data_9ECT
# 
_entry.id   9ECT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ECT         pdb_00009ect 10.2210/pdb9ect/pdb 
WWPDB D_1000290191 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ECT 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              tholyoak@uwaterloo.ca 
_pdbx_contact_author.name_first         Todd 
_pdbx_contact_author.name_last          Holyoak 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7329-1115 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tran, N.'    1 0000-0002-9372-9444 
'Holyoak, T.' 2 0000-0002-7329-1115 
# 
_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            'Acta Crystallogr.,Sect.F' 
_citation.journal_id_ASTM           ACSFEN 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2053-230X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            81 
_citation.language                  ? 
_citation.page_first                124 
_citation.page_last                 129 
_citation.title                     'The structure of the Gemella haemolysans M26 IgA1 protease trypsin-like domain.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2053230X25001219 
_citation.pdbx_database_id_PubMed   40019192 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tran, N.'          1 ? 
primary 'Redzic, J.S.'      2 ? 
primary 'Eisenmesser, E.Z.' 3 ? 
primary 'Holyoak, T.'       4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'LPXTG-motif cell wall anchor domain protein' 23612.195 2   ? ? ? 
'N-terminus contains two non-native residues (GS) as a consequence of the thrombin cleavage sequence' 
2 water   nat water                                         18.015    542 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSNNVPKNASALLRMNFVKGNQVLSGTGSATFIAPNVLLTVAHNFINNSADNSTGEFIGDKSKNTYEWQTPDGQKGSFTS
EDIHFYNKKDYPKGFIYDLAVITLPQSTRRQHANLVENYSKVNVNDKLNVYGYPRGEYAHLKDTTVEIEQKYANNTYGVQ
YQGGKAGMSGGGIFNSKGEVIGLHQNGAENRSGGLILSPTQLDWIRSIIKGKEIT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSNNVPKNASALLRMNFVKGNQVLSGTGSATFIAPNVLLTVAHNFINNSADNSTGEFIGDKSKNTYEWQTPDGQKGSFTS
EDIHFYNKKDYPKGFIYDLAVITLPQSTRRQHANLVENYSKVNVNDKLNVYGYPRGEYAHLKDTTVEIEQKYANNTYGVQ
YQGGKAGMSGGGIFNSKGEVIGLHQNGAENRSGGLILSPTQLDWIRSIIKGKEIT
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ASN n 
1 4   ASN n 
1 5   VAL n 
1 6   PRO n 
1 7   LYS n 
1 8   ASN n 
1 9   ALA n 
1 10  SER n 
1 11  ALA n 
1 12  LEU n 
1 13  LEU n 
1 14  ARG n 
1 15  MET n 
1 16  ASN n 
1 17  PHE n 
1 18  VAL n 
1 19  LYS n 
1 20  GLY n 
1 21  ASN n 
1 22  GLN n 
1 23  VAL n 
1 24  LEU n 
1 25  SER n 
1 26  GLY n 
1 27  THR n 
1 28  GLY n 
1 29  SER n 
1 30  ALA n 
1 31  THR n 
1 32  PHE n 
1 33  ILE n 
1 34  ALA n 
1 35  PRO n 
1 36  ASN n 
1 37  VAL n 
1 38  LEU n 
1 39  LEU n 
1 40  THR n 
1 41  VAL n 
1 42  ALA n 
1 43  HIS n 
1 44  ASN n 
1 45  PHE n 
1 46  ILE n 
1 47  ASN n 
1 48  ASN n 
1 49  SER n 
1 50  ALA n 
1 51  ASP n 
1 52  ASN n 
1 53  SER n 
1 54  THR n 
1 55  GLY n 
1 56  GLU n 
1 57  PHE n 
1 58  ILE n 
1 59  GLY n 
1 60  ASP n 
1 61  LYS n 
1 62  SER n 
1 63  LYS n 
1 64  ASN n 
1 65  THR n 
1 66  TYR n 
1 67  GLU n 
1 68  TRP n 
1 69  GLN n 
1 70  THR n 
1 71  PRO n 
1 72  ASP n 
1 73  GLY n 
1 74  GLN n 
1 75  LYS n 
1 76  GLY n 
1 77  SER n 
1 78  PHE n 
1 79  THR n 
1 80  SER n 
1 81  GLU n 
