEU A 1 100 ? 49.524 40.424 51.022 1.00 14.01  ? 100 LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 100 ? 50.317 41.435 50.191 1.00 14.02  ? 100 LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 100 ? 51.477 40.770 49.470 1.00 14.00  ? 100 LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 100 ? 49.396 42.145 49.214 1.00 14.30  ? 100 LEU A CD2 1 
ATOM   759  N  N   . LEU A 1 101 ? 48.838 39.505 54.010 1.00 12.50  ? 101 LEU A N   1 
ATOM   760  C  CA  . LEU A 1 101 ? 48.306 38.537 54.953 1.00 12.40  ? 101 LEU A CA  1 
ATOM   761  C  C   . LEU A 1 101 ? 47.204 39.130 55.812 1.00 12.70  ? 101 LEU A C   1 
ATOM   762  O  O   . LEU A 1 101 ? 46.341 38.387 56.274 1.00 13.49  ? 101 LEU A O   1 
ATOM   763  C  CB  . LEU A 1 101 ? 49.371 38.009 55.892 1.00 12.65  ? 101 LEU A CB  1 
ATOM   764  C  CG  . LEU A 1 101 ? 48.935 36.863 56.819 1.00 12.85  ? 101 LEU A CG  1 
ATOM   765  C  CD1 . LEU A 1 101 ? 48.282 35.737 56.045 1.00 13.09  ? 101 LEU A CD1 1 
ATOM   766  C  CD2 . LEU A 1 101 ? 50.126 36.306 57.558 1.00 12.96  ? 101 LEU A CD2 1 
ATOM   767  N  N   . SER A 1 102 ? 47.237 40.441 56.049 1.00 11.97  ? 102 SER A N   1 
ATOM   768  C  CA  . SER A 1 102 ? 46.178 41.107 56.789 1.00 11.43  ? 102 SER A CA  1 
ATOM   769  C  C   . SER A 1 102 ? 44.945 41.249 55.985 1.00 11.20  ? 102 SER A C   1 
ATOM   770  O  O   . SER A 1 102 ? 43.862 41.197 56.530 1.00 11.06  ? 102 SER A O   1 
ATOM   771  C  CB  . SER A 1 102 ? 46.604 42.484 57.204 1.00 12.16  ? 102 SER A CB  1 
ATOM   772  O  OG  . SER A 1 102 ? 47.686 42.402 58.122 1.00 13.20  ? 102 SER A OG  1 
ATOM   773  N  N   . HIS A 1 103 ? 45.104 41.461 54.687 1.00 12.18  ? 103 HIS A N   1 
ATOM   774  C  CA  . HIS A 1 103 ? 43.969 41.461 53.744 1.00 13.31  ? 103 HIS A CA  1 
ATOM   775  C  C   . HIS A 1 103 ? 43.297 40.105 53.611 1.00 14.23  ? 103 HIS A C   1 
ATOM   776  O  O   . HIS A 1 103 ? 42.072 40.003 53.605 1.00 14.71  ? 103 HIS A O   1 
ATOM   777  C  CB  . HIS A 1 103 ? 44.438 41.874 52.359 1.00 13.37  ? 103 HIS A CB  1 
ATOM   778  C  CG  . HIS A 1 103 ? 43.373 41.801 51.316 1.00 13.33  ? 103 HIS A CG  1 
ATOM   779  N  ND1 . HIS A 1 103 ? 42.284 42.647 51.310 1.00 13.37  ? 103 HIS A ND1 1 
ATOM   780  C  CD2 . HIS A 1 103 ? 43.234 40.990 50.240 1.00 13.22  ? 103 HIS A CD2 1 
ATOM   781  C  CE1 . HIS A 1 103 ? 41.522 42.363 50.269 1.00 13.47  ? 103 HIS A CE1 1 
ATOM   782  N  NE2 . HIS A 1 103 ? 42.074 41.360 49.607 1.00 13.48  ? 103 HIS A NE2 1 
ATOM   783  N  N   . CYS A 1 104 ? 44.109 39.070 53.483 1.00 15.30  ? 104 CYS A N   1 
ATOM   784  C  CA  . CYS A 1 104 ? 43.588 37.737 53.344 1.00 16.42  ? 104 CYS A CA  1 
ATOM   785  C  C   . CYS A 1 104 ? 42.993 37.156 54.601 1.00 15.20  ? 104 CYS A C   1 
ATOM   786  O  O   . CYS A 1 104 ? 42.241 36.212 54.503 1.00 15.53  ? 104 CYS A O   1 
ATOM   787  C  CB  . CYS A 1 104 ? 44.654 36.829 52.782 1.00 19.40  ? 104 CYS A CB  1 
ATOM   788  S  SG  . CYS A 1 104 ? 44.896 37.165 51.014 1.00 26.94  ? 104 CYS A SG  1 
ATOM   789  N  N   . LEU A 1 105 ? 43.302 37.696 55.769 1.00 14.82  ? 105 LEU A N   1 
ATOM   790  C  CA  . LEU A 1 105 ? 42.535 37.343 56.957 1.00 15.01  ? 105 LEU A CA  1 
ATOM   791  C  C   . LEU A 1 105 ? 41.175 37.959 56.981 1.00 14.60  ? 105 LEU A C   1 
ATOM   792  O  O   . LEU A 1 105 ? 40.261 37.322 57.482 1.00 15.65  ? 105 LEU A O   1 
ATOM   793  C  CB  . LEU A 1 105 ? 43.202 37.778 58.240 1.00 16.09  ? 105 LEU A CB  1 
ATOM   794  C  CG  . LEU A 1 105 ? 44.174 36.768 58.806 1.00 17.23  ? 105 LEU A CG  1 
ATOM   795  C  CD1 . LEU A 1 105 ? 45.072 37.441 59.843 1.00 17.69  ? 105 LEU A CD1 1 
ATOM   796  C  CD2 . LEU A 1 105 ? 43.391 35.613 59.406 1.00 17.82  ? 105 LEU A CD2 1 
ATOM   797  N  N   . LEU A 1 106 ? 41.025 39.192 56.506 1.00 14.11  ? 106 LEU A N   1 
ATOM   798  C  CA  . LEU A 1 106 ? 39.705 39.839 56.538 1.00 14.12  ? 106 LEU A CA  1 
ATOM   799  C  C   . LEU A 1 106 ? 38.762 39.240 55.536 1.00 13.18  ? 106 LEU A C   1 
ATOM   800  O  O   . LEU A 1 106 ? 37.594 39.053 55.841 1.00 13.34  ? 106 LEU A O   1 
ATOM   801  C  CB  . LEU A 1 106 ? 39.783 41.343 56.333 1.00 15.04  ? 106 LEU A CB  1 
ATOM   802  C  CG  . LEU A 1 106 ? 40.613 42.013 57.435 1.00 16.46  ? 106 LEU A CG  1 
ATOM   803  C  CD1 . LEU A 1 106 ? 40.609 43.524 57.217 1.00 16.94  ? 106 LEU A CD1 1 
ATOM   804  C  CD2 . LEU A 1 106 ? 40.155 41.637 58.858 1.00 16.79  ? 106 LEU A CD2 1 
ATOM   805  N  N   . VAL A 1 107 ? 39.255 38.913 54.354 1.00 12.57  ? 107 VAL A N   1 
ATOM   806  C  CA  . VAL A 1 107 ? 38.438 38.187 53.405 1.00 12.59  ? 107 VAL A CA  1 
ATOM   807  C  C   . VAL A 1 107 ? 37.933 36.888 54.033 1.00 13.24  ? 107 VAL A C   1 
ATOM   808  O  O   . VAL A 1 107 ? 36.754 36.581 53.935 1.00 13.58  ? 107 VAL A O   1 
ATOM   809  C  CB  . VAL A 1 107 ? 39.192 37.940 52.087 1.00 12.15  ? 107 VAL A CB  1 
ATOM   810  C  CG1 . VAL A 1 107 ? 38.589 36.779 51.296 1.00 12.06  ? 107 VAL A CG1 1 
ATOM   811  C  CG2 . VAL A 1 107 ? 39.207 39.219 51.254 1.00 11.75  ? 107 VAL A CG2 1 
ATOM   812  N  N   . THR A 1 108 ? 38.813 36.153 54.693 1.00 14.45  ? 108 THR A N   1 
ATOM   813  C  CA  . THR A 1 108 ? 38.443 34.902 55.331 1.00 15.77  ? 108 THR A CA  1 
ATOM   814  C  C   . THR A 1 108 ? 37.393 35.052 56.420 1.00 16.72  ? 108 THR A C   1 
ATOM   815  O  O   . THR A 1 108 ? 36.461 34.264 56.461 1.00 17.90  ? 108 THR A O   1 
ATOM   816  C  CB  . THR A 1 108 ? 39.670 34.222 55.938 1.00 16.83  ? 108 THR A CB  1 
ATOM   817  O  OG1 . THR A 1 108 ? 40.590 33.916 54.887 1.00 18.04  ? 108 THR A OG1 1 
ATOM   818  C  CG2 . THR A 1 108 ? 39.309 32.923 56.624 1.00 17.57  ? 108 THR A CG2 1 
ATOM   819  N  N   . LEU A 1 109 ? 37.527 36.027 57.305 1.00 17.92  ? 109 LEU A N   1 
ATOM   820  C  CA  . LEU A 1 109 ? 36.474 36.263 58.286 1.00 19.29  ? 109 LEU A CA  1 
ATOM   821  C  C   . LEU A 1 109 ? 35.167 36.648 57.644 1.00 19.89  ? 109 LEU A C   1 
ATOM   822  O  O   . LEU A 1 109 ? 34.134 36.131 58.036 1.00 21.77  ? 109 LEU A O   1 
ATOM   823  C  CB  . LEU A 1 109 ? 36.836 37.363 59.265 1.00 21.11  ? 109 LEU A CB  1 
ATOM   824  C  CG  . LEU A 1 109 ? 37.963 37.004 60.222 1.00 23.20  ? 109 LEU A CG  1 
ATOM   825  C  CD1 . LEU A 1 109 ? 38.155 38.152 61.202 1.00 24.09  ? 109 LEU A CD1 1 
ATOM   826  C  CD2 . LEU A 1 109 ? 37.691 35.694 60.945 1.00 23.78  ? 109 LEU A CD2 1 
ATOM   827  N  N   . ALA A 1 110 ? 35.187 37.541 56.665 1.00 20.23  ? 110 ALA A N   1 
ATOM   828  C  CA  . ALA A 1 110 ? 33.942 37.953 56.010 1.00 21.02  ? 110 ALA A CA  1 
ATOM   829  C  C   . ALA A 1 110 ? 33.240 36.794 55.300 1.00 21.87  ? 110 ALA A C   1 
ATOM   830  O  O   . ALA A 1 110 ? 32.017 36.778 55.200 1.00 23.02  ? 110 ALA A O   1 
ATOM   831  C  CB  . ALA A 1 110 ? 34.197 39.085 55.031 1.00 21.52  ? 110 ALA A CB  1 
ATOM   832  N  N   . ALA A 1 111 ? 34.008 35.826 54.821 1.00 23.05  ? 111 ALA A N   1 
ATOM   833  C  CA  . ALA A 1 111 ? 33.439 34.642 54.201 1.00 25.08  ? 111 ALA A CA  1 
ATOM   834  C  C   . ALA A 1 111 ? 32.978 33.578 55.202 1.00 28.88  ? 111 ALA A C   1 
ATOM   835  O  O   . ALA A 1 111 ? 32.513 32.521 54.777 1.00 31.41  ? 111 ALA A O   1 
ATOM   836  C  CB  . ALA A 1 111 ? 34.444 34.042 53.228 1.00 24.80  ? 111 ALA A CB  1 
ATOM   837  N  N   . HIS A 1 112 ? 33.131 33.817 56.507 1.00 33.59  ? 112 HIS A N   1 
ATOM   838  C  CA  . HIS A 1 112 ? 32.729 32.845 57.535 1.00 37.99  ? 112 HIS A CA  1 
ATOM   839  C  C   . HIS A 1 112 ? 31.946 33.352 58.750 1.00 42.39  ? 112 HIS A C   1 
ATOM   840  O  O   . HIS A 1 112 ? 31.301 32.552 59.421 1.00 43.88  ? 112 HIS A O   1 
ATOM   841  C  CB  . HIS A 1 112 ? 33.962 32.093 58.002 1.00 38.76  ? 112 HIS A CB  1 
ATOM   842  C  CG  . HIS A 1 112 ? 34.440 31.084 57.014 1.00 42.81  ? 112 HIS A CG  1 
ATOM   843  N  ND1 . HIS A 1 112 ? 35.172 31.426 55.899 1.00 45.12  ? 112 HIS A ND1 1 
ATOM   844  C  CD2 . HIS A 1 112 ? 34.266 29.744 56.954 1.00 48.33  ? 112 HIS A CD2 1 
ATOM   845  C  CE1 . HIS A 1 112 ? 35.435 30.339 55.198 1.00 47.51  ? 112 HIS A CE1 1 
ATOM   846  N  NE2 . HIS A 1 112 ? 34.901 29.303 55.819 1.00 49.92  ? 112 HIS A NE2 1 
ATOM   847  N  N   . LEU A 1 113 ? 31.999 34.651 59.034 1.00 50.39  ? 113 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 113 ? 31.248 35.256 60.128 1.00 59.87  ? 113 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 113 ? 30.486 36.431 59.568 1.00 66.15  ? 113 LEU A C   1 
ATOM   850  O  O   . LEU A 1 113 ? 30.755 37.574 59.933 1.00 78.28  ? 113 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 113 ? 32.197 35.745 61.226 1.00 66.55  ? 113 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 113 ? 33.117 34.716 61.878 1.00 75.71  ? 113 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 113 ? 34.039 35.435 62.856 1.00 79.13  ? 113 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 113 ? 32.327 33.608 62.568 1.00 78.61  ? 113 LEU A CD2 1 
ATOM   855  N  N   . PRO A 1 114 ? 29.528 36.169 58.673 1.00 72.91  ? 114 PRO A N   1 
ATOM   856  C  CA  . PRO A 1 114 ? 28.912 37.280 57.947 1.00 74.94  ? 114 PRO A CA  1 
ATOM   857  C  C   . PRO A 1 114 ? 28.164 38.263 58.841 1.00 75.24  ? 114 PRO A C   1 
ATOM   858  O  O   . PRO A 1 114 ? 28.163 39.462 58.561 1.00 72.54  ? 114 PRO A O   1 
ATOM   859  C  CB  . PRO A 1 114 ? 27.942 36.580 56.985 1.00 83.14  ? 114 PRO A CB  1 
ATOM   860  C  CG  . PRO A 1 114 ? 28.328 35.133 57.010 1.00 87.42  ? 114 PRO A CG  1 
ATOM   861  C  CD  . PRO A 1 114 ? 28.844 34.901 58.389 1.00 79.69  ? 114 PRO A CD  1 
ATOM   862  N  N   . ALA A 1 115 ? 27.552 37.751 59.907 1.00 82.91  ? 115 ALA A N   1 
ATOM   863  C  CA  . ALA A 1 115 ? 26.765 38.571 60.828 1.00 92.83  ? 115 ALA A CA  1 
ATOM   864  C  C   . ALA A 1 115 ? 27.616 39.492 61.709 1.00 92.47  ? 115 ALA A C   1 
ATOM   865  O  O   . ALA A 1 115 ? 27.207 40.616 62.014 1.00 91.43  ? 115 ALA A O   1 
ATOM   866  C  CB  . ALA A 1 115 ? 25.895 37.676 61.697 1.00 100.87 ? 115 ALA A CB  1 
ATOM   867  N  N   . GLU A 1 116 ? 28.795 39.014 62.106 1.00 93.71  ? 116 GLU A N   1 
ATOM   868  C  CA  . GLU A 1 116 ? 29.694 39.766 62.991 1.00 96.39  ? 116 GLU A CA  1 
ATOM   869  C  C   . GLU A 1 116 ? 30.560 40.808 62.278 1.00 82.73  ? 116 GLU A C   1 
ATOM   870  O  O   . GLU A 1 116 ? 31.302 41.535 62.934 1.00 83.27  ? 116 GLU A O   1 
ATOM   871  C  CB  . GLU A 1 116 ? 30.601 38.789 63.761 1.00 112.42 ? 116 GLU A CB  1 
ATOM   872  C  CG  . GLU A 1 116 ? 29.847 37.801 64.651 1.00 132.80 ? 116 GLU A CG  1 
ATOM   873  C  CD  . GLU A 1 116 ? 29.045 38.471 65.767 1.00 151.81 ? 116 GLU A CD  1 
ATOM   874  O  OE1 . GLU A 1 116 ? 29.540 39.455 66.365 1.00 162.38 ? 116 GLU A OE1 1 
ATOM   875  O  OE2 . GLU A 1 116 ? 27.918 38.007 66.057 1.00 153.12 ? 116 GLU A OE2 1 
ATOM   876  N  N   . PHE A 1 117 ? 30.448 40.899 60.954 1.00 72.90  ? 117 PHE A N   1 
ATOM   877  C  CA  . PHE A 1 117 ? 31.359 41.683 60.132 1.00 65.67  ? 117 PHE A CA  1 
ATOM   878  C  C   . PHE A 1 117 ? 30.679 42.988 59.693 1.00 60.96  ? 117 PHE A C   1 
ATOM   879  O  O   . PHE A 1 117 ? 30.540 43.274 58.504 1.00 59.90  ? 117 PHE A O   1 
ATOM   880  C  CB  . PHE A 1 117 ? 31.817 40.822 58.936 1.00 64.65  ? 117 PHE A CB  1 
ATOM   881  C  CG  . PHE A 1 117 ? 33.089 41.295 58.299 1.00 67.65  ? 117 PHE A CG  1 
ATOM   882  C  CD1 . PHE A 1 117 ? 34.317 41.084 58.932 1.00 65.74  ? 117 PHE A CD1 1 
ATOM   883  C  CD2 . PHE A 1 117 ? 33.067 41.966 57.068 1.00 68.76  ? 117 PHE A CD2 1 
ATOM   884  C  CE1 . PHE A 1 117 ? 35.498 41.540 58.356 1.00 66.05  ? 117 PHE A CE1 1 
ATOM   885  C  CE2 . PHE A 1 117 ? 34.246 42.421 56.487 1.00 67.61  ? 117 PHE A CE2 1 
ATOM   886  C  CZ  . PHE A 1 117 ? 35.463 42.206 57.132 1.00 67.56  ? 117 PHE A CZ  1 
ATOM   887  N  N   . THR A 1 118 ? 30.258 43.779 60.674 1.00 60.22  ? 118 THR A N   1 
ATOM   888  C  CA  . THR A 1 118 ? 29.694 45.099 60.412 1.00 63.12  ? 118 THR A CA  1 
ATOM   889  C  C   . THR A 1 118 ? 30.832 46.058 60.123 1.00 58.25  ? 118 THR A C   1 
ATOM   890  O  O   . THR A 1 118 ? 31.967 45.782 60.512 1.00 63.20  ? 118 THR A O   1 
ATOM   891  C  CB  . THR A 1 118 ? 28.938 45.662 61.635 1.00 75.87  ? 118 THR A CB  1 
ATOM   892  O  OG1 . THR A 1 118 ? 29.831 45.784 62.757 1.00 78.70  ? 118 THR A OG1 1 
ATOM   893  C  CG2 . THR A 1 118 ? 27.763 44.767 62.008 1.00 82.78  ? 118 THR A CG2 1 
ATOM   894  N  N   . PRO A 1 119 ? 30.541 47.203 59.476 1.00 51.62  ? 119 PRO A N   1 
ATOM   895  C  CA  . PRO A 1 119 ? 31.573 48.210 59.218 1.00 47.17  ? 119 PRO A CA  1 
ATOM   896  C  C   . PRO A 1 119 ? 32.441 48.571 60.404 1.00 41.79  ? 119 PRO A C   1 
ATOM   897  O  O   . PRO A 1 119 ? 33.653 48.639 60.250 1.00 42.75  ? 119 PRO A O   1 
ATOM   898  C  CB  . PRO A 1 119 ? 30.763 49.407 58.751 1.00 49.69  ? 119 PRO A CB  1 
ATOM   899  C  CG  . PRO A 1 119 ? 29.670 48.757 57.984 1.00 51.42  ? 119 PRO A CG  1 
ATOM   900  C  CD  . PRO A 1 119 ? 29.274 47.578 58.825 1.00 51.55  ? 119 PRO A CD  1 
ATOM   901  N  N   . ALA A 1 120 ? 31.848 48.766 61.572 1.00 40.68  ? 120 ALA A N   1 
ATOM   902  C  CA  . ALA A 1 120 ? 32.630 49.128 62.756 1.00 43.38  ? 120 ALA A CA  1 
ATOM   903  C  C   . ALA A 1 120 ? 33.625 48.048 63.186 1.00 39.05  ? 120 ALA A C   1 
ATOM   904  O  O   . ALA A 1 120 ? 34.708 48.358 63.682 1.00 40.44  ? 120 ALA A O   1 
ATOM   905  C  CB  . ALA A 1 120 ? 31.711 49.476 63.911 1.00 50.29  ? 120 ALA A CB  1 
ATOM   906  N  N   . VAL A 1 121 ? 33.254 46.794 62.999 1.00 34.15  ? 121 VAL A N   1 
ATOM   907  C  CA  . VAL A 1 121 ? 34.179 45.700 63.225 1.00 33.45  ? 121 VAL A CA  1 
ATOM   908  C  C   . VAL A 1 121 ? 35.264 45.652 62.143 1.00 29.89  ? 121 VAL A C   1 
ATOM   909  O  O   . VAL A 1 121 ? 36.432 45.447 62.468 1.00 31.10  ? 121 VAL A O   1 
ATOM   910  C  CB  . VAL A 1 121 ? 33.428 44.361 63.299 1.00 37.37  ? 121 VAL A CB  1 
ATOM   911  C  CG1 . VAL A 1 121 ? 34.393 43.175 63.300 1.00 38.25  ? 121 VAL A CG1 1 
ATOM   912  C  CG2 . VAL A 1 121 ? 32.545 44.353 64.546 1.00 40.42  ? 121 VAL A CG2 1 
ATOM   913  N  N   . HIS A 1 122 ? 34.878 45.817 60.875 1.00 24.73  ? 122 HIS A N   1 
ATOM   914  C  CA  . HIS A 1 122 ? 35.828 45.898 59.762 1.00 21.81  ? 122 HIS A CA  1 
ATOM   915  C  C   . HIS A 1 122 ? 36.842 46.981 60.081 1.00 21.08  ? 122 HIS A C   1 
ATOM   916  O  O   . HIS A 1 122 ? 38.042 46.743 60.005 1.00 22.20  ? 122 HIS A O   1 
ATOM   917  C  CB  . HIS A 1 122 ? 35.100 46.232 58.455 1.00 20.94  ? 122 HIS A CB  1 
ATOM   918  C  CG  . HIS A 1 122 ? 35.935 46.109 57.209 1.00 21.17  ? 122 HIS A CG  1 
ATOM   919  N  ND1 . HIS A 1 122 ? 35.367 45.966 55.961 1.00 20.74  ? 122 HIS A ND1 1 
ATOM   920  C  CD2 . HIS A 1 122 ? 37.278 46.112 57.007 1.00 21.57  ? 122 HIS A CD2 1 
ATOM   921  C  CE1 . HIS A 1 122 ? 36.319 45.891 55.047 1.00 20.73  ? 122 HIS A CE1 1 
ATOM   922  N  NE2 . HIS A 1 122 ? 37.488 45.972 55.655 1.00 20.83  ? 122 HIS A NE2 1 
ATOM   923  N  N   . ALA A 1 123 ? 36.358 48.153 60.474 1.00 20.35  ? 123 ALA A N   1 
ATOM   924  C  CA  . ALA A 1 123 ? 37.220 49.298 60.766 1.00 20.19  ? 123 ALA A CA  1 
ATOM   925  C  C   . ALA A 1 123 ? 38.195 49.056 61.898 1.00 20.76  ? 123 ALA A C   1 
ATOM   926  O  O   . ALA A 1 123 ? 39.359 49.445 61.796 1.00 22.39  ? 123 ALA A O   1 
ATOM   927  C  CB  . ALA A 1 123 ? 36.389 50.513 61.093 1.00 20.44  ? 123 ALA A CB  1 
ATOM   928  N  N   . SER A 1 124 ? 37.730 48.435 62.976 1.00 20.58  ? 124 SER A N   1 
ATOM   929  C  CA  . SER A 1 124 ? 38.599 48.121 64.107 1.00 20.50  ? 124 SER A CA  1 
ATOM   930  C  C   . SER A 1 124 ? 39.583 47.022 63.785 1.00 20.18  ? 124 SER A C   1 
ATOM   931  O  O   . SER A 1 124 ? 40.766 47.192 64.011 1.00 20.38  ? 124 SER A O   1 
ATOM   932  C  CB  . SER A 1 124 ? 37.778 47.705 65.307 1.00 21.30  ? 124 SER A CB  1 
ATOM   933  O  OG  . SER A 1 124 ? 36.810 48.696 65.601 1.00 22.72  ? 124 SER A OG  1 
ATOM   934  N  N   . LEU A 1 125 ? 39.102 45.904 63.252 1.00 21.65  ? 125 LEU A N   1 
ATOM   935  C  CA  . LEU A 1 125 ? 39.980 44.776 62.936 1.00 23.44  ? 125 LEU A CA  1 
ATOM   936  C  C   . LEU A 1 125 ? 41.080 45.126 61.970 1.00 24.80  ? 125 LEU A C   1 
ATOM   937  O  O   . LEU A 1 125 ? 42.123 44.482 61.995 1.00 26.74  ? 125 LEU A O   1 
ATOM   938  C  CB  . LEU A 1 125 ? 39.214 43.576 62.376 1.00 25.14  ? 125 LEU A CB  1 
ATOM   939  C  CG  . LEU A 1 125 ? 38.764 42.531 63.402 1.00 26.91  ? 125 LEU A CG  1 
ATOM   940  C  CD1 . LEU A 1 125 ? 37.722 41.580 62.831 1.00 27.50  ? 125 LEU A CD1 1 
ATOM   941  C  CD2 . LEU A 1 125 ? 39.955 41.727 63.905 1.00 28.44  ? 125 LEU A CD2 1 
ATOM   942  N  N   . ASP A 1 126 ? 40.854 46.124 61.122 1.00 26.95  ? 126 ASP A N   1 
ATOM   943  C  CA  . ASP A 1 126 ? 41.886 46.616 60.212 1.00 29.23  ? 126 ASP A CA  1 
ATOM   944  C  C   . ASP A 1 126 ? 43.029 47.344 60.927 1.00 26.39  ? 126 ASP A C   1 
ATOM   945  O  O   . ASP A 1 126 ? 44.200 47.106 60.619 1.00 24.62  ? 126 ASP A O   1 
ATOM   946  C  CB  . ASP A 1 126 ? 41.262 47.539 59.176 1.00 36.02  ? 126 ASP A CB  1 
ATOM   947  C  CG  . ASP A 1 126 ? 42.212 47.854 58.026 1.00 45.75  ? 126 ASP A CG  1 
ATOM   948  O  OD1 . ASP A 1 126 ? 42.227 47.098 57.014 1.00 49.15  ? 126 ASP A OD1 1 
ATOM   949  O  OD2 . ASP A 1 126 ? 42.936 48.877 58.137 1.00 52.37  ? 126 ASP A OD2 1 
ATOM   950  N  N   . LYS A 1 127 ? 42.680 48.236 61.857 1.00 25.59  ? 127 LYS A N   1 
ATOM   951  C  CA  . LYS A 1 127 ? 43.669 48.912 62.727 1.00 25.45  ? 127 LYS A CA  1 
ATOM   952  C  C   . LYS A 1 127 ? 44.463 47.966 63.613 1.00 21.73  ? 127 LYS A C   1 
ATOM   953  O  O   . LYS A 1 127 ? 45.662 48.153 63.816 1.00 21.77  ? 127 LYS A O   1 
ATOM   954  C  CB  . LYS A 1 127 ? 43.002 49.935 63.637 1.00 28.05  ? 127 LYS A CB  1 
ATOM   955  C  CG  . LYS A 1 127 ? 42.579 51.174 62.896 1.00 33.25  ? 127 LYS A CG  1 
ATOM   956  C  CD  . LYS A 1 127 ? 41.804 52.140 63.795 1.00 39.75  ? 127 LYS A CD  1 
ATOM   957  C  CE  . LYS A 1 127 ? 42.669 53.241 64.421 1.00 42.26  ? 127 LYS A CE  1 
ATOM   958  N  NZ  . LYS A 1 127 ? 41.843 54.333 65.033 1.00 41.65  ? 127 LYS A NZ  1 
ATOM   959  N  N   . PHE A 1 128 ? 43.774 46.981 64.169 1.00 18.32  ? 128 PHE A N   1 
ATOM   960  C  CA  . PHE A 1 128 ? 44.398 46.028 65.042 1.00 15.98  ? 128 PHE A CA  1 
ATOM   961  C  C   . PHE A 1 128 ? 45.492 45.309 64.300 1.00 14.61  ? 128 PHE A C   1 
ATOM   962  O  O   . PHE A 1 128 ? 46.633 45.331 64.755 1.00 14.87  ? 128 PHE A O   1 
ATOM   963  C  CB  . PHE A 1 128 ? 43.398 45.010 65.559 1.00 16.03  ? 128 PHE A CB  1 
ATOM   964  C  CG  . PHE A 1 128 ? 44.047 43.886 66.287 1.00 16.45  ? 128 PHE A CG  1 
ATOM   965  C  CD1 . PHE A 1 128 ? 44.821 44.142 67.421 1.00 16.20  ? 128 PHE A CD1 1 
ATOM   966  C  CD2 . PHE A 1 128 ? 43.946 42.577 65.819 1.00 16.49  ? 128 PHE A CD2 1 
ATOM   967  C  CE1 . PHE A 1 128 ? 45.463 43.106 68.089 1.00 15.94  ? 128 PHE A CE1 1 
ATOM   968  C  CE2 . PHE A 1 128 ? 44.593 41.542 66.485 1.00 16.33  ? 128 PHE A CE2 1 
ATOM   969  C  CZ  . PHE A 1 128 ? 45.351 41.808 67.622 1.00 15.85  ? 128 PHE A CZ  1 
ATOM   970  N  N   . LEU A 1 129 ? 45.147 44.672 63.173 1.00 13.07  ? 129 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 129 ? 46.123 43.925 62.343 1.00 12.10  ? 129 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 129 ? 47.289 44.773 61.891 1.00 12.27  ? 129 LEU A C   1 
ATOM   973  O  O   . LEU A 1 129 ? 48.421 44.296 61.808 1.00 11.82  ? 129 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 129 ? 45.468 43.351 61.107 1.00 11.24  ? 129 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 129 ? 44.584 42.155 61.395 1.00 11.02  ? 129 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 129 ? 43.754 41.822 60.167 1.00 10.94  ? 129 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 129 ? 45.408 40.955 61.825 1.00 11.00  ? 129 LEU A CD2 1 
ATOM   978  N  N   . ALA A 1 130 ? 46.993 46.038 61.603 1.00 12.93  ? 130 ALA A N   1 
ATOM   979  C  CA  . ALA A 1 130 ? 48.007 47.021 61.235 1.00 13.30  ? 130 ALA A CA  1 
ATOM   980  C  C   . ALA A 1 130 ? 48.999 47.331 62.355 1.00 13.40  ? 130 ALA A C   1 
ATOM   981  O  O   . ALA A 1 130 ? 50.187 47.498 62.090 1.00 13.65  ? 130 ALA A O   1 
ATOM   982  C  CB  . ALA A 1 130 ? 47.342 48.295 60.765 1.00 13.54  ? 130 ALA A CB  1 
ATOM   983  N  N   . SER A 1 131 ? 48.512 47.433 63.588 1.00 13.87  ? 131 SER A N   1 
ATOM   984  C  CA  . SER A 1 131 ? 49.396 47.593 64.745 1.00 14.40  ? 131 SER A CA  1 
ATOM   985  C  C   . SER A 1 131 ? 50.317 46.404 64.875 1.00 13.99  ? 131 SER A C   1 
ATOM   986  O  O   . SER A 1 131 ? 51.531 46.563 64.993 1.00 14.35  ? 131 SER A O   1 
ATOM   987  C  CB  . SER A 1 131 ? 48.610 47.755 66.054 1.00 15.04  ? 131 SER A CB  1 
ATOM   988  O  OG  . SER A 1 131 ? 48.035 49.049 66.125 1.00 15.95  ? 131 SER A OG  1 
ATOM   989  N  N   . VAL A 1 132 ? 49.727 45.224 64.851 1.00 13.36  ? 132 VAL A N   1 
ATOM   990  C  CA  . VAL A 1 132 ? 50.479 44.010 65.004 1.00 13.60  ? 132 VAL A CA  1 
ATOM   991  C  C   . VAL A 1 132 ? 51.582 43.956 63.938 1.00 14.36  ? 132 VAL A C   1 
ATOM   992  O  O   . VAL A 1 132 ? 52.731 43.627 64.255 1.00 14.59  ? 132 VAL A O   1 
ATOM   993  C  CB  . VAL A 1 132 ? 49.542 42.774 64.954 1.00 13.56  ? 132 VAL A CB  1 
ATOM   994  C  CG1 . VAL A 1 132 ? 50.298 41.454 64.786 1.00 13.49  ? 132 VAL A CG1 1 
ATOM   995  C  CG2 . VAL A 1 132 ? 48.696 42.724 66.207 1.00 13.54  ? 132 VAL A CG2 1 
ATOM   996  N  N   . SER A 1 133 ? 51.249 44.302 62.695 1.00 15.11  ? 133 SER A N   1 
ATOM   997  C  CA  . SER A 1 133 ? 52.221 44.258 61.592 1.00 16.15  ? 133 SER A CA  1 
ATOM   998  C  C   . SER A 1 133 ? 53.434 45.147 61.836 1.00 16.75  ? 133 SER A C   1 
ATOM   999  O  O   . SER A 1 133 ? 54.553 44.802 61.468 1.00 16.67  ? 133 SER A O   1 
ATOM   1000 C  CB  . SER A 1 133 ? 51.562 44.703 60.288 1.00 17.06  ? 133 SER A CB  1 
ATOM   1001 O  OG  . SER A 1 133 ? 50.446 43.883 59.959 1.00 17.67  ? 133 SER A OG  1 
ATOM   1002 N  N   . THR A 1 134 ? 53.187 46.290 62.463 1.00 18.00  ? 134 THR A N   1 
ATOM   1003 C  CA  . THR A 1 134 ? 54.226 47.261 62.805 1.00 18.86  ? 134 THR A CA  1 
ATOM   1004 C  C   . THR A 1 134 ? 55.178 46.825 63.940 1.00 17.86  ? 134 THR A C   1 
ATOM   1005 O  O   . THR A 1 134 ? 56.377 47.104 63.888 1.00 17.81  ? 134 THR A O   1 
ATOM   1006 C  CB  . THR A 1 134 ? 53.568 48.608 63.151 1.00 20.48  ? 134 THR A CB  1 
ATOM   1007 O  OG1 . THR A 1 134 ? 52.803 49.058 62.014 1.00 20.91  ? 134 THR A OG1 1 
ATOM   1008 C  CG2 . THR A 1 134 ? 54.620 49.658 63.523 1.00 21.36  ? 134 THR A CG2 1 
ATOM   1009 N  N   . VAL A 1 135 ? 54.653 46.147 64.949 1.00 16.98  ? 135 VAL A N   1 
ATOM   1010 C  CA  . VAL A 1 135 ? 55.501 45.564 65.984 1.00 16.58  ? 135 VAL A CA  1 
ATOM   1011 C  C   . VAL A 1 135 ? 56.407 44.493 65.397 1.00 16.29  ? 135 VAL A C   1 
ATOM   1012 O  O   . VAL A 1 135 ? 57.591 44.471 65.706 1.00 16.67  ? 135 VAL A O   1 
ATOM   1013 C  CB  . VAL A 1 135 ? 54.673 44.951 67.131 1.00 16.76  ? 135 VAL A CB  1 
ATOM   1014 C  CG1 . VAL A 1 135 ? 55.542 44.138 68.086 1.00 16.57  ? 135 VAL A CG1 1 
ATOM   1015 C  CG2 . VAL A 1 135 ? 53.955 46.054 67.892 1.00 17.11  ? 135 VAL A CG2 1 
ATOM   1016 N  N   . LEU A 1 136 ? 55.871 43.607 64.570 1.00 15.95  ? 136 LEU A N   1 
ATOM   1017 C  CA  . LEU A 1 136 ? 56.695 42.537 64.041 1.00 16.67  ? 136 LEU A CA  1 
ATOM   1018 C  C   . LEU A 1 136 ? 57.701 42.963 62.975 1.00 18.17  ? 136 LEU A C   1 
ATOM   1019 O  O   . LEU A 1 136 ? 58.559 42.175 62.638 1.00 18.51  ? 136 LEU A O   1 
ATOM   1020 C  CB  . LEU A 1 136 ? 55.851 41.410 63.462 1.00 16.69  ? 136 LEU A CB  1 
ATOM   1021 C  CG  . LEU A 1 136 ? 54.759 40.759 64.307 1.00 16.79  ? 136 LEU A CG  1 
ATOM   1022 C  CD1 . LEU A 1 136 ? 54.204 39.564 63.561 1.00 16.85  ? 136 LEU A CD1 1 
ATOM   1023 C  CD2 . LEU A 1 136 ? 55.259 40.307 65.649 1.00 16.95  ? 136 LEU A CD2 1 
ATOM   1024 N  N   . THR A 1 137 ? 57.618 44.164 62.420 1.00 21.45  ? 137 THR A N   1 
ATOM   1025 C  CA  . THR A 1 137 ? 58.596 44.581 61.397 1.00 25.12  ? 137 THR A CA  1 
ATOM   1026 C  C   . THR A 1 137 ? 59.574 45.663 61.891 1.00 28.35  ? 137 THR A C   1 
ATOM   1027 O  O   . THR A 1 137 ? 60.012 46.530 61.114 1.00 29.27  ? 137 THR A O   1 
ATOM   1028 C  CB  . THR A 1 137 ? 57.884 45.096 60.126 1.00 26.56  ? 137 THR A CB  1 
ATOM   1029 O  OG1 . THR A 1 137 ? 56.941 46.124 60.474 1.00 27.90  ? 137 THR A OG1 1 
ATOM   1030 C  CG2 . THR A 1 137 ? 57.168 43.991 59.443 1.00 26.22  ? 137 THR A CG2 1 
ATOM   1031 N  N   . SER A 1 138 ? 59.929 45.607 63.170 1.00 29.47  ? 138 SER A N   1 
ATOM   1032 C  CA  . SER A 1 138 ? 60.830 46.589 63.748 1.00 30.50  ? 138 SER A CA  1 
ATOM   1033 C  C   . SER A 1 138 ? 61.792 45.972 64.740 1.00 34.38  ? 138 SER A C   1 
ATOM   1034 O  O   . SER A 1 138 ? 61.500 44.925 65.317 1.00 34.33  ? 138 SER A O   1 
ATOM   1035 C  CB  . SER A 1 138 ? 60.030 47.683 64.417 1.00 29.37  ? 138 SER A CB  1 
ATOM   1036 O  OG  . SER A 1 138 ? 59.119 47.136 65.342 1.00 29.82  ? 138 SER A OG  1 
ATOM   1037 N  N   . LYS A 1 139 ? 62.950 46.606 64.875 1.00 39.84  ? 139 LYS A N   1 
ATOM   1038 C  CA  . LYS A 1 139 ? 63.990 46.147 65.772 1.00 44.45  ? 139 LYS A CA  1 
ATOM   1039 C  C   . LYS A 1 139 ? 64.082 46.951 67.051 1.00 46.63  ? 139 LYS A C   1 
ATOM   1040 O  O   . LYS A 1 139 ? 64.692 48.009 67.092 1.00 49.78  ? 139 LYS A O   1 
ATOM   1041 C  CB  . LYS A 1 139 ? 65.345 46.204 65.073 1.00 47.50  ? 139 LYS A CB  1 
ATOM   1042 C  CG  . LYS A 1 139 ? 65.492 45.239 63.916 1.00 51.28  ? 139 LYS A CG  1 
ATOM   1043 C  CD  . LYS A 1 139 ? 66.856 45.383 63.269 1.00 58.21  ? 139 LYS A CD  1 
ATOM   1044 C  CE  . LYS A 1 139 ? 67.040 44.409 62.121 1.00 64.70  ? 139 LYS A CE  1 
ATOM   1045 N  NZ  . LYS A 1 139 ? 68.373 44.579 61.481 1.00 66.07  ? 139 LYS A NZ  1 
ATOM   1046 N  N   . TYR A 1 140 ? 63.432 46.443 68.084 1.00 50.66  ? 140 TYR A N   1 
ATOM   1047 C  CA  . TYR A 1 140 ? 63.436 47.056 69.395 1.00 58.95  ? 140 TYR A CA  1 
ATOM   1048 C  C   . TYR A 1 140 ? 63.721 45.957 70.410 1.00 81.58  ? 140 TYR A C   1 
ATOM   1049 O  O   . TYR A 1 140 ? 63.323 44.806 70.207 1.00 94.17  ? 140 TYR A O   1 
ATOM   1050 C  CB  . TYR A 1 140 ? 62.095 47.721 69.681 1.00 54.79  ? 140 TYR A CB  1 
ATOM   1051 C  CG  . TYR A 1 140 ? 60.979 46.739 69.930 1.00 53.46  ? 140 TYR A CG  1 
ATOM   1052 C  CD1 . TYR A 1 140 ? 60.457 45.981 68.897 1.00 55.12  ? 140 TYR A CD1 1 
ATOM   1053 C  CD2 . TYR A 1 140 ? 60.454 46.564 71.198 1.00 52.21  ? 140 TYR A CD2 1 
ATOM   1054 C  CE1 . TYR A 1 140 ? 59.443 45.077 69.118 1.00 53.98  ? 140 TYR A CE1 1 
ATOM   1055 C  CE2 . TYR A 1 140 ? 59.440 45.660 71.428 1.00 52.95  ? 140 TYR A CE2 1 
ATOM   1056 C  CZ  . TYR A 1 140 ? 58.939 44.922 70.384 1.00 53.66  ? 140 TYR A CZ  1 
ATOM   1057 O  OH  . TYR A 1 140 ? 57.928 44.022 70.608 1.00 53.88  ? 140 TYR A OH  1 
ATOM   1058 N  N   . ARG A 1 141 ? 64.407 46.303 71.495 1.00 105.38 ? 141 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 141 ? 65.109 45.318 72.317 1.00 125.41 ? 141 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 141 ? 65.822 44.288 71.445 1.00 133.11 ? 141 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 141 ? 65.955 43.120 71.803 1.00 136.97 ? 141 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 141 ? 64.160 44.620 73.303 1.00 141.72 ? 141 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 141 ? 62.915 45.413 73.665 1.00 156.85 ? 141 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 141 ? 61.972 44.590 74.526 1.00 172.04 ? 141 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 141 ? 60.702 45.271 74.767 1.00 187.18 ? 141 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 141 ? 60.584 46.563 75.059 1.00 199.18 ? 141 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 141 ? 61.661 47.330 75.146 1.00 202.63 ? 141 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 141 ? 59.385 47.090 75.265 1.00 198.47 ? 141 ARG A NH2 1 
ATOM   1069 O  OXT . ARG A 1 141 ? 66.279 44.608 70.350 1.00 134.73 ? 141 ARG A OXT 1 
ATOM   1070 N  N   . VAL B 2 1   ? 45.414 42.264 30.971 1.00 154.17 ? 1   VAL B N   1 
ATOM   1071 C  CA  . VAL B 2 1   ? 45.692 41.328 32.103 1.00 147.97 ? 1   VAL B CA  1 
ATOM   1072 C  C   . VAL B 2 1   ? 45.424 39.875 31.676 1.00 149.50 ? 1   VAL B C   1 
ATOM   1073 O  O   . VAL B 2 1   ? 44.387 39.574 31.080 1.00 147.93 ? 1   VAL B O   1 
ATOM   1074 C  CB  . VAL B 2 1   ? 44.899 41.725 33.379 1.00 140.62 ? 1   VAL B CB  1 
ATOM   1075 C  CG1 . VAL B 2 1   ? 43.394 41.756 33.132 1.00 133.53 ? 1   VAL B CG1 1 
ATOM   1076 C  CG2 . VAL B 2 1   ? 45.244 40.808 34.545 1.00 147.95 ? 1   VAL B CG2 1 
ATOM   1077 N  N   . HIS B 2 2   ? 46.372 38.989 31.978 1.00 156.16 ? 2   HIS B N   1 
ATOM   1078 C  CA  . HIS B 2 2   ? 46.353 37.617 31.466 1.00 167.32 ? 2   HIS B CA  1 
ATOM   1079 C  C   . HIS B 2 2   ? 45.485 36.699 32.317 1.00 149.85 ? 2   HIS B C   1 
ATOM   1080 O  O   . HIS B 2 2   ? 45.910 36.246 33.383 1.00 152.20 ? 2   HIS B O   1 
ATOM   1081 C  CB  . HIS B 2 2   ? 47.775 37.053 31.401 1.00 201.76 ? 2   HIS B CB  1 
ATOM   1082 C  CG  . HIS B 2 2   ? 48.689 37.825 30.503 1.00 241.35 ? 2   HIS B CG  1 
ATOM   1083 N  ND1 . HIS B 2 2   ? 48.623 37.747 29.129 1.00 265.32 ? 2   HIS B ND1 1 
ATOM   1084 C  CD2 . HIS B 2 2   ? 49.694 38.689 30.784 1.00 265.64 ? 2   HIS B CD2 1 
ATOM   1085 C  CE1 . HIS B 2 2   ? 49.547 38.530 28.601 1.00 282.40 ? 2   HIS B CE1 1 
ATOM   1086 N  NE2 . HIS B 2 2   ? 50.211 39.113 29.583 1.00 278.51 ? 2   HIS B NE2 1 
ATOM   1087 N  N   . LEU B 2 3   ? 44.269 36.430 31.842 1.00 130.88 ? 3   LEU B N   1 
ATOM   1088 C  CA  . LEU B 2 3   ? 43.378 35.460 32.477 1.00 119.43 ? 3   LEU B CA  1 
ATOM   1089 C  C   . LEU B 2 3   ? 43.214 34.238 31.577 1.00 122.09 ? 3   LEU B C   1 
ATOM   1090 O  O   . LEU B 2 3   ? 43.108 34.364 30.354 1.00 121.03 ? 3   LEU B O   1 
ATOM   1091 C  CB  . LEU B 2 3   ? 42.004 36.077 32.780 1.00 109.10 ? 3   LEU B CB  1 
ATOM   1092 C  CG  . LEU B 2 3   ? 41.871 36.865 34.089 1.00 99.51  ? 3   LEU B CG  1 
ATOM   1093 C  CD1 . LEU B 2 3   ? 42.423 38.274 33.940 1.00 98.39  ? 3   LEU B CD1 1 
ATOM   1094 C  CD2 . LEU B 2 3   ? 40.422 36.917 34.544 1.00 96.23  ? 3   LEU B CD2 1 
ATOM   1095 N  N   . THR B 2 4   ? 43.201 33.060 32.197 1.00 127.91 ? 4   THR B N   1 
ATOM   1096 C  CA  . THR B 2 4   ? 42.877 31.816 31.506 1.00 136.84 ? 4   THR B CA  1 
ATOM   1097 C  C   . THR B 2 4   ? 41.354 31.687 31.376 1.00 147.28 ? 4   THR B C   1 
ATOM   1098 O  O   . THR B 2 4   ? 40.622 32.360 32.107 1.00 160.66 ? 4   THR B O   1 
ATOM   1099 C  CB  . THR B 2 4   ? 43.412 30.599 32.277 1.00 142.44 ? 4   THR B CB  1 
ATOM   1100 O  OG1 . THR B 2 4   ? 42.875 30.593 33.606 1.00 145.96 ? 4   THR B OG1 1 
ATOM   1101 C  CG2 . THR B 2 4   ? 44.928 30.645 32.350 1.00 148.98 ? 4   THR B CG2 1 
ATOM   1102 N  N   . PRO B 2 5   ? 40.867 30.822 30.459 1.00 152.82 ? 5   PRO B N   1 
ATOM   1103 C  CA  . PRO B 2 5   ? 39.411 30.629 30.296 1.00 155.46 ? 5   PRO B CA  1 
ATOM   1104 C  C   . PRO B 2 5   ? 38.653 30.084 31.517 1.00 156.53 ? 5   PRO B C   1 
ATOM   1105 O  O   . PRO B 2 5   ? 37.435 30.250 31.594 1.00 157.61 ? 5   PRO B O   1 
ATOM   1106 C  CB  . PRO B 2 5   ? 39.316 29.631 29.138 1.00 156.93 ? 5   PRO B CB  1 
ATOM   1107 C  CG  . PRO B 2 5   ? 40.583 29.811 28.384 1.00 160.29 ? 5   PRO B CG  1 
ATOM   1108 C  CD  . PRO B 2 5   ? 41.620 30.084 29.428 1.00 154.85 ? 5   PRO B CD  1 
ATOM   1109 N  N   . GLU B 2 6   ? 39.361 29.441 32.446 1.00 153.94 ? 6   GLU B N   1 
ATOM   1110 C  CA  . GLU B 2 6   ? 38.764 28.957 33.693 1.00 155.89 ? 6   GLU B CA  1 
ATOM   1111 C  C   . GLU B 2 6   ? 38.559 30.103 34.680 1.00 142.78 ? 6   GLU B C   1 
ATOM   1112 O  O   . GLU B 2 6   ? 37.525 30.176 35.346 1.00 138.36 ? 6   GLU B O   1 
ATOM   1113 C  CB  . GLU B 2 6   ? 39.632 27.871 34.338 1.00 174.53 ? 6   GLU B CB  1 
ATOM   1114 C  CG  . GLU B 2 6   ? 39.659 26.547 33.578 1.00 194.21 ? 6   GLU B CG  1 
ATOM   1115 C  CD  . GLU B 2 6   ? 40.610 26.521 32.385 1.00 206.92 ? 6   GLU B CD  1 
ATOM   1116 O  OE1 . GLU B 2 6   ? 41.192 27.570 32.030 1.00 206.68 ? 6   GLU B OE1 1 
ATOM   1117 O  OE2 . GLU B 2 6   ? 40.773 25.433 31.792 1.00 217.39 ? 6   GLU B OE2 1 
ATOM   1118 N  N   . GLU B 2 7   ? 39.556 30.980 34.781 1.00 133.45 ? 7   GLU B N   1 
ATOM   1119 C  CA  . GLU B 2 7   ? 39.453 32.180 35.613 1.00 130.83 ? 7   GLU B CA  1 
ATOM   1120 C  C   . GLU B 2 7   ? 38.387 33.132 35.080 1.00 116.84 ? 7   GLU B C   1 
ATOM   1121 O  O   . GLU B 2 7   ? 37.548 33.613 35.842 1.00 113.41 ? 7   GLU B O   1 
ATOM   1122 C  CB  . GLU B 2 7   ? 40.804 32.900 35.718 1.00 145.42 ? 7   GLU B CB  1 
ATOM   1123 C  CG  . GLU B 2 7   ? 41.833 32.162 36.572 1.00 158.53 ? 7   GLU B CG  1 
ATOM   1124 C  CD  . GLU B 2 7   ? 43.108 32.961 36.818 1.00 167.44 ? 7   GLU B CD  1 
ATOM   1125 O  OE1 . GLU B 2 7   ? 43.410 33.890 36.036 1.00 170.14 ? 7   GLU B OE1 1 
ATOM   1126 O  OE2 . GLU B 2 7   ? 43.819 32.650 37.799 1.00 168.94 ? 7   GLU B OE2 1 
ATOM   1127 N  N   . LYS B 2 8   ? 38.415 33.385 33.775 1.00 114.36 ? 8   LYS B N   1 
ATOM   1128 C  CA  . LYS B 2 8   ? 37.423 34.252 33.139 1.00 121.28 ? 8   LYS B CA  1 
ATOM   1129 C  C   . LYS B 2 8   ? 35.998 33.685 33.237 1.00 118.42 ? 8   LYS B C   1 
ATOM   1130 O  O   . LYS B 2 8   ? 35.039 34.452 33.326 1.00 116.14 ? 8   LYS B O   1 
ATOM   1131 C  CB  . LYS B 2 8   ? 37.792 34.528 31.678 1.00 132.75 ? 8   LYS B CB  1 
ATOM   1132 C  CG  . LYS B 2 8   ? 37.031 35.692 31.059 1.00 150.75 ? 8   LYS B CG  1 
ATOM   1133 C  CD  . LYS B 2 8   ? 37.433 35.920 29.610 1.00 172.33 ? 8   LYS B CD  1 
ATOM   1134 C  CE  . LYS B 2 8   ? 36.498 36.904 28.920 1.00 188.28 ? 8   LYS B CE  1 
ATOM   1135 N  NZ  . LYS B 2 8   ? 36.804 37.062 27.470 1.00 194.69 ? 8   LYS B NZ  1 
ATOM   1136 N  N   . SER B 2 9   ? 35.859 32.358 33.227 1.00 123.35 ? 9   SER B N   1 
ATOM   1137 C  CA  . SER B 2 9   ? 34.557 31.722 33.467 1.00 132.86 ? 9   SER B CA  1 
ATOM   1138 C  C   . SER B 2 9   ? 34.071 31.961 34.900 1.00 132.68 ? 9   SER B C   1 
ATOM   1139 O  O   . SER B 2 9   ? 32.889 32.243 35.120 1.00 135.84 ? 9   SER B O   1 
ATOM   1140 C  CB  . SER B 2 9   ? 34.600 30.214 33.173 1.00 138.56 ? 9   SER B CB  1 
ATOM   1141 O  OG  . SER B 2 9   ? 35.428 29.518 34.088 1.00 134.40 ? 9   SER B OG  1 
ATOM   1142 N  N   . ALA B 2 10  ? 34.988 31.847 35.862 1.00 120.16 ? 10  ALA B N   1 
ATOM   1143 C  CA  . ALA B 2 10  ? 34.678 32.088 37.273 1.00 108.20 ? 10  ALA B CA  1 
ATOM   1144 C  C   . ALA B 2 10  ? 34.298 33.546 37.529 1.00 93.94  ? 10  ALA B C   1 
ATOM   1145 O  O   . ALA B 2 10  ? 33.300 33.820 38.197 1.00 95.95  ? 10  ALA B O   1 
ATOM   1146 C  CB  . ALA B 2 10  ? 35.854 31.686 38.150 1.00 110.52 ? 10  ALA B CB  1 
ATOM   1147 N  N   . VAL B 2 11  ? 35.096 34.464 36.990 1.00 76.17  ? 11  VAL B N   1 
ATOM   1148 C  CA  . VAL B 2 11  ? 34.838 35.894 37.114 1.00 68.96  ? 11  VAL B CA  1 
ATOM   1149 C  C   . VAL B 2 11  ? 33.432 36.221 36.622 1.00 69.40  ? 11  VAL B C   1 
ATOM   1150 O  O   . VAL B 2 11  ? 32.642 36.792 37.361 1.00 70.75  ? 11  VAL B O   1 
ATOM   1151 C  CB  . VAL B 2 11  ? 35.887 36.720 36.332 1.00 68.34  ? 11  VAL B CB  1 
ATOM   1152 C  CG1 . VAL B 2 11  ? 35.451 38.166 36.144 1.00 68.23  ? 11  VAL B CG1 1 
ATOM   1153 C  CG2 . VAL B 2 11  ? 37.234 36.678 37.035 1.00 69.57  ? 11  VAL B CG2 1 
ATOM   1154 N  N   . THR B 2 12  ? 33.126 35.839 35.386 1.00 77.46  ? 12  THR B N   1 
ATOM   1155 C  CA  . THR B 2 12  ? 31.835 36.169 34.765 1.00 85.89  ? 12  THR B CA  1 
ATOM   1156 C  C   . THR B 2 12  ? 30.631 35.498 35.426 1.00 86.63  ? 12  THR B C   1 
ATOM   1157 O  O   . THR B 2 12  ? 29.538 36.069 35.436 1.00 83.96  ? 12  THR B O   1 
ATOM   1158 C  CB  . THR B 2 12  ? 31.818 35.802 33.267 1.00 96.69  ? 12  THR B CB  1 
ATOM   1159 O  OG1 . THR B 2 12  ? 32.316 34.466 33.091 1.00 98.06  ? 12  THR B OG1 1 
ATOM   1160 C  CG2 . THR B 2 12  ? 32.670 36.786 32.464 1.00 100.19 ? 12  THR B CG2 1 
ATOM   1161 N  N   . ALA B 2 13  ? 30.834 34.292 35.961 1.00 89.43  ? 13  ALA B N   1 
ATOM   1162 C  CA  . ALA B 2 13  ? 29.765 33.538 36.628 1.00 90.89  ? 13  ALA B CA  1 
ATOM   1163 C  C   . ALA B 2 13  ? 29.343 34.199 37.941 1.00 89.15  ? 13  ALA B C   1 
ATOM   1164 O  O   . ALA B 2 13  ? 28.160 34.482 38.147 1.00 87.86  ? 13  ALA B O   1 
ATOM   1165 C  CB  . ALA B 2 13  ? 30.202 32.102 36.879 1.00 90.07  ? 13  ALA B CB  1 
ATOM   1166 N  N   . LEU B 2 14  ? 30.317 34.441 38.817 1.00 83.39  ? 14  LEU B N   1 
ATOM   1167 C  CA  . LEU B 2 14  ? 30.051 35.115 40.088 1.00 78.84  ? 14  LEU B CA  1 
ATOM   1168 C  C   . LEU B 2 14  ? 29.772 36.586 39.925 1.00 72.73  ? 14  LEU B C   1 
ATOM   1169 O  O   . LEU B 2 14  ? 29.205 37.175 40.827 1.00 80.74  ? 14  LEU B O   1 
ATOM   1170 C  CB  . LEU B 2 14  ? 31.187 34.936 41.097 1.00 86.60  ? 14  LEU B CB  1 
ATOM   1171 C  CG  . LEU B 2 14  ? 31.049 33.678 41.955 1.00 102.27 ? 14  LEU B CG  1 
ATOM   1172 C  CD1 . LEU B 2 14  ? 31.388 32.429 41.141 1.00 108.90 ? 14  LEU B CD1 1 
ATOM   1173 C  CD2 . LEU B 2 14  ? 31.908 33.777 43.216 1.00 109.39 ? 14  LEU B CD2 1 
ATOM   1174 N  N   . TRP B 2 15  ? 30.175 37.196 38.813 1.00 70.21  ? 15  TRP B N   1 
ATOM   1175 C  CA  . TRP B 2 15  ? 29.760 38.571 38.537 1.00 70.30  ? 15  TRP B CA  1 
ATOM   1176 C  C   . TRP B 2 15  ? 28.317 38.621 38.083 1.00 73.67  ? 15  TRP B C   1 
ATOM   1177 O  O   . TRP B 2 15  ? 27.606 39.580 38.382 1.00 71.74  ? 15  TRP B O   1 
ATOM   1178 C  CB  . TRP B 2 15  ? 30.625 39.246 37.484 1.00 70.08  ? 15  TRP B CB  1 
ATOM   1179 C  CG  . TRP B 2 15  ? 30.320 40.694 37.419 1.00 68.05  ? 15  TRP B CG  1 
ATOM   1180 C  CD1 . TRP B 2 15  ? 29.527 41.327 36.514 1.00 70.55  ? 15  TRP B CD1 1 
ATOM   1181 C  CD2 . TRP B 2 15  ? 30.750 41.685 38.342 1.00 64.64  ? 15  TRP B CD2 1 
ATOM   1182 N  NE1 . TRP B 2 15  ? 29.461 42.667 36.799 1.00 69.44  ? 15  TRP B NE1 1 
ATOM   1183 C  CE2 . TRP B 2 15  ? 30.205 42.912 37.921 1.00 66.45  ? 15  TRP B CE2 1 
ATOM   1184 C  CE3 . TRP B 2 15  ? 31.561 41.661 39.478 1.00 65.24  ? 15  TRP B CE3 1 
ATOM   1185 C  CZ2 . TRP B 2 15  ? 30.439 44.103 38.601 1.00 68.22  ? 15  TRP B CZ2 1 
ATOM   1186 C  CZ3 . TRP B 2 15  ? 31.795 42.848 40.154 1.00 69.26  ? 15  TRP B CZ3 1 
ATOM   1187 C  CH2 . TRP B 2 15  ? 31.233 44.051 39.713 1.00 68.52  ? 15  TRP B CH2 1 
ATOM   1188 N  N   . GLY B 2 16  ? 27.899 37.600 37.340 1.00 84.02  ? 16  GLY B N   1 
ATOM   1189 C  CA  . GLY B 2 16  ? 26.505 37.452 36.931 1.00 95.17  ? 16  GLY B CA  1 
ATOM   1190 C  C   . GLY B 2 16  ? 25.506 37.381 38.080 1.00 100.43 ? 16  GLY B C   1 
ATOM   1191 O  O   . GLY B 2 16  ? 24.367 37.832 37.934 1.00 106.00 ? 16  GLY B O   1 
ATOM   1192 N  N   . LYS B 2 17  ? 25.928 36.825 39.217 1.00 100.33 ? 17  LYS B N   1 
ATOM   1193 C  CA  . LYS B 2 17  ? 25.071 36.713 40.406 1.00 104.05 ? 17  LYS B CA  1 
ATOM   1194 C  C   . LYS B 2 17  ? 25.034 37.964 41.304 1.00 95.40  ? 17  LYS B C   1 
ATOM   1195 O  O   . LYS B 2 17  ? 24.242 38.012 42.249 1.00 92.68  ? 17  LYS B O   1 
ATOM   1196 C  CB  . LYS B 2 17  ? 25.501 35.505 41.246 1.00 119.23 ? 17  LYS B CB  1 
ATOM   1197 C  CG  . LYS B 2 17  ? 25.422 34.177 40.512 1.00 131.43 ? 17  LYS B CG  1 
ATOM   1198 C  CD  . LYS B 2 17  ? 25.727 33.014 41.442 1.00 142.22 ? 17  LYS B CD  1 
ATOM   1199 C  CE  . LYS B 2 17  ? 25.462 31.680 40.762 1.00 152.88 ? 17  LYS B CE  1 
ATOM   1200 N  NZ  . LYS B 2 17  ? 25.725 30.523 41.663 1.00 159.56 ? 17  LYS B NZ  1 
ATOM   1201 N  N   . VAL B 2 18  ? 25.872 38.963 41.015 1.00 91.57  ? 18  VAL B N   1 
ATOM   1202 C  CA  . VAL B 2 18  ? 25.969 40.179 41.835 1.00 91.22  ? 18  VAL B CA  1 
ATOM   1203 C  C   . VAL B 2 18  ? 24.685 40.982 41.709 1.00 97.15  ? 18  VAL B C   1 
ATOM   1204 O  O   . VAL B 2 18  ? 24.188 41.183 40.599 1.00 105.60 ? 18  VAL B O   1 
ATOM   1205 C  CB  . VAL B 2 18  ? 27.144 41.091 41.385 1.00 92.30  ? 18  VAL B CB  1 
ATOM   1206 C  CG1 . VAL B 2 18  ? 27.116 42.445 42.089 1.00 90.18  ? 18  VAL B CG1 1 
ATOM   1207 C  CG2 . VAL B 2 18  ? 28.484 40.419 41.628 1.00 96.13  ? 18  VAL B CG2 1 
ATOM   1208 N  N   . ASN B 2 19  ? 24.158 41.443 42.839 1.00 101.56 ? 19  ASN B N   1 
ATOM   1209 C  CA  . ASN B 2 19  ? 23.066 42.409 42.828 1.00 106.12 ? 19  ASN B CA  1 
ATOM   1210 C  C   . ASN B 2 19  ? 23.664 43.800 42.635 1.00 108.76 ? 19  ASN B C   1 
ATOM   1211 O  O   . ASN B 2 19  ? 24.171 44.409 43.580 1.00 102.26 ? 19  ASN B O   1 
ATOM   1212 C  CB  . ASN B 2 19  ? 22.261 42.340 44.124 1.00 114.23 ? 19  ASN B CB  1 
ATOM   1213 C  CG  . ASN B 2 19  ? 21.083 43.300 44.136 1.00 122.79 ? 19  ASN B CG  1 
ATOM   1214 O  OD1 . ASN B 2 19  ? 20.623 43.771 43.091 1.00 122.71 ? 19  ASN B OD1 1 
ATOM   1215 N  ND2 . ASN B 2 19  ? 20.581 43.590 45.331 1.00 135.12 ? 19  ASN B ND2 1 
ATOM   1216 N  N   . VAL B 2 20  ? 23.568 44.311 41.408 1.00 117.56 ? 20  VAL B N   1 
ATOM   1217 C  CA  . VAL B 2 20  ? 24.265 45.549 41.012 1.00 120.07 ? 20  VAL B CA  1 
ATOM   1218 C  C   . VAL B 2 20  ? 23.613 46.861 41.490 1.00 118.45 ? 20  VAL B C   1 
ATOM   1219 O  O   . VAL B 2 20  ? 23.893 47.927 40.936 1.00 120.65 ? 20  VAL B O   1 
ATOM   1220 C  CB  . VAL B 2 20  ? 24.501 45.598 39.477 1.00 122.85 ? 20  VAL B CB  1 
ATOM   1221 C  CG1 . VAL B 2 20  ? 25.457 44.489 39.056 1.00 121.85 ? 20  VAL B CG1 1 
ATOM   1222 C  CG2 . VAL B 2 20  ? 23.188 45.525 38.694 1.00 124.27 ? 20  VAL B CG2 1 
ATOM   1223 N  N   . ASP B 2 21  ? 22.749 46.783 42.501 1.00 121.90 ? 21  ASP B N   1 
ATOM   1224 C  CA  . ASP B 2 21  ? 22.226 47.961 43.188 1.00 130.41 ? 21  ASP B CA  1 
ATOM   1225 C  C   . ASP B 2 21  ? 22.962 48.226 44.506 1.00 125.91 ? 21  ASP B C   1 
ATOM   1226 O  O   . ASP B 2 21  ? 23.381 49.357 44.773 1.00 123.88 ? 21  ASP B O   1 
ATOM   1227 C  CB  . ASP B 2 21  ? 20.736 47.773 43.471 1.00 142.64 ? 21  ASP B CB  1 
ATOM   1228 C  CG  . ASP B 2 21  ? 20.091 49.020 44.052 1.00 155.17 ? 21  ASP B CG  1 
ATOM   1229 O  OD1 . ASP B 2 21  ? 19.930 50.007 43.303 1.00 167.55 ? 21  ASP B OD1 1 
ATOM   1230 O  OD2 . ASP B 2 21  ? 19.745 49.012 45.254 1.00 153.56 ? 21  ASP B OD2 1 
ATOM   1231 N  N   . GLU B 2 22  ? 23.109 47.181 45.320 1.00 116.67 ? 22  GLU B N   1 
ATOM   1232 C  CA  . GLU B 2 22  ? 23.558 47.317 46.707 1.00 107.09 ? 22  GLU B CA  1 
ATOM   1233 C  C   . GLU B 2 22  ? 25.071 47.219 46.896 1.00 82.47  ? 22  GLU B C   1 
ATOM   1234 O  O   . GLU B 2 22  ? 25.622 47.848 47.799 1.00 78.32  ? 22  GLU B O   1 
ATOM   1235 C  CB  . GLU B 2 22  ? 22.864 46.253 47.568 1.00 124.92 ? 22  GLU B CB  1 
ATOM   1236 C  CG  . GLU B 2 22  ? 22.838 46.555 49.063 1.00 146.36 ? 22  GLU B CG  1 
ATOM   1237 C  CD  . GLU B 2 22  ? 22.096 47.840 49.419 1.00 161.57 ? 22  GLU B CD  1 
ATOM   1238 O  OE1 . GLU B 2 22  ? 21.117 48.189 48.722 1.00 173.05 ? 22  GLU B OE1 1 
ATOM   1239 O  OE2 . GLU B 2 22  ? 22.493 48.503 50.404 1.00 165.21 ? 22  GLU B OE2 1 
ATOM   1240 N  N   . VAL B 2 23  ? 25.730 46.440 46.047 1.00 65.15  ? 23  VAL B N   1 
ATOM   1241 C  CA  . VAL B 2 23  ? 27.156 46.169 46.194 1.00 57.31  ? 23  VAL B CA  1 
ATOM   1242 C  C   . VAL B 2 23  ? 27.994 47.443 46.139 1.00 56.54  ? 23  VAL B C   1 
ATOM   1243 O  O   . VAL B 2 23  ? 28.782 47.699 47.053 1.00 59.22  ? 23  VAL B O   1 
ATOM   1244 C  CB  . VAL B 2 23  ? 27.629 45.149 45.142 1.00 54.23  ? 23  VAL B CB  1 
ATOM   1245 C  CG1 . VAL B 2 23  ? 29.149 45.045 45.085 1.00 53.00  ? 23  VAL B CG1 1 
ATOM   1246 C  CG2 . VAL B 2 23  ? 27.026 43.795 45.466 1.00 56.85  ? 23  VAL B CG2 1 
ATOM   1247 N  N   . GLY B 2 24  ? 27.820 48.237 45.084 1.00 54.18  ? 24  GLY B N   1 
ATOM   1248 C  CA  . GLY B 2 24  ? 28.501 49.535 44.967 1.00 52.32  ? 24  GLY B CA  1 
ATOM   1249 C  C   . GLY B 2 24  ? 28.248 50.474 46.146 1.00 50.09  ? 24  GLY B C   1 
ATOM   1250 O  O   . GLY B 2 24  ? 29.152 51.192 46.591 1.00 48.10  ? 24  GLY B O   1 
ATOM   1251 N  N   . GLY B 2 25  ? 27.011 50.464 46.642 1.00 47.24  ? 25  GLY B N   1 
ATOM   1252 C  CA  . GLY B 2 25  ? 26.630 51.235 47.812 1.00 44.78  ? 25  GLY B CA  1 
ATOM   1253 C  C   . GLY B 2 25  ? 27.321 50.766 49.070 1.00 43.82  ? 25  GLY B C   1 
ATOM   1254 O  O   . GLY B 2 25  ? 27.717 51.584 49.897 1.00 44.80  ? 25  GLY B O   1 
ATOM   1255 N  N   . GLU B 2 26  ? 27.455 49.453 49.223 1.00 44.75  ? 26  GLU B N   1 
ATOM   1256 C  CA  . GLU B 2 26  ? 28.165 48.894 50.365 1.00 46.55  ? 26  GLU B CA  1 
ATOM   1257 C  C   . GLU B 2 26  ? 29.634 49.158 50.250 1.00 38.96  ? 26  GLU B C   1 
ATOM   1258 O  O   . GLU B 2 26  ? 30.235 49.650 51.203 1.00 39.90  ? 26  GLU B O   1 
ATOM   1259 C  CB  . GLU B 2 26  ? 27.936 47.394 50.495 1.00 62.00  ? 26  GLU B CB  1 
ATOM   1260 C  CG  . GLU B 2 26  ? 26.601 47.054 51.142 1.00 81.59  ? 26  GLU B CG  1 
ATOM   1261 C  CD  . GLU B 2 26  ? 26.283 45.561 51.169 1.00 95.78  ? 26  GLU B CD  1 
ATOM   1262 O  OE1 . GLU B 2 26  ? 27.130 44.745 50.738 1.00 105.90 ? 26  GLU B OE1 1 
ATOM   1263 O  OE2 . GLU B 2 26  ? 25.173 45.201 51.630 1.00 101.30 ? 26  GLU B OE2 1 
ATOM   1264 N  N   . ALA B 2 27  ? 30.213 48.845 49.090 1.00 32.67  ? 27  ALA B N   1 
ATOM   1265 C  CA  . ALA B 2 27  ? 31.661 48.991 48.891 1.00 29.51  ? 27  ALA B CA  1 
ATOM   1266 C  C   . ALA B 2 27  ? 32.124 50.410 49.183 1.00 26.23  ? 27  ALA B C   1 
ATOM   1267 O  O   . ALA B 2 27  ? 32.985 50.631 50.029 1.00 26.75  ? 27  ALA B O   1 
ATOM   1268 C  CB  . ALA B 2 27  ? 32.071 48.580 47.492 1.00 29.34  ? 27  ALA B CB  1 
ATOM   1269 N  N   . LEU B 2 28  ? 31.523 51.372 48.516 1.00 23.66  ? 28  LEU B N   1 
ATOM   1270 C  CA  . LEU B 2 28  ? 31.850 52.755 48.775 1.00 22.51  ? 28  LEU B CA  1 
ATOM   1271 C  C   . LEU B 2 28  ? 31.474 53.215 50.213 1.00 20.76  ? 28  LEU B C   1 