1 82  ASP n 
1 83  ILE n 
1 84  HIS n 
1 85  PHE n 
1 86  TYR n 
1 87  ASN n 
1 88  LYS n 
1 89  LYS n 
1 90  ASP n 
1 91  TYR n 
1 92  PRO n 
1 93  LYS n 
1 94  GLY n 
1 95  PHE n 
1 96  ILE n 
1 97  TYR n 
1 98  ASP n 
1 99  LEU n 
1 100 ALA n 
1 101 VAL n 
1 102 ILE n 
1 103 THR n 
1 104 LEU n 
1 105 PRO n 
1 106 GLN n 
1 107 SER n 
1 108 THR n 
1 109 ARG n 
1 110 ARG n 
1 111 GLN n 
1 112 HIS n 
1 113 ALA n 
1 114 ASN n 
1 115 LEU n 
1 116 VAL n 
1 117 GLU n 
1 118 ASN n 
1 119 TYR n 
1 120 SER n 
1 121 LYS n 
1 122 VAL n 
1 123 ASN n 
1 124 VAL n 
1 125 ASN n 
1 126 ASP n 
1 127 LYS n 
1 128 LEU n 
1 129 ASN n 
1 130 VAL n 
1 131 TYR n 
1 132 GLY n 
1 133 TYR n 
1 134 PRO n 
1 135 ARG n 
1 136 GLY n 
1 137 GLU n 
1 138 TYR n 
1 139 ALA n 
1 140 HIS n 
1 141 LEU n 
1 142 LYS n 
1 143 ASP n 
1 144 THR n 
1 145 THR n 
1 146 VAL n 
1 147 GLU n 
1 148 ILE n 
1 149 GLU n 
1 150 GLN n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 ASN n 
1 155 ASN n 
1 156 THR n 
1 157 TYR n 
1 158 GLY n 
1 159 VAL n 
1 160 GLN n 
1 161 TYR n 
1 162 GLN n 
1 163 GLY n 
1 164 GLY n 
1 165 LYS n 
1 166 ALA n 
1 167 GLY n 
1 168 MET n 
1 169 SER n 
1 170 GLY n 
1 171 GLY n 
1 172 GLY n 
1 173 ILE n 
1 174 PHE n 
1 175 ASN n 
1 176 SER n 
1 177 LYS n 
1 178 GLY n 
1 179 GLU n 
1 180 VAL n 
1 181 ILE n 
1 182 GLY n 
1 183 LEU n 
1 184 HIS n 
1 185 GLN n 
1 186 ASN n 
1 187 GLY n 
1 188 ALA n 
1 189 GLU n 
1 190 ASN n 
1 191 ARG n 
1 192 SER n 
1 193 GLY n 
1 194 GLY n 
1 195 LEU n 
1 196 ILE n 
1 197 LEU n 
1 198 SER n 
1 199 PRO n 
1 200 THR n 
1 201 GLN n 
1 202 LEU n 
1 203 ASP n 
1 204 TRP n 
1 205 ILE n 
1 206 ARG n 
1 207 SER n 
1 208 ILE n 
1 209 ILE n 
1 210 LYS n 
1 211 GLY n 
1 212 LYS n 
1 213 GLU n 
1 214 ILE n 
1 215 THR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   215 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GEMHA0001_0491 
_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      'Gemella haemolysans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1379 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
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 
# 
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   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   SER 2   -1  -1  SER SER A . n 
A 1 3   ASN 3   684 684 ASN ASN A . n 
A 1 4   ASN 4   685 685 ASN ASN A . n 
A 1 5   VAL 5   686 686 VAL VAL A . n 
A 1 6   PRO 6   687 687 PRO PRO A . n 
A 1 7   LYS 7   688 688 LYS LYS A . n 
A 1 8   ASN 8   689 689 ASN ASN A . n 
A 1 9   ALA 9   690 690 ALA ALA A . n 
A 1 10  SER 10  691 691 SER SER A . n 
A 1 11  ALA 11  692 692 ALA ALA A . n 
A 1 12  LEU 12  693 693 LEU LEU A . n 
A 1 13  LEU 13  694 694 LEU LEU A . n 
A 1 14  ARG 14  695 695 ARG ARG A . n 
A 1 15  MET 15  696 696 MET MET A . n 
A 1 16  ASN 16  697 697 ASN ASN A . n 
A 1 17  PHE 17  698 698 PHE PHE A . n 
A 1 18  VAL 18  699 699 VAL VAL A . n 
A 1 19  LYS 19  700 700 LYS LYS A . n 
A 1 20  GLY 20  701 701 GLY GLY A . n 
A 1 21  ASN 21  702 702 ASN ASN A . n 
A 1 22  GLN 22  703 703 GLN GLN A . n 
A 1 23  VAL 23  704 704 VAL VAL A . n 
A 1 24  LEU 24  705 705 LEU LEU A . n 
A 1 25  SER 25  706 706 SER SER A . n 
A 1 26  GLY 26  707 707 GLY GLY A . n 
A 1 27  THR 27  708 708 THR THR A . n 
A 1 28  GLY 28  709 709 GLY GLY A . n 
A 1 29  SER 29  710 710 SER SER A . n 
A 1 30  ALA 30  711 711 ALA ALA A . n 
A 1 31  THR 31  712 712 THR THR A . n 
A 1 32  PHE 32  713 713 PHE PHE A . n 
A 1 33  ILE 33  714 714 ILE ILE A . n 
A 1 34  ALA 34  715 715 ALA ALA A . n 
A 1 35  PRO 35  716 716 PRO PRO A . n 
A 1 36  ASN 36  717 717 ASN ASN A . n 
A 1 37  VAL 37  718 718 VAL VAL A . n 
A 1 38  LEU 38  719 719 LEU LEU A . n 
A 1 39  LEU 39  720 720 LEU LEU A . n 
A 1 40  THR 40  721 721 THR THR A . n 
A 1 41  VAL 41  722 722 VAL VAL A . n 
A 1 42  ALA 42  723 723 ALA ALA A . n 
A 1 43  HIS 43  724 724 HIS HIS A . n 
A 1 44  ASN 44  725 725 ASN ASN A . n 
A 1 45  PHE 45  726 726 PHE PHE A . n 
A 1 46  ILE 46  727 727 ILE ILE A . n 
A 1 47  ASN 47  728 728 ASN ASN A . n 
A 1 48  ASN 48  729 729 ASN ASN A . n 
A 1 49  SER 49  730 730 SER SER A . n 
A 1 50  ALA 50  731 731 ALA ALA A . n 
A 1 51  ASP 51  732 732 ASP ASP A . n 
A 1 52  ASN 52  733 733 ASN ASN A . n 
A 1 53  SER 53  734 734 SER SER A . n 
A 1 54  THR 54  735 735 THR THR A . n 
A 1 55  GLY 55  736 736 GLY GLY A . n 
A 1 56  GLU 56  737 737 GLU GLU A . n 
A 1 57  PHE 57  738 738 PHE PHE A . n 
A 1 58  ILE 58  739 739 ILE ILE A . n 
A 1 59  GLY 59  740 740 GLY GLY A . n 
A 1 60  ASP 60  741 741 ASP ASP A . n 
A 1 61  LYS 61  742 742 LYS LYS A . n 
A 1 62  SER 62  743 743 SER SER A . n 
A 1 63  LYS 63  744 744 LYS LYS A . n 
A 1 64  ASN 64  745 745 ASN ASN A . n 
A 1 65  THR 65  746 746 THR THR A . n 
A 1 66  TYR 66  747 747 TYR TYR A . n 
A 1 67  GLU 67  748 748 GLU GLU A . n 
A 1 68  TRP 68  749 749 TRP TRP A . n 
A 1 69  GLN 69  750 750 GLN GLN A . n 
A 1 70  THR 70  751 751 THR THR A . n 
A 1 71  PRO 71  752 752 PRO PRO A . n 
A 1 72  ASP 72  753 753 ASP ASP A . n 
A 1 73  GLY 73  754 754 GLY GLY A . n 
A 1 74  GLN 74  755 755 GLN GLN A . n 
A 1 75  LYS 75  756 756 LYS LYS A . n 
A 1 76  GLY 76  757 757 GLY GLY A . n 
A 1 77  SER 77  758 758 SER SER A . n 
A 1 78  PHE 78  759 759 PHE PHE A . n 
A 1 79  THR 79  760 760 THR THR A . n 
A 1 80  SER 80  761 761 SER SER A . n 
A 1 81  GLU 81  762 762 GLU GLU A . n 
A 1 82  ASP 82  763 763 ASP ASP A . n 
A 1 83  ILE 83  764 764 ILE ILE A . n 
A 1 84  HIS 84  765 765 HIS HIS A . n 
A 1 85  PHE 85  766 766 PHE PHE A . n 
A 1 86  TYR 86  767 767 TYR TYR A . n 
A 1 87  ASN 87  768 768 ASN ASN A . n 
A 1 88  LYS 88  769 769 LYS LYS A . n 
A 1 89  LYS 89  770 770 LYS LYS A . n 
A 1 90  ASP 90  771 771 ASP ASP A . n 
A 1 91  TYR 91  772 772 TYR TYR A . n 
A 1 92  PRO 92  773 773 PRO PRO A . n 
A 1 93  LYS 93  774 774 LYS LYS A . n 
A 1 94  GLY 94  775 775 GLY GLY A . n 
A 1 95  PHE 95  776 776 PHE PHE A . n 
A 1 96  ILE 96  777 777 ILE ILE A . n 
A 1 97  TYR 97  778 778 TYR TYR A . n 
A 1 98  ASP 98  779 779 ASP ASP A . n 
A 1 99  LEU 99  780 780 LEU LEU A . n 
A 1 100 ALA 100 781 781 ALA ALA A . n 
A 1 101 VAL 101 782 782 VAL VAL A . n 
A 1 102 ILE 102 783 783 ILE ILE A . n 
A 1 103 THR 103 784 784 THR THR A . n 
A 1 104 LEU 104 785 785 LEU LEU A . n 
A 1 105 PRO 105 786 786 PRO PRO A . n 
A 1 106 GLN 106 787 787 GLN GLN A . n 
A 1 107 SER 107 788 788 SER SER A . n 
A 1 108 THR 108 789 789 THR THR A . n 
A 1 109 ARG 109 790 790 ARG ARG A . n 
A 1 110 ARG 110 791 791 ARG ARG A . n 
A 1 111 GLN 111 792 792 GLN GLN A . n 
A 1 112 HIS 112 793 793 HIS HIS A . n 