ATOM   1272 O  O   . LEU B 2 28  ? 32.097 54.123 50.767 1.00 20.76  ? 28  LEU B O   1 
ATOM   1273 C  CB  . LEU B 2 28  ? 31.164 53.632 47.746 1.00 23.15  ? 28  LEU B CB  1 
ATOM   1274 C  CG  . LEU B 2 28  ? 31.679 55.062 47.788 1.00 24.51  ? 28  LEU B CG  1 
ATOM   1275 C  CD1 . LEU B 2 28  ? 33.031 55.136 47.086 1.00 25.70  ? 28  LEU B CD1 1 
ATOM   1276 C  CD2 . LEU B 2 28  ? 30.655 55.996 47.183 1.00 24.83  ? 28  LEU B CD2 1 
ATOM   1277 N  N   . GLY B 2 29  ? 30.450 52.616 50.802 1.00 18.20  ? 29  GLY B N   1 
ATOM   1278 C  CA  . GLY B 2 29  ? 30.112 52.901 52.183 1.00 16.51  ? 29  GLY B CA  1 
ATOM   1279 C  C   . GLY B 2 29  ? 31.233 52.446 53.103 1.00 15.43  ? 29  GLY B C   1 
ATOM   1280 O  O   . GLY B 2 29  ? 31.632 53.195 54.005 1.00 16.24  ? 29  GLY B O   1 
ATOM   1281 N  N   . ARG B 2 30  ? 31.748 51.229 52.889 1.00 12.80  ? 30  ARG B N   1 
ATOM   1282 C  CA  . ARG B 2 30  ? 32.822 50.711 53.744 1.00 10.90  ? 30  ARG B CA  1 
ATOM   1283 C  C   . ARG B 2 30  ? 34.069 51.537 53.612 1.00 7.69   ? 30  ARG B C   1 
ATOM   1284 O  O   . ARG B 2 30  ? 34.741 51.776 54.614 1.00 7.62   ? 30  ARG B O   1 
ATOM   1285 C  CB  . ARG B 2 30  ? 33.137 49.244 53.475 1.00 13.18  ? 30  ARG B CB  1 
ATOM   1286 C  CG  . ARG B 2 30  ? 32.259 48.371 54.325 1.00 16.34  ? 30  ARG B CG  1 
ATOM   1287 C  CD  . ARG B 2 30  ? 32.318 46.895 53.985 1.00 20.11  ? 30  ARG B CD  1 
ATOM   1288 N  NE  . ARG B 2 30  ? 31.187 46.231 54.656 1.00 24.02  ? 30  ARG B NE  1 
ATOM   1289 C  CZ  . ARG B 2 30  ? 31.145 45.857 55.940 1.00 26.47  ? 30  ARG B CZ  1 
ATOM   1290 N  NH1 . ARG B 2 30  ? 32.189 46.015 56.739 1.00 27.57  ? 30  ARG B NH1 1 
ATOM   1291 N  NH2 . ARG B 2 30  ? 30.043 45.292 56.428 1.00 28.31  ? 30  ARG B NH2 1 
ATOM   1292 N  N   . LEU B 2 31  ? 34.364 51.994 52.389 1.00 4.44   ? 31  LEU B N   1 
ATOM   1293 C  CA  . LEU B 2 31  ? 35.555 52.804 52.135 1.00 1.82   ? 31  LEU B CA  1 
ATOM   1294 C  C   . LEU B 2 31  ? 35.582 53.995 53.040 1.00 1.00   ? 31  LEU B C   1 
ATOM   1295 O  O   . LEU B 2 31  ? 36.598 54.236 53.673 1.00 1.00   ? 31  LEU B O   1 
ATOM   1296 C  CB  . LEU B 2 31  ? 35.628 53.291 50.698 1.00 1.52   ? 31  LEU B CB  1 
ATOM   1297 C  CG  . LEU B 2 31  ? 36.994 53.909 50.361 1.00 1.39   ? 31  LEU B CG  1 
ATOM   1298 C  CD1 . LEU B 2 31  ? 37.990 52.786 50.054 1.00 1.29   ? 31  LEU B CD1 1 
ATOM   1299 C  CD2 . LEU B 2 31  ? 36.941 54.931 49.225 1.00 1.27   ? 31  LEU B CD2 1 
ATOM   1300 N  N   . LEU B 2 32  ? 34.466 54.709 53.122 1.00 1.00   ? 32  LEU B N   1 
ATOM   1301 C  CA  . LEU B 2 32  ? 34.395 55.920 53.947 1.00 1.00   ? 32  LEU B CA  1 
ATOM   1302 C  C   . LEU B 2 32  ? 34.463 55.708 55.437 1.00 1.00   ? 32  LEU B C   1 
ATOM   1303 O  O   . LEU B 2 32  ? 34.774 56.647 56.165 1.00 1.00   ? 32  LEU B O   1 
ATOM   1304 C  CB  . LEU B 2 32  ? 33.141 56.729 53.679 1.00 1.00   ? 32  LEU B CB  1 
ATOM   1305 C  CG  . LEU B 2 32  ? 33.317 57.709 52.537 1.00 1.00   ? 32  LEU B CG  1 
ATOM   1306 C  CD1 . LEU B 2 32  ? 33.633 56.991 51.230 1.00 1.00   ? 32  LEU B CD1 1 
ATOM   1307 C  CD2 . LEU B 2 32  ? 32.021 58.499 52.408 1.00 1.00   ? 32  LEU B CD2 1 
ATOM   1308 N  N   . VAL B 2 33  ? 34.168 54.504 55.900 1.00 1.00   ? 33  VAL B N   1 
ATOM   1309 C  CA  . VAL B 2 33  ? 34.275 54.169 57.333 1.00 1.00   ? 33  VAL B CA  1 
ATOM   1310 C  C   . VAL B 2 33  ? 35.669 53.635 57.741 1.00 1.00   ? 33  VAL B C   1 
ATOM   1311 O  O   . VAL B 2 33  ? 36.195 53.971 58.797 1.00 1.00   ? 33  VAL B O   1 
ATOM   1312 C  CB  . VAL B 2 33  ? 33.185 53.135 57.674 1.00 1.00   ? 33  VAL B CB  1 
ATOM   1313 C  CG1 . VAL B 2 33  ? 33.354 52.577 59.082 1.00 1.00   ? 33  VAL B CG1 1 
ATOM   1314 C  CG2 . VAL B 2 33  ? 31.820 53.776 57.465 1.00 1.00   ? 33  VAL B CG2 1 
ATOM   1315 N  N   . VAL B 2 34  ? 36.243 52.808 56.888 1.00 1.00   ? 34  VAL B N   1 
ATOM   1316 C  CA  . VAL B 2 34  ? 37.517 52.181 57.154 1.00 1.00   ? 34  VAL B CA  1 
ATOM   1317 C  C   . VAL B 2 34  ? 38.748 53.054 56.826 1.00 1.00   ? 34  VAL B C   1 
ATOM   1318 O  O   . VAL B 2 34  ? 39.804 52.865 57.457 1.00 1.00   ? 34  VAL B O   1 
ATOM   1319 C  CB  . VAL B 2 34  ? 37.592 50.864 56.382 1.00 1.00   ? 34  VAL B CB  1 
ATOM   1320 C  CG1 . VAL B 2 34  ? 38.969 50.209 56.493 1.00 1.00   ? 34  VAL B CG1 1 
ATOM   1321 C  CG2 . VAL B 2 34  ? 36.505 49.947 56.912 1.00 1.00   ? 34  VAL B CG2 1 
ATOM   1322 N  N   . TYR B 2 35  ? 38.650 53.987 55.869 1.00 1.00   ? 35  TYR B N   1 
ATOM   1323 C  CA  . TYR B 2 35  ? 39.791 54.864 55.532 1.00 1.00   ? 35  TYR B CA  1 
ATOM   1324 C  C   . TYR B 2 35  ? 39.393 56.337 55.590 1.00 1.00   ? 35  TYR B C   1 
ATOM   1325 O  O   . TYR B 2 35  ? 39.451 57.053 54.591 1.00 1.00   ? 35  TYR B O   1 
ATOM   1326 C  CB  . TYR B 2 35  ? 40.362 54.478 54.176 1.00 1.00   ? 35  TYR B CB  1 
ATOM   1327 C  CG  . TYR B 2 35  ? 40.823 53.040 54.121 1.00 1.00   ? 35  TYR B CG  1 
ATOM   1328 C  CD1 . TYR B 2 35  ? 41.741 52.561 55.061 1.00 1.00   ? 35  TYR B CD1 1 
ATOM   1329 C  CD2 . TYR B 2 35  ? 40.344 52.139 53.134 1.00 1.00   ? 35  TYR B CD2 1 
ATOM   1330 C  CE1 . TYR B 2 35  ? 42.181 51.246 55.038 1.00 1.00   ? 35  TYR B CE1 1 
ATOM   1331 C  CE2 . TYR B 2 35  ? 40.779 50.810 53.101 1.00 1.00   ? 35  TYR B CE2 1 
ATOM   1332 C  CZ  . TYR B 2 35  ? 41.705 50.375 54.061 1.00 1.00   ? 35  TYR B CZ  1 
ATOM   1333 O  OH  . TYR B 2 35  ? 42.189 49.082 54.113 1.00 1.00   ? 35  TYR B OH  1 
ATOM   1334 N  N   . PRO B 2 36  ? 39.014 56.803 56.789 1.00 1.00   ? 36  PRO B N   1 
ATOM   1335 C  CA  . PRO B 2 36  ? 38.306 58.077 57.034 1.00 1.00   ? 36  PRO B CA  1 
ATOM   1336 C  C   . PRO B 2 36  ? 38.727 59.257 56.166 1.00 1.00   ? 36  PRO B C   1 
ATOM   1337 O  O   . PRO B 2 36  ? 37.859 60.011 55.696 1.00 1.00   ? 36  PRO B O   1 
ATOM   1338 C  CB  . PRO B 2 36  ? 38.648 58.400 58.484 1.00 1.00   ? 36  PRO B CB  1 
ATOM   1339 C  CG  . PRO B 2 36  ? 38.935 57.080 59.113 1.00 1.00   ? 36  PRO B CG  1 
ATOM   1340 C  CD  . PRO B 2 36  ? 39.448 56.166 58.047 1.00 1.00   ? 36  PRO B CD  1 
ATOM   1341 N  N   . TRP B 2 37  ? 40.035 59.430 55.958 1.00 1.00   ? 37  TRP B N   1 
ATOM   1342 C  CA  . TRP B 2 37  ? 40.510 60.561 55.145 1.00 1.00   ? 37  TRP B CA  1 
ATOM   1343 C  C   . TRP B 2 37  ? 39.871 60.617 53.771 1.00 1.00   ? 37  TRP B C   1 
ATOM   1344 O  O   . TRP B 2 37  ? 39.955 61.647 53.119 1.00 1.00   ? 37  TRP B O   1 
ATOM   1345 C  CB  . TRP B 2 37  ? 42.022 60.573 54.977 1.00 1.00   ? 37  TRP B CB  1 
ATOM   1346 C  CG  . TRP B 2 37  ? 42.511 59.411 54.270 1.00 1.00   ? 37  TRP B CG  1 
ATOM   1347 C  CD1 . TRP B 2 37  ? 42.603 59.229 52.897 1.00 1.00   ? 37  TRP B CD1 1 
ATOM   1348 C  CD2 . TRP B 2 37  ? 42.956 58.209 54.866 1.00 1.00   ? 37  TRP B CD2 1 
ATOM   1349 N  NE1 . TRP B 2 37  ? 43.105 57.975 52.622 1.00 1.00   ? 37  TRP B NE1 1 
ATOM   1350 C  CE2 . TRP B 2 37  ? 43.326 57.324 53.811 1.00 1.00   ? 37  TRP B CE2 1 
ATOM   1351 C  CE3 . TRP B 2 37  ? 43.083 57.783 56.187 1.00 1.00   ? 37  TRP B CE3 1 
ATOM   1352 C  CZ2 . TRP B 2 37  ? 43.808 56.039 54.048 1.00 1.00   ? 37  TRP B CZ2 1 
ATOM   1353 C  CZ3 . TRP B 2 37  ? 43.574 56.497 56.422 1.00 1.00   ? 37  TRP B CZ3 1 
ATOM   1354 C  CH2 . TRP B 2 37  ? 43.934 55.642 55.352 1.00 1.00   ? 37  TRP B CH2 1 
ATOM   1355 N  N   . THR B 2 38  ? 39.296 59.506 53.304 1.00 1.00   ? 38  THR B N   1 
ATOM   1356 C  CA  . THR B 2 38  ? 38.605 59.501 52.029 1.00 1.00   ? 38  THR B CA  1 
ATOM   1357 C  C   . THR B 2 38  ? 37.365 60.346 52.059 1.00 1.00   ? 38  THR B C   1 
ATOM   1358 O  O   . THR B 2 38  ? 36.936 60.807 51.007 1.00 1.00   ? 38  THR B O   1 
ATOM   1359 C  CB  . THR B 2 38  ? 38.161 58.107 51.618 1.00 1.00   ? 38  THR B CB  1 
ATOM   1360 O  OG1 . THR B 2 38  ? 37.489 57.506 52.727 1.00 1.00   ? 38  THR B OG1 1 
ATOM   1361 C  CG2 . THR B 2 38  ? 39.357 57.269 51.177 1.00 1.00   ? 38  THR B CG2 1 
ATOM   1362 N  N   . GLN B 2 39  ? 36.779 60.550 53.233 1.00 4.93   ? 39  GLN B N   1 
ATOM   1363 C  CA  . GLN B 2 39  ? 35.625 61.433 53.320 1.00 8.60   ? 39  GLN B CA  1 
ATOM   1364 C  C   . GLN B 2 39  ? 35.857 62.819 52.798 1.00 11.11  ? 39  GLN B C   1 
ATOM   1365 O  O   . GLN B 2 39  ? 34.945 63.403 52.220 1.00 11.88  ? 39  GLN B O   1 
ATOM   1366 C  CB  . GLN B 2 39  ? 35.116 61.555 54.733 1.00 9.81   ? 39  GLN B CB  1 
ATOM   1367 C  CG  . GLN B 2 39  ? 34.246 60.365 55.088 1.00 11.21  ? 39  GLN B CG  1 
ATOM   1368 C  CD  . GLN B 2 39  ? 34.187 60.141 56.575 1.00 12.79  ? 39  GLN B CD  1 
ATOM   1369 O  OE1 . GLN B 2 39  ? 34.545 61.038 57.369 1.00 14.37  ? 39  GLN B OE1 1 
ATOM   1370 N  NE2 . GLN B 2 39  ? 33.745 58.942 56.977 1.00 13.23  ? 39  GLN B NE2 1 
ATOM   1371 N  N   . ARG B 2 40  ? 37.054 63.352 52.985 1.00 14.31  ? 40  ARG B N   1 
ATOM   1372 C  CA  . ARG B 2 40  ? 37.349 64.680 52.498 1.00 17.53  ? 40  ARG B CA  1 
ATOM   1373 C  C   . ARG B 2 40  ? 36.908 64.868 51.043 1.00 19.52  ? 40  ARG B C   1 
ATOM   1374 O  O   . ARG B 2 40  ? 36.486 65.965 50.688 1.00 19.97  ? 40  ARG B O   1 
ATOM   1375 C  CB  . ARG B 2 40  ? 38.828 64.970 52.664 1.00 20.28  ? 40  ARG B CB  1 
ATOM   1376 C  CG  . ARG B 2 40  ? 39.304 66.286 52.094 1.00 23.70  ? 40  ARG B CG  1 
ATOM   1377 C  CD  . ARG B 2 40  ? 40.816 66.306 51.994 1.00 28.06  ? 40  ARG B CD  1 
ATOM   1378 N  NE  . ARG B 2 40  ? 41.283 67.565 51.427 1.00 33.43  ? 40  ARG B NE  1 
ATOM   1379 C  CZ  . ARG B 2 40  ? 41.276 68.743 52.067 1.00 41.57  ? 40  ARG B CZ  1 
ATOM   1380 N  NH1 . ARG B 2 40  ? 41.732 69.826 51.432 1.00 46.55  ? 40  ARG B NH1 1 
ATOM   1381 N  NH2 . ARG B 2 40  ? 40.820 68.873 53.329 1.00 41.65  ? 40  ARG B NH2 1 
ATOM   1382 N  N   . PHE B 2 41  ? 36.977 63.828 50.210 1.00 22.40  ? 41  PHE B N   1 
ATOM   1383 C  CA  . PHE B 2 41  ? 36.539 63.966 48.816 1.00 26.46  ? 41  PHE B CA  1 
ATOM   1384 C  C   . PHE B 2 41  ? 35.025 64.121 48.655 1.00 30.02  ? 41  PHE B C   1 
ATOM   1385 O  O   . PHE B 2 41  ? 34.580 64.870 47.789 1.00 32.55  ? 41  PHE B O   1 
ATOM   1386 C  CB  . PHE B 2 41  ? 37.038 62.818 47.947 1.00 27.91  ? 41  PHE B CB  1 
ATOM   1387 C  CG  . PHE B 2 41  ? 38.525 62.709 47.906 1.00 30.79  ? 41  PHE B CG  1 
ATOM   1388 C  CD1 . PHE B 2 41  ? 39.296 63.747 47.386 1.00 32.88  ? 41  PHE B CD1 1 
ATOM   1389 C  CD2 . PHE B 2 41  ? 39.173 61.582 48.412 1.00 32.90  ? 41  PHE B CD2 1 
ATOM   1390 C  CE1 . PHE B 2 41  ? 40.692 63.660 47.363 1.00 34.13  ? 41  PHE B CE1 1 
ATOM   1391 C  CE2 . PHE B 2 41  ? 40.565 61.486 48.388 1.00 34.52  ? 41  PHE B CE2 1 
ATOM   1392 C  CZ  . PHE B 2 41  ? 41.329 62.527 47.862 1.00 34.15  ? 41  PHE B CZ  1 
ATOM   1393 N  N   . PHE B 2 42  ? 34.239 63.434 49.475 1.00 32.96  ? 42  PHE B N   1 
ATOM   1394 C  CA  . PHE B 2 42  ? 32.788 63.480 49.352 1.00 36.42  ? 42  PHE B CA  1 
ATOM   1395 C  C   . PHE B 2 42  ? 32.109 64.389 50.387 1.00 44.63  ? 42  PHE B C   1 
ATOM   1396 O  O   . PHE B 2 42  ? 30.964 64.133 50.742 1.00 47.40  ? 42  PHE B O   1 
ATOM   1397 C  CB  . PHE B 2 42  ? 32.210 62.071 49.509 1.00 34.96  ? 42  PHE B CB  1 
ATOM   1398 C  CG  . PHE B 2 42  ? 32.866 61.041 48.663 1.00 34.05  ? 42  PHE B CG  1 
ATOM   1399 C  CD1 . PHE B 2 42  ? 32.547 60.929 47.329 1.00 35.11  ? 42  PHE B CD1 1 
ATOM   1400 C  CD2 . PHE B 2 42  ? 33.785 60.153 49.202 1.00 35.33  ? 42  PHE B CD2 1 
ATOM   1401 C  CE1 . PHE B 2 42  ? 33.148 59.960 46.526 1.00 35.99  ? 42  PHE B CE1 1 
ATOM   1402 C  CE2 . PHE B 2 42  ? 34.395 59.180 48.403 1.00 35.90  ? 42  PHE B CE2 1 
ATOM   1403 C  CZ  . PHE B 2 42  ? 34.079 59.085 47.062 1.00 34.81  ? 42  PHE B CZ  1 
ATOM   1404 N  N   . GLU B 2 43  ? 32.755 65.448 50.873 1.00 59.08  ? 43  GLU B N   1 
ATOM   1405 C  CA  . GLU B 2 43  ? 32.104 66.310 51.892 1.00 76.28  ? 43  GLU B CA  1 
ATOM   1406 C  C   . GLU B 2 43  ? 30.823 67.012 51.395 1.00 79.54  ? 43  GLU B C   1 
ATOM   1407 O  O   . GLU B 2 43  ? 30.003 67.460 52.201 1.00 77.83  ? 43  GLU B O   1 
ATOM   1408 C  CB  . GLU B 2 43  ? 33.084 67.330 52.486 1.00 96.91  ? 43  GLU B CB  1 
ATOM   1409 C  CG  . GLU B 2 43  ? 33.516 68.464 51.557 1.00 116.57 ? 43  GLU B CG  1 
ATOM   1410 C  CD  . GLU B 2 43  ? 34.718 69.248 52.087 1.00 137.82 ? 43  GLU B CD  1 
ATOM   1411 O  OE1 . GLU B 2 43  ? 35.002 69.194 53.307 1.00 146.00 ? 43  GLU B OE1 1 
ATOM   1412 O  OE2 . GLU B 2 43  ? 35.387 69.928 51.276 1.00 149.12 ? 43  GLU B OE2 1 
ATOM   1413 N  N   . SER B 2 44  ? 30.664 67.089 50.072 1.00 81.32  ? 44  SER B N   1 
ATOM   1414 C  CA  . SER B 2 44  ? 29.416 67.512 49.428 1.00 80.39  ? 44  SER B CA  1 
ATOM   1415 C  C   . SER B 2 44  ? 28.214 66.541 49.547 1.00 74.58  ? 44  SER B C   1 
ATOM   1416 O  O   . SER B 2 44  ? 27.110 66.896 49.127 1.00 74.62  ? 44  SER B O   1 
ATOM   1417 C  CB  . SER B 2 44  ? 29.689 67.772 47.945 1.00 83.88  ? 44  SER B CB  1 
ATOM   1418 O  OG  . SER B 2 44  ? 30.173 66.598 47.308 1.00 82.90  ? 44  SER B OG  1 
ATOM   1419 N  N   . PHE B 2 45  ? 28.417 65.338 50.095 1.00 66.72  ? 45  PHE B N   1 
ATOM   1420 C  CA  . PHE B 2 45  ? 27.325 64.379 50.320 1.00 63.06  ? 45  PHE B CA  1 
ATOM   1421 C  C   . PHE B 2 45  ? 26.688 64.500 51.710 1.00 65.69  ? 45  PHE B C   1 
ATOM   1422 O  O   . PHE B 2 45  ? 26.066 63.548 52.188 1.00 63.91  ? 45  PHE B O   1 
ATOM   1423 C  CB  . PHE B 2 45  ? 27.808 62.924 50.141 1.00 60.99  ? 45  PHE B CB  1 
ATOM   1424 C  CG  . PHE B 2 45  ? 28.218 62.542 48.738 1.00 59.18  ? 45  PHE B CG  1 
ATOM   1425 C  CD1 . PHE B 2 45  ? 28.118 63.417 47.647 1.00 61.66  ? 45  PHE B CD1 1 
ATOM   1426 C  CD2 . PHE B 2 45  ? 28.681 61.247 48.507 1.00 56.71  ? 45  PHE B CD2 1 
ATOM   1427 C  CE1 . PHE B 2 45  ? 28.498 63.006 46.374 1.00 64.12  ? 45  PHE B CE1 1 
ATOM   1428 C  CE2 . PHE B 2 45  ? 29.061 60.838 47.239 1.00 58.70  ? 45  PHE B CE2 1 
ATOM   1429 C  CZ  . PHE B 2 45  ? 28.967 61.713 46.169 1.00 61.45  ? 45  PHE B CZ  1 
ATOM   1430 N  N   . GLY B 2 46  ? 26.822 65.647 52.367 1.00 75.81  ? 46  GLY B N   1 
ATOM   1431 C  CA  . GLY B 2 46  ? 26.125 65.865 53.630 1.00 91.26  ? 46  GLY B CA  1 
ATOM   1432 C  C   . GLY B 2 46  ? 26.743 65.089 54.779 1.00 103.01 ? 46  GLY B C   1 
ATOM   1433 O  O   . GLY B 2 46  ? 27.970 65.051 54.914 1.00 110.63 ? 46  GLY B O   1 
ATOM   1434 N  N   . ASP B 2 47  ? 25.902 64.459 55.598 1.00 107.35 ? 47  ASP B N   1 
ATOM   1435 C  CA  . ASP B 2 47  ? 26.359 63.880 56.861 1.00 110.43 ? 47  ASP B CA  1 
ATOM   1436 C  C   . ASP B 2 47  ? 27.069 62.547 56.663 1.00 93.21  ? 47  ASP B C   1 
ATOM   1437 O  O   . ASP B 2 47  ? 26.533 61.643 56.024 1.00 89.67  ? 47  ASP B O   1 
ATOM   1438 C  CB  . ASP B 2 47  ? 25.185 63.698 57.826 1.00 132.37 ? 47  ASP B CB  1 
ATOM   1439 C  CG  . ASP B 2 47  ? 25.639 63.425 59.256 1.00 150.50 ? 47  ASP B CG  1 
ATOM   1440 O  OD1 . ASP B 2 47  ? 26.444 64.220 59.791 1.00 162.40 ? 47  ASP B OD1 1 
ATOM   1441 O  OD2 . ASP B 2 47  ? 25.187 62.419 59.845 1.00 156.11 ? 47  ASP B OD2 1 
ATOM   1442 N  N   . LEU B 2 48  ? 28.299 62.447 57.160 1.00 83.34  ? 48  LEU B N   1 
ATOM   1443 C  CA  . LEU B 2 48  ? 29.074 61.208 57.091 1.00 79.90  ? 48  LEU B CA  1 
ATOM   1444 C  C   . LEU B 2 48  ? 29.703 60.828 58.443 1.00 85.15  ? 48  LEU B C   1 
ATOM   1445 O  O   . LEU B 2 48  ? 30.597 59.990 58.504 1.00 81.95  ? 48  LEU B O   1 
ATOM   1446 C  CB  . LEU B 2 48  ? 30.151 61.312 56.012 1.00 70.62  ? 48  LEU B CB  1 
ATOM   1447 C  CG  . LEU B 2 48  ? 29.678 61.750 54.628 1.00 62.36  ? 48  LEU B CG  1 
ATOM   1448 C  CD1 . LEU B 2 48  ? 30.702 62.662 53.979 1.00 61.35  ? 48  LEU B CD1 1 
ATOM   1449 C  CD2 . LEU B 2 48  ? 29.411 60.543 53.748 1.00 59.62  ? 48  LEU B CD2 1 
ATOM   1450 N  N   . SER B 2 49  ? 29.221 61.437 59.520 1.00 95.57  ? 49  SER B N   1 
ATOM   1451 C  CA  . SER B 2 49  ? 29.789 61.237 60.861 1.00 108.04 ? 49  SER B CA  1 
ATOM   1452 C  C   . SER B 2 49  ? 29.773 59.855 61.540 1.00 108.32 ? 49  SER B C   1 
ATOM   1453 O  O   . SER B 2 49  ? 30.770 59.459 62.143 1.00 104.81 ? 49  SER B O   1 
ATOM   1454 C  CB  . SER B 2 49  ? 29.173 62.255 61.824 1.00 115.44 ? 49  SER B CB  1 
ATOM   1455 O  OG  . SER B 2 49  ? 27.816 61.943 62.079 1.00 116.27 ? 49  SER B OG  1 
ATOM   1456 N  N   . THR B 2 50  ? 28.670 59.122 61.451 1.00 106.76 ? 50  THR B N   1 
ATOM   1457 C  CA  . THR B 2 50  ? 28.587 57.822 62.120 1.00 103.54 ? 50  THR B CA  1 
ATOM   1458 C  C   . THR B 2 50  ? 28.363 56.678 61.146 1.00 92.91  ? 50  THR B C   1 
ATOM   1459 O  O   . THR B 2 50  ? 27.549 56.792 60.234 1.00 90.18  ? 50  THR B O   1 
ATOM   1460 C  CB  . THR B 2 50  ? 27.480 57.806 63.189 1.00 113.28 ? 50  THR B CB  1 
ATOM   1461 O  OG1 . THR B 2 50  ? 27.402 56.503 63.780 1.00 116.61 ? 50  THR B OG1 1 
ATOM   1462 C  CG2 . THR B 2 50  ? 26.139 58.157 62.574 1.00 117.33 ? 50  THR B CG2 1 
ATOM   1463 N  N   . PRO B 2 51  ? 29.081 55.562 61.331 1.00 91.05  ? 51  PRO B N   1 
ATOM   1464 C  CA  . PRO B 2 51  ? 28.849 54.508 60.348 1.00 92.20  ? 51  PRO B CA  1 
ATOM   1465 C  C   . PRO B 2 51  ? 27.421 54.396 59.820 1.00 95.85  ? 51  PRO B C   1 
ATOM   1466 O  O   . PRO B 2 51  ? 27.236 54.139 58.630 1.00 102.59 ? 51  PRO B O   1 
ATOM   1467 C  CB  . PRO B 2 51  ? 29.219 53.246 61.119 1.00 93.26  ? 51  PRO B CB  1 
ATOM   1468 C  CG  . PRO B 2 51  ? 30.333 53.692 62.000 1.00 95.41  ? 51  PRO B CG  1 
ATOM   1469 C  CD  . PRO B 2 51  ? 30.090 55.141 62.323 1.00 93.19  ? 51  PRO B CD  1 
ATOM   1470 N  N   . ASP B 2 52  ? 26.430 54.585 60.687 1.00 103.40 ? 52  ASP B N   1 
ATOM   1471 C  CA  . ASP B 2 52  ? 25.022 54.476 60.282 1.00 116.44 ? 52  ASP B CA  1 
ATOM   1472 C  C   . ASP B 2 52  ? 24.561 55.593 59.331 1.00 109.18 ? 52  ASP B C   1 
ATOM   1473 O  O   . ASP B 2 52  ? 23.667 55.379 58.505 1.00 108.91 ? 52  ASP B O   1 
ATOM   1474 C  CB  . ASP B 2 52  ? 24.115 54.418 61.516 1.00 135.14 ? 52  ASP B CB  1 
ATOM   1475 C  CG  . ASP B 2 52  ? 24.361 53.178 62.370 1.00 153.10 ? 52  ASP B CG  1 
ATOM   1476 O  OD1 . ASP B 2 52  ? 24.696 52.107 61.815 1.00 164.87 ? 52  ASP B OD1 1 
ATOM   1477 O  OD2 . ASP B 2 52  ? 24.210 53.274 63.606 1.00 170.81 ? 52  ASP B OD2 1 
ATOM   1478 N  N   . ALA B 2 53  ? 25.182 56.766 59.442 1.00 95.42  ? 53  ALA B N   1 
ATOM   1479 C  CA  . ALA B 2 53  ? 24.885 57.895 58.565 1.00 86.29  ? 53  ALA B CA  1 
ATOM   1480 C  C   . ALA B 2 53  ? 25.462 57.670 57.176 1.00 80.17  ? 53  ALA B C   1 
ATOM   1481 O  O   . ALA B 2 53  ? 24.850 58.069 56.188 1.00 87.79  ? 53  ALA B O   1 
ATOM   1482 C  CB  . ALA B 2 53  ? 25.434 59.186 59.153 1.00 87.21  ? 53  ALA B CB  1 
ATOM   1483 N  N   . VAL B 2 54  ? 26.638 57.045 57.108 1.00 70.44  ? 54  VAL B N   1 
ATOM   1484 C  CA  . VAL B 2 54  ? 27.296 56.752 55.835 1.00 64.92  ? 54  VAL B CA  1 
ATOM   1485 C  C   . VAL B 2 54  ? 26.551 55.657 55.093 1.00 64.19  ? 54  VAL B C   1 
ATOM   1486 O  O   . VAL B 2 54  ? 26.344 55.759 53.888 1.00 66.80  ? 54  VAL B O   1 
ATOM   1487 C  CB  . VAL B 2 54  ? 28.775 56.356 56.028 1.00 63.88  ? 54  VAL B CB  1 
ATOM   1488 C  CG1 . VAL B 2 54  ? 29.403 55.856 54.731 1.00 66.45  ? 54  VAL B CG1 1 
ATOM   1489 C  CG2 . VAL B 2 54  ? 29.566 57.540 56.553 1.00 66.74  ? 54  VAL B CG2 1 
ATOM   1490 N  N   . MET B 2 55  ? 26.158 54.609 55.799 1.00 68.59  ? 55  MET B N   1 
ATOM   1491 C  CA  . MET B 2 55  ? 25.378 53.549 55.176 1.00 81.12  ? 55  MET B CA  1 
ATOM   1492 C  C   . MET B 2 55  ? 23.954 54.007 54.857 1.00 88.04  ? 55  MET B C   1 
ATOM   1493 O  O   . MET B 2 55  ? 23.371 53.550 53.872 1.00 91.98  ? 55  MET B O   1 
ATOM   1494 C  CB  . MET B 2 55  ? 25.372 52.291 56.054 1.00 90.81  ? 55  MET B CB  1 
ATOM   1495 C  CG  . MET B 2 55  ? 26.744 51.629 56.202 1.00 96.26  ? 55  MET B CG  1 
ATOM   1496 S  SD  . MET B 2 55  ? 27.418 50.971 54.655 1.00 102.45 ? 55  MET B SD  1 
ATOM   1497 C  CE  . MET B 2 55  ? 29.048 50.429 55.153 1.00 95.83  ? 55  MET B CE  1 
ATOM   1498 N  N   . GLY B 2 56  ? 23.408 54.915 55.671 1.00 97.86  ? 56  GLY B N   1 
ATOM   1499 C  CA  . GLY B 2 56  ? 22.061 55.470 55.455 1.00 105.78 ? 56  GLY B CA  1 
ATOM   1500 C  C   . GLY B 2 56  ? 21.911 56.601 54.434 1.00 105.14 ? 56  GLY B C   1 
ATOM   1501 O  O   . GLY B 2 56  ? 20.788 57.012 54.132 1.00 108.54 ? 56  GLY B O   1 
ATOM   1502 N  N   . ASN B 2 57  ? 23.026 57.102 53.902 1.00 97.92  ? 57  ASN B N   1 
ATOM   1503 C  CA  . ASN B 2 57  ? 23.019 58.224 52.963 1.00 93.24  ? 57  ASN B CA  1 
ATOM   1504 C  C   . ASN B 2 57  ? 22.550 57.745 51.579 1.00 95.77  ? 57  ASN B C   1 
ATOM   1505 O  O   . ASN B 2 57  ? 23.075 56.750 51.076 1.00 101.31 ? 57  ASN B O   1 
ATOM   1506 C  CB  . ASN B 2 57  ? 24.431 58.807 52.862 1.00 93.37  ? 57  ASN B CB  1 
ATOM   1507 C  CG  . ASN B 2 57  ? 24.466 60.197 52.262 1.00 99.21  ? 57  ASN B CG  1 
ATOM   1508 O  OD1 . ASN B 2 57  ? 23.517 60.656 51.627 1.00 104.83 ? 57  ASN B OD1 1 
ATOM   1509 N  ND2 . ASN B 2 57  ? 25.583 60.880 52.464 1.00 104.70 ? 57  ASN B ND2 1 
ATOM   1510 N  N   . PRO B 2 58  ? 21.562 58.434 50.962 1.00 97.47  ? 58  PRO B N   1 
ATOM   1511 C  CA  . PRO B 2 58  ? 21.144 58.069 49.590 1.00 100.29 ? 58  PRO B CA  1 
ATOM   1512 C  C   . PRO B 2 58  ? 22.153 58.369 48.470 1.00 99.81  ? 58  PRO B C   1 
ATOM   1513 O  O   . PRO B 2 58  ? 22.242 57.599 47.506 1.00 97.00  ? 58  PRO B O   1 
ATOM   1514 C  CB  . PRO B 2 58  ? 19.870 58.896 49.374 1.00 102.04 ? 58  PRO B CB  1 
ATOM   1515 C  CG  . PRO B 2 58  ? 19.382 59.215 50.741 1.00 101.70 ? 58  PRO B CG  1 
ATOM   1516 C  CD  . PRO B 2 58  ? 20.613 59.383 51.573 1.00 97.64  ? 58  PRO B CD  1 
ATOM   1517 N  N   . LYS B 2 59  ? 22.878 59.484 48.589 1.00 96.83  ? 59  LYS B N   1 
ATOM   1518 C  CA  . LYS B 2 59  ? 23.872 59.887 47.583 1.00 94.24  ? 59  LYS B CA  1 
ATOM   1519 C  C   . LYS B 2 59  ? 25.041 58.922 47.507 1.00 83.52  ? 59  LYS B C   1 
ATOM   1520 O  O   . LYS B 2 59  ? 25.587 58.691 46.422 1.00 81.02  ? 59  LYS B O   1 
ATOM   1521 C  CB  . LYS B 2 59  ? 24.417 61.281 47.872 1.00 101.14 ? 59  LYS B CB  1 
ATOM   1522 C  CG  . LYS B 2 59  ? 23.398 62.387 47.720 1.00 112.54 ? 59  LYS B CG  1 
ATOM   1523 C  CD  . LYS B 2 59  ? 24.037 63.732 48.003 1.00 125.34 ? 59  LYS B CD  1 
ATOM   1524 C  CE  . LYS B 2 59  ? 23.012 64.851 47.994 1.00 136.47 ? 59  LYS B CE  1 
ATOM   1525 N  NZ  . LYS B 2 59  ? 23.650 66.180 48.201 1.00 141.54 ? 59  LYS B NZ  1 
ATOM   1526 N  N   . VAL B 2 60  ? 25.425 58.374 48.659 1.00 69.63  ? 60  VAL B N   1 
ATOM   1527 C  CA  . VAL B 2 60  ? 26.492 57.393 48.709 1.00 63.37  ? 60  VAL B CA  1 
ATOM   1528 C  C   . VAL B 2 60  ? 26.066 56.190 47.894 1.00 64.83  ? 60  VAL B C   1 
ATOM   1529 O  O   . VAL B 2 60  ? 26.777 55.797 46.972 1.00 71.85  ? 60  VAL B O   1 
ATOM   1530 C  CB  . VAL B 2 60  ? 26.868 57.005 50.151 1.00 60.59  ? 60  VAL B CB  1 
ATOM   1531 C  CG1 . VAL B 2 60  ? 27.851 55.831 50.182 1.00 58.76  ? 60  VAL B CG1 1 
ATOM   1532 C  CG2 . VAL B 2 60  ? 27.474 58.211 50.856 1.00 63.25  ? 60  VAL B CG2 1 
ATOM   1533 N  N   . LYS B 2 61  ? 24.896 55.633 48.193 1.00 66.79  ? 61  LYS B N   1 
ATOM   1534 C  CA  . LYS B 2 61  ? 24.412 54.483 47.431 1.00 70.46  ? 61  LYS B CA  1 
ATOM   1535 C  C   . LYS B 2 61  ? 24.257 54.830 45.956 1.00 64.29  ? 61  LYS B C   1 
ATOM   1536 O  O   . LYS B 2 61  ? 24.578 54.015 45.094 1.00 65.38  ? 61  LYS B O   1 
ATOM   1537 C  CB  . LYS B 2 61  ? 23.098 53.943 47.987 1.00 82.05  ? 61  LYS B CB  1 
ATOM   1538 C  CG  . LYS B 2 61  ? 22.733 52.577 47.417 1.00 97.81  ? 61  LYS B CG  1 
ATOM   1539 C  CD  . LYS B 2 61  ? 21.471 51.990 48.039 1.00 115.49 ? 61  LYS B CD  1 
ATOM   1540 C  CE  . LYS B 2 61  ? 20.181 52.549 47.437 1.00 128.64 ? 61  LYS B CE  1 
ATOM   1541 N  NZ  . LYS B 2 61  ? 19.782 53.898 47.940 1.00 135.16 ? 61  LYS B NZ  1 
ATOM   1542 N  N   . ALA B 2 62  ? 23.784 56.041 45.680 1.00 62.06  ? 62  ALA B N   1 
ATOM   1543 C  CA  . ALA B 2 62  ? 23.626 56.514 44.310 1.00 63.83  ? 62  ALA B CA  1 
ATOM   1544 C  C   . ALA B 2 62  ? 24.951 56.561 43.556 1.00 60.18  ? 62  ALA B C   1 
ATOM   1545 O  O   . ALA B 2 62  ? 25.061 56.023 42.446 1.00 58.76  ? 62  ALA B O   1 
ATOM   1546 C  CB  . ALA B 2 62  ? 22.979 57.886 44.304 1.00 69.76  ? 62  ALA B CB  1 
ATOM   1547 N  N   . HIS B 2 63  ? 25.944 57.204 44.166 1.00 55.20  ? 63  HIS B N   1 
ATOM   1548 C  CA  . HIS B 2 63  ? 27.279 57.306 43.576 1.00 53.12  ? 63  HIS B CA  1 
ATOM   1549 C  C   . HIS B 2 63  ? 27.969 55.948 43.457 1.00 49.42  ? 63  HIS B C   1 
ATOM   1550 O  O   . HIS B 2 63  ? 28.684 55.693 42.492 1.00 47.67  ? 63  HIS B O   1 
ATOM   1551 C  CB  . HIS B 2 63  ? 28.157 58.248 44.387 1.00 53.13  ? 63  HIS B CB  1 
ATOM   1552 C  CG  . HIS B 2 63  ? 29.540 58.370 43.848 1.00 54.16  ? 63  HIS B CG  1 
ATOM   1553 N  ND1 . HIS B 2 63  ? 29.878 59.300 42.893 1.00 60.07  ? 63  HIS B ND1 1 
ATOM   1554 C  CD2 . HIS B 2 63  ? 30.660 57.651 44.091 1.00 55.02  ? 63  HIS B CD2 1 
ATOM   1555 C  CE1 . HIS B 2 63  ? 31.154 59.159 42.582 1.00 64.83  ? 63  HIS B CE1 1 
ATOM   1556 N  NE2 . HIS B 2 63  ? 31.653 58.167 43.298 1.00 60.26  ? 63  HIS B NE2 1 
ATOM   1557 N  N   . GLY B 2 64  ? 27.759 55.095 44.451 1.00 48.46  ? 64  GLY B N   1 
ATOM   1558 C  CA  . GLY B 2 64  ? 28.241 53.733 44.409 1.00 50.75  ? 64  GLY B CA  1 
ATOM   1559 C  C   . GLY B 2 64  ? 27.803 53.003 43.158 1.00 55.77  ? 64  GLY B C   1 
ATOM   1560 O  O   . GLY B 2 64  ? 28.610 52.322 42.529 1.00 61.17  ? 64  GLY B O   1 
ATOM   1561 N  N   . LYS B 2 65  ? 26.537 53.158 42.779 1.00 62.43  ? 65  LYS B N   1 
ATOM   1562 C  CA  . LYS B 2 65  ? 26.009 52.478 41.597 1.00 68.68  ? 65  LYS B CA  1 
ATOM   1563 C  C   . LYS B 2 65  ? 26.827 52.771 40.331 1.00 66.89  ? 65  LYS B C   1 
ATOM   1564 O  O   . LYS B 2 65  ? 27.024 51.874 39.504 1.00 66.55  ? 65  LYS B O   1 
ATOM   1565 C  CB  . LYS B 2 65  ? 24.542 52.834 41.369 1.00 79.43  ? 65  LYS B CB  1 
ATOM   1566 C  CG  . LYS B 2 65  ? 23.870 51.973 40.303 1.00 94.45  ? 65  LYS B CG  1 
ATOM   1567 C  CD  . LYS B 2 65  ? 22.423 52.376 40.039 1.00 107.40 ? 65  LYS B CD  1 
ATOM   1568 C  CE  . LYS B 2 65  ? 21.428 51.687 40.971 1.00 111.92 ? 65  LYS B CE  1 
ATOM   1569 N  NZ  . LYS B 2 65  ? 21.453 52.185 42.377 1.00 111.91 ? 65  LYS B NZ  1 
ATOM   1570 N  N   . LYS B 2 66  ? 27.297 54.012 40.189 1.00 63.03  ? 66  LYS B N   1 
ATOM   1571 C  CA  . LYS B 2 66  ? 28.150 54.393 39.052 1.00 61.92  ? 66  LYS B CA  1 
ATOM   1572 C  C   . LYS B 2 66  ? 29.521 53.716 39.077 1.00 51.06  ? 66  LYS B C   1 
ATOM   1573 O  O   . LYS B 2 66  ? 30.027 53.299 38.034 1.00 46.52  ? 66  LYS B O   1 
ATOM   1574 C  CB  . LYS B 2 66  ? 28.303 55.918 38.963 1.00 69.37  ? 66  LYS B CB  1 
ATOM   1575 C  CG  . LYS B 2 66  ? 27.040 56.596 38.460 1.00 82.48  ? 66  LYS B CG  1 
ATOM   1576 C  CD  . LYS B 2 66  ? 27.146 58.116 38.409 1.00 93.82  ? 66  LYS B CD  1 
ATOM   1577 C  CE  . LYS B 2 66  ? 26.915 58.762 39.774 1.00 101.69 ? 66  LYS B CE  1 
ATOM   1578 N  NZ  . LYS B 2 66  ? 26.781 60.247 39.704 1.00 102.34 ? 66  LYS B NZ  1 
ATOM   1579 N  N   . VAL B 2 67  ? 30.102 53.608 40.270 1.00 44.81  ? 67  VAL B N   1 
ATOM   1580 C  CA  . VAL B 2 67  ? 31.432 53.042 40.438 1.00 41.09  ? 67  VAL B CA  1 
ATOM   1581 C  C   . VAL B 2 67  ? 31.421 51.611 39.991 1.00 40.97  ? 67  VAL B C   1 
ATOM   1582 O  O   . VAL B 2 67  ? 32.265 51.215 39.205 1.00 41.42  ? 67  VAL B O   1 
ATOM   1583 C  CB  . VAL B 2 67  ? 31.917 53.094 41.900 1.00 40.74  ? 67  VAL B CB  1 
ATOM   1584 C  CG1 . VAL B 2 67  ? 33.177 52.266 42.094 1.00 40.85  ? 67  VAL B CG1 1 
ATOM   1585 C  CG2 . VAL B 2 67  ? 32.181 54.529 42.331 1.00 42.77  ? 67  VAL B CG2 1 
ATOM   1586 N  N   . LEU B 2 68  ? 30.469 50.835 40.490 1.00 46.12  ? 68  LEU B N   1 
ATOM   1587 C  CA  . LEU B 2 68  ? 30.385 49.426 40.114 1.00 53.46  ? 68  LEU B CA  1 
ATOM   1588 C  C   . LEU B 2 68  ? 30.048 49.243 38.624 1.00 57.42  ? 68  LEU B C   1 
ATOM   1589 O  O   . LEU B 2 68  ? 30.512 48.288 37.991 1.00 53.47  ? 68  LEU B O   1 
ATOM   1590 C  CB  . LEU B 2 68  ? 29.383 48.672 40.988 1.00 57.29  ? 68  LEU B CB  1 
ATOM   1591 C  CG  . LEU B 2 68  ? 29.644 47.160 41.035 1.00 61.10  ? 68  LEU B CG  1 
ATOM   1592 C  CD1 . LEU B 2 68  ? 30.910 46.847 41.822 1.00 61.08  ? 68  LEU B CD1 1 
ATOM   1593 C  CD2 . LEU B 2 68  ? 28.453 46.424 41.628 1.00 67.48  ? 68  LEU B CD2 1 
ATOM   1594 N  N   . GLY B 2 69  ? 29.254 50.161 38.072 1.00 62.00  ? 69  GLY B N   1 
ATOM   1595 C  CA  . GLY B 2 69  ? 29.059 50.245 36.624 1.00 63.80  ? 69  GLY B CA  1 
ATOM   1596 C  C   . GLY B 2 69  ? 30.379 50.343 35.870 1.00 64.60  ? 69  GLY B C   1 
ATOM   1597 O  O   . GLY B 2 69  ? 30.598 49.619 34.897 1.00 66.26  ? 69  GLY B O   1 
ATOM   1598 N  N   . ALA B 2 70  ? 31.264 51.224 36.333 1.00 63.24  ? 70  ALA B N   1 
ATOM   1599 C  CA  . ALA B 2 70  ? 32.591 51.391 35.725 1.00 59.03  ? 70  ALA B CA  1 
ATOM   1600 C  C   . ALA B 2 70  ? 33.498 50.173 35.874 1.00 54.17  ? 70  ALA B C   1 
ATOM   1601 O  O   . ALA B 2 70  ? 34.325 49.947 35.004 1.00 55.07  ? 70  ALA B O   1 
ATOM   1602 C  CB  . ALA B 2 70  ? 33.287 52.628 36.272 1.00 59.23  ? 70  ALA B CB  1 
ATOM   1603 N  N   . PHE B 2 71  ? 33.373 49.416 36.965 1.00 52.64  ? 71  PHE B N   1 
ATOM   1604 C  CA  . PHE B 2 71  ? 34.087 48.139 37.081 1.00 55.12  ? 71  PHE B CA  1 
ATOM   1605 C  C   . PHE B 2 71  ? 33.551 47.137 36.088 1.00 61.34  ? 71  PHE B C   1 
ATOM   1606 O  O   . PHE B 2 71  ? 34.321 46.364 35.528 1.00 62.26  ? 71  PHE B O   1 
ATOM   1607 C  CB  . PHE B 2 71  ? 33.973 47.519 38.468 1.00 56.96  ? 71  PHE B CB  1 
ATOM   1608 C  CG  . PHE B 2 71  ? 35.032 47.965 39.418 1.00 61.68  ? 71  PHE B CG  1 
ATOM   1609 C  CD1 . PHE B 2 71  ? 36.255 47.316 39.465 1.00 62.34  ? 71  PHE B CD1 1 
ATOM   1610 C  CD2 . PHE B 2 71  ? 34.799 49.033 40.291 1.00 66.45  ? 71  PHE B CD2 1 
ATOM   1611 C  CE1 . PHE B 2 71  ? 37.235 47.734 40.360 1.00 68.54  ? 71  PHE B CE1 1 
ATOM   1612 C  CE2 . PHE B 2 71  ? 35.771 49.454 41.191 1.00 66.11  ? 71  PHE B CE2 1 
ATOM   1613 C  CZ  . PHE B 2 71  ? 36.992 48.803 41.226 1.00 69.17  ? 71  PHE B CZ  1 
ATOM   1614 N  N   . SER B 2 72  ? 32.231 47.133 35.895 1.00 70.62  ? 72  SER B N   1 
ATOM   1615 C  CA  . SER B 2 72  ? 31.584 46.204 34.959 1.00 77.56  ? 72  SER B CA  1 
ATOM   1616 C  C   . SER B 2 72  ? 32.044 46.450 33.524 1.00 84.04  ? 72  SER B C   1 
ATOM   1617 O  O   . SER B 2 72  ? 32.362 45.505 32.799 1.00 84.79  ? 72  SER B O   1 
ATOM   1618 C  CB  . SER B 2 72  ? 30.060 46.320 35.037 1.00 80.79  ? 72  SER B CB  1 
ATOM   1619 O  OG  . SER B 2 72  ? 29.601 46.350 36.377 1.00 79.07  ? 72  SER B OG  1 
ATOM   1620 N  N   . ASP B 2 73  ? 32.086 47.725 33.138 1.00 93.17  ? 73  ASP B N   1 
ATOM   1621 C  CA  . ASP B 2 73  ? 32.613 48.156 31.836 1.00 101.22 ? 73  ASP B CA  1 
ATOM   1622 C  C   . ASP B 2 73  ? 34.055 47.676 31.616 1.00 86.16  ? 73  ASP B C   1 
ATOM   1623 O  O   . ASP B 2 73  ? 34.386 47.130 30.564 1.00 79.44  ? 73  ASP B O   1 
ATOM   1624 C  CB  . ASP B 2 73  ? 32.546 49.693 31.734 1.00 122.36 ? 73  ASP B CB  1 
ATOM   1625 C  CG  . ASP B 2 73  ? 32.845 50.216 30.330 1.00 141.49 ? 73  ASP B CG  1 
ATOM   1626 O  OD1 . ASP B 2 73  ? 32.166 49.790 29.370 1.00 158.24 ? 73  ASP B OD1 1 
ATOM   1627 O  OD2 . ASP B 2 73  ? 33.746 51.072 30.193 1.00 147.98 ? 73  ASP B OD2 1 
ATOM   1628 N  N   . GLY B 2 74  ? 34.894 47.875 32.628 1.00 83.28  ? 74  GLY B N   1 
ATOM   1629 C  CA  . GLY B 2 74  ? 36.298 47.474 32.587 1.00 78.17  ? 74  GLY B CA  1 
ATOM   1630 C  C   . GLY B 2 74  ? 36.529 45.981 32.666 1.00 73.91  ? 74  GLY B C   1 
ATOM   1631 O  O   . GLY B 2 74  ? 37.603 45.507 32.315 1.00 73.14  ? 74  GLY B O   1 
ATOM   1632 N  N   . LEU B 2 75  ? 35.538 45.243 33.152 1.00 79.71  ? 75  LEU B N   1 
ATOM   1633 C  CA  . LEU B 2 75  ? 35.580 43.781 33.155 1.00 88.43  ? 75  LEU B CA  1 
ATOM   1634 C  C   . LEU B 2 75  ? 35.157 43.202 31.799 1.00 98.36  ? 75  LEU B C   1 
ATOM   1635 O  O   . LEU B 2 75  ? 35.528 42.073 31.462 1.00 100.35 ? 75  LEU B O   1 
ATOM   1636 C  CB  . LEU B 2 75  ? 34.695 43.242 34.277 1.00 87.83  ? 75  LEU B CB  1 
ATOM   1637 C  CG  . LEU B 2 75  ? 34.934 41.798 34.730 1.00 84.50  ? 75  LEU B CG  1 
ATOM   1638 C  CD1 . LEU B 2 75  ? 34.688 41.713 36.232 1.00 84.51  ? 75  LEU B CD1 1 
ATOM   1639 C  CD2 . LEU B 2 75  ? 34.068 40.803 33.961 1.00 88.61  ? 75  LEU B CD2 1 
ATOM   1640 N  N   . ALA B 2 76  ? 34.386 43.972 31.029 1.00 102.75 ? 76  ALA B N   1 
ATOM   1641 C  CA  . ALA B 2 76  ? 34.061 43.614 29.642 1.00 105.31 ? 76  ALA B CA  1 
ATOM   1642 C  C   . ALA B 2 76  ? 35.312 43.604 28.755 1.00 103.84 ? 76  ALA B C   1 
ATOM   1643 O  O   . ALA B 2 76  ? 35.598 42.610 28.085 1.00 101.46 ? 76  ALA B O   1 
ATOM   1644 C  CB  . ALA B 2 76  ? 33.019 44.569 29.070 1.00 106.07 ? 76  ALA B CB  1 
ATOM   1645 N  N   . HIS B 2 77  ? 36.054 44.709 28.783 1.00 103.78 ? 77  HIS B N   1 
ATOM   1646 C  CA  . HIS B 2 77  ? 37.224 44.906 27.928 1.00 107.00 ? 77  HIS B CA  1 
ATOM   1647 C  C   . HIS B 2 77  ? 38.541 44.723 28.685 1.00 104.12 ? 77  HIS B C   1 
ATOM   1648 O  O   . HIS B 2 77  ? 39.284 45.687 28.888 1.00 107.25 ? 77  HIS B O   1 
ATOM   1649 C  CB  . HIS B 2 77  ? 37.180 46.313 27.327 1.00 117.03 ? 77  HIS B CB  1 
ATOM   1650 C  CG  . HIS B 2 77  ? 35.967 46.579 26.499 1.00 131.99 ? 77  HIS B CG  1 
ATOM   1651 N  ND1 . HIS B 2 77  ? 34.827 47.158 27.014 1.00 136.44 ? 77  HIS B ND1 1 
ATOM   1652 C  CD2 . HIS B 2 77  ? 35.718 46.354 25.187 1.00 144.81 ? 77  HIS B CD2 1 
ATOM   1653 C  CE1 . HIS B 2 77  ? 33.926 47.276 26.055 1.00 147.54 ? 77  HIS B CE1 1 
ATOM   1654 N  NE2 . HIS B 2 77  ? 34.441 46.795 24.937 1.00 150.95 ? 77  HIS B NE2 1 
ATOM   1655 N  N   . LEU B 2 78  ? 38.840 43.491 29.091 1.00 102.64 ? 78  LEU B N   1 
ATOM   1656 C  CA  . LEU B 2 78  ? 40.092 43.204 29.811 1.00 106.15 ? 78  LEU B CA  1 
ATOM   1657 C  C   . LEU B 2 78  ? 41.345 43.415 28.950 1.00 109.60 ? 78  LEU B C   1 
ATOM   1658 O  O   . LEU B 2 78  ? 42.393 43.821 29.456 1.00 105.50 ? 78  LEU B O   1 
ATOM   1659 C  CB  . LEU B 2 78  ? 40.081 41.781 30.372 1.00 109.66 ? 78  LEU B CB  1 
ATOM   1660 C  CG  . LEU B 2 78  ? 39.043 41.490 31.458 1.00 115.63 ? 78  LEU B CG  1 
ATOM   1661 C  CD1 . LEU B 2 78  ? 39.076 40.013 31.821 1.00 120.11 ? 78  LEU B CD1 1 
ATOM   1662 C  CD2 . LEU B 2 78  ? 39.263 42.352 32.696 1.00 116.27 ? 78  LEU B CD2 1 
ATOM   1663 N  N   . ASP B 2 79  ? 41.226 43.125 27.658 1.00 122.48 ? 79  ASP B N   1 
ATOM   1664 C  CA  . ASP B 2 79  ? 42.298 43.374 26.684 1.00 131.19 ? 79  ASP B CA  1 
ATOM   1665 C  C   . ASP B 2 79  ? 42.824 44.818 26.673 1.00 120.75 ? 79  ASP B C   1 
ATOM   1666 O  O   . ASP B 2 79  ? 44.036 45.039 26.689 1.00 112.46 ? 79  ASP B O   1 
ATOM   1667 C  CB  . ASP B 2 79  ? 41.854 42.953 25.261 1.00 150.74 ? 79  ASP B CB  1 
ATOM   1668 C  CG  . ASP B 2 79  ? 40.525 43.599 24.810 1.00 159.82 ? 79  ASP B CG  1 
ATOM   1669 O  OD1 . ASP B 2 79  ? 39.878 44.315 25.608 1.00 165.60 ? 79  ASP B OD1 1 
ATOM   1670 O  OD2 . ASP B 2 79  ? 40.123 43.375 23.648 1.00 164.28 ? 79  ASP B OD2 1 
ATOM   1671 N  N   . ASN B 2 80  ? 41.904 45.780 26.665 1.00 122.55 ? 80  ASN B N   1 
ATOM   1672 C  CA  . ASN B 2 80  ? 42.222 47.195 26.499 1.00 129.14 ? 80  ASN B CA  1 
ATOM   1673 C  C   . ASN B 2 80  ? 41.624 47.962 27.669 1.00 123.43 ? 80  ASN B C   1 
ATOM   1674 O  O   . ASN B 2 80  ? 40.486 48.437 27.604 1.00 128.29 ? 80  ASN B O   1 
ATOM   1675 C  CB  . ASN B 2 80  ? 41.665 47.701 25.155 1.00 144.16 ? 80  ASN B CB  1 
ATOM   1676 C  CG  . ASN B 2 80  ? 41.974 49.171 24.888 1.00 157.03 ? 80  ASN B CG  1 
ATOM   1677 O  OD1 . ASN B 2 80  ? 42.876 49.761 25.490 1.00 165.21 ? 80  ASN B OD1 1 
ATOM   1678 N  ND2 . ASN B 2 80  ? 41.222 49.767 23.967 1.00 163.81 ? 80  ASN B ND2 1 
ATOM   1679 N  N   . LEU B 2 81  ? 42.398 48.069 28.743 1.00 111.40 ? 81  LEU B N   1 
ATOM   1680 C  CA  . LEU B 2 81  ? 41.958 48.777 29.941 1.00 105.53 ? 81  LEU B CA  1 
ATOM   1681 C  C   . LEU B 2 81  ? 42.333 50.256 29.908 1.00 114.31 ? 81  LEU B C   1 
ATOM   1682 O  O   . LEU B 2 81  ? 41.549 51.098 30.350 1.00 117.63 ? 81  LEU B O   1 
ATOM   1683 C  CB  . LEU B 2 81  ? 42.514 48.100 31.195 1.00 97.18  ? 81  LEU B CB  1 
ATOM   1684 C  CG  . LEU B 2 81  ? 41.758 46.843 31.639 1.00 88.85  ? 81  LEU B CG  1 
ATOM   1685 C  CD1 . LEU B 2 81  ? 42.579 46.034 32.634 1.00 89.28  ? 81  LEU B CD1 1 
ATOM   1686 C  CD2 . LEU B 2 81  ? 40.407 47.199 32.240 1.00 81.84  ? 81  LEU B CD2 1 
ATOM   1687 N  N   . LYS B 2 82  ? 43.518 50.569 29.386 1.00 124.92 ? 82  LYS B N   1 
ATOM   1688 C  CA  . LYS B 2 82  ? 43.990 51.959 29.301 1.00 136.07 ? 82  LYS B CA  1 
ATOM   1689 C  C   . LYS B 2 82  ? 43.108 52.833 28.391 1.00 136.10 ? 82  LYS B C   1 
ATOM   1690 O  O   . LYS B 2 82  ? 42.898 54.018 28.673 1.00 138.93 ? 82  LYS B O   1 
ATOM   1691 C  CB  . LYS B 2 82  ? 45.449 52.007 28.831 1.00 148.90 ? 82  LYS B CB  1 
ATOM   1692 C  CG  . LYS B 2 82  ? 46.438 51.411 29.823 1.00 161.68 ? 82  LYS B CG  1 
ATOM   1693 C  CD  . LYS B 2 82  ? 47.869 51.525 29.319 1.00 178.57 ? 82  LYS B CD  1 
ATOM   1694 C  CE  . LYS B 2 82  ? 48.869 51.005 30.342 1.00 186.98 ? 82  LYS B CE  1 
ATOM   1695 N  NZ  . LYS B 2 82  ? 50.277 51.128 29.870 1.00 187.59 ? 82  LYS B NZ  1 
ATOM   1696 N  N   . GLY B 2 83  ? 42.601 52.244 27.310 1.00 126.20 ? 83  GLY B N   1 
ATOM   1697 C  CA  . GLY B 2 83  ? 41.656 52.922 26.427 1.00 120.17 ? 83  GLY B CA  1 
ATOM   1698 C  C   . GLY B 2 83  ? 40.298 53.147 27.065 1.00 113.50 ? 83  GLY B C   1 
ATOM   1699 O  O   . GLY B 2 83  ? 39.648 54.163 26.807 1.00 120.25 ? 83  GLY B O   1 
ATOM   1700 N  N   . THR B 2 84  ? 39.867 52.195 27.889 1.00 99.34  ? 84  THR B N   1 
ATOM   1701 C  CA  . THR B 2 84  ? 38.579 52.272 28.573 1.00 93.95  ? 84  THR B CA  1 
ATOM   1702 C  C   . THR B 2 84  ? 38.542 53.406 29.602 1.00 89.85  ? 84  THR B C   1 
ATOM   1703 O  O   . THR B 2 84  ? 37.681 54.289 29.542 1.00 87.25  ? 84  THR B O   1 
ATOM   1704 C  CB  . THR B 2 84  ? 38.272 50.938 29.281 1.00 95.57  ? 84  THR B CB  1 
ATOM   1705 O  OG1 . THR B 2 84  ? 38.349 49.867 28.333 1.00 96.78  ? 84  THR B OG1 1 
ATOM   1706 C  CG2 . THR B 2 84  ? 36.887 50.958 29.922 1.00 99.02  ? 84  THR B CG2 1 
ATOM   1707 N  N   . PHE B 2 85  ? 39.495 53.372 30.530 1.00 83.76  ? 85  PHE B N   1 
ATOM   1708 C  CA  . PHE B 2 85  ? 39.572 54.320 31.639 1.00 77.13  ? 85  PHE B CA  1 
ATOM   1709 C  C   . PHE B 2 85  ? 40.486 55.482 31.275 1.00 78.17  ? 85  PHE B C   1 
ATOM   1710 O  O   . PHE B 2 85  ? 41.505 55.717 31.927 1.00 79.88  ? 85  PHE B O   1 
ATOM   1711 C  CB  . PHE B 2 85  ? 40.105 53.610 32.888 1.00 73.28  ? 85  PHE B CB  1 
ATOM   1712 C  CG  . PHE B 2 85  ? 39.212 52.520 33.396 1.00 68.81  ? 85  PHE B CG  1 
ATOM   1713 C  CD1 . PHE B 2 85  ? 38.035 52.840 34.059 1.00 65.99  ? 85  PHE B CD1 1 
ATOM   1714 C  CD2 . PHE B 2 85  ? 39.547 51.179 33.235 1.00 66.99  ? 85  PHE B CD2 1 
ATOM   1715 C  CE1 . PHE B 2 85  ? 37.195 51.855 34.546 1.00 62.97  ? 85  PHE B CE1 1 
ATOM   1716 C  CE2 . PHE B 2 85  ? 38.708 50.184 33.718 1.00 65.62  ? 85  PHE B CE2 1 
ATOM   1717 C  CZ  . PHE B 2 85  ? 37.534 50.523 34.375 1.00 64.64  ? 85  PHE B CZ  1 
ATOM   1718 N  N   . ALA B 2 86  ? 40.128 56.206 30.225 1.00 79.60  ? 86  ALA B N   1 
ATOM   1719 C  CA  . ALA B 2 86  ? 40.955 57.305 29.752 1.00 83.68  ? 86  ALA B CA  1 
ATOM   1720 C  C   . ALA B 2 86  ? 40.486 58.596 30.392 1.00 83.19  ? 86  ALA B C   1 
ATOM   1721 O  O   . ALA B 2 86  ? 41.267 59.293 31.029 1.00 84.26  ? 86  ALA B O   1 
ATOM   1722 C  CB  . ALA B 2 86  ? 40.889 57.405 28.243 1.00 89.78  ? 86  ALA B CB  1 
ATOM   1723 N  N   . THR B 2 87  ? 39.203 58.901 30.221 1.00 85.52  ? 87  THR B N   1 
ATOM   1724 C  CA  . THR B 2 87  ? 38.605 60.122 30.765 1.00 89.10  ? 87  THR B CA  1 
ATOM   1725 C  C   . THR B 2 87  ? 38.555 60.113 32.299 1.00 84.51  ? 87  THR B C   1 
ATOM   1726 O  O   . THR B 2 87  ? 38.610 61.175 32.930 1.00 84.97  ? 87  THR B O   1 
ATOM   1727 C  CB  . THR B 2 87  ? 37.178 60.343 30.207 1.00 97.50  ? 87  THR B CB  1 
ATOM   1728 O  OG1 . THR B 2 87  ? 37.201 60.261 28.775 1.00 98.69  ? 87  THR B OG1 1 
ATOM   1729 C  CG2 . THR B 2 87  ? 36.619 61.708 30.624 1.00 102.43 ? 87  THR B CG2 1 
ATOM   1730 N  N   . LEU B 2 88  ? 38.450 58.924 32.892 1.00 74.10  ? 88  LEU B N   1 
ATOM   1731 C  CA  . LEU B 2 88  ? 38.425 58.809 34.346 1.00 66.14  ? 88  LEU B CA  1 
ATOM   1732 C  C   . LEU B 2 88  ? 39.794 59.062 34.953 1.00 62.67  ? 88  LEU B C   1 
ATOM   1733 O  O   . LEU B 2 88  ? 39.901 59.800 35.934 1.00 62.46  ? 88  LEU B O   1 
ATOM   1734 C  CB  . LEU B 2 88  ? 37.869 57.454 34.790 1.00 63.84  ? 88  LEU B CB  1 
ATOM   1735 C  CG  . LEU B 2 88  ? 36.355 57.259 34.624 1.00 62.03  ? 88  LEU B CG  1 
ATOM   1736 C  CD1 . LEU B 2 88  ? 35.947 55.902 35.166 1.00 62.04  ? 88  LEU B CD1 1 
ATOM   1737 C  CD2 . LEU B 2 88  ? 35.519 58.336 35.307 1.00 61.44  ? 88  LEU B CD2 1 
ATOM   1738 N  N   . SER B 2 89  ? 40.839 58.482 34.370 1.00 59.74  ? 89  SER B N   1 
ATOM   1739 C  CA  . SER B 2 89  ? 42.195 58.787 34.824 1.00 61.35  ? 89  SER B CA  1 
ATOM   1740 C  C   . SER B 2 89  ? 42.470 60.288 34.781 1.00 64.82  ? 89  SER B C   1 
ATOM   1741 O  O   . SER B 2 89  ? 43.126 60.808 35.670 1.00 69.47  ? 89  SER B O   1 
ATOM   1742 C  CB  . SER B 2 89  ? 43.259 58.011 34.039 1.00 60.80  ? 89  SER B CB  1 
ATOM   1743 O  OG  . SER B 2 89  ? 43.028 58.059 32.645 1.00 65.45  ? 89  SER B OG  1 
ATOM   1744 N  N   . GLU B 2 90  ? 41.941 60.977 33.769 1.00 72.56  ? 90  GLU B N   1 
ATOM   1745 C  CA  . GLU B 2 90  ? 42.034 62.439 33.681 1.00 77.58  ? 90  GLU B CA  1 
ATOM   1746 C  C   . GLU B 2 90  ? 41.200 63.075 34.785 1.00 69.47  ? 90  GLU B C   1 
ATOM   1747 O  O   . GLU B 2 90  ? 41.648 64.008 35.455 1.00 68.30  ? 90  GLU B O   1 
ATOM   1748 C  CB  . GLU B 2 90  ? 41.520 62.952 32.330 1.00 94.83  ? 90  GLU B CB  1 
ATOM   1749 C  CG  . GLU B 2 90  ? 42.247 62.425 31.090 1.00 111.73 ? 90  GLU B CG  1 
ATOM   1750 C  CD  . GLU B 2 90  ? 43.526 63.168 30.738 1.00 128.26 ? 90  GLU B CD  1 
ATOM   1751 O  OE1 . GLU B 2 90  ? 43.725 64.317 31.191 1.00 140.51 ? 90  GLU B OE1 1 
ATOM   1752 O  OE2 . GLU B 2 90  ? 44.337 62.591 29.978 1.00 136.09 ? 90  GLU B OE2 1 
ATOM   1753 N  N   . LEU B 2 91  ? 39.981 62.568 34.952 1.00 61.03  ? 91  LEU B N   1 
ATOM   1754 C  CA  . LEU B 2 91  ? 39.037 63.099 35.931 1.00 57.25  ? 91  LEU B CA  1 
ATOM   1755 C  C   . LEU B 2 91  ? 39.568 63.014 37.354 1.00 52.82  ? 91  LEU B C   1 
ATOM   1756 O  O   . LEU B 2 91  ? 39.630 64.026 38.057 1.00 52.38  ? 91  LEU B O   1 
ATOM   1757 C  CB  . LEU B 2 91  ? 37.694 62.356 35.843 1.00 57.92  ? 91  LEU B CB  1 
ATOM   1758 C  CG  . LEU B 2 91  ? 36.624 62.691 36.894 1.00 59.01  ? 91  LEU B CG  1 
ATOM   1759 C  CD1 . LEU B 2 91  ? 36.390 64.191 36.994 1.00 61.38  ? 91  LEU B CD1 1 
ATOM   1760 C  CD2 . LEU B 2 91  ? 35.324 61.964 36.590 1.00 58.55  ? 91  LEU B CD2 1 
ATOM   1761 N  N   . HIS B 2 92  ? 39.922 61.797 37.770 1.00 45.61  ? 92  HIS B N   1 
ATOM   1762 C  CA  . HIS B 2 92  ? 40.369 61.552 39.130 1.00 38.29  ? 92  HIS B CA  1 
ATOM   1763 C  C   . HIS B 2 92  ? 41.750 62.222 39.370 1.00 41.05  ? 92  HIS B C   1 
ATOM   1764 O  O   . HIS B 2 92  ? 42.014 62.647 40.487 1.00 41.31  ? 92  HIS B O   1 
ATOM   1765 C  CB  . HIS B 2 92  ? 40.388 60.047 39.459 1.00 32.45  ? 92  HIS B CB  1 
ATOM   1766 C  CG  . HIS B 2 92  ? 39.034 59.404 39.672 1.00 30.33  ? 92  HIS B CG  1 
ATOM   1767 N  ND1 . HIS B 2 92  ? 38.473 58.563 38.743 1.00 29.00  ? 92  HIS B ND1 1 
ATOM   1768 C  CD2 . HIS B 2 92  ? 38.190 59.372 40.745 1.00 31.90  ? 92  HIS B CD2 1 
ATOM   1769 C  CE1 . HIS B 2 92  ? 37.325 58.083 39.199 1.00 29.60  ? 92  HIS B CE1 1 
ATOM   1770 N  NE2 . HIS B 2 92  ? 37.129 58.530 40.432 1.00 30.78  ? 92  HIS B NE2 1 
ATOM   1771 N  N   . CYS B 2 93  ? 42.592 62.380 38.342 1.00 48.79  ? 93  CYS B N   1 
ATOM   1772 C  CA  . CYS B 2 93  ? 43.917 63.048 38.500 1.00 61.01  ? 93  CYS B CA  1 
ATOM   1773 C  C   . CYS B 2 93  ? 43.956 64.583 38.391 1.00 66.91  ? 93  CYS B C   1 
ATOM   1774 O  O   . CYS B 2 93  ? 44.474 65.266 39.287 1.00 64.15  ? 93  CYS B O   1 
ATOM   1775 C  CB  . CYS B 2 93  ? 44.938 62.498 37.489 1.00 68.92  ? 93  CYS B CB  1 
ATOM   1776 S  SG  . CYS B 2 93  ? 46.586 63.281 37.540 1.00 78.67  ? 93  CYS B SG  1 
ATOM   1777 N  N   . ASP B 2 94  ? 43.476 65.113 37.271 1.00 77.51  ? 94  ASP B N   1 
ATOM   1778 C  CA  . ASP B 2 94  ? 43.700 66.522 36.943 1.00 92.49  ? 94  ASP B CA  1 
ATOM   1779 C  C   . ASP B 2 94  ? 42.768 67.486 37.671 1.00 91.97  ? 94  ASP B C   1 
ATOM   1780 O  O   . ASP B 2 94  ? 43.057 68.682 37.730 1.00 103.66 ? 94  ASP B O   1 
ATOM   1781 C  CB  . ASP B 2 94  ? 43.620 66.761 35.420 1.00 111.04 ? 94  ASP B CB  1 
ATOM   1782 C  CG  . ASP B 2 94  ? 44.883 66.309 34.674 1.00 122.77 ? 94  ASP B CG  1 
ATOM   1783 O  OD1 . ASP B 2 94  ? 46.011 66.551 35.166 1.00 129.40 ? 94  ASP B OD1 1 
ATOM   1784 O  OD2 . ASP B 2 94  ? 44.746 65.729 33.575 1.00 125.47 ? 94  ASP B OD2 1 
ATOM   1785 N  N   . LYS B 2 95  ? 41.667 66.983 38.222 1.00 85.76  ? 95  LYS B N   1 
ATOM   1786 C  CA  . LYS B 2 95  ? 40.674 67.839 38.858 1.00 86.16  ? 95  LYS B CA  1 
ATOM   1787 C  C   . LYS B 2 95  ? 40.524 67.534 40.349 1.00 79.05  ? 95  LYS B C   1 
ATOM   1788 O  O   . LYS B 2 95  ? 40.697 68.418 41.186 1.00 83.94  ? 95  LYS B O   1 
ATOM   1789 C  CB  . LYS B 2 95  ? 39.341 67.695 38.115 1.00 98.28  ? 95  LYS B CB  1 
ATOM   1790 C  CG  . LYS B 2 95  ? 38.348 68.828 38.350 1.00 110.60 ? 95  LYS B CG  1 
ATOM   1791 C  CD  . LYS B 2 95  ? 37.209 68.433 39.285 1.00 123.17 ? 95  LYS B CD  1 