A 1 113 ALA 113 794 794 ALA ALA A . n 
A 1 114 ASN 114 795 795 ASN ASN A . n 
A 1 115 LEU 115 796 796 LEU LEU A . n 
A 1 116 VAL 116 797 797 VAL VAL A . n 
A 1 117 GLU 117 798 798 GLU GLU A . n 
A 1 118 ASN 118 799 799 ASN ASN A . n 
A 1 119 TYR 119 800 800 TYR TYR A . n 
A 1 120 SER 120 801 801 SER SER A . n 
A 1 121 LYS 121 802 802 LYS LYS A . n 
A 1 122 VAL 122 803 803 VAL VAL A . n 
A 1 123 ASN 123 804 804 ASN ASN A . n 
A 1 124 VAL 124 805 805 VAL VAL A . n 
A 1 125 ASN 125 806 806 ASN ASN A . n 
A 1 126 ASP 126 807 807 ASP ASP A . n 
A 1 127 LYS 127 808 808 LYS LYS A . n 
A 1 128 LEU 128 809 809 LEU LEU A . n 
A 1 129 ASN 129 810 810 ASN ASN A . n 
A 1 130 VAL 130 811 811 VAL VAL A . n 
A 1 131 TYR 131 812 812 TYR TYR A . n 
A 1 132 GLY 132 813 813 GLY GLY A . n 
A 1 133 TYR 133 814 814 TYR TYR A . n 
A 1 134 PRO 134 815 815 PRO PRO A . n 
A 1 135 ARG 135 816 816 ARG ARG A . n 
A 1 136 GLY 136 817 817 GLY GLY A . n 
A 1 137 GLU 137 818 818 GLU GLU A . n 
A 1 138 TYR 138 819 819 TYR TYR A . n 
A 1 139 ALA 139 820 820 ALA ALA A . n 
A 1 140 HIS 140 821 821 HIS HIS A . n 
A 1 141 LEU 141 822 822 LEU LEU A . n 
A 1 142 LYS 142 823 823 LYS LYS A . n 
A 1 143 ASP 143 824 824 ASP ASP A . n 
A 1 144 THR 144 825 825 THR THR A . n 
A 1 145 THR 145 826 826 THR THR A . n 
A 1 146 VAL 146 827 827 VAL VAL A . n 
A 1 147 GLU 147 828 828 GLU GLU A . n 
A 1 148 ILE 148 829 829 ILE ILE A . n 
A 1 149 GLU 149 830 830 GLU GLU A . n 
A 1 150 GLN 150 831 831 GLN GLN A . n 
A 1 151 LYS 151 832 832 LYS LYS A . n 
A 1 152 TYR 152 833 833 TYR TYR A . n 
A 1 153 ALA 153 834 834 ALA ALA A . n 
A 1 154 ASN 154 835 835 ASN ASN A . n 
A 1 155 ASN 155 836 836 ASN ASN A . n 
A 1 156 THR 156 837 837 THR THR A . n 
A 1 157 TYR 157 838 838 TYR TYR A . n 
A 1 158 GLY 158 839 839 GLY GLY A . n 
A 1 159 VAL 159 840 840 VAL VAL A . n 
A 1 160 GLN 160 841 841 GLN GLN A . n 
A 1 161 TYR 161 842 842 TYR TYR A . n 
A 1 162 GLN 162 843 843 GLN GLN A . n 
A 1 163 GLY 163 844 844 GLY GLY A . n 
A 1 164 GLY 164 845 845 GLY GLY A . n 
A 1 165 LYS 165 846 846 LYS LYS A . n 
A 1 166 ALA 166 847 847 ALA ALA A . n 
A 1 167 GLY 167 848 848 GLY GLY A . n 
A 1 168 MET 168 849 849 MET MET A . n 
A 1 169 SER 169 850 850 SER SER A . n 
A 1 170 GLY 170 851 851 GLY GLY A . n 
A 1 171 GLY 171 852 852 GLY GLY A . n 
A 1 172 GLY 172 853 853 GLY GLY A . n 
A 1 173 ILE 173 854 854 ILE ILE A . n 
A 1 174 PHE 174 855 855 PHE PHE A . n 
A 1 175 ASN 175 856 856 ASN ASN A . n 
A 1 176 SER 176 857 857 SER SER A . n 
A 1 177 LYS 177 858 858 LYS LYS A . n 
A 1 178 GLY 178 859 859 GLY GLY A . n 
A 1 179 GLU 179 860 860 GLU GLU A . n 
A 1 180 VAL 180 861 861 VAL VAL A . n 
A 1 181 ILE 181 862 862 ILE ILE A . n 
A 1 182 GLY 182 863 863 GLY GLY A . n 
A 1 183 LEU 183 864 864 LEU LEU A . n 
A 1 184 HIS 184 865 865 HIS HIS A . n 
A 1 185 GLN 185 866 866 GLN GLN A . n 
A 1 186 ASN 186 867 867 ASN ASN A . n 
A 1 187 GLY 187 868 868 GLY GLY A . n 
A 1 188 ALA 188 869 869 ALA ALA A . n 
A 1 189 GLU 189 870 870 GLU GLU A . n 
A 1 190 ASN 190 871 871 ASN ASN A . n 
A 1 191 ARG 191 872 872 ARG ARG A . n 
A 1 192 SER 192 873 873 SER SER A . n 
A 1 193 GLY 193 874 874 GLY GLY A . n 
A 1 194 GLY 194 875 875 GLY GLY A . n 
A 1 195 LEU 195 876 876 LEU LEU A . n 
A 1 196 ILE 196 877 877 ILE ILE A . n 
A 1 197 LEU 197 878 878 LEU LEU A . n 
A 1 198 SER 198 879 879 SER SER A . n 
A 1 199 PRO 199 880 880 PRO PRO A . n 
A 1 200 THR 200 881 881 THR THR A . n 
A 1 201 GLN 201 882 882 GLN GLN A . n 
A 1 202 LEU 202 883 883 LEU LEU A . n 
A 1 203 ASP 203 884 884 ASP ASP A . n 
A 1 204 TRP 204 885 885 TRP TRP A . n 
A 1 205 ILE 205 886 886 ILE ILE A . n 
A 1 206 ARG 206 887 887 ARG ARG A . n 
A 1 207 SER 207 888 888 SER SER A . n 
A 1 208 ILE 208 889 889 ILE ILE A . n 
A 1 209 ILE 209 890 890 ILE ILE A . n 
A 1 210 LYS 210 891 891 LYS LYS A . n 
A 1 211 GLY 211 892 892 GLY GLY A . n 
A 1 212 LYS 212 893 893 LYS LYS A . n 
A 1 213 GLU 213 894 ?   ?   ?   A . n 
A 1 214 ILE 214 895 ?   ?   ?   A . n 
A 1 215 THR 215 896 ?   ?   ?   A . n 
B 1 1   GLY 1   -2  ?   ?   ?   B . n 
B 1 2   SER 2   -1  -1  SER SER B . n 
B 1 3   ASN 3   684 684 ASN ASN B . n 
B 1 4   ASN 4   685 685 ASN ASN B . n 
B 1 5   VAL 5   686 686 VAL VAL B . n 
B 1 6   PRO 6   687 687 PRO PRO B . n 
B 1 7   LYS 7   688 688 LYS LYS B . n 
B 1 8   ASN 8   689 689 ASN ASN B . n 
B 1 9   ALA 9   690 690 ALA ALA B . n 
B 1 10  SER 10  691 691 SER SER B . n 
B 1 11  ALA 11  692 692 ALA ALA B . n 
B 1 12  LEU 12  693 693 LEU LEU B . n 
B 1 13  LEU 13  694 694 LEU LEU B . n 
B 1 14  ARG 14  695 695 ARG ARG B . n 
B 1 15  MET 15  696 696 MET MET B . n 
B 1 16  ASN 16  697 697 ASN ASN B . n 
B 1 17  PHE 17  698 698 PHE PHE B . n 
B 1 18  VAL 18  699 699 VAL VAL B . n 
B 1 19  LYS 19  700 700 LYS LYS B . n 
B 1 20  GLY 20  701 701 GLY GLY B . n 
B 1 21  ASN 21  702 702 ASN ASN B . n 
B 1 22  GLN 22  703 703 GLN GLN B . n 
B 1 23  VAL 23  704 704 VAL VAL B . n 
B 1 24  LEU 24  705 705 LEU LEU B . n 
B 1 25  SER 25  706 706 SER SER B . n 
B 1 26  GLY 26  707 707 GLY GLY B . n 
B 1 27  THR 27  708 708 THR THR B . n 
B 1 28  GLY 28  709 709 GLY GLY B . n 
B 1 29  SER 29  710 710 SER SER B . n 
B 1 30  ALA 30  711 711 ALA ALA B . n 
B 1 31  THR 31  712 712 THR THR B . n 
B 1 32  PHE 32  713 713 PHE PHE B . n 
B 1 33  ILE 33  714 714 ILE ILE B . n 
B 1 34  ALA 34  715 715 ALA ALA B . n 
B 1 35  PRO 35  716 716 PRO PRO B . n 
B 1 36  ASN 36  717 717 ASN ASN B . n 
B 1 37  VAL 37  718 718 VAL VAL B . n 
B 1 38  LEU 38  719 719 LEU LEU B . n 
B 1 39  LEU 39  720 720 LEU LEU B . n 
B 1 40  THR 40  721 721 THR THR B . n 
B 1 41  VAL 41  722 722 VAL VAL B . n 
B 1 42  ALA 42  723 723 ALA ALA B . n 
B 1 43  HIS 43  724 724 HIS HIS B . n 
B 1 44  ASN 44  725 725 ASN ASN B . n 
B 1 45  PHE 45  726 726 PHE PHE B . n 
B 1 46  ILE 46  727 727 ILE ILE B . n 
B 1 47  ASN 47  728 728 ASN ASN B . n 
B 1 48  ASN 48  729 729 ASN ASN B . n 
B 1 49  SER 49  730 730 SER SER B . n 
B 1 50  ALA 50  731 731 ALA ALA B . n 
B 1 51  ASP 51  732 732 ASP ASP B . n 
B 1 52  ASN 52  733 733 ASN ASN B . n 
B 1 53  SER 53  734 734 SER SER B . n 
B 1 54  THR 54  735 735 THR THR B . n 
B 1 55  GLY 55  736 736 GLY GLY B . n 
B 1 56  GLU 56  737 737 GLU GLU B . n 
B 1 57  PHE 57  738 738 PHE PHE B . n 
B 1 58  ILE 58  739 739 ILE ILE B . n 
B 1 59  GLY 59  740 740 GLY GLY B . n 
B 1 60  ASP 60  741 741 ASP ASP B . n 
B 1 61  LYS 61  742 742 LYS LYS B . n 
B 1 62  SER 62  743 743 SER SER B . n 
B 1 63  LYS 63  744 744 LYS LYS B . n 
B 1 64  ASN 64  745 745 ASN ASN B . n 
B 1 65  THR 65  746 746 THR THR B . n 