ATOM   1792 C  CE  . LYS B 2 95  ? 36.144 67.613 38.564 1.00 131.32 ? 95  LYS B CE  1 
ATOM   1793 N  NZ  . LYS B 2 95  ? 34.967 67.295 39.427 1.00 132.40 ? 95  LYS B NZ  1 
ATOM   1794 N  N   . LEU B 2 96  ? 40.213 66.282 40.671 1.00 69.89  ? 96  LEU B N   1 
ATOM   1795 C  CA  . LEU B 2 96  ? 39.927 65.864 42.047 1.00 62.32  ? 96  LEU B CA  1 
ATOM   1796 C  C   . LEU B 2 96  ? 41.168 65.702 42.926 1.00 61.25  ? 96  LEU B C   1 
ATOM   1797 O  O   . LEU B 2 96  ? 41.090 65.918 44.135 1.00 59.88  ? 96  LEU B O   1 
ATOM   1798 C  CB  . LEU B 2 96  ? 39.150 64.553 42.021 1.00 59.69  ? 96  LEU B CB  1 
ATOM   1799 C  CG  . LEU B 2 96  ? 37.779 64.679 41.360 1.00 59.20  ? 96  LEU B CG  1 
ATOM   1800 C  CD1 . LEU B 2 96  ? 37.296 63.332 40.847 1.00 59.97  ? 96  LEU B CD1 1 
ATOM   1801 C  CD2 . LEU B 2 96  ? 36.782 65.300 42.333 1.00 60.46  ? 96  LEU B CD2 1 
ATOM   1802 N  N   . HIS B 2 97  ? 42.288 65.310 42.309 1.00 60.47  ? 97  HIS B N   1 
ATOM   1803 C  CA  . HIS B 2 97  ? 43.580 65.077 42.978 1.00 60.64  ? 97  HIS B CA  1 
ATOM   1804 C  C   . HIS B 2 97  ? 43.572 63.872 43.925 1.00 51.98  ? 97  HIS B C   1 
ATOM   1805 O  O   . HIS B 2 97  ? 44.228 63.901 44.962 1.00 56.62  ? 97  HIS B O   1 
ATOM   1806 C  CB  . HIS B 2 97  ? 44.074 66.323 43.743 1.00 71.99  ? 97  HIS B CB  1 
ATOM   1807 C  CG  . HIS B 2 97  ? 44.141 67.574 42.920 1.00 84.84  ? 97  HIS B CG  1 
ATOM   1808 N  ND1 . HIS B 2 97  ? 45.216 67.872 42.107 1.00 93.20  ? 97  HIS B ND1 1 
ATOM   1809 C  CD2 . HIS B 2 97  ? 43.293 68.626 42.822 1.00 87.79  ? 97  HIS B CD2 1 
ATOM   1810 C  CE1 . HIS B 2 97  ? 45.016 69.044 41.529 1.00 97.62  ? 97  HIS B CE1 1 
ATOM   1811 N  NE2 . HIS B 2 97  ? 43.856 69.521 41.944 1.00 92.94  ? 97  HIS B NE2 1 
ATOM   1812 N  N   . VAL B 2 98  ? 42.839 62.818 43.573 1.00 44.01  ? 98  VAL B N   1 
ATOM   1813 C  CA  . VAL B 2 98  ? 42.803 61.584 44.370 1.00 39.41  ? 98  VAL B CA  1 
ATOM   1814 C  C   . VAL B 2 98  ? 44.110 60.867 44.087 1.00 39.42  ? 98  VAL B C   1 
ATOM   1815 O  O   . VAL B 2 98  ? 44.355 60.515 42.942 1.00 37.94  ? 98  VAL B O   1 
ATOM   1816 C  CB  . VAL B 2 98  ? 41.599 60.679 43.964 1.00 36.42  ? 98  VAL B CB  1 
ATOM   1817 C  CG1 . VAL B 2 98  ? 41.701 59.283 44.558 1.00 36.23  ? 98  VAL B CG1 1 
ATOM   1818 C  CG2 . VAL B 2 98  ? 40.269 61.310 44.353 1.00 33.99  ? 98  VAL B CG2 1 
ATOM   1819 N  N   . ASP B 2 99  ? 44.949 60.656 45.104 1.00 44.73  ? 99  ASP B N   1 
ATOM   1820 C  CA  . ASP B 2 99  ? 46.266 59.990 44.897 1.00 50.66  ? 99  ASP B CA  1 
ATOM   1821 C  C   . ASP B 2 99  ? 46.155 58.465 44.732 1.00 45.60  ? 99  ASP B C   1 
ATOM   1822 O  O   . ASP B 2 99  ? 45.328 57.831 45.389 1.00 46.57  ? 99  ASP B O   1 
ATOM   1823 C  CB  . ASP B 2 99  ? 47.264 60.322 46.010 1.00 62.51  ? 99  ASP B CB  1 
ATOM   1824 C  CG  . ASP B 2 99  ? 46.771 59.911 47.394 1.00 80.09  ? 99  ASP B CG  1 
ATOM   1825 O  OD1 . ASP B 2 99  ? 45.538 59.815 47.596 1.00 93.23  ? 99  ASP B OD1 1 
ATOM   1826 O  OD2 . ASP B 2 99  ? 47.618 59.704 48.290 1.00 87.96  ? 99  ASP B OD2 1 
ATOM   1827 N  N   . PRO B 2 100 ? 47.007 57.870 43.884 1.00 41.65  ? 100 PRO B N   1 
ATOM   1828 C  CA  . PRO B 2 100 ? 46.729 56.537 43.364 1.00 42.83  ? 100 PRO B CA  1 
ATOM   1829 C  C   . PRO B 2 100 ? 46.813 55.346 44.330 1.00 46.51  ? 100 PRO B C   1 
ATOM   1830 O  O   . PRO B 2 100 ? 46.405 54.239 43.953 1.00 47.89  ? 100 PRO B O   1 
ATOM   1831 C  CB  . PRO B 2 100 ? 47.773 56.369 42.254 1.00 43.30  ? 100 PRO B CB  1 
ATOM   1832 C  CG  . PRO B 2 100 ? 48.336 57.721 42.030 1.00 42.78  ? 100 PRO B CG  1 
ATOM   1833 C  CD  . PRO B 2 100 ? 48.297 58.345 43.384 1.00 42.63  ? 100 PRO B CD  1 
ATOM   1834 N  N   . GLU B 2 101 ? 47.341 55.547 45.537 1.00 46.53  ? 101 GLU B N   1 
ATOM   1835 C  CA  . GLU B 2 101 ? 47.225 54.536 46.585 1.00 45.69  ? 101 GLU B CA  1 
ATOM   1836 C  C   . GLU B 2 101 ? 45.763 54.262 46.948 1.00 37.41  ? 101 GLU B C   1 
ATOM   1837 O  O   . GLU B 2 101 ? 45.417 53.141 47.318 1.00 37.12  ? 101 GLU B O   1 
ATOM   1838 C  CB  . GLU B 2 101 ? 48.016 54.952 47.833 1.00 59.34  ? 101 GLU B CB  1 
ATOM   1839 C  CG  . GLU B 2 101 ? 47.848 54.057 49.081 1.00 76.88  ? 101 GLU B CG  1 
ATOM   1840 C  CD  . GLU B 2 101 ? 48.168 52.561 48.877 1.00 87.93  ? 101 GLU B CD  1 
ATOM   1841 O  OE1 . GLU B 2 101 ? 48.951 52.207 47.957 1.00 95.60  ? 101 GLU B OE1 1 
ATOM   1842 O  OE2 . GLU B 2 101 ? 47.644 51.732 49.666 1.00 81.40  ? 101 GLU B OE2 1 
ATOM   1843 N  N   . ASN B 2 102 ? 44.906 55.272 46.835 1.00 30.70  ? 102 ASN B N   1 
ATOM   1844 C  CA  . ASN B 2 102 ? 43.502 55.110 47.187 1.00 26.06  ? 102 ASN B CA  1 
ATOM   1845 C  C   . ASN B 2 102 ? 42.749 54.192 46.253 1.00 23.57  ? 102 ASN B C   1 
ATOM   1846 O  O   . ASN B 2 102 ? 41.767 53.606 46.677 1.00 23.60  ? 102 ASN B O   1 
ATOM   1847 C  CB  . ASN B 2 102 ? 42.809 56.454 47.249 1.00 25.74  ? 102 ASN B CB  1 
ATOM   1848 C  CG  . ASN B 2 102 ? 43.397 57.368 48.313 1.00 26.70  ? 102 ASN B CG  1 
ATOM   1849 O  OD1 . ASN B 2 102 ? 44.064 56.929 49.256 1.00 27.45  ? 102 ASN B OD1 1 
ATOM   1850 N  ND2 . ASN B 2 102 ? 43.146 58.658 48.164 1.00 27.72  ? 102 ASN B ND2 1 
ATOM   1851 N  N   . PHE B 2 103 ? 43.209 54.031 45.010 1.00 22.84  ? 103 PHE B N   1 
ATOM   1852 C  CA  . PHE B 2 103 ? 42.549 53.121 44.060 1.00 22.23  ? 103 PHE B CA  1 
ATOM   1853 C  C   . PHE B 2 103 ? 42.715 51.686 44.464 1.00 22.31  ? 103 PHE B C   1 
ATOM   1854 O  O   . PHE B 2 103 ? 41.730 50.951 44.482 1.00 22.24  ? 103 PHE B O   1 
ATOM   1855 C  CB  . PHE B 2 103 ? 43.017 53.325 42.620 1.00 21.93  ? 103 PHE B CB  1 
ATOM   1856 C  CG  . PHE B 2 103 ? 42.832 54.729 42.143 1.00 22.44  ? 103 PHE B CG  1 
ATOM   1857 C  CD1 . PHE B 2 103 ? 41.572 55.322 42.173 1.00 22.93  ? 103 PHE B CD1 1 
ATOM   1858 C  CD2 . PHE B 2 103 ? 43.912 55.487 41.726 1.00 22.39  ? 103 PHE B CD2 1 
ATOM   1859 C  CE1 . PHE B 2 103 ? 41.387 56.643 41.783 1.00 22.90  ? 103 PHE B CE1 1 
ATOM   1860 C  CE2 . PHE B 2 103 ? 43.738 56.808 41.330 1.00 23.10  ? 103 PHE B CE2 1 
ATOM   1861 C  CZ  . PHE B 2 103 ? 42.473 57.390 41.358 1.00 22.93  ? 103 PHE B CZ  1 
ATOM   1862 N  N   . ARG B 2 104 ? 43.927 51.281 44.822 1.00 23.76  ? 104 ARG B N   1 
ATOM   1863 C  CA  . ARG B 2 104 ? 44.114 49.909 45.283 1.00 26.80  ? 104 ARG B CA  1 
ATOM   1864 C  C   . ARG B 2 104 ? 43.472 49.599 46.653 1.00 23.24  ? 104 ARG B C   1 
ATOM   1865 O  O   . ARG B 2 104 ? 43.321 48.423 46.997 1.00 22.15  ? 104 ARG B O   1 
ATOM   1866 C  CB  . ARG B 2 104 ? 45.586 49.503 45.251 1.00 34.54  ? 104 ARG B CB  1 
ATOM   1867 C  CG  . ARG B 2 104 ? 46.441 50.022 46.391 1.00 45.00  ? 104 ARG B CG  1 
ATOM   1868 C  CD  . ARG B 2 104 ? 47.624 49.103 46.679 1.00 55.20  ? 104 ARG B CD  1 
ATOM   1869 N  NE  . ARG B 2 104 ? 47.242 47.846 47.353 1.00 64.60  ? 104 ARG B NE  1 
ATOM   1870 C  CZ  . ARG B 2 104 ? 46.968 47.696 48.661 1.00 73.08  ? 104 ARG B CZ  1 
ATOM   1871 N  NH1 . ARG B 2 104 ? 46.991 48.730 49.513 1.00 71.94  ? 104 ARG B NH1 1 
ATOM   1872 N  NH2 . ARG B 2 104 ? 46.652 46.483 49.128 1.00 75.74  ? 104 ARG B NH2 1 
ATOM   1873 N  N   . LEU B 2 105 ? 43.124 50.638 47.425 1.00 20.15  ? 105 LEU B N   1 
ATOM   1874 C  CA  . LEU B 2 105 ? 42.296 50.481 48.625 1.00 17.94  ? 105 LEU B CA  1 
ATOM   1875 C  C   . LEU B 2 105 ? 40.877 50.160 48.259 1.00 16.25  ? 105 LEU B C   1 
ATOM   1876 O  O   . LEU B 2 105 ? 40.332 49.207 48.803 1.00 17.17  ? 105 LEU B O   1 
ATOM   1877 C  CB  . LEU B 2 105 ? 42.286 51.724 49.516 1.00 18.51  ? 105 LEU B CB  1 
ATOM   1878 C  CG  . LEU B 2 105 ? 43.528 52.014 50.375 1.00 18.92  ? 105 LEU B CG  1 
ATOM   1879 C  CD1 . LEU B 2 105 ? 43.338 53.262 51.241 1.00 18.67  ? 105 LEU B CD1 1 
ATOM   1880 C  CD2 . LEU B 2 105 ? 43.880 50.820 51.252 1.00 19.23  ? 105 LEU B CD2 1 
ATOM   1881 N  N   . LEU B 2 106 ? 40.272 50.929 47.352 1.00 14.64  ? 106 LEU B N   1 
ATOM   1882 C  CA  . LEU B 2 106 ? 38.876 50.667 46.940 1.00 13.87  ? 106 LEU B CA  1 
ATOM   1883 C  C   . LEU B 2 106 ? 38.682 49.284 46.369 1.00 13.30  ? 106 LEU B C   1 
ATOM   1884 O  O   . LEU B 2 106 ? 37.706 48.621 46.691 1.00 13.33  ? 106 LEU B O   1 
ATOM   1885 C  CB  . LEU B 2 106 ? 38.380 51.659 45.903 1.00 13.85  ? 106 LEU B CB  1 
ATOM   1886 C  CG  . LEU B 2 106 ? 36.884 51.540 45.587 1.00 13.83  ? 106 LEU B CG  1 
ATOM   1887 C  CD1 . LEU B 2 106 ? 36.055 51.930 46.801 1.00 13.91  ? 106 LEU B CD1 1 
ATOM   1888 C  CD2 . LEU B 2 106 ? 36.507 52.403 44.403 1.00 13.90  ? 106 LEU B CD2 1 
ATOM   1889 N  N   . GLY B 2 107 ? 39.611 48.876 45.510 1.00 13.25  ? 107 GLY B N   1 
ATOM   1890 C  CA  . GLY B 2 107 ? 39.686 47.509 44.991 1.00 13.15  ? 107 GLY B CA  1 
ATOM   1891 C  C   . GLY B 2 107 ? 39.671 46.419 46.050 1.00 12.99  ? 107 GLY B C   1 
ATOM   1892 O  O   . GLY B 2 107 ? 38.977 45.420 45.887 1.00 13.35  ? 107 GLY B O   1 
ATOM   1893 N  N   . ASN B 2 108 ? 40.418 46.600 47.133 1.00 12.91  ? 108 ASN B N   1 
ATOM   1894 C  CA  . ASN B 2 108 ? 40.431 45.608 48.203 1.00 13.11  ? 108 ASN B CA  1 
ATOM   1895 C  C   . ASN B 2 108 ? 39.175 45.603 49.046 1.00 12.88  ? 108 ASN B C   1 
ATOM   1896 O  O   . ASN B 2 108 ? 38.798 44.544 49.540 1.00 13.33  ? 108 ASN B O   1 
ATOM   1897 C  CB  . ASN B 2 108 ? 41.648 45.774 49.099 1.00 14.06  ? 108 ASN B CB  1 
ATOM   1898 C  CG  . ASN B 2 108 ? 42.909 45.198 48.471 1.00 15.34  ? 108 ASN B CG  1 
ATOM   1899 O  OD1 . ASN B 2 108 ? 43.007 45.080 47.239 1.00 16.05  ? 108 ASN B OD1 1 
ATOM   1900 N  ND2 . ASN B 2 108 ? 43.891 44.836 49.315 1.00 15.81  ? 108 ASN B ND2 1 
ATOM   1901 N  N   . VAL B 2 109 ? 38.528 46.754 49.224 1.00 12.25  ? 109 VAL B N   1 
ATOM   1902 C  CA  . VAL B 2 109 ? 37.258 46.797 49.945 1.00 11.95  ? 109 VAL B CA  1 
ATOM   1903 C  C   . VAL B 2 109 ? 36.187 46.096 49.155 1.00 12.36  ? 109 VAL B C   1 
ATOM   1904 O  O   . VAL B 2 109 ? 35.374 45.378 49.720 1.00 12.61  ? 109 VAL B O   1 
ATOM   1905 C  CB  . VAL B 2 109 ? 36.796 48.218 50.226 1.00 11.96  ? 109 VAL B CB  1 
ATOM   1906 C  CG1 . VAL B 2 109 ? 35.377 48.234 50.777 1.00 12.06  ? 109 VAL B CG1 1 
ATOM   1907 C  CG2 . VAL B 2 109 ? 37.724 48.862 51.242 1.00 12.37  ? 109 VAL B CG2 1 
ATOM   1908 N  N   . LEU B 2 110 ? 36.191 46.295 47.845 1.00 13.38  ? 110 LEU B N   1 
ATOM   1909 C  CA  . LEU B 2 110 ? 35.289 45.565 46.950 1.00 14.08  ? 110 LEU B CA  1 
ATOM   1910 C  C   . LEU B 2 110 ? 35.333 44.063 47.144 1.00 14.37  ? 110 LEU B C   1 
ATOM   1911 O  O   . LEU B 2 110 ? 34.294 43.434 47.332 1.00 14.99  ? 110 LEU B O   1 
ATOM   1912 C  CB  . LEU B 2 110 ? 35.610 45.855 45.491 1.00 14.32  ? 110 LEU B CB  1 
ATOM   1913 C  CG  . LEU B 2 110 ? 34.561 45.383 44.497 1.00 15.01  ? 110 LEU B CG  1 
ATOM   1914 C  CD1 . LEU B 2 110 ? 33.191 45.948 44.815 1.00 15.16  ? 110 LEU B CD1 1 
ATOM   1915 C  CD2 . LEU B 2 110 ? 34.977 45.854 43.122 1.00 15.99  ? 110 LEU B CD2 1 
ATOM   1916 N  N   . VAL B 2 111 ? 36.535 43.501 47.099 1.00 14.42  ? 111 VAL B N   1 
ATOM   1917 C  CA  . VAL B 2 111 ? 36.723 42.064 47.272 1.00 14.55  ? 111 VAL B CA  1 
ATOM   1918 C  C   . VAL B 2 111 ? 36.265 41.563 48.632 1.00 15.12  ? 111 VAL B C   1 
ATOM   1919 O  O   . VAL B 2 111 ? 35.830 40.433 48.732 1.00 15.14  ? 111 VAL B O   1 
ATOM   1920 C  CB  . VAL B 2 111 ? 38.179 41.655 46.972 1.00 14.57  ? 111 VAL B CB  1 
ATOM   1921 C  CG1 . VAL B 2 111 ? 38.519 40.261 47.494 1.00 14.60  ? 111 VAL B CG1 1 
ATOM   1922 C  CG2 . VAL B 2 111 ? 38.410 41.710 45.466 1.00 14.68  ? 111 VAL B CG2 1 
ATOM   1923 N  N   . CYS B 2 112 ? 36.336 42.391 49.666 1.00 17.34  ? 112 CYS B N   1 
ATOM   1924 C  CA  . CYS B 2 112 ? 35.766 42.020 50.967 1.00 19.32  ? 112 CYS B CA  1 
ATOM   1925 C  C   . CYS B 2 112 ? 34.254 42.002 50.963 1.00 19.20  ? 112 CYS B C   1 
ATOM   1926 O  O   . CYS B 2 112 ? 33.667 41.129 51.590 1.00 19.73  ? 112 CYS B O   1 
ATOM   1927 C  CB  . CYS B 2 112 ? 36.237 42.946 52.071 1.00 21.62  ? 112 CYS B CB  1 
ATOM   1928 S  SG  . CYS B 2 112 ? 37.934 42.613 52.584 1.00 27.34  ? 112 CYS B SG  1 
ATOM   1929 N  N   . VAL B 2 113 ? 33.631 42.952 50.275 1.00 19.44  ? 113 VAL B N   1 
ATOM   1930 C  CA  . VAL B 2 113 ? 32.174 42.960 50.120 1.00 20.92  ? 113 VAL B CA  1 
ATOM   1931 C  C   . VAL B 2 113 ? 31.641 41.740 49.370 1.00 21.53  ? 113 VAL B C   1 
ATOM   1932 O  O   . VAL B 2 113 ? 30.580 41.221 49.705 1.00 21.12  ? 113 VAL B O   1 
ATOM   1933 C  CB  . VAL B 2 113 ? 31.703 44.249 49.416 1.00 22.47  ? 113 VAL B CB  1 
ATOM   1934 C  CG1 . VAL B 2 113 ? 30.267 44.144 48.889 1.00 22.44  ? 113 VAL B CG1 1 
ATOM   1935 C  CG2 . VAL B 2 113 ? 31.825 45.411 50.386 1.00 23.64  ? 113 VAL B CG2 1 
ATOM   1936 N  N   . LEU B 2 114 ? 32.364 41.302 48.349 1.00 23.40  ? 114 LEU B N   1 
ATOM   1937 C  CA  . LEU B 2 114 ? 31.956 40.141 47.583 1.00 25.01  ? 114 LEU B CA  1 
ATOM   1938 C  C   . LEU B 2 114 ? 32.036 38.864 48.406 1.00 25.81  ? 114 LEU B C   1 
ATOM   1939 O  O   . LEU B 2 114 ? 31.071 38.107 48.442 1.00 28.50  ? 114 LEU B O   1 
ATOM   1940 C  CB  . LEU B 2 114 ? 32.766 40.023 46.300 1.00 26.86  ? 114 LEU B CB  1 
ATOM   1941 C  CG  . LEU B 2 114 ? 32.431 41.146 45.308 1.00 29.76  ? 114 LEU B CG  1 
ATOM   1942 C  CD1 . LEU B 2 114 ? 33.436 41.169 44.162 1.00 31.73  ? 114 LEU B CD1 1 
ATOM   1943 C  CD2 . LEU B 2 114 ? 31.007 41.023 44.770 1.00 30.08  ? 114 LEU B CD2 1 
ATOM   1944 N  N   . ALA B 2 115 ? 33.144 38.628 49.092 1.00 26.29  ? 115 ALA B N   1 
ATOM   1945 C  CA  . ALA B 2 115 ? 33.229 37.485 50.004 1.00 27.93  ? 115 ALA B CA  1 
ATOM   1946 C  C   . ALA B 2 115 ? 32.161 37.515 51.111 1.00 31.58  ? 115 ALA B C   1 
ATOM   1947 O  O   . ALA B 2 115 ? 31.698 36.468 51.545 1.00 33.61  ? 115 ALA B O   1 
ATOM   1948 C  CB  . ALA B 2 115 ? 34.603 37.400 50.624 1.00 27.77  ? 115 ALA B CB  1 
ATOM   1949 N  N   . HIS B 2 116 ? 31.769 38.698 51.563 1.00 36.16  ? 116 HIS B N   1 
ATOM   1950 C  CA  . HIS B 2 116 ? 30.666 38.828 52.516 1.00 41.65  ? 116 HIS B CA  1 
ATOM   1951 C  C   . HIS B 2 116 ? 29.346 38.323 51.962 1.00 46.34  ? 116 HIS B C   1 
ATOM   1952 O  O   . HIS B 2 116 ? 28.595 37.673 52.678 1.00 47.25  ? 116 HIS B O   1 
ATOM   1953 C  CB  . HIS B 2 116 ? 30.482 40.290 52.899 1.00 48.03  ? 116 HIS B CB  1 
ATOM   1954 C  CG  . HIS B 2 116 ? 29.629 40.508 54.107 1.00 52.18  ? 116 HIS B CG  1 
ATOM   1955 N  ND1 . HIS B 2 116 ? 28.865 41.642 54.276 1.00 54.94  ? 116 HIS B ND1 1 
ATOM   1956 C  CD2 . HIS B 2 116 ? 29.436 39.754 55.215 1.00 56.23  ? 116 HIS B CD2 1 
ATOM   1957 C  CE1 . HIS B 2 116 ? 28.234 41.575 55.434 1.00 58.40  ? 116 HIS B CE1 1 
ATOM   1958 N  NE2 . HIS B 2 116 ? 28.563 40.439 56.024 1.00 57.80  ? 116 HIS B NE2 1 
ATOM   1959 N  N   . HIS B 2 117 ? 29.058 38.652 50.703 1.00 55.28  ? 117 HIS B N   1 
ATOM   1960 C  CA  . HIS B 2 117 ? 27.808 38.236 50.056 1.00 64.55  ? 117 HIS B CA  1 
ATOM   1961 C  C   . HIS B 2 117 ? 27.806 36.775 49.650 1.00 65.57  ? 117 HIS B C   1 
ATOM   1962 O  O   . HIS B 2 117 ? 26.866 36.051 49.980 1.00 71.39  ? 117 HIS B O   1 
ATOM   1963 C  CB  . HIS B 2 117 ? 27.487 39.080 48.816 1.00 73.74  ? 117 HIS B CB  1 
ATOM   1964 C  CG  . HIS B 2 117 ? 26.839 40.390 49.126 1.00 86.11  ? 117 HIS B CG  1 
ATOM   1965 N  ND1 . HIS B 2 117 ? 26.563 41.326 48.152 1.00 95.72  ? 117 HIS B ND1 1 
ATOM   1966 C  CD2 . HIS B 2 117 ? 26.422 40.930 50.296 1.00 96.54  ? 117 HIS B CD2 1 
ATOM   1967 C  CE1 . HIS B 2 117 ? 25.994 42.381 48.707 1.00 103.40 ? 117 HIS B CE1 1 
ATOM   1968 N  NE2 . HIS B 2 117 ? 25.898 42.167 50.007 1.00 103.60 ? 117 HIS B NE2 1 
ATOM   1969 N  N   . PHE B 2 118 ? 28.833 36.343 48.927 1.00 64.78  ? 118 PHE B N   1 
ATOM   1970 C  CA  . PHE B 2 118 ? 28.868 34.971 48.404 1.00 70.05  ? 118 PHE B CA  1 
ATOM   1971 C  C   . PHE B 2 118 ? 29.412 33.908 49.367 1.00 74.44  ? 118 PHE B C   1 
ATOM   1972 O  O   . PHE B 2 118 ? 29.460 32.729 48.998 1.00 76.56  ? 118 PHE B O   1 
ATOM   1973 C  CB  . PHE B 2 118 ? 29.645 34.901 47.089 1.00 72.27  ? 118 PHE B CB  1 
ATOM   1974 C  CG  . PHE B 2 118 ? 29.151 35.836 46.022 1.00 76.65  ? 118 PHE B CG  1 
ATOM   1975 C  CD1 . PHE B 2 118 ? 27.818 36.265 45.969 1.00 79.98  ? 118 PHE B CD1 1 
ATOM   1976 C  CD2 . PHE B 2 118 ? 30.033 36.264 45.033 1.00 81.36  ? 118 PHE B CD2 1 
ATOM   1977 C  CE1 . PHE B 2 118 ? 27.395 37.122 44.972 1.00 86.04  ? 118 PHE B CE1 1 
ATOM   1978 C  CE2 . PHE B 2 118 ? 29.616 37.118 44.033 1.00 86.61  ? 118 PHE B CE2 1 
ATOM   1979 C  CZ  . PHE B 2 118 ? 28.294 37.549 44.003 1.00 91.88  ? 118 PHE B CZ  1 
ATOM   1980 N  N   . GLY B 2 119 ? 29.812 34.301 50.579 1.00 76.76  ? 119 GLY B N   1 
ATOM   1981 C  CA  . GLY B 2 119 ? 30.196 33.344 51.621 1.00 79.71  ? 119 GLY B CA  1 
ATOM   1982 C  C   . GLY B 2 119 ? 31.188 32.309 51.122 1.00 88.66  ? 119 GLY B C   1 
ATOM   1983 O  O   . GLY B 2 119 ? 32.279 32.660 50.676 1.00 95.96  ? 119 GLY B O   1 
ATOM   1984 N  N   . LYS B 2 120 ? 30.796 31.038 51.155 1.00 99.57  ? 120 LYS B N   1 
ATOM   1985 C  CA  . LYS B 2 120 ? 31.695 29.943 50.771 1.00 110.63 ? 120 LYS B CA  1 
ATOM   1986 C  C   . LYS B 2 120 ? 31.816 29.711 49.259 1.00 105.73 ? 120 LYS B C   1 
ATOM   1987 O  O   . LYS B 2 120 ? 32.693 28.962 48.819 1.00 99.78  ? 120 LYS B O   1 
ATOM   1988 C  CB  . LYS B 2 120 ? 31.287 28.650 51.481 1.00 132.28 ? 120 LYS B CB  1 
ATOM   1989 C  CG  . LYS B 2 120 ? 31.605 28.665 52.972 1.00 148.92 ? 120 LYS B CG  1 
ATOM   1990 C  CD  . LYS B 2 120 ? 31.308 27.333 53.654 1.00 164.15 ? 120 LYS B CD  1 
ATOM   1991 C  CE  . LYS B 2 120 ? 32.276 26.218 53.260 1.00 174.06 ? 120 LYS B CE  1 
ATOM   1992 N  NZ  . LYS B 2 120 ? 33.702 26.508 53.590 1.00 176.97 ? 120 LYS B NZ  1 
ATOM   1993 N  N   . GLU B 2 121 ? 30.949 30.348 48.472 1.00 106.59 ? 121 GLU B N   1 
ATOM   1994 C  CA  . GLU B 2 121 ? 31.056 30.315 47.006 1.00 109.13 ? 121 GLU B CA  1 
ATOM   1995 C  C   . GLU B 2 121 ? 32.304 31.066 46.488 1.00 94.38  ? 121 GLU B C   1 
ATOM   1996 O  O   . GLU B 2 121 ? 32.828 30.751 45.411 1.00 89.65  ? 121 GLU B O   1 
ATOM   1997 C  CB  . GLU B 2 121 ? 29.783 30.895 46.383 1.00 127.11 ? 121 GLU B CB  1 
ATOM   1998 C  CG  . GLU B 2 121 ? 29.594 30.585 44.904 1.00 148.25 ? 121 GLU B CG  1 
ATOM   1999 C  CD  . GLU B 2 121 ? 28.291 31.133 44.336 1.00 164.66 ? 121 GLU B CD  1 
ATOM   2000 O  OE1 . GLU B 2 121 ? 27.511 31.776 45.077 1.00 173.32 ? 121 GLU B OE1 1 
ATOM   2001 O  OE2 . GLU B 2 121 ? 28.045 30.920 43.129 1.00 173.34 ? 121 GLU B OE2 1 
ATOM   2002 N  N   . PHE B 2 122 ? 32.761 32.048 47.268 1.00 78.08  ? 122 PHE B N   1 
ATOM   2003 C  CA  . PHE B 2 122 ? 33.984 32.813 46.999 1.00 62.64  ? 122 PHE B CA  1 
ATOM   2004 C  C   . PHE B 2 122 ? 35.220 32.020 47.471 1.00 60.20  ? 122 PHE B C   1 
ATOM   2005 O  O   . PHE B 2 122 ? 35.714 32.208 48.588 1.00 56.19  ? 122 PHE B O   1 
ATOM   2006 C  CB  . PHE B 2 122 ? 33.871 34.177 47.702 1.00 53.74  ? 122 PHE B CB  1 
ATOM   2007 C  CG  . PHE B 2 122 ? 34.792 35.213 47.163 1.00 47.50  ? 122 PHE B CG  1 
ATOM   2008 C  CD1 . PHE B 2 122 ? 34.517 35.831 45.956 1.00 45.04  ? 122 PHE B CD1 1 
ATOM   2009 C  CD2 . PHE B 2 122 ? 35.934 35.571 47.859 1.00 44.28  ? 122 PHE B CD2 1 
ATOM   2010 C  CE1 . PHE B 2 122 ? 35.374 36.789 45.446 1.00 43.85  ? 122 PHE B CE1 1 
ATOM   2011 C  CE2 . PHE B 2 122 ? 36.798 36.519 47.358 1.00 41.67  ? 122 PHE B CE2 1 
ATOM   2012 C  CZ  . PHE B 2 122 ? 36.518 37.131 46.149 1.00 43.11  ? 122 PHE B CZ  1 
ATOM   2013 N  N   . THR B 2 123 ? 35.693 31.117 46.609 1.00 60.86  ? 123 THR B N   1 
ATOM   2014 C  CA  . THR B 2 123 ? 36.822 30.216 46.916 1.00 60.83  ? 123 THR B CA  1 
ATOM   2015 C  C   . THR B 2 123 ? 38.151 30.878 46.588 1.00 57.53  ? 123 THR B C   1 
ATOM   2016 O  O   . THR B 2 123 ? 38.160 31.899 45.902 1.00 63.26  ? 123 THR B O   1 
ATOM   2017 C  CB  . THR B 2 123 ? 36.746 28.916 46.094 1.00 66.36  ? 123 THR B CB  1 
ATOM   2018 O  OG1 . THR B 2 123 ? 36.841 29.211 44.693 1.00 64.67  ? 123 THR B OG1 1 
ATOM   2019 C  CG2 . THR B 2 123 ? 35.442 28.200 46.359 1.00 73.40  ? 123 THR B CG2 1 
ATOM   2020 N  N   . PRO B 2 124 ? 39.278 30.309 47.066 1.00 52.66  ? 124 PRO B N   1 
ATOM   2021 C  CA  . PRO B 2 124 ? 40.582 30.873 46.717 1.00 52.19  ? 124 PRO B CA  1 
ATOM   2022 C  C   . PRO B 2 124 ? 40.870 31.072 45.224 1.00 54.83  ? 124 PRO B C   1 
ATOM   2023 O  O   . PRO B 2 124 ? 41.370 32.141 44.856 1.00 58.86  ? 124 PRO B O   1 
ATOM   2024 C  CB  . PRO B 2 124 ? 41.569 29.923 47.392 1.00 48.75  ? 124 PRO B CB  1 
ATOM   2025 C  CG  . PRO B 2 124 ? 40.848 29.532 48.625 1.00 50.26  ? 124 PRO B CG  1 
ATOM   2026 C  CD  . PRO B 2 124 ? 39.391 29.429 48.240 1.00 52.73  ? 124 PRO B CD  1 
ATOM   2027 N  N   . PRO B 2 125 ? 40.536 30.090 44.366 1.00 56.23  ? 125 PRO B N   1 
ATOM   2028 C  CA  . PRO B 2 125 ? 40.725 30.292 42.905 1.00 55.79  ? 125 PRO B CA  1 
ATOM   2029 C  C   . PRO B 2 125 ? 39.981 31.492 42.295 1.00 48.45  ? 125 PRO B C   1 
ATOM   2030 O  O   . PRO B 2 125 ? 40.524 32.198 41.434 1.00 47.50  ? 125 PRO B O   1 
ATOM   2031 C  CB  . PRO B 2 125 ? 40.184 28.993 42.307 1.00 60.39  ? 125 PRO B CB  1 
ATOM   2032 C  CG  . PRO B 2 125 ? 40.354 27.984 43.395 1.00 60.87  ? 125 PRO B CG  1 
ATOM   2033 C  CD  . PRO B 2 125 ? 40.111 28.711 44.676 1.00 55.93  ? 125 PRO B CD  1 
ATOM   2034 N  N   . VAL B 2 126 ? 38.746 31.683 42.742 1.00 41.77  ? 126 VAL B N   1 
ATOM   2035 C  CA  . VAL B 2 126 ? 37.934 32.820 42.351 1.00 38.57  ? 126 VAL B CA  1 
ATOM   2036 C  C   . VAL B 2 126 ? 38.595 34.090 42.862 1.00 36.25  ? 126 VAL B C   1 
ATOM   2037 O  O   . VAL B 2 126 ? 38.764 35.039 42.100 1.00 38.10  ? 126 VAL B O   1 
ATOM   2038 C  CB  . VAL B 2 126 ? 36.503 32.715 42.925 1.00 39.30  ? 126 VAL B CB  1 
ATOM   2039 C  CG1 . VAL B 2 126 ? 35.712 34.004 42.718 1.00 39.30  ? 126 VAL B CG1 1 
ATOM   2040 C  CG2 . VAL B 2 126 ? 35.771 31.540 42.300 1.00 40.46  ? 126 VAL B CG2 1 
ATOM   2041 N  N   . GLN B 2 127 ? 38.967 34.108 44.141 1.00 32.27  ? 127 GLN B N   1 
ATOM   2042 C  CA  . GLN B 2 127 ? 39.595 35.288 44.722 1.00 30.27  ? 127 GLN B CA  1 
ATOM   2043 C  C   . GLN B 2 127 ? 40.799 35.702 43.905 1.00 28.12  ? 127 GLN B C   1 
ATOM   2044 O  O   . GLN B 2 127 ? 40.908 36.860 43.513 1.00 27.33  ? 127 GLN B O   1 
ATOM   2045 C  CB  . GLN B 2 127 ? 40.031 35.074 46.170 1.00 29.96  ? 127 GLN B CB  1 
ATOM   2046 C  CG  . GLN B 2 127 ? 40.398 36.396 46.827 1.00 31.22  ? 127 GLN B CG  1 
ATOM   2047 C  CD  . GLN B 2 127 ? 41.253 36.254 48.051 1.00 32.62  ? 127 GLN B CD  1 
ATOM   2048 O  OE1 . GLN B 2 127 ? 41.301 35.193 48.662 1.00 33.73  ? 127 GLN B OE1 1 
ATOM   2049 N  NE2 . GLN B 2 127 ? 41.943 37.341 48.425 1.00 32.59  ? 127 GLN B NE2 1 
ATOM   2050 N  N   . ALA B 2 128 ? 41.684 34.746 43.649 1.00 28.05  ? 128 ALA B N   1 
ATOM   2051 C  CA  . ALA B 2 128 ? 42.891 34.990 42.863 1.00 29.37  ? 128 ALA B CA  1 
ATOM   2052 C  C   . ALA B 2 128 ? 42.596 35.654 41.520 1.00 31.62  ? 128 ALA B C   1 
ATOM   2053 O  O   . ALA B 2 128 ? 43.346 36.537 41.089 1.00 35.17  ? 128 ALA B O   1 
ATOM   2054 C  CB  . ALA B 2 128 ? 43.652 33.697 42.643 1.00 29.57  ? 128 ALA B CB  1 
ATOM   2055 N  N   . ALA B 2 129 ? 41.513 35.234 40.867 1.00 30.88  ? 129 ALA B N   1 
ATOM   2056 C  CA  . ALA B 2 129 ? 41.063 35.863 39.624 1.00 29.42  ? 129 ALA B CA  1 
ATOM   2057 C  C   . ALA B 2 129 ? 40.688 37.333 39.819 1.00 27.92  ? 129 ALA B C   1 
ATOM   2058 O  O   . ALA B 2 129 ? 41.311 38.204 39.223 1.00 26.70  ? 129 ALA B O   1 
ATOM   2059 C  CB  . ALA B 2 129 ? 39.892 35.092 39.053 1.00 30.72  ? 129 ALA B CB  1 
ATOM   2060 N  N   . TYR B 2 130 ? 39.696 37.595 40.673 1.00 27.75  ? 130 TYR B N   1 
ATOM   2061 C  CA  . TYR B 2 130 ? 39.268 38.962 40.984 1.00 28.61  ? 130 TYR B CA  1 
ATOM   2062 C  C   . TYR B 2 130 ? 40.371 39.877 41.499 1.00 28.74  ? 130 TYR B C   1 
ATOM   2063 O  O   . TYR B 2 130 ? 40.308 41.082 41.268 1.00 30.29  ? 130 TYR B O   1 
ATOM   2064 C  CB  . TYR B 2 130 ? 38.145 38.981 42.009 1.00 30.32  ? 130 TYR B CB  1 
ATOM   2065 C  CG  . TYR B 2 130 ? 36.786 38.781 41.416 1.00 33.77  ? 130 TYR B CG  1 
ATOM   2066 C  CD1 . TYR B 2 130 ? 36.070 39.847 40.881 1.00 36.17  ? 130 TYR B CD1 1 
ATOM   2067 C  CD2 . TYR B 2 130 ? 36.200 37.525 41.393 1.00 37.37  ? 130 TYR B CD2 1 
ATOM   2068 C  CE1 . TYR B 2 130 ? 34.804 39.663 40.339 1.00 36.64  ? 130 TYR B CE1 1 
ATOM   2069 C  CE2 . TYR B 2 130 ? 34.938 37.326 40.854 1.00 37.88  ? 130 TYR B CE2 1 
ATOM   2070 C  CZ  . TYR B 2 130 ? 34.246 38.396 40.333 1.00 37.99  ? 130 TYR B CZ  1 
ATOM   2071 O  OH  . TYR B 2 130 ? 32.999 38.181 39.806 1.00 41.38  ? 130 TYR B OH  1 
ATOM   2072 N  N   . GLN B 2 131 ? 41.356 39.342 42.211 1.00 28.56  ? 131 GLN B N   1 
ATOM   2073 C  CA  . GLN B 2 131 ? 42.483 40.174 42.634 1.00 29.58  ? 131 GLN B CA  1 
ATOM   2074 C  C   . GLN B 2 131 ? 43.230 40.715 41.437 1.00 30.71  ? 131 GLN B C   1 
ATOM   2075 O  O   . GLN B 2 131 ? 43.678 41.857 41.483 1.00 31.92  ? 131 GLN B O   1 
ATOM   2076 C  CB  . GLN B 2 131 ? 43.462 39.428 43.547 1.00 30.25  ? 131 GLN B CB  1 
ATOM   2077 C  CG  . GLN B 2 131 ? 42.979 39.242 44.977 1.00 30.11  ? 131 GLN B CG  1 
ATOM   2078 C  CD  . GLN B 2 131 ? 42.847 40.546 45.733 1.00 30.83  ? 131 GLN B CD  1 
ATOM   2079 O  OE1 . GLN B 2 131 ? 43.531 41.533 45.432 1.00 30.94  ? 131 GLN B OE1 1 
ATOM   2080 N  NE2 . GLN B 2 131 ? 41.963 40.559 46.725 1.00 30.73  ? 131 GLN B NE2 1 
ATOM   2081 N  N   . LYS B 2 132 ? 43.366 39.907 40.380 1.00 32.62  ? 132 LYS B N   1 
ATOM   2082 C  CA  . LYS B 2 132 ? 44.056 40.343 39.152 1.00 35.09  ? 132 LYS B CA  1 
ATOM   2083 C  C   . LYS B 2 132 ? 43.266 41.388 38.373 1.00 29.47  ? 132 LYS B C   1 
ATOM   2084 O  O   . LYS B 2 132 ? 43.852 42.294 37.785 1.00 28.85  ? 132 LYS B O   1 
ATOM   2085 C  CB  . LYS B 2 132 ? 44.391 39.160 38.247 1.00 44.34  ? 132 LYS B CB  1 
ATOM   2086 C  CG  . LYS B 2 132 ? 45.424 38.216 38.851 1.00 56.77  ? 132 LYS B CG  1 
ATOM   2087 C  CD  . LYS B 2 132 ? 45.611 36.934 38.038 1.00 67.59  ? 132 LYS B CD  1 
ATOM   2088 C  CE  . LYS B 2 132 ? 46.207 37.179 36.648 1.00 77.44  ? 132 LYS B CE  1 
ATOM   2089 N  NZ  . LYS B 2 132 ? 47.552 37.836 36.651 1.00 82.62  ? 132 LYS B NZ  1 
ATOM   2090 N  N   . VAL B 2 133 ? 41.945 41.261 38.374 1.00 25.16  ? 133 VAL B N   1 
ATOM   2091 C  CA  . VAL B 2 133 ? 41.089 42.263 37.768 1.00 22.93  ? 133 VAL B CA  1 
ATOM   2092 C  C   . VAL B 2 133 ? 41.273 43.587 38.497 1.00 21.46  ? 133 VAL B C   1 
ATOM   2093 O  O   . VAL B 2 133 ? 41.806 44.521 37.912 1.00 21.61  ? 133 VAL B O   1 
ATOM   2094 C  CB  . VAL B 2 133 ? 39.604 41.825 37.726 1.00 22.33  ? 133 VAL B CB  1 
ATOM   2095 C  CG1 . VAL B 2 133 ? 38.684 42.990 37.381 1.00 21.94  ? 133 VAL B CG1 1 
ATOM   2096 C  CG2 . VAL B 2 133 ? 39.424 40.693 36.721 1.00 21.93  ? 133 VAL B CG2 1 
ATOM   2097 N  N   . VAL B 2 134 ? 40.881 43.671 39.765 1.00 21.04  ? 134 VAL B N   1 
ATOM   2098 C  CA  . VAL B 2 134 ? 40.950 44.967 40.474 1.00 21.86  ? 134 VAL B CA  1 
ATOM   2099 C  C   . VAL B 2 134 ? 42.357 45.569 40.591 1.00 22.18  ? 134 VAL B C   1 
ATOM   2100 O  O   . VAL B 2 134 ? 42.487 46.761 40.889 1.00 22.43  ? 134 VAL B O   1 
ATOM   2101 C  CB  . VAL B 2 134 ? 40.290 44.974 41.879 1.00 21.47  ? 134 VAL B CB  1 
ATOM   2102 C  CG1 . VAL B 2 134 ? 38.803 44.658 41.783 1.00 21.39  ? 134 VAL B CG1 1 
ATOM   2103 C  CG2 . VAL B 2 134 ? 41.019 44.042 42.842 1.00 21.56  ? 134 VAL B CG2 1 
ATOM   2104 N  N   . ALA B 2 135 ? 43.395 44.764 40.377 1.00 22.97  ? 135 ALA B N   1 
ATOM   2105 C  CA  . ALA B 2 135 ? 44.743 45.307 40.209 1.00 24.47  ? 135 ALA B CA  1 
ATOM   2106 C  C   . ALA B 2 135 ? 44.793 46.079 38.911 1.00 23.95  ? 135 ALA B C   1 
ATOM   2107 O  O   . ALA B 2 135 ? 45.100 47.268 38.909 1.00 24.17  ? 135 ALA B O   1 
ATOM   2108 C  CB  . ALA B 2 135 ? 45.803 44.208 40.208 1.00 25.25  ? 135 ALA B CB  1 
ATOM   2109 N  N   . GLY B 2 136 ? 44.474 45.397 37.814 1.00 23.87  ? 136 GLY B N   1 
ATOM   2110 C  CA  . GLY B 2 136 ? 44.481 46.013 36.486 1.00 23.99  ? 136 GLY B CA  1 
ATOM   2111 C  C   . GLY B 2 136 ? 43.757 47.348 36.458 1.00 22.81  ? 136 GLY B C   1 
ATOM   2112 O  O   . GLY B 2 136 ? 44.333 48.366 36.067 1.00 22.34  ? 136 GLY B O   1 
ATOM   2113 N  N   . VAL B 2 137 ? 42.515 47.323 36.934 1.00 21.26  ? 137 VAL B N   1 
ATOM   2114 C  CA  . VAL B 2 137 ? 41.622 48.467 36.901 1.00 20.41  ? 137 VAL B CA  1 
ATOM   2115 C  C   . VAL B 2 137 ? 42.186 49.616 37.680 1.00 22.07  ? 137 VAL B C   1 
ATOM   2116 O  O   . VAL B 2 137 ? 42.077 50.739 37.244 1.00 23.00  ? 137 VAL B O   1 
ATOM   2117 C  CB  . VAL B 2 137 ? 40.255 48.118 37.490 1.00 19.47  ? 137 VAL B CB  1 
ATOM   2118 C  CG1 . VAL B 2 137 ? 39.405 49.370 37.720 1.00 19.15  ? 137 VAL B CG1 1 
ATOM   2119 C  CG2 . VAL B 2 137 ? 39.549 47.117 36.582 1.00 19.21  ? 137 VAL B CG2 1 
ATOM   2120 N  N   . ALA B 2 138 ? 42.774 49.338 38.836 1.00 25.77  ? 138 ALA B N   1 
ATOM   2121 C  CA  . ALA B 2 138 ? 43.439 50.372 39.630 1.00 28.73  ? 138 ALA B CA  1 
ATOM   2122 C  C   . ALA B 2 138 ? 44.729 50.855 38.969 1.00 32.17  ? 138 ALA B C   1 
ATOM   2123 O  O   . ALA B 2 138 ? 44.961 52.056 38.852 1.00 31.19  ? 138 ALA B O   1 
ATOM   2124 C  CB  . ALA B 2 138 ? 43.732 49.846 41.016 1.00 29.14  ? 138 ALA B CB  1 
ATOM   2125 N  N   . ASN B 2 139 ? 45.554 49.907 38.528 1.00 40.91  ? 139 ASN B N   1 
ATOM   2126 C  CA  . ASN B 2 139 ? 46.829 50.211 37.860 1.00 48.26  ? 139 ASN B CA  1 
ATOM   2127 C  C   . ASN B 2 139 ? 46.649 50.935 36.547 1.00 46.40  ? 139 ASN B C   1 
ATOM   2128 O  O   . ASN B 2 139 ? 47.570 51.611 36.099 1.00 51.35  ? 139 ASN B O   1 
ATOM   2129 C  CB  . ASN B 2 139 ? 47.655 48.938 37.610 1.00 59.65  ? 139 ASN B CB  1 
ATOM   2130 C  CG  . ASN B 2 139 ? 48.298 48.387 38.887 1.00 74.70  ? 139 ASN B CG  1 
ATOM   2131 O  OD1 . ASN B 2 139 ? 48.973 49.117 39.625 1.00 84.42  ? 139 ASN B OD1 1 
ATOM   2132 N  ND2 . ASN B 2 139 ? 48.101 47.089 39.145 1.00 79.07  ? 139 ASN B ND2 1 
ATOM   2133 N  N   . ALA B 2 140 ? 45.478 50.776 35.929 1.00 43.49  ? 140 ALA B N   1 
ATOM   2134 C  CA  . ALA B 2 140 ? 45.134 51.444 34.669 1.00 39.67  ? 140 ALA B CA  1 
ATOM   2135 C  C   . ALA B 2 140 ? 44.422 52.764 34.845 1.00 33.77  ? 140 ALA B C   1 
ATOM   2136 O  O   . ALA B 2 140 ? 44.530 53.620 34.001 1.00 32.91  ? 140 ALA B O   1 
ATOM   2137 C  CB  . ALA B 2 140 ? 44.268 50.531 33.831 1.00 41.72  ? 140 ALA B CB  1 
ATOM   2138 N  N   . LEU B 2 141 ? 43.676 52.919 35.926 1.00 33.80  ? 141 LEU B N   1 
ATOM   2139 C  CA  . LEU B 2 141 ? 42.938 54.150 36.179 1.00 34.74  ? 141 LEU B CA  1 
ATOM   2140 C  C   . LEU B 2 141 ? 43.828 55.225 36.743 1.00 38.18  ? 141 LEU B C   1 
ATOM   2141 O  O   . LEU B 2 141 ? 43.382 56.342 36.948 1.00 38.10  ? 141 LEU B O   1 
ATOM   2142 C  CB  . LEU B 2 141 ? 41.798 53.877 37.143 1.00 34.13  ? 141 LEU B CB  1 
ATOM   2143 C  CG  . LEU B 2 141 ? 40.684 54.900 37.338 1.00 33.97  ? 141 LEU B CG  1 
ATOM   2144 C  CD1 . LEU B 2 141 ? 39.342 54.183 37.303 1.00 35.01  ? 141 LEU B CD1 1 
ATOM   2145 C  CD2 . LEU B 2 141 ? 40.823 55.669 38.645 1.00 34.31  ? 141 LEU B CD2 1 
ATOM   2146 N  N   . ALA B 2 142 ? 45.081 54.894 37.012 1.00 46.68  ? 142 ALA B N   1 
ATOM   2147 C  CA  . ALA B 2 142 ? 46.037 55.883 37.417 1.00 57.43  ? 142 ALA B CA  1 
ATOM   2148 C  C   . ALA B 2 142 ? 47.328 55.652 36.672 1.00 71.33  ? 142 ALA B C   1 
ATOM   2149 O  O   . ALA B 2 142 ? 48.326 55.213 37.251 1.00 77.47  ? 142 ALA B O   1 
ATOM   2150 C  CB  . ALA B 2 142 ? 46.247 55.793 38.908 1.00 60.15  ? 142 ALA B CB  1 
ATOM   2151 N  N   . HIS B 2 143 ? 47.282 55.902 35.366 1.00 94.07  ? 143 HIS B N   1 
ATOM   2152 C  CA  . HIS B 2 143 ? 48.494 56.047 34.553 1.00 119.03 ? 143 HIS B CA  1 
ATOM   2153 C  C   . HIS B 2 143 ? 48.669 57.466 33.994 1.00 128.86 ? 143 HIS B C   1 
ATOM   2154 O  O   . HIS B 2 143 ? 49.695 57.750 33.373 1.00 139.27 ? 143 HIS B O   1 
ATOM   2155 C  CB  . HIS B 2 143 ? 48.547 55.005 33.420 1.00 132.25 ? 143 HIS B CB  1 
ATOM   2156 C  CG  . HIS B 2 143 ? 47.591 55.269 32.296 1.00 143.82 ? 143 HIS B CG  1 
ATOM   2157 N  ND1 . HIS B 2 143 ? 47.711 56.351 31.449 1.00 150.36 ? 143 HIS B ND1 1 
ATOM   2158 C  CD2 . HIS B 2 143 ? 46.510 54.577 31.868 1.00 148.49 ? 143 HIS B CD2 1 
ATOM   2159 C  CE1 . HIS B 2 143 ? 46.734 56.324 30.561 1.00 154.65 ? 143 HIS B CE1 1 
ATOM   2160 N  NE2 . HIS B 2 143 ? 45.992 55.256 30.792 1.00 152.85 ? 143 HIS B NE2 1 
ATOM   2161 N  N   . LYS B 2 144 ? 47.687 58.347 34.197 1.00 134.48 ? 144 LYS B N   1 
ATOM   2162 C  CA  . LYS B 2 144 ? 47.833 59.739 33.791 1.00 150.00 ? 144 LYS B CA  1 
ATOM   2163 C  C   . LYS B 2 144 ? 48.829 60.485 34.694 1.00 155.48 ? 144 LYS B C   1 
ATOM   2164 O  O   . LYS B 2 144 ? 49.398 61.503 34.290 1.00 162.62 ? 144 LYS B O   1 
ATOM   2165 C  CB  . LYS B 2 144 ? 46.469 60.442 33.763 1.00 163.45 ? 144 LYS B CB  1 
ATOM   2166 C  CG  . LYS B 2 144 ? 46.473 61.862 33.200 1.00 184.19 ? 144 LYS B CG  1 
ATOM   2167 C  CD  . LYS B 2 144 ? 47.082 61.960 31.802 1.00 206.85 ? 144 LYS B CD  1 
ATOM   2168 C  CE  . LYS B 2 144 ? 47.232 63.403 31.349 1.00 222.96 ? 144 LYS B CE  1 
ATOM   2169 N  NZ  . LYS B 2 144 ? 47.897 63.498 30.019 1.00 227.62 ? 144 LYS B NZ  1 
ATOM   2170 N  N   . TYR B 2 145 ? 49.050 59.963 35.900 1.00 165.75 ? 145 TYR B N   1 
ATOM   2171 C  CA  . TYR B 2 145 ? 50.055 60.496 36.822 1.00 186.60 ? 145 TYR B CA  1 
ATOM   2172 C  C   . TYR B 2 145 ? 51.469 60.216 36.307 1.00 211.73 ? 145 TYR B C   1 
ATOM   2173 O  O   . TYR B 2 145 ? 52.313 61.116 36.285 1.00 220.13 ? 145 TYR B O   1 
ATOM   2174 C  CB  . TYR B 2 145 ? 49.894 59.885 38.223 1.00 185.64 ? 145 TYR B CB  1 
ATOM   2175 C  CG  . TYR B 2 145 ? 48.569 60.181 38.896 1.00 180.28 ? 145 TYR B CG  1 
ATOM   2176 C  CD1 . TYR B 2 145 ? 48.414 61.302 39.717 1.00 180.74 ? 145 TYR B CD1 1 
ATOM   2177 C  CD2 . TYR B 2 145 ? 47.469 59.332 38.724 1.00 175.29 ? 145 TYR B CD2 1 
ATOM   2178 C  CE1 . TYR B 2 145 ? 47.200 61.571 40.339 1.00 181.93 ? 145 TYR B CE1 1 
ATOM   2179 C  CE2 . TYR B 2 145 ? 46.255 59.594 39.336 1.00 172.99 ? 145 TYR B CE2 1 
ATOM   2180 C  CZ  . TYR B 2 145 ? 46.124 60.710 40.142 1.00 179.45 ? 145 TYR B CZ  1 
ATOM   2181 O  OH  . TYR B 2 145 ? 44.915 60.956 40.740 1.00 178.28 ? 145 TYR B OH  1 
ATOM   2182 N  N   . HIS B 2 146 ? 51.709 58.968 35.895 1.00 241.71 ? 146 HIS B N   1 
ATOM   2183 C  CA  . HIS B 2 146 ? 53.021 58.515 35.406 1.00 268.51 ? 146 HIS B CA  1 
ATOM   2184 C  C   . HIS B 2 146 ? 52.900 57.868 34.019 1.00 298.47 ? 146 HIS B C   1 
ATOM   2185 O  O   . HIS B 2 146 ? 52.579 58.555 33.048 1.00 314.69 ? 146 HIS B O   1 
ATOM   2186 C  CB  . HIS B 2 146 ? 53.692 57.565 36.420 1.00 268.14 ? 146 HIS B CB  1 
ATOM   2187 C  CG  . HIS B 2 146 ? 52.843 56.398 36.831 1.00 263.55 ? 146 HIS B CG  1 
ATOM   2188 N  ND1 . HIS B 2 146 ? 52.847 55.199 36.150 1.00 266.40 ? 146 HIS B ND1 1 
ATOM   2189 C  CD2 . HIS B 2 146 ? 51.971 56.245 37.856 1.00 258.58 ? 146 HIS B CD2 1 
ATOM   2190 C  CE1 . HIS B 2 146 ? 52.010 54.360 36.735 1.00 265.82 ? 146 HIS B CE1 1 
ATOM   2191 N  NE2 . HIS B 2 146 ? 51.466 54.970 37.773 1.00 259.26 ? 146 HIS B NE2 1 
ATOM   2192 O  OXT . HIS B 2 146 ? 53.115 56.671 33.805 1.00 316.18 ? 146 HIS B OXT 1 
ATOM   2193 N  N   . VAL C 1 1   ? 59.289 49.277 67.162 1.00 80.79  ? 1   VAL C N   1 
ATOM   2194 C  CA  . VAL C 1 1   ? 58.589 50.514 67.604 1.00 80.62  ? 1   VAL C CA  1 
ATOM   2195 C  C   . VAL C 1 1   ? 59.575 51.696 67.685 1.00 75.72  ? 1   VAL C C   1 
ATOM   2196 O  O   . VAL C 1 1   ? 59.537 52.582 66.835 1.00 78.68  ? 1   VAL C O   1 
ATOM   2197 C  CB  . VAL C 1 1   ? 57.857 50.285 68.948 1.00 88.32  ? 1   VAL C CB  1 
ATOM   2198 C  CG1 . VAL C 1 1   ? 57.109 51.552 69.368 1.00 102.85 ? 1   VAL C CG1 1 
ATOM   2199 C  CG2 . VAL C 1 1   ? 56.920 49.084 68.839 1.00 83.86  ? 1   VAL C CG2 1 
ATOM   2200 N  N   . LEU C 1 2   ? 60.450 51.684 68.694 1.00 68.84  ? 2   LEU C N   1 
ATOM   2201 C  CA  . LEU C 1 2   ? 61.524 52.671 68.870 1.00 62.01  ? 2   LEU C CA  1 
ATOM   2202 C  C   . LEU C 1 2   ? 62.486 52.114 69.908 1.00 62.96  ? 2   LEU C C   1 
ATOM   2203 O  O   . LEU C 1 2   ? 62.125 52.017 71.086 1.00 64.26  ? 2   LEU C O   1 
ATOM   2204 C  CB  . LEU C 1 2   ? 60.974 54.007 69.375 1.00 60.28  ? 2   LEU C CB  1 
ATOM   2205 C  CG  . LEU C 1 2   ? 60.728 55.150 68.390 1.00 60.51  ? 2   LEU C CG  1 
ATOM   2206 C  CD1 . LEU C 1 2   ? 60.009 56.279 69.109 1.00 62.88  ? 2   LEU C CD1 1 
ATOM   2207 C  CD2 . LEU C 1 2   ? 62.020 55.658 67.764 1.00 57.85  ? 2   LEU C CD2 1 
ATOM   2208 N  N   . SER C 1 3   ? 63.690 51.732 69.491 1.00 64.93  ? 3   SER C N   1 
ATOM   2209 C  CA  . SER C 1 3   ? 64.666 51.182 70.435 1.00 70.45  ? 3   SER C CA  1 
ATOM   2210 C  C   . SER C 1 3   ? 65.168 52.264 71.393 1.00 78.98  ? 3   SER C C   1 
ATOM   2211 O  O   . SER C 1 3   ? 65.071 53.456 71.076 1.00 83.26  ? 3   SER C O   1 
ATOM   2212 C  CB  . SER C 1 3   ? 65.843 50.515 69.708 1.00 71.38  ? 3   SER C CB  1 
ATOM   2213 O  OG  . SER C 1 3   ? 66.373 51.340 68.689 1.00 71.67  ? 3   SER C OG  1 
ATOM   2214 N  N   . PRO C 1 4   ? 65.687 51.861 72.573 1.00 81.91  ? 4   PRO C N   1 
ATOM   2215 C  CA  . PRO C 1 4   ? 66.241 52.854 73.503 1.00 83.97  ? 4   PRO C CA  1 
ATOM   2216 C  C   . PRO C 1 4   ? 67.476 53.599 72.968 1.00 81.29  ? 4   PRO C C   1 
ATOM   2217 O  O   . PRO C 1 4   ? 67.721 54.740 73.377 1.00 81.09  ? 4   PRO C O   1 
ATOM   2218 C  CB  . PRO C 1 4   ? 66.587 52.021 74.743 1.00 85.72  ? 4   PRO C CB  1 
ATOM   2219 C  CG  . PRO C 1 4   ? 66.744 50.633 74.239 1.00 83.51  ? 4   PRO C CG  1 
ATOM   2220 C  CD  . PRO C 1 4   ? 65.731 50.504 73.148 1.00 80.91  ? 4   PRO C CD  1 
ATOM   2221 N  N   . ALA C 1 5   ? 68.233 52.961 72.071 1.00 76.81  ? 5   ALA C N   1 
ATOM   2222 C  CA  . ALA C 1 5   ? 69.302 53.638 71.325 1.00 78.92  ? 5   ALA C CA  1 
ATOM   2223 C  C   . ALA C 1 5   ? 68.773 54.722 70.359 1.00 79.56  ? 5   ALA C C   1 
ATOM   2224 O  O   . ALA C 1 5   ? 69.383 55.787 70.226 1.00 83.08  ? 5   ALA C O   1 
ATOM   2225 C  CB  . ALA C 1 5   ? 70.143 52.621 70.572 1.00 77.46  ? 5   ALA C CB  1 
ATOM   2226 N  N   . ASP C 1 6   ? 67.651 54.444 69.692 1.00 74.42  ? 6   ASP C N   1 
ATOM   2227 C  CA  . ASP C 1 6   ? 67.004 55.424 68.818 1.00 70.51  ? 6   ASP C CA  1 
ATOM   2228 C  C   . ASP C 1 6   ? 66.428 56.603 69.584 1.00 64.12  ? 6   ASP C C   1 
ATOM   2229 O  O   . ASP C 1 6   ? 66.474 57.721 69.085 1.00 67.80  ? 6   ASP C O   1 
ATOM   2230 C  CB  . ASP C 1 6   ? 65.896 54.778 67.969 1.00 83.66  ? 6   ASP C CB  1 
ATOM   2231 C  CG  . ASP C 1 6   ? 66.439 53.858 66.862 1.00 97.06  ? 6   ASP C CG  1 
ATOM   2232 O  OD1 . ASP C 1 6   ? 67.668 53.833 66.614 1.00 107.01 ? 6   ASP C OD1 1 
ATOM   2233 O  OD2 . ASP C 1 6   ? 65.621 53.148 66.235 1.00 94.39  ? 6   ASP C OD2 1 
ATOM   2234 N  N   . LYS C 1 7   ? 65.884 56.370 70.777 1.00 63.16  ? 7   LYS C N   1 
ATOM   2235 C  CA  . LYS C 1 7   ? 65.367 57.469 71.604 1.00 65.72  ? 7   LYS C CA  1 
ATOM   2236 C  C   . LYS C 1 7   ? 66.469 58.428 72.013 1.00 64.48  ? 7   LYS C C   1 
ATOM   2237 O  O   . LYS C 1 7   ? 66.259 59.638 72.034 1.00 70.40  ? 7   LYS C O   1 
ATOM   2238 C  CB  . LYS C 1 7   ? 64.688 56.958 72.863 1.00 74.26  ? 7   LYS C CB  1 
ATOM   2239 C  CG  . LYS C 1 7   ? 63.396 56.206 72.614 1.00 85.67  ? 7   LYS C CG  1 
ATOM   2240 C  CD  . LYS C 1 7   ? 62.912 55.519 73.887 1.00 94.62  ? 7   LYS C CD  1 
ATOM   2241 C  CE  . LYS C 1 7   ? 61.737 54.585 73.625 1.00 99.16  ? 7   LYS C CE  1 
ATOM   2242 N  NZ  . LYS C 1 7   ? 60.475 55.311 73.289 1.00 101.26 ? 7   LYS C NZ  1 
ATOM   2243 N  N   . THR C 1 8   ? 67.638 57.891 72.346 1.00 62.39  ? 8   THR C N   1 
ATOM   2244 C  CA  . THR C 1 8   ? 68.801 58.719 72.649 1.00 62.53  ? 8   THR C CA  1 
ATOM   2245 C  C   . THR C 1 8   ? 69.191 59.566 71.444 1.00 58.76  ? 8   THR C C   1 
ATOM   2246 O  O   . THR C 1 8   ? 69.260 60.792 71.544 1.00 58.18  ? 8   THR C O   1 
ATOM   2247 C  CB  . THR C 1 8   ? 70.001 57.859 73.070 1.00 67.88  ? 8   THR C CB  1 
ATOM   2248 O  OG1 . THR C 1 8   ? 69.660 57.118 74.251 1.00 70.69  ? 8   THR C OG1 1 
ATOM   2249 C  CG2 . THR C 1 8   ? 71.238 58.728 73.340 1.00 71.38  ? 8   THR C CG2 1 
ATOM   2250 N  N   . ASN C 1 9   ? 69.433 58.899 70.317 1.00 54.22  ? 9   ASN C N   1 
ATOM   2251 C  CA  . ASN C 1 9   ? 69.800 59.567 69.067 1.00 51.81  ? 9   ASN C CA  1 
ATOM   2252 C  C   . ASN C 1 9   ? 68.872 60.705 68.681 1.00 47.09  ? 9   ASN C C   1 
ATOM   2253 O  O   . ASN C 1 9   ? 69.339 61.754 68.246 1.00 48.74  ? 9   ASN C O   1 
ATOM   2254 C  CB  . ASN C 1 9   ? 69.839 58.572 67.899 1.00 55.39  ? 9   ASN C CB  1 
ATOM   2255 C  CG  . ASN C 1 9   ? 71.111 57.754 67.858 1.00 58.74  ? 9   ASN C CG  1 
ATOM   2256 O  OD1 . ASN C 1 9   ? 71.118 56.626 67.359 1.00 59.75  ? 9   ASN C OD1 1 
ATOM   2257 N  ND2 . ASN C 1 9   ? 72.202 58.321 68.362 1.00 65.07  ? 9   ASN C ND2 1 
ATOM   2258 N  N   . VAL C 1 10  ? 67.570 60.495 68.817 1.00 44.18  ? 10  VAL C N   1 
ATOM   2259 C  CA  . VAL C 1 10  ? 66.612 61.536 68.491 1.00 45.83  ? 10  VAL C CA  1 
ATOM   2260 C  C   . VAL C 1 10  ? 66.807 62.714 69.432 1.00 49.12  ? 10  VAL C C   1 
ATOM   2261 O  O   . VAL C 1 10  ? 66.873 63.852 68.976 1.00 51.15  ? 10  VAL C O   1 
ATOM   2262 C  CB  . VAL C 1 10  ? 65.158 61.021 68.529 1.00 46.32  ? 10  VAL C CB  1 
ATOM   2263 C  CG1 . VAL C 1 10  ? 64.136 62.162 68.489 1.00 46.11  ? 10  VAL C CG1 1 
ATOM   2264 C  CG2 . VAL C 1 10  ? 64.929 60.086 67.357 1.00 47.40  ? 10  VAL C CG2 1 
ATOM   2265 N  N   . LYS C 1 11  ? 66.920 62.448 70.730 1.00 53.18  ? 11  LYS C N   1 
ATOM   2266 C  CA  . LYS C 1 11  ? 67.101 63.529 71.704 1.00 59.45  ? 11  LYS C CA  1 
ATOM   2267 C  C   . LYS C 1 11  ? 68.362 64.345 71.440 1.00 61.04  ? 11  LYS C C   1 
ATOM   2268 O  O   . LYS C 1 11  ? 68.314 65.581 71.403 1.00 60.48  ? 11  LYS C O   1 
ATOM   2269 C  CB  . LYS C 1 11  ? 67.112 62.983 73.131 1.00 64.98  ? 11  LYS C CB  1 
ATOM   2270 C  CG  . LYS C 1 11  ? 65.723 62.614 73.601 1.00 70.70  ? 11  LYS C CG  1 
ATOM   2271 C  CD  . LYS C 1 11  ? 65.715 61.989 74.981 1.00 76.24  ? 11  LYS C CD  1 
ATOM   2272 C  CE  . LYS C 1 11  ? 64.321 61.474 75.313 1.00 83.54  ? 11  LYS C CE  1 
ATOM   2273 N  NZ  . LYS C 1 11  ? 63.260 62.525 75.229 1.00 85.75  ? 11  LYS C NZ  1 
ATOM   2274 N  N   . ALA C 1 12  ? 69.470 63.638 71.237 1.00 60.09  ? 12  ALA C N   1 
ATOM   2275 C  CA  . ALA C 1 12  ? 70.765 64.254 70.962 1.00 59.22  ? 12  ALA C CA  1 
ATOM   2276 C  C   . ALA C 1 12  ? 70.759 65.071 69.673 1.00 57.15  ? 12  ALA C C   1 
ATOM   2277 O  O   . ALA C 1 12  ? 71.118 66.247 69.686 1.00 58.70  ? 12  ALA C O   1 
ATOM   2278 C  CB  . ALA C 1 12  ? 71.841 63.184 70.888 1.00 62.27  ? 12  ALA C CB  1 
ATOM   2279 N  N   . ALA C 1 13  ? 70.343 64.445 68.576 1.00 53.31  ? 13  ALA C N   1 
ATOM   2280 C  CA  . ALA C 1 13  ? 70.349 65.095 67.266 1.00 52.08  ? 13  ALA C CA  1 
ATOM   2281 C  C   . ALA C 1 13  ? 69.350 66.239 67.154 1.00 50.87  ? 13  ALA C C   1 
ATOM   2282 O  O   . ALA C 1 13  ? 69.636 67.221 66.478 1.00 54.09  ? 13  ALA C O   1 
ATOM   2283 C  CB  . ALA C 1 13  ? 70.096 64.084 66.165 1.00 53.84  ? 13  ALA C CB  1 
ATOM   2284 N  N   . TRP C 1 14  ? 68.188 66.119 67.793 1.00 51.26  ? 14  TRP C N   1 
ATOM   2285 C  CA  . TRP C 1 14  ? 67.220 67.222 67.814 1.00 52.05  ? 14  TRP C CA  1 
ATOM   2286 C  C   . TRP C 1 14  ? 67.650 68.326 68.782 1.00 57.40  ? 14  TRP C C   1 
ATOM   2287 O  O   . TRP C 1 14  ? 67.251 69.481 68.622 1.00 57.56  ? 14  TRP C O   1 
ATOM   2288 C  CB  . TRP C 1 14  ? 65.819 66.735 68.158 1.00 50.52  ? 14  TRP C CB  1 
ATOM   2289 C  CG  . TRP C 1 14  ? 64.802 67.758 67.871 1.00 49.26  ? 14  TRP C CG  1 
ATOM   2290 C  CD1 . TRP C 1 14  ? 64.198 68.592 68.767 1.00 53.73  ? 14  TRP C CD1 1 
ATOM   2291 C  CD2 . TRP C 1 14  ? 64.289 68.100 66.595 1.00 48.19  ? 14  TRP C CD2 1 
ATOM   2292 N  NE1 . TRP C 1 14  ? 63.319 69.430 68.124 1.00 50.73  ? 14  TRP C NE1 1 
ATOM   2293 C  CE2 . TRP C 1 14  ? 63.357 69.151 66.787 1.00 48.46  ? 14  TRP C CE2 1 
ATOM   2294 C  CE3 . TRP C 1 14  ? 64.520 67.621 65.303 1.00 49.22  ? 14  TRP C CE3 1 
ATOM   2295 C  CZ2 . TRP C 1 14  ? 62.664 69.736 65.737 1.00 50.85  ? 14  TRP C CZ2 1 
ATOM   2296 C  CZ3 . TRP C 1 14  ? 63.834 68.205 64.248 1.00 52.87  ? 14  TRP C CZ3 1 
ATOM   2297 C  CH2 . TRP C 1 14  ? 62.910 69.255 64.474 1.00 54.78  ? 14  TRP C CH2 1 
ATOM   2298 N  N   . GLY C 1 15  ? 68.453 67.971 69.784 1.00 65.43  ? 15  GLY C N   1 
ATOM   2299 C  CA  . GLY C 1 15  ? 69.148 68.965 70.608 1.00 73.97  ? 15  GLY C CA  1 
ATOM   2300 C  C   . GLY C 1 15  ? 70.083 69.888 69.827 1.00 77.74  ? 15  GLY C C   1 
ATOM   2301 O  O   . GLY C 1 15  ? 70.140 71.088 70.101 1.00 77.43  ? 15  GLY C O   1 
ATOM   2302 N  N   . LYS C 1 16  ? 70.804 69.329 68.853 1.00 81.90  ? 16  LYS C N   1 
ATOM   2303 C  CA  . LYS C 1 16  ? 71.758 70.097 68.038 1.00 84.79  ? 16  LYS C CA  1 
ATOM   2304 C  C   . LYS C 1 16  ? 71.074 71.049 67.064 1.00 75.27  ? 16  LYS C C   1 
ATOM   2305 O  O   . LYS C 1 16  ? 71.662 72.056 66.677 1.00 73.42  ? 16  LYS C O   1 
ATOM   2306 C  CB  . LYS C 1 16  ? 72.698 69.168 67.262 1.00 98.30  ? 16  LYS C CB  1 
ATOM   2307 C  CG  . LYS C 1 16  ? 73.551 68.252 68.132 1.00 118.82 ? 16  LYS C CG  1 
ATOM   2308 C  CD  . LYS C 1 16  ? 74.608 69.002 68.933 1.00 132.98 ? 16  LYS C CD  1 
ATOM   2309 C  CE  . LYS C 1 16  ? 75.450 68.045 69.769 1.00 145.19 ? 16  LYS C CE  1 
ATOM   2310 N  NZ  . LYS C 1 16  ? 74.656 67.323 70.807 1.00 150.29 ? 16  LYS C NZ  1 
ATOM   2311 N  N   . VAL C 1 17  ? 69.850 70.722 66.656 1.00 74.69  ? 17  VAL C N   1 
ATOM   2312 C  CA  . VAL C 1 17  ? 69.022 71.647 65.883 1.00 77.41  ? 17  VAL C CA  1 
ATOM   2313 C  C   . VAL C 1 17  ? 68.798 72.872 66.752 1.00 80.02  ? 17  VAL C C   1 
ATOM   2314 O  O   . VAL C 1 17  ? 69.162 73.986 66.373 1.00 77.49  ? 17  VAL C O   1 
ATOM   2315 C  CB  . VAL C 1 17  ? 67.662 71.019 65.485 1.00 77.98  ? 17  VAL C CB  1 
ATOM   2316 C  CG1 . VAL C 1 17  ? 66.687 72.073 64.965 1.00 77.56  ? 17  VAL C CG1 1 
ATOM   2317 C  CG2 . VAL C 1 17  ? 67.864 69.920 64.452 1.00 78.26  ? 17  VAL C CG2 1 
ATOM   2318 N  N   . GLY C 1 18  ? 68.209 72.637 67.922 1.00 86.34  ? 18  GLY C N   1 
ATOM   2319 C  CA  . GLY C 1 18  ? 68.060 73.652 68.956 1.00 91.50  ? 18  GLY C CA  1 
ATOM   2320 C  C   . GLY C 1 18  ? 67.198 74.838 68.571 1.00 89.91  ? 18  GLY C C   1 
ATOM   2321 O  O   . GLY C 1 18  ? 65.987 74.701 68.379 1.00 93.56  ? 18  GLY C O   1 
ATOM   2322 N  N   . ALA C 1 19  ? 67.840 75.996 68.438 1.00 88.31  ? 19  ALA C N   1 
ATOM   2323 C  CA  . ALA C 1 19  ? 67.149 77.280 68.331 1.00 91.97  ? 19  ALA C CA  1 
ATOM   2324 C  C   . ALA C 1 19  ? 66.901 77.777 66.902 1.00 92.62  ? 19  ALA C C   1 
ATOM   2325 O  O   . ALA C 1 19  ? 66.316 78.846 66.725 1.00 93.79  ? 19  ALA C O   1 
ATOM   2326 C  CB  . ALA C 1 19  ? 67.917 78.330 69.114 1.00 95.34  ? 19  ALA C CB  1 
ATOM   2327 N  N   . HIS C 1 20  ? 67.333 77.020 65.894 1.00 96.80  ? 20  HIS C N   1 
ATOM   2328 C  CA  . HIS C 1 20  ? 66.997 77.324 64.498 1.00 100.92 ? 20  HIS C CA  1 
ATOM   2329 C  C   . HIS C 1 20  ? 65.769 76.530 64.042 1.00 90.60  ? 20  HIS C C   1 
ATOM   2330 O  O   . HIS C 1 20  ? 65.558 76.337 62.840 1.00 90.28  ? 20  HIS C O   1 
ATOM   2331 C  CB  . HIS C 1 20  ? 68.191 77.021 63.588 1.00 116.11 ? 20  HIS C CB  1 
ATOM   2332 C  CG  . HIS C 1 20  ? 69.409 77.825 63.909 1.00 132.11 ? 20  HIS C CG  1 
ATOM   2333 N  ND1 . HIS C 1 20  ? 70.428 77.347 64.705 1.00 140.99 ? 20  HIS C ND1 1 
ATOM   2334 C  CD2 . HIS C 1 20  ? 69.769 79.079 63.547 1.00 144.32 ? 20  HIS C CD2 1 
ATOM   2335 C  CE1 . HIS C 1 20  ? 71.365 78.272 64.817 1.00 150.50 ? 20  HIS C CE1 1 
ATOM   2336 N  NE2 . HIS C 1 20  ? 70.989 79.332 64.124 1.00 152.94 ? 20  HIS C NE2 1 
ATOM   2337 N  N   . ALA C 1 21  ? 64.947 76.097 64.997 1.00 80.04  ? 21  ALA C N   1 
ATOM   2338 C  CA  . ALA C 1 21  ? 63.824 75.226 64.706 1.00 74.25  ? 21  ALA C CA  1 
ATOM   2339 C  C   . ALA C 1 21  ? 62.808 75.950 63.840 1.00 68.99  ? 21  ALA C C   1 
ATOM   2340 O  O   . ALA C 1 21  ? 62.286 75.372 62.894 1.00 76.15  ? 21  ALA C O   1 
ATOM   2341 C  CB  . ALA C 1 21  ? 63.186 74.734 65.994 1.00 75.25  ? 21  ALA C CB  1 
ATOM   2342 N  N   . GLY C 1 22  ? 62.553 77.217 64.146 1.00 65.38  ? 22  GLY C N   1 
ATOM   2343 C  CA  . GLY C 1 22  ? 61.681 78.037 63.321 1.00 66.77  ? 22  GLY C CA  1 
ATOM   2344 C  C   . GLY C 1 22  ? 62.085 78.032 61.862 1.00 66.16  ? 22  GLY C C   1 
ATOM   2345 O  O   . GLY C 1 22  ? 61.265 77.771 60.983 1.00 65.56  ? 22  GLY C O   1 
ATOM   2346 N  N   . GLU C 1 23  ? 63.360 78.294 61.611 1.00 71.60  ? 23  GLU C N   1 
ATOM   2347 C  CA  . GLU C 1 23  ? 63.853 78.422 60.248 1.00 78.36  ? 23  GLU C CA  1 
ATOM   2348 C  C   . GLU C 1 23  ? 63.829 77.097 59.502 1.00 64.14  ? 23  GLU C C   1 
ATOM   2349 O  O   . GLU C 1 23  ? 63.445 77.064 58.333 1.00 65.84  ? 23  GLU C O   1 
ATOM   2350 C  CB  . GLU C 1 23  ? 65.266 79.002 60.244 1.00 101.17 ? 23  GLU C CB  1 
ATOM   2351 C  CG  . GLU C 1 23  ? 65.763 79.444 58.872 1.00 121.46 ? 23  GLU C CG  1 
ATOM   2352 C  CD  . GLU C 1 23  ? 67.185 79.993 58.896 1.00 147.89 ? 23  GLU C CD  1 
ATOM   2353 O  OE1 . GLU C 1 23  ? 67.789 80.099 59.990 1.00 161.79 ? 23  GLU C OE1 1 
ATOM   2354 O  OE2 . GLU C 1 23  ? 67.706 80.322 57.808 1.00 164.87 ? 23  GLU C OE2 1 
ATOM   2355 N  N   . TYR C 1 24  ? 64.239 76.017 60.163 1.00 52.41  ? 24  TYR C N   1 
ATOM   2356 C  CA  . TYR C 1 24  ? 64.221 74.701 59.529 1.00 47.41  ? 24  TYR C CA  1 
ATOM   2357 C  C   . TYR C 1 24  ? 62.807 74.256 59.224 1.00 43.22  ? 24  TYR C C   1 
ATOM   2358 O  O   . TYR C 1 24  ? 62.567 73.676 58.166 1.00 47.94  ? 24  TYR C O   1 
ATOM   2359 C  CB  . TYR C 1 24  ? 64.934 73.639 60.368 1.00 48.11  ? 24  TYR C CB  1 
ATOM   2360 C  CG  . TYR C 1 24  ? 66.425 73.867 60.563 1.00 53.96  ? 24  TYR C CG  1 
ATOM   2361 C  CD1 . TYR C 1 24  ? 67.171 74.727 59.721 1.00 56.46  ? 24  TYR C CD1 1 
ATOM   2362 C  CD2 . TYR C 1 24  ? 67.111 73.201 61.585 1.00 56.32  ? 24  TYR C CD2 1 
ATOM   2363 C  CE1 . TYR C 1 24  ? 68.535 74.923 59.919 1.00 58.68  ? 24  TYR C CE1 1 
ATOM   2364 C  CE2 . TYR C 1 24  ? 68.476 73.386 61.787 1.00 56.99  ? 24  TYR C CE2 1 
ATOM   2365 C  CZ  . TYR C 1 24  ? 69.183 74.247 60.957 1.00 60.60  ? 24  TYR C CZ  1 
ATOM   2366 O  OH  . TYR C 1 24  ? 70.534 74.435 61.163 1.00 64.50  ? 24  TYR C OH  1 
ATOM   2367 N  N   . GLY C 1 25  ? 61.874 74.537 60.129 1.00 36.17  ? 25  GLY C N   1 
ATOM   2368 C  CA  . GLY C 1 25  ? 60.467 74.239 59.905 1.00 31.34  ? 25  GLY C CA  1 
ATOM   2369 C  C   . GLY C 1 25  ? 59.917 74.949 58.689 1.00 28.88  ? 25  GLY C C   1 
ATOM   2370 O  O   . GLY C 1 25  ? 59.130 74.380 57.943 1.00 29.13  ? 25  GLY C O   1 
ATOM   2371 N  N   . ALA C 1 26  ? 60.337 76.188 58.487 1.00 28.39  ? 26  ALA C N   1 
ATOM   2372 C  CA  . ALA C 1 26  ? 59.858 76.985 57.374 1.00 29.92  ? 26  ALA C CA  1 
ATOM   2373 C  C   . ALA C 1 26  ? 60.373 76.451 56.062 1.00 31.90  ? 26  ALA C C   1 
ATOM   2374 O  O   . ALA C 1 26  ? 59.622 76.307 55.105 1.00 33.38  ? 26  ALA C O   1 
ATOM   2375 C  CB  . ALA C 1 26  ? 60.299 78.427 57.538 1.00 30.88  ? 26  ALA C CB  1 
ATOM   2376 N  N   . GLU C 1 27  ? 61.668 76.175 56.022 1.00 36.93  ? 27  GLU C N   1 
ATOM   2377 C  CA  . GLU C 1 27  ? 62.321 75.677 54.821 1.00 41.46  ? 27  GLU C CA  1 
ATOM   2378 C  C   . GLU C 1 27  ? 61.765 74.318 54.406 1.00 37.34  ? 27  GLU C C   1 
ATOM   2379 O  O   . GLU C 1 27  ? 61.600 74.064 53.218 1.00 37.95  ? 27  GLU C O   1 
ATOM   2380 C  CB  . GLU C 1 27  ? 63.821 75.570 55.064 1.00 52.92  ? 27  GLU C CB  1 
ATOM   2381 C  CG  . GLU C 1 27  ? 64.649 75.239 53.831 1.00 66.10  ? 27  GLU C CG  1 
ATOM   2382 C  CD  . GLU C 1 27  ? 66.121 74.986 54.148 1.00 79.18  ? 27  GLU C CD  1 
ATOM   2383 O  OE1 . GLU C 1 27  ? 66.578 75.337 55.263 1.00 87.05  ? 27  GLU C OE1 1 
ATOM   2384 O  OE2 . GLU C 1 27  ? 66.826 74.436 53.270 1.00 84.69  ? 27  GLU C OE2 1 
ATOM   2385 N  N   . ALA C 1 28  ? 61.479 73.457 55.385 1.00 32.66  ? 28  ALA C N   1 
ATOM   2386 C  CA  . ALA C 1 28  ? 60.797 72.183 55.138 1.00 28.71  ? 28  ALA C CA  1 
ATOM   2387 C  C   . ALA C 1 28  ? 59.455 72.379 54.423 1.00 27.38  ? 28  ALA C C   1 
ATOM   2388 O  O   . ALA C 1 28  ? 59.259 71.831 53.337 1.00 26.80  ? 28  ALA C O   1 
ATOM   2389 C  CB  . ALA C 1 28  ? 60.609 71.407 56.434 1.00 27.07  ? 28  ALA C CB  1 
ATOM   2390 N  N   . LEU C 1 29  ? 58.553 73.170 54.999 1.00 27.91  ? 29  LEU C N   1 
ATOM   2391 C  CA  . LEU C 1 29  ? 57.299 73.501 54.315 1.00 30.12  ? 29  LEU C CA  1 
ATOM   2392 C  C   . LEU C 1 29  ? 57.510 74.045 52.920 1.00 32.15  ? 29  LEU C C   1 
ATOM   2393 O  O   . LEU C 1 29  ? 56.749 73.709 52.023 1.00 36.56  ? 29  LEU C O   1 
ATOM   2394 C  CB  . LEU C 1 29  ? 56.463 74.516 55.085 1.00 31.13  ? 29  LEU C CB  1 
ATOM   2395 C  CG  . LEU C 1 29  ? 55.813 73.988 56.355 1.00 34.40  ? 29  LEU C CG  1 
ATOM   2396 C  CD1 . LEU C 1 29  ? 55.027 75.086 57.049 1.00 34.59  ? 29  LEU C CD1 1 
ATOM   2397 C  CD2 . LEU C 1 29  ? 54.909 72.799 56.060 1.00 37.53  ? 29  LEU C CD2 1 
ATOM   2398 N  N   . GLU C 1 30  ? 58.529 74.871 52.729 1.00 33.80  ? 30  GLU C N   1 
ATOM   2399 C  CA  . GLU C 1 30  ? 58.759 75.493 51.436 1.00 36.26  ? 30  GLU C CA  1 
ATOM   2400 C  C   . GLU C 1 30  ? 59.200 74.501 50.357 1.00 29.75  ? 30  GLU C C   1 
ATOM   2401 O  O   . GLU C 1 30  ? 58.746 74.596 49.219 1.00 29.01  ? 30  GLU C O   1 
ATOM   2402 C  CB  . GLU C 1 30  ? 59.780 76.607 51.578 1.00 49.47  ? 30  GLU C CB  1 
ATOM   2403 C  CG  . GLU C 1 30  ? 59.835 77.548 50.383 1.00 65.29  ? 30  GLU C CG  1 
ATOM   2404 C  CD  . GLU C 1 30  ? 60.913 78.619 50.521 1.00 82.81  ? 30  GLU C CD  1 
ATOM   2405 O  OE1 . GLU C 1 30  ? 61.192 79.067 51.663 1.00 95.17  ? 30  GLU C OE1 1 
ATOM   2406 O  OE2 . GLU C 1 30  ? 61.483 79.019 49.478 1.00 92.92  ? 30  GLU C OE2 1 
ATOM   2407 N  N   . ARG C 1 31  ? 60.090 73.575 50.711 1.00 25.16  ? 31  ARG C N   1 
ATOM   2408 C  CA  . ARG C 1 31  ? 60.511 72.508 49.803 1.00 22.50  ? 31  ARG C CA  1 
ATOM   2409 C  C   . ARG C 1 31  ? 59.336 71.654 49.442 1.00 22.56  ? 31  ARG C C   1 
ATOM   2410 O  O   . ARG C 1 31  ? 59.148 71.351 48.271 1.00 23.11  ? 31  ARG C O   1 
ATOM   2411 C  CB  . ARG C 1 31  ? 61.556 71.597 50.437 1.00 21.81  ? 31  ARG C CB  1 
ATOM   2412 C  CG  . ARG C 1 31  ? 62.938 72.194 50.494 1.00 22.05  ? 31  ARG C CG  1 
ATOM   2413 C  CD  . ARG C 1 31  ? 63.863 71.400 51.399 1.00 22.31  ? 31  ARG C CD  1 
ATOM   2414 N  NE  . ARG C 1 31  ? 65.151 72.080 51.519 1.00 23.01  ? 31  ARG C NE  1 
ATOM   2415 C  CZ  . ARG C 1 31  ? 66.108 72.091 50.589 1.00 23.88  ? 31  ARG C CZ  1 
ATOM   2416 N  NH1 . ARG C 1 31  ? 67.235 72.761 50.817 1.00 24.81  ? 31  ARG C NH1 1 
ATOM   2417 N  NH2 . ARG C 1 31  ? 65.967 71.434 49.435 1.00 23.81  ? 31  ARG C NH2 1 
ATOM   2418 N  N   . MET C 1 32  ? 58.559 71.249 50.448 1.00 23.02  ? 32  MET C N   1 
ATOM   2419 C  CA  . MET C 1 32  ? 57.383 70.422 50.226 1.00 23.92  ? 32  MET C CA  1 
ATOM   2420 C  C   . MET C 1 32  ? 56.388 71.058 49.237 1.00 23.92  ? 32  MET C C   1 
ATOM   2421 O  O   . MET C 1 32  ? 56.032 70.407 48.267 1.00 24.70  ? 32  MET C O   1 
ATOM   2422 C  CB  . MET C 1 32  ? 56.693 70.082 51.540 1.00 27.08  ? 32  MET C CB  1 
ATOM   2423 C  CG  . MET C 1 32  ? 55.524 69.105 51.378 1.00 31.59  ? 32  MET C CG  1 
ATOM   2424 S  SD  . MET C 1 32  ? 54.543 68.676 52.849 1.00 37.51  ? 32  MET C SD  1 
ATOM   2425 C  CE  . MET C 1 32  ? 54.008 70.280 53.502 1.00 36.28  ? 32  MET C CE  1 
ATOM   2426 N  N   . PHE C 1 33  ? 55.957 72.304 49.443 1.00 24.63  ? 33  PHE C N   1 
ATOM   2427 C  CA  . PHE C 1 33  ? 55.056 72.961 48.477 1.00 25.98  ? 33  PHE C CA  1 
ATOM   2428 C  C   . PHE C 1 33  ? 55.614 73.012 47.055 1.00 29.44  ? 33  PHE C C   1 
ATOM   2429 O  O   . PHE C 1 33  ? 54.857 72.823 46.113 1.00 32.57  ? 33  PHE C O   1 
ATOM   2430 C  CB  . PHE C 1 33  ? 54.688 74.391 48.871 1.00 26.45  ? 33  PHE C CB  1 
ATOM   2431 C  CG  . PHE C 1 33  ? 53.876 74.493 50.122 1.00 27.51  ? 33  PHE C CG  1 
ATOM   2432 C  CD1 . PHE C 1 33  ? 52.695 73.804 50.254 1.00 30.26  ? 33  PHE C CD1 1 
ATOM   2433 C  CD2 . PHE C 1 33  ? 54.285 75.301 51.169 1.00 28.79  ? 33  PHE C CD2 1 
ATOM   2434 C  CE1 . PHE C 1 33  ? 51.949 73.891 51.426 1.00 31.71  ? 33  PHE C CE1 1 
ATOM   2435 C  CE2 . PHE C 1 33  ? 53.552 75.393 52.345 1.00 29.58  ? 33  PHE C CE2 1 
ATOM   2436 C  CZ  . PHE C 1 33  ? 52.378 74.691 52.474 1.00 30.41  ? 33  PHE C CZ  1 
ATOM   2437 N  N   . LEU C 1 34  ? 56.911 73.281 46.882 1.00 32.98  ? 34  LEU C N   1 
ATOM   2438 C  CA  . LEU C 1 34  ? 57.533 73.270 45.528 1.00 34.23  ? 34  LEU C CA  1 
ATOM   2439 C  C   . LEU C 1 34  ? 57.609 71.904 44.897 1.00 31.39  ? 34  LEU C C   1 
ATOM   2440 O  O   . LEU C 1 34  ? 57.300 71.760 43.722 1.00 31.99  ? 34  LEU C O   1 
ATOM   2441 C  CB  . LEU C 1 34  ? 58.956 73.815 45.546 1.00 38.03  ? 34  LEU C CB  1 
ATOM   2442 C  CG  . LEU C 1 34  ? 59.048 75.324 45.456 1.00 44.66  ? 34  LEU C CG  1 
ATOM   2443 C  CD1 . LEU C 1 34  ? 60.414 75.790 45.945 1.00 49.40  ? 34  LEU C CD1 1 
ATOM   2444 C  CD2 . LEU C 1 34  ? 58.782 75.776 44.023 1.00 47.39  ? 34  LEU C CD2 1 
ATOM   2445 N  N   . SER C 1 35  ? 58.055 70.922 45.673 1.00 30.22  ? 35  SER C N   1 
ATOM   2446 C  CA  . SER C 1 35  ? 58.310 69.577 45.162 1.00 30.76  ? 35  SER C CA  1 
ATOM   2447 C  C   . SER C 1 35  ? 57.025 68.823 44.828 1.00 31.93  ? 35  SER C C   1 
ATOM   2448 O  O   . SER C 1 35  ? 56.950 68.169 43.785 1.00 34.90  ? 35  SER C O   1 
ATOM   2449 C  CB  . SER C 1 35  ? 59.139 68.758 46.158 1.00 30.50  ? 35  SER C CB  1 
ATOM   2450 O  OG  . SER C 1 35  ? 60.435 69.308 46.317 1.00 31.20  ? 35  SER C OG  1 
ATOM   2451 N  N   . PHE C 1 36  ? 56.028 68.914 45.706 1.00 30.48  ? 36  PHE C N   1 
ATOM   2452 C  CA  . PHE C 1 36  ? 54.795 68.135 45.587 1.00 30.10  ? 36  PHE C CA  1 
ATOM   2453 C  C   . PHE C 1 36  ? 53.596 69.070 45.656 1.00 32.32  ? 36  PHE C C   1 
ATOM   2454 O  O   . PHE C 1 36  ? 52.887 69.120 46.659 1.00 34.80  ? 36  PHE C O   1 
ATOM   2455 C  CB  . PHE C 1 36  ? 54.711 67.121 46.714 1.00 28.97  ? 36  PHE C CB  1 
ATOM   2456 C  CG  . PHE C 1 36  ? 55.969 66.382 46.937 1.00 28.67  ? 36  PHE C CG  1 
ATOM   2457 C  CD1 . PHE C 1 36  ? 56.330 65.367 46.073 1.00 29.02  ? 36  PHE C CD1 1 
ATOM   2458 C  CD2 . PHE C 1 36  ? 56.801 66.703 48.012 1.00 29.25  ? 36  PHE C CD2 1 
ATOM   2459 C  CE1 . PHE C 1 36  ? 57.507 64.668 46.271 1.00 30.70  ? 36  PHE C CE1 1 
ATOM   2460 C  CE2 . PHE C 1 36  ? 57.981 66.014 48.220 1.00 30.28  ? 36  PHE C CE2 1 
ATOM   2461 C  CZ  . PHE C 1 36  ? 58.335 64.989 47.348 1.00 31.62  ? 36  PHE C CZ  1 
ATOM   2462 N  N   . PRO C 1 37  ? 53.342 69.804 44.583 1.00 33.19  ? 37  PRO C N   1 
ATOM   2463 C  CA  . PRO C 1 37  ? 52.400 70.921 44.648 1.00 33.73  ? 37  PRO C CA  1 
ATOM   2464 C  C   . PRO C 1 37  ? 50.930 70.594 44.933 1.00 33.34  ? 37  PRO C C   1 
ATOM   2465 O  O   . PRO C 1 37  ? 50.175 71.500 45.284 1.00 32.96  ? 37  PRO C O   1 
ATOM   2466 C  CB  . PRO C 1 37  ? 52.558 71.578 43.285 1.00 36.48  ? 37  PRO C CB  1 
ATOM   2467 C  CG  . PRO C 1 37  ? 53.021 70.466 42.398 1.00 37.62  ? 37  PRO C CG  1 
ATOM   2468 C  CD  . PRO C 1 37  ? 53.899 69.609 43.239 1.00 34.67  ? 37  PRO C CD  1 
ATOM   2469 N  N   . THR C 1 38  ? 50.525 69.336 44.813 1.00 35.66  ? 38  THR C N   1 
ATOM   2470 C  CA  . THR C 1 38  ? 49.180 68.929 45.253 1.00 40.04  ? 38  THR C CA  1 
ATOM   2471 C  C   . THR C 1 38  ? 48.969 68.972 46.768 1.00 37.42  ? 38  THR C C   1 
ATOM   2472 O  O   . THR C 1 38  ? 47.835 68.866 47.236 1.00 37.11  ? 38  THR C O   1 
ATOM   2473 C  CB  . THR C 1 38  ? 48.852 67.504 44.795 1.00 47.03  ? 38  THR C CB  1 
ATOM   2474 O  OG1 . THR C 1 38  ? 49.922 66.622 45.171 1.00 49.36  ? 38  THR C OG1 1 
ATOM   2475 C  CG2 . THR C 1 38  ? 48.663 67.476 43.286 1.00 53.36  ? 38  THR C CG2 1 
ATOM   2476 N  N   . THR C 1 39  ? 50.060 69.089 47.524 1.00 33.45  ? 39  THR C N   1 
ATOM   2477 C  CA  . THR C 1 39  ? 49.993 69.299 48.960 1.00 30.77  ? 39  THR C CA  1 
ATOM   2478 C  C   . THR C 1 39  ? 49.452 70.692 49.340 1.00 31.54  ? 39  THR C C   1 
ATOM   2479 O  O   . THR C 1 39  ? 49.054 70.900 50.481 1.00 31.83  ? 39  THR C O   1 
ATOM   2480 C  CB  . THR C 1 39  ? 51.376 69.082 49.606 1.00 28.48  ? 39  THR C CB  1 
ATOM   2481 O  OG1 . THR C 1 39  ? 51.222 68.839 51.006 1.00 29.45  ? 39  THR C OG1 1 
ATOM   2482 C  CG2 . THR C 1 39  ? 52.279 70.288 49.406 1.00 27.95  ? 39  THR C CG2 1 
ATOM   2483 N  N   . LYS C 1 40  ? 49.461 71.643 48.404 1.00 32.67  ? 40  LYS C N   1 
ATOM   2484 C  CA  . LYS C 1 40  ? 48.986 72.998 48.680 1.00 33.30  ? 40  LYS C CA  1 
ATOM   2485 C  C   . LYS C 1 40  ? 47.522 73.036 49.030 1.00 32.25  ? 40  LYS C C   1 
ATOM   2486 O  O   . LYS C 1 40  ? 47.106 73.838 49.863 1.00 32.25  ? 40  LYS C O   1 
ATOM   2487 C  CB  . LYS C 1 40  ? 49.208 73.911 47.484 1.00 37.43  ? 40  LYS C CB  1 
ATOM   2488 C  CG  . LYS C 1 40  ? 50.654 74.280 47.250 1.00 41.49  ? 40  LYS C CG  1 
ATOM   2489 C  CD  . LYS C 1 40  ? 50.786 75.138 46.005 1.00 47.01  ? 40  LYS C CD  1 
ATOM   2490 C  CE  . LYS C 1 40  ? 52.247 75.328 45.629 1.00 54.21  ? 40  LYS C CE  1 
ATOM   2491 N  NZ  . LYS C 1 40  ? 52.430 75.824 44.234 1.00 58.40  ? 40  LYS C NZ  1 
ATOM   2492 N  N   . THR C 1 41  ? 46.747 72.151 48.422 1.00 31.71  ? 41  THR C N   1 
ATOM   2493 C  CA  . THR C 1 41  ? 45.290 72.186 48.551 1.00 32.40  ? 41  THR C CA  1 
ATOM   2494 C  C   . THR C 1 41  ? 44.738 72.155 49.988 1.00 29.67  ? 41  THR C C   1 
ATOM   2495 O  O   . THR C 1 41  ? 43.592 72.550 50.212 1.00 29.51  ? 41  THR C O   1 
ATOM   2496 C  CB  . THR C 1 41  ? 44.631 71.044 47.751 1.00 35.15  ? 41  THR C CB  1 
ATOM   2497 O  OG1 . THR C 1 41  ? 45.032 69.775 48.279 1.00 35.66  ? 41  THR C OG1 1 
ATOM   2498 C  CG2 . THR C 1 41  ? 45.014 71.133 46.273 1.00 37.21  ? 41  THR C CG2 1 
ATOM   2499 N  N   . TYR C 1 42  ? 45.533 71.681 50.943 1.00 26.87  ? 42  TYR C N   1 
ATOM   2500 C  CA  . TYR C 1 42  ? 45.152 71.748 52.351 1.00 25.24  ? 42  TYR C CA  1 
ATOM   2501 C  C   . TYR C 1 42  ? 45.247 73.158 52.884 1.00 25.93  ? 42  TYR C C   1 
ATOM   2502 O  O   . TYR C 1 42  ? 44.556 73.477 53.843 1.00 27.13  ? 42  TYR C O   1 
ATOM   2503 C  CB  . TYR C 1 42  ? 45.998 70.801 53.204 1.00 23.47  ? 42  TYR C CB  1 
ATOM   2504 C  CG  . TYR C 1 42  ? 45.713 69.373 52.867 1.00 22.14  ? 42  TYR C CG  1 
ATOM   2505 C  CD1 . TYR C 1 42  ? 44.656 68.698 53.455 1.00 21.76  ? 42  TYR C CD1 1 
ATOM   2506 C  CD2 . TYR C 1 42  ? 46.463 68.712 51.927 1.00 22.11  ? 42  TYR C CD2 1 
ATOM   2507 C  CE1 . TYR C 1 42  ? 44.372 67.387 53.135 1.00 22.01  ? 42  TYR C CE1 1 
ATOM   2508 C  CE2 . TYR C 1 42  ? 46.188 67.406 51.587 1.00 23.20  ? 42  TYR C CE2 1 
ATOM   2509 C  CZ  . TYR C 1 42  ? 45.140 66.738 52.191 1.00 23.35  ? 42  TYR C CZ  1 
ATOM   2510 O  OH  . TYR C 1 42  ? 44.877 65.422 51.844 1.00 23.95  ? 42  TYR C OH  1 
ATOM   2511 N  N   . PHE C 1 43  ? 46.094 73.989 52.277 1.00 26.46  ? 43  PHE C N   1 
ATOM   2512 C  CA  . PHE C 1 43  ? 46.229 75.389 52.645 1.00 28.81  ? 43  PHE C CA  1 
ATOM   2513 C  C   . PHE C 1 43  ? 45.638 76.286 51.556 1.00 37.79  ? 43  PHE C C   1 
ATOM   2514 O  O   . PHE C 1 43  ? 46.378 76.890 50.774 1.00 40.46  ? 43  PHE C O   1 
ATOM   2515 C  CB  . PHE C 1 43  ? 47.693 75.746 52.795 1.00 25.52  ? 43  PHE C CB  1 
ATOM   2516 C  CG  . PHE C 1 43  ? 48.434 74.916 53.779 1.00 23.65  ? 43  PHE C CG  1 
ATOM   2517 C  CD1 . PHE C 1 43  ? 48.624 75.362 55.074 1.00 23.39  ? 43  PHE C CD1 1 
ATOM   2518 C  CD2 . PHE C 1 43  ? 48.996 73.715 53.399 1.00 23.16  ? 43  PHE C CD2 1 
ATOM   2519 C  CE1 . PHE C 1 43  ? 49.336 74.610 55.989 1.00 22.31  ? 43  PHE C CE1 1 
ATOM   2520 C  CE2 . PHE C 1 43  ? 49.711 72.954 54.304 1.00 22.81  ? 43  PHE C CE2 1 
ATOM   2521 C  CZ  . PHE C 1 43  ? 49.881 73.404 55.602 1.00 22.57  ? 43  PHE C CZ  1 
ATOM   2522 N  N   . PRO C 1 44  ? 44.304 76.400 51.492 1.00 47.53  ? 44  PRO C N   1 
ATOM   2523 C  CA  . PRO C 1 44  ? 43.711 77.209 50.423 1.00 52.89  ? 44  PRO C CA  1 
ATOM   2524 C  C   . PRO C 1 44  ? 43.861 78.724 50.632 1.00 60.73  ? 44  PRO C C   1 
ATOM   2525 O  O   . PRO C 1 44  ? 43.961 79.475 49.663 1.00 61.44  ? 44  PRO C O   1 
ATOM   2526 C  CB  . PRO C 1 44  ? 42.242 76.819 50.503 1.00 53.16  ? 44  PRO C CB  1 
ATOM   2527 C  CG  . PRO C 1 44  ? 42.026 76.597 51.963 1.00 51.96  ? 44  PRO C CG  1 
ATOM   2528 C  CD  . PRO C 1 44  ? 43.280 75.927 52.441 1.00 48.88  ? 44  PRO C CD  1 
ATOM   2529 N  N   . HIS C 1 45  ? 43.905 79.144 51.892 1.00 72.92  ? 45  HIS C N   1 
ATOM   2530 C  CA  . HIS C 1 45  ? 43.797 80.550 52.273 1.00 86.86  ? 45  HIS C CA  1 
ATOM   2531 C  C   . HIS C 1 45  ? 45.154 81.202 52.584 1.00 84.70  ? 45  HIS C C   1 
ATOM   2532 O  O   . HIS C 1 45  ? 45.218 82.413 52.803 1.00 86.74  ? 45  HIS C O   1 
ATOM   2533 C  CB  . HIS C 1 45  ? 42.850 80.687 53.476 1.00 102.83 ? 45  HIS C CB  1 
ATOM   2534 C  CG  . HIS C 1 45  ? 43.315 79.956 54.697 1.00 118.32 ? 45  HIS C CG  1 
ATOM   2535 N  ND1 . HIS C 1 45  ? 43.056 78.618 54.907 1.00 125.51 ? 45  HIS C ND1 1 
ATOM   2536 C  CD2 . HIS C 1 45  ? 44.039 80.371 55.764 1.00 129.92 ? 45  HIS C CD2 1 
ATOM   2537 C  CE1 . HIS C 1 45  ? 43.598 78.241 56.051 1.00 134.29 ? 45  HIS C CE1 1 
ATOM   2538 N  NE2 . HIS C 1 45  ? 44.199 79.286 56.592 1.00 135.00 ? 45  HIS C NE2 1 
ATOM   2539 N  N   . PHE C 1 46  ? 46.226 80.412 52.614 1.00 80.95  ? 46  PHE C N   1 
ATOM   2540 C  CA  . PHE C 1 46  ? 47.570 80.949 52.808 1.00 82.37  ? 46  PHE C CA  1 
ATOM   2541 C  C   . PHE C 1 46  ? 48.052 81.623 51.532 1.00 97.15  ? 46  PHE C C   1 
ATOM   2542 O  O   . PHE C 1 46  ? 47.552 81.349 50.437 1.00 99.77  ? 46  PHE C O   1 
ATOM   2543 C  CB  . PHE C 1 46  ? 48.563 79.837 53.180 1.00 77.43  ? 46  PHE C CB  1 
ATOM   2544 C  CG  . PHE C 1 46  ? 48.607 79.488 54.651 1.00 71.96  ? 46  PHE C CG  1 
ATOM   2545 C  CD1 . PHE C 1 46  ? 47.536 79.753 55.512 1.00 69.52  ? 46  PHE C CD1 1 
ATOM   2546 C  CD2 . PHE C 1 46  ? 49.736 78.843 55.171 1.00 66.50  ? 46  PHE C CD2 1 
ATOM   2547 C  CE1 . PHE C 1 46  ? 47.605 79.402 56.854 1.00 67.81  ? 46  PHE C CE1 1 
ATOM   2548 C  CE2 . PHE C 1 46  ? 49.807 78.492 56.512 1.00 63.99  ? 46  PHE C CE2 1 
ATOM   2549 C  CZ  . PHE C 1 46  ? 48.740 78.769 57.354 1.00 65.83  ? 46  PHE C CZ  1 
ATOM   2550 N  N   . ASP C 1 47  ? 49.043 82.495 51.700 1.00 115.45 ? 47  ASP C N   1 
ATOM   2551 C  CA  . ASP C 1 47  ? 49.762 83.128 50.587 1.00 124.88 ? 47  ASP C CA  1 
ATOM   2552 C  C   . ASP C 1 47  ? 51.076 82.374 50.382 1.00 107.53 ? 47  ASP C C   1 
ATOM   2553 O  O   . ASP C 1 47  ? 52.074 82.644 51.051 1.00 101.34 ? 47  ASP C O   1 
ATOM   2554 C  CB  . ASP C 1 47  ? 49.992 84.642 50.823 1.00 148.59 ? 47  ASP C CB  1 
ATOM   2555 C  CG  . ASP C 1 47  ? 50.452 84.985 52.253 1.00 165.85 ? 47  ASP C CG  1 
ATOM   2556 O  OD1 . ASP C 1 47  ? 50.462 84.093 53.129 1.00 170.39 ? 47  ASP C OD1 1 
ATOM   2557 O  OD2 . ASP C 1 47  ? 50.797 86.161 52.498 1.00 178.14 ? 47  ASP C OD2 1 
ATOM   2558 N  N   . LEU C 1 48  ? 51.068 81.424 49.453 1.00 98.32  ? 48  LEU C N   1 
ATOM   2559 C  CA  . LEU C 1 48  ? 52.180 80.492 49.294 1.00 99.82  ? 48  LEU C CA  1 
ATOM   2560 C  C   . LEU C 1 48  ? 53.200 80.964 48.263 1.00 108.88 ? 48  LEU C C   1 
ATOM   2561 O  O   . LEU C 1 48  ? 53.619 80.196 47.391 1.00 112.99 ? 48  LEU C O   1 
ATOM   2562 C  CB  . LEU C 1 48  ? 51.646 79.117 48.909 1.00 98.00  ? 48  LEU C CB  1 
ATOM   2563 C  CG  . LEU C 1 48  ? 50.625 78.510 49.862 1.00 95.78  ? 48  LEU C CG  1 
ATOM   2564 C  CD1 . LEU C 1 48  ? 50.138 77.207 49.261 1.00 98.46  ? 48  LEU C CD1 1 
ATOM   2565 C  CD2 . LEU C 1 48  ? 51.221 78.281 51.244 1.00 92.55  ? 48  LEU C CD2 1 
ATOM   2566 N  N   . SER C 1 49  ? 53.609 82.226 48.378 1.00 118.83 ? 49  SER C N   1 
ATOM   2567 C  CA  . SER C 1 49  ? 54.679 82.781 47.557 1.00 126.53 ? 49  SER C CA  1 
ATOM   2568 C  C   . SER C 1 49  ? 56.011 82.548 48.270 1.00 130.79 ? 49  SER C C   1 
ATOM   2569 O  O   . SER C 1 49  ? 56.061 81.886 49.313 1.00 130.47 ? 49  SER C O   1 
ATOM   2570 C  CB  . SER C 1 49  ? 54.434 84.276 47.313 1.00 127.50 ? 49  SER C CB  1 
ATOM   2571 O  OG  . SER C 1 49  ? 54.556 85.033 48.507 1.00 124.38 ? 49  SER C OG  1 
ATOM   2572 N  N   . HIS C 1 50  ? 57.088 83.079 47.703 1.00 138.98 ? 50  HIS C N   1 
ATOM   2573 C  CA  . HIS C 1 50  ? 58.397 83.008 48.338 1.00 147.43 ? 50  HIS C CA  1 
ATOM   2574 C  C   . HIS C 1 50  ? 58.507 84.035 49.470 1.00 145.70 ? 50  HIS C C   1 
ATOM   2575 O  O   . HIS C 1 50  ? 58.343 85.238 49.247 1.00 142.49 ? 50  HIS C O   1 
ATOM   2576 C  CB  . HIS C 1 50  ? 59.496 83.242 47.302 1.00 160.03 ? 50  HIS C CB  1 
ATOM   2577 C  CG  . HIS C 1 50  ? 60.879 83.068 47.843 1.00 168.79 ? 50  HIS C CG  1 
ATOM   2578 N  ND1 . HIS C 1 50  ? 61.392 81.837 48.190 1.00 171.36 ? 50  HIS C ND1 1 
ATOM   2579 C  CD2 . HIS C 1 50  ? 61.856 83.969 48.100 1.00 180.22 ? 50  HIS C CD2 1 
ATOM   2580 C  CE1 . HIS C 1 50  ? 62.626 81.987 48.637 1.00 176.60 ? 50  HIS C CE1 1 
ATOM   2581 N  NE2 . HIS C 1 50  ? 62.932 83.271 48.592 1.00 181.61 ? 50  HIS C NE2 1 
ATOM   2582 N  N   . GLY C 1 51  ? 58.905 83.560 50.650 1.00 142.86 ? 51  GLY C N   1 
ATOM   2583 C  CA  . GLY C 1 51  ? 59.091 84.394 51.831 1.00 142.46 ? 51  GLY C CA  1 
ATOM   2584 C  C   . GLY C 1 51  ? 57.918 85.044 52.548 1.00 136.71 ? 51  GLY C C   1 
ATOM   2585 O  O   . GLY C 1 51  ? 58.068 86.126 53.112 1.00 146.50 ? 51  GLY C O   1 
ATOM   2586 N  N   . SER C 1 52  ? 56.758 84.397 52.534 1.00 125.18 ? 52  SER C N   1 
ATOM   2587 C  CA  . SER C 1 52  ? 55.563 84.925 53.195 1.00 119.89 ? 52  SER C CA  1 
ATOM   2588 C  C   . SER C 1 52  ? 55.677 84.772 54.697 1.00 109.75 ? 52  SER C C   1 
ATOM   2589 O  O   . SER C 1 52  ? 56.204 83.770 55.186 1.00 113.10 ? 52  SER C O   1 
ATOM   2590 C  CB  . SER C 1 52  ? 54.313 84.192 52.722 1.00 128.49 ? 52  SER C CB  1 
ATOM   2591 O  OG  . SER C 1 52  ? 54.149 84.336 51.324 1.00 143.74 ? 52  SER C OG  1 
ATOM   2592 N  N   . ALA C 1 53  ? 55.166 85.760 55.424 1.00 101.55 ? 53  ALA C N   1 
ATOM   2593 C  CA  . ALA C 1 53  ? 55.159 85.721 56.884 1.00 101.07 ? 53  ALA C CA  1 
ATOM   2594 C  C   . ALA C 1 53  ? 54.223 84.644 57.432 1.00 93.67  ? 53  ALA C C   1 
ATOM   2595 O  O   . ALA C 1 53  ? 54.423 84.157 58.547 1.00 96.15  ? 53  ALA C O   1 
ATOM   2596 C  CB  . ALA C 1 53  ? 54.774 87.080 57.444 1.00 110.14 ? 53  ALA C CB  1 
ATOM   2597 N  N   . GLN C 1 54  ? 53.203 84.286 56.652 1.00 84.07  ? 54  GLN C N   1 
ATOM   2598 C  CA  . GLN C 1 54  ? 52.264 83.231 57.022 1.00 77.28  ? 54  GLN C CA  1 
ATOM   2599 C  C   . GLN C 1 54  ? 52.964 81.878 57.138 1.00 66.08  ? 54  GLN C C   1 
ATOM   2600 O  O   . GLN C 1 54  ? 52.839 81.191 58.154 1.00 64.87  ? 54  GLN C O   1 
ATOM   2601 C  CB  . GLN C 1 54  ? 51.137 83.153 55.989 1.00 83.92  ? 54  GLN C CB  1 
ATOM   2602 C  CG  . GLN C 1 54  ? 49.931 82.336 56.416 1.00 94.63  ? 54  GLN C CG  1 
ATOM   2603 C  CD  . GLN C 1 54  ? 49.144 82.996 57.529 1.00 105.52 ? 54  GLN C CD  1 
ATOM   2604 O  OE1 . GLN C 1 54  ? 49.339 82.695 58.709 1.00 119.97 ? 54  GLN C OE1 1 
ATOM   2605 N  NE2 . GLN C 1 54  ? 48.259 83.914 57.161 1.00 110.00 ? 54  GLN C NE2 1 
ATOM   2606 N  N   . VAL C 1 55  ? 53.711 81.519 56.100 1.00 56.89  ? 55  VAL C N   1 
ATOM   2607 C  CA  . VAL C 1 55  ? 54.433 80.257 56.070 1.00 52.87  ? 55  VAL C CA  1 
ATOM   2608 C  C   . VAL C 1 55  ? 55.520 80.239 57.125 1.00 57.36  ? 55  VAL C C   1 
ATOM   2609 O  O   . VAL C 1 55  ? 55.624 79.274 57.879 1.00 61.48  ? 55  VAL C O   1 
ATOM   2610 C  CB  . VAL C 1 55  ? 55.026 79.977 54.679 1.00 49.86  ? 55  VAL C CB  1 
ATOM   2611 C  CG1 . VAL C 1 55  ? 55.995 78.798 54.695 1.00 47.96  ? 55  VAL C CG1 1 
ATOM   2612 C  CG2 . VAL C 1 55  ? 53.897 79.703 53.699 1.00 50.91  ? 55  VAL C CG2 1 
ATOM   2613 N  N   . LYS C 1 56  ? 56.321 81.296 57.190 1.00 64.94  ? 56  LYS C N   1 
ATOM   2614 C  CA  . LYS C 1 56  ? 57.389 81.375 58.198 1.00 74.65  ? 56  LYS C CA  1 
ATOM   2615 C  C   . LYS C 1 56  ? 56.871 81.223 59.630 1.00 67.66  ? 56  LYS C C   1 
ATOM   2616 O  O   . LYS C 1 56  ? 57.552 80.648 60.484 1.00 62.54  ? 56  LYS C O   1 
ATOM   2617 C  CB  . LYS C 1 56  ? 58.177 82.679 58.061 1.00 89.93  ? 56  LYS C CB  1 
ATOM   2618 C  CG  . LYS C 1 56  ? 59.050 82.721 56.816 1.00 107.55 ? 56  LYS C CG  1 
ATOM   2619 C  CD  . LYS C 1 56  ? 59.870 84.003 56.731 1.00 124.76 ? 56  LYS C CD  1 
ATOM   2620 C  CE  . LYS C 1 56  ? 61.086 83.987 57.652 1.00 136.80 ? 56  LYS C CE  1 
ATOM   2621 N  NZ  . LYS C 1 56  ? 62.083 82.928 57.311 1.00 138.74 ? 56  LYS C NZ  1 
ATOM   2622 N  N   . GLY C 1 57  ? 55.667 81.741 59.871 1.00 66.75  ? 57  GLY C N   1 
ATOM   2623 C  CA  . GLY C 1 57  ? 54.996 81.615 61.158 1.00 65.54  ? 57  GLY C CA  1 
ATOM   2624 C  C   . GLY C 1 57  ? 54.538 80.199 61.412 1.00 62.17  ? 57  GLY C C   1 
ATOM   2625 O  O   . GLY C 1 57  ? 54.758 79.657 62.497 1.00 67.62  ? 57  GLY C O   1 
ATOM   2626 N  N   . HIS C 1 58  ? 53.912 79.596 60.406 1.00 53.25  ? 58  HIS C N   1 
ATOM   2627 C  CA  . HIS C 1 58  ? 53.427 78.221 60.520 1.00 47.10  ? 58  HIS C CA  1 
ATOM   2628 C  C   . HIS C 1 58  ? 54.548 77.232 60.851 1.00 41.68  ? 58  HIS C C   1 
ATOM   2629 O  O   . HIS C 1 58  ? 54.395 76.377 61.723 1.00 39.53  ? 58  HIS C O   1 
ATOM   2630 C  CB  . HIS C 1 58  ? 52.732 77.797 59.235 1.00 45.11  ? 58  HIS C CB  1 
ATOM   2631 C  CG  . HIS C 1 58  ? 52.020 76.498 59.361 1.00 44.75  ? 58  HIS C CG  1 
ATOM   2632 N  ND1 . HIS C 1 58  ? 52.630 75.290 59.112 1.00 44.07  ? 58  HIS C ND1 1 
ATOM   2633 C  CD2 . HIS C 1 58  ? 50.759 76.212 59.753 1.00 47.86  ? 58  HIS C CD2 1 
ATOM   2634 C  CE1 . HIS C 1 58  ? 51.768 74.313 59.323 1.00 46.18  ? 58  HIS C CE1 1 
ATOM   2635 N  NE2 . HIS C 1 58  ? 50.624 74.846 59.716 1.00 48.38  ? 58  HIS C NE2 1 
ATOM   2636 N  N   . GLY C 1 59  ? 55.667 77.375 60.149 1.00 37.07  ? 59  GLY C N   1 
ATOM   2637 C  CA  . GLY C 1 59  ? 56.832 76.552 60.368 1.00 35.29  ? 59  GLY C CA  1 
ATOM   2638 C  C   . GLY C 1 59  ? 57.350 76.620 61.785 1.00 35.66  ? 59  GLY C C   1 
ATOM   2639 O  O   . GLY C 1 59  ? 57.907 75.647 62.286 1.00 36.70  ? 59  GLY C O   1 
ATOM   2640 N  N   . LYS C 1 60  ? 57.190 77.764 62.433 1.00 38.74  ? 60  LYS C N   1 
ATOM   2641 C  CA  . LYS C 1 60  ? 57.581 77.888 63.821 1.00 43.34  ? 60  LYS C CA  1 
ATOM   2642 C  C   . LYS C 1 60  ? 56.765 76.935 64.646 1.00 39.86  ? 60  LYS C C   1 
ATOM   2643 O  O   . LYS C 1 60  ? 57.316 76.202 65.463 1.00 39.22  ? 60  LYS C O   1 
ATOM   2644 C  CB  . LYS C 1 60  ? 57.370 79.314 64.322 1.00 55.72  ? 60  LYS C CB  1 
ATOM   2645 C  CG  . LYS C 1 60  ? 57.864 79.589 65.734 1.00 67.69  ? 60  LYS C CG  1 
ATOM   2646 C  CD  . LYS C 1 60  ? 59.337 79.243 65.908 1.00 79.87  ? 60  LYS C CD  1 
ATOM   2647 C  CE  . LYS C 1 60  ? 59.925 79.869 67.168 1.00 94.19  ? 60  LYS C CE  1 
ATOM   2648 N  NZ  . LYS C 1 60  ? 59.434 79.251 68.437 1.00 99.06  ? 60  LYS C NZ  1 
ATOM   2649 N  N   . LYS C 1 61  ? 55.455 76.933 64.411 1.00 38.98  ? 61  LYS C N   1 
ATOM   2650 C  CA  . LYS C 1 61  ? 54.535 76.099 65.184 1.00 39.25  ? 61  LYS C CA  1 
ATOM   2651 C  C   . LYS C 1 61  ? 54.843 74.604 65.052 1.00 33.05  ? 61  LYS C C   1 
ATOM   2652 O  O   . LYS C 1 61  ? 55.058 73.924 66.063 1.00 31.31  ? 61  LYS C O   1 
ATOM   2653 C  CB  . LYS C 1 61  ? 53.086 76.401 64.803 1.00 46.20  ? 61  LYS C CB  1 
ATOM   2654 C  CG  . LYS C 1 61  ? 52.620 77.767 65.272 1.00 54.49  ? 61  LYS C CG  1 
ATOM   2655 C  CD  . LYS C 1 61  ? 51.192 78.046 64.838 1.00 63.53  ? 61  LYS C CD  1 
ATOM   2656 C  CE  . LYS C 1 61  ? 50.807 79.506 65.029 1.00 76.80  ? 61  LYS C CE  1 
ATOM   2657 N  NZ  . LYS C 1 61  ? 51.552 80.457 64.147 1.00 81.67  ? 61  LYS C NZ  1 
ATOM   2658 N  N   . VAL C 1 62  ? 54.903 74.125 63.808 1.00 26.85  ? 62  VAL C N   1 
ATOM   2659 C  CA  . VAL C 1 62  ? 55.279 72.741 63.505 1.00 23.01  ? 62  VAL C CA  1 
ATOM   2660 C  C   . VAL C 1 62  ? 56.538 72.368 64.238 1.00 24.06  ? 62  VAL C C   1 
ATOM   2661 O  O   . VAL C 1 62  ? 56.569 71.397 64.978 1.00 24.45  ? 62  VAL C O   1 
ATOM   2662 C  CB  . VAL C 1 62  ? 55.576 72.532 62.022 1.00 20.69  ? 62  VAL C CB  1 
ATOM   2663 C  CG1 . VAL C 1 62  ? 56.161 71.152 61.763 1.00 20.12  ? 62  VAL C CG1 1 
ATOM   2664 C  CG2 . VAL C 1 62  ? 54.320 72.714 61.215 1.00 21.55  ? 62  VAL C CG2 1 
ATOM   2665 N  N   . ALA C 1 63  ? 57.584 73.146 64.030 1.00 26.78  ? 63  ALA C N   1 
ATOM   2666 C  CA  . ALA C 1 63  ? 58.857 72.844 64.642 1.00 30.39  ? 63  ALA C CA  1 
ATOM   2667 C  C   . ALA C 1 63  ? 58.757 72.762 66.167 1.00 34.54  ? 63  ALA C C   1 
ATOM   2668 O  O   . ALA C 1 63  ? 59.432 71.943 66.783 1.00 34.59  ? 63  ALA C O   1 
ATOM   2669 C  CB  . ALA C 1 63  ? 59.895 73.863 64.226 1.00 30.44  ? 63  ALA C CB  1 
ATOM   2670 N  N   . ASP C 1 64  ? 57.909 73.586 66.769 1.00 41.62  ? 64  ASP C N   1 
ATOM   2671 C  CA  . ASP C 1 64  ? 57.709 73.520 68.208 1.00 51.40  ? 64  ASP C CA  1 
ATOM   2672 C  C   . ASP C 1 64  ? 56.925 72.299 68.663 1.00 48.91  ? 64  ASP C C   1 
ATOM   2673 O  O   . ASP C 1 64  ? 57.273 71.693 69.683 1.00 49.80  ? 64  ASP C O   1 
ATOM   2674 C  CB  . ASP C 1 64  ? 57.056 74.799 68.714 1.00 69.11  ? 64  ASP C CB  1 
ATOM   2675 C  CG  . ASP C 1 64  ? 58.016 75.997 68.685 1.00 91.40  ? 64  ASP C CG  1 
ATOM   2676 O  OD1 . ASP C 1 64  ? 59.229 75.819 68.391 1.00 95.78  ? 64  ASP C OD1 1 
ATOM   2677 O  OD2 . ASP C 1 64  ? 57.554 77.128 68.969 1.00 107.05 ? 64  ASP C OD2 1 
ATOM   2678 N  N   . ALA C 1 65  ? 55.891 71.925 67.910 1.00 43.25  ? 65  ALA C N   1 
ATOM   2679 C  CA  . ALA C 1 65  ? 55.131 70.694 68.192 1.00 37.73  ? 65  ALA C CA  1 
ATOM   2680 C  C   . ALA C 1 65  ? 56.011 69.450 68.164 1.00 32.50  ? 65  ALA C C   1 
ATOM   2681 O  O   . ALA C 1 65  ? 55.827 68.551 68.971 1.00 31.40  ? 65  ALA C O   1 
ATOM   2682 C  CB  . ALA C 1 65  ? 53.985 70.535 67.206 1.00 37.52  ? 65  ALA C CB  1 
ATOM   2683 N  N   . LEU C 1 66  ? 56.944 69.405 67.219 1.00 29.91  ? 66  LEU C N   1 
ATOM   2684 C  CA  . LEU C 1 66  ? 57.922 68.335 67.160 1.00 30.24  ? 66  LEU C CA  1 
ATOM   2685 C  C   . LEU C 1 66  ? 58.893 68.356 68.332 1.00 35.52  ? 66  LEU C C   1 
ATOM   2686 O  O   . LEU C 1 66  ? 59.359 67.295 68.758 1.00 36.13  ? 66  LEU C O   1 
ATOM   2687 C  CB  . LEU C 1 66  ? 58.745 68.425 65.894 1.00 28.08  ? 66  LEU C CB  1 
ATOM   2688 C  CG  . LEU C 1 66  ? 58.092 67.971 64.614 1.00 26.38  ? 66  LEU C CG  1 
ATOM   2689 C  CD1 . LEU C 1 66  ? 58.994 68.366 63.462 1.00 25.69  ? 66  LEU C CD1 1 
ATOM   2690 C  CD2 . LEU C 1 66  ? 57.860 66.470 64.640 1.00 26.72  ? 66  LEU C CD2 1 
ATOM   2691 N  N   . THR C 1 67  ? 59.235 69.550 68.824 1.00 40.34  ? 67  THR C N   1 
ATOM   2692 C  CA  . THR C 1 67  ? 60.097 69.678 70.011 1.00 43.12  ? 67  THR C CA  1 
ATOM   2693 C  C   . THR C 1 67  ? 59.416 69.094 71.245 1.00 45.03  ? 67  THR C C   1 
ATOM   2694 O  O   . THR C 1 67  ? 60.032 68.335 72.006 1.00 44.94  ? 67  THR C O   1 
ATOM   2695 C  CB  . THR C 1 67  ? 60.483 71.138 70.306 1.00 43.70  ? 67  THR C CB  1 
ATOM   2696 O  OG1 . THR C 1 67  ? 60.796 71.816 69.084 1.00 45.09  ? 67  THR C OG1 1 
ATOM   2697 C  CG2 . THR C 1 67  ? 61.697 71.184 71.223 1.00 45.27  ? 67  THR C CG2 1 
ATOM   2698 N  N   . ASN C 1 68  ? 58.143 69.450 71.420 1.00 45.65  ? 68  ASN C N   1 
ATOM   2699 C  CA  . ASN C 1 68  ? 57.303 68.855 72.453 1.00 47.06  ? 68  ASN C CA  1 
ATOM   2700 C  C   . ASN C 1 68  ? 57.246 67.325 72.354 1.00 43.80  ? 68  ASN C C   1 
ATOM   2701 O  O   . ASN C 1 68  ? 57.390 66.637 73.359 1.00 45.26  ? 68  ASN C O   1 
ATOM   2702 C  CB  . ASN C 1 68  ? 55.886 69.424 72.386 1.00 51.68  ? 68  ASN C CB  1 
ATOM   2703 C  CG  . ASN C 1 68  ? 55.014 68.957 73.537 1.00 57.81  ? 68  ASN C CG  1 
ATOM   2704 O  OD1 . ASN C 1 68  ? 55.483 68.800 74.669 1.00 61.43  ? 68  ASN C OD1 1 
ATOM   2705 N  ND2 . ASN C 1 68  ? 53.731 68.735 73.254 1.00 64.11  ? 68  ASN C ND2 1 
ATOM   2706 N  N   . ALA C 1 69  ? 57.042 66.800 71.151 1.00 40.57  ? 69  ALA C N   1 
ATOM   2707 C  CA  . ALA C 1 69  ? 57.001 65.353 70.952 1.00 38.74  ? 69  ALA C CA  1 
ATOM   2708 C  C   . ALA C 1 69  ? 58.265 64.691 71.439 1.00 39.50  ? 69  ALA C C   1 
ATOM   2709 O  O   . ALA C 1 69  ? 58.188 63.644 72.074 1.00 42.35  ? 69  ALA C O   1 
ATOM   2710 C  CB  . ALA C 1 69  ? 56.779 65.001 69.492 1.00 38.29  ? 69  ALA C CB  1 
ATOM   2711 N  N   . VAL C 1 70  ? 59.422 65.288 71.155 1.00 40.56  ? 70  VAL C N   1 
ATOM   2712 C  CA  . VAL C 1 70  ? 60.700 64.681 71.548 1.00 43.08  ? 70  VAL C CA  1 
ATOM   2713 C  C   . VAL C 1 70  ? 60.873 64.662 73.066 1.00 47.78  ? 70  VAL C C   1 
ATOM   2714 O  O   . VAL C 1 70  ? 61.496 63.742 73.605 1.00 46.24  ? 70  VAL C O   1 
ATOM   2715 C  CB  . VAL C 1 70  ? 61.902 65.350 70.857 1.00 41.17  ? 70  VAL C CB  1 
ATOM   2716 C  CG1 . VAL C 1 70  ? 63.225 64.812 71.389 1.00 41.33  ? 70  VAL C CG1 1 
ATOM   2717 C  CG2 . VAL C 1 70  ? 61.844 65.084 69.368 1.00 41.62  ? 70  VAL C CG2 1 
ATOM   2718 N  N   . ALA C 1 71  ? 60.309 65.663 73.743 1.00 53.94  ? 71  ALA C N   1 
ATOM   2719 C  CA  . ALA C 1 71  ? 60.294 65.706 75.212 1.00 59.65  ? 71  ALA C CA  1 
ATOM   2720 C  C   . ALA C 1 71  ? 59.603 64.492 75.846 1.00 61.45  ? 71  ALA C C   1 
ATOM   2721 O  O   . ALA C 1 71  ? 60.113 63.929 76.817 1.00 63.45  ? 71  ALA C O   1 
ATOM   2722 C  CB  . ALA C 1 71  ? 59.632 66.989 75.702 1.00 62.00  ? 71  ALA C CB  1 
ATOM   2723 N  N   . HIS C 1 72  ? 58.456 64.103 75.290 1.00 62.68  ? 72  HIS C N   1 
ATOM   2724 C  CA  . HIS C 1 72  ? 57.668 62.974 75.789 1.00 63.39  ? 72  HIS C CA  1 
ATOM   2725 C  C   . HIS C 1 72  ? 57.722 61.800 74.805 1.00 57.80  ? 72  HIS C C   1 
ATOM   2726 O  O   . HIS C 1 72  ? 56.686 61.219 74.476 1.00 56.79  ? 72  HIS C O   1 
ATOM   2727 C  CB  . HIS C 1 72  ? 56.193 63.389 75.992 1.00 69.96  ? 72  HIS C CB  1 
ATOM   2728 C  CG  . HIS C 1 72  ? 56.002 64.665 76.750 1.00 76.04  ? 72  HIS C CG  1 
ATOM   2729 N  ND1 . HIS C 1 72  ? 56.188 64.756 78.112 1.00 88.25  ? 72  HIS C ND1 1 
ATOM   2730 C  CD2 . HIS C 1 72  ? 55.604 65.893 76.341 1.00 77.87  ? 72  HIS C CD2 1 
ATOM   2731 C  CE1 . HIS C 1 72  ? 55.934 65.992 78.507 1.00 93.22  ? 72  HIS C CE1 1 
ATOM   2732 N  NE2 . HIS C 1 72  ? 55.578 66.702 77.451 1.00 86.37  ? 72  HIS C NE2 1 
ATOM   2733 N  N   . VAL C 1 73  ? 58.911 61.416 74.353 1.00 57.36  ? 73  VAL C N   1 
ATOM   2734 C  CA  . VAL C 1 73  ? 59.017 60.362 73.325 1.00 63.04  ? 73  VAL C CA  1 
ATOM   2735 C  C   . VAL C 1 73  ? 58.508 58.976 73.786 1.00 69.68  ? 73  VAL C C   1 
ATOM   2736 O  O   . VAL C 1 73  ? 58.378 58.058 72.976 1.00 64.98  ? 73  VAL C O   1 
ATOM   2737 C  CB  . VAL C 1 73  ? 60.462 60.262 72.766 1.00 65.12  ? 73  VAL C CB  1 
ATOM   2738 C  CG1 . VAL C 1 73  ? 61.376 59.474 73.700 1.00 70.12  ? 73  VAL C CG1 1 
ATOM   2739 C  CG2 . VAL C 1 73  ? 60.482 59.656 71.370 1.00 64.56  ? 73  VAL C CG2 1 
ATOM   2740 N  N   . ASP C 1 74  ? 58.217 58.843 75.082 1.00 87.23  ? 74  ASP C N   1 
ATOM   2741 C  CA  . ASP C 1 74  ? 57.749 57.594 75.685 1.00 100.25 ? 74  ASP C CA  1 
ATOM   2742 C  C   . ASP C 1 74  ? 56.215 57.474 75.767 1.00 95.67  ? 74  ASP C C   1 
ATOM   2743 O  O   . ASP C 1 74  ? 55.679 56.372 75.637 1.00 94.41  ? 74  ASP C O   1 
ATOM   2744 C  CB  . ASP C 1 74  ? 58.357 57.457 77.090 1.00 118.29 ? 74  ASP C CB  1 
ATOM   2745 C  CG  . ASP C 1 74  ? 59.884 57.625 77.099 1.00 130.22 ? 74  ASP C CG  1 
ATOM   2746 O  OD1 . ASP C 1 74  ? 60.552 57.168 76.144 1.00 134.72 ? 74  ASP C OD1 1 
ATOM   2747 O  OD2 . ASP C 1 74  ? 60.413 58.215 78.067 1.00 137.43 ? 74  ASP C OD2 1 
ATOM   2748 N  N   . ASP C 1 75  ? 55.523 58.593 75.992 1.00 96.55  ? 75  ASP C N   1 
ATOM   2749 C  CA  . ASP C 1 75  ? 54.057 58.621 76.114 1.00 101.23 ? 75  ASP C CA  1 
ATOM   2750 C  C   . ASP C 1 75  ? 53.463 59.644 75.131 1.00 90.07  ? 75  ASP C C   1 
ATOM   2751 O  O   . ASP C 1 75  ? 52.847 60.650 75.510 1.00 90.29  ? 75  ASP C O   1 
ATOM   2752 C  CB  . ASP C 1 75  ? 53.665 58.938 77.561 1.00 124.47 ? 75  ASP C CB  1 
ATOM   2753 C  CG  . ASP C 1 75  ? 52.164 58.842 77.801 1.00 143.91 ? 75  ASP C CG  1 
ATOM   2754 O  OD1 . ASP C 1 75  ? 51.569 57.790 77.476 1.00 156.46 ? 75  ASP C OD1 1 
ATOM   2755 O  OD2 . ASP C 1 75  ? 51.584 59.824 78.316 1.00 154.55 ? 75  ASP C OD2 1 
ATOM   2756 N  N   . MET C 1 76  ? 53.645 59.348 73.854 1.00 75.86  ? 76  MET C N   1 
ATOM   2757 C  CA  . MET C 1 76  ? 53.420 60.317 72.791 1.00 65.90  ? 76  MET C CA  1 
ATOM   2758 C  C   . MET C 1 76  ? 51.953 60.599 72.452 1.00 57.14  ? 76  MET C C   1 
ATOM   2759 O  O   . MET C 1 76  ? 51.625 61.742 72.154 1.00 56.92  ? 76  MET C O   1 
ATOM   2760 C  CB  . MET C 1 76  ? 54.180 59.876 71.544 1.00 68.38  ? 76  MET C CB  1 
ATOM   2761 C  CG  . MET C 1 76  ? 54.492 60.987 70.568 1.00 71.83  ? 76  MET C CG  1 
ATOM   2762 S  SD  . MET C 1 76  ? 55.375 60.292 69.157 1.00 77.89  ? 76  MET C SD  1 
ATOM   2763 C  CE  . MET C 1 76  ? 57.008 60.100 69.863 1.00 76.73  ? 76  MET C CE  1 
ATOM   2764 N  N   . PRO C 1 77  ? 51.079 59.570 72.461 1.00 54.01  ? 77  PRO C N   1 
ATOM   2765 C  CA  . PRO C 1 77  ? 49.655 59.779 72.171 1.00 55.13  ? 77  PRO C CA  1 
ATOM   2766 C  C   . PRO C 1 77  ? 48.888 60.705 73.098 1.00 62.27  ? 77  PRO C C   1 
ATOM   2767 O  O   . PRO C 1 77  ? 47.866 61.252 72.686 1.00 65.70  ? 77  PRO C O   1 
ATOM   2768 C  CB  . PRO C 1 77  ? 49.073 58.379 72.279 1.00 52.20  ? 77  PRO C CB  1 
ATOM   2769 C  CG  . PRO C 1 77  ? 50.178 57.529 71.806 1.00 53.59  ? 77  PRO C CG  1 
ATOM   2770 C  CD  . PRO C 1 77  ? 51.396 58.133 72.433 1.00 54.53  ? 77  PRO C CD  1 
ATOM   2771 N  N   . ASN C 1 78  ? 49.345 60.879 74.330 1.00 70.18  ? 78  ASN C N   1 
ATOM   2772 C  CA  . ASN C 1 78  ? 48.717 61.860 75.208 1.00 79.50  ? 78  ASN C CA  1 
ATOM   2773 C  C   . ASN C 1 78  ? 49.177 63.275 74.867 1.00 76.14  ? 78  ASN C C   1 
ATOM   2774 O  O   . ASN C 1 78  ? 48.348 64.185 74.739 1.00 73.71  ? 78  ASN C O   1 
ATOM   2775 C  CB  . ASN C 1 78  ? 48.981 61.517 76.670 1.00 93.04  ? 78  ASN C CB  1 
ATOM   2776 C  CG  . ASN C 1 78  ? 48.255 60.255 77.101 1.00 106.40 ? 78  ASN C CG  1 
ATOM   2777 O  OD1 . ASN C 1 78  ? 47.076 60.062 76.790 1.00 111.72 ? 78  ASN C OD1 1 
ATOM   2778 N  ND2 . ASN C 1 78  ? 48.955 59.387 77.819 1.00 119.43 ? 78  ASN C ND2 1 
ATOM   2779 N  N   . ALA C 1 79  ? 50.491 63.448 74.708 1.00 67.46  ? 79  ALA C N   1 
ATOM   2780 C  CA  . ALA C 1 79  ? 51.085 64.750 74.371 1.00 60.95  ? 79  ALA C CA  1 
ATOM   2781 C  C   . ALA C 1 79  ? 50.493 65.356 73.104 1.00 53.13  ? 79  ALA C C   1 
ATOM   2782 O  O   . ALA C 1 79  ? 50.065 66.505 73.105 1.00 54.67  ? 79  ALA C O   1 
ATOM   2783 C  CB  . ALA C 1 79  ? 52.595 64.624 74.228 1.00 62.23  ? 79  ALA C CB  1 
ATOM   2784 N  N   . LEU C 1 80  ? 50.441 64.559 72.042 1.00 47.69  ? 80  LEU C N   1 
ATOM   2785 C  CA  . LEU C 1 80  ? 49.970 65.006 70.730 1.00 44.21  ? 80  LEU C CA  1 
ATOM   2786 C  C   . LEU C 1 80  ? 48.449 64.870 70.513 1.00 44.13  ? 80  LEU C C   1 
ATOM   2787 O  O   . LEU C 1 80  ? 47.991 64.740 69.375 1.00 44.34  ? 80  LEU C O   1 
ATOM   2788 C  CB  . LEU C 1 80  ? 50.713 64.217 69.644 1.00 41.20  ? 80  LEU C CB  1 
ATOM   2789 C  CG  . LEU C 1 80  ? 52.222 64.357 69.553 1.00 39.24  ? 80  LEU C CG  1 
ATOM   2790 C  CD1 . LEU C 1 80  ? 52.716 63.495 68.406 1.00 37.66  ? 80  LEU C CD1 1 
ATOM   2791 C  CD2 . LEU C 1 80  ? 52.606 65.812 69.329 1.00 39.57  ? 80  LEU C CD2 1 
ATOM   2792 N  N   . SER C 1 81  ? 47.658 64.938 71.582 1.00 44.32  ? 81  SER C N   1 
ATOM   2793 C  CA  . SER C 1 81  ? 46.234 64.602 71.488 1.00 43.47  ? 81  SER C CA  1 
ATOM   2794 C  C   . SER C 1 81  ? 45.399 65.683 70.816 1.00 41.15  ? 81  SER C C   1 
ATOM   2795 O  O   . SER C 1 81  ? 44.430 65.363 70.141 1.00 40.50  ? 81  SER C O   1 
ATOM   2796 C  CB  . SER C 1 81  ? 45.675 64.286 72.859 1.00 45.40  ? 81  SER C CB  1 
ATOM   2797 N  N   . ALA C 1 82  ? 45.765 66.947 71.004 1.00 39.95  ? 82  ALA C N   1 
ATOM   2798 C  CA  . ALA C 1 82  ? 45.082 68.058 70.326 1.00 41.11  ? 82  ALA C CA  1 
ATOM   2799 C  C   . ALA C 1 82  ? 45.382 68.120 68.836 1.00 36.76  ? 82  ALA C C   1 
ATOM   2800 O  O   . ALA C 1 82  ? 44.546 68.589 68.053 1.00 34.48  ? 82  ALA C O   1 
ATOM   2801 C  CB  . ALA C 1 82  ? 45.467 69.385 70.960 1.00 46.12  ? 82  ALA C CB  1 
ATOM   2802 N  N   . LEU C 1 83  ? 46.586 67.691 68.463 1.00 32.05  ? 83  LEU C N   1 
ATOM   2803 C  CA  . LEU C 1 83  ? 46.990 67.704 67.071 1.00 29.59  ? 83  LEU C CA  1 
ATOM   2804 C  C   . LEU C 1 83  ? 46.317 66.615 66.305 1.00 28.20  ? 83  LEU C C   1 
ATOM   2805 O  O   . LEU C 1 83  ? 45.846 66.842 65.190 1.00 28.78  ? 83  LEU C O   1 
ATOM   2806 C  CB  . LEU C 1 83  ? 48.489 67.557 66.936 1.00 28.66  ? 83  LEU C CB  1 
ATOM   2807 C  CG  . LEU C 1 83  ? 49.302 68.717 67.472 1.00 28.73  ? 83  LEU C CG  1 
ATOM   2808 C  CD1 . LEU C 1 83  ? 50.742 68.515 67.040 1.00 29.83  ? 83  LEU C CD1 1 
ATOM   2809 C  CD2 . LEU C 1 83  ? 48.795 70.059 66.966 1.00 28.44  ? 83  LEU C CD2 1 
ATOM   2810 N  N   . SER C 1 84  ? 46.269 65.433 66.893 1.00 26.98  ? 84  SER C N   1 
ATOM   2811 C  CA  . SER C 1 84  ? 45.510 64.375 66.300 1.00 28.15  ? 84  SER C CA  1 
ATOM   2812 C  C   . SER C 1 84  ? 44.085 64.824 66.057 1.00 30.39  ? 84  SER C C   1 
ATOM   2813 O  O   . SER C 1 84  ? 43.549 64.610 64.985 1.00 30.26  ? 84  SER C O   1 
ATOM   2814 C  CB  . SER C 1 84  ? 45.502 63.155 67.182 1.00 29.07  ? 84  SER C CB  1 
ATOM   2815 O  OG  . SER C 1 84  ? 44.476 62.272 66.755 1.00 30.84  ? 84  SER C OG  1 
ATOM   2816 N  N   . ASP C 1 85  ? 43.480 65.469 67.042 1.00 37.73  ? 85  ASP C N   1 
ATOM   2817 C  CA  . ASP C 1 85  ? 42.108 65.946 66.894 1.00 45.08  ? 85  ASP C CA  1 
ATOM   2818 C  C   . ASP C 1 85  ? 41.941 66.907 65.736 1.00 38.76  ? 85  ASP C C   1 
ATOM   2819 O  O   . ASP C 1 85  ? 40.875 66.967 65.145 1.00 38.92  ? 85  ASP C O   1 
ATOM   2820 C  CB  . ASP C 1 85  ? 41.604 66.603 68.185 1.00 61.81  ? 85  ASP C CB  1 
ATOM   2821 C  CG  . ASP C 1 85  ? 41.434 65.594 69.342 1.00 85.50  ? 85  ASP C CG  1 
ATOM   2822 O  OD1 . ASP C 1 85  ? 41.617 64.369 69.122 1.00 100.67 ? 85  ASP C OD1 1 
ATOM   2823 O  OD2 . ASP C 1 85  ? 41.128 66.029 70.481 1.00 95.61  ? 85  ASP C OD2 1 
ATOM   2824 N  N   . LEU C 1 86  ? 42.995 67.651 65.417 1.00 35.62  ? 86  LEU C N   1 
ATOM   2825 C  CA  . LEU C 1 86  ? 42.973 68.634 64.331 1.00 32.24  ? 86  LEU C CA  1 
ATOM   2826 C  C   . LEU C 1 86  ? 43.265 68.004 62.980 1.00 27.73  ? 86  LEU C C   1 
ATOM   2827 O  O   . LEU C 1 86  ? 42.452 68.141 62.062 1.00 28.68  ? 86  LEU C O   1 
ATOM   2828 C  CB  . LEU C 1 86  ? 43.989 69.740 64.608 1.00 33.84  ? 86  LEU C CB  1 
ATOM   2829 C  CG  . LEU C 1 86  ? 43.719 71.078 63.938 1.00 35.39  ? 86  LEU C CG  1 
ATOM   2830 C  CD1 . LEU C 1 86  ? 44.566 72.124 64.642 1.00 41.14  ? 86  LEU C CD1 1 
ATOM   2831 C  CD2 . LEU C 1 86  ? 44.046 71.072 62.463 1.00 35.47  ? 86  LEU C CD2 1 