B 1 66  TYR 66  747 747 TYR TYR B . n 
B 1 67  GLU 67  748 748 GLU GLU B . n 
B 1 68  TRP 68  749 749 TRP TRP B . n 
B 1 69  GLN 69  750 750 GLN GLN B . n 
B 1 70  THR 70  751 751 THR THR B . n 
B 1 71  PRO 71  752 752 PRO PRO B . n 
B 1 72  ASP 72  753 753 ASP ASP B . n 
B 1 73  GLY 73  754 754 GLY GLY B . n 
B 1 74  GLN 74  755 755 GLN GLN B . n 
B 1 75  LYS 75  756 756 LYS LYS B . n 
B 1 76  GLY 76  757 757 GLY GLY B . n 
B 1 77  SER 77  758 758 SER SER B . n 
B 1 78  PHE 78  759 759 PHE PHE B . n 
B 1 79  THR 79  760 760 THR THR B . n 
B 1 80  SER 80  761 761 SER SER B . n 
B 1 81  GLU 81  762 762 GLU GLU B . n 
B 1 82  ASP 82  763 763 ASP ASP B . n 
B 1 83  ILE 83  764 764 ILE ILE B . n 
B 1 84  HIS 84  765 765 HIS HIS B . n 
B 1 85  PHE 85  766 766 PHE PHE B . n 
B 1 86  TYR 86  767 767 TYR TYR B . n 
B 1 87  ASN 87  768 768 ASN ASN B . n 
B 1 88  LYS 88  769 769 LYS LYS B . n 
B 1 89  LYS 89  770 770 LYS LYS B . n 
B 1 90  ASP 90  771 771 ASP ASP B . n 
B 1 91  TYR 91  772 772 TYR TYR B . n 
B 1 92  PRO 92  773 773 PRO PRO B . n 
B 1 93  LYS 93  774 774 LYS LYS B . n 
B 1 94  GLY 94  775 775 GLY GLY B . n 
B 1 95  PHE 95  776 776 PHE PHE B . n 
B 1 96  ILE 96  777 777 ILE ILE B . n 
B 1 97  TYR 97  778 778 TYR TYR B . n 
B 1 98  ASP 98  779 779 ASP ASP B . n 
B 1 99  LEU 99  780 780 LEU LEU B . n 
B 1 100 ALA 100 781 781 ALA ALA B . n 
B 1 101 VAL 101 782 782 VAL VAL B . n 
B 1 102 ILE 102 783 783 ILE ILE B . n 
B 1 103 THR 103 784 784 THR THR B . n 
B 1 104 LEU 104 785 785 LEU LEU B . n 
B 1 105 PRO 105 786 786 PRO PRO B . n 
B 1 106 GLN 106 787 787 GLN GLN B . n 
B 1 107 SER 107 788 788 SER SER B . n 
B 1 108 THR 108 789 789 THR THR B . n 
B 1 109 ARG 109 790 790 ARG ARG B . n 
B 1 110 ARG 110 791 791 ARG ARG B . n 
B 1 111 GLN 111 792 792 GLN GLN B . n 
B 1 112 HIS 112 793 793 HIS HIS B . n 
B 1 113 ALA 113 794 794 ALA ALA B . n 
B 1 114 ASN 114 795 795 ASN ASN B . n 
B 1 115 LEU 115 796 796 LEU LEU B . n 
B 1 116 VAL 116 797 797 VAL VAL B . n 
B 1 117 GLU 117 798 798 GLU GLU B . n 
B 1 118 ASN 118 799 799 ASN ASN B . n 
B 1 119 TYR 119 800 800 TYR TYR B . n 
B 1 120 SER 120 801 801 SER SER B . n 
B 1 121 LYS 121 802 802 LYS LYS B . n 
B 1 122 VAL 122 803 803 VAL VAL B . n 
B 1 123 ASN 123 804 804 ASN ASN B . n 
B 1 124 VAL 124 805 805 VAL VAL B . n 
B 1 125 ASN 125 806 806 ASN ASN B . n 
B 1 126 ASP 126 807 807 ASP ASP B . n 
B 1 127 LYS 127 808 808 LYS LYS B . n 
B 1 128 LEU 128 809 809 LEU LEU B . n 
B 1 129 ASN 129 810 810 ASN ASN B . n 
B 1 130 VAL 130 811 811 VAL VAL B . n 
B 1 131 TYR 131 812 812 TYR TYR B . n 
B 1 132 GLY 132 813 813 GLY GLY B . n 
B 1 133 TYR 133 814 814 TYR TYR B . n 
B 1 134 PRO 134 815 815 PRO PRO B . n 
B 1 135 ARG 135 816 816 ARG ARG B . n 
B 1 136 GLY 136 817 817 GLY GLY B . n 
B 1 137 GLU 137 818 818 GLU GLU B . n 
B 1 138 TYR 138 819 819 TYR TYR B . n 
B 1 139 ALA 139 820 820 ALA ALA B . n 
B 1 140 HIS 140 821 821 HIS HIS B . n 
B 1 141 LEU 141 822 822 LEU LEU B . n 
B 1 142 LYS 142 823 823 LYS LYS B . n 
B 1 143 ASP 143 824 824 ASP ASP B . n 
B 1 144 THR 144 825 825 THR THR B . n 
B 1 145 THR 145 826 826 THR THR B . n 
B 1 146 VAL 146 827 827 VAL VAL B . n 
B 1 147 GLU 147 828 828 GLU GLU B . n 
B 1 148 ILE 148 829 829 ILE ILE B . n 
B 1 149 GLU 149 830 830 GLU GLU B . n 
B 1 150 GLN 150 831 831 GLN GLN B . n 