ATOM   2832 N  N   . HIS C 1 87  ? 44.425 67.351 62.840 1.00 21.13  ? 87  HIS C N   1 
ATOM   2833 C  CA  . HIS C 1 87  ? 44.804 66.797 61.556 1.00 17.27  ? 87  HIS C CA  1 
ATOM   2834 C  C   . HIS C 1 87  ? 43.896 65.619 61.175 1.00 17.13  ? 87  HIS C C   1 
ATOM   2835 O  O   . HIS C 1 87  ? 43.681 65.397 60.001 1.00 17.54  ? 87  HIS C O   1 
ATOM   2836 C  CB  . HIS C 1 87  ? 46.284 66.415 61.493 1.00 14.91  ? 87  HIS C CB  1 
ATOM   2837 C  CG  . HIS C 1 87  ? 47.242 67.574 61.531 1.00 13.51  ? 87  HIS C CG  1 
ATOM   2838 N  ND1 . HIS C 1 87  ? 47.824 67.988 62.696 1.00 12.95  ? 87  HIS C ND1 1 
ATOM   2839 C  CD2 . HIS C 1 87  ? 47.780 68.358 60.552 1.00 13.20  ? 87  HIS C CD2 1 
ATOM   2840 C  CE1 . HIS C 1 87  ? 48.664 68.980 62.447 1.00 13.12  ? 87  HIS C CE1 1 
ATOM   2841 N  NE2 . HIS C 1 87  ? 48.681 69.227 61.146 1.00 12.75  ? 87  HIS C NE2 1 
ATOM   2842 N  N   . ALA C 1 88  ? 43.319 64.897 62.134 1.00 18.79  ? 88  ALA C N   1 
ATOM   2843 C  CA  . ALA C 1 88  ? 42.572 63.659 61.817 1.00 21.42  ? 88  ALA C CA  1 
ATOM   2844 C  C   . ALA C 1 88  ? 41.065 63.799 61.724 1.00 23.96  ? 88  ALA C C   1 
ATOM   2845 O  O   . ALA C 1 88  ? 40.481 63.267 60.790 1.00 24.38  ? 88  ALA C O   1 
ATOM   2846 C  CB  . ALA C 1 88  ? 42.913 62.542 62.801 1.00 21.72  ? 88  ALA C CB  1 
ATOM   2847 N  N   . HIS C 1 89  ? 40.433 64.455 62.695 1.00 29.47  ? 89  HIS C N   1 
ATOM   2848 C  CA  . HIS C 1 89  ? 38.974 64.608 62.681 1.00 35.33  ? 89  HIS C CA  1 
ATOM   2849 C  C   . HIS C 1 89  ? 38.542 65.717 61.759 1.00 37.24  ? 89  HIS C C   1 
ATOM   2850 O  O   . HIS C 1 89  ? 37.712 65.500 60.884 1.00 40.56  ? 89  HIS C O   1 
ATOM   2851 C  CB  . HIS C 1 89  ? 38.410 64.884 64.062 1.00 42.15  ? 89  HIS C CB  1 
ATOM   2852 C  CG  . HIS C 1 89  ? 38.661 63.790 65.044 1.00 54.28  ? 89  HIS C CG  1 
ATOM   2853 N  ND1 . HIS C 1 89  ? 39.888 63.592 65.645 1.00 58.23  ? 89  HIS C ND1 1 
ATOM   2854 C  CD2 . HIS C 1 89  ? 37.840 62.832 65.540 1.00 65.17  ? 89  HIS C CD2 1 
ATOM   2855 C  CE1 . HIS C 1 89  ? 39.813 62.559 66.467 1.00 61.97  ? 89  HIS C CE1 1 
ATOM   2856 N  NE2 . HIS C 1 89  ? 38.582 62.079 66.422 1.00 64.78  ? 89  HIS C NE2 1 
ATOM   2857 N  N   . LYS C 1 90  ? 39.100 66.905 61.957 1.00 39.96  ? 90  LYS C N   1 
ATOM   2858 C  CA  . LYS C 1 90  ? 38.636 68.097 61.265 1.00 42.78  ? 90  LYS C CA  1 
ATOM   2859 C  C   . LYS C 1 90  ? 39.186 68.189 59.845 1.00 38.18  ? 90  LYS C C   1 
ATOM   2860 O  O   . LYS C 1 90  ? 38.418 68.203 58.885 1.00 39.59  ? 90  LYS C O   1 
ATOM   2861 C  CB  . LYS C 1 90  ? 39.009 69.335 62.066 1.00 53.72  ? 90  LYS C CB  1 
ATOM   2862 C  CG  . LYS C 1 90  ? 38.420 70.622 61.518 1.00 68.46  ? 90  LYS C CG  1 
ATOM   2863 C  CD  . LYS C 1 90  ? 38.615 71.790 62.484 1.00 83.47  ? 90  LYS C CD  1 
ATOM   2864 C  CE  . LYS C 1 90  ? 40.009 72.410 62.387 1.00 91.30  ? 90  LYS C CE  1 
ATOM   2865 N  NZ  . LYS C 1 90  ? 40.182 73.293 61.193 1.00 91.87  ? 90  LYS C NZ  1 
ATOM   2866 N  N   . LEU C 1 91  ? 40.507 68.243 59.715 1.00 33.78  ? 91  LEU C N   1 
ATOM   2867 C  CA  . LEU C 1 91  ? 41.156 68.436 58.410 1.00 31.21  ? 91  LEU C CA  1 
ATOM   2868 C  C   . LEU C 1 91  ? 41.156 67.230 57.494 1.00 29.53  ? 91  LEU C C   1 
ATOM   2869 O  O   . LEU C 1 91  ? 41.104 67.398 56.280 1.00 31.27  ? 91  LEU C O   1 
ATOM   2870 C  CB  . LEU C 1 91  ? 42.603 68.872 58.586 1.00 30.00  ? 91  LEU C CB  1 
ATOM   2871 C  CG  . LEU C 1 91  ? 42.774 70.286 59.090 1.00 29.49  ? 91  LEU C CG  1 
ATOM   2872 C  CD1 . LEU C 1 91  ? 44.255 70.573 59.268 1.00 28.95  ? 91  LEU C CD1 1 
ATOM   2873 C  CD2 . LEU C 1 91  ? 42.134 71.260 58.111 1.00 30.67  ? 91  LEU C CD2 1 
ATOM   2874 N  N   . ARG C 1 92  ? 41.264 66.035 58.068 1.00 27.55  ? 92  ARG C N   1 
ATOM   2875 C  CA  . ARG C 1 92  ? 41.306 64.790 57.310 1.00 26.27  ? 92  ARG C CA  1 
ATOM   2876 C  C   . ARG C 1 92  ? 42.415 64.820 56.263 1.00 21.63  ? 92  ARG C C   1 
ATOM   2877 O  O   . ARG C 1 92  ? 42.176 64.740 55.062 1.00 20.92  ? 92  ARG C O   1 
ATOM   2878 C  CB  . ARG C 1 92  ? 39.933 64.480 56.717 1.00 30.99  ? 92  ARG C CB  1 
ATOM   2879 C  CG  . ARG C 1 92  ? 38.867 64.322 57.793 1.00 39.46  ? 92  ARG C CG  1 
ATOM   2880 C  CD  . ARG C 1 92  ? 37.498 63.935 57.251 1.00 49.43  ? 92  ARG C CD  1 
ATOM   2881 N  NE  . ARG C 1 92  ? 36.953 64.995 56.390 1.00 61.50  ? 92  ARG C NE  1 
ATOM   2882 C  CZ  . ARG C 1 92  ? 36.088 65.953 56.750 1.00 69.16  ? 92  ARG C CZ  1 
ATOM   2883 N  NH1 . ARG C 1 92  ? 35.599 66.032 57.992 1.00 74.77  ? 92  ARG C NH1 1 
ATOM   2884 N  NH2 . ARG C 1 92  ? 35.698 66.852 55.841 1.00 66.45  ? 92  ARG C NH2 1 
ATOM   2885 N  N   . VAL C 1 93  ? 43.635 64.972 56.751 1.00 18.66  ? 93  VAL C N   1 
ATOM   2886 C  CA  . VAL C 1 93  ? 44.815 64.885 55.916 1.00 17.47  ? 93  VAL C CA  1 
ATOM   2887 C  C   . VAL C 1 93  ? 45.013 63.405 55.781 1.00 17.13  ? 93  VAL C C   1 
ATOM   2888 O  O   . VAL C 1 93  ? 44.850 62.681 56.772 1.00 16.33  ? 93  VAL C O   1 
ATOM   2889 C  CB  . VAL C 1 93  ? 46.064 65.518 56.581 1.00 16.73  ? 93  VAL C CB  1 
ATOM   2890 C  CG1 . VAL C 1 93  ? 47.291 65.415 55.678 1.00 16.05  ? 93  VAL C CG1 1 
ATOM   2891 C  CG2 . VAL C 1 93  ? 45.794 66.974 56.917 1.00 16.64  ? 93  VAL C CG2 1 
ATOM   2892 N  N   . ASP C 1 94  ? 45.347 62.950 54.572 1.00 17.53  ? 94  ASP C N   1 
ATOM   2893 C  CA  . ASP C 1 94  ? 45.581 61.523 54.349 1.00 18.23  ? 94  ASP C CA  1 
ATOM   2894 C  C   . ASP C 1 94  ? 47.030 61.224 54.508 1.00 16.82  ? 94  ASP C C   1 
ATOM   2895 O  O   . ASP C 1 94  ? 47.868 62.090 54.257 1.00 16.68  ? 94  ASP C O   1 
ATOM   2896 C  CB  . ASP C 1 94  ? 45.113 61.053 52.981 1.00 20.62  ? 94  ASP C CB  1 
ATOM   2897 C  CG  . ASP C 1 94  ? 46.025 61.460 51.886 1.00 22.80  ? 94  ASP C CG  1 
ATOM   2898 O  OD1 . ASP C 1 94  ? 46.339 62.680 51.850 1.00 23.87  ? 94  ASP C OD1 1 
ATOM   2899 O  OD2 . ASP C 1 94  ? 46.401 60.562 51.077 1.00 23.15  ? 94  ASP C OD2 1 
ATOM   2900 N  N   . PRO C 1 95  ? 47.339 59.985 54.883 1.00 15.97  ? 95  PRO C N   1 
ATOM   2901 C  CA  . PRO C 1 95  ? 48.610 59.796 55.537 1.00 16.98  ? 95  PRO C CA  1 
ATOM   2902 C  C   . PRO C 1 95  ? 49.831 59.819 54.587 1.00 17.71  ? 95  PRO C C   1 
ATOM   2903 O  O   . PRO C 1 95  ? 50.968 59.960 55.058 1.00 18.07  ? 95  PRO C O   1 
ATOM   2904 C  CB  . PRO C 1 95  ? 48.421 58.449 56.252 1.00 16.37  ? 95  PRO C CB  1 
ATOM   2905 C  CG  . PRO C 1 95  ? 46.965 58.148 56.124 1.00 15.57  ? 95  PRO C CG  1 
ATOM   2906 C  CD  . PRO C 1 95  ? 46.616 58.721 54.810 1.00 15.07  ? 95  PRO C CD  1 
ATOM   2907 N  N   . VAL C 1 96  ? 49.582 59.707 53.281 1.00 17.20  ? 96  VAL C N   1 
ATOM   2908 C  CA  . VAL C 1 96  ? 50.586 59.970 52.246 1.00 16.95  ? 96  VAL C CA  1 
ATOM   2909 C  C   . VAL C 1 96  ? 51.292 61.301 52.378 1.00 15.82  ? 96  VAL C C   1 
ATOM   2910 O  O   . VAL C 1 96  ? 52.490 61.384 52.104 1.00 16.86  ? 96  VAL C O   1 
ATOM   2911 C  CB  . VAL C 1 96  ? 49.924 59.939 50.860 1.00 18.79  ? 96  VAL C CB  1 
ATOM   2912 C  CG1 . VAL C 1 96  ? 50.729 60.659 49.771 1.00 18.70  ? 96  VAL C CG1 1 
ATOM   2913 C  CG2 . VAL C 1 96  ? 49.699 58.488 50.490 1.00 21.19  ? 96  VAL C CG2 1 
ATOM   2914 N  N   . ASN C 1 97  ? 50.568 62.342 52.761 1.00 13.55  ? 97  ASN C N   1 
ATOM   2915 C  CA  . ASN C 1 97  ? 51.165 63.657 52.799 1.00 12.41  ? 97  ASN C CA  1 
ATOM   2916 C  C   . ASN C 1 97  ? 52.072 63.814 53.978 1.00 11.91  ? 97  ASN C C   1 
ATOM   2917 O  O   . ASN C 1 97  ? 52.885 64.723 53.982 1.00 12.01  ? 97  ASN C O   1 
ATOM   2918 C  CB  . ASN C 1 97  ? 50.109 64.731 52.852 1.00 12.72  ? 97  ASN C CB  1 
ATOM   2919 C  CG  . ASN C 1 97  ? 49.123 64.638 51.708 1.00 13.16  ? 97  ASN C CG  1 
ATOM   2920 O  OD1 . ASN C 1 97  ? 47.985 65.079 51.843 1.00 13.29  ? 97  ASN C OD1 1 
ATOM   2921 N  ND2 . ASN C 1 97  ? 49.541 64.048 50.581 1.00 13.46  ? 97  ASN C ND2 1 
ATOM   2922 N  N   . PHE C 1 98  ? 51.940 62.952 54.987 1.00 11.75  ? 98  PHE C N   1 
ATOM   2923 C  CA  . PHE C 1 98  ? 52.911 62.918 56.078 1.00 11.79  ? 98  PHE C CA  1 
ATOM   2924 C  C   . PHE C 1 98  ? 54.247 62.413 55.632 1.00 13.71  ? 98  PHE C C   1 
ATOM   2925 O  O   . PHE C 1 98  ? 55.266 62.932 56.053 1.00 14.39  ? 98  PHE C O   1 
ATOM   2926 C  CB  . PHE C 1 98  ? 52.402 62.111 57.238 1.00 10.55  ? 98  PHE C CB  1 
ATOM   2927 C  CG  . PHE C 1 98  ? 51.430 62.858 58.025 1.00 9.81   ? 98  PHE C CG  1 
ATOM   2928 C  CD1 . PHE C 1 98  ? 51.868 63.726 58.999 1.00 9.52   ? 98  PHE C CD1 1 
ATOM   2929 C  CD2 . PHE C 1 98  ? 50.087 62.794 57.720 1.00 9.52   ? 98  PHE C CD2 1 
ATOM   2930 C  CE1 . PHE C 1 98  ? 50.973 64.495 59.709 1.00 9.63   ? 98  PHE C CE1 1 
ATOM   2931 C  CE2 . PHE C 1 98  ? 49.179 63.572 58.412 1.00 9.68   ? 98  PHE C CE2 1 
ATOM   2932 C  CZ  . PHE C 1 98  ? 49.620 64.419 59.421 1.00 9.72   ? 98  PHE C CZ  1 
ATOM   2933 N  N   . LYS C 1 99  ? 54.244 61.436 54.745 1.00 16.56  ? 99  LYS C N   1 
ATOM   2934 C  CA  . LYS C 1 99  ? 55.474 60.934 54.192 1.00 19.31  ? 99  LYS C CA  1 
ATOM   2935 C  C   . LYS C 1 99  ? 56.261 61.920 53.355 1.00 17.44  ? 99  LYS C C   1 
ATOM   2936 O  O   . LYS C 1 99  ? 57.440 61.686 53.123 1.00 18.44  ? 99  LYS C O   1 
ATOM   2937 C  CB  . LYS C 1 99  ? 55.211 59.695 53.379 1.00 25.58  ? 99  LYS C CB  1 
ATOM   2938 C  CG  . LYS C 1 99  ? 54.919 58.502 54.266 1.00 34.73  ? 99  LYS C CG  1 
ATOM   2939 C  CD  . LYS C 1 99  ? 54.309 57.336 53.493 1.00 46.19  ? 99  LYS C CD  1 
ATOM   2940 C  CE  . LYS C 1 99  ? 55.239 56.797 52.399 1.00 55.40  ? 99  LYS C CE  1 
ATOM   2941 N  NZ  . LYS C 1 99  ? 54.595 55.691 51.629 1.00 61.12  ? 99  LYS C NZ  1 
ATOM   2942 N  N   . LEU C 1 100 ? 55.648 63.003 52.897 1.00 15.20  ? 100 LEU C N   1 
ATOM   2943 C  CA  . LEU C 1 100 ? 56.368 63.992 52.105 1.00 13.99  ? 100 LEU C CA  1 
ATOM   2944 C  C   . LEU C 1 100 ? 56.912 65.094 52.997 1.00 13.25  ? 100 LEU C C   1 
ATOM   2945 O  O   . LEU C 1 100 ? 58.011 65.584 52.756 1.00 13.35  ? 100 LEU C O   1 
ATOM   2946 C  CB  . LEU C 1 100 ? 55.475 64.584 51.024 1.00 13.99  ? 100 LEU C CB  1 
ATOM   2947 C  CG  . LEU C 1 100 ? 54.683 63.573 50.194 1.00 13.98  ? 100 LEU C CG  1 
ATOM   2948 C  CD1 . LEU C 1 100 ? 53.523 64.236 49.472 1.00 13.97  ? 100 LEU C CD1 1 
ATOM   2949 C  CD2 . LEU C 1 100 ? 55.605 62.864 49.218 1.00 14.26  ? 100 LEU C CD2 1 
ATOM   2950 N  N   . LEU C 1 101 ? 56.160 65.503 54.014 1.00 12.48  ? 101 LEU C N   1 
ATOM   2951 C  CA  . LEU C 1 101 ? 56.691 66.471 54.957 1.00 12.39  ? 101 LEU C CA  1 
ATOM   2952 C  C   . LEU C 1 101 ? 57.793 65.878 55.815 1.00 12.69  ? 101 LEU C C   1 
ATOM   2953 O  O   . LEU C 1 101 ? 58.656 66.622 56.278 1.00 13.49  ? 101 LEU C O   1 
ATOM   2954 C  CB  . LEU C 1 101 ? 55.626 66.998 55.896 1.00 12.64  ? 101 LEU C CB  1 
ATOM   2955 C  CG  . LEU C 1 101 ? 56.061 68.144 56.823 1.00 12.83  ? 101 LEU C CG  1 
ATOM   2956 C  CD1 . LEU C 1 101 ? 56.714 69.271 56.049 1.00 13.07  ? 101 LEU C CD1 1 
ATOM   2957 C  CD2 . LEU C 1 101 ? 54.869 68.699 57.561 1.00 12.96  ? 101 LEU C CD2 1 
ATOM   2958 N  N   . SER C 1 102 ? 57.761 64.566 56.050 1.00 11.96  ? 102 SER C N   1 
ATOM   2959 C  CA  . SER C 1 102 ? 58.820 63.900 56.789 1.00 11.43  ? 102 SER C CA  1 
ATOM   2960 C  C   . SER C 1 102 ? 60.054 63.757 55.986 1.00 11.21  ? 102 SER C C   1 
ATOM   2961 O  O   . SER C 1 102 ? 61.137 63.809 56.532 1.00 11.09  ? 102 SER C O   1 
ATOM   2962 C  CB  . SER C 1 102 ? 58.395 62.522 57.204 1.00 12.15  ? 102 SER C CB  1 
ATOM   2963 O  OG  . SER C 1 102 ? 57.314 62.605 58.123 1.00 13.18  ? 102 SER C OG  1 
ATOM   2964 N  N   . HIS C 1 103 ? 59.896 63.546 54.688 1.00 12.19  ? 103 HIS C N   1 
ATOM   2965 C  CA  . HIS C 1 103 ? 61.031 63.547 53.745 1.00 13.32  ? 103 HIS C CA  1 
ATOM   2966 C  C   . HIS C 1 103 ? 61.702 64.906 53.613 1.00 14.26  ? 103 HIS C C   1 
ATOM   2967 O  O   . HIS C 1 103 ? 62.928 65.008 53.609 1.00 14.75  ? 103 HIS C O   1 
ATOM   2968 C  CB  . HIS C 1 103 ? 60.562 63.135 52.360 1.00 13.36  ? 103 HIS C CB  1 
ATOM   2969 C  CG  . HIS C 1 103 ? 61.626 63.208 51.317 1.00 13.34  ? 103 HIS C CG  1 
ATOM   2970 N  ND1 . HIS C 1 103 ? 62.716 62.363 51.312 1.00 13.37  ? 103 HIS C ND1 1 
ATOM   2971 C  CD2 . HIS C 1 103 ? 61.764 64.018 50.241 1.00 13.26  ? 103 HIS C CD2 1 
ATOM   2972 C  CE1 . HIS C 1 103 ? 63.477 62.646 50.270 1.00 13.48  ? 103 HIS C CE1 1 
ATOM   2973 N  NE2 . HIS C 1 103 ? 62.924 63.648 49.607 1.00 13.51  ? 103 HIS C NE2 1 
ATOM   2974 N  N   . CYS C 1 104 ? 60.890 65.940 53.487 1.00 15.31  ? 104 CYS C N   1 
ATOM   2975 C  CA  . CYS C 1 104 ? 61.411 67.272 53.349 1.00 16.43  ? 104 CYS C CA  1 
ATOM   2976 C  C   . CYS C 1 104 ? 62.005 67.852 54.606 1.00 15.22  ? 104 CYS C C   1 
ATOM   2977 O  O   . CYS C 1 104 ? 62.759 68.795 54.510 1.00 15.58  ? 104 CYS C O   1 
ATOM   2978 C  CB  . CYS C 1 104 ? 60.345 68.180 52.786 1.00 19.44  ? 104 CYS C CB  1 
ATOM   2979 S  SG  . CYS C 1 104 ? 60.102 67.840 51.019 1.00 26.99  ? 104 CYS C SG  1 
ATOM   2980 N  N   . LEU C 1 105 ? 61.696 67.311 55.774 1.00 14.83  ? 105 LEU C N   1 
ATOM   2981 C  CA  . LEU C 1 105 ? 62.461 67.663 56.963 1.00 15.03  ? 105 LEU C CA  1 
ATOM   2982 C  C   . LEU C 1 105 ? 63.822 67.049 56.986 1.00 14.62  ? 105 LEU C C   1 
ATOM   2983 O  O   . LEU C 1 105 ? 64.735 67.687 57.488 1.00 15.71  ? 105 LEU C O   1 
ATOM   2984 C  CB  . LEU C 1 105 ? 61.793 67.227 58.245 1.00 16.12  ? 105 LEU C CB  1 
ATOM   2985 C  CG  . LEU C 1 105 ? 60.822 68.238 58.811 1.00 17.28  ? 105 LEU C CG  1 
ATOM   2986 C  CD1 . LEU C 1 105 ? 59.923 67.565 59.846 1.00 17.74  ? 105 LEU C CD1 1 
ATOM   2987 C  CD2 . LEU C 1 105 ? 61.604 69.393 59.412 1.00 17.87  ? 105 LEU C CD2 1 
ATOM   2988 N  N   . LEU C 1 106 ? 63.973 65.817 56.509 1.00 14.11  ? 106 LEU C N   1 
ATOM   2989 C  CA  . LEU C 1 106 ? 65.294 65.172 56.540 1.00 14.14  ? 106 LEU C CA  1 
ATOM   2990 C  C   . LEU C 1 106 ? 66.238 65.770 55.539 1.00 13.21  ? 106 LEU C C   1 
ATOM   2991 O  O   . LEU C 1 106 ? 67.405 65.958 55.846 1.00 13.40  ? 106 LEU C O   1 
ATOM   2992 C  CB  . LEU C 1 106 ? 65.216 63.668 56.334 1.00 15.05  ? 106 LEU C CB  1 
ATOM   2993 C  CG  . LEU C 1 106 ? 64.388 62.997 57.438 1.00 16.47  ? 106 LEU C CG  1 
ATOM   2994 C  CD1 . LEU C 1 106 ? 64.393 61.486 57.219 1.00 16.93  ? 106 LEU C CD1 1 
ATOM   2995 C  CD2 . LEU C 1 106 ? 64.844 63.373 58.861 1.00 16.81  ? 106 LEU C CD2 1 
ATOM   2996 N  N   . VAL C 1 107 ? 65.746 66.096 54.357 1.00 12.60  ? 107 VAL C N   1 
ATOM   2997 C  CA  . VAL C 1 107 ? 66.563 66.825 53.410 1.00 12.62  ? 107 VAL C CA  1 
ATOM   2998 C  C   . VAL C 1 107 ? 67.066 68.125 54.040 1.00 13.27  ? 107 VAL C C   1 
ATOM   2999 O  O   . VAL C 1 107 ? 68.245 68.433 53.944 1.00 13.61  ? 107 VAL C O   1 
ATOM   3000 C  CB  . VAL C 1 107 ? 65.810 67.072 52.091 1.00 12.18  ? 107 VAL C CB  1 
ATOM   3001 C  CG1 . VAL C 1 107 ? 66.412 68.233 51.301 1.00 12.10  ? 107 VAL C CG1 1 
ATOM   3002 C  CG2 . VAL C 1 107 ? 65.795 65.792 51.259 1.00 11.75  ? 107 VAL C CG2 1 
ATOM   3003 N  N   . THR C 1 108 ? 66.184 68.859 54.699 1.00 14.46  ? 108 THR C N   1 
ATOM   3004 C  CA  . THR C 1 108 ? 66.552 70.110 55.338 1.00 15.79  ? 108 THR C CA  1 
ATOM   3005 C  C   . THR C 1 108 ? 67.602 69.958 56.425 1.00 16.71  ? 108 THR C C   1 
ATOM   3006 O  O   . THR C 1 108 ? 68.535 70.747 56.468 1.00 17.91  ? 108 THR C O   1 
ATOM   3007 C  CB  . THR C 1 108 ? 65.325 70.789 55.944 1.00 16.89  ? 108 THR C CB  1 
ATOM   3008 O  OG1 . THR C 1 108 ? 64.405 71.094 54.893 1.00 18.11  ? 108 THR C OG1 1 
ATOM   3009 C  CG2 . THR C 1 108 ? 65.685 72.088 56.631 1.00 17.68  ? 108 THR C CG2 1 
ATOM   3010 N  N   . LEU C 1 109 ? 67.469 68.982 57.309 1.00 17.89  ? 109 LEU C N   1 
ATOM   3011 C  CA  . LEU C 1 109 ? 68.521 68.746 58.291 1.00 19.27  ? 109 LEU C CA  1 
ATOM   3012 C  C   . LEU C 1 109 ? 69.828 68.362 57.650 1.00 19.86  ? 109 LEU C C   1 
ATOM   3013 O  O   . LEU C 1 109 ? 70.861 68.881 58.044 1.00 21.80  ? 109 LEU C O   1 
ATOM   3014 C  CB  . LEU C 1 109 ? 68.159 67.645 59.269 1.00 21.08  ? 109 LEU C CB  1 
ATOM   3015 C  CG  . LEU C 1 109 ? 67.033 68.004 60.227 1.00 23.19  ? 109 LEU C CG  1 
ATOM   3016 C  CD1 . LEU C 1 109 ? 66.842 66.856 61.206 1.00 24.05  ? 109 LEU C CD1 1 
ATOM   3017 C  CD2 . LEU C 1 109 ? 67.306 69.314 60.951 1.00 23.81  ? 109 LEU C CD2 1 
ATOM   3018 N  N   . ALA C 1 110 ? 69.810 67.470 56.671 1.00 20.16  ? 110 ALA C N   1 
ATOM   3019 C  CA  . ALA C 1 110 ? 71.056 67.061 56.015 1.00 20.92  ? 110 ALA C CA  1 
ATOM   3020 C  C   . ALA C 1 110 ? 71.758 68.221 55.305 1.00 21.82  ? 110 ALA C C   1 
ATOM   3021 O  O   . ALA C 1 110 ? 72.981 68.238 55.206 1.00 22.94  ? 110 ALA C O   1 
ATOM   3022 C  CB  . ALA C 1 110 ? 70.803 65.929 55.035 1.00 21.37  ? 110 ALA C CB  1 
ATOM   3023 N  N   . ALA C 1 111 ? 70.991 69.188 54.825 1.00 23.03  ? 111 ALA C N   1 
ATOM   3024 C  CA  . ALA C 1 111 ? 71.559 70.373 54.208 1.00 25.08  ? 111 ALA C CA  1 
ATOM   3025 C  C   . ALA C 1 111 ? 72.018 71.438 55.211 1.00 28.97  ? 111 ALA C C   1 
ATOM   3026 O  O   . ALA C 1 111 ? 72.482 72.496 54.787 1.00 31.59  ? 111 ALA C O   1 
ATOM   3027 C  CB  . ALA C 1 111 ? 70.556 70.972 53.233 1.00 24.81  ? 111 ALA C CB  1 
ATOM   3028 N  N   . HIS C 1 112 ? 71.865 71.197 56.516 1.00 33.62  ? 112 HIS C N   1 
ATOM   3029 C  CA  . HIS C 1 112 ? 72.265 72.169 57.544 1.00 38.03  ? 112 HIS C CA  1 
ATOM   3030 C  C   . HIS C 1 112 ? 73.048 71.661 58.757 1.00 42.45  ? 112 HIS C C   1 
ATOM   3031 O  O   . HIS C 1 112 ? 73.694 72.461 59.429 1.00 44.07  ? 112 HIS C O   1 
ATOM   3032 C  CB  . HIS C 1 112 ? 71.031 72.920 58.010 1.00 38.90  ? 112 HIS C CB  1 
ATOM   3033 C  CG  . HIS C 1 112 ? 70.554 73.930 57.022 1.00 42.94  ? 112 HIS C CG  1 
ATOM   3034 N  ND1 . HIS C 1 112 ? 69.822 73.589 55.907 1.00 45.05  ? 112 HIS C ND1 1 
ATOM   3035 C  CD2 . HIS C 1 112 ? 70.728 75.270 56.964 1.00 48.53  ? 112 HIS C CD2 1 
ATOM   3036 C  CE1 . HIS C 1 112 ? 69.559 74.676 55.206 1.00 47.46  ? 112 HIS C CE1 1 
ATOM   3037 N  NE2 . HIS C 1 112 ? 70.093 75.711 55.828 1.00 50.09  ? 112 HIS C NE2 1 
ATOM   3038 N  N   . LEU C 1 113 ? 72.995 70.362 59.042 1.00 50.40  ? 113 LEU C N   1 
ATOM   3039 C  CA  . LEU C 1 113 ? 73.745 69.758 60.136 1.00 59.93  ? 113 LEU C CA  1 
ATOM   3040 C  C   . LEU C 1 113 ? 74.509 68.583 59.574 1.00 65.96  ? 113 LEU C C   1 
ATOM   3041 O  O   . LEU C 1 113 ? 74.240 67.440 59.939 1.00 77.72  ? 113 LEU C O   1 
ATOM   3042 C  CB  . LEU C 1 113 ? 72.797 69.267 61.233 1.00 66.71  ? 113 LEU C CB  1 
ATOM   3043 C  CG  . LEU C 1 113 ? 71.877 70.296 61.886 1.00 76.05  ? 113 LEU C CG  1 
ATOM   3044 C  CD1 . LEU C 1 113 ? 70.955 69.577 62.865 1.00 79.51  ? 113 LEU C CD1 1 
ATOM   3045 C  CD2 . LEU C 1 113 ? 72.668 71.404 62.578 1.00 79.04  ? 113 LEU C CD2 1 
ATOM   3046 N  N   . PRO C 1 114 ? 75.467 68.847 58.680 1.00 72.74  ? 114 PRO C N   1 
ATOM   3047 C  CA  . PRO C 1 114 ? 76.084 67.736 57.955 1.00 74.63  ? 114 PRO C CA  1 
ATOM   3048 C  C   . PRO C 1 114 ? 76.833 66.754 58.848 1.00 74.89  ? 114 PRO C C   1 
ATOM   3049 O  O   . PRO C 1 114 ? 76.834 65.555 58.568 1.00 71.89  ? 114 PRO C O   1 
ATOM   3050 C  CB  . PRO C 1 114 ? 77.054 68.437 56.994 1.00 82.84  ? 114 PRO C CB  1 
ATOM   3051 C  CG  . PRO C 1 114 ? 76.668 69.885 57.019 1.00 87.26  ? 114 PRO C CG  1 
ATOM   3052 C  CD  . PRO C 1 114 ? 76.150 70.116 58.398 1.00 79.63  ? 114 PRO C CD  1 
ATOM   3053 N  N   . ALA C 1 115 ? 77.445 67.265 59.914 1.00 82.86  ? 115 ALA C N   1 
ATOM   3054 C  CA  . ALA C 1 115 ? 78.232 66.446 60.835 1.00 92.91  ? 115 ALA C CA  1 
ATOM   3055 C  C   . ALA C 1 115 ? 77.381 65.523 61.715 1.00 92.50  ? 115 ALA C C   1 
ATOM   3056 O  O   . ALA C 1 115 ? 77.790 64.399 62.018 1.00 91.17  ? 115 ALA C O   1 
ATOM   3057 C  CB  . ALA C 1 115 ? 79.102 67.341 61.705 1.00 101.07 ? 115 ALA C CB  1 
ATOM   3058 N  N   . GLU C 1 116 ? 76.202 66.001 62.113 1.00 93.89  ? 116 GLU C N   1 
ATOM   3059 C  CA  . GLU C 1 116 ? 75.304 65.248 62.998 1.00 96.59  ? 116 GLU C CA  1 
ATOM   3060 C  C   . GLU C 1 116 ? 74.439 64.206 62.285 1.00 82.83  ? 116 GLU C C   1 
ATOM   3061 O  O   . GLU C 1 116 ? 73.697 63.478 62.940 1.00 83.29  ? 116 GLU C O   1 
ATOM   3062 C  CB  . GLU C 1 116 ? 74.397 66.224 63.768 1.00 112.71 ? 116 GLU C CB  1 
ATOM   3063 C  CG  . GLU C 1 116 ? 75.150 67.213 64.659 1.00 133.10 ? 116 GLU C CG  1 
ATOM   3064 C  CD  . GLU C 1 116 ? 75.952 66.542 65.775 1.00 152.07 ? 116 GLU C CD  1 
ATOM   3065 O  OE1 . GLU C 1 116 ? 75.457 65.557 66.372 1.00 162.72 ? 116 GLU C OE1 1 
ATOM   3066 O  OE2 . GLU C 1 116 ? 77.079 67.007 66.066 1.00 153.33 ? 116 GLU C OE2 1 
ATOM   3067 N  N   . PHE C 1 117 ? 74.551 64.115 60.960 1.00 73.02  ? 117 PHE C N   1 
ATOM   3068 C  CA  . PHE C 1 117 ? 73.640 63.331 60.138 1.00 65.72  ? 117 PHE C CA  1 
ATOM   3069 C  C   . PHE C 1 117 ? 74.319 62.027 59.698 1.00 60.97  ? 117 PHE C C   1 
ATOM   3070 O  O   . PHE C 1 117 ? 74.458 61.742 58.509 1.00 59.83  ? 117 PHE C O   1 
ATOM   3071 C  CB  . PHE C 1 117 ? 73.182 64.192 58.943 1.00 64.73  ? 117 PHE C CB  1 
ATOM   3072 C  CG  . PHE C 1 117 ? 71.910 63.717 58.305 1.00 67.60  ? 117 PHE C CG  1 
ATOM   3073 C  CD1 . PHE C 1 117 ? 70.682 63.926 58.938 1.00 65.77  ? 117 PHE C CD1 1 
ATOM   3074 C  CD2 . PHE C 1 117 ? 71.933 63.048 57.073 1.00 68.58  ? 117 PHE C CD2 1 
ATOM   3075 C  CE1 . PHE C 1 117 ? 69.502 63.470 58.362 1.00 66.01  ? 117 PHE C CE1 1 
ATOM   3076 C  CE2 . PHE C 1 117 ? 70.754 62.593 56.491 1.00 67.37  ? 117 PHE C CE2 1 
ATOM   3077 C  CZ  . PHE C 1 117 ? 69.537 62.805 57.137 1.00 67.38  ? 117 PHE C CZ  1 
ATOM   3078 N  N   . THR C 1 118 ? 74.741 61.235 60.678 1.00 60.28  ? 118 THR C N   1 
ATOM   3079 C  CA  . THR C 1 118 ? 75.307 59.916 60.416 1.00 63.09  ? 118 THR C CA  1 
ATOM   3080 C  C   . THR C 1 118 ? 74.169 58.957 60.126 1.00 58.15  ? 118 THR C C   1 
ATOM   3081 O  O   . THR C 1 118 ? 73.034 59.233 60.515 1.00 63.05  ? 118 THR C O   1 
ATOM   3082 C  CB  . THR C 1 118 ? 76.063 59.352 61.638 1.00 75.84  ? 118 THR C CB  1 
ATOM   3083 O  OG1 . THR C 1 118 ? 75.170 59.229 62.760 1.00 78.65  ? 118 THR C OG1 1 
ATOM   3084 C  CG2 . THR C 1 118 ? 77.237 60.248 62.012 1.00 82.95  ? 118 THR C CG2 1 
ATOM   3085 N  N   . PRO C 1 119 ? 74.461 57.812 59.479 1.00 51.64  ? 119 PRO C N   1 
ATOM   3086 C  CA  . PRO C 1 119 ? 73.430 56.803 59.220 1.00 47.14  ? 119 PRO C CA  1 
ATOM   3087 C  C   . PRO C 1 119 ? 72.560 56.440 60.405 1.00 41.73  ? 119 PRO C C   1 
ATOM   3088 O  O   . PRO C 1 119 ? 71.349 56.372 60.251 1.00 42.63  ? 119 PRO C O   1 
ATOM   3089 C  CB  . PRO C 1 119 ? 74.240 55.607 58.753 1.00 49.57  ? 119 PRO C CB  1 
ATOM   3090 C  CG  . PRO C 1 119 ? 75.334 56.259 57.987 1.00 51.38  ? 119 PRO C CG  1 
ATOM   3091 C  CD  . PRO C 1 119 ? 75.729 57.437 58.829 1.00 51.62  ? 119 PRO C CD  1 
ATOM   3092 N  N   . ALA C 1 120 ? 73.153 56.244 61.573 1.00 40.62  ? 120 ALA C N   1 
ATOM   3093 C  CA  . ALA C 1 120 ? 72.371 55.883 62.756 1.00 43.24  ? 120 ALA C CA  1 
ATOM   3094 C  C   . ALA C 1 120 ? 71.376 56.963 63.187 1.00 38.91  ? 120 ALA C C   1 
ATOM   3095 O  O   . ALA C 1 120 ? 70.292 56.653 63.682 1.00 40.21  ? 120 ALA C O   1 
ATOM   3096 C  CB  . ALA C 1 120 ? 73.290 55.535 63.911 1.00 50.15  ? 120 ALA C CB  1 
ATOM   3097 N  N   . VAL C 1 121 ? 71.747 58.218 63.001 1.00 34.11  ? 121 VAL C N   1 
ATOM   3098 C  CA  . VAL C 1 121 ? 70.822 59.310 63.228 1.00 33.44  ? 121 VAL C CA  1 
ATOM   3099 C  C   . VAL C 1 121 ? 69.736 59.357 62.146 1.00 29.86  ? 121 VAL C C   1 
ATOM   3100 O  O   . VAL C 1 121 ? 68.568 59.562 62.471 1.00 31.02  ? 121 VAL C O   1 
ATOM   3101 C  CB  . VAL C 1 121 ? 71.572 60.650 63.303 1.00 37.45  ? 121 VAL C CB  1 
ATOM   3102 C  CG1 . VAL C 1 121 ? 70.606 61.836 63.304 1.00 38.38  ? 121 VAL C CG1 1 
ATOM   3103 C  CG2 . VAL C 1 121 ? 72.455 60.659 64.549 1.00 40.52  ? 121 VAL C CG2 1 
ATOM   3104 N  N   . HIS C 1 122 ? 70.122 59.192 60.878 1.00 24.71  ? 122 HIS C N   1 
ATOM   3105 C  CA  . HIS C 1 122 ? 69.172 59.111 59.764 1.00 21.79  ? 122 HIS C CA  1 
ATOM   3106 C  C   . HIS C 1 122 ? 68.159 58.029 60.082 1.00 21.05  ? 122 HIS C C   1 
ATOM   3107 O  O   . HIS C 1 122 ? 66.960 58.267 60.006 1.00 22.16  ? 122 HIS C O   1 
ATOM   3108 C  CB  . HIS C 1 122 ? 69.900 58.777 58.457 1.00 20.92  ? 122 HIS C CB  1 
ATOM   3109 C  CG  . HIS C 1 122 ? 69.066 58.899 57.211 1.00 21.13  ? 122 HIS C CG  1 
ATOM   3110 N  ND1 . HIS C 1 122 ? 69.634 59.041 55.962 1.00 20.70  ? 122 HIS C ND1 1 
ATOM   3111 C  CD2 . HIS C 1 122 ? 67.723 58.894 57.008 1.00 21.51  ? 122 HIS C CD2 1 
ATOM   3112 C  CE1 . HIS C 1 122 ? 68.682 59.114 55.048 1.00 20.67  ? 122 HIS C CE1 1 
ATOM   3113 N  NE2 . HIS C 1 122 ? 67.512 59.033 55.656 1.00 20.77  ? 122 HIS C NE2 1 
ATOM   3114 N  N   . ALA C 1 123 ? 68.643 56.857 60.474 1.00 20.36  ? 123 ALA C N   1 
ATOM   3115 C  CA  . ALA C 1 123 ? 67.780 55.711 60.764 1.00 20.22  ? 123 ALA C CA  1 
ATOM   3116 C  C   . ALA C 1 123 ? 66.806 55.951 61.898 1.00 20.81  ? 123 ALA C C   1 
ATOM   3117 O  O   . ALA C 1 123 ? 65.643 55.561 61.796 1.00 22.43  ? 123 ALA C O   1 
ATOM   3118 C  CB  . ALA C 1 123 ? 68.610 54.494 61.088 1.00 20.44  ? 123 ALA C CB  1 
ATOM   3119 N  N   . SER C 1 124 ? 67.270 56.573 62.976 1.00 20.64  ? 124 SER C N   1 
ATOM   3120 C  CA  . SER C 1 124 ? 66.401 56.886 64.107 1.00 20.54  ? 124 SER C CA  1 
ATOM   3121 C  C   . SER C 1 124 ? 65.417 57.985 63.785 1.00 20.22  ? 124 SER C C   1 
ATOM   3122 O  O   . SER C 1 124 ? 64.234 57.814 64.010 1.00 20.40  ? 124 SER C O   1 
ATOM   3123 C  CB  . SER C 1 124 ? 67.221 57.302 65.308 1.00 21.36  ? 124 SER C CB  1 
ATOM   3124 O  OG  . SER C 1 124 ? 68.190 56.312 65.601 1.00 22.79  ? 124 SER C OG  1 
ATOM   3125 N  N   . LEU C 1 125 ? 65.898 59.104 63.253 1.00 21.70  ? 125 LEU C N   1 
ATOM   3126 C  CA  . LEU C 1 125 ? 65.020 60.232 62.937 1.00 23.48  ? 125 LEU C CA  1 
ATOM   3127 C  C   . LEU C 1 125 ? 63.920 59.882 61.972 1.00 24.79  ? 125 LEU C C   1 
ATOM   3128 O  O   . LEU C 1 125 ? 62.876 60.525 61.998 1.00 26.71  ? 125 LEU C O   1 
ATOM   3129 C  CB  . LEU C 1 125 ? 65.786 61.432 62.378 1.00 25.18  ? 125 LEU C CB  1 
ATOM   3130 C  CG  . LEU C 1 125 ? 66.235 62.477 63.405 1.00 26.96  ? 125 LEU C CG  1 
ATOM   3131 C  CD1 . LEU C 1 125 ? 67.276 63.428 62.834 1.00 27.58  ? 125 LEU C CD1 1 
ATOM   3132 C  CD2 . LEU C 1 125 ? 65.043 63.280 63.908 1.00 28.51  ? 125 LEU C CD2 1 
ATOM   3133 N  N   . ASP C 1 126 ? 64.147 58.884 61.123 1.00 26.91  ? 126 ASP C N   1 
ATOM   3134 C  CA  . ASP C 1 126 ? 63.115 58.392 60.213 1.00 29.23  ? 126 ASP C CA  1 
ATOM   3135 C  C   . ASP C 1 126 ? 61.972 57.663 60.926 1.00 26.39  ? 126 ASP C C   1 
ATOM   3136 O  O   . ASP C 1 126 ? 60.802 57.900 60.618 1.00 24.65  ? 126 ASP C O   1 
ATOM   3137 C  CB  . ASP C 1 126 ? 63.740 57.470 59.177 1.00 36.03  ? 126 ASP C CB  1 
ATOM   3138 C  CG  . ASP C 1 126 ? 62.791 57.155 58.026 1.00 45.71  ? 126 ASP C CG  1 
ATOM   3139 O  OD1 . ASP C 1 126 ? 62.775 57.912 57.014 1.00 49.14  ? 126 ASP C OD1 1 
ATOM   3140 O  OD2 . ASP C 1 126 ? 62.067 56.132 58.136 1.00 52.20  ? 126 ASP C OD2 1 
ATOM   3141 N  N   . LYS C 1 127 ? 62.321 56.771 61.856 1.00 25.62  ? 127 LYS C N   1 
ATOM   3142 C  CA  . LYS C 1 127 ? 61.331 56.094 62.725 1.00 25.47  ? 127 LYS C CA  1 
ATOM   3143 C  C   . LYS C 1 127 ? 60.538 57.040 63.613 1.00 21.74  ? 127 LYS C C   1 
ATOM   3144 O  O   . LYS C 1 127 ? 59.338 56.852 63.816 1.00 21.77  ? 127 LYS C O   1 
ATOM   3145 C  CB  . LYS C 1 127 ? 61.997 55.070 63.634 1.00 28.07  ? 127 LYS C CB  1 
ATOM   3146 C  CG  . LYS C 1 127 ? 62.422 53.832 62.892 1.00 33.28  ? 127 LYS C CG  1 
ATOM   3147 C  CD  . LYS C 1 127 ? 63.198 52.867 63.791 1.00 39.80  ? 127 LYS C CD  1 
ATOM   3148 C  CE  . LYS C 1 127 ? 62.334 51.765 64.417 1.00 42.27  ? 127 LYS C CE  1 
ATOM   3149 N  NZ  . LYS C 1 127 ? 63.161 50.674 65.030 1.00 41.64  ? 127 LYS C NZ  1 
ATOM   3150 N  N   . PHE C 1 128 ? 61.226 58.024 64.170 1.00 18.33  ? 128 PHE C N   1 
ATOM   3151 C  CA  . PHE C 1 128 ? 60.602 58.977 65.043 1.00 15.98  ? 128 PHE C CA  1 
ATOM   3152 C  C   . PHE C 1 128 ? 59.507 59.695 64.300 1.00 14.61  ? 128 PHE C C   1 
ATOM   3153 O  O   . PHE C 1 128 ? 58.367 59.671 64.755 1.00 14.87  ? 128 PHE C O   1 
ATOM   3154 C  CB  . PHE C 1 128 ? 61.601 59.995 65.560 1.00 16.03  ? 128 PHE C CB  1 
ATOM   3155 C  CG  . PHE C 1 128 ? 60.952 61.119 66.288 1.00 16.45  ? 128 PHE C CG  1 
ATOM   3156 C  CD1 . PHE C 1 128 ? 60.176 60.862 67.421 1.00 16.19  ? 128 PHE C CD1 1 
ATOM   3157 C  CD2 . PHE C 1 128 ? 61.051 62.427 65.820 1.00 16.49  ? 128 PHE C CD2 1 
ATOM   3158 C  CE1 . PHE C 1 128 ? 59.534 61.897 68.090 1.00 15.93  ? 128 PHE C CE1 1 
ATOM   3159 C  CE2 . PHE C 1 128 ? 60.404 63.462 66.487 1.00 16.33  ? 128 PHE C CE2 1 
ATOM   3160 C  CZ  . PHE C 1 128 ? 59.646 63.195 67.623 1.00 15.86  ? 128 PHE C CZ  1 
ATOM   3161 N  N   . LEU C 1 129 ? 59.853 60.332 63.173 1.00 13.08  ? 129 LEU C N   1 
ATOM   3162 C  CA  . LEU C 1 129 ? 58.877 61.079 62.343 1.00 12.11  ? 129 LEU C CA  1 
ATOM   3163 C  C   . LEU C 1 129 ? 57.712 60.231 61.891 1.00 12.27  ? 129 LEU C C   1 
ATOM   3164 O  O   . LEU C 1 129 ? 56.580 60.708 61.808 1.00 11.81  ? 129 LEU C O   1 
ATOM   3165 C  CB  . LEU C 1 129 ? 59.532 61.654 61.108 1.00 11.25  ? 129 LEU C CB  1 
ATOM   3166 C  CG  . LEU C 1 129 ? 60.415 62.851 61.397 1.00 11.04  ? 129 LEU C CG  1 
ATOM   3167 C  CD1 . LEU C 1 129 ? 61.245 63.184 60.169 1.00 10.97  ? 129 LEU C CD1 1 
ATOM   3168 C  CD2 . LEU C 1 129 ? 59.589 64.050 61.827 1.00 11.03  ? 129 LEU C CD2 1 
ATOM   3169 N  N   . ALA C 1 130 ? 58.008 58.967 61.603 1.00 12.93  ? 130 ALA C N   1 
ATOM   3170 C  CA  . ALA C 1 130 ? 56.994 57.984 61.234 1.00 13.31  ? 130 ALA C CA  1 
ATOM   3171 C  C   . ALA C 1 130 ? 56.003 57.672 62.353 1.00 13.41  ? 130 ALA C C   1 
ATOM   3172 O  O   . ALA C 1 130 ? 54.815 57.504 62.087 1.00 13.66  ? 130 ALA C O   1 
ATOM   3173 C  CB  . ALA C 1 130 ? 57.660 56.711 60.762 1.00 13.54  ? 130 ALA C CB  1 
ATOM   3174 N  N   . SER C 1 131 ? 56.489 57.571 63.586 1.00 13.90  ? 131 SER C N   1 
ATOM   3175 C  CA  . SER C 1 131 ? 55.604 57.409 64.743 1.00 14.43  ? 131 SER C CA  1 
ATOM   3176 C  C   . SER C 1 131 ? 54.682 58.598 64.874 1.00 14.02  ? 131 SER C C   1 
ATOM   3177 O  O   . SER C 1 131 ? 53.469 58.439 64.991 1.00 14.37  ? 131 SER C O   1 
ATOM   3178 C  CB  . SER C 1 131 ? 56.390 57.246 66.052 1.00 15.07  ? 131 SER C CB  1 
ATOM   3179 O  OG  . SER C 1 131 ? 56.966 55.953 66.123 1.00 15.97  ? 131 SER C OG  1 
ATOM   3180 N  N   . VAL C 1 132 ? 55.272 59.778 64.852 1.00 13.40  ? 132 VAL C N   1 
ATOM   3181 C  CA  . VAL C 1 132 ? 54.519 60.992 65.005 1.00 13.65  ? 132 VAL C CA  1 
ATOM   3182 C  C   . VAL C 1 132 ? 53.417 61.045 63.938 1.00 14.41  ? 132 VAL C C   1 
ATOM   3183 O  O   . VAL C 1 132 ? 52.268 61.374 64.256 1.00 14.62  ? 132 VAL C O   1 
ATOM   3184 C  CB  . VAL C 1 132 ? 55.456 62.228 64.955 1.00 13.62  ? 132 VAL C CB  1 
ATOM   3185 C  CG1 . VAL C 1 132 ? 54.700 63.548 64.786 1.00 13.56  ? 132 VAL C CG1 1 
ATOM   3186 C  CG2 . VAL C 1 132 ? 56.302 62.279 66.208 1.00 13.60  ? 132 VAL C CG2 1 
ATOM   3187 N  N   . SER C 1 133 ? 53.750 60.700 62.695 1.00 15.16  ? 133 SER C N   1 
ATOM   3188 C  CA  . SER C 1 133 ? 52.779 60.744 61.592 1.00 16.19  ? 133 SER C CA  1 
ATOM   3189 C  C   . SER C 1 133 ? 51.566 59.856 61.835 1.00 16.78  ? 133 SER C C   1 
ATOM   3190 O  O   . SER C 1 133 ? 50.447 60.201 61.467 1.00 16.68  ? 133 SER C O   1 
ATOM   3191 C  CB  . SER C 1 133 ? 53.439 60.300 60.288 1.00 17.10  ? 133 SER C CB  1 
ATOM   3192 O  OG  . SER C 1 133 ? 54.554 61.120 59.960 1.00 17.73  ? 133 SER C OG  1 
ATOM   3193 N  N   . THR C 1 134 ? 51.813 58.713 62.461 1.00 18.04  ? 134 THR C N   1 
ATOM   3194 C  CA  . THR C 1 134 ? 50.775 57.740 62.802 1.00 18.90  ? 134 THR C CA  1 
ATOM   3195 C  C   . THR C 1 134 ? 49.823 58.175 63.937 1.00 17.87  ? 134 THR C C   1 
ATOM   3196 O  O   . THR C 1 134 ? 48.624 57.894 63.885 1.00 17.77  ? 134 THR C O   1 
ATOM   3197 C  CB  . THR C 1 134 ? 51.434 56.394 63.148 1.00 20.54  ? 134 THR C CB  1 
ATOM   3198 O  OG1 . THR C 1 134 ? 52.200 55.943 62.011 1.00 20.95  ? 134 THR C OG1 1 
ATOM   3199 C  CG2 . THR C 1 134 ? 50.383 55.342 63.519 1.00 21.42  ? 134 THR C CG2 1 
ATOM   3200 N  N   . VAL C 1 135 ? 50.346 58.852 64.947 1.00 16.99  ? 135 VAL C N   1 
ATOM   3201 C  CA  . VAL C 1 135 ? 49.498 59.435 65.982 1.00 16.59  ? 135 VAL C CA  1 
ATOM   3202 C  C   . VAL C 1 135 ? 48.591 60.506 65.396 1.00 16.27  ? 135 VAL C C   1 
ATOM   3203 O  O   . VAL C 1 135 ? 47.407 60.527 65.704 1.00 16.62  ? 135 VAL C O   1 
ATOM   3204 C  CB  . VAL C 1 135 ? 50.326 60.049 67.129 1.00 16.77  ? 135 VAL C CB  1 
ATOM   3205 C  CG1 . VAL C 1 135 ? 49.457 60.861 68.083 1.00 16.58  ? 135 VAL C CG1 1 
ATOM   3206 C  CG2 . VAL C 1 135 ? 51.044 58.945 67.890 1.00 17.12  ? 135 VAL C CG2 1 
ATOM   3207 N  N   . LEU C 1 136 ? 49.127 61.393 64.570 1.00 15.93  ? 136 LEU C N   1 
ATOM   3208 C  CA  . LEU C 1 136 ? 48.303 62.464 64.041 1.00 16.64  ? 136 LEU C CA  1 
ATOM   3209 C  C   . LEU C 1 136 ? 47.297 62.038 62.975 1.00 18.11  ? 136 LEU C C   1 
ATOM   3210 O  O   . LEU C 1 136 ? 46.438 62.823 62.639 1.00 18.49  ? 136 LEU C O   1 
ATOM   3211 C  CB  . LEU C 1 136 ? 49.147 63.592 63.463 1.00 16.65  ? 136 LEU C CB  1 
ATOM   3212 C  CG  . LEU C 1 136 ? 50.239 64.242 64.308 1.00 16.76  ? 136 LEU C CG  1 
ATOM   3213 C  CD1 . LEU C 1 136 ? 50.794 65.437 63.562 1.00 16.81  ? 136 LEU C CD1 1 
ATOM   3214 C  CD2 . LEU C 1 136 ? 49.741 64.693 65.650 1.00 16.91  ? 136 LEU C CD2 1 
ATOM   3215 N  N   . THR C 1 137 ? 47.384 60.838 62.418 1.00 21.31  ? 137 THR C N   1 
ATOM   3216 C  CA  . THR C 1 137 ? 46.406 60.420 61.398 1.00 24.83  ? 137 THR C CA  1 
ATOM   3217 C  C   . THR C 1 137 ? 45.436 59.335 61.896 1.00 28.05  ? 137 THR C C   1 
ATOM   3218 O  O   . THR C 1 137 ? 45.006 58.461 61.122 1.00 29.42  ? 137 THR C O   1 
ATOM   3219 C  CB  . THR C 1 137 ? 47.116 59.906 60.125 1.00 26.22  ? 137 THR C CB  1 
ATOM   3220 O  OG1 . THR C 1 137 ? 48.059 58.878 60.469 1.00 27.57  ? 137 THR C OG1 1 
ATOM   3221 C  CG2 . THR C 1 137 ? 47.829 61.012 59.440 1.00 25.94  ? 137 THR C CG2 1 
ATOM   3222 N  N   . SER C 1 138 ? 45.075 59.393 63.172 1.00 29.04  ? 138 SER C N   1 
ATOM   3223 C  CA  . SER C 1 138 ? 44.172 58.409 63.747 1.00 30.02  ? 138 SER C CA  1 
ATOM   3224 C  C   . SER C 1 138 ? 43.210 59.024 64.737 1.00 33.82  ? 138 SER C C   1 
ATOM   3225 O  O   . SER C 1 138 ? 43.499 60.072 65.314 1.00 33.84  ? 138 SER C O   1 
ATOM   3226 C  CB  . SER C 1 138 ? 44.971 57.314 64.414 1.00 28.99  ? 138 SER C CB  1 
ATOM   3227 O  OG  . SER C 1 138 ? 45.881 57.859 65.341 1.00 29.47  ? 138 SER C OG  1 
ATOM   3228 N  N   . LYS C 1 139 ? 42.051 58.390 64.871 1.00 39.20  ? 139 LYS C N   1 
ATOM   3229 C  CA  . LYS C 1 139 ? 41.011 58.849 65.768 1.00 43.79  ? 139 LYS C CA  1 
ATOM   3230 C  C   . LYS C 1 139 ? 40.919 58.047 67.048 1.00 46.20  ? 139 LYS C C   1 
ATOM   3231 O  O   . LYS C 1 139 ? 40.310 56.988 67.090 1.00 49.37  ? 139 LYS C O   1 
ATOM   3232 C  CB  . LYS C 1 139 ? 39.656 58.791 65.069 1.00 46.47  ? 139 LYS C CB  1 
ATOM   3233 C  CG  . LYS C 1 139 ? 39.508 59.755 63.910 1.00 49.81  ? 139 LYS C CG  1 
ATOM   3234 C  CD  . LYS C 1 139 ? 38.144 59.609 63.264 1.00 56.36  ? 139 LYS C CD  1 
ATOM   3235 C  CE  . LYS C 1 139 ? 37.960 60.582 62.115 1.00 62.59  ? 139 LYS C CE  1 
ATOM   3236 N  NZ  . LYS C 1 139 ? 36.626 60.411 61.475 1.00 63.66  ? 139 LYS C NZ  1 
ATOM   3237 N  N   . TYR C 1 140 ? 41.567 58.556 68.081 1.00 50.50  ? 140 TYR C N   1 
ATOM   3238 C  CA  . TYR C 1 140 ? 41.562 57.946 69.393 1.00 59.01  ? 140 TYR C CA  1 
ATOM   3239 C  C   . TYR C 1 140 ? 41.277 59.046 70.407 1.00 81.91  ? 140 TYR C C   1 
ATOM   3240 O  O   . TYR C 1 140 ? 41.673 60.196 70.203 1.00 94.52  ? 140 TYR C O   1 
ATOM   3241 C  CB  . TYR C 1 140 ? 42.903 57.280 69.680 1.00 54.86  ? 140 TYR C CB  1 
ATOM   3242 C  CG  . TYR C 1 140 ? 44.019 58.262 69.929 1.00 53.41  ? 140 TYR C CG  1 
ATOM   3243 C  CD1 . TYR C 1 140 ? 44.541 59.020 68.896 1.00 55.02  ? 140 TYR C CD1 1 
ATOM   3244 C  CD2 . TYR C 1 140 ? 44.544 58.437 71.197 1.00 51.99  ? 140 TYR C CD2 1 
ATOM   3245 C  CE1 . TYR C 1 140 ? 45.555 59.924 69.118 1.00 53.81  ? 140 TYR C CE1 1 
ATOM   3246 C  CE2 . TYR C 1 140 ? 45.558 59.341 71.428 1.00 52.73  ? 140 TYR C CE2 1 
ATOM   3247 C  CZ  . TYR C 1 140 ? 46.059 60.079 70.383 1.00 53.45  ? 140 TYR C CZ  1 
ATOM   3248 O  OH  . TYR C 1 140 ? 47.071 60.978 70.608 1.00 53.56  ? 140 TYR C OH  1 
ATOM   3249 N  N   . ARG C 1 141 ? 40.592 58.700 71.493 1.00 106.31 ? 141 ARG C N   1 
ATOM   3250 C  CA  . ARG C 1 141 ? 39.892 59.684 72.316 1.00 127.13 ? 141 ARG C CA  1 
ATOM   3251 C  C   . ARG C 1 141 ? 39.177 60.714 71.445 1.00 134.27 ? 141 ARG C C   1 
ATOM   3252 O  O   . ARG C 1 141 ? 39.045 61.883 71.803 1.00 137.78 ? 141 ARG C O   1 
ATOM   3253 C  CB  . ARG C 1 141 ? 40.842 60.384 73.300 1.00 145.76 ? 141 ARG C CB  1 
ATOM   3254 C  CG  . ARG C 1 141 ? 42.088 59.591 73.660 1.00 162.48 ? 141 ARG C CG  1 
ATOM   3255 C  CD  . ARG C 1 141 ? 43.028 60.412 74.526 1.00 178.92 ? 141 ARG C CD  1 
ATOM   3256 N  NE  . ARG C 1 141 ? 44.297 59.731 74.770 1.00 194.31 ? 141 ARG C NE  1 
ATOM   3257 C  CZ  . ARG C 1 141 ? 44.416 58.438 75.059 1.00 205.49 ? 141 ARG C CZ  1 
ATOM   3258 N  NH1 . ARG C 1 141 ? 43.339 57.670 75.140 1.00 208.68 ? 141 ARG C NH1 1 
ATOM   3259 N  NH2 . ARG C 1 141 ? 45.615 57.912 75.267 1.00 204.39 ? 141 ARG C NH2 1 
ATOM   3260 O  OXT . ARG C 1 141 ? 38.717 60.394 70.351 1.00 135.83 ? 141 ARG C OXT 1 
ATOM   3261 N  N   . VAL D 2 1   ? 59.594 62.749 30.972 1.00 154.45 ? 1   VAL D N   1 
ATOM   3262 C  CA  . VAL D 2 1   ? 59.315 63.685 32.103 1.00 148.35 ? 1   VAL D CA  1 
ATOM   3263 C  C   . VAL D 2 1   ? 59.582 65.137 31.676 1.00 149.88 ? 1   VAL D C   1 
ATOM   3264 O  O   . VAL D 2 1   ? 60.620 65.439 31.082 1.00 148.39 ? 1   VAL D O   1 
ATOM   3265 C  CB  . VAL D 2 1   ? 60.107 63.287 33.380 1.00 141.23 ? 1   VAL D CB  1 
ATOM   3266 C  CG1 . VAL D 2 1   ? 61.612 63.257 33.135 1.00 134.33 ? 1   VAL D CG1 1 
ATOM   3267 C  CG2 . VAL D 2 1   ? 59.761 64.204 34.546 1.00 148.67 ? 1   VAL D CG2 1 
ATOM   3268 N  N   . HIS D 2 2   ? 58.634 66.023 31.979 1.00 156.38 ? 2   HIS D N   1 
ATOM   3269 C  CA  . HIS D 2 2   ? 58.652 67.395 31.466 1.00 167.43 ? 2   HIS D CA  1 
ATOM   3270 C  C   . HIS D 2 2   ? 59.520 68.314 32.318 1.00 149.89 ? 2   HIS D C   1 
ATOM   3271 O  O   . HIS D 2 2   ? 59.094 68.766 33.384 1.00 152.24 ? 2   HIS D O   1 
ATOM   3272 C  CB  . HIS D 2 2   ? 57.231 67.959 31.400 1.00 201.89 ? 2   HIS D CB  1 
ATOM   3273 C  CG  . HIS D 2 2   ? 56.317 67.186 30.502 1.00 241.50 ? 2   HIS D CG  1 
ATOM   3274 N  ND1 . HIS D 2 2   ? 56.384 67.265 29.128 1.00 265.50 ? 2   HIS D ND1 1 
ATOM   3275 C  CD2 . HIS D 2 2   ? 55.313 66.322 30.781 1.00 265.78 ? 2   HIS D CD2 1 
ATOM   3276 C  CE1 . HIS D 2 2   ? 55.462 66.481 28.599 1.00 282.59 ? 2   HIS D CE1 1 
ATOM   3277 N  NE2 . HIS D 2 2   ? 54.798 65.898 29.581 1.00 278.70 ? 2   HIS D NE2 1 
ATOM   3278 N  N   . LEU D 2 3   ? 60.736 68.582 31.844 1.00 130.91 ? 3   LEU D N   1 
ATOM   3279 C  CA  . LEU D 2 3   ? 61.627 69.554 32.480 1.00 119.59 ? 3   LEU D CA  1 
ATOM   3280 C  C   . LEU D 2 3   ? 61.790 70.776 31.580 1.00 122.23 ? 3   LEU D C   1 
ATOM   3281 O  O   . LEU D 2 3   ? 61.897 70.649 30.357 1.00 121.07 ? 3   LEU D O   1 
ATOM   3282 C  CB  . LEU D 2 3   ? 63.000 68.936 32.784 1.00 109.28 ? 3   LEU D CB  1 
ATOM   3283 C  CG  . LEU D 2 3   ? 63.132 68.149 34.093 1.00 99.55  ? 3   LEU D CG  1 
ATOM   3284 C  CD1 . LEU D 2 3   ? 62.581 66.740 33.944 1.00 98.23  ? 3   LEU D CD1 1 
ATOM   3285 C  CD2 . LEU D 2 3   ? 64.581 68.097 34.548 1.00 96.36  ? 3   LEU D CD2 1 
ATOM   3286 N  N   . THR D 2 4   ? 61.803 71.954 32.199 1.00 128.08 ? 4   THR D N   1 
ATOM   3287 C  CA  . THR D 2 4   ? 62.127 73.198 31.510 1.00 137.05 ? 4   THR D CA  1 
ATOM   3288 C  C   . THR D 2 4   ? 63.649 73.327 31.380 1.00 147.31 ? 4   THR D C   1 
ATOM   3289 O  O   . THR D 2 4   ? 64.382 72.654 32.112 1.00 160.52 ? 4   THR D O   1 
ATOM   3290 C  CB  . THR D 2 4   ? 61.590 74.415 32.280 1.00 142.90 ? 4   THR D CB  1 
ATOM   3291 O  OG1 . THR D 2 4   ? 62.126 74.420 33.609 1.00 146.48 ? 4   THR D OG1 1 
ATOM   3292 C  CG2 . THR D 2 4   ? 60.074 74.368 32.352 1.00 149.43 ? 4   THR D CG2 1 
ATOM   3293 N  N   . PRO D 2 5   ? 64.137 74.192 30.464 1.00 152.69 ? 5   PRO D N   1 
ATOM   3294 C  CA  . PRO D 2 5   ? 65.593 74.386 30.303 1.00 155.23 ? 5   PRO D CA  1 
ATOM   3295 C  C   . PRO D 2 5   ? 66.350 74.931 31.524 1.00 156.22 ? 5   PRO D C   1 
ATOM   3296 O  O   . PRO D 2 5   ? 67.568 74.765 31.602 1.00 157.10 ? 5   PRO D O   1 
ATOM   3297 C  CB  . PRO D 2 5   ? 65.689 75.384 29.145 1.00 156.72 ? 5   PRO D CB  1 
ATOM   3298 C  CG  . PRO D 2 5   ? 64.422 75.204 28.390 1.00 160.11 ? 5   PRO D CG  1 
ATOM   3299 C  CD  . PRO D 2 5   ? 63.385 74.930 29.433 1.00 154.72 ? 5   PRO D CD  1 
ATOM   3300 N  N   . GLU D 2 6   ? 65.641 75.573 32.452 1.00 153.76 ? 6   GLU D N   1 
ATOM   3301 C  CA  . GLU D 2 6   ? 66.237 76.058 33.700 1.00 155.90 ? 6   GLU D CA  1 
ATOM   3302 C  C   . GLU D 2 6   ? 66.441 74.912 34.686 1.00 142.81 ? 6   GLU D C   1 
ATOM   3303 O  O   . GLU D 2 6   ? 67.474 74.839 35.354 1.00 138.44 ? 6   GLU D O   1 
ATOM   3304 C  CB  . GLU D 2 6   ? 65.368 77.143 34.344 1.00 174.66 ? 6   GLU D CB  1 
ATOM   3305 C  CG  . GLU D 2 6   ? 65.341 78.468 33.584 1.00 194.32 ? 6   GLU D CG  1 
ATOM   3306 C  CD  . GLU D 2 6   ? 64.391 78.494 32.391 1.00 207.02 ? 6   GLU D CD  1 
ATOM   3307 O  OE1 . GLU D 2 6   ? 63.809 77.444 32.035 1.00 206.92 ? 6   GLU D OE1 1 
ATOM   3308 O  OE2 . GLU D 2 6   ? 64.228 79.581 31.797 1.00 217.41 ? 6   GLU D OE2 1 
ATOM   3309 N  N   . GLU D 2 7   ? 65.445 74.034 34.786 1.00 133.41 ? 7   GLU D N   1 
ATOM   3310 C  CA  . GLU D 2 7   ? 65.547 72.834 35.619 1.00 130.70 ? 7   GLU D CA  1 
ATOM   3311 C  C   . GLU D 2 7   ? 66.614 71.883 35.087 1.00 116.68 ? 7   GLU D C   1 
ATOM   3312 O  O   . GLU D 2 7   ? 67.452 71.402 35.850 1.00 113.18 ? 7   GLU D O   1 
ATOM   3313 C  CB  . GLU D 2 7   ? 64.196 72.114 35.723 1.00 145.09 ? 7   GLU D CB  1 
ATOM   3314 C  CG  . GLU D 2 7   ? 63.167 72.851 36.576 1.00 158.25 ? 7   GLU D CG  1 
ATOM   3315 C  CD  . GLU D 2 7   ? 61.892 72.052 36.822 1.00 167.20 ? 7   GLU D CD  1 
ATOM   3316 O  OE1 . GLU D 2 7   ? 61.590 71.123 36.039 1.00 169.89 ? 7   GLU D OE1 1 
ATOM   3317 O  OE2 . GLU D 2 7   ? 61.180 72.363 37.802 1.00 168.85 ? 7   GLU D OE2 1 
ATOM   3318 N  N   . LYS D 2 8   ? 66.587 71.629 33.782 1.00 114.18 ? 8   LYS D N   1 
ATOM   3319 C  CA  . LYS D 2 8   ? 67.580 70.763 33.147 1.00 121.07 ? 8   LYS D CA  1 
ATOM   3320 C  C   . LYS D 2 8   ? 69.005 71.331 33.246 1.00 118.16 ? 8   LYS D C   1 
ATOM   3321 O  O   . LYS D 2 8   ? 69.964 70.564 33.335 1.00 115.55 ? 8   LYS D O   1 
ATOM   3322 C  CB  . LYS D 2 8   ? 67.212 70.487 31.686 1.00 132.60 ? 8   LYS D CB  1 
ATOM   3323 C  CG  . LYS D 2 8   ? 67.974 69.324 31.067 1.00 150.65 ? 8   LYS D CG  1 
ATOM   3324 C  CD  . LYS D 2 8   ? 67.574 69.096 29.618 1.00 172.23 ? 8   LYS D CD  1 
ATOM   3325 C  CE  . LYS D 2 8   ? 68.510 68.112 28.928 1.00 188.20 ? 8   LYS D CE  1 
ATOM   3326 N  NZ  . LYS D 2 8   ? 68.205 67.955 27.477 1.00 194.59 ? 8   LYS D NZ  1 
ATOM   3327 N  N   . SER D 2 9   ? 69.143 72.658 33.236 1.00 123.24 ? 9   SER D N   1 
ATOM   3328 C  CA  . SER D 2 9   ? 70.445 73.295 33.477 1.00 132.85 ? 9   SER D CA  1 
ATOM   3329 C  C   . SER D 2 9   ? 70.929 73.055 34.911 1.00 132.75 ? 9   SER D C   1 
ATOM   3330 O  O   . SER D 2 9   ? 72.111 72.774 35.131 1.00 135.97 ? 9   SER D O   1 
ATOM   3331 C  CB  . SER D 2 9   ? 70.401 74.802 33.183 1.00 138.50 ? 9   SER D CB  1 
ATOM   3332 O  OG  . SER D 2 9   ? 69.573 75.499 34.098 1.00 134.37 ? 9   SER D OG  1 
ATOM   3333 N  N   . ALA D 2 10  ? 70.012 73.169 35.871 1.00 120.28 ? 10  ALA D N   1 
ATOM   3334 C  CA  . ALA D 2 10  ? 70.321 72.928 37.282 1.00 108.40 ? 10  ALA D CA  1 
ATOM   3335 C  C   . ALA D 2 10  ? 70.701 71.471 37.538 1.00 94.16  ? 10  ALA D C   1 
ATOM   3336 O  O   . ALA D 2 10  ? 71.699 71.196 38.208 1.00 96.20  ? 10  ALA D O   1 
ATOM   3337 C  CB  . ALA D 2 10  ? 69.144 73.329 38.159 1.00 110.75 ? 10  ALA D CB  1 
ATOM   3338 N  N   . VAL D 2 11  ? 69.905 70.552 36.998 1.00 76.33  ? 11  VAL D N   1 
ATOM   3339 C  CA  . VAL D 2 11  ? 70.163 69.122 37.123 1.00 69.06  ? 11  VAL D CA  1 
ATOM   3340 C  C   . VAL D 2 11  ? 71.569 68.794 36.632 1.00 69.54  ? 11  VAL D C   1 
ATOM   3341 O  O   . VAL D 2 11  ? 72.359 68.223 37.371 1.00 70.95  ? 11  VAL D O   1 
ATOM   3342 C  CB  . VAL D 2 11  ? 69.115 68.295 36.340 1.00 68.26  ? 11  VAL D CB  1 
ATOM   3343 C  CG1 . VAL D 2 11  ? 69.551 66.850 36.153 1.00 67.99  ? 11  VAL D CG1 1 
ATOM   3344 C  CG2 . VAL D 2 11  ? 67.767 68.337 37.042 1.00 69.52  ? 11  VAL D CG2 1 
ATOM   3345 N  N   . THR D 2 12  ? 71.876 69.176 35.396 1.00 77.55  ? 12  THR D N   1 
ATOM   3346 C  CA  . THR D 2 12  ? 73.168 68.848 34.776 1.00 85.94  ? 12  THR D CA  1 
ATOM   3347 C  C   . THR D 2 12  ? 74.371 69.519 35.439 1.00 86.77  ? 12  THR D C   1 
ATOM   3348 O  O   . THR D 2 12  ? 75.464 68.948 35.449 1.00 84.06  ? 12  THR D O   1 
ATOM   3349 C  CB  . THR D 2 12  ? 73.185 69.215 33.279 1.00 96.67  ? 12  THR D CB  1 
ATOM   3350 O  OG1 . THR D 2 12  ? 72.687 70.550 33.102 1.00 98.13  ? 12  THR D OG1 1 
ATOM   3351 C  CG2 . THR D 2 12  ? 72.334 68.230 32.476 1.00 100.11 ? 12  THR D CG2 1 