B 1 151 LYS 151 832 832 LYS LYS B . n 
B 1 152 TYR 152 833 833 TYR TYR B . n 
B 1 153 ALA 153 834 834 ALA ALA B . n 
B 1 154 ASN 154 835 835 ASN ASN B . n 
B 1 155 ASN 155 836 836 ASN ASN B . n 
B 1 156 THR 156 837 837 THR THR B . n 
B 1 157 TYR 157 838 838 TYR TYR B . n 
B 1 158 GLY 158 839 839 GLY GLY B . n 
B 1 159 VAL 159 840 840 VAL VAL B . n 
B 1 160 GLN 160 841 841 GLN GLN B . n 
B 1 161 TYR 161 842 842 TYR TYR B . n 
B 1 162 GLN 162 843 843 GLN GLN B . n 
B 1 163 GLY 163 844 844 GLY GLY B . n 
B 1 164 GLY 164 845 845 GLY GLY B . n 
B 1 165 LYS 165 846 846 LYS LYS B . n 
B 1 166 ALA 166 847 847 ALA ALA B . n 
B 1 167 GLY 167 848 848 GLY GLY B . n 
B 1 168 MET 168 849 849 MET MET B . n 
B 1 169 SER 169 850 850 SER SER B . n 
B 1 170 GLY 170 851 851 GLY GLY B . n 
B 1 171 GLY 171 852 852 GLY GLY B . n 
B 1 172 GLY 172 853 853 GLY GLY B . n 
B 1 173 ILE 173 854 854 ILE ILE B . n 
B 1 174 PHE 174 855 855 PHE PHE B . n 
B 1 175 ASN 175 856 856 ASN ASN B . n 
B 1 176 SER 176 857 857 SER SER B . n 
B 1 177 LYS 177 858 858 LYS LYS B . n 
B 1 178 GLY 178 859 859 GLY GLY B . n 
B 1 179 GLU 179 860 860 GLU GLU B . n 
B 1 180 VAL 180 861 861 VAL VAL B . n 
B 1 181 ILE 181 862 862 ILE ILE B . n 
B 1 182 GLY 182 863 863 GLY GLY B . n 
B 1 183 LEU 183 864 864 LEU LEU B . n 
B 1 184 HIS 184 865 865 HIS HIS B . n 
B 1 185 GLN 185 866 866 GLN GLN B . n 
B 1 186 ASN 186 867 867 ASN ASN B . n 
B 1 187 GLY 187 868 868 GLY GLY B . n 
B 1 188 ALA 188 869 869 ALA ALA B . n 
B 1 189 GLU 189 870 870 GLU GLU B . n 
B 1 190 ASN 190 871 871 ASN ASN B . n 
B 1 191 ARG 191 872 872 ARG ARG B . n 
B 1 192 SER 192 873 873 SER SER B . n 
B 1 193 GLY 193 874 874 GLY GLY B . n 
B 1 194 GLY 194 875 875 GLY GLY B . n 
B 1 195 LEU 195 876 876 LEU LEU B . n 
B 1 196 ILE 196 877 877 ILE ILE B . n 
B 1 197 LEU 197 878 878 LEU LEU B . n 
B 1 198 SER 198 879 879 SER SER B . n 
B 1 199 PRO 199 880 880 PRO PRO B . n 
B 1 200 THR 200 881 881 THR THR B . n 
B 1 201 GLN 201 882 882 GLN GLN B . n 
B 1 202 LEU 202 883 883 LEU LEU B . n 
B 1 203 ASP 203 884 884 ASP ASP B . n 
B 1 204 TRP 204 885 885 TRP TRP B . n 
B 1 205 ILE 205 886 886 ILE ILE B . n 
B 1 206 ARG 206 887 887 ARG ARG B . n 
B 1 207 SER 207 888 888 SER SER B . n 
B 1 208 ILE 208 889 889 ILE ILE B . n 
B 1 209 ILE 209 890 890 ILE ILE B . n 
B 1 210 LYS 210 891 891 LYS LYS B . n 
B 1 211 GLY 211 892 892 GLY GLY B . n 
B 1 212 LYS 212 893 ?   ?   ?   B . n 
B 1 213 GLU 213 894 ?   ?   ?   B . n 
B 1 214 ILE 214 895 ?   ?   ?   B . n 
B 1 215 THR 215 896 ?   ?   ?   B . 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 
C 2 HOH 1   901  308 HOH HOH A . 
C 2 HOH 2   902  481 HOH HOH A . 
C 2 HOH 3   903  534 HOH HOH A . 
C 2 HOH 4   904  97  HOH HOH A . 
C 2 HOH 5   905  312 HOH HOH A . 
C 2 HOH 6   906  93  HOH HOH A . 
C 2 HOH 7   907  537 HOH HOH A . 
C 2 HOH 8   908  182 HOH HOH A . 
C 2 HOH 9   909  157 HOH HOH A . 
C 2 HOH 10  910  332 HOH HOH A . 
C 2 HOH 11  911  488 HOH HOH A . 
C 2 HOH 12  912  535 HOH HOH A . 
C 2 HOH 13  913  256 HOH HOH A . 
C 2 HOH 14  914  254 HOH HOH A . 
C 2 HOH 15  915  530 HOH HOH A . 
C 2 HOH 16  916  219 HOH HOH A . 
C 2 HOH 17  917  274 HOH HOH A . 
C 2 HOH 18  918  484 HOH HOH A . 
C 2 HOH 19  919  507 HOH HOH A . 
C 2 HOH 20  920  150 HOH HOH A . 