ATOM   3352 N  N   . ALA D 2 13  ? 74.168 70.725 35.973 1.00 89.59  ? 13  ALA D N   1 
ATOM   3353 C  CA  . ALA D 2 13  ? 75.236 71.479 36.641 1.00 91.01  ? 13  ALA D CA  1 
ATOM   3354 C  C   . ALA D 2 13  ? 75.656 70.818 37.954 1.00 89.30  ? 13  ALA D C   1 
ATOM   3355 O  O   . ALA D 2 13  ? 76.839 70.535 38.162 1.00 88.01  ? 13  ALA D O   1 
ATOM   3356 C  CB  . ALA D 2 13  ? 74.798 72.915 36.891 1.00 90.30  ? 13  ALA D CB  1 
ATOM   3357 N  N   . LEU D 2 14  ? 74.681 70.576 38.830 1.00 83.59  ? 14  LEU D N   1 
ATOM   3358 C  CA  . LEU D 2 14  ? 74.945 69.902 40.101 1.00 79.12  ? 14  LEU D CA  1 
ATOM   3359 C  C   . LEU D 2 14  ? 75.225 68.432 39.938 1.00 72.79  ? 14  LEU D C   1 
ATOM   3360 O  O   . LEU D 2 14  ? 75.791 67.843 40.841 1.00 80.81  ? 14  LEU D O   1 
ATOM   3361 C  CB  . LEU D 2 14  ? 73.809 70.082 41.109 1.00 87.09  ? 14  LEU D CB  1 
ATOM   3362 C  CG  . LEU D 2 14  ? 73.947 71.341 41.968 1.00 103.14 ? 14  LEU D CG  1 
ATOM   3363 C  CD1 . LEU D 2 14  ? 73.608 72.590 41.153 1.00 109.87 ? 14  LEU D CD1 1 
ATOM   3364 C  CD2 . LEU D 2 14  ? 73.086 71.241 43.228 1.00 110.45 ? 14  LEU D CD2 1 
ATOM   3365 N  N   . TRP D 2 15  ? 74.824 67.822 38.825 1.00 70.20  ? 15  TRP D N   1 
ATOM   3366 C  CA  . TRP D 2 15  ? 75.240 66.447 38.550 1.00 70.32  ? 15  TRP D CA  1 
ATOM   3367 C  C   . TRP D 2 15  ? 76.684 66.398 38.097 1.00 73.73  ? 15  TRP D C   1 
ATOM   3368 O  O   . TRP D 2 15  ? 77.395 65.439 38.396 1.00 71.75  ? 15  TRP D O   1 
ATOM   3369 C  CB  . TRP D 2 15  ? 74.377 65.773 37.495 1.00 70.07  ? 15  TRP D CB  1 
ATOM   3370 C  CG  . TRP D 2 15  ? 74.682 64.324 37.430 1.00 68.02  ? 15  TRP D CG  1 
ATOM   3371 C  CD1 . TRP D 2 15  ? 75.476 63.691 36.525 1.00 70.37  ? 15  TRP D CD1 1 
ATOM   3372 C  CD2 . TRP D 2 15  ? 74.251 63.331 38.352 1.00 64.68  ? 15  TRP D CD2 1 
ATOM   3373 N  NE1 . TRP D 2 15  ? 75.541 62.351 36.809 1.00 69.19  ? 15  TRP D NE1 1 
ATOM   3374 C  CE2 . TRP D 2 15  ? 74.796 62.105 37.931 1.00 66.23  ? 15  TRP D CE2 1 
ATOM   3375 C  CE3 . TRP D 2 15  ? 73.438 63.355 39.487 1.00 65.47  ? 15  TRP D CE3 1 
ATOM   3376 C  CZ2 . TRP D 2 15  ? 74.561 60.913 38.609 1.00 67.86  ? 15  TRP D CZ2 1 
ATOM   3377 C  CZ3 . TRP D 2 15  ? 73.204 62.167 40.161 1.00 69.37  ? 15  TRP D CZ3 1 
ATOM   3378 C  CH2 . TRP D 2 15  ? 73.766 60.964 39.720 1.00 68.30  ? 15  TRP D CH2 1 
ATOM   3379 N  N   . GLY D 2 16  ? 77.103 67.418 37.354 1.00 84.20  ? 16  GLY D N   1 
ATOM   3380 C  CA  . GLY D 2 16  ? 78.497 67.567 36.947 1.00 95.38  ? 16  GLY D CA  1 
ATOM   3381 C  C   . GLY D 2 16  ? 79.495 67.637 38.096 1.00 100.66 ? 16  GLY D C   1 
ATOM   3382 O  O   . GLY D 2 16  ? 80.634 67.187 37.952 1.00 106.13 ? 16  GLY D O   1 
ATOM   3383 N  N   . LYS D 2 17  ? 79.072 68.194 39.233 1.00 100.70 ? 17  LYS D N   1 
ATOM   3384 C  CA  . LYS D 2 17  ? 79.928 68.307 40.422 1.00 104.41 ? 17  LYS D CA  1 
ATOM   3385 C  C   . LYS D 2 17  ? 79.966 67.055 41.320 1.00 95.68  ? 17  LYS D C   1 
ATOM   3386 O  O   . LYS D 2 17  ? 80.757 67.007 42.265 1.00 93.19  ? 17  LYS D O   1 
ATOM   3387 C  CB  . LYS D 2 17  ? 79.496 69.514 41.262 1.00 119.64 ? 17  LYS D CB  1 
ATOM   3388 C  CG  . LYS D 2 17  ? 79.575 70.843 40.529 1.00 131.73 ? 17  LYS D CG  1 
ATOM   3389 C  CD  . LYS D 2 17  ? 79.270 72.006 41.459 1.00 142.58 ? 17  LYS D CD  1 
ATOM   3390 C  CE  . LYS D 2 17  ? 79.534 73.340 40.779 1.00 153.32 ? 17  LYS D CE  1 
ATOM   3391 N  NZ  . LYS D 2 17  ? 79.270 74.496 41.680 1.00 160.16 ? 17  LYS D NZ  1 
ATOM   3392 N  N   . VAL D 2 18  ? 79.128 66.055 41.029 1.00 91.61  ? 18  VAL D N   1 
ATOM   3393 C  CA  . VAL D 2 18  ? 79.031 64.840 41.849 1.00 91.14  ? 18  VAL D CA  1 
ATOM   3394 C  C   . VAL D 2 18  ? 80.314 64.037 41.724 1.00 96.85  ? 18  VAL D C   1 
ATOM   3395 O  O   . VAL D 2 18  ? 80.813 63.835 40.615 1.00 104.95 ? 18  VAL D O   1 
ATOM   3396 C  CB  . VAL D 2 18  ? 77.856 63.927 41.399 1.00 92.02  ? 18  VAL D CB  1 
ATOM   3397 C  CG1 . VAL D 2 18  ? 77.884 62.573 42.102 1.00 89.74  ? 18  VAL D CG1 1 
ATOM   3398 C  CG2 . VAL D 2 18  ? 76.515 64.599 41.641 1.00 96.00  ? 18  VAL D CG2 1 
ATOM   3399 N  N   . ASN D 2 19  ? 80.841 63.576 42.854 1.00 101.50 ? 19  ASN D N   1 
ATOM   3400 C  CA  . ASN D 2 19  ? 81.934 62.611 42.845 1.00 106.05 ? 19  ASN D CA  1 
ATOM   3401 C  C   . ASN D 2 19  ? 81.336 61.220 42.651 1.00 108.45 ? 19  ASN D C   1 
ATOM   3402 O  O   . ASN D 2 19  ? 80.828 60.611 43.596 1.00 102.07 ? 19  ASN D O   1 
ATOM   3403 C  CB  . ASN D 2 19  ? 82.737 62.681 44.141 1.00 114.47 ? 19  ASN D CB  1 
ATOM   3404 C  CG  . ASN D 2 19  ? 83.915 61.721 44.155 1.00 122.98 ? 19  ASN D CG  1 
ATOM   3405 O  OD1 . ASN D 2 19  ? 84.376 61.249 43.110 1.00 122.61 ? 19  ASN D OD1 1 
ATOM   3406 N  ND2 . ASN D 2 19  ? 84.417 61.431 45.350 1.00 135.46 ? 19  ASN D ND2 1 
ATOM   3407 N  N   . VAL D 2 20  ? 81.433 60.708 41.425 1.00 117.35 ? 20  VAL D N   1 
ATOM   3408 C  CA  . VAL D 2 20  ? 80.736 59.470 41.029 1.00 119.94 ? 20  VAL D CA  1 
ATOM   3409 C  C   . VAL D 2 20  ? 81.388 58.158 41.507 1.00 118.12 ? 20  VAL D C   1 
ATOM   3410 O  O   . VAL D 2 20  ? 81.110 57.092 40.953 1.00 119.77 ? 20  VAL D O   1 
ATOM   3411 C  CB  . VAL D 2 20  ? 80.501 59.421 39.493 1.00 122.55 ? 20  VAL D CB  1 
ATOM   3412 C  CG1 . VAL D 2 20  ? 79.545 60.530 39.072 1.00 121.71 ? 20  VAL D CG1 1 
ATOM   3413 C  CG2 . VAL D 2 20  ? 81.815 59.494 38.711 1.00 123.85 ? 20  VAL D CG2 1 
ATOM   3414 N  N   . ASP D 2 21  ? 82.251 58.237 42.519 1.00 121.74 ? 21  ASP D N   1 
ATOM   3415 C  CA  . ASP D 2 21  ? 82.774 57.059 43.205 1.00 130.14 ? 21  ASP D CA  1 
ATOM   3416 C  C   . ASP D 2 21  ? 82.038 56.793 44.523 1.00 125.71 ? 21  ASP D C   1 
ATOM   3417 O  O   . ASP D 2 21  ? 81.618 55.662 44.790 1.00 123.42 ? 21  ASP D O   1 
ATOM   3418 C  CB  . ASP D 2 21  ? 84.264 57.247 43.490 1.00 142.43 ? 21  ASP D CB  1 
ATOM   3419 C  CG  . ASP D 2 21  ? 84.909 56.001 44.072 1.00 154.84 ? 21  ASP D CG  1 
ATOM   3420 O  OD1 . ASP D 2 21  ? 85.071 55.014 43.323 1.00 167.12 ? 21  ASP D OD1 1 
ATOM   3421 O  OD2 . ASP D 2 21  ? 85.254 56.009 45.274 1.00 153.38 ? 21  ASP D OD2 1 
ATOM   3422 N  N   . GLU D 2 22  ? 81.890 57.838 45.337 1.00 116.67 ? 22  GLU D N   1 
ATOM   3423 C  CA  . GLU D 2 22  ? 81.440 57.702 46.724 1.00 107.19 ? 22  GLU D CA  1 
ATOM   3424 C  C   . GLU D 2 22  ? 79.927 57.799 46.910 1.00 82.58  ? 22  GLU D C   1 
ATOM   3425 O  O   . GLU D 2 22  ? 79.375 57.170 47.812 1.00 78.51  ? 22  GLU D O   1 
ATOM   3426 C  CB  . GLU D 2 22  ? 82.133 58.766 47.586 1.00 125.26 ? 22  GLU D CB  1 
ATOM   3427 C  CG  . GLU D 2 22  ? 82.157 58.465 49.081 1.00 146.84 ? 22  GLU D CG  1 
ATOM   3428 C  CD  . GLU D 2 22  ? 82.900 57.181 49.438 1.00 161.96 ? 22  GLU D CD  1 
ATOM   3429 O  OE1 . GLU D 2 22  ? 83.880 56.832 48.742 1.00 173.18 ? 22  GLU D OE1 1 
ATOM   3430 O  OE2 . GLU D 2 22  ? 82.502 56.517 50.422 1.00 165.61 ? 22  GLU D OE2 1 
ATOM   3431 N  N   . VAL D 2 23  ? 79.268 58.576 46.059 1.00 65.25  ? 23  VAL D N   1 
ATOM   3432 C  CA  . VAL D 2 23  ? 77.843 58.847 46.204 1.00 57.53  ? 23  VAL D CA  1 
ATOM   3433 C  C   . VAL D 2 23  ? 77.005 57.573 46.149 1.00 56.73  ? 23  VAL D C   1 
ATOM   3434 O  O   . VAL D 2 23  ? 76.215 57.318 47.062 1.00 59.62  ? 23  VAL D O   1 
ATOM   3435 C  CB  . VAL D 2 23  ? 77.370 59.868 45.152 1.00 54.45  ? 23  VAL D CB  1 
ATOM   3436 C  CG1 . VAL D 2 23  ? 75.850 59.971 45.094 1.00 53.21  ? 23  VAL D CG1 1 
ATOM   3437 C  CG2 . VAL D 2 23  ? 77.972 61.221 45.477 1.00 57.24  ? 23  VAL D CG2 1 
ATOM   3438 N  N   . GLY D 2 24  ? 77.181 56.779 45.095 1.00 54.28  ? 24  GLY D N   1 
ATOM   3439 C  CA  . GLY D 2 24  ? 76.501 55.481 44.978 1.00 52.39  ? 24  GLY D CA  1 
ATOM   3440 C  C   . GLY D 2 24  ? 76.753 54.541 46.157 1.00 50.21  ? 24  GLY D C   1 
ATOM   3441 O  O   . GLY D 2 24  ? 75.849 53.824 46.601 1.00 48.31  ? 24  GLY D O   1 
ATOM   3442 N  N   . GLY D 2 25  ? 77.989 54.551 46.655 1.00 47.33  ? 25  GLY D N   1 
ATOM   3443 C  CA  . GLY D 2 25  ? 78.368 53.780 47.825 1.00 44.83  ? 25  GLY D CA  1 
ATOM   3444 C  C   . GLY D 2 25  ? 77.676 54.249 49.083 1.00 43.95  ? 25  GLY D C   1 
ATOM   3445 O  O   . GLY D 2 25  ? 77.278 53.432 49.908 1.00 44.96  ? 25  GLY D O   1 
ATOM   3446 N  N   . GLU D 2 26  ? 77.542 55.562 49.236 1.00 44.86  ? 26  GLU D N   1 
ATOM   3447 C  CA  . GLU D 2 26  ? 76.833 56.121 50.377 1.00 46.67  ? 26  GLU D CA  1 
ATOM   3448 C  C   . GLU D 2 26  ? 75.363 55.855 50.260 1.00 39.03  ? 26  GLU D C   1 
ATOM   3449 O  O   . GLU D 2 26  ? 74.762 55.364 51.212 1.00 40.02  ? 26  GLU D O   1 
ATOM   3450 C  CB  . GLU D 2 26  ? 77.061 57.622 50.507 1.00 62.30  ? 26  GLU D CB  1 
ATOM   3451 C  CG  . GLU D 2 26  ? 78.394 57.964 51.158 1.00 81.80  ? 26  GLU D CG  1 
ATOM   3452 C  CD  . GLU D 2 26  ? 78.711 59.457 51.184 1.00 95.99  ? 26  GLU D CD  1 
ATOM   3453 O  OE1 . GLU D 2 26  ? 77.864 60.272 50.752 1.00 106.10 ? 26  GLU D OE1 1 
ATOM   3454 O  OE2 . GLU D 2 26  ? 79.821 59.817 51.646 1.00 101.61 ? 26  GLU D OE2 1 
ATOM   3455 N  N   . ALA D 2 27  ? 74.787 56.166 49.098 1.00 32.73  ? 27  ALA D N   1 
ATOM   3456 C  CA  . ALA D 2 27  ? 73.339 56.022 48.897 1.00 29.64  ? 27  ALA D CA  1 
ATOM   3457 C  C   . ALA D 2 27  ? 72.874 54.604 49.190 1.00 26.36  ? 27  ALA D C   1 
ATOM   3458 O  O   . ALA D 2 27  ? 72.010 54.385 50.033 1.00 27.01  ? 27  ALA D O   1 
ATOM   3459 C  CB  . ALA D 2 27  ? 72.931 56.433 47.498 1.00 29.46  ? 27  ALA D CB  1 
ATOM   3460 N  N   . LEU D 2 28  ? 73.477 53.642 48.525 1.00 23.76  ? 28  LEU D N   1 
ATOM   3461 C  CA  . LEU D 2 28  ? 73.149 52.259 48.785 1.00 22.63  ? 28  LEU D CA  1 
ATOM   3462 C  C   . LEU D 2 28  ? 73.526 51.798 50.222 1.00 20.93  ? 28  LEU D C   1 
ATOM   3463 O  O   . LEU D 2 28  ? 72.903 50.890 50.776 1.00 20.94  ? 28  LEU D O   1 
ATOM   3464 C  CB  . LEU D 2 28  ? 73.835 51.383 47.755 1.00 23.22  ? 28  LEU D CB  1 
ATOM   3465 C  CG  . LEU D 2 28  ? 73.319 49.953 47.797 1.00 24.52  ? 28  LEU D CG  1 
ATOM   3466 C  CD1 . LEU D 2 28  ? 71.969 49.878 47.093 1.00 25.68  ? 28  LEU D CD1 1 
ATOM   3467 C  CD2 . LEU D 2 28  ? 74.344 49.018 47.193 1.00 24.80  ? 28  LEU D CD2 1 
ATOM   3468 N  N   . GLY D 2 29  ? 74.549 52.398 50.813 1.00 18.44  ? 29  GLY D N   1 
ATOM   3469 C  CA  . GLY D 2 29  ? 74.883 52.112 52.195 1.00 16.81  ? 29  GLY D CA  1 
ATOM   3470 C  C   . GLY D 2 29  ? 73.761 52.568 53.113 1.00 15.80  ? 29  GLY D C   1 
ATOM   3471 O  O   . GLY D 2 29  ? 73.359 51.819 54.014 1.00 16.64  ? 29  GLY D O   1 
ATOM   3472 N  N   . ARG D 2 30  ? 73.247 53.785 52.899 1.00 13.17  ? 30  ARG D N   1 
ATOM   3473 C  CA  . ARG D 2 30  ? 72.173 54.304 53.752 1.00 11.27  ? 30  ARG D CA  1 
ATOM   3474 C  C   . ARG D 2 30  ? 70.928 53.477 53.618 1.00 8.06   ? 30  ARG D C   1 
ATOM   3475 O  O   . ARG D 2 30  ? 70.254 53.238 54.620 1.00 8.00   ? 30  ARG D O   1 
ATOM   3476 C  CB  . ARG D 2 30  ? 71.860 55.771 53.481 1.00 13.58  ? 30  ARG D CB  1 
ATOM   3477 C  CG  . ARG D 2 30  ? 72.738 56.644 54.331 1.00 16.80  ? 30  ARG D CG  1 
ATOM   3478 C  CD  . ARG D 2 30  ? 72.679 58.121 53.993 1.00 20.66  ? 30  ARG D CD  1 
ATOM   3479 N  NE  . ARG D 2 30  ? 73.808 58.784 54.666 1.00 24.61  ? 30  ARG D NE  1 
ATOM   3480 C  CZ  . ARG D 2 30  ? 73.849 59.157 55.950 1.00 27.10  ? 30  ARG D CZ  1 
ATOM   3481 N  NH1 . ARG D 2 30  ? 72.804 58.999 56.747 1.00 28.26  ? 30  ARG D NH1 1 
ATOM   3482 N  NH2 . ARG D 2 30  ? 74.950 59.722 56.440 1.00 29.01  ? 30  ARG D NH2 1 
ATOM   3483 N  N   . LEU D 2 31  ? 70.636 53.017 52.396 1.00 4.82   ? 31  LEU D N   1 
ATOM   3484 C  CA  . LEU D 2 31  ? 69.445 52.206 52.140 1.00 2.36   ? 31  LEU D CA  1 
ATOM   3485 C  C   . LEU D 2 31  ? 69.415 51.016 53.044 1.00 1.00   ? 31  LEU D C   1 
ATOM   3486 O  O   . LEU D 2 31  ? 68.398 50.775 53.676 1.00 1.00   ? 31  LEU D O   1 
ATOM   3487 C  CB  . LEU D 2 31  ? 69.373 51.718 50.703 1.00 2.14   ? 31  LEU D CB  1 
ATOM   3488 C  CG  . LEU D 2 31  ? 68.006 51.101 50.368 1.00 2.05   ? 31  LEU D CG  1 
ATOM   3489 C  CD1 . LEU D 2 31  ? 67.011 52.223 50.059 1.00 1.99   ? 31  LEU D CD1 1 
ATOM   3490 C  CD2 . LEU D 2 31  ? 68.059 50.079 49.233 1.00 1.96   ? 31  LEU D CD2 1 
ATOM   3491 N  N   . LEU D 2 32  ? 70.531 50.302 53.129 1.00 1.00   ? 32  LEU D N   1 
ATOM   3492 C  CA  . LEU D 2 32  ? 70.600 49.091 53.955 1.00 1.00   ? 32  LEU D CA  1 
ATOM   3493 C  C   . LEU D 2 32  ? 70.533 49.303 55.445 1.00 1.00   ? 32  LEU D C   1 
ATOM   3494 O  O   . LEU D 2 32  ? 70.221 48.365 56.173 1.00 1.00   ? 32  LEU D O   1 
ATOM   3495 C  CB  . LEU D 2 32  ? 71.852 48.280 53.688 1.00 1.00   ? 32  LEU D CB  1 
ATOM   3496 C  CG  . LEU D 2 32  ? 71.678 47.301 52.544 1.00 1.00   ? 32  LEU D CG  1 
ATOM   3497 C  CD1 . LEU D 2 32  ? 71.365 48.021 51.238 1.00 1.00   ? 32  LEU D CD1 1 
ATOM   3498 C  CD2 . LEU D 2 32  ? 72.974 46.512 52.415 1.00 1.00   ? 32  LEU D CD2 1 
ATOM   3499 N  N   . VAL D 2 33  ? 70.829 50.507 55.908 1.00 1.00   ? 33  VAL D N   1 
ATOM   3500 C  CA  . VAL D 2 33  ? 70.719 50.841 57.341 1.00 1.00   ? 33  VAL D CA  1 
ATOM   3501 C  C   . VAL D 2 33  ? 69.323 51.375 57.745 1.00 1.00   ? 33  VAL D C   1 
ATOM   3502 O  O   . VAL D 2 33  ? 68.793 51.035 58.798 1.00 1.00   ? 33  VAL D O   1 
ATOM   3503 C  CB  . VAL D 2 33  ? 71.807 51.876 57.683 1.00 1.00   ? 33  VAL D CB  1 
ATOM   3504 C  CG1 . VAL D 2 33  ? 71.635 52.433 59.092 1.00 1.00   ? 33  VAL D CG1 1 
ATOM   3505 C  CG2 . VAL D 2 33  ? 73.173 51.236 57.476 1.00 1.00   ? 33  VAL D CG2 1 
ATOM   3506 N  N   . VAL D 2 34  ? 68.752 52.204 56.892 1.00 1.00   ? 34  VAL D N   1 
ATOM   3507 C  CA  . VAL D 2 34  ? 67.478 52.830 57.156 1.00 1.00   ? 34  VAL D CA  1 
ATOM   3508 C  C   . VAL D 2 34  ? 66.248 51.955 56.830 1.00 1.00   ? 34  VAL D C   1 
ATOM   3509 O  O   . VAL D 2 34  ? 65.190 52.145 57.461 1.00 1.00   ? 34  VAL D O   1 
ATOM   3510 C  CB  . VAL D 2 34  ? 67.402 54.146 56.384 1.00 1.00   ? 34  VAL D CB  1 
ATOM   3511 C  CG1 . VAL D 2 34  ? 66.025 54.800 56.492 1.00 1.00   ? 34  VAL D CG1 1 
ATOM   3512 C  CG2 . VAL D 2 34  ? 68.488 55.064 56.916 1.00 1.00   ? 34  VAL D CG2 1 
ATOM   3513 N  N   . TYR D 2 35  ? 66.347 51.022 55.875 1.00 1.00   ? 35  TYR D N   1 
ATOM   3514 C  CA  . TYR D 2 35  ? 65.205 50.146 55.536 1.00 1.00   ? 35  TYR D CA  1 
ATOM   3515 C  C   . TYR D 2 35  ? 65.601 48.672 55.597 1.00 1.00   ? 35  TYR D C   1 
ATOM   3516 O  O   . TYR D 2 35  ? 65.551 47.959 54.595 1.00 1.00   ? 35  TYR D O   1 
ATOM   3517 C  CB  . TYR D 2 35  ? 64.636 50.533 54.178 1.00 1.00   ? 35  TYR D CB  1 
ATOM   3518 C  CG  . TYR D 2 35  ? 64.173 51.971 54.123 1.00 1.00   ? 35  TYR D CG  1 
ATOM   3519 C  CD1 . TYR D 2 35  ? 63.253 52.449 55.063 1.00 1.00   ? 35  TYR D CD1 1 
ATOM   3520 C  CD2 . TYR D 2 35  ? 64.652 52.873 53.137 1.00 1.00   ? 35  TYR D CD2 1 
ATOM   3521 C  CE1 . TYR D 2 35  ? 62.811 53.763 55.040 1.00 1.00   ? 35  TYR D CE1 1 
ATOM   3522 C  CE2 . TYR D 2 35  ? 64.215 54.201 53.104 1.00 1.00   ? 35  TYR D CE2 1 
ATOM   3523 C  CZ  . TYR D 2 35  ? 63.287 54.636 54.064 1.00 1.00   ? 35  TYR D CZ  1 
ATOM   3524 O  OH  . TYR D 2 35  ? 62.802 55.928 54.115 1.00 1.00   ? 35  TYR D OH  1 
ATOM   3525 N  N   . PRO D 2 36  ? 65.965 48.202 56.800 1.00 1.00   ? 36  PRO D N   1 
ATOM   3526 C  CA  . PRO D 2 36  ? 66.684 46.934 57.042 1.00 1.00   ? 36  PRO D CA  1 
ATOM   3527 C  C   . PRO D 2 36  ? 66.260 45.753 56.181 1.00 1.00   ? 36  PRO D C   1 
ATOM   3528 O  O   . PRO D 2 36  ? 67.128 45.000 55.708 1.00 1.00   ? 36  PRO D O   1 
ATOM   3529 C  CB  . PRO D 2 36  ? 66.369 46.611 58.496 1.00 1.00   ? 36  PRO D CB  1 
ATOM   3530 C  CG  . PRO D 2 36  ? 66.036 47.920 59.124 1.00 1.00   ? 36  PRO D CG  1 
ATOM   3531 C  CD  . PRO D 2 36  ? 65.518 48.830 58.058 1.00 1.00   ? 36  PRO D CD  1 
ATOM   3532 N  N   . TRP D 2 37  ? 64.954 45.578 55.977 1.00 1.00   ? 37  TRP D N   1 
ATOM   3533 C  CA  . TRP D 2 37  ? 64.483 44.450 55.159 1.00 1.00   ? 37  TRP D CA  1 
ATOM   3534 C  C   . TRP D 2 37  ? 65.123 44.394 53.781 1.00 1.00   ? 37  TRP D C   1 
ATOM   3535 O  O   . TRP D 2 37  ? 65.038 43.363 53.128 1.00 1.00   ? 37  TRP D O   1 
ATOM   3536 C  CB  . TRP D 2 37  ? 62.971 44.438 54.991 1.00 1.00   ? 37  TRP D CB  1 
ATOM   3537 C  CG  . TRP D 2 37  ? 62.484 45.598 54.281 1.00 1.00   ? 37  TRP D CG  1 
ATOM   3538 C  CD1 . TRP D 2 37  ? 62.392 45.779 52.905 1.00 1.00   ? 37  TRP D CD1 1 
ATOM   3539 C  CD2 . TRP D 2 37  ? 62.040 46.800 54.876 1.00 1.00   ? 37  TRP D CD2 1 
ATOM   3540 N  NE1 . TRP D 2 37  ? 61.891 47.033 52.630 1.00 1.00   ? 37  TRP D NE1 1 
ATOM   3541 C  CE2 . TRP D 2 37  ? 61.670 47.685 53.819 1.00 1.00   ? 37  TRP D CE2 1 
ATOM   3542 C  CE3 . TRP D 2 37  ? 61.914 47.226 56.196 1.00 1.00   ? 37  TRP D CE3 1 
ATOM   3543 C  CZ2 . TRP D 2 37  ? 61.189 48.971 54.055 1.00 1.00   ? 37  TRP D CZ2 1 
ATOM   3544 C  CZ3 . TRP D 2 37  ? 61.425 48.508 56.432 1.00 1.00   ? 37  TRP D CZ3 1 
ATOM   3545 C  CH2 . TRP D 2 37  ? 61.064 49.367 55.360 1.00 1.00   ? 37  TRP D CH2 1 
ATOM   3546 N  N   . THR D 2 38  ? 65.700 45.503 53.312 1.00 1.00   ? 38  THR D N   1 
ATOM   3547 C  CA  . THR D 2 38  ? 66.391 45.507 52.035 1.00 1.00   ? 38  THR D CA  1 
ATOM   3548 C  C   . THR D 2 38  ? 67.631 44.663 52.065 1.00 1.00   ? 38  THR D C   1 
ATOM   3549 O  O   . THR D 2 38  ? 68.063 44.205 51.013 1.00 1.00   ? 38  THR D O   1 
ATOM   3550 C  CB  . THR D 2 38  ? 66.836 46.901 51.621 1.00 1.00   ? 38  THR D CB  1 
ATOM   3551 O  OG1 . THR D 2 38  ? 67.505 47.505 52.731 1.00 1.00   ? 38  THR D OG1 1 
ATOM   3552 C  CG2 . THR D 2 38  ? 65.640 47.737 51.177 1.00 1.00   ? 38  THR D CG2 1 
ATOM   3553 N  N   . GLN D 2 39  ? 68.217 44.460 53.239 1.00 5.21   ? 39  GLN D N   1 
ATOM   3554 C  CA  . GLN D 2 39  ? 69.373 43.580 53.327 1.00 8.88   ? 39  GLN D CA  1 
ATOM   3555 C  C   . GLN D 2 39  ? 69.145 42.194 52.804 1.00 11.34  ? 39  GLN D C   1 
ATOM   3556 O  O   . GLN D 2 39  ? 70.058 41.612 52.229 1.00 12.10  ? 39  GLN D O   1 
ATOM   3557 C  CB  . GLN D 2 39  ? 69.881 43.457 54.741 1.00 10.16  ? 39  GLN D CB  1 
ATOM   3558 C  CG  . GLN D 2 39  ? 70.754 44.646 55.098 1.00 11.64  ? 39  GLN D CG  1 
ATOM   3559 C  CD  . GLN D 2 39  ? 70.809 44.872 56.585 1.00 13.30  ? 39  GLN D CD  1 
ATOM   3560 O  OE1 . GLN D 2 39  ? 70.448 43.977 57.378 1.00 14.96  ? 39  GLN D OE1 1 
ATOM   3561 N  NE2 . GLN D 2 39  ? 71.250 46.071 56.987 1.00 13.78  ? 39  GLN D NE2 1 
ATOM   3562 N  N   . ARG D 2 40  ? 67.947 41.660 52.989 1.00 14.51  ? 40  ARG D N   1 
ATOM   3563 C  CA  . ARG D 2 40  ? 67.654 40.332 52.501 1.00 17.66  ? 40  ARG D CA  1 
ATOM   3564 C  C   . ARG D 2 40  ? 68.094 40.143 51.047 1.00 19.62  ? 40  ARG D C   1 
ATOM   3565 O  O   . ARG D 2 40  ? 68.516 39.046 50.693 1.00 20.04  ? 40  ARG D O   1 
ATOM   3566 C  CB  . ARG D 2 40  ? 66.175 40.040 52.669 1.00 20.37  ? 40  ARG D CB  1 
ATOM   3567 C  CG  . ARG D 2 40  ? 65.699 38.725 52.097 1.00 23.71  ? 40  ARG D CG  1 
ATOM   3568 C  CD  . ARG D 2 40  ? 64.187 38.706 51.996 1.00 28.04  ? 40  ARG D CD  1 
ATOM   3569 N  NE  . ARG D 2 40  ? 63.720 37.448 51.429 1.00 33.37  ? 40  ARG D NE  1 
ATOM   3570 C  CZ  . ARG D 2 40  ? 63.726 36.270 52.069 1.00 41.41  ? 40  ARG D CZ  1 
ATOM   3571 N  NH1 . ARG D 2 40  ? 63.269 35.187 51.433 1.00 46.29  ? 40  ARG D NH1 1 
ATOM   3572 N  NH2 . ARG D 2 40  ? 64.181 36.140 53.331 1.00 41.50  ? 40  ARG D NH2 1 
ATOM   3573 N  N   . PHE D 2 41  ? 68.025 41.182 50.213 1.00 22.52  ? 41  PHE D N   1 
ATOM   3574 C  CA  . PHE D 2 41  ? 68.463 41.044 48.820 1.00 26.55  ? 41  PHE D CA  1 
ATOM   3575 C  C   . PHE D 2 41  ? 69.977 40.890 48.660 1.00 30.07  ? 41  PHE D C   1 
ATOM   3576 O  O   . PHE D 2 41  ? 70.424 40.141 47.796 1.00 32.51  ? 41  PHE D O   1 
ATOM   3577 C  CB  . PHE D 2 41  ? 67.965 42.191 47.950 1.00 28.06  ? 41  PHE D CB  1 
ATOM   3578 C  CG  . PHE D 2 41  ? 66.477 42.301 47.909 1.00 30.97  ? 41  PHE D CG  1 
ATOM   3579 C  CD1 . PHE D 2 41  ? 65.706 41.264 47.387 1.00 33.00  ? 41  PHE D CD1 1 
ATOM   3580 C  CD2 . PHE D 2 41  ? 65.830 43.428 48.415 1.00 33.17  ? 41  PHE D CD2 1 
ATOM   3581 C  CE1 . PHE D 2 41  ? 64.310 41.351 47.364 1.00 34.25  ? 41  PHE D CE1 1 
ATOM   3582 C  CE2 . PHE D 2 41  ? 64.437 43.523 48.391 1.00 34.81  ? 41  PHE D CE2 1 
ATOM   3583 C  CZ  . PHE D 2 41  ? 63.673 42.483 47.864 1.00 34.37  ? 41  PHE D CZ  1 
ATOM   3584 N  N   . PHE D 2 42  ? 70.763 41.578 49.480 1.00 33.02  ? 42  PHE D N   1 
ATOM   3585 C  CA  . PHE D 2 42  ? 72.214 41.533 49.358 1.00 36.42  ? 42  PHE D CA  1 
ATOM   3586 C  C   . PHE D 2 42  ? 72.893 40.625 50.393 1.00 44.61  ? 42  PHE D C   1 
ATOM   3587 O  O   . PHE D 2 42  ? 74.037 40.882 50.750 1.00 47.47  ? 42  PHE D O   1 
ATOM   3588 C  CB  . PHE D 2 42  ? 72.790 42.942 49.514 1.00 34.98  ? 42  PHE D CB  1 
ATOM   3589 C  CG  . PHE D 2 42  ? 72.133 43.971 48.669 1.00 34.04  ? 42  PHE D CG  1 
ATOM   3590 C  CD1 . PHE D 2 42  ? 72.453 44.083 47.335 1.00 35.04  ? 42  PHE D CD1 1 
ATOM   3591 C  CD2 . PHE D 2 42  ? 71.214 44.859 49.208 1.00 35.39  ? 42  PHE D CD2 1 
ATOM   3592 C  CE1 . PHE D 2 42  ? 71.851 45.052 46.533 1.00 35.96  ? 42  PHE D CE1 1 
ATOM   3593 C  CE2 . PHE D 2 42  ? 70.603 45.832 48.409 1.00 35.99  ? 42  PHE D CE2 1 
ATOM   3594 C  CZ  . PHE D 2 42  ? 70.919 45.927 47.068 1.00 34.86  ? 42  PHE D CZ  1 
ATOM   3595 N  N   . GLU D 2 43  ? 72.247 39.566 50.879 1.00 58.99  ? 43  GLU D N   1 
ATOM   3596 C  CA  . GLU D 2 43  ? 72.897 38.705 51.900 1.00 76.24  ? 43  GLU D CA  1 
ATOM   3597 C  C   . GLU D 2 43  ? 74.178 38.002 51.404 1.00 79.55  ? 43  GLU D C   1 
ATOM   3598 O  O   . GLU D 2 43  ? 74.997 37.555 52.211 1.00 77.88  ? 43  GLU D O   1 
ATOM   3599 C  CB  . GLU D 2 43  ? 71.917 37.685 52.494 1.00 96.77  ? 43  GLU D CB  1 
ATOM   3600 C  CG  . GLU D 2 43  ? 71.487 36.551 51.565 1.00 116.30 ? 43  GLU D CG  1 
ATOM   3601 C  CD  . GLU D 2 43  ? 70.284 35.767 52.094 1.00 137.54 ? 43  GLU D CD  1 
ATOM   3602 O  OE1 . GLU D 2 43  ? 69.999 35.821 53.314 1.00 145.74 ? 43  GLU D OE1 1 
ATOM   3603 O  OE2 . GLU D 2 43  ? 69.616 35.086 51.283 1.00 148.75 ? 43  GLU D OE2 1 
ATOM   3604 N  N   . SER D 2 44  ? 74.339 37.926 50.082 1.00 81.34  ? 44  SER D N   1 
ATOM   3605 C  CA  . SER D 2 44  ? 75.588 37.504 49.439 1.00 80.35  ? 44  SER D CA  1 
ATOM   3606 C  C   . SER D 2 44  ? 76.789 38.476 49.559 1.00 74.61  ? 44  SER D C   1 
ATOM   3607 O  O   . SER D 2 44  ? 77.894 38.121 49.140 1.00 74.68  ? 44  SER D O   1 
ATOM   3608 C  CB  . SER D 2 44  ? 75.316 37.243 47.955 1.00 83.64  ? 44  SER D CB  1 
ATOM   3609 O  OG  . SER D 2 44  ? 74.832 38.417 47.319 1.00 82.73  ? 44  SER D OG  1 
ATOM   3610 N  N   . PHE D 2 45  ? 76.586 39.679 50.107 1.00 66.75  ? 45  PHE D N   1 
ATOM   3611 C  CA  . PHE D 2 45  ? 77.678 40.638 50.333 1.00 63.09  ? 45  PHE D CA  1 
ATOM   3612 C  C   . PHE D 2 45  ? 78.314 40.517 51.723 1.00 65.78  ? 45  PHE D C   1 
ATOM   3613 O  O   . PHE D 2 45  ? 78.937 41.468 52.201 1.00 64.19  ? 45  PHE D O   1 
ATOM   3614 C  CB  . PHE D 2 45  ? 77.193 42.092 50.154 1.00 61.13  ? 45  PHE D CB  1 
ATOM   3615 C  CG  . PHE D 2 45  ? 76.783 42.474 48.750 1.00 59.24  ? 45  PHE D CG  1 
ATOM   3616 C  CD1 . PHE D 2 45  ? 76.884 41.599 47.660 1.00 61.50  ? 45  PHE D CD1 1 
ATOM   3617 C  CD2 . PHE D 2 45  ? 76.319 43.768 48.519 1.00 56.93  ? 45  PHE D CD2 1 
ATOM   3618 C  CE1 . PHE D 2 45  ? 76.504 42.009 46.387 1.00 63.97  ? 45  PHE D CE1 1 
ATOM   3619 C  CE2 . PHE D 2 45  ? 75.940 44.178 47.251 1.00 58.92  ? 45  PHE D CE2 1 
ATOM   3620 C  CZ  . PHE D 2 45  ? 76.035 43.302 46.181 1.00 61.45  ? 45  PHE D CZ  1 
ATOM   3621 N  N   . GLY D 2 46  ? 78.179 39.371 52.381 1.00 75.72  ? 46  GLY D N   1 
ATOM   3622 C  CA  . GLY D 2 46  ? 78.875 39.153 53.644 1.00 91.14  ? 46  GLY D CA  1 
ATOM   3623 C  C   . GLY D 2 46  ? 78.255 39.929 54.793 1.00 102.97 ? 46  GLY D C   1 
ATOM   3624 O  O   . GLY D 2 46  ? 77.028 39.966 54.927 1.00 110.52 ? 46  GLY D O   1 
ATOM   3625 N  N   . ASP D 2 47  ? 79.096 40.558 55.613 1.00 107.34 ? 47  ASP D N   1 
ATOM   3626 C  CA  . ASP D 2 47  ? 78.637 41.137 56.876 1.00 110.49 ? 47  ASP D CA  1 
ATOM   3627 C  C   . ASP D 2 47  ? 77.926 42.469 56.676 1.00 93.33  ? 47  ASP D C   1 
ATOM   3628 O  O   . ASP D 2 47  ? 78.462 43.374 56.037 1.00 89.82  ? 47  ASP D O   1 
ATOM   3629 C  CB  . ASP D 2 47  ? 79.810 41.321 57.841 1.00 132.54 ? 47  ASP D CB  1 
ATOM   3630 C  CG  . ASP D 2 47  ? 79.355 41.593 59.270 1.00 150.74 ? 47  ASP D CG  1 
ATOM   3631 O  OD1 . ASP D 2 47  ? 78.550 40.797 59.805 1.00 162.62 ? 47  ASP D OD1 1 
ATOM   3632 O  OD2 . ASP D 2 47  ? 79.807 42.599 59.861 1.00 156.40 ? 47  ASP D OD2 1 
ATOM   3633 N  N   . LEU D 2 48  ? 76.695 42.567 57.169 1.00 83.47  ? 48  LEU D N   1 
ATOM   3634 C  CA  . LEU D 2 48  ? 75.917 43.805 57.098 1.00 80.08  ? 48  LEU D CA  1 
ATOM   3635 C  C   . LEU D 2 48  ? 75.288 44.182 58.450 1.00 85.25  ? 48  LEU D C   1 
ATOM   3636 O  O   . LEU D 2 48  ? 74.392 45.019 58.511 1.00 82.10  ? 48  LEU D O   1 
ATOM   3637 C  CB  . LEU D 2 48  ? 74.842 43.698 56.018 1.00 70.84  ? 48  LEU D CB  1 
ATOM   3638 C  CG  . LEU D 2 48  ? 75.318 43.253 54.637 1.00 62.42  ? 48  LEU D CG  1 
ATOM   3639 C  CD1 . LEU D 2 48  ? 74.299 42.330 53.994 1.00 61.26  ? 48  LEU D CD1 1 
ATOM   3640 C  CD2 . LEU D 2 48  ? 75.577 44.455 53.748 1.00 59.80  ? 48  LEU D CD2 1 
ATOM   3641 N  N   . SER D 2 49  ? 75.772 43.574 59.527 1.00 95.56  ? 49  SER D N   1 
ATOM   3642 C  CA  . SER D 2 49  ? 75.205 43.772 60.868 1.00 108.00 ? 49  SER D CA  1 
ATOM   3643 C  C   . SER D 2 49  ? 75.217 45.154 61.547 1.00 108.18 ? 49  SER D C   1 
ATOM   3644 O  O   . SER D 2 49  ? 74.220 45.546 62.152 1.00 104.70 ? 49  SER D O   1 
ATOM   3645 C  CB  . SER D 2 49  ? 75.825 42.756 61.830 1.00 115.34 ? 49  SER D CB  1 
ATOM   3646 O  OG  . SER D 2 49  ? 77.184 43.064 62.073 1.00 116.09 ? 49  SER D OG  1 
ATOM   3647 N  N   . THR D 2 50  ? 76.317 45.891 61.457 1.00 106.40 ? 50  THR D N   1 
ATOM   3648 C  CA  . THR D 2 50  ? 76.396 47.192 62.126 1.00 103.22 ? 50  THR D CA  1 
ATOM   3649 C  C   . THR D 2 50  ? 76.621 48.336 61.152 1.00 92.43  ? 50  THR D C   1 
ATOM   3650 O  O   . THR D 2 50  ? 77.429 48.221 60.236 1.00 89.14  ? 50  THR D O   1 
ATOM   3651 C  CB  . THR D 2 50  ? 77.501 47.209 63.198 1.00 113.03 ? 50  THR D CB  1 
ATOM   3652 O  OG1 . THR D 2 50  ? 77.594 48.518 63.770 1.00 116.62 ? 50  THR D OG1 1 
ATOM   3653 C  CG2 . THR D 2 50  ? 78.839 46.832 62.591 1.00 116.87 ? 50  THR D CG2 1 
ATOM   3654 N  N   . PRO D 2 51  ? 75.908 49.455 61.343 1.00 90.88  ? 51  PRO D N   1 
ATOM   3655 C  CA  . PRO D 2 51  ? 76.141 50.508 60.360 1.00 91.97  ? 51  PRO D CA  1 
ATOM   3656 C  C   . PRO D 2 51  ? 77.569 50.621 59.834 1.00 95.37  ? 51  PRO D C   1 
ATOM   3657 O  O   . PRO D 2 51  ? 77.755 50.878 58.644 1.00 101.80 ? 51  PRO D O   1 
ATOM   3658 C  CB  . PRO D 2 51  ? 75.770 51.770 61.130 1.00 93.39  ? 51  PRO D CB  1 
ATOM   3659 C  CG  . PRO D 2 51  ? 74.656 51.324 62.011 1.00 95.65  ? 51  PRO D CG  1 
ATOM   3660 C  CD  . PRO D 2 51  ? 74.899 49.875 62.335 1.00 93.28  ? 51  PRO D CD  1 
ATOM   3661 N  N   . ASP D 2 52  ? 78.560 50.432 60.701 1.00 103.03 ? 52  ASP D N   1 
ATOM   3662 C  CA  . ASP D 2 52  ? 79.968 50.542 60.298 1.00 116.14 ? 52  ASP D CA  1 
ATOM   3663 C  C   . ASP D 2 52  ? 80.430 49.425 59.348 1.00 108.97 ? 52  ASP D C   1 
ATOM   3664 O  O   . ASP D 2 52  ? 81.326 49.640 58.523 1.00 108.67 ? 52  ASP D O   1 
ATOM   3665 C  CB  . ASP D 2 52  ? 80.874 50.600 61.532 1.00 135.02 ? 52  ASP D CB  1 
ATOM   3666 C  CG  . ASP D 2 52  ? 80.627 51.841 62.387 1.00 153.25 ? 52  ASP D CG  1 
ATOM   3667 O  OD1 . ASP D 2 52  ? 80.292 52.912 61.831 1.00 165.25 ? 52  ASP D OD1 1 
ATOM   3668 O  OD2 . ASP D 2 52  ? 80.776 51.744 63.623 1.00 171.08 ? 52  ASP D OD2 1 
ATOM   3669 N  N   . ALA D 2 53  ? 79.809 48.252 59.456 1.00 95.35  ? 53  ALA D N   1 
ATOM   3670 C  CA  . ALA D 2 53  ? 80.108 47.123 58.580 1.00 86.09  ? 53  ALA D CA  1 
ATOM   3671 C  C   . ALA D 2 53  ? 79.532 47.346 57.190 1.00 79.88  ? 53  ALA D C   1 
ATOM   3672 O  O   . ALA D 2 53  ? 80.146 46.948 56.203 1.00 87.25  ? 53  ALA D O   1 
ATOM   3673 C  CB  . ALA D 2 53  ? 79.560 45.832 59.167 1.00 86.94  ? 53  ALA D CB  1 
ATOM   3674 N  N   . VAL D 2 54  ? 78.356 47.970 57.120 1.00 70.34  ? 54  VAL D N   1 
ATOM   3675 C  CA  . VAL D 2 54  ? 77.700 48.262 55.845 1.00 64.75  ? 54  VAL D CA  1 
ATOM   3676 C  C   . VAL D 2 54  ? 78.445 49.359 55.105 1.00 63.94  ? 54  VAL D C   1 
ATOM   3677 O  O   . VAL D 2 54  ? 78.654 49.257 53.901 1.00 66.09  ? 54  VAL D O   1 
ATOM   3678 C  CB  . VAL D 2 54  ? 76.220 48.657 56.037 1.00 63.97  ? 54  VAL D CB  1 
ATOM   3679 C  CG1 . VAL D 2 54  ? 75.594 49.157 54.739 1.00 66.53  ? 54  VAL D CG1 1 
ATOM   3680 C  CG2 . VAL D 2 54  ? 75.429 47.473 56.562 1.00 66.77  ? 54  VAL D CG2 1 
ATOM   3681 N  N   . MET D 2 55  ? 78.836 50.407 55.811 1.00 68.62  ? 55  MET D N   1 
ATOM   3682 C  CA  . MET D 2 55  ? 79.615 51.469 55.190 1.00 81.16  ? 55  MET D CA  1 
ATOM   3683 C  C   . MET D 2 55  ? 81.040 51.011 54.872 1.00 88.05  ? 55  MET D C   1 
ATOM   3684 O  O   . MET D 2 55  ? 81.623 51.467 53.887 1.00 91.88  ? 55  MET D O   1 
ATOM   3685 C  CB  . MET D 2 55  ? 79.620 52.727 56.068 1.00 90.77  ? 55  MET D CB  1 
ATOM   3686 C  CG  . MET D 2 55  ? 78.248 53.388 56.215 1.00 96.06  ? 55  MET D CG  1 
ATOM   3687 S  SD  . MET D 2 55  ? 77.574 54.043 54.667 1.00 101.80 ? 55  MET D SD  1 
ATOM   3688 C  CE  . MET D 2 55  ? 75.945 54.588 55.164 1.00 95.59  ? 55  MET D CE  1 
ATOM   3689 N  N   . GLY D 2 56  ? 81.585 50.104 55.688 1.00 97.93  ? 56  GLY D N   1 
ATOM   3690 C  CA  . GLY D 2 56  ? 82.933 49.550 55.473 1.00 106.04 ? 56  GLY D CA  1 
ATOM   3691 C  C   . GLY D 2 56  ? 83.084 48.419 54.452 1.00 105.55 ? 56  GLY D C   1 
ATOM   3692 O  O   . GLY D 2 56  ? 84.208 48.008 54.152 1.00 108.89 ? 56  GLY D O   1 
ATOM   3693 N  N   . ASN D 2 57  ? 81.970 47.918 53.919 1.00 98.31  ? 57  ASN D N   1 
ATOM   3694 C  CA  . ASN D 2 57  ? 81.979 46.795 52.980 1.00 93.33  ? 57  ASN D CA  1 
ATOM   3695 C  C   . ASN D 2 57  ? 82.448 47.274 51.597 1.00 95.84  ? 57  ASN D C   1 
ATOM   3696 O  O   . ASN D 2 57  ? 81.923 48.269 51.093 1.00 101.42 ? 57  ASN D O   1 
ATOM   3697 C  CB  . ASN D 2 57  ? 80.566 46.212 52.878 1.00 93.34  ? 57  ASN D CB  1 
ATOM   3698 C  CG  . ASN D 2 57  ? 80.533 44.822 52.277 1.00 98.72  ? 57  ASN D CG  1 
ATOM   3699 O  OD1 . ASN D 2 57  ? 81.483 44.364 51.642 1.00 104.02 ? 57  ASN D OD1 1 
ATOM   3700 N  ND2 . ASN D 2 57  ? 79.416 44.138 52.477 1.00 104.06 ? 57  ASN D ND2 1 
ATOM   3701 N  N   . PRO D 2 58  ? 83.436 46.585 50.980 1.00 97.58  ? 58  PRO D N   1 
ATOM   3702 C  CA  . PRO D 2 58  ? 83.856 46.950 49.608 1.00 100.44 ? 58  PRO D CA  1 
ATOM   3703 C  C   . PRO D 2 58  ? 82.847 46.650 48.487 1.00 99.94  ? 58  PRO D C   1 
ATOM   3704 O  O   . PRO D 2 58  ? 82.760 47.421 47.523 1.00 97.24  ? 58  PRO D O   1 
ATOM   3705 C  CB  . PRO D 2 58  ? 85.129 46.123 49.393 1.00 102.05 ? 58  PRO D CB  1 
ATOM   3706 C  CG  . PRO D 2 58  ? 85.616 45.804 50.760 1.00 101.85 ? 58  PRO D CG  1 
ATOM   3707 C  CD  . PRO D 2 58  ? 84.385 45.636 51.592 1.00 97.77  ? 58  PRO D CD  1 
ATOM   3708 N  N   . LYS D 2 59  ? 82.123 45.535 48.606 1.00 96.88  ? 59  LYS D N   1 
ATOM   3709 C  CA  . LYS D 2 59  ? 81.129 45.133 47.598 1.00 94.11  ? 59  LYS D CA  1 
ATOM   3710 C  C   . LYS D 2 59  ? 79.959 46.097 47.521 1.00 83.29  ? 59  LYS D C   1 
ATOM   3711 O  O   . LYS D 2 59  ? 79.415 46.328 46.436 1.00 80.65  ? 59  LYS D O   1 
ATOM   3712 C  CB  . LYS D 2 59  ? 80.584 43.738 47.886 1.00 100.92 ? 59  LYS D CB  1 
ATOM   3713 C  CG  . LYS D 2 59  ? 81.605 42.633 47.735 1.00 112.26 ? 59  LYS D CG  1 
ATOM   3714 C  CD  . LYS D 2 59  ? 80.966 41.288 48.019 1.00 124.99 ? 59  LYS D CD  1 
ATOM   3715 C  CE  . LYS D 2 59  ? 81.992 40.170 48.010 1.00 135.94 ? 59  LYS D CE  1 
ATOM   3716 N  NZ  . LYS D 2 59  ? 81.354 38.840 48.217 1.00 140.90 ? 59  LYS D NZ  1 
ATOM   3717 N  N   . VAL D 2 60  ? 79.573 46.644 48.673 1.00 69.45  ? 60  VAL D N   1 
ATOM   3718 C  CA  . VAL D 2 60  ? 78.506 47.623 48.722 1.00 63.20  ? 60  VAL D CA  1 
ATOM   3719 C  C   . VAL D 2 60  ? 78.934 48.827 47.908 1.00 64.71  ? 60  VAL D C   1 
ATOM   3720 O  O   . VAL D 2 60  ? 78.223 49.220 46.985 1.00 71.62  ? 60  VAL D O   1 
ATOM   3721 C  CB  . VAL D 2 60  ? 78.128 48.012 50.163 1.00 60.63  ? 60  VAL D CB  1 
ATOM   3722 C  CG1 . VAL D 2 60  ? 77.145 49.185 50.193 1.00 58.94  ? 60  VAL D CG1 1 
ATOM   3723 C  CG2 . VAL D 2 60  ? 77.523 46.805 50.868 1.00 63.23  ? 60  VAL D CG2 1 
ATOM   3724 N  N   . LYS D 2 61  ? 80.103 49.384 48.208 1.00 66.84  ? 61  LYS D N   1 
ATOM   3725 C  CA  . LYS D 2 61  ? 80.589 50.534 47.446 1.00 70.55  ? 61  LYS D CA  1 
ATOM   3726 C  C   . LYS D 2 61  ? 80.744 50.188 45.972 1.00 64.20  ? 61  LYS D C   1 
ATOM   3727 O  O   . LYS D 2 61  ? 80.425 51.004 45.110 1.00 65.29  ? 61  LYS D O   1 
ATOM   3728 C  CB  . LYS D 2 61  ? 81.902 51.075 48.004 1.00 82.15  ? 61  LYS D CB  1 
ATOM   3729 C  CG  . LYS D 2 61  ? 82.267 52.441 47.434 1.00 97.98  ? 61  LYS D CG  1 
ATOM   3730 C  CD  . LYS D 2 61  ? 83.527 53.030 48.057 1.00 115.71 ? 61  LYS D CD  1 
ATOM   3731 C  CE  . LYS D 2 61  ? 84.818 52.472 47.456 1.00 128.68 ? 61  LYS D CE  1 
ATOM   3732 N  NZ  . LYS D 2 61  ? 85.218 51.123 47.961 1.00 135.14 ? 61  LYS D NZ  1 
ATOM   3733 N  N   . ALA D 2 62  ? 81.217 48.977 45.696 1.00 61.96  ? 62  ALA D N   1 
ATOM   3734 C  CA  . ALA D 2 62  ? 81.377 48.505 44.326 1.00 63.76  ? 62  ALA D CA  1 
ATOM   3735 C  C   . ALA D 2 62  ? 80.053 48.457 43.570 1.00 60.11  ? 62  ALA D C   1 
ATOM   3736 O  O   . ALA D 2 62  ? 79.944 48.994 42.460 1.00 58.69  ? 62  ALA D O   1 
ATOM   3737 C  CB  . ALA D 2 62  ? 82.025 47.133 44.322 1.00 69.56  ? 62  ALA D CB  1 
ATOM   3738 N  N   . HIS D 2 63  ? 79.060 47.813 44.179 1.00 55.17  ? 63  HIS D N   1 
ATOM   3739 C  CA  . HIS D 2 63  ? 77.725 47.711 43.587 1.00 53.04  ? 63  HIS D CA  1 
ATOM   3740 C  C   . HIS D 2 63  ? 77.035 49.069 43.468 1.00 49.37  ? 63  HIS D C   1 
ATOM   3741 O  O   . HIS D 2 63  ? 76.321 49.325 42.501 1.00 47.43  ? 63  HIS D O   1 
ATOM   3742 C  CB  . HIS D 2 63  ? 76.848 46.768 44.396 1.00 53.08  ? 63  HIS D CB  1 
ATOM   3743 C  CG  . HIS D 2 63  ? 75.465 46.646 43.857 1.00 54.08  ? 63  HIS D CG  1 
ATOM   3744 N  ND1 . HIS D 2 63  ? 75.126 45.716 42.903 1.00 59.77  ? 63  HIS D ND1 1 
ATOM   3745 C  CD2 . HIS D 2 63  ? 74.345 47.365 44.100 1.00 55.07  ? 63  HIS D CD2 1 
ATOM   3746 C  CE1 . HIS D 2 63  ? 73.850 45.857 42.592 1.00 64.45  ? 63  HIS D CE1 1 
ATOM   3747 N  NE2 . HIS D 2 63  ? 73.352 46.849 43.307 1.00 60.06  ? 63  HIS D NE2 1 
ATOM   3748 N  N   . GLY D 2 64  ? 77.243 49.922 44.462 1.00 48.65  ? 64  GLY D N   1 
ATOM   3749 C  CA  . GLY D 2 64  ? 76.759 51.283 44.420 1.00 51.13  ? 64  GLY D CA  1 
ATOM   3750 C  C   . GLY D 2 64  ? 77.199 52.014 43.169 1.00 56.16  ? 64  GLY D C   1 
ATOM   3751 O  O   . GLY D 2 64  ? 76.393 52.697 42.541 1.00 61.72  ? 64  GLY D O   1 
ATOM   3752 N  N   . LYS D 2 65  ? 78.465 51.859 42.791 1.00 62.65  ? 65  LYS D N   1 
ATOM   3753 C  CA  . LYS D 2 65  ? 78.995 52.538 41.611 1.00 68.80  ? 65  LYS D CA  1 
ATOM   3754 C  C   . LYS D 2 65  ? 78.178 52.246 40.344 1.00 66.95  ? 65  LYS D C   1 
ATOM   3755 O  O   . LYS D 2 65  ? 77.983 53.143 39.516 1.00 66.63  ? 65  LYS D O   1 
ATOM   3756 C  CB  . LYS D 2 65  ? 80.462 52.182 41.383 1.00 79.37  ? 65  LYS D CB  1 
ATOM   3757 C  CG  . LYS D 2 65  ? 81.135 53.045 40.319 1.00 94.37  ? 65  LYS D CG  1 
ATOM   3758 C  CD  . LYS D 2 65  ? 82.583 52.643 40.057 1.00 107.29 ? 65  LYS D CD  1 
ATOM   3759 C  CE  . LYS D 2 65  ? 83.576 53.333 40.989 1.00 112.04 ? 65  LYS D CE  1 
ATOM   3760 N  NZ  . LYS D 2 65  ? 83.550 52.836 42.395 1.00 112.22 ? 65  LYS D NZ  1 
ATOM   3761 N  N   . LYS D 2 66  ? 77.707 51.006 40.202 1.00 63.13  ? 66  LYS D N   1 
ATOM   3762 C  CA  . LYS D 2 66  ? 76.855 50.625 39.064 1.00 62.09  ? 66  LYS D CA  1 
ATOM   3763 C  C   . LYS D 2 66  ? 75.483 51.300 39.088 1.00 51.20  ? 66  LYS D C   1 
ATOM   3764 O  O   . LYS D 2 66  ? 74.977 51.716 38.044 1.00 46.61  ? 66  LYS D O   1 
ATOM   3765 C  CB  . LYS D 2 66  ? 76.702 49.100 38.975 1.00 69.55  ? 66  LYS D CB  1 
ATOM   3766 C  CG  . LYS D 2 66  ? 77.966 48.422 38.473 1.00 82.77  ? 66  LYS D CG  1 
ATOM   3767 C  CD  . LYS D 2 66  ? 77.859 46.902 38.422 1.00 94.17  ? 66  LYS D CD  1 
ATOM   3768 C  CE  . LYS D 2 66  ? 78.092 46.257 39.787 1.00 102.26 ? 66  LYS D CE  1 
ATOM   3769 N  NZ  . LYS D 2 66  ? 78.226 44.771 39.717 1.00 102.81 ? 66  LYS D NZ  1 
ATOM   3770 N  N   . VAL D 2 67  ? 74.900 51.407 40.279 1.00 44.90  ? 67  VAL D N   1 
ATOM   3771 C  CA  . VAL D 2 67  ? 73.570 51.973 40.446 1.00 41.13  ? 67  VAL D CA  1 
ATOM   3772 C  C   . VAL D 2 67  ? 73.582 53.405 40.000 1.00 41.08  ? 67  VAL D C   1 
ATOM   3773 O  O   . VAL D 2 67  ? 72.739 53.801 39.213 1.00 41.48  ? 67  VAL D O   1 
ATOM   3774 C  CB  . VAL D 2 67  ? 73.084 51.919 41.906 1.00 40.85  ? 67  VAL D CB  1 
ATOM   3775 C  CG1 . VAL D 2 67  ? 71.823 52.747 42.100 1.00 41.06  ? 67  VAL D CG1 1 
ATOM   3776 C  CG2 . VAL D 2 67  ? 72.819 50.484 42.336 1.00 42.75  ? 67  VAL D CG2 1 
ATOM   3777 N  N   . LEU D 2 68  ? 74.533 54.181 40.501 1.00 46.30  ? 68  LEU D N   1 
ATOM   3778 C  CA  . LEU D 2 68  ? 74.617 55.591 40.126 1.00 53.62  ? 68  LEU D CA  1 
ATOM   3779 C  C   . LEU D 2 68  ? 74.955 55.773 38.636 1.00 57.53  ? 68  LEU D C   1 
ATOM   3780 O  O   . LEU D 2 68  ? 74.492 56.729 38.003 1.00 53.71  ? 68  LEU D O   1 
ATOM   3781 C  CB  . LEU D 2 68  ? 75.619 56.345 41.001 1.00 57.55  ? 68  LEU D CB  1 
ATOM   3782 C  CG  . LEU D 2 68  ? 75.357 57.858 41.047 1.00 61.51  ? 68  LEU D CG  1 
ATOM   3783 C  CD1 . LEU D 2 68  ? 74.091 58.171 41.832 1.00 61.59  ? 68  LEU D CD1 1 
ATOM   3784 C  CD2 . LEU D 2 68  ? 76.548 58.594 41.641 1.00 68.04  ? 68  LEU D CD2 1 
ATOM   3785 N  N   . GLY D 2 69  ? 75.750 54.856 38.085 1.00 61.99  ? 69  GLY D N   1 
ATOM   3786 C  CA  . GLY D 2 69  ? 75.947 54.773 36.637 1.00 63.74  ? 69  GLY D CA  1 
ATOM   3787 C  C   . GLY D 2 69  ? 74.628 54.675 35.881 1.00 64.49  ? 69  GLY D C   1 
ATOM   3788 O  O   . GLY D 2 69  ? 74.409 55.399 34.909 1.00 66.14  ? 69  GLY D O   1 
ATOM   3789 N  N   . ALA D 2 70  ? 73.743 53.793 36.343 1.00 63.16  ? 70  ALA D N   1 
ATOM   3790 C  CA  . ALA D 2 70  ? 72.415 53.626 35.733 1.00 58.90  ? 70  ALA D CA  1 
ATOM   3791 C  C   . ALA D 2 70  ? 71.507 54.842 35.882 1.00 54.10  ? 70  ALA D C   1 
ATOM   3792 O  O   . ALA D 2 70  ? 70.681 55.068 35.011 1.00 54.92  ? 70  ALA D O   1 
ATOM   3793 C  CB  . ALA D 2 70  ? 71.720 52.388 36.279 1.00 58.98  ? 70  ALA D CB  1 
ATOM   3794 N  N   . PHE D 2 71  ? 71.631 55.600 36.973 1.00 52.61  ? 71  PHE D N   1 
ATOM   3795 C  CA  . PHE D 2 71  ? 70.916 56.876 37.088 1.00 55.09  ? 71  PHE D CA  1 
ATOM   3796 C  C   . PHE D 2 71  ? 71.453 57.877 36.096 1.00 61.36  ? 71  PHE D C   1 
ATOM   3797 O  O   . PHE D 2 71  ? 70.684 58.650 35.534 1.00 62.26  ? 71  PHE D O   1 
ATOM   3798 C  CB  . PHE D 2 71  ? 71.028 57.496 38.475 1.00 57.02  ? 71  PHE D CB  1 
ATOM   3799 C  CG  . PHE D 2 71  ? 69.969 57.048 39.424 1.00 61.68  ? 71  PHE D CG  1 
ATOM   3800 C  CD1 . PHE D 2 71  ? 68.745 57.697 39.470 1.00 62.32  ? 71  PHE D CD1 1 
ATOM   3801 C  CD2 . PHE D 2 71  ? 70.202 55.980 40.297 1.00 66.41  ? 71  PHE D CD2 1 
ATOM   3802 C  CE1 . PHE D 2 71  ? 67.765 57.278 40.364 1.00 68.58  ? 71  PHE D CE1 1 
ATOM   3803 C  CE2 . PHE D 2 71  ? 69.230 55.558 41.195 1.00 66.03  ? 71  PHE D CE2 1 
ATOM   3804 C  CZ  . PHE D 2 71  ? 68.008 56.208 41.230 1.00 69.17  ? 71  PHE D CZ  1 
ATOM   3805 N  N   . SER D 2 72  ? 72.774 57.882 35.904 1.00 70.64  ? 72  SER D N   1 
ATOM   3806 C  CA  . SER D 2 72  ? 73.422 58.812 34.970 1.00 77.54  ? 72  SER D CA  1 
ATOM   3807 C  C   . SER D 2 72  ? 72.963 58.567 33.535 1.00 83.84  ? 72  SER D C   1 
ATOM   3808 O  O   . SER D 2 72  ? 72.647 59.512 32.810 1.00 84.64  ? 72  SER D O   1 
ATOM   3809 C  CB  . SER D 2 72  ? 74.946 58.697 35.049 1.00 80.78  ? 72  SER D CB  1 
ATOM   3810 O  OG  . SER D 2 72  ? 75.405 58.667 36.389 1.00 79.10  ? 72  SER D OG  1 
ATOM   3811 N  N   . ASP D 2 73  ? 72.922 57.292 33.148 1.00 92.91  ? 73  ASP D N   1 
ATOM   3812 C  CA  . ASP D 2 73  ? 72.395 56.861 31.846 1.00 101.03 ? 73  ASP D CA  1 
ATOM   3813 C  C   . ASP D 2 73  ? 70.953 57.340 31.625 1.00 85.93  ? 73  ASP D C   1 
ATOM   3814 O  O   . ASP D 2 73  ? 70.623 57.886 30.573 1.00 79.12  ? 73  ASP D O   1 
ATOM   3815 C  CB  . ASP D 2 73  ? 72.464 55.324 31.744 1.00 122.12 ? 73  ASP D CB  1 
ATOM   3816 C  CG  . ASP D 2 73  ? 72.166 54.802 30.341 1.00 141.24 ? 73  ASP D CG  1 
ATOM   3817 O  OD1 . ASP D 2 73  ? 72.846 55.227 29.381 1.00 158.10 ? 73  ASP D OD1 1 
ATOM   3818 O  OD2 . ASP D 2 73  ? 71.266 53.945 30.202 1.00 147.56 ? 73  ASP D OD2 1 
ATOM   3819 N  N   . GLY D 2 74  ? 70.114 57.141 32.636 1.00 82.96  ? 74  GLY D N   1 
ATOM   3820 C  CA  . GLY D 2 74  ? 68.710 57.542 32.594 1.00 77.76  ? 74  GLY D CA  1 
ATOM   3821 C  C   . GLY D 2 74  ? 68.478 59.035 32.672 1.00 73.65  ? 74  GLY D C   1 
ATOM   3822 O  O   . GLY D 2 74  ? 67.404 59.508 32.320 1.00 72.72  ? 74  GLY D O   1 
ATOM   3823 N  N   . LEU D 2 75  ? 69.468 59.773 33.160 1.00 79.68  ? 75  LEU D N   1 
ATOM   3824 C  CA  . LEU D 2 75  ? 69.426 61.235 33.164 1.00 88.38  ? 75  LEU D CA  1 
ATOM   3825 C  C   . LEU D 2 75  ? 69.849 61.814 31.808 1.00 98.25  ? 75  LEU D C   1 
ATOM   3826 O  O   . LEU D 2 75  ? 69.478 62.943 31.471 1.00 100.14 ? 75  LEU D O   1 
ATOM   3827 C  CB  . LEU D 2 75  ? 70.310 61.774 34.286 1.00 87.75  ? 75  LEU D CB  1 
ATOM   3828 C  CG  . LEU D 2 75  ? 70.071 63.217 34.739 1.00 84.62  ? 75  LEU D CG  1 
ATOM   3829 C  CD1 . LEU D 2 75  ? 70.316 63.302 36.241 1.00 84.78  ? 75  LEU D CD1 1 
ATOM   3830 C  CD2 . LEU D 2 75  ? 70.937 64.213 33.971 1.00 88.91  ? 75  LEU D CD2 1 
ATOM   3831 N  N   . ALA D 2 76  ? 70.622 61.044 31.038 1.00 102.60 ? 76  ALA D N   1 
ATOM   3832 C  CA  . ALA D 2 76  ? 70.948 61.403 29.652 1.00 105.21 ? 76  ALA D CA  1 
ATOM   3833 C  C   . ALA D 2 76  ? 69.698 61.412 28.764 1.00 103.78 ? 76  ALA D C   1 
ATOM   3834 O  O   . ALA D 2 76  ? 69.412 62.406 28.094 1.00 101.58 ? 76  ALA D O   1 
ATOM   3835 C  CB  . ALA D 2 76  ? 71.991 60.448 29.081 1.00 105.94 ? 76  ALA D CB  1 
ATOM   3836 N  N   . HIS D 2 77  ? 68.956 60.307 28.791 1.00 103.60 ? 77  HIS D N   1 
ATOM   3837 C  CA  . HIS D 2 77  ? 67.787 60.109 27.935 1.00 106.70 ? 77  HIS D CA  1 
ATOM   3838 C  C   . HIS D 2 77  ? 66.470 60.292 28.691 1.00 103.76 ? 77  HIS D C   1 
ATOM   3839 O  O   . HIS D 2 77  ? 65.726 59.328 28.893 1.00 106.68 ? 77  HIS D O   1 
ATOM   3840 C  CB  . HIS D 2 77  ? 67.832 58.703 27.334 1.00 116.58 ? 77  HIS D CB  1 
ATOM   3841 C  CG  . HIS D 2 77  ? 69.046 58.437 26.507 1.00 131.64 ? 77  HIS D CG  1 
ATOM   3842 N  ND1 . HIS D 2 77  ? 70.185 57.858 27.022 1.00 136.30 ? 77  HIS D ND1 1 
ATOM   3843 C  CD2 . HIS D 2 77  ? 69.296 58.662 25.196 1.00 144.51 ? 77  HIS D CD2 1 
ATOM   3844 C  CE1 . HIS D 2 77  ? 71.087 57.741 26.064 1.00 147.55 ? 77  HIS D CE1 1 
ATOM   3845 N  NE2 . HIS D 2 77  ? 70.573 58.222 24.946 1.00 150.84 ? 77  HIS D NE2 1 
ATOM   3846 N  N   . LEU D 2 78  ? 66.170 61.524 29.097 1.00 102.40 ? 78  LEU D N   1 
ATOM   3847 C  CA  . LEU D 2 78  ? 64.917 61.810 29.816 1.00 105.86 ? 78  LEU D CA  1 
ATOM   3848 C  C   . LEU D 2 78  ? 63.665 61.598 28.954 1.00 109.24 ? 78  LEU D C   1 
ATOM   3849 O  O   . LEU D 2 78  ? 62.617 61.192 29.459 1.00 105.02 ? 78  LEU D O   1 
ATOM   3850 C  CB  . LEU D 2 78  ? 64.927 63.234 30.377 1.00 109.57 ? 78  LEU D CB  1 
ATOM   3851 C  CG  . LEU D 2 78  ? 65.964 63.525 31.464 1.00 115.68 ? 78  LEU D CG  1 
ATOM   3852 C  CD1 . LEU D 2 78  ? 65.930 65.002 31.827 1.00 120.27 ? 78  LEU D CD1 1 
ATOM   3853 C  CD2 . LEU D 2 78  ? 65.743 62.662 32.702 1.00 116.27 ? 78  LEU D CD2 1 
ATOM   3854 N  N   . ASP D 2 79  ? 63.785 61.888 27.662 1.00 122.34 ? 79  ASP D N   1 
ATOM   3855 C  CA  . ASP D 2 79  ? 62.713 61.640 26.687 1.00 131.16 ? 79  ASP D CA  1 
ATOM   3856 C  C   . ASP D 2 79  ? 62.187 60.195 26.676 1.00 120.65 ? 79  ASP D C   1 
ATOM   3857 O  O   . ASP D 2 79  ? 60.976 59.975 26.692 1.00 112.02 ? 79  ASP D O   1 
ATOM   3858 C  CB  . ASP D 2 79  ? 63.158 62.061 25.265 1.00 150.78 ? 79  ASP D CB  1 
ATOM   3859 C  CG  . ASP D 2 79  ? 64.488 61.415 24.815 1.00 159.88 ? 79  ASP D CG  1 
ATOM   3860 O  OD1 . ASP D 2 79  ? 65.134 60.700 25.613 1.00 165.74 ? 79  ASP D OD1 1 
ATOM   3861 O  OD2 . ASP D 2 79  ? 64.891 61.639 23.652 1.00 164.30 ? 79  ASP D OD2 1 
ATOM   3862 N  N   . ASN D 2 80  ? 63.108 59.234 26.668 1.00 122.56 ? 80  ASN D N   1 
ATOM   3863 C  CA  . ASN D 2 80  ? 62.790 57.819 26.502 1.00 129.06 ? 80  ASN D CA  1 
ATOM   3864 C  C   . ASN D 2 80  ? 63.388 57.051 27.673 1.00 123.51 ? 80  ASN D C   1 
ATOM   3865 O  O   . ASN D 2 80  ? 64.526 56.577 27.608 1.00 128.47 ? 80  ASN D O   1 
ATOM   3866 C  CB  . ASN D 2 80  ? 63.348 57.314 25.159 1.00 143.96 ? 80  ASN D CB  1 
ATOM   3867 C  CG  . ASN D 2 80  ? 63.041 55.843 24.891 1.00 156.59 ? 80  ASN D CG  1 
ATOM   3868 O  OD1 . ASN D 2 80  ? 62.139 55.253 25.492 1.00 164.68 ? 80  ASN D OD1 1 
ATOM   3869 N  ND2 . ASN D 2 80  ? 63.793 55.248 23.970 1.00 163.29 ? 80  ASN D ND2 1 
ATOM   3870 N  N   . LEU D 2 81  ? 62.613 56.944 28.746 1.00 111.43 ? 81  LEU D N   1 
ATOM   3871 C  CA  . LEU D 2 81  ? 63.053 56.236 29.945 1.00 105.49 ? 81  LEU D CA  1 
ATOM   3872 C  C   . LEU D 2 81  ? 62.679 54.758 29.911 1.00 114.21 ? 81  LEU D C   1 
ATOM   3873 O  O   . LEU D 2 81  ? 63.463 53.916 30.354 1.00 117.63 ? 81  LEU D O   1 
ATOM   3874 C  CB  . LEU D 2 81  ? 62.495 56.913 31.198 1.00 97.05  ? 81  LEU D CB  1 
ATOM   3875 C  CG  . LEU D 2 81  ? 63.251 58.170 31.644 1.00 88.89  ? 81  LEU D CG  1 
ATOM   3876 C  CD1 . LEU D 2 81  ? 62.428 58.978 32.638 1.00 89.34  ? 81  LEU D CD1 1 
ATOM   3877 C  CD2 . LEU D 2 81  ? 64.601 57.814 32.246 1.00 81.95  ? 81  LEU D CD2 1 
ATOM   3878 N  N   . LYS D 2 82  ? 61.494 54.444 29.388 1.00 124.75 ? 82  LYS D N   1 
ATOM   3879 C  CA  . LYS D 2 82  ? 61.023 53.054 29.302 1.00 135.83 ? 82  LYS D CA  1 
ATOM   3880 C  C   . LYS D 2 82  ? 61.906 52.181 28.393 1.00 135.78 ? 82  LYS D C   1 
ATOM   3881 O  O   . LYS D 2 82  ? 62.116 50.996 28.675 1.00 138.52 ? 82  LYS D O   1 
ATOM   3882 C  CB  . LYS D 2 82  ? 59.564 53.006 28.831 1.00 148.53 ? 82  LYS D CB  1 
ATOM   3883 C  CG  . LYS D 2 82  ? 58.574 53.601 29.822 1.00 161.31 ? 82  LYS D CG  1 
ATOM   3884 C  CD  . LYS D 2 82  ? 57.143 53.487 29.317 1.00 178.24 ? 82  LYS D CD  1 
ATOM   3885 C  CE  . LYS D 2 82  ? 56.143 54.007 30.340 1.00 186.71 ? 82  LYS D CE  1 
ATOM   3886 N  NZ  . LYS D 2 82  ? 54.735 53.884 29.866 1.00 187.30 ? 82  LYS D NZ  1 
ATOM   3887 N  N   . GLY D 2 83  ? 62.413 52.769 27.312 1.00 125.98 ? 83  GLY D N   1 
ATOM   3888 C  CA  . GLY D 2 83  ? 63.359 52.092 26.430 1.00 120.05 ? 83  GLY D CA  1 
ATOM   3889 C  C   . GLY D 2 83  ? 64.717 51.867 27.069 1.00 113.42 ? 83  GLY D C   1 
ATOM   3890 O  O   . GLY D 2 83  ? 65.368 50.851 26.812 1.00 120.06 ? 83  GLY D O   1 
ATOM   3891 N  N   . THR D 2 84  ? 65.147 52.820 27.893 1.00 99.35  ? 84  THR D N   1 
ATOM   3892 C  CA  . THR D 2 84  ? 66.434 52.743 28.579 1.00 94.07  ? 84  THR D CA  1 
ATOM   3893 C  C   . THR D 2 84  ? 66.470 51.608 29.607 1.00 89.87  ? 84  THR D C   1 
ATOM   3894 O  O   . THR D 2 84  ? 67.331 50.725 29.547 1.00 87.29  ? 84  THR D O   1 
ATOM   3895 C  CB  . THR D 2 84  ? 66.740 54.077 29.287 1.00 95.97  ? 84  THR D CB  1 
ATOM   3896 O  OG1 . THR D 2 84  ? 66.663 55.148 28.339 1.00 97.22  ? 84  THR D OG1 1 
ATOM   3897 C  CG2 . THR D 2 84  ? 68.125 54.058 29.928 1.00 99.57  ? 84  THR D CG2 1 
ATOM   3898 N  N   . PHE D 2 85  ? 65.516 51.643 30.534 1.00 83.66  ? 85  PHE D N   1 
ATOM   3899 C  CA  . PHE D 2 85  ? 65.439 50.695 31.644 1.00 76.90  ? 85  PHE D CA  1 
ATOM   3900 C  C   . PHE D 2 85  ? 64.525 49.532 31.279 1.00 77.79  ? 85  PHE D C   1 
ATOM   3901 O  O   . PHE D 2 85  ? 63.506 49.297 31.930 1.00 79.42  ? 85  PHE D O   1 
ATOM   3902 C  CB  . PHE D 2 85  ? 64.904 51.404 32.892 1.00 72.96  ? 85  PHE D CB  1 
ATOM   3903 C  CG  . PHE D 2 85  ? 65.797 52.494 33.402 1.00 68.64  ? 85  PHE D CG  1 
ATOM   3904 C  CD1 . PHE D 2 85  ? 66.973 52.175 34.064 1.00 65.87  ? 85  PHE D CD1 1 
ATOM   3905 C  CD2 . PHE D 2 85  ? 65.462 53.835 33.240 1.00 66.99  ? 85  PHE D CD2 1 
ATOM   3906 C  CE1 . PHE D 2 85  ? 67.813 53.160 34.552 1.00 63.10  ? 85  PHE D CE1 1 
ATOM   3907 C  CE2 . PHE D 2 85  ? 66.300 54.831 33.723 1.00 65.81  ? 85  PHE D CE2 1 
ATOM   3908 C  CZ  . PHE D 2 85  ? 67.474 54.491 34.381 1.00 64.96  ? 85  PHE D CZ  1 
ATOM   3909 N  N   . ALA D 2 86  ? 64.884 48.808 30.230 1.00 79.29  ? 86  ALA D N   1 
ATOM   3910 C  CA  . ALA D 2 86  ? 64.058 47.709 29.756 1.00 83.30  ? 86  ALA D CA  1 
ATOM   3911 C  C   . ALA D 2 86  ? 64.527 46.417 30.395 1.00 82.73  ? 86  ALA D C   1 
ATOM   3912 O  O   . ALA D 2 86  ? 63.745 45.720 31.032 1.00 83.39  ? 86  ALA D O   1 
ATOM   3913 C  CB  . ALA D 2 86  ? 64.125 47.610 28.247 1.00 89.35  ? 86  ALA D CB  1 
ATOM   3914 N  N   . THR D 2 87  ? 65.810 46.113 30.224 1.00 85.29  ? 87  THR D N   1 
ATOM   3915 C  CA  . THR D 2 87  ? 66.408 44.892 30.770 1.00 88.84  ? 87  THR D CA  1 
ATOM   3916 C  C   . THR D 2 87  ? 66.457 44.901 32.303 1.00 84.28  ? 87  THR D C   1 
ATOM   3917 O  O   . THR D 2 87  ? 66.401 43.839 32.934 1.00 84.68  ? 87  THR D O   1 
ATOM   3918 C  CB  . THR D 2 87  ? 67.835 44.671 30.212 1.00 97.35  ? 87  THR D CB  1 
ATOM   3919 O  OG1 . THR D 2 87  ? 67.814 44.753 28.780 1.00 98.44  ? 87  THR D OG1 1 
ATOM   3920 C  CG2 . THR D 2 87  ? 68.395 43.307 30.630 1.00 102.22 ? 87  THR D CG2 1 
ATOM   3921 N  N   . LEU D 2 88  ? 66.561 46.090 32.897 1.00 73.99  ? 88  LEU D N   1 
ATOM   3922 C  CA  . LEU D 2 88  ? 66.585 46.204 34.350 1.00 66.11  ? 88  LEU D CA  1 
ATOM   3923 C  C   . LEU D 2 88  ? 65.217 45.951 34.956 1.00 62.70  ? 88  LEU D C   1 
ATOM   3924 O  O   . LEU D 2 88  ? 65.109 45.214 35.938 1.00 62.59  ? 88  LEU D O   1 
ATOM   3925 C  CB  . LEU D 2 88  ? 67.142 47.559 34.795 1.00 63.91  ? 88  LEU D CB  1 
ATOM   3926 C  CG  . LEU D 2 88  ? 68.657 47.754 34.631 1.00 62.10  ? 88  LEU D CG  1 
ATOM   3927 C  CD1 . LEU D 2 88  ? 69.062 49.112 35.173 1.00 62.27  ? 88  LEU D CD1 1 
ATOM   3928 C  CD2 . LEU D 2 88  ? 69.494 46.678 35.313 1.00 61.45  ? 88  LEU D CD2 1 
ATOM   3929 N  N   . SER D 2 89  ? 64.171 46.530 34.372 1.00 59.75  ? 89  SER D N   1 
ATOM   3930 C  CA  . SER D 2 89  ? 62.815 46.225 34.826 1.00 61.30  ? 89  SER D CA  1 
ATOM   3931 C  C   . SER D 2 89  ? 62.541 44.724 34.783 1.00 64.60  ? 89  SER D C   1 
ATOM   3932 O  O   . SER D 2 89  ? 61.885 44.204 35.672 1.00 69.04  ? 89  SER D O   1 
ATOM   3933 C  CB  . SER D 2 89  ? 61.751 46.999 34.039 1.00 60.77  ? 89  SER D CB  1 
ATOM   3934 O  OG  . SER D 2 89  ? 61.985 46.952 32.645 1.00 65.33  ? 89  SER D OG  1 
ATOM   3935 N  N   . GLU D 2 90  ? 63.071 44.036 33.772 1.00 72.52  ? 90  GLU D N   1 
ATOM   3936 C  CA  . GLU D 2 90  ? 62.979 42.574 33.684 1.00 77.63  ? 90  GLU D CA  1 
ATOM   3937 C  C   . GLU D 2 90  ? 63.812 41.937 34.788 1.00 69.47  ? 90  GLU D C   1 
ATOM   3938 O  O   . GLU D 2 90  ? 63.363 41.006 35.458 1.00 68.16  ? 90  GLU D O   1 
ATOM   3939 C  CB  . GLU D 2 90  ? 63.494 42.061 32.334 1.00 94.93  ? 90  GLU D CB  1 
ATOM   3940 C  CG  . GLU D 2 90  ? 62.768 42.588 31.093 1.00 111.76 ? 90  GLU D CG  1 
ATOM   3941 C  CD  . GLU D 2 90  ? 61.489 41.845 30.739 1.00 127.92 ? 90  GLU D CD  1 
ATOM   3942 O  OE1 . GLU D 2 90  ? 61.291 40.695 31.192 1.00 139.82 ? 90  GLU D OE1 1 
ATOM   3943 O  OE2 . GLU D 2 90  ? 60.680 42.421 29.979 1.00 135.69 ? 90  GLU D OE2 1 
ATOM   3944 N  N   . LEU D 2 91  ? 65.031 42.445 34.956 1.00 61.12  ? 91  LEU D N   1 
ATOM   3945 C  CA  . LEU D 2 91  ? 65.975 41.913 35.934 1.00 57.33  ? 91  LEU D CA  1 
ATOM   3946 C  C   . LEU D 2 91  ? 65.442 41.998 37.357 1.00 52.92  ? 91  LEU D C   1 
ATOM   3947 O  O   . LEU D 2 91  ? 65.380 40.986 38.060 1.00 52.33  ? 91  LEU D O   1 
ATOM   3948 C  CB  . LEU D 2 91  ? 67.318 42.657 35.847 1.00 58.05  ? 91  LEU D CB  1 
ATOM   3949 C  CG  . LEU D 2 91  ? 68.388 42.323 36.899 1.00 59.16  ? 91  LEU D CG  1 
ATOM   3950 C  CD1 . LEU D 2 91  ? 68.622 40.823 36.999 1.00 61.40  ? 91  LEU D CD1 1 
ATOM   3951 C  CD2 . LEU D 2 91  ? 69.687 43.051 36.595 1.00 58.81  ? 91  LEU D CD2 1 
ATOM   3952 N  N   . HIS D 2 92  ? 65.086 43.214 37.773 1.00 45.72  ? 92  HIS D N   1 
ATOM   3953 C  CA  . HIS D 2 92  ? 64.638 43.459 39.133 1.00 38.34  ? 92  HIS D CA  1 
ATOM   3954 C  C   . HIS D 2 92  ? 63.258 42.788 39.372 1.00 41.06  ? 92  HIS D C   1 
ATOM   3955 O  O   . HIS D 2 92  ? 62.993 42.362 40.488 1.00 41.34  ? 92  HIS D O   1 
ATOM   3956 C  CB  . HIS D 2 92  ? 64.617 44.962 39.461 1.00 32.52  ? 92  HIS D CB  1 
ATOM   3957 C  CG  . HIS D 2 92  ? 65.971 45.605 39.674 1.00 30.42  ? 92  HIS D CG  1 
ATOM   3958 N  ND1 . HIS D 2 92  ? 66.532 46.446 38.743 1.00 29.10  ? 92  HIS D ND1 1 
ATOM   3959 C  CD2 . HIS D 2 92  ? 66.816 45.637 40.746 1.00 32.01  ? 92  HIS D CD2 1 
ATOM   3960 C  CE1 . HIS D 2 92  ? 67.680 46.926 39.199 1.00 29.73  ? 92  HIS D CE1 1 
ATOM   3961 N  NE2 . HIS D 2 92  ? 67.876 46.478 40.432 1.00 30.87  ? 92  HIS D NE2 1 
ATOM   3962 N  N   . CYS D 2 93  ? 62.416 42.631 38.343 1.00 48.77  ? 93  CYS D N   1 
ATOM   3963 C  CA  . CYS D 2 93  ? 61.092 41.964 38.500 1.00 60.97  ? 93  CYS D CA  1 
ATOM   3964 C  C   . CYS D 2 93  ? 61.053 40.429 38.391 1.00 66.89  ? 93  CYS D C   1 
ATOM   3965 O  O   . CYS D 2 93  ? 60.535 39.746 39.287 1.00 64.23  ? 93  CYS D O   1 
ATOM   3966 C  CB  . CYS D 2 93  ? 60.072 42.513 37.488 1.00 68.86  ? 93  CYS D CB  1 
ATOM   3967 S  SG  . CYS D 2 93  ? 58.424 41.730 37.538 1.00 78.50  ? 93  CYS D SG  1 
ATOM   3968 N  N   . ASP D 2 94  ? 61.535 39.900 37.272 1.00 77.49  ? 94  ASP D N   1 
ATOM   3969 C  CA  . ASP D 2 94  ? 61.312 38.490 36.944 1.00 92.27  ? 94  ASP D CA  1 
ATOM   3970 C  C   . ASP D 2 94  ? 62.244 37.526 37.672 1.00 91.59  ? 94  ASP D C   1 
ATOM   3971 O  O   . ASP D 2 94  ? 61.954 36.330 37.731 1.00 102.91 ? 94  ASP D O   1 
ATOM   3972 C  CB  . ASP D 2 94  ? 61.394 38.251 35.421 1.00 110.96 ? 94  ASP D CB  1 
ATOM   3973 C  CG  . ASP D 2 94  ? 60.131 38.703 34.674 1.00 122.79 ? 94  ASP D CG  1 
ATOM   3974 O  OD1 . ASP D 2 94  ? 59.003 38.461 35.165 1.00 129.54 ? 94  ASP D OD1 1 
ATOM   3975 O  OD2 . ASP D 2 94  ? 60.269 39.284 33.576 1.00 125.55 ? 94  ASP D OD2 1 
ATOM   3976 N  N   . LYS D 2 95  ? 63.344 38.029 38.224 1.00 85.69  ? 95  LYS D N   1 
ATOM   3977 C  CA  . LYS D 2 95  ? 64.337 37.174 38.861 1.00 86.12  ? 95  LYS D CA  1 
ATOM   3978 C  C   . LYS D 2 95  ? 64.486 37.479 40.352 1.00 79.02  ? 95  LYS D C   1 
ATOM   3979 O  O   . LYS D 2 95  ? 64.312 36.594 41.189 1.00 83.71  ? 95  LYS D O   1 
ATOM   3980 C  CB  . LYS D 2 95  ? 65.670 37.318 38.119 1.00 98.41  ? 95  LYS D CB  1 
ATOM   3981 C  CG  . LYS D 2 95  ? 66.664 36.185 38.355 1.00 110.71 ? 95  LYS D CG  1 
ATOM   3982 C  CD  . LYS D 2 95  ? 67.802 36.582 39.291 1.00 123.39 ? 95  LYS D CD  1 
ATOM   3983 C  CE  . LYS D 2 95  ? 68.868 37.403 38.571 1.00 131.63 ? 95  LYS D CE  1 
ATOM   3984 N  NZ  . LYS D 2 95  ? 70.044 37.721 39.434 1.00 132.71 ? 95  LYS D NZ  1 
ATOM   3985 N  N   . LEU D 2 96  ? 64.796 38.730 40.674 1.00 69.88  ? 96  LEU D N   1 
ATOM   3986 C  CA  . LEU D 2 96  ? 65.081 39.149 42.051 1.00 62.31  ? 96  LEU D CA  1 
ATOM   3987 C  C   . LEU D 2 96  ? 63.839 39.309 42.928 1.00 61.25  ? 96  LEU D C   1 
ATOM   3988 O  O   . LEU D 2 96  ? 63.916 39.091 44.137 1.00 59.88  ? 96  LEU D O   1 
ATOM   3989 C  CB  . LEU D 2 96  ? 65.857 40.460 42.024 1.00 59.75  ? 96  LEU D CB  1 
ATOM   3990 C  CG  . LEU D 2 96  ? 67.229 40.334 41.363 1.00 59.19  ? 96  LEU D CG  1 
ATOM   3991 C  CD1 . LEU D 2 96  ? 67.712 41.681 40.851 1.00 60.07  ? 96  LEU D CD1 1 
ATOM   3992 C  CD2 . LEU D 2 96  ? 68.225 39.713 42.337 1.00 60.43  ? 96  LEU D CD2 1 
ATOM   3993 N  N   . HIS D 2 97  ? 62.719 39.702 42.311 1.00 60.45  ? 97  HIS D N   1 
ATOM   3994 C  CA  . HIS D 2 97  ? 61.427 39.936 42.979 1.00 60.60  ? 97  HIS D CA  1 
ATOM   3995 C  C   . HIS D 2 97  ? 61.433 41.140 43.925 1.00 52.00  ? 97  HIS D C   1 
ATOM   3996 O  O   . HIS D 2 97  ? 60.776 41.112 44.962 1.00 56.66  ? 97  HIS D O   1 
ATOM   3997 C  CB  . HIS D 2 97  ? 60.933 38.690 43.744 1.00 71.96  ? 97  HIS D CB  1 
ATOM   3998 C  CG  . HIS D 2 97  ? 60.866 37.438 42.921 1.00 84.98  ? 97  HIS D CG  1 
ATOM   3999 N  ND1 . HIS D 2 97  ? 59.792 37.139 42.109 1.00 93.37  ? 97  HIS D ND1 1 
ATOM   4000 C  CD2 . HIS D 2 97  ? 61.715 36.387 42.824 1.00 88.05  ? 97  HIS D CD2 1 
ATOM   4001 C  CE1 . HIS D 2 97  ? 59.993 35.968 41.530 1.00 97.80  ? 97  HIS D CE1 1 
ATOM   4002 N  NE2 . HIS D 2 97  ? 61.153 35.491 41.946 1.00 93.13  ? 97  HIS D NE2 1 
ATOM   4003 N  N   . VAL D 2 98  ? 62.166 42.194 43.575 1.00 44.07  ? 98  VAL D N   1 
ATOM   4004 C  CA  . VAL D 2 98  ? 62.201 43.428 44.372 1.00 39.46  ? 98  VAL D CA  1 
ATOM   4005 C  C   . VAL D 2 98  ? 60.893 44.143 44.087 1.00 39.53  ? 98  VAL D C   1 
ATOM   4006 O  O   . VAL D 2 98  ? 60.649 44.494 42.942 1.00 38.10  ? 98  VAL D O   1 
ATOM   4007 C  CB  . VAL D 2 98  ? 63.405 44.334 43.966 1.00 36.43  ? 98  VAL D CB  1 
ATOM   4008 C  CG1 . VAL D 2 98  ? 63.304 45.729 44.561 1.00 36.27  ? 98  VAL D CG1 1 
ATOM   4009 C  CG2 . VAL D 2 98  ? 64.735 43.701 44.355 1.00 33.95  ? 98  VAL D CG2 1 
ATOM   4010 N  N   . ASP D 2 99  ? 60.054 44.354 45.104 1.00 44.84  ? 99  ASP D N   1 
ATOM   4011 C  CA  . ASP D 2 99  ? 58.737 45.020 44.897 1.00 50.75  ? 99  ASP D CA  1 
ATOM   4012 C  C   . ASP D 2 99  ? 58.847 46.545 44.732 1.00 45.68  ? 99  ASP D C   1 
ATOM   4013 O  O   . ASP D 2 99  ? 59.673 47.180 45.390 1.00 46.72  ? 99  ASP D O   1 
ATOM   4014 C  CB  . ASP D 2 99  ? 57.739 44.688 46.009 1.00 62.65  ? 99  ASP D CB  1 
ATOM   4015 C  CG  . ASP D 2 99  ? 58.231 45.099 47.394 1.00 80.43  ? 99  ASP D CG  1 
ATOM   4016 O  OD1 . ASP D 2 99  ? 59.464 45.196 47.596 1.00 93.62  ? 99  ASP D OD1 1 
ATOM   4017 O  OD2 . ASP D 2 99  ? 57.384 45.306 48.289 1.00 88.52  ? 99  ASP D OD2 1 
ATOM   4018 N  N   . PRO D 2 100 ? 57.995 47.140 43.883 1.00 41.63  ? 100 PRO D N   1 
ATOM   4019 C  CA  . PRO D 2 100 ? 58.273 48.473 43.363 1.00 42.86  ? 100 PRO D CA  1 
ATOM   4020 C  C   . PRO D 2 100 ? 58.188 49.664 44.330 1.00 46.51  ? 100 PRO D C   1 
ATOM   4021 O  O   . PRO D 2 100 ? 58.597 50.771 43.954 1.00 48.00  ? 100 PRO D O   1 
ATOM   4022 C  CB  . PRO D 2 100 ? 57.229 48.641 42.253 1.00 43.31  ? 100 PRO D CB  1 
ATOM   4023 C  CG  . PRO D 2 100 ? 56.668 47.288 42.028 1.00 42.67  ? 100 PRO D CG  1 
ATOM   4024 C  CD  . PRO D 2 100 ? 56.706 46.663 43.381 1.00 42.49  ? 100 PRO D CD  1 
ATOM   4025 N  N   . GLU D 2 101 ? 57.660 49.462 45.537 1.00 46.40  ? 101 GLU D N   1 
ATOM   4026 C  CA  . GLU D 2 101 ? 57.775 50.473 46.585 1.00 45.60  ? 101 GLU D CA  1 
ATOM   4027 C  C   . GLU D 2 101 ? 59.237 50.747 46.948 1.00 37.40  ? 101 GLU D C   1 
ATOM   4028 O  O   . GLU D 2 101 ? 59.583 51.868 47.319 1.00 37.25  ? 101 GLU D O   1 
ATOM   4029 C  CB  . GLU D 2 101 ? 56.984 50.057 47.832 1.00 59.13  ? 101 GLU D CB  1 
ATOM   4030 C  CG  . GLU D 2 101 ? 57.150 50.953 49.080 1.00 76.58  ? 101 GLU D CG  1 
ATOM   4031 C  CD  . GLU D 2 101 ? 56.830 52.449 48.875 1.00 87.49  ? 101 GLU D CD  1 
ATOM   4032 O  OE1 . GLU D 2 101 ? 56.048 52.803 47.954 1.00 95.02  ? 101 GLU D OE1 1 
ATOM   4033 O  OE2 . GLU D 2 101 ? 57.353 53.278 49.665 1.00 80.90  ? 101 GLU D OE2 1 
ATOM   4034 N  N   . ASN D 2 102 ? 60.094 49.737 46.834 1.00 30.67  ? 102 ASN D N   1 
ATOM   4035 C  CA  . ASN D 2 102 ? 61.498 49.899 47.186 1.00 26.07  ? 102 ASN D CA  1 
ATOM   4036 C  C   . ASN D 2 102 ? 62.251 50.818 46.253 1.00 23.60  ? 102 ASN D C   1 
ATOM   4037 O  O   . ASN D 2 102 ? 63.234 51.403 46.678 1.00 23.71  ? 102 ASN D O   1 
ATOM   4038 C  CB  . ASN D 2 102 ? 62.191 48.554 47.248 1.00 25.73  ? 102 ASN D CB  1 
ATOM   4039 C  CG  . ASN D 2 102 ? 61.604 47.640 48.312 1.00 26.67  ? 102 ASN D CG  1 
ATOM   4040 O  OD1 . ASN D 2 102 ? 60.936 48.079 49.255 1.00 27.46  ? 102 ASN D OD1 1 
ATOM   4041 N  ND2 . ASN D 2 102 ? 61.855 46.351 48.164 1.00 27.56  ? 102 ASN D ND2 1 
ATOM   4042 N  N   . PHE D 2 103 ? 61.792 50.978 45.010 1.00 22.81  ? 103 PHE D N   1 
ATOM   4043 C  CA  . PHE D 2 103 ? 62.451 51.890 44.062 1.00 22.19  ? 103 PHE D CA  1 
ATOM   4044 C  C   . PHE D 2 103 ? 62.285 53.325 44.466 1.00 22.31  ? 103 PHE D C   1 
ATOM   4045 O  O   . PHE D 2 103 ? 63.269 54.060 44.486 1.00 22.30  ? 103 PHE D O   1 
ATOM   4046 C  CB  . PHE D 2 103 ? 61.985 51.686 42.622 1.00 21.89  ? 103 PHE D CB  1 
ATOM   4047 C  CG  . PHE D 2 103 ? 62.170 50.281 42.146 1.00 22.38  ? 103 PHE D CG  1 
ATOM   4048 C  CD1 . PHE D 2 103 ? 63.431 49.689 42.175 1.00 22.87  ? 103 PHE D CD1 1 
ATOM   4049 C  CD2 . PHE D 2 103 ? 61.091 49.523 41.728 1.00 22.28  ? 103 PHE D CD2 1 
ATOM   4050 C  CE1 . PHE D 2 103 ? 63.616 48.369 41.786 1.00 22.77  ? 103 PHE D CE1 1 
ATOM   4051 C  CE2 . PHE D 2 103 ? 61.267 48.201 41.332 1.00 22.93  ? 103 PHE D CE2 1 
ATOM   4052 C  CZ  . PHE D 2 103 ? 62.531 47.620 41.360 1.00 22.77  ? 103 PHE D CZ  1 
ATOM   4053 N  N   . ARG D 2 104 ? 61.072 53.728 44.824 1.00 23.73  ? 104 ARG D N   1 
ATOM   4054 C  CA  . ARG D 2 104 ? 60.884 55.100 45.285 1.00 26.78  ? 104 ARG D CA  1 
ATOM   4055 C  C   . ARG D 2 104 ? 61.525 55.410 46.655 1.00 23.21  ? 104 ARG D C   1 
ATOM   4056 O  O   . ARG D 2 104 ? 61.677 56.586 47.000 1.00 22.17  ? 104 ARG D O   1 
ATOM   4057 C  CB  . ARG D 2 104 ? 59.413 55.505 45.253 1.00 34.56  ? 104 ARG D CB  1 
ATOM   4058 C  CG  . ARG D 2 104 ? 58.557 54.987 46.393 1.00 44.99  ? 104 ARG D CG  1 
ATOM   4059 C  CD  . ARG D 2 104 ? 57.374 55.906 46.680 1.00 55.25  ? 104 ARG D CD  1 
ATOM   4060 N  NE  . ARG D 2 104 ? 57.755 57.164 47.353 1.00 64.72  ? 104 ARG D NE  1 
ATOM   4061 C  CZ  . ARG D 2 104 ? 58.029 57.315 48.661 1.00 73.23  ? 104 ARG D CZ  1 
ATOM   4062 N  NH1 . ARG D 2 104 ? 58.006 56.281 49.513 1.00 71.98  ? 104 ARG D NH1 1 
ATOM   4063 N  NH2 . ARG D 2 104 ? 58.344 58.528 49.128 1.00 75.95  ? 104 ARG D NH2 1 
ATOM   4064 N  N   . LEU D 2 105 ? 61.874 54.370 47.426 1.00 20.10  ? 105 LEU D N   1 
ATOM   4065 C  CA  . LEU D 2 105 ? 62.702 54.527 48.626 1.00 17.92  ? 105 LEU D CA  1 
ATOM   4066 C  C   . LEU D 2 105 ? 64.120 54.849 48.262 1.00 16.27  ? 105 LEU D C   1 
ATOM   4067 O  O   . LEU D 2 105 ? 64.665 55.801 48.807 1.00 17.24  ? 105 LEU D O   1 
ATOM   4068 C  CB  . LEU D 2 105 ? 62.712 53.283 49.517 1.00 18.48  ? 105 LEU D CB  1 
ATOM   4069 C  CG  . LEU D 2 105 ? 61.470 52.994 50.375 1.00 18.91  ? 105 LEU D CG  1 
ATOM   4070 C  CD1 . LEU D 2 105 ? 61.659 51.746 51.241 1.00 18.64  ? 105 LEU D CD1 1 
ATOM   4071 C  CD2 . LEU D 2 105 ? 61.117 54.188 51.254 1.00 19.25  ? 105 LEU D CD2 1 
ATOM   4072 N  N   . LEU D 2 106 ? 64.726 54.081 47.355 1.00 14.63  ? 106 LEU D N   1 
ATOM   4073 C  CA  . LEU D 2 106 ? 66.121 54.344 46.943 1.00 13.86  ? 106 LEU D CA  1 
ATOM   4074 C  C   . LEU D 2 106 ? 66.315 55.728 46.372 1.00 13.32  ? 106 LEU D C   1 
ATOM   4075 O  O   . LEU D 2 106 ? 67.290 56.392 46.696 1.00 13.38  ? 106 LEU D O   1 
ATOM   4076 C  CB  . LEU D 2 106 ? 66.618 53.352 45.906 1.00 13.83  ? 106 LEU D CB  1 
ATOM   4077 C  CG  . LEU D 2 106 ? 68.115 53.471 45.592 1.00 13.81  ? 106 LEU D CG  1 
ATOM   4078 C  CD1 . LEU D 2 106 ? 68.943 53.082 46.807 1.00 13.90  ? 106 LEU D CD1 1 
ATOM   4079 C  CD2 . LEU D 2 106 ? 68.494 52.607 44.409 1.00 13.86  ? 106 LEU D CD2 1 
ATOM   4080 N  N   . GLY D 2 107 ? 65.388 56.136 45.511 1.00 13.26  ? 107 GLY D N   1 
ATOM   4081 C  CA  . GLY D 2 107 ? 65.311 57.503 44.994 1.00 13.16  ? 107 GLY D CA  1 
ATOM   4082 C  C   . GLY D 2 107 ? 65.326 58.592 46.054 1.00 13.02  ? 107 GLY D C   1 
ATOM   4083 O  O   . GLY D 2 107 ? 66.021 59.591 45.893 1.00 13.41  ? 107 GLY D O   1 
ATOM   4084 N  N   . ASN D 2 108 ? 64.578 58.409 47.137 1.00 12.94  ? 108 ASN D N   1 
ATOM   4085 C  CA  . ASN D 2 108 ? 64.563 59.400 48.208 1.00 13.15  ? 108 ASN D CA  1 
ATOM   4086 C  C   . ASN D 2 108 ? 65.819 59.406 49.051 1.00 12.91  ? 108 ASN D C   1 
ATOM   4087 O  O   . ASN D 2 108 ? 66.196 60.465 49.545 1.00 13.39  ? 108 ASN D O   1 
ATOM   4088 C  CB  . ASN D 2 108 ? 63.346 59.232 49.102 1.00 14.12  ? 108 ASN D CB  1 
ATOM   4089 C  CG  . ASN D 2 108 ? 62.086 59.809 48.474 1.00 15.43  ? 108 ASN D CG  1 
ATOM   4090 O  OD1 . ASN D 2 108 ? 61.988 59.927 47.242 1.00 16.15  ? 108 ASN D OD1 1 
ATOM   4091 N  ND2 . ASN D 2 108 ? 61.104 60.172 49.318 1.00 15.92  ? 108 ASN D ND2 1 
ATOM   4092 N  N   . VAL D 2 109 ? 66.467 58.254 49.227 1.00 12.26  ? 109 VAL D N   1 
ATOM   4093 C  CA  . VAL D 2 109 ? 67.738 58.212 49.948 1.00 11.96  ? 109 VAL D CA  1 
ATOM   4094 C  C   . VAL D 2 109 ? 68.809 58.914 49.160 1.00 12.38  ? 109 VAL D C   1 
ATOM   4095 O  O   . VAL D 2 109 ? 69.621 59.634 49.727 1.00 12.66  ? 109 VAL D O   1 
ATOM   4096 C  CB  . VAL D 2 109 ? 68.200 56.791 50.228 1.00 11.94  ? 109 VAL D CB  1 
ATOM   4097 C  CG1 . VAL D 2 109 ? 69.619 56.775 50.779 1.00 12.04  ? 109 VAL D CG1 1 
ATOM   4098 C  CG2 . VAL D 2 109 ? 67.273 56.146 51.243 1.00 12.35  ? 109 VAL D CG2 1 
ATOM   4099 N  N   . LEU D 2 110 ? 68.806 58.716 47.850 1.00 13.38  ? 110 LEU D N   1 
ATOM   4100 C  CA  . LEU D 2 110 ? 69.708 59.447 46.957 1.00 14.06  ? 110 LEU D CA  1 
ATOM   4101 C  C   . LEU D 2 110 ? 69.662 60.950 47.151 1.00 14.38  ? 110 LEU D C   1 
ATOM   4102 O  O   . LEU D 2 110 ? 70.701 61.580 47.343 1.00 15.04  ? 110 LEU D O   1 
ATOM   4103 C  CB  . LEU D 2 110 ? 69.387 59.157 45.497 1.00 14.28  ? 110 LEU D CB  1 
ATOM   4104 C  CG  . LEU D 2 110 ? 70.437 59.628 44.504 1.00 14.97  ? 110 LEU D CG  1 
ATOM   4105 C  CD1 . LEU D 2 110 ? 71.807 59.064 44.823 1.00 15.12  ? 110 LEU D CD1 1 
ATOM   4106 C  CD2 . LEU D 2 110 ? 70.022 59.158 43.130 1.00 15.91  ? 110 LEU D CD2 1 
ATOM   4107 N  N   . VAL D 2 111 ? 68.460 61.512 47.105 1.00 14.42  ? 111 VAL D N   1 
ATOM   4108 C  CA  . VAL D 2 111 ? 68.272 62.948 47.278 1.00 14.55  ? 111 VAL D CA  1 
ATOM   4109 C  C   . VAL D 2 111 ? 68.730 63.448 48.638 1.00 15.13  ? 111 VAL D C   1 
ATOM   4110 O  O   . VAL D 2 111 ? 69.166 64.578 48.739 1.00 15.18  ? 111 VAL D O   1 
ATOM   4111 C  CB  . VAL D 2 111 ? 66.816 63.356 46.978 1.00 14.57  ? 111 VAL D CB  1 
ATOM   4112 C  CG1 . VAL D 2 111 ? 66.475 64.749 47.500 1.00 14.63  ? 111 VAL D CG1 1 
ATOM   4113 C  CG2 . VAL D 2 111 ? 66.585 63.299 45.472 1.00 14.67  ? 111 VAL D CG2 1 
ATOM   4114 N  N   . CYS D 2 112 ? 68.658 62.619 49.672 1.00 17.35  ? 112 CYS D N   1 
ATOM   4115 C  CA  . CYS D 2 112 ? 69.226 62.988 50.973 1.00 19.36  ? 112 CYS D CA  1 
ATOM   4116 C  C   . CYS D 2 112 ? 70.738 63.009 50.971 1.00 19.22  ? 112 CYS D C   1 
ATOM   4117 O  O   . CYS D 2 112 ? 71.324 63.883 51.599 1.00 19.77  ? 112 CYS D O   1 
ATOM   4118 C  CB  . CYS D 2 112 ? 68.756 62.060 52.076 1.00 21.68  ? 112 CYS D CB  1 
ATOM   4119 S  SG  . CYS D 2 112 ? 67.058 62.388 52.587 1.00 27.55  ? 112 CYS D SG  1 
ATOM   4120 N  N   . VAL D 2 113 ? 71.362 62.060 50.282 1.00 19.42  ? 113 VAL D N   1 
ATOM   4121 C  CA  . VAL D 2 113 ? 72.819 62.053 50.127 1.00 20.91  ? 113 VAL D CA  1 
ATOM   4122 C  C   . VAL D 2 113 ? 73.353 63.273 49.378 1.00 21.54  ? 113 VAL D C   1 
ATOM   4123 O  O   . VAL D 2 113 ? 74.414 63.792 49.715 1.00 21.18  ? 113 VAL D O   1 
ATOM   4124 C  CB  . VAL D 2 113 ? 73.291 60.765 49.423 1.00 22.38  ? 113 VAL D CB  1 
ATOM   4125 C  CG1 . VAL D 2 113 ? 74.727 60.870 48.897 1.00 22.32  ? 113 VAL D CG1 1 
ATOM   4126 C  CG2 . VAL D 2 113 ? 73.169 59.603 50.394 1.00 23.51  ? 113 VAL D CG2 1 
ATOM   4127 N  N   . LEU D 2 114 ? 72.631 63.712 48.357 1.00 23.39  ? 114 LEU D N   1 
ATOM   4128 C  CA  . LEU D 2 114 ? 73.040 64.873 47.593 1.00 24.99  ? 114 LEU D CA  1 
ATOM   4129 C  C   . LEU D 2 114 ? 72.957 66.150 48.417 1.00 25.82  ? 114 LEU D C   1 
ATOM   4130 O  O   . LEU D 2 114 ? 73.922 66.908 48.454 1.00 28.50  ? 114 LEU D O   1 
ATOM   4131 C  CB  . LEU D 2 114 ? 72.231 64.991 46.310 1.00 26.85  ? 114 LEU D CB  1 
ATOM   4132 C  CG  . LEU D 2 114 ? 72.566 63.867 45.318 1.00 29.69  ? 114 LEU D CG  1 
ATOM   4133 C  CD1 . LEU D 2 114 ? 71.562 63.845 44.171 1.00 31.62  ? 114 LEU D CD1 1 
ATOM   4134 C  CD2 . LEU D 2 114 ? 73.991 63.989 44.782 1.00 30.01  ? 114 LEU D CD2 1 
ATOM   4135 N  N   . ALA D 2 115 ? 71.848 66.385 49.101 1.00 26.28  ? 115 ALA D N   1 
ATOM   4136 C  CA  . ALA D 2 115 ? 71.762 67.526 50.014 1.00 27.94  ? 115 ALA D CA  1 
ATOM   4137 C  C   . ALA D 2 115 ? 72.830 67.498 51.120 1.00 31.57  ? 115 ALA D C   1 
ATOM   4138 O  O   . ALA D 2 115 ? 73.292 68.545 51.554 1.00 33.75  ? 115 ALA D O   1 
ATOM   4139 C  CB  . ALA D 2 115 ? 70.387 67.609 50.634 1.00 27.81  ? 115 ALA D CB  1 
ATOM   4140 N  N   . HIS D 2 116 ? 73.223 66.314 51.572 1.00 36.04  ? 116 HIS D N   1 
ATOM   4141 C  CA  . HIS D 2 116 ? 74.325 66.185 52.525 1.00 41.54  ? 116 HIS D CA  1 
ATOM   4142 C  C   . HIS D 2 116 ? 75.645 66.691 51.974 1.00 46.21  ? 116 HIS D C   1 
ATOM   4143 O  O   . HIS D 2 116 ? 76.395 67.341 52.691 1.00 47.23  ? 116 HIS D O   1 
ATOM   4144 C  CB  . HIS D 2 116 ? 74.510 64.723 52.908 1.00 47.83  ? 116 HIS D CB  1 
ATOM   4145 C  CG  . HIS D 2 116 ? 75.363 64.506 54.117 1.00 52.07  ? 116 HIS D CG  1 
ATOM   4146 N  ND1 . HIS D 2 116 ? 76.127 63.372 54.288 1.00 54.60  ? 116 HIS D ND1 1 
ATOM   4147 C  CD2 . HIS D 2 116 ? 75.554 65.260 55.225 1.00 56.35  ? 116 HIS D CD2 1 
ATOM   4148 C  CE1 . HIS D 2 116 ? 76.757 63.440 55.447 1.00 58.10  ? 116 HIS D CE1 1 
ATOM   4149 N  NE2 . HIS D 2 116 ? 76.426 64.576 56.036 1.00 57.78  ? 116 HIS D NE2 1 
ATOM   4150 N  N   . HIS D 2 117 ? 75.934 66.363 50.715 1.00 55.13  ? 117 HIS D N   1 
ATOM   4151 C  CA  . HIS D 2 117 ? 77.184 66.781 50.068 1.00 64.46  ? 117 HIS D CA  1 
ATOM   4152 C  C   . HIS D 2 117 ? 77.186 68.242 49.663 1.00 65.64  ? 117 HIS D C   1 
ATOM   4153 O  O   . HIS D 2 117 ? 78.126 68.967 49.993 1.00 71.57  ? 117 HIS D O   1 
ATOM   4154 C  CB  . HIS D 2 117 ? 77.506 65.938 48.829 1.00 73.53  ? 117 HIS D CB  1 
ATOM   4155 C  CG  . HIS D 2 117 ? 78.154 64.628 49.140 1.00 85.78  ? 117 HIS D CG  1 
ATOM   4156 N  ND1 . HIS D 2 117 ? 78.432 63.693 48.166 1.00 95.04  ? 117 HIS D ND1 1 
ATOM   4157 C  CD2 . HIS D 2 117 ? 78.570 64.088 50.310 1.00 96.22  ? 117 HIS D CD2 1 
ATOM   4158 C  CE1 . HIS D 2 117 ? 79.000 62.638 48.722 1.00 102.52 ? 117 HIS D CE1 1 
ATOM   4159 N  NE2 . HIS D 2 117 ? 79.095 62.851 50.022 1.00 103.07 ? 117 HIS D NE2 1 
ATOM   4160 N  N   . PHE D 2 118 ? 76.158 68.674 48.940 1.00 64.87  ? 118 PHE D N   1 
ATOM   4161 C  CA  . PHE D 2 118 ? 76.124 70.046 48.418 1.00 70.17  ? 118 PHE D CA  1 
ATOM   4162 C  C   . PHE D 2 118 ? 75.578 71.110 49.380 1.00 74.59  ? 118 PHE D C   1 
ATOM   4163 O  O   . PHE D 2 118 ? 75.531 72.289 49.012 1.00 76.73  ? 118 PHE D O   1 
ATOM   4164 C  CB  . PHE D 2 118 ? 75.347 70.116 47.102 1.00 72.33  ? 118 PHE D CB  1 
ATOM   4165 C  CG  . PHE D 2 118 ? 75.843 69.181 46.036 1.00 76.54  ? 118 PHE D CG  1 
ATOM   4166 C  CD1 . PHE D 2 118 ? 77.176 68.752 45.985 1.00 79.71  ? 118 PHE D CD1 1 
ATOM   4167 C  CD2 . PHE D 2 118 ? 74.962 68.753 45.046 1.00 81.15  ? 118 PHE D CD2 1 
ATOM   4168 C  CE1 . PHE D 2 118 ? 77.600 67.895 44.988 1.00 85.48  ? 118 PHE D CE1 1 
ATOM   4169 C  CE2 . PHE D 2 118 ? 75.380 67.899 44.046 1.00 86.03  ? 118 PHE D CE2 1 
ATOM   4170 C  CZ  . PHE D 2 118 ? 76.702 67.468 44.017 1.00 91.08  ? 118 PHE D CZ  1 
ATOM   4171 N  N   . GLY D 2 119 ? 75.177 70.717 50.593 1.00 76.84  ? 119 GLY D N   1 
ATOM   4172 C  CA  . GLY D 2 119 ? 74.792 71.673 51.634 1.00 79.94  ? 119 GLY D CA  1 
ATOM   4173 C  C   . GLY D 2 119 ? 73.800 72.708 51.134 1.00 89.04  ? 119 GLY D C   1 
ATOM   4174 O  O   . GLY D 2 119 ? 72.709 72.357 50.687 1.00 96.19  ? 119 GLY D O   1 
ATOM   4175 N  N   . LYS D 2 120 ? 74.192 73.979 51.168 1.00 99.98  ? 120 LYS D N   1 
ATOM   4176 C  CA  . LYS D 2 120 ? 73.294 75.074 50.783 1.00 111.11 ? 120 LYS D CA  1 
ATOM   4177 C  C   . LYS D 2 120 ? 73.173 75.305 49.271 1.00 106.07 ? 120 LYS D C   1 
ATOM   4178 O  O   . LYS D 2 120 ? 72.296 76.053 48.830 1.00 100.30 ? 120 LYS D O   1 
ATOM   4179 C  CB  . LYS D 2 120 ? 73.700 76.367 51.494 1.00 132.86 ? 120 LYS D CB  1 
ATOM   4180 C  CG  . LYS D 2 120 ? 73.381 76.353 52.984 1.00 149.48 ? 120 LYS D CG  1 
ATOM   4181 C  CD  . LYS D 2 120 ? 73.677 77.684 53.666 1.00 164.65 ? 120 LYS D CD  1 
ATOM   4182 C  CE  . LYS D 2 120 ? 72.708 78.799 53.272 1.00 174.56 ? 120 LYS D CE  1 
ATOM   4183 N  NZ  . LYS D 2 120 ? 71.282 78.508 53.601 1.00 177.41 ? 120 LYS D NZ  1 
ATOM   4184 N  N   . GLU D 2 121 ? 74.040 74.668 48.484 1.00 106.75 ? 121 GLU D N   1 
ATOM   4185 C  CA  . GLU D 2 121 ? 73.935 74.701 47.018 1.00 109.28 ? 121 GLU D CA  1 
ATOM   4186 C  C   . GLU D 2 121 ? 72.688 73.950 46.499 1.00 94.58  ? 121 GLU D C   1 
ATOM   4187 O  O   . GLU D 2 121 ? 72.166 74.264 45.422 1.00 89.85  ? 121 GLU D O   1 
ATOM   4188 C  CB  . GLU D 2 121 ? 75.208 74.121 46.397 1.00 127.04 ? 121 GLU D CB  1 
ATOM   4189 C  CG  . GLU D 2 121 ? 75.398 74.432 44.918 1.00 148.13 ? 121 GLU D CG  1 
ATOM   4190 C  CD  . GLU D 2 121 ? 76.702 73.885 44.351 1.00 164.58 ? 121 GLU D CD  1 
ATOM   4191 O  OE1 . GLU D 2 121 ? 77.482 73.243 45.093 1.00 173.27 ? 121 GLU D OE1 1 
ATOM   4192 O  OE2 . GLU D 2 121 ? 76.948 74.098 43.144 1.00 173.29 ? 121 GLU D OE2 1 
ATOM   4193 N  N   . PHE D 2 122 ? 72.230 72.967 47.279 1.00 78.26  ? 122 PHE D N   1 
ATOM   4194 C  CA  . PHE D 2 122 ? 71.009 72.202 47.008 1.00 62.68  ? 122 PHE D CA  1 
ATOM   4195 C  C   . PHE D 2 122 ? 69.771 72.993 47.479 1.00 60.19  ? 122 PHE D C   1 
ATOM   4196 O  O   . PHE D 2 122 ? 69.276 72.805 48.595 1.00 56.25  ? 122 PHE D O   1 
ATOM   4197 C  CB  . PHE D 2 122 ? 71.123 70.837 47.711 1.00 53.72  ? 122 PHE D CB  1 
ATOM   4198 C  CG  . PHE D 2 122 ? 70.203 69.800 47.172 1.00 47.52  ? 122 PHE D CG  1 
ATOM   4199 C  CD1 . PHE D 2 122 ? 70.479 69.181 45.965 1.00 44.99  ? 122 PHE D CD1 1 
ATOM   4200 C  CD2 . PHE D 2 122 ? 69.060 69.441 47.867 1.00 44.42  ? 122 PHE D CD2 1 
ATOM   4201 C  CE1 . PHE D 2 122 ? 69.624 68.223 45.455 1.00 43.74  ? 122 PHE D CE1 1 
ATOM   4202 C  CE2 . PHE D 2 122 ? 68.197 68.491 47.365 1.00 41.71  ? 122 PHE D CE2 1 
ATOM   4203 C  CZ  . PHE D 2 122 ? 68.479 67.880 46.157 1.00 43.02  ? 122 PHE D CZ  1 
ATOM   4204 N  N   . THR D 2 123 ? 69.299 73.897 46.616 1.00 60.64  ? 123 THR D N   1 
ATOM   4205 C  CA  . THR D 2 123 ? 68.170 74.797 46.923 1.00 60.56  ? 123 THR D CA  1 
ATOM   4206 C  C   . THR D 2 123 ? 66.841 74.135 46.593 1.00 57.11  ? 123 THR D C   1 
ATOM   4207 O  O   . THR D 2 123 ? 66.833 73.115 45.908 1.00 62.54  ? 123 THR D O   1 
ATOM   4208 C  CB  . THR D 2 123 ? 68.246 76.097 46.100 1.00 66.07  ? 123 THR D CB  1 
ATOM   4209 O  OG1 . THR D 2 123 ? 68.152 75.802 44.699 1.00 64.14  ? 123 THR D OG1 1 
ATOM   4210 C  CG2 . THR D 2 123 ? 69.550 76.814 46.367 1.00 73.05  ? 123 THR D CG2 1 
ATOM   4211 N  N   . PRO D 2 124 ? 65.714 74.703 47.073 1.00 52.36  ? 124 PRO D N   1 
ATOM   4212 C  CA  . PRO D 2 124 ? 64.411 74.138 46.723 1.00 51.85  ? 124 PRO D CA  1 
ATOM   4213 C  C   . PRO D 2 124 ? 64.123 73.940 45.229 1.00 54.47  ? 124 PRO D C   1 
ATOM   4214 O  O   . PRO D 2 124 ? 63.623 72.872 44.860 1.00 58.41  ? 124 PRO D O   1 
ATOM   4215 C  CB  . PRO D 2 124 ? 63.422 75.088 47.398 1.00 48.56  ? 124 PRO D CB  1 
ATOM   4216 C  CG  . PRO D 2 124 ? 64.143 75.479 48.631 1.00 50.09  ? 124 PRO D CG  1 
ATOM   4217 C  CD  . PRO D 2 124 ? 65.600 75.582 48.247 1.00 52.51  ? 124 PRO D CD  1 
ATOM   4218 N  N   . PRO D 2 125 ? 64.459 74.923 44.372 1.00 55.97  ? 125 PRO D N   1 
ATOM   4219 C  CA  . PRO D 2 125 ? 64.270 74.721 42.911 1.00 55.61  ? 125 PRO D CA  1 
ATOM   4220 C  C   . PRO D 2 125 ? 65.014 73.521 42.300 1.00 48.30  ? 125 PRO D C   1 
ATOM   4221 O  O   . PRO D 2 125 ? 64.471 72.815 41.440 1.00 47.20  ? 125 PRO D O   1 
ATOM   4222 C  CB  . PRO D 2 125 ? 64.812 76.020 42.313 1.00 60.22  ? 125 PRO D CB  1 
ATOM   4223 C  CG  . PRO D 2 125 ? 64.640 77.028 43.401 1.00 60.74  ? 125 PRO D CG  1 
ATOM   4224 C  CD  . PRO D 2 125 ? 64.883 76.302 44.682 1.00 55.74  ? 125 PRO D CD  1 
ATOM   4225 N  N   . VAL D 2 126 ? 66.249 73.329 42.748 1.00 41.77  ? 126 VAL D N   1 
ATOM   4226 C  CA  . VAL D 2 126 ? 67.061 72.192 42.356 1.00 38.54  ? 126 VAL D CA  1 
ATOM   4227 C  C   . VAL D 2 126 ? 66.401 70.921 42.866 1.00 36.16  ? 126 VAL D C   1 
ATOM   4228 O  O   . VAL D 2 126 ? 66.233 69.973 42.105 1.00 37.88  ? 126 VAL D O   1 
ATOM   4229 C  CB  . VAL D 2 126 ? 68.493 72.297 42.930 1.00 39.33  ? 126 VAL D CB  1 
ATOM   4230 C  CG1 . VAL D 2 126 ? 69.283 71.008 42.722 1.00 39.23  ? 126 VAL D CG1 1 
ATOM   4231 C  CG2 . VAL D 2 126 ? 69.225 73.473 42.306 1.00 40.55  ? 126 VAL D CG2 1 
ATOM   4232 N  N   . GLN D 2 127 ? 66.029 70.903 44.145 1.00 32.25  ? 127 GLN D N   1 
ATOM   4233 C  CA  . GLN D 2 127 ? 65.401 69.722 44.726 1.00 30.23  ? 127 GLN D CA  1 
ATOM   4234 C  C   . GLN D 2 127 ? 64.198 69.308 43.908 1.00 28.07  ? 127 GLN D C   1 
ATOM   4235 O  O   . GLN D 2 127 ? 64.090 68.151 43.516 1.00 27.18  ? 127 GLN D O   1 
ATOM   4236 C  CB  . GLN D 2 127 ? 64.965 69.935 46.174 1.00 29.97  ? 127 GLN D CB  1 
ATOM   4237 C  CG  . GLN D 2 127 ? 64.598 68.614 46.831 1.00 31.20  ? 127 GLN D CG  1 
ATOM   4238 C  CD  . GLN D 2 127 ? 63.741 68.755 48.055 1.00 32.70  ? 127 GLN D CD  1 
ATOM   4239 O  OE1 . GLN D 2 127 ? 63.693 69.816 48.666 1.00 33.94  ? 127 GLN D OE1 1 
ATOM   4240 N  NE2 . GLN D 2 127 ? 63.051 67.668 48.427 1.00 32.59  ? 127 GLN D NE2 1 
ATOM   4241 N  N   . ALA D 2 128 ? 63.312 70.263 43.653 1.00 28.06  ? 128 ALA D N   1 
ATOM   4242 C  CA  . ALA D 2 128 ? 62.105 70.019 42.867 1.00 29.38  ? 128 ALA D CA  1 
ATOM   4243 C  C   . ALA D 2 128 ? 62.401 69.356 41.524 1.00 31.57  ? 128 ALA D C   1 
ATOM   4244 O  O   . ALA D 2 128 ? 61.652 68.473 41.093 1.00 34.98  ? 128 ALA D O   1 
ATOM   4245 C  CB  . ALA D 2 128 ? 61.344 71.312 42.646 1.00 29.66  ? 128 ALA D CB  1 
ATOM   4246 N  N   . ALA D 2 129 ? 63.485 69.777 40.872 1.00 30.90  ? 129 ALA D N   1 
ATOM   4247 C  CA  . ALA D 2 129 ? 63.935 69.149 39.628 1.00 29.45  ? 129 ALA D CA  1 
ATOM   4248 C  C   . ALA D 2 129 ? 64.311 67.678 39.822 1.00 27.90  ? 129 ALA D C   1 
ATOM   4249 O  O   . ALA D 2 129 ? 63.689 66.809 39.225 1.00 26.59  ? 129 ALA D O   1 
ATOM   4250 C  CB  . ALA D 2 129 ? 65.106 69.921 39.058 1.00 30.78  ? 129 ALA D CB  1 
ATOM   4251 N  N   . TYR D 2 130 ? 65.302 67.415 40.676 1.00 27.78  ? 130 TYR D N   1 
ATOM   4252 C  CA  . TYR D 2 130 ? 65.731 66.048 40.985 1.00 28.62  ? 130 TYR D CA  1 
ATOM   4253 C  C   . TYR D 2 130 ? 64.629 65.133 41.501 1.00 28.71  ? 130 TYR D C   1 
ATOM   4254 O  O   . TYR D 2 130 ? 64.692 63.928 41.270 1.00 30.14  ? 130 TYR D O   1 
ATOM   4255 C  CB  . TYR D 2 130 ? 66.853 66.028 42.012 1.00 30.39  ? 130 TYR D CB  1 
ATOM   4256 C  CG  . TYR D 2 130 ? 68.213 66.230 41.421 1.00 33.85  ? 130 TYR D CG  1 
ATOM   4257 C  CD1 . TYR D 2 130 ? 68.930 65.165 40.886 1.00 36.14  ? 130 TYR D CD1 1 
ATOM   4258 C  CD2 . TYR D 2 130 ? 68.797 67.486 41.398 1.00 37.62  ? 130 TYR D CD2 1 
ATOM   4259 C  CE1 . TYR D 2 130 ? 70.196 65.350 40.346 1.00 36.61  ? 130 TYR D CE1 1 
ATOM   4260 C  CE2 . TYR D 2 130 ? 70.061 67.687 40.861 1.00 38.12  ? 130 TYR D CE2 1 
ATOM   4261 C  CZ  . TYR D 2 130 ? 70.754 66.617 40.340 1.00 38.10  ? 130 TYR D CZ  1 
ATOM   4262 O  OH  . TYR D 2 130 ? 72.001 66.833 39.815 1.00 41.50  ? 130 TYR D OH  1 
ATOM   4263 N  N   . GLN D 2 131 ? 63.643 65.667 42.213 1.00 28.59  ? 131 GLN D N   1 
ATOM   4264 C  CA  . GLN D 2 131 ? 62.517 64.835 42.636 1.00 29.59  ? 131 GLN D CA  1 
ATOM   4265 C  C   . GLN D 2 131 ? 61.770 64.294 41.439 1.00 30.67  ? 131 GLN D C   1 
ATOM   4266 O  O   . GLN D 2 131 ? 61.322 63.152 41.485 1.00 31.77  ? 131 GLN D O   1 
ATOM   4267 C  CB  . GLN D 2 131 ? 61.536 65.580 43.548 1.00 30.29  ? 131 GLN D CB  1 
ATOM   4268 C  CG  . GLN D 2 131 ? 62.020 65.767 44.979 1.00 30.14  ? 131 GLN D CG  1 
ATOM   4269 C  CD  . GLN D 2 131 ? 62.151 64.463 45.734 1.00 30.77  ? 131 GLN D CD  1 
ATOM   4270 O  OE1 . GLN D 2 131 ? 61.467 63.477 45.433 1.00 30.84  ? 131 GLN D OE1 1 
ATOM   4271 N  NE2 . GLN D 2 131 ? 63.034 64.450 46.727 1.00 30.63  ? 131 GLN D NE2 1 
ATOM   4272 N  N   . LYS D 2 132 ? 61.633 65.102 40.382 1.00 32.65  ? 132 LYS D N   1 
ATOM   4273 C  CA  . LYS D 2 132 ? 60.944 64.667 39.154 1.00 35.13  ? 132 LYS D CA  1 
ATOM   4274 C  C   . LYS D 2 132 ? 61.734 63.622 38.375 1.00 29.46  ? 132 LYS D C   1 
ATOM   4275 O  O   . LYS D 2 132 ? 61.148 62.716 37.788 1.00 28.75  ? 132 LYS D O   1 
ATOM   4276 C  CB  . LYS D 2 132 ? 60.608 65.850 38.249 1.00 44.47  ? 132 LYS D CB  1 
ATOM   4277 C  CG  . LYS D 2 132 ? 59.575 66.795 38.852 1.00 56.97  ? 132 LYS D CG  1 
ATOM   4278 C  CD  . LYS D 2 132 ? 59.389 68.077 38.040 1.00 67.87  ? 132 LYS D CD  1 
ATOM   4279 C  CE  . LYS D 2 132 ? 58.794 67.833 36.650 1.00 77.76  ? 132 LYS D CE  1 
ATOM   4280 N  NZ  . LYS D 2 132 ? 57.450 67.176 36.651 1.00 82.96  ? 132 LYS D NZ  1 
ATOM   4281 N  N   . VAL D 2 133 ? 63.055 63.749 38.377 1.00 25.21  ? 133 VAL D N   1 
ATOM   4282 C  CA  . VAL D 2 133 ? 63.912 62.747 37.770 1.00 22.96  ? 133 VAL D CA  1 
ATOM   4283 C  C   . VAL D 2 133 ? 63.729 61.423 38.498 1.00 21.45  ? 133 VAL D C   1 
ATOM   4284 O  O   . VAL D 2 133 ? 63.196 60.490 37.913 1.00 21.53  ? 133 VAL D O   1 
ATOM   4285 C  CB  . VAL D 2 133 ? 65.397 63.186 37.728 1.00 22.38  ? 133 VAL D CB  1 
ATOM   4286 C  CG1 . VAL D 2 133 ? 66.317 62.021 37.383 1.00 21.95  ? 133 VAL D CG1 1 
ATOM   4287 C  CG2 . VAL D 2 133 ? 65.577 64.317 36.722 1.00 22.00  ? 133 VAL D CG2 1 
ATOM   4288 N  N   . VAL D 2 134 ? 64.121 61.339 39.767 1.00 21.05  ? 134 VAL D N   1 
ATOM   4289 C  CA  . VAL D 2 134 ? 64.052 60.043 40.476 1.00 21.85  ? 134 VAL D CA  1 
ATOM   4290 C  C   . VAL D 2 134 ? 62.646 59.440 40.592 1.00 22.16  ? 134 VAL D C   1 
ATOM   4291 O  O   . VAL D 2 134 ? 62.516 58.248 40.890 1.00 22.37  ? 134 VAL D O   1 
ATOM   4292 C  CB  . VAL D 2 134 ? 64.710 60.035 41.881 1.00 21.47  ? 134 VAL D CB  1 
ATOM   4293 C  CG1 . VAL D 2 134 ? 66.198 60.352 41.788 1.00 21.40  ? 134 VAL D CG1 1 
ATOM   4294 C  CG2 . VAL D 2 134 ? 63.980 60.967 42.844 1.00 21.58  ? 134 VAL D CG2 1 
ATOM   4295 N  N   . ALA D 2 135 ? 61.608 60.245 40.379 1.00 23.01  ? 135 ALA D N   1 
ATOM   4296 C  CA  . ALA D 2 135 ? 60.259 59.701 40.211 1.00 24.50  ? 135 ALA D CA  1 
ATOM   4297 C  C   . ALA D 2 135 ? 60.210 58.930 38.913 1.00 23.91  ? 135 ALA D C   1 
ATOM   4298 O  O   . ALA D 2 135 ? 59.902 57.742 38.911 1.00 24.04  ? 135 ALA D O   1 
ATOM   4299 C  CB  . ALA D 2 135 ? 59.198 60.800 40.211 1.00 25.32  ? 135 ALA D CB  1 
ATOM   4300 N  N   . GLY D 2 136 ? 60.528 59.612 37.817 1.00 23.85  ? 136 GLY D N   1 
ATOM   4301 C  CA  . GLY D 2 136 ? 60.521 58.997 36.489 1.00 23.97  ? 136 GLY D CA  1 
ATOM   4302 C  C   . GLY D 2 136 ? 61.246 57.662 36.460 1.00 22.78  ? 136 GLY D C   1 
ATOM   4303 O  O   . GLY D 2 136 ? 60.672 56.644 36.069 1.00 22.27  ? 136 GLY D O   1 
ATOM   4304 N  N   . VAL D 2 137 ? 62.488 57.687 36.935 1.00 21.28  ? 137 VAL D N   1 
ATOM   4305 C  CA  . VAL D 2 137 ? 63.382 56.543 36.902 1.00 20.42  ? 137 VAL D CA  1 
ATOM   4306 C  C   . VAL D 2 137 ? 62.819 55.394 37.681 1.00 22.05  ? 137 VAL D C   1 
ATOM   4307 O  O   . VAL D 2 137 ? 62.931 54.271 37.246 1.00 22.88  ? 137 VAL D O   1 
ATOM   4308 C  CB  . VAL D 2 137 ? 64.749 56.892 37.490 1.00 19.51  ? 137 VAL D CB  1 
ATOM   4309 C  CG1 . VAL D 2 137 ? 65.599 55.640 37.722 1.00 19.17  ? 137 VAL D CG1 1 
ATOM   4310 C  CG2 . VAL D 2 137 ? 65.456 57.894 36.583 1.00 19.26  ? 137 VAL D CG2 1 
ATOM   4311 N  N   . ALA D 2 138 ? 62.230 55.672 38.836 1.00 25.83  ? 138 ALA D N   1 
ATOM   4312 C  CA  . ALA D 2 138 ? 61.566 54.637 39.631 1.00 28.81  ? 138 ALA D CA  1 
ATOM   4313 C  C   . ALA D 2 138 ? 60.275 54.154 38.970 1.00 32.23  ? 138 ALA D C   1 
ATOM   4314 O  O   . ALA D 2 138 ? 60.043 52.953 38.853 1.00 31.12  ? 138 ALA D O   1 
ATOM   4315 C  CB  . ALA D 2 138 ? 61.272 55.163 41.017 1.00 29.23  ? 138 ALA D CB  1 
ATOM   4316 N  N   . ASN D 2 139 ? 59.450 55.102 38.529 1.00 41.09  ? 139 ASN D N   1 
ATOM   4317 C  CA  . ASN D 2 139 ? 58.175 54.798 37.860 1.00 48.45  ? 139 ASN D CA  1 
ATOM   4318 C  C   . ASN D 2 139 ? 58.356 54.074 36.547 1.00 46.49  ? 139 ASN D C   1 
ATOM   4319 O  O   . ASN D 2 139 ? 57.435 53.398 36.099 1.00 51.25  ? 139 ASN D O   1 
ATOM   4320 C  CB  . ASN D 2 139 ? 57.349 56.071 37.610 1.00 59.96  ? 139 ASN D CB  1 
ATOM   4321 C  CG  . ASN D 2 139 ? 56.706 56.623 38.886 1.00 75.00  ? 139 ASN D CG  1 
ATOM   4322 O  OD1 . ASN D 2 139 ? 56.030 55.894 39.623 1.00 84.54  ? 139 ASN D OD1 1 
ATOM   4323 N  ND2 . ASN D 2 139 ? 56.903 57.921 39.144 1.00 79.43  ? 139 ASN D ND2 1 
ATOM   4324 N  N   . ALA D 2 140 ? 59.527 54.233 35.930 1.00 43.64  ? 140 ALA D N   1 
ATOM   4325 C  CA  . ALA D 2 140 ? 59.871 53.566 34.670 1.00 39.81  ? 140 ALA D CA  1 
ATOM   4326 C  C   . ALA D 2 140 ? 60.583 52.247 34.846 1.00 33.84  ? 140 ALA D C   1 
ATOM   4327 O  O   . ALA D 2 140 ? 60.476 51.390 34.002 1.00 32.85  ? 140 ALA D O   1 
ATOM   4328 C  CB  . ALA D 2 140 ? 60.736 54.479 33.832 1.00 41.99  ? 140 ALA D CB  1 
ATOM   4329 N  N   . LEU D 2 141 ? 61.329 52.091 35.926 1.00 33.90  ? 141 LEU D N   1 
ATOM   4330 C  CA  . LEU D 2 141 ? 62.069 50.860 36.179 1.00 34.79  ? 141 LEU D CA  1 
ATOM   4331 C  C   . LEU D 2 141 ? 61.180 49.785 36.743 1.00 38.16  ? 141 LEU D C   1 
ATOM   4332 O  O   . LEU D 2 141 ? 61.626 48.668 36.949 1.00 37.99  ? 141 LEU D O   1 
ATOM   4333 C  CB  . LEU D 2 141 ? 63.209 51.133 37.144 1.00 34.19  ? 141 LEU D CB  1 
ATOM   4334 C  CG  . LEU D 2 141 ? 64.323 50.110 37.340 1.00 33.95  ? 141 LEU D CG  1 
ATOM   4335 C  CD1 . LEU D 2 141 ? 65.665 50.827 37.305 1.00 35.05  ? 141 LEU D CD1 1 
ATOM   4336 C  CD2 . LEU D 2 141 ? 64.183 49.342 38.647 1.00 34.23  ? 141 LEU D CD2 1 
ATOM   4337 N  N   . ALA D 2 142 ? 59.927 50.115 37.011 1.00 46.70  ? 142 ALA D N   1 
ATOM   4338 C  CA  . ALA D 2 142 ? 58.970 49.126 37.417 1.00 57.40  ? 142 ALA D CA  1 
ATOM   4339 C  C   . ALA D 2 142 ? 57.680 49.356 36.671 1.00 71.23  ? 142 ALA D C   1 
ATOM   4340 O  O   . ALA D 2 142 ? 56.681 49.794 37.249 1.00 77.22  ? 142 ALA D O   1 
ATOM   4341 C  CB  . ALA D 2 142 ? 58.760 49.218 38.907 1.00 60.09  ? 142 ALA D CB  1 
ATOM   4342 N  N   . HIS D 2 143 ? 57.727 49.108 35.365 1.00 94.04  ? 143 HIS D N   1 
ATOM   4343 C  CA  . HIS D 2 143 ? 56.515 48.964 34.551 1.00 118.92 ? 143 HIS D CA  1 
ATOM   4344 C  C   . HIS D 2 143 ? 56.342 47.545 33.991 1.00 128.71 ? 143 HIS D C   1 
ATOM   4345 O  O   . HIS D 2 143 ? 55.316 47.261 33.369 1.00 138.97 ? 143 HIS D O   1 
ATOM   4346 C  CB  . HIS D 2 143 ? 56.463 50.007 33.418 1.00 132.24 ? 143 HIS D CB  1 
ATOM   4347 C  CG  . HIS D 2 143 ? 57.420 49.743 32.294 1.00 143.80 ? 143 HIS D CG  1 
ATOM   4348 N  ND1 . HIS D 2 143 ? 57.302 48.660 31.447 1.00 150.14 ? 143 HIS D ND1 1 
ATOM   4349 C  CD2 . HIS D 2 143 ? 58.501 50.436 31.866 1.00 148.51 ? 143 HIS D CD2 1 
ATOM   4350 C  CE1 . HIS D 2 143 ? 58.279 48.688 30.560 1.00 154.47 ? 143 HIS D CE1 1 
ATOM   4351 N  NE2 . HIS D 2 143 ? 59.020 49.757 30.791 1.00 152.76 ? 143 HIS D NE2 1 
ATOM   4352 N  N   . LYS D 2 144 ? 57.324 46.665 34.195 1.00 134.49 ? 144 LYS D N   1 
ATOM   4353 C  CA  . LYS D 2 144 ? 57.179 45.272 33.788 1.00 149.92 ? 144 LYS D CA  1 
ATOM   4354 C  C   . LYS D 2 144 ? 56.182 44.526 34.691 1.00 155.18 ? 144 LYS D C   1 
ATOM   4355 O  O   . LYS D 2 144 ? 55.615 43.508 34.286 1.00 162.07 ? 144 LYS D O   1 
ATOM   4356 C  CB  . LYS D 2 144 ? 58.543 44.571 33.762 1.00 163.54 ? 144 LYS D CB  1 
ATOM   4357 C  CG  . LYS D 2 144 ? 58.541 43.150 33.198 1.00 184.21 ? 144 LYS D CG  1 
ATOM   4358 C  CD  . LYS D 2 144 ? 57.933 43.053 31.800 1.00 206.84 ? 144 LYS D CD  1 
ATOM   4359 C  CE  . LYS D 2 144 ? 57.784 41.609 31.347 1.00 223.07 ? 144 LYS D CE  1 
ATOM   4360 N  NZ  . LYS D 2 144 ? 57.120 41.514 30.017 1.00 227.80 ? 144 LYS D NZ  1 
ATOM   4361 N  N   . TYR D 2 145 ? 55.961 45.048 35.897 1.00 165.53 ? 145 TYR D N   1 
ATOM   4362 C  CA  . TYR D 2 145 ? 54.955 44.515 36.818 1.00 186.34 ? 145 TYR D CA  1 
ATOM   4363 C  C   . TYR D 2 145 ? 53.541 44.794 36.302 1.00 211.51 ? 145 TYR D C   1 
ATOM   4364 O  O   . TYR D 2 145 ? 52.698 43.894 36.279 1.00 219.84 ? 145 TYR D O   1 
ATOM   4365 C  CB  . TYR D 2 145 ? 55.115 45.126 38.219 1.00 185.49 ? 145 TYR D CB  1 
ATOM   4366 C  CG  . TYR D 2 145 ? 56.440 44.830 38.893 1.00 180.21 ? 145 TYR D CG  1 
ATOM   4367 C  CD1 . TYR D 2 145 ? 56.595 43.709 39.714 1.00 180.70 ? 145 TYR D CD1 1 
ATOM   4368 C  CD2 . TYR D 2 145 ? 57.539 45.679 38.722 1.00 175.27 ? 145 TYR D CD2 1 
ATOM   4369 C  CE1 . TYR D 2 145 ? 57.808 43.440 40.337 1.00 181.98 ? 145 TYR D CE1 1 
ATOM   4370 C  CE2 . TYR D 2 145 ? 58.753 45.418 39.335 1.00 172.99 ? 145 TYR D CE2 1 
ATOM   4371 C  CZ  . TYR D 2 145 ? 58.884 44.302 40.141 1.00 179.39 ? 145 TYR D CZ  1 
ATOM   4372 O  OH  . TYR D 2 145 ? 60.093 44.056 40.740 1.00 178.10 ? 145 TYR D OH  1 
ATOM   4373 N  N   . HIS D 2 146 ? 53.302 46.042 35.890 1.00 241.75 ? 146 HIS D N   1 
ATOM   4374 C  CA  . HIS D 2 146 ? 51.990 46.495 35.400 1.00 268.73 ? 146 HIS D CA  1 
ATOM   4375 C  C   . HIS D 2 146 ? 52.112 47.142 34.013 1.00 298.84 ? 146 HIS D C   1 
ATOM   4376 O  O   . HIS D 2 146 ? 52.433 46.454 33.043 1.00 315.02 ? 146 HIS D O   1 
ATOM   4377 C  CB  . HIS D 2 146 ? 51.318 47.445 36.414 1.00 268.38 ? 146 HIS D CB  1 
ATOM   4378 C  CG  . HIS D 2 146 ? 52.166 48.612 36.825 1.00 263.80 ? 146 HIS D CG  1 
ATOM   4379 N  ND1 . HIS D 2 146 ? 52.162 49.811 36.145 1.00 266.71 ? 146 HIS D ND1 1 
ATOM   4380 C  CD2 . HIS D 2 146 ? 53.037 48.765 37.851 1.00 258.76 ? 146 HIS D CD2 1 
ATOM   4381 C  CE1 . HIS D 2 146 ? 52.998 50.650 36.730 1.00 266.06 ? 146 HIS D CE1 1 
ATOM   4382 N  NE2 . HIS D 2 146 ? 53.542 50.041 37.768 1.00 259.46 ? 146 HIS D NE2 1 
ATOM   4383 O  OXT . HIS D 2 146 ? 51.896 48.338 33.799 1.00 316.75 ? 146 HIS D OXT 1 
HETATM 4384 C  CHA . HEM E 3 .   ? 56.814 31.995 61.724 1.00 15.42  ? 201 HEM A CHA 1 
HETATM 4385 C  CHB . HEM E 3 .   ? 53.153 34.655 63.376 1.00 12.45  ? 201 HEM A CHB 1 
HETATM 4386 C  CHC . HEM E 3 .   ? 53.073 37.233 59.281 1.00 10.38  ? 201 HEM A CHC 1 
HETATM 4387 C  CHD . HEM E 3 .   ? 56.572 34.416 57.530 1.00 12.36  ? 201 HEM A CHD 1 
HETATM 4388 C  C1A . HEM E 3 .   ? 55.831 32.516 62.509 1.00 15.99  ? 201 HEM A C1A 1 
HETATM 4389 C  C2A . HEM E 3 .   ? 55.570 32.133 63.834 1.00 19.19  ? 201 HEM A C2A 1 
HETATM 4390 C  C3A . HEM E 3 .   ? 54.556 32.875 64.289 1.00 16.29  ? 201 HEM A C3A 1 
HETATM 4391 C  C4A . HEM E 3 .   ? 54.154 33.724 63.256 1.00 14.16  ? 201 HEM A C4A 1 
HETATM 4392 C  CMA . HEM E 3 .   ? 53.929 32.818 65.649 1.00 17.03  ? 201 HEM A CMA 1 
HETATM 4393 C  CAA . HEM E 3 .   ? 56.331 31.133 64.628 1.00 26.85  ? 201 HEM A CAA 1 
HETATM 4394 C  CBA . HEM E 3 .   ? 56.047 29.726 64.154 1.00 37.60  ? 201 HEM A CBA 1 
HETATM 4395 C  CGA . HEM E 3 .   ? 57.338 28.945 64.190 1.00 50.42  ? 201 HEM A CGA 1 
HETATM 4396 O  O1A . HEM E 3 .   ? 58.136 29.075 65.162 1.00 56.66  ? 201 HEM A O1A 1 
HETATM 4397 O  O2A . HEM E 3 .   ? 57.605 28.172 63.231 1.00 60.05  ? 201 HEM A O2A 1 
HETATM 4398 C  C1B . HEM E 3 .   ? 52.836 35.584 62.394 1.00 11.14  ? 201 HEM A C1B 1 
HETATM 4399 C  C2B . HEM E 3 .   ? 51.832 36.544 62.585 1.00 10.58  ? 201 HEM A C2B 1 
HETATM 4400 C  C3B . HEM E 3 .   ? 51.758 37.283 61.483 1.00 10.61  ? 201 HEM A C3B 1 
HETATM 4401 C  C4B . HEM E 3 .   ? 52.785 36.744 60.559 1.00 10.48  ? 201 HEM A C4B 1 
HETATM 4402 C  CMB . HEM E 3 .   ? 50.964 36.788 63.784 1.00 10.58  ? 201 HEM A CMB 1 
HETATM 4403 C  CAB . HEM E 3 .   ? 50.752 38.359 61.407 1.00 11.57  ? 201 HEM A CAB 1 
HETATM 4404 C  CBB . HEM E 3 .   ? 50.415 39.048 60.316 1.00 12.57  ? 201 HEM A CBB 1 
HETATM 4405 C  C1C . HEM E 3 .   ? 54.030 36.696 58.413 1.00 10.52  ? 201 HEM A C1C 1 
HETATM 4406 C  C2C . HEM E 3 .   ? 54.238 37.072 57.083 1.00 9.97   ? 201 HEM A C2C 1 
HETATM 4407 C  C3C . HEM E 3 .   ? 55.234 36.264 56.579 1.00 10.28  ? 201 HEM A C3C 1 
HETATM 4408 C  C4C . HEM E 3 .   ? 55.615 35.381 57.616 1.00 11.02  ? 201 HEM A C4C 1 
HETATM 4409 C  CMC . HEM E 3 .   ? 53.516 38.174 56.375 1.00 9.82   ? 201 HEM A CMC 1 
HETATM 4410 C  CAC . HEM E 3 .   ? 55.798 36.199 55.219 1.00 10.47  ? 201 HEM A CAC 1 
HETATM 4411 C  CBC . HEM E 3 .   ? 55.220 36.703 54.129 1.00 10.50  ? 201 HEM A CBC 1 
HETATM 4412 C  C1D . HEM E 3 .   ? 56.901 33.561 58.581 1.00 13.92  ? 201 HEM A C1D 1 
HETATM 4413 C  C2D . HEM E 3 .   ? 57.969 32.558 58.433 1.00 15.77  ? 201 HEM A C2D 1 
HETATM 4414 C  C3D . HEM E 3 .   ? 58.027 31.906 59.582 1.00 18.70  ? 201 HEM A C3D 1 
HETATM 4415 C  C4D . HEM E 3 .   ? 57.001 32.482 60.445 1.00 15.60  ? 201 HEM A C4D 1 
HETATM 4416 C  CMD . HEM E 3 .   ? 58.864 32.257 57.257 1.00 15.67  ? 201 HEM A CMD 1 
HETATM 4417 C  CAD . HEM E 3 .   ? 59.000 30.805 59.880 1.00 25.92  ? 201 HEM A CAD 1 
HETATM 4418 C  CBD . HEM E 3 .   ? 58.454 29.473 59.373 1.00 35.02  ? 201 HEM A CBD 1 
HETATM 4419 C  CGD . HEM E 3 .   ? 59.517 28.387 59.506 1.00 45.40  ? 201 HEM A CGD 1 
HETATM 4420 O  O1D . HEM E 3 .   ? 59.669 27.559 58.569 1.00 49.42  ? 201 HEM A O1D 1 
HETATM 4421 O  O2D . HEM E 3 .   ? 60.244 28.298 60.541 1.00 49.65  ? 201 HEM A O2D 1 
HETATM 4422 N  NA  . HEM E 3 .   ? 54.944 33.504 62.162 1.00 14.01  ? 201 HEM A NA  1 
HETATM 4423 N  NB  . HEM E 3 .   ? 53.372 35.730 61.198 1.00 11.09  ? 201 HEM A NB  1 
HETATM 4424 N  NC  . HEM E 3 .   ? 54.852 35.642 58.699 1.00 11.28  ? 201 HEM A NC  1 
HETATM 4425 N  ND  . HEM E 3 .   ? 56.341 33.478 59.802 1.00 13.74  ? 201 HEM A ND  1 
HETATM 4426 FE FE  . HEM E 3 .   ? 54.929 34.546 60.472 1.00 11.95  ? 201 HEM A FE  1 
HETATM 4427 C  CHA . HEM F 3 .   ? 33.792 60.050 40.271 1.00 34.33  ? 201 HEM B CHA 1 
HETATM 4428 C  CHB . HEM F 3 .   ? 34.807 55.475 39.068 1.00 32.71  ? 201 HEM B CHB 1 
HETATM 4429 C  CHC . HEM F 3 .   ? 38.064 55.275 42.669 1.00 26.81  ? 201 HEM B CHC 1 
HETATM 4430 C  CHD . HEM F 3 .   ? 36.450 59.524 44.279 1.00 28.92  ? 201 HEM B CHD 1 
HETATM 4431 C  C1A . HEM F 3 .   ? 33.836 58.853 39.622 1.00 37.68  ? 201 HEM B C1A 1 
HETATM 4432 C  C2A . HEM F 3 .   ? 33.092 58.533 38.469 1.00 45.74  ? 201 HEM B C2A 1 
HETATM 4433 C  C3A . HEM F 3 .   ? 33.375 57.255 38.126 1.00 39.83  ? 201 HEM B C3A 1 
HETATM 4434 C  C4A . HEM F 3 .   ? 34.274 56.755 39.083 1.00 35.99  ? 201 HEM B C4A 1 
HETATM 4435 C  CMA . HEM F 3 .   ? 32.808 56.499 36.953 1.00 41.11  ? 201 HEM B CMA 1 
HETATM 4436 C  CAA . HEM F 3 .   ? 32.184 59.471 37.716 1.00 60.89  ? 201 HEM B CAA 1 
HETATM 4437 C  CBA . HEM F 3 .   ? 30.931 59.805 38.527 1.00 76.93  ? 201 HEM B CBA 1 
HETATM 4438 C  CGA . HEM F 3 .   ? 30.665 61.286 38.389 1.00 95.02  ? 201 HEM B CGA 1 
HETATM 4439 O  O1A . HEM F 3 .   ? 30.304 61.745 37.277 1.00 106.01 ? 201 HEM B O1A 1 
HETATM 4440 O  O2A . HEM F 3 .   ? 30.817 62.050 39.374 1.00 98.98  ? 201 HEM B O2A 1 
HETATM 4441 C  C1B . HEM F 3 .   ? 35.803 55.027 39.948 1.00 29.90  ? 201 HEM B C1B 1 
HETATM 4442 C  C2B . HEM F 3 .   ? 36.434 53.754 39.834 1.00 28.70  ? 201 HEM B C2B 1 
HETATM 4443 C  C3B . HEM F 3 .   ? 37.362 53.642 40.813 1.00 28.17  ? 201 HEM B C3B 1 
HETATM 4444 C  C4B . HEM F 3 .   ? 37.297 54.945 41.552 1.00 27.93  ? 201 HEM B C4B 1 
HETATM 4445 C  CMB . HEM F 3 .   ? 36.183 52.664 38.826 1.00 29.31  ? 201 HEM B CMB 1 
HETATM 4446 C  CAB . HEM F 3 .   ? 38.194 52.414 40.932 1.00 29.32  ? 201 HEM B CAB 1 
HETATM 4447 C  CBB . HEM F 3 .   ? 39.219 52.199 41.756 1.00 30.96  ? 201 HEM B CBB 1 
HETATM 4448 C  C1C . HEM F 3 .   ? 37.902 56.416 43.457 1.00 26.82  ? 201 HEM B C1C 1 
HETATM 4449 C  C2C . HEM F 3 .   ? 38.508 56.637 44.707 1.00 25.67  ? 201 HEM B C2C 1 
HETATM 4450 C  C3C . HEM F 3 .   ? 38.058 57.859 45.183 1.00 26.10  ? 201 HEM B C3C 1 
HETATM 4451 C  C4C . HEM F 3 .   ? 37.148 58.357 44.200 1.00 27.24  ? 201 HEM B C4C 1 
HETATM 4452 C  CMC . HEM F 3 .   ? 39.490 55.720 45.376 1.00 25.69  ? 201 HEM B CMC 1 
HETATM 4453 C  CAC . HEM F 3 .   ? 38.389 58.558 46.451 1.00 26.05  ? 201 HEM B CAC 1 
HETATM 4454 C  CBC . HEM F 3 .   ? 39.162 58.107 47.437 1.00 25.93  ? 201 HEM B CBC 1 
HETATM 4455 C  C1D . HEM F 3 .   ? 35.603 59.972 43.273 1.00 30.83  ? 201 HEM B C1D 1 
HETATM 4456 C  C2D . HEM F 3 .   ? 34.999 61.309 43.365 1.00 32.84  ? 201 HEM B C2D 1 
HETATM 4457 C  C3D . HEM F 3 .   ? 34.273 61.465 42.257 1.00 37.07  ? 201 HEM B C3D 1 
HETATM 4458 C  C4D . HEM F 3 .   ? 34.437 60.228 41.478 1.00 33.57  ? 201 HEM B C4D 1 
HETATM 4459 C  CMD . HEM F 3 .   ? 35.149 62.325 44.474 1.00 32.43  ? 201 HEM B CMD 1 
HETATM 4460 C  CAD . HEM F 3 .   ? 33.464 62.697 41.934 1.00 45.47  ? 201 HEM B CAD 1 
HETATM 4461 C  CBD . HEM F 3 .   ? 32.301 62.800 42.926 1.00 54.93  ? 201 HEM B CBD 1 
HETATM 4462 C  CGD . HEM F 3 .   ? 31.218 63.720 42.419 1.00 68.56  ? 201 HEM B CGD 1 
HETATM 4463 O  O1D . HEM F 3 .   ? 30.057 63.608 42.894 1.00 74.13  ? 201 HEM B O1D 1 
HETATM 4464 O  O2D . HEM F 3 .   ? 31.468 64.589 41.542 1.00 78.50  ? 201 HEM B O2D 1 
HETATM 4465 N  NA  . HEM F 3 .   ? 34.536 57.745 40.005 1.00 34.75  ? 201 HEM B NA  1 
HETATM 4466 N  NB  . HEM F 3 .   ? 36.347 55.700 40.964 1.00 29.04  ? 201 HEM B NB  1 
HETATM 4467 N  NC  . HEM F 3 .   ? 37.052 57.453 43.193 1.00 27.59  ? 201 HEM B NC  1 
HETATM 4468 N  ND  . HEM F 3 .   ? 35.251 59.363 42.125 1.00 31.25  ? 201 HEM B ND  1 
HETATM 4469 FE FE  . HEM F 3 .   ? 35.773 57.633 41.561 1.00 28.76  ? 201 HEM B FE  1 
HETATM 4470 C  CHA . HEM G 3 .   ? 48.184 73.007 61.724 1.00 15.38  ? 201 HEM C CHA 1 
HETATM 4471 C  CHB . HEM G 3 .   ? 51.845 70.346 63.375 1.00 12.42  ? 201 HEM C CHB 1 
HETATM 4472 C  CHC . HEM G 3 .   ? 51.924 67.767 59.281 1.00 10.35  ? 201 HEM C CHC 1 
HETATM 4473 C  CHD . HEM G 3 .   ? 48.425 70.584 57.531 1.00 12.33  ? 201 HEM C CHD 1 
HETATM 4474 C  C1A . HEM G 3 .   ? 49.167 72.486 62.509 1.00 15.95  ? 201 HEM C C1A 1 
HETATM 4475 C  C2A . HEM G 3 .   ? 49.427 72.868 63.834 1.00 19.16  ? 201 HEM C C2A 1 
HETATM 4476 C  C3A . HEM G 3 .   ? 50.442 72.126 64.289 1.00 16.26  ? 201 HEM C C3A 1 
HETATM 4477 C  C4A . HEM G 3 .   ? 50.844 71.278 63.256 1.00 14.14  ? 201 HEM C C4A 1 
HETATM 4478 C  CMA . HEM G 3 .   ? 51.069 72.182 65.649 1.00 17.01  ? 201 HEM C CMA 1 
HETATM 4479 C  CAA . HEM G 3 .   ? 48.667 73.868 64.630 1.00 26.81  ? 201 HEM C CAA 1 
HETATM 4480 C  CBA . HEM G 3 .   ? 48.954 75.275 64.160 1.00 37.56  ? 201 HEM C CBA 1 
HETATM 4481 C  CGA . HEM G 3 .   ? 47.661 76.053 64.184 1.00 50.37  ? 201 HEM C CGA 1 
HETATM 4482 O  O1A . HEM G 3 .   ? 47.389 76.808 63.212 1.00 59.84  ? 201 HEM C O1A 1 
HETATM 4483 O  O2A . HEM G 3 .   ? 46.865 75.937 65.159 1.00 56.68  ? 201 HEM C O2A 1 
HETATM 4484 C  C1B . HEM G 3 .   ? 52.161 69.417 62.393 1.00 11.11  ? 201 HEM C C1B 1 
HETATM 4485 C  C2B . HEM G 3 .   ? 53.165 68.457 62.584 1.00 10.56  ? 201 HEM C C2B 1 
HETATM 4486 C  C3B . HEM G 3 .   ? 53.239 67.718 61.483 1.00 10.58  ? 201 HEM C C3B 1 
HETATM 4487 C  C4B . HEM G 3 .   ? 52.212 68.257 60.559 1.00 10.45  ? 201 HEM C C4B 1 
HETATM 4488 C  CMB . HEM G 3 .   ? 54.033 68.213 63.784 1.00 10.56  ? 201 HEM C CMB 1 
HETATM 4489 C  CAB . HEM G 3 .   ? 54.246 66.642 61.407 1.00 11.55  ? 201 HEM C CAB 1 
HETATM 4490 C  CBB . HEM G 3 .   ? 54.583 65.953 60.316 1.00 12.55  ? 201 HEM C CBB 1 
HETATM 4491 C  C1C . HEM G 3 .   ? 50.968 68.304 58.414 1.00 10.49  ? 201 HEM C C1C 1 
HETATM 4492 C  C2C . HEM G 3 .   ? 50.759 67.927 57.084 1.00 9.95   ? 201 HEM C C2C 1 
HETATM 4493 C  C3C . HEM G 3 .   ? 49.763 68.735 56.579 1.00 10.25  ? 201 HEM C C3C 1 
HETATM 4494 C  C4C . HEM G 3 .   ? 49.382 69.619 57.616 1.00 10.99  ? 201 HEM C C4C 1 
HETATM 4495 C  CMC . HEM G 3 .   ? 51.481 66.824 56.377 1.00 9.79   ? 201 HEM C CMC 1 
HETATM 4496 C  CAC . HEM G 3 .   ? 49.199 68.799 55.220 1.00 10.44  ? 201 HEM C CAC 1 
HETATM 4497 C  CBC . HEM G 3 .   ? 49.776 68.294 54.130 1.00 10.47  ? 201 HEM C CBC 1 
HETATM 4498 C  C1D . HEM G 3 .   ? 48.097 71.439 58.582 1.00 13.88  ? 201 HEM C C1D 1 
HETATM 4499 C  C2D . HEM G 3 .   ? 47.029 72.443 58.433 1.00 15.72  ? 201 HEM C C2D 1 
HETATM 4500 C  C3D . HEM G 3 .   ? 46.971 73.095 59.582 1.00 18.65  ? 201 HEM C C3D 1 
HETATM 4501 C  C4D . HEM G 3 .   ? 47.998 72.519 60.445 1.00 15.56  ? 201 HEM C C4D 1 
HETATM 4502 C  CMD . HEM G 3 .   ? 46.133 72.744 57.257 1.00 15.62  ? 201 HEM C CMD 1 
HETATM 4503 C  CAD . HEM G 3 .   ? 45.998 74.197 59.880 1.00 25.84  ? 201 HEM C CAD 1 
HETATM 4504 C  CBD . HEM G 3 .   ? 46.547 75.529 59.377 1.00 34.89  ? 201 HEM C CBD 1 
HETATM 4505 C  CGD . HEM G 3 .   ? 45.483 76.615 59.507 1.00 45.19  ? 201 HEM C CGD 1 
HETATM 4506 O  O1D . HEM G 3 .   ? 45.337 77.445 58.570 1.00 49.19  ? 201 HEM C O1D 1 
HETATM 4507 O  O2D . HEM G 3 .   ? 44.751 76.703 60.537 1.00 49.40  ? 201 HEM C O2D 1 
HETATM 4508 N  NA  . HEM G 3 .   ? 50.053 71.498 62.161 1.00 13.98  ? 201 HEM C NA  1 
HETATM 4509 N  NB  . HEM G 3 .   ? 51.625 69.271 61.198 1.00 11.06  ? 201 HEM C NB  1 
HETATM 4510 N  NC  . HEM G 3 .   ? 50.145 69.359 58.699 1.00 11.25  ? 201 HEM C NC  1 
HETATM 4511 N  ND  . HEM G 3 .   ? 48.656 71.523 59.802 1.00 13.70  ? 201 HEM C ND  1 
HETATM 4512 FE FE  . HEM G 3 .   ? 50.069 70.455 60.472 1.00 11.92  ? 201 HEM C FE  1 
HETATM 4513 C  CHA . HEM H 3 .   ? 71.207 44.955 40.271 1.00 34.30  ? 201 HEM D CHA 1 
HETATM 4514 C  CHB . HEM H 3 .   ? 70.193 49.530 39.069 1.00 32.68  ? 201 HEM D CHB 1 
HETATM 4515 C  CHC . HEM H 3 .   ? 66.936 49.728 42.670 1.00 26.78  ? 201 HEM D CHC 1 
HETATM 4516 C  CHD . HEM H 3 .   ? 68.550 45.479 44.280 1.00 28.89  ? 201 HEM D CHD 1 
HETATM 4517 C  C1A . HEM H 3 .   ? 71.163 46.152 39.623 1.00 37.62  ? 201 HEM D C1A 1 
HETATM 4518 C  C2A . HEM H 3 .   ? 71.907 46.472 38.469 1.00 45.63  ? 201 HEM D C2A 1 
HETATM 4519 C  C3A . HEM H 3 .   ? 71.623 47.749 38.126 1.00 39.74  ? 201 HEM D C3A 1 
HETATM 4520 C  C4A . HEM H 3 .   ? 70.725 48.249 39.084 1.00 35.94  ? 201 HEM D C4A 1 
HETATM 4521 C  CMA . HEM H 3 .   ? 72.193 48.502 36.953 1.00 41.04  ? 201 HEM D CMA 1 
HETATM 4522 C  CAA . HEM H 3 .   ? 72.815 45.535 37.715 1.00 60.75  ? 201 HEM D CAA 1 
HETATM 4523 C  CBA . HEM H 3 .   ? 74.067 45.200 38.526 1.00 76.86  ? 201 HEM D CBA 1 
HETATM 4524 C  CGA . HEM H 3 .   ? 74.330 43.718 38.395 1.00 94.99  ? 201 HEM D CGA 1 
HETATM 4525 O  O1A . HEM H 3 .   ? 74.685 43.252 37.284 1.00 106.10 ? 201 HEM D O1A 1 
HETATM 4526 O  O2A . HEM H 3 .   ? 74.179 42.958 39.385 1.00 98.99  ? 201 HEM D O2A 1 
HETATM 4527 C  C1B . HEM H 3 .   ? 69.196 49.979 39.948 1.00 29.86  ? 201 HEM D C1B 1 
HETATM 4528 C  C2B . HEM H 3 .   ? 68.564 51.252 39.835 1.00 28.67  ? 201 HEM D C2B 1 
HETATM 4529 C  C3B . HEM H 3 .   ? 67.636 51.362 40.814 1.00 28.14  ? 201 HEM D C3B 1 
HETATM 4530 C  C4B . HEM H 3 .   ? 67.702 50.060 41.552 1.00 27.89  ? 201 HEM D C4B 1 
HETATM 4531 C  CMB . HEM H 3 .   ? 68.814 52.342 38.826 1.00 29.32  ? 201 HEM D CMB 1 
HETATM 4532 C  CAB . HEM H 3 .   ? 66.803 52.590 40.934 1.00 29.33  ? 201 HEM D CAB 1 
HETATM 4533 C  CBB . HEM H 3 .   ? 65.781 52.806 41.760 1.00 30.96  ? 201 HEM D CBB 1 
HETATM 4534 C  C1C . HEM H 3 .   ? 67.098 48.586 43.458 1.00 26.77  ? 201 HEM D C1C 1 
HETATM 4535 C  C2C . HEM H 3 .   ? 66.491 48.365 44.707 1.00 25.61  ? 201 HEM D C2C 1 
HETATM 4536 C  C3C . HEM H 3 .   ? 66.941 47.144 45.184 1.00 26.04  ? 201 HEM D C3C 1 
HETATM 4537 C  C4C . HEM H 3 .   ? 67.852 46.645 44.201 1.00 27.20  ? 201 HEM D C4C 1 
HETATM 4538 C  CMC . HEM H 3 .   ? 65.508 49.282 45.375 1.00 25.65  ? 201 HEM D CMC 1 
HETATM 4539 C  CAC . HEM H 3 .   ? 66.610 46.444 46.451 1.00 25.98  ? 201 HEM D CAC 1 
HETATM 4540 C  CBC . HEM H 3 .   ? 65.835 46.896 47.435 1.00 25.90  ? 201 HEM D CBC 1 
HETATM 4541 C  C1D . HEM H 3 .   ? 69.397 45.033 43.273 1.00 30.84  ? 201 HEM D C1D 1 
HETATM 4542 C  C2D . HEM H 3 .   ? 70.001 43.696 43.364 1.00 32.86  ? 201 HEM D C2D 1 
HETATM 4543 C  C3D . HEM H 3 .   ? 70.726 43.540 42.256 1.00 37.08  ? 201 HEM D C3D 1 
HETATM 4544 C  C4D . HEM H 3 .   ? 70.563 44.778 41.478 1.00 33.56  ? 201 HEM D C4D 1 
HETATM 4545 C  CMD . HEM H 3 .   ? 69.850 42.681 44.473 1.00 32.46  ? 201 HEM D CMD 1 
HETATM 4546 C  CAD . HEM H 3 .   ? 71.534 42.309 41.931 1.00 45.51  ? 201 HEM D CAD 1 
HETATM 4547 C  CBD . HEM H 3 .   ? 72.704 42.212 42.915 1.00 55.01  ? 201 HEM D CBD 1 
HETATM 4548 C  CGD . HEM H 3 .   ? 73.763 41.255 42.428 1.00 68.66  ? 201 HEM D CGD 1 
HETATM 4549 O  O1D . HEM H 3 .   ? 74.914 41.317 42.937 1.00 74.30  ? 201 HEM D O1D 1 
HETATM 4550 O  O2D . HEM H 3 .   ? 73.506 40.404 41.535 1.00 78.49  ? 201 HEM D O2D 1 
HETATM 4551 N  NA  . HEM H 3 .   ? 70.464 47.259 40.008 1.00 34.71  ? 201 HEM D NA  1 
HETATM 4552 N  NB  . HEM H 3 .   ? 68.653 49.307 40.965 1.00 29.00  ? 201 HEM D NB  1 
HETATM 4553 N  NC  . HEM H 3 .   ? 67.949 47.549 43.194 1.00 27.56  ? 201 HEM D NC  1 
HETATM 4554 N  ND  . HEM H 3 .   ? 69.750 45.645 42.126 1.00 31.24  ? 201 HEM D ND  1 
HETATM 4555 FE FE  . HEM H 3 .   ? 69.225 47.375 41.562 1.00 28.76  ? 201 HEM D FE  1 
HETATM 4556 O  O   . HOH I 4 .   ? 45.203 49.301 56.928 1.00 12.70  ? 301 HOH A O   1 
HETATM 4557 O  O   . HOH I 4 .   ? 45.570 45.452 54.476 1.00 16.28  ? 302 HOH A O   1 
HETATM 4558 O  O   . HOH I 4 .   ? 53.060 39.157 42.620 1.00 25.04  ? 303 HOH A O   1 
HETATM 4559 O  O   . HOH I 4 .   ? 70.075 47.324 60.618 1.00 29.72  ? 304 HOH A O   1 
HETATM 4560 O  O   . HOH I 4 .   ? 59.920 41.744 48.803 1.00 8.17   ? 305 HOH A O   1 
HETATM 4561 O  O   . HOH I 4 .   ? 45.033 45.349 57.555 1.00 6.46   ? 306 HOH A O   1 
HETATM 4562 O  O   . HOH I 4 .   ? 40.092 46.162 53.511 1.00 32.42  ? 307 HOH A O   1 
HETATM 4563 O  O   . HOH J 4 .   ? 40.489 52.046 60.293 1.00 22.03  ? 301 HOH B O   1 
HETATM 4564 O  O   . HOH J 4 .   ? 43.474 47.201 51.267 1.00 1.00   ? 302 HOH B O   1 
HETATM 4565 O  O   . HOH J 4 .   ? 47.473 51.039 42.039 1.00 38.91  ? 303 HOH B O   1 
HETATM 4566 O  O   . HOH J 4 .   ? 44.899 45.585 44.107 1.00 42.30  ? 304 HOH B O   1 
HETATM 4567 O  O   . HOH J 4 .   ? 38.257 53.825 62.216 1.00 23.56  ? 305 HOH B O   1 
HETATM 4568 O  O   . HOH K 4 .   ? 59.802 55.694 56.929 1.00 12.34  ? 301 HOH C O   1 
HETATM 4569 O  O   . HOH K 4 .   ? 59.414 59.533 54.460 1.00 16.51  ? 302 HOH C O   1 
HETATM 4570 O  O   . HOH K 4 .   ? 65.226 58.423 53.336 1.00 31.64  ? 303 HOH C O   1 
HETATM 4571 O  O   . HOH K 4 .   ? 34.924 57.677 60.618 1.00 31.04  ? 304 HOH C O   1 
HETATM 4572 O  O   . HOH K 4 .   ? 51.939 65.842 42.619 1.00 25.75  ? 305 HOH C O   1 
HETATM 4573 O  O   . HOH K 4 .   ? 45.078 63.251 48.793 1.00 7.77   ? 306 HOH C O   1 
HETATM 4574 O  O   . HOH K 4 .   ? 59.954 59.649 57.553 1.00 6.77   ? 307 HOH C O   1 
HETATM 4575 O  O   . HOH L 4 .   ? 64.518 52.936 60.299 1.00 21.44  ? 301 HOH D O   1 
HETATM 4576 O  O   . HOH L 4 .   ? 61.527 57.794 51.266 1.00 1.00   ? 302 HOH D O   1 
HETATM 4577 O  O   . HOH L 4 .   ? 57.525 53.960 42.040 1.00 39.71  ? 303 HOH D O   1 
HETATM 4578 O  O   . HOH L 4 .   ? 60.099 59.418 44.108 1.00 42.52  ? 304 HOH D O   1 
HETATM 4579 O  O   . HOH L 4 .   ? 66.745 51.174 62.217 1.00 22.77  ? 305 HOH D 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   VAL 1   1   1   VAL VAL A . n 
A 1 2   LEU 2   2   2   LEU LEU A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   ASN 9   9   9   ASN ASN A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  HIS 20  20  20  HIS HIS A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  HIS 58  58  58  HIS HIS A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  HIS 89  89  89  HIS HIS A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 CYS 104 104 104 CYS CYS A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
B 2 1   VAL 1   1   1   VAL VAL B . n 
B 2 2   HIS 2   2   2   HIS HIS B . n 
B 2 3   LEU 3   3   3   LEU LEU B . n 
B 2 4   THR 4   4   4   THR THR B . n 
B 2 5   PRO 5   5   5   PRO PRO B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   GLU 7   7   7   GLU GLU B . n 
B 2 8   LYS 8   8   8   LYS LYS B . n 
B 2 9   SER 9   9   9   SER SER B . n 
B 2 10  ALA 10  10  10  ALA ALA B . n 
B 2 11  VAL 11  11  11  VAL VAL B . n 
B 2 12  THR 12  12  12  THR THR B . n 
B 2 13  ALA 13  13  13  ALA ALA B . n 
B 2 14  LEU 14  14  14  LEU LEU B . n 
B 2 15  TRP 15  15  15  TRP TRP B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  LYS 17  17  17  LYS LYS B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASN 19  19  19  ASN ASN B . n 
B 2 20  VAL 20  20  20  VAL VAL B . n 
B 2 21  ASP 21  21  21  ASP ASP B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  VAL 23  23  23  VAL VAL B . n 
B 2 24  GLY 24  24  24  GLY GLY B . n 
B 2 25  GLY 25  25  25  GLY GLY B . n 
B 2 26  GLU 26  26  26  GLU GLU B . n 
B 2 27  ALA 27  27  27  ALA ALA B . n 
B 2 28  LEU 28  28  28  LEU LEU B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ARG 30  30  30  ARG ARG B . n 
B 2 31  LEU 31  31  31  LEU LEU B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  VAL 33  33  33  VAL VAL B . n 
B 2 34  VAL 34  34  34  VAL VAL B . n 
B 2 35  TYR 35  35  35  TYR TYR B . n 
B 2 36  PRO 36  36  36  PRO PRO B . n 
B 2 37  TRP 37  37  37  TRP TRP B . n 
B 2 38  THR 38  38  38  THR THR B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ARG 40  40  40  ARG ARG B . n 
B 2 41  PHE 41  41  41  PHE PHE B . n 
B 2 42  PHE 42  42  42  PHE PHE B . n 
B 2 43  GLU 43  43  43  GLU GLU B . n 
B 2 44  SER 44  44  44  SER SER B . n 
B 2 45  PHE 45  45  45  PHE PHE B . n 
B 2 46  GLY 46  46  46  GLY GLY B . n 
B 2 47  ASP 47  47  47  ASP ASP B . n 
B 2 48  LEU 48  48  48  LEU LEU B . n 
B 2 49  SER 49  49  49  SER SER B . n 
B 2 50  THR 50  50  50  THR THR B . n 
B 2 51  PRO 51  51  51  PRO PRO B . n 
B 2 52  ASP 52  52  52  ASP ASP B . n 
B 2 53  ALA 53  53  53  ALA ALA B . n 
B 2 54  VAL 54  54  54  VAL VAL B . n 
B 2 55  MET 55  55  55  MET MET B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  PRO 58  58  58  PRO PRO B . n 
B 2 59  LYS 59  59  59  LYS LYS B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  LYS 61  61  61  LYS LYS B . n 
B 2 62  ALA 62  62  62  ALA ALA B . n 
B 2 63  HIS 63  63  63  HIS HIS B . n 
B 2 64  GLY 64  64  64  GLY GLY B . n 
B 2 65  LYS 65  65  65  LYS LYS B . n 
B 2 66  LYS 66  66  66  LYS LYS B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLY 69  69  69  GLY GLY B . n 
B 2 70  ALA 70  70  70  ALA ALA B . n 
B 2 71  PHE 71  71  71  PHE PHE B . n 
B 2 72  SER 72  72  72  SER SER B . n 
B 2 73  ASP 73  73  73  ASP ASP B . n 
B 2 74  GLY 74  74  74  GLY GLY B . n 
B 2 75  LEU 75  75  75  LEU LEU B . n 
B 2 76  ALA 76  76  76  ALA ALA B . n 
B 2 77  HIS 77  77  77  HIS HIS B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  ASP 79  79  79  ASP ASP B . n 
B 2 80  ASN 80  80  80  ASN ASN B . n 
B 2 81  LEU 81  81  81  LEU LEU B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  GLY 83  83  83  GLY GLY B . n 
B 2 84  THR 84  84  84  THR THR B . n 
B 2 85  PHE 85  85  85  PHE PHE B . n 
B 2 86  ALA 86  86  86  ALA ALA B . n 
B 2 87  THR 87  87  87  THR THR B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  SER 89  89  89  SER SER B . n 
B 2 90  GLU 90  90  90  GLU GLU B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  HIS 92  92  92  HIS HIS B . n 
B 2 93  CYS 93  93  93  CYS CYS B . n 
B 2 94  ASP 94  94  94  ASP ASP B . n 
B 2 95  LYS 95  95  95  LYS LYS B . n 
B 2 96  LEU 96  96  96  LEU LEU B . n 
B 2 97  HIS 97  97  97  HIS HIS B . n 
B 2 98  VAL 98  98  98  VAL VAL B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 PRO 100 100 100 PRO PRO B . n 
B 2 101 GLU 101 101 101 GLU GLU B . n 
B 2 102 ASN 102 102 102 ASN ASN B . n 
B 2 103 PHE 103 103 103 PHE PHE B . n 
B 2 104 ARG 104 104 104 ARG ARG B . n 
B 2 105 LEU 105 105 105 LEU LEU B . n 
B 2 106 LEU 106 106 106 LEU LEU B . n 
B 2 107 GLY 107 107 107 GLY GLY B . n 
B 2 108 ASN 108 108 108 ASN ASN B . n 
B 2 109 VAL 109 109 109 VAL VAL B . n 
B 2 110 LEU 110 110 110 LEU LEU B . n 
B 2 111 VAL 111 111 111 VAL VAL B . n 
B 2 112 CYS 112 112 112 CYS CYS B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 ALA 115 115 115 ALA ALA B . n 
B 2 116 HIS 116 116 116 HIS HIS B . n 
B 2 117 HIS 117 117 117 HIS HIS B . n 
B 2 118 PHE 118 118 118 PHE PHE B . n 
B 2 119 GLY 119 119 119 GLY GLY B . n 
B 2 120 LYS 120 120 120 LYS LYS B . n 
B 2 121 GLU 121 121 121 GLU GLU B . n 
B 2 122 PHE 122 122 122 PHE PHE B . n 
B 2 123 THR 123 123 123 THR THR B . n 
B 2 124 PRO 124 124 124 PRO PRO B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 VAL 126 126 126 VAL VAL B . n 
B 2 127 GLN 127 127 127 GLN GLN B . n 
B 2 128 ALA 128 128 128 ALA ALA B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 TYR 130 130 130 TYR TYR B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 LYS 132 132 132 LYS LYS B . n 
B 2 133 VAL 133 133 133 VAL VAL B . n 
B 2 134 VAL 134 134 134 VAL VAL B . n 
B 2 135 ALA 135 135 135 ALA ALA B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 VAL 137 137 137 VAL VAL B . n 
B 2 138 ALA 138 138 138 ALA ALA B . n 
B 2 139 ASN 139 139 139 ASN ASN B . n 
B 2 140 ALA 140 140 140 ALA ALA B . n 
B 2 141 LEU 141 141 141 LEU LEU B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 HIS 143 143 143 HIS HIS B . n 
B 2 144 LYS 144 144 144 LYS LYS B . n 
B 2 145 TYR 145 145 145 TYR TYR B . n 
B 2 146 HIS 146 146 146 HIS HIS B . n 
C 1 1   VAL 1   1   1   VAL VAL C . n 
C 1 2   LEU 2   2   2   LEU LEU C . n 
C 1 3   SER 3   3   3   SER SER C . n 
C 1 4   PRO 4   4   4   PRO PRO C . n 
C 1 5   ALA 5   5   5   ALA ALA C . n 
C 1 6   ASP 6   6   6   ASP ASP C . n 
C 1 7   LYS 7   7   7   LYS LYS C . n 
C 1 8   THR 8   8   8   THR THR C . n 
C 1 9   ASN 9   9   9   ASN ASN C . n 
C 1 10  VAL 10  10  10  VAL VAL C . n 
C 1 11  LYS 11  11  11  LYS LYS C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  ALA 13  13  13  ALA ALA C . n 
C 1 14  TRP 14  14  14  TRP TRP C . n 
C 1 15  GLY 15  15  15  GLY GLY C . n 
C 1 16  LYS 16  16  16  LYS LYS C . n 
C 1 17  VAL 17  17  17  VAL VAL C . n 
C 1 18  GLY 18  18  18  GLY GLY C . n 
C 1 19  ALA 19  19  19  ALA ALA C . n 
C 1 20  HIS 20  20  20  HIS HIS C . n 
C 1 21  ALA 21  21  21  ALA ALA C . n 
C 1 22  GLY 22  22  22  GLY GLY C . n 
C 1 23  GLU 23  23  23  GLU GLU C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  GLY 25  25  25  GLY GLY C . n 
C 1 26  ALA 26  26  26  ALA ALA C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  LEU 29  29  29  LEU LEU C . n 
C 1 30  GLU 30  30  30  GLU GLU C . n 
C 1 31  ARG 31  31  31  ARG ARG C . n 
C 1 32  MET 32  32  32  MET MET C . n 
C 1 33  PHE 33  33  33  PHE PHE C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  SER 35  35  35  SER SER C . n 
C 1 36  PHE 36  36  36  PHE PHE C . n 
C 1 37  PRO 37  37  37  PRO PRO C . n 
C 1 38  THR 38  38  38  THR THR C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  LYS 40  40  40  LYS LYS C . n 
C 1 41  THR 41  41  41  THR THR C . n 
C 1 42  TYR 42  42  42  TYR TYR C . n 
C 1 43  PHE 43  43  43  PHE PHE C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  HIS 45  45  45  HIS HIS C . n 
C 1 46  PHE 46  46  46  PHE PHE C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  LEU 48  48  48  LEU LEU C . n 
C 1 49  SER 49  49  49  SER SER C . n 
C 1 50  HIS 50  50  50  HIS HIS C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  ALA 53  53  53  ALA ALA C . n 
C 1 54  GLN 54  54  54  GLN GLN C . n 
C 1 55  VAL 55  55  55  VAL VAL C . n 
C 1 56  LYS 56  56  56  LYS LYS C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  HIS 58  58  58  HIS HIS C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  LYS 60  60  60  LYS LYS C . n 
C 1 61  LYS 61  61  61  LYS LYS C . n 
C 1 62  VAL 62  62  62  VAL VAL C . n 
C 1 63  ALA 63  63  63  ALA ALA C . n 
C 1 64  ASP 64  64  64  ASP ASP C . n 
C 1 65  ALA 65  65  65  ALA ALA C . n 
C 1 66  LEU 66  66  66  LEU LEU C . n 
C 1 67  THR 67  67  67  THR THR C . n 
C 1 68  ASN 68  68  68  ASN ASN C . n 
C 1 69  ALA 69  69  69  ALA ALA C . n 
C 1 70  VAL 70  70  70  VAL VAL C . n 
C 1 71  ALA 71  71  71  ALA ALA C . n 
C 1 72  HIS 72  72  72  HIS HIS C . n 
C 1 73  VAL 73  73  73  VAL VAL C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  PRO 77  77  77  PRO PRO C . n 
C 1 78  ASN 78  78  78  ASN ASN C . n 
C 1 79  ALA 79  79  79  ALA ALA C . n 
C 1 80  LEU 80  80  80  LEU LEU C . n 
C 1 81  SER 81  81  81  SER ALA C . n 
C 1 82  ALA 82  82  82  ALA ALA C . n 
C 1 83  LEU 83  83  83  LEU LEU C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  LEU 86  86  86  LEU LEU C . n 
C 1 87  HIS 87  87  87  HIS HIS C . n 
C 1 88  ALA 88  88  88  ALA ALA C . n 
C 1 89  HIS 89  89  89  HIS HIS C . n 
C 1 90  LYS 90  90  90  LYS LYS C . n 
C 1 91  LEU 91  91  91  LEU LEU C . n 
C 1 92  ARG 92  92  92  ARG ARG C . n 
C 1 93  VAL 93  93  93  VAL VAL C . n 
C 1 94  ASP 94  94  94  ASP ASP C . n 
C 1 95  PRO 95  95  95  PRO PRO C . n 
C 1 96  VAL 96  96  96  VAL VAL C . n 
C 1 97  ASN 97  97  97  ASN ASN C . n 
C 1 98  PHE 98  98  98  PHE PHE C . n 
C 1 99  LYS 99  99  99  LYS LYS C . n 
C 1 100 LEU 100 100 100 LEU LEU C . n 
C 1 101 LEU 101 101 101 LEU LEU C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 HIS 103 103 103 HIS HIS C . n 
C 1 104 CYS 104 104 104 CYS CYS C . n 
C 1 105 LEU 105 105 105 LEU LEU C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 THR 108 108 108 THR THR C . n 
C 1 109 LEU 109 109 109 LEU LEU C . n 
C 1 110 ALA 110 110 110 ALA ALA C . n 
C 1 111 ALA 111 111 111 ALA ALA C . n 
C 1 112 HIS 112 112 112 HIS HIS C . n 
C 1 113 LEU 113 113 113 LEU LEU C . n 
C 1 114 PRO 114 114 114 PRO PRO C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 GLU 116 116 116 GLU GLU C . n 
C 1 117 PHE 117 117 117 PHE PHE C . n 
C 1 118 THR 118 118 118 THR THR C . n 
C 1 119 PRO 119 119 119 PRO PRO C . n 
C 1 120 ALA 120 120 120 ALA ALA C . n 
C 1 121 VAL 121 121 121 VAL VAL C . n 
C 1 122 HIS 122 122 122 HIS HIS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 SER 124 124 124 SER SER C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 ASP 126 126 126 ASP ASP C . n 
C 1 127 LYS 127 127 127 LYS LYS C . n 
C 1 128 PHE 128 128 128 PHE PHE C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 ALA 130 130 130 ALA ALA C . n 
C 1 131 SER 131 131 131 SER SER C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 THR 134 134 134 THR THR C . n 
C 1 135 VAL 135 135 135 VAL VAL C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 SER 138 138 138 SER SER C . n 
C 1 139 LYS 139 139 139 LYS LYS C . n 
C 1 140 TYR 140 140 140 TYR TYR C . n 
C 1 141 ARG 141 141 141 ARG ARG C . n 
D 2 1   VAL 1   1   1   VAL VAL D . n 
D 2 2   HIS 2   2   2   HIS HIS D . n 
D 2 3   LEU 3   3   3   LEU LEU D . n 
D 2 4   THR 4   4   4   THR THR D . n 
D 2 5   PRO 5   5   5   PRO PRO D . n 
D 2 6   GLU 6   6   6   GLU GLU D . n 
D 2 7   GLU 7   7   7   GLU GLU D . n 
D 2 8   LYS 8   8   8   LYS LYS D . n 
D 2 9   SER 9   9   9   SER SER D . n 
D 2 10  ALA 10  10  10  ALA ALA D . n 
D 2 11  VAL 11  11  11  VAL VAL D . n 
D 2 12  THR 12  12  12  THR THR D . n 
D 2 13  ALA 13  13  13  ALA ALA D . n 
D 2 14  LEU 14  14  14  LEU LEU D . n 
D 2 15  TRP 15  15  15  TRP TRP D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  LYS 17  17  17  LYS LYS D . n 
D 2 18  VAL 18  18  18  VAL VAL D . n 
D 2 19  ASN 19  19  19  ASN ASN D . n 
D 2 20  VAL 20  20  20  VAL VAL D . n 
D 2 21  ASP 21  21  21  ASP ASP D . n 
D 2 22  GLU 22  22  22  GLU GLU D . n 
D 2 23  VAL 23  23  23  VAL VAL D . n 
D 2 24  GLY 24  24  24  GLY GLY D . n 
D 2 25  GLY 25  25  25  GLY GLY D . n 
D 2 26  GLU 26  26  26  GLU GLU D . n 
D 2 27  ALA 27  27  27  ALA ALA D . n 
D 2 28  LEU 28  28  28  LEU LEU D . n 
D 2 29  GLY 29  29  29  GLY GLY D . n 
D 2 30  ARG 30  30  30  ARG ARG D . n 
D 2 31  LEU 31  31  31  LEU LEU D . n 
D 2 32  LEU 32  32  32  LEU LEU D . n 
D 2 33  VAL 33  33  33  VAL VAL D . n 
D 2 34  VAL 34  34  34  VAL VAL D . n 
D 2 35  TYR 35  35  35  TYR TYR D . n 
D 2 36  PRO 36  36  36  PRO PRO D . n 
D 2 37  TRP 37  37  37  TRP TRP D . n 
D 2 38  THR 38  38  38  THR THR D . n 
D 2 39  GLN 39  39  39  GLN GLN D . n 
D 2 40  ARG 40  40  40  ARG ARG D . n 
D 2 41  PHE 41  41  41  PHE PHE D . n 
D 2 42  PHE 42  42  42  PHE PHE D . n 
D 2 43  GLU 43  43  43  GLU GLU D . n 
D 2 44  SER 44  44  44  SER SER D . n 
D 2 45  PHE 45  45  45  PHE PHE D . n 
D 2 46  GLY 46  46  46  GLY GLY D . n 
D 2 47  ASP 47  47  47  ASP ASP D . n 
D 2 48  LEU 48  48  48  LEU LEU D . n 
D 2 49  SER 49  49  49  SER SER D . n 
D 2 50  THR 50  50  50  THR THR D . n 
D 2 51  PRO 51  51  51  PRO PRO D . n 
D 2 52  ASP 52  52  52  ASP ASP D . n 
D 2 53  ALA 53  53  53  ALA ALA D . n 
D 2 54  VAL 54  54  54  VAL VAL D . n 
D 2 55  MET 55  55  55  MET MET D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  ASN 57  57  57  ASN ASN D . n 
D 2 58  PRO 58  58  58  PRO PRO D . n 
D 2 59  LYS 59  59  59  LYS LYS D . n 
D 2 60  VAL 60  60  60  VAL VAL D . n 
D 2 61  LYS 61  61  61  LYS LYS D . n 
D 2 62  ALA 62  62  62  ALA ALA D . n 
D 2 63  HIS 63  63  63  HIS HIS D . n 
D 2 64  GLY 64  64  64  GLY GLY D . n 
D 2 65  LYS 65  65  65  LYS LYS D . n 
D 2 66  LYS 66  66  66  LYS LYS D . n 
D 2 67  VAL 67  67  67  VAL VAL D . n 
D 2 68  LEU 68  68  68  LEU LEU D . n 
D 2 69  GLY 69  69  69  GLY GLY D . n 
D 2 70  ALA 70  70  70  ALA ALA D . n 
D 2 71  PHE 71  71  71  PHE PHE D . n 
D 2 72  SER 72  72  72  SER SER D . n 
D 2 73  ASP 73  73  73  ASP ASP D . n 
D 2 74  GLY 74  74  74  GLY GLY D . n 
D 2 75  LEU 75  75  75  LEU LEU D . n 
D 2 76  ALA 76  76  76  ALA ALA D . n 
D 2 77  HIS 77  77  77  HIS HIS D . n 
D 2 78  LEU 78  78  78  LEU LEU D . n 
D 2 79  ASP 79  79  79  ASP ASP D . n 
D 2 80  ASN 80  80  80  ASN ASN D . n 
D 2 81  LEU 81  81  81  LEU LEU D . n 
D 2 82  LYS 82  82  82  LYS LYS D . n 
D 2 83  GLY 83  83  83  GLY GLY D . n 
D 2 84  THR 84  84  84  THR THR D . n 
D 2 85  PHE 85  85  85  PHE PHE D . n 
D 2 86  ALA 86  86  86  ALA ALA D . n 
D 2 87  THR 87  87  87  THR THR D . n 
D 2 88  LEU 88  88  88  LEU LEU D . n 
D 2 89  SER 89  89  89  SER SER D . n 
D 2 90  GLU 90  90  90  GLU GLU D . n 
D 2 91  LEU 91  91  91  LEU LEU D . n 
D 2 92  HIS 92  92  92  HIS HIS D . n 
D 2 93  CYS 93  93  93  CYS CYS D . n 
D 2 94  ASP 94  94  94  ASP ASP D . n 
D 2 95  LYS 95  95  95  LYS LYS D . n 
D 2 96  LEU 96  96  96  LEU LEU D . n 
D 2 97  HIS 97  97  97  HIS HIS D . n 
D 2 98  VAL 98  98  98  VAL VAL D . n 
D 2 99  ASP 99  99  99  ASP ASP D . n 
D 2 100 PRO 100 100 100 PRO PRO D . n 
D 2 101 GLU 101 101 101 GLU GLU D . n 
D 2 102 ASN 102 102 102 ASN ASN D . n 
D 2 103 PHE 103 103 103 PHE PHE D . n 
D 2 104 ARG 104 104 104 ARG ARG D . n 
D 2 105 LEU 105 105 105 LEU LEU D . n 
D 2 106 LEU 106 106 106 LEU LEU D . n 
D 2 107 GLY 107 107 107 GLY GLY D . n 
D 2 108 ASN 108 108 108 ASN ASN D . n 
D 2 109 VAL 109 109 109 VAL VAL D . n 
D 2 110 LEU 110 110 110 LEU LEU D . n 
D 2 111 VAL 111 111 111 VAL VAL D . n 
D 2 112 CYS 112 112 112 CYS CYS D . n 
D 2 113 VAL 113 113 113 VAL VAL D . n 
D 2 114 LEU 114 114 114 LEU LEU D . n 
D 2 115 ALA 115 115 115 ALA ALA D . n 
D 2 116 HIS 116 116 116 HIS HIS D . n 
D 2 117 HIS 117 117 117 HIS HIS D . n 
D 2 118 PHE 118 118 118 PHE PHE D . n 
D 2 119 GLY 119 119 119 GLY GLY D . n 
D 2 120 LYS 120 120 120 LYS LYS D . n 
D 2 121 GLU 121 121 121 GLU GLU D . n 
D 2 122 PHE 122 122 122 PHE PHE D . n 
D 2 123 THR 123 123 123 THR THR D . n 
D 2 124 PRO 124 124 124 PRO PRO D . n 
D 2 125 PRO 125 125 125 PRO PRO D . n 
D 2 126 VAL 126 126 126 VAL VAL D . n 
D 2 127 GLN 127 127 127 GLN GLN D . n 
D 2 128 ALA 128 128 128 ALA ALA D . n 
D 2 129 ALA 129 129 129 ALA ALA D . n 
D 2 130 TYR 130 130 130 TYR TYR D . n 
D 2 131 GLN 131 131 131 GLN GLN D . n 
D 2 132 LYS 132 132 132 LYS LYS D . n 
D 2 133 VAL 133 133 133 VAL VAL D . n 
D 2 134 VAL 134 134 134 VAL VAL D . n 
D 2 135 ALA 135 135 135 ALA ALA D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 VAL 137 137 137 VAL VAL D . n 
D 2 138 ALA 138 138 138 ALA ALA D . n 
D 2 139 ASN 139 139 139 ASN ASN D . n 
D 2 140 ALA 140 140 140 ALA ALA D . n 
D 2 141 LEU 141 141 141 LEU LEU D . n 
D 2 142 ALA 142 142 142 ALA ALA D . n 
D 2 143 HIS 143 143 143 HIS HIS D . n 
D 2 144 LYS 144 144 144 LYS LYS D . n 
D 2 145 TYR 145 145 145 TYR TYR D . n 
D 2 146 HIS 146 146 146 HIS HIS D . 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 
E 3 HEM 1 201 201 HEM HEM A . 
F 3 HEM 1 201 201 HEM HEM B . 
G 3 HEM 1 201 201 HEM HEM C . 
H 3 HEM 1 201 201 HEM HEM D . 
I 4 HOH 1 301 10  HOH HOH A . 
I 4 HOH 2 302 2   HOH HOH A . 
I 4 HOH 3 303 9   HOH HOH A . 
I 4 HOH 4 304 24  HOH HOH A . 
I 4 HOH 5 305 5   HOH HOH A . 
I 4 HOH 6 306 8   HOH HOH A . 
I 4 HOH 7 307 18  HOH HOH A . 
J 4 HOH 1 301 21  HOH HOH B . 
J 4 HOH 2 302 3   HOH HOH B . 
J 4 HOH 3 303 15  HOH HOH B . 
J 4 HOH 4 304 14  HOH HOH B . 
J 4 HOH 5 305 19  HOH HOH B . 
K 4 HOH 1 301 12  HOH HOH C . 
K 4 HOH 2 302 1   HOH HOH C . 
K 4 HOH 3 303 17  HOH HOH C . 
K 4 HOH 4 304 23  HOH HOH C . 
K 4 HOH 5 305 11  HOH HOH C . 
K 4 HOH 6 306 6   HOH HOH C . 
K 4 HOH 7 307 7   HOH HOH C . 
L 4 HOH 1 301 22  HOH HOH D . 
L 4 HOH 2 302 4   HOH HOH D . 
L 4 HOH 3 303 16  HOH HOH D . 
L 4 HOH 4 304 13  HOH HOH D . 
L 4 HOH 5 305 20  HOH HOH D . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_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   ? 
_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  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 NA ? E HEM . ? A HEM 201 ? 1_555 91.8  ? 
2  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 NB ? E HEM . ? A HEM 201 ? 1_555 93.1  ? 
3  NA  ? E HEM .  ? A HEM 201 ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 NB ? E HEM . ? A HEM 201 ? 1_555 90.4  ? 
4  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 NC ? E HEM . ? A HEM 201 ? 1_555 89.3  ? 
5  NA  ? E HEM .  ? A HEM 201 ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 NC ? E HEM . ? A HEM 201 ? 1_555 178.3 ? 
6  NB  ? E HEM .  ? A HEM 201 ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 NC ? E HEM . ? A HEM 201 ? 1_555 88.3  ? 
7  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 ND ? E HEM . ? A HEM 201 ? 1_555 87.0  ? 
8  NA  ? E HEM .  ? A HEM 201 ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 ND ? E HEM . ? A HEM 201 ? 1_555 90.0  ? 
9  NB  ? E HEM .  ? A HEM 201 ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 ND ? E HEM . ? A HEM 201 ? 1_555 179.6 ? 
10 NC  ? E HEM .  ? A HEM 201 ? 1_555 FE ? E HEM . ? A HEM 201 ? 1_555 ND ? E HEM . ? A HEM 201 ? 1_555 91.3  ? 
11 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NA ? F HEM . ? B HEM 201 ? 1_555 87.4  ? 
12 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NB ? F HEM . ? B HEM 201 ? 1_555 93.9  ? 
13 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NB ? F HEM . ? B HEM 201 ? 1_555 90.0  ? 
14 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NC ? F HEM . ? B HEM 201 ? 1_555 93.8  ? 
15 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NC ? F HEM . ? B HEM 201 ? 1_555 178.2 ? 
16 NB  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NC ? F HEM . ? B HEM 201 ? 1_555 88.6  ? 
17 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 86.8  ? 
18 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 90.6  ? 
19 NB  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 179.1 ? 
20 NC  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 90.9  ? 
21 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 NA ? G HEM . ? C HEM 201 ? 1_555 91.8  ? 
22 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 NB ? G HEM . ? C HEM 201 ? 1_555 93.0  ? 
23 NA  ? G HEM .  ? C HEM 201 ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 NB ? G HEM . ? C HEM 201 ? 1_555 90.5  ? 
24 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 NC ? G HEM . ? C HEM 201 ? 1_555 89.4  ? 
25 NA  ? G HEM .  ? C HEM 201 ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 NC ? G HEM . ? C HEM 201 ? 1_555 178.4 ? 
26 NB  ? G HEM .  ? C HEM 201 ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 NC ? G HEM . ? C HEM 201 ? 1_555 88.3  ? 
27 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 ND ? G HEM . ? C HEM 201 ? 1_555 87.0  ? 
28 NA  ? G HEM .  ? C HEM 201 ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 ND ? G HEM . ? C HEM 201 ? 1_555 89.9  ? 
29 NB  ? G HEM .  ? C HEM 201 ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 ND ? G HEM . ? C HEM 201 ? 1_555 179.6 ? 
30 NC  ? G HEM .  ? C HEM 201 ? 1_555 FE ? G HEM . ? C HEM 201 ? 1_555 ND ? G HEM . ? C HEM 201 ? 1_555 91.3  ? 
31 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 NA ? H HEM . ? D HEM 201 ? 1_555 87.3  ? 
32 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 NB ? H HEM . ? D HEM 201 ? 1_555 94.0  ? 
33 NA  ? H HEM .  ? D HEM 201 ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 NB ? H HEM . ? D HEM 201 ? 1_555 90.1  ? 
34 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 NC ? H HEM . ? D HEM 201 ? 1_555 93.9  ? 
35 NA  ? H HEM .  ? D HEM 201 ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 NC ? H HEM . ? D HEM 201 ? 1_555 178.4 ? 
36 NB  ? H HEM .  ? D HEM 201 ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 NC ? H HEM . ? D HEM 201 ? 1_555 88.8  ? 
37 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 ND ? H HEM . ? D HEM 201 ? 1_555 86.8  ? 
38 NA  ? H HEM .  ? D HEM 201 ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 ND ? H HEM . ? D HEM 201 ? 1_555 90.4  ? 
39 NB  ? H HEM .  ? D HEM 201 ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 ND ? H HEM . ? D HEM 201 ? 1_555 179.1 ? 
40 NC  ? H HEM .  ? D HEM 201 ? 1_555 FE ? H HEM . ? D HEM 201 ? 1_555 ND ? H HEM . ? D HEM 201 ? 1_555 90.7  ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2017-04-12 
# 
_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         ? 
# 
_software.citation_id            ? 
_software.classification         refinement 
_software.compiler_name          ? 
_software.compiler_version       ? 
_software.contact_author         ? 
_software.contact_author_email   ? 
_software.date                   ? 
_software.description            ? 
_software.dependencies           ? 
_software.hardware               ? 
_software.language               ? 
_software.location               ? 
_software.mods                   ? 
_software.name                   REFMAC 
_software.os                     ? 
_software.os_version             ? 
_software.type                   ? 
_software.version                5.8.0158 
_software.pdbx_ordinal           1 
# 
_em_3d_reconstruction.entry_id                    5NI1 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.num_particles               175300 
_em_3d_reconstruction.resolution                  3.2 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.symmetry_type               POINT 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.magnification_calibration   ? 
# 
_em_buffer.id            1 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.details              ? 
_em_entity_assembly.name                 Hemoglobin 
_em_entity_assembly.source               NATURAL 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
# 
_em_image_scans.entry_id                5NI1 
_em_image_scans.citation_id             ? 
_em_image_scans.id                      1 
_em_image_scans.image_recording_id      1 
_em_image_scans.number_digital_images   ? 
_em_image_scans.od_range                ? 
_em_image_scans.quant_bit_size          ? 
_em_image_scans.sampling_size           ? 
_em_image_scans.scanner_model           ? 
_em_image_scans.details                 ? 
# 
_em_imaging.id                              1 
_em_imaging.entry_id                        5NI1 
_em_imaging.accelerating_voltage            300 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.cryogen                         ? 
_em_imaging.details                         ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.illumination_mode               OTHER 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_max             ? 
_em_imaging.nominal_defocus_min             ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.specimen_id                     1 
_em_imaging.citation_id                     ? 
_em_imaging.date                            ? 
_em_imaging.temperature                     ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.astigmatism                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.specimen_holder_type            ? 
# 
_em_sample_support.id               1 
_em_sample_support.specimen_id      1 
_em_sample_support.method           ? 
_em_sample_support.film_material    ? 
_em_sample_support.grid_material    ? 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        ? 
_em_sample_support.details          ? 
# 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.cryogen_name          ETHANE-PROPANE 
_em_vitrification.details               ? 
_em_vitrification.humidity              100 
_em_vitrification.instrument            ? 
_em_vitrification.entry_id              5NI1 
_em_vitrification.citation_id           ? 
_em_vitrification.method                ? 
_em_vitrification.temp                  ? 
_em_vitrification.time_resolved_state   ? 
# 
_em_experiment.entry_id                5NI1 
_em_experiment.id                      1 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.entity_assembly_id      1 
# 
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 LEU A 2   ? ? -166.05 110.32 
2  1 PHE A 43  ? ? -108.93 77.01  
3  1 LEU A 48  ? ? -93.24  48.47  
4  1 HIS A 72  ? ? -109.99 49.04  
5  1 PHE A 117 ? ? -104.19 58.40  
6  1 PRO B 51  ? ? -34.58  -38.74 
7  1 HIS B 77  ? ? -103.58 68.79  
8  1 LEU C 2   ? ? -166.03 110.27 
9  1 PHE C 43  ? ? -108.89 77.03  
10 1 LEU C 48  ? ? -93.20  48.37  
11 1 PHE C 117 ? ? -104.22 58.39  
12 1 PRO D 51  ? ? -35.06  -38.66 
13 1 HIS D 77  ? ? -103.57 68.76  
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     C 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      81 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     OG 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    C 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     81 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    OG 
# 
_em_ctf_correction.id                       1 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
_em_ctf_correction.details                  ? 
# 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
# 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
_em_image_processing.details              ? 
# 
_em_image_recording.id                            1 
_em_image_recording.imaging_id                    1 
_em_image_recording.avg_electron_dose_per_image   40 
_em_image_recording.average_exposure_time         ? 
_em_image_recording.details                       ? 
_em_image_recording.detector_mode                 ? 
_em_image_recording.film_or_detector_model        'GATAN K2 SUMMIT (4k x 4k)' 
_em_image_recording.num_diffraction_images        ? 
_em_image_recording.num_grids_imaged              ? 
_em_image_recording.num_real_images               ? 
# 
loop_
_em_software.id 
_em_software.category 
_em_software.details 
_em_software.name 
_em_software.version 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
1  'PARTICLE SELECTION'       ? ? ? 1 ? ? 
2  'IMAGE ACQUISITION'        ? ? ? ? ? 1 
3  MASKING                    ? ? ? ? ? ? 
4  'CTF CORRECTION'           ? ? ? 1 ? ? 
5  'LAYERLINE INDEXING'       ? ? ? ? ? ? 
6  'DIFFRACTION INDEXING'     ? ? ? ? ? ? 
7  'MODEL FITTING'            ? ? ? ? ? ? 
8  'MODEL REFINEMENT'         ? ? ? ? ? ? 
9  OTHER                      ? ? ? ? ? ? 
10 'INITIAL EULER ASSIGNMENT' ? ? ? 1 ? ? 
11 'FINAL EULER ASSIGNMENT'   ? ? ? 1 ? ? 
12 CLASSIFICATION             ? ? ? 1 ? ? 
13 RECONSTRUCTION             ? ? ? 1 ? ? 
# 
_em_specimen.id                      1 
_em_specimen.experiment_id           1 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
4 water                             HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   microscopy 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