C 2 HOH 21  921  405 HOH HOH A . 
C 2 HOH 22  922  69  HOH HOH A . 
C 2 HOH 23  923  396 HOH HOH A . 
C 2 HOH 24  924  394 HOH HOH A . 
C 2 HOH 25  925  9   HOH HOH A . 
C 2 HOH 26  926  170 HOH HOH A . 
C 2 HOH 27  927  252 HOH HOH A . 
C 2 HOH 28  928  66  HOH HOH A . 
C 2 HOH 29  929  59  HOH HOH A . 
C 2 HOH 30  930  139 HOH HOH A . 
C 2 HOH 31  931  390 HOH HOH A . 
C 2 HOH 32  932  322 HOH HOH A . 
C 2 HOH 33  933  366 HOH HOH A . 
C 2 HOH 34  934  269 HOH HOH A . 
C 2 HOH 35  935  341 HOH HOH A . 
C 2 HOH 36  936  104 HOH HOH A . 
C 2 HOH 37  937  494 HOH HOH A . 
C 2 HOH 38  938  85  HOH HOH A . 
C 2 HOH 39  939  83  HOH HOH A . 
C 2 HOH 40  940  270 HOH HOH A . 
C 2 HOH 41  941  175 HOH HOH A . 
C 2 HOH 42  942  297 HOH HOH A . 
C 2 HOH 43  943  17  HOH HOH A . 
C 2 HOH 44  944  10  HOH HOH A . 
C 2 HOH 45  945  8   HOH HOH A . 
C 2 HOH 46  946  55  HOH HOH A . 
C 2 HOH 47  947  106 HOH HOH A . 
C 2 HOH 48  948  387 HOH HOH A . 
C 2 HOH 49  949  321 HOH HOH A . 
C 2 HOH 50  950  310 HOH HOH A . 
C 2 HOH 51  951  419 HOH HOH A . 
C 2 HOH 52  952  369 HOH HOH A . 
C 2 HOH 53  953  467 HOH HOH A . 
C 2 HOH 54  954  202 HOH HOH A . 
C 2 HOH 55  955  7   HOH HOH A . 
C 2 HOH 56  956  21  HOH HOH A . 
C 2 HOH 57  957  12  HOH HOH A . 
C 2 HOH 58  958  32  HOH HOH A . 
C 2 HOH 59  959  119 HOH HOH A . 
C 2 HOH 60  960  63  HOH HOH A . 
C 2 HOH 61  961  194 HOH HOH A . 
C 2 HOH 62  962  233 HOH HOH A . 
C 2 HOH 63  963  377 HOH HOH A . 
C 2 HOH 64  964  1   HOH HOH A . 
C 2 HOH 65  965  424 HOH HOH A . 
C 2 HOH 66  966  103 HOH HOH A . 
C 2 HOH 67  967  142 HOH HOH A . 
C 2 HOH 68  968  180 HOH HOH A . 
C 2 HOH 69  969  58  HOH HOH A . 
C 2 HOH 70  970  522 HOH HOH A . 
C 2 HOH 71  971  460 HOH HOH A . 
C 2 HOH 72  972  538 HOH HOH A . 
C 2 HOH 73  973  198 HOH HOH A . 
C 2 HOH 74  974  371 HOH HOH A . 
C 2 HOH 75  975  151 HOH HOH A . 
C 2 HOH 76  976  343 HOH HOH A . 
C 2 HOH 77  977  192 HOH HOH A . 
C 2 HOH 78  978  23  HOH HOH A . 
C 2 HOH 79  979  169 HOH HOH A . 
C 2 HOH 80  980  22  HOH HOH A . 
C 2 HOH 81  981  145 HOH HOH A . 
C 2 HOH 82  982  16  HOH HOH A . 
C 2 HOH 83  983  65  HOH HOH A . 
C 2 HOH 84  984  473 HOH HOH A . 
C 2 HOH 85  985  368 HOH HOH A . 
C 2 HOH 86  986  51  HOH HOH A . 
C 2 HOH 87  987  236 HOH HOH A . 
C 2 HOH 88  988  80  HOH HOH A . 
C 2 HOH 89  989  70  HOH HOH A . 
C 2 HOH 90  990  136 HOH HOH A . 
C 2 HOH 91  991  101 HOH HOH A . 
C 2 HOH 92  992  91  HOH HOH A . 
C 2 HOH 93  993  13  HOH HOH A . 
C 2 HOH 94  994  475 HOH HOH A . 
C 2 HOH 95  995  61  HOH HOH A . 
C 2 HOH 96  996  27  HOH HOH A . 
C 2 HOH 97  997  172 HOH HOH A . 
C 2 HOH 98  998  114 HOH HOH A . 
C 2 HOH 99  999  352 HOH HOH A . 
C 2 HOH 100 1000 318 HOH HOH A . 
C 2 HOH 101 1001 20  HOH HOH A . 
C 2 HOH 102 1002 258 HOH HOH A . 
C 2 HOH 103 1003 92  HOH HOH A . 
C 2 HOH 104 1004 420 HOH HOH A . 
C 2 HOH 105 1005 54  HOH HOH A . 
C 2 HOH 106 1006 290 HOH HOH A . 
C 2 HOH 107 1007 30  HOH HOH A . 
C 2 HOH 108 1008 230 HOH HOH A . 
C 2 HOH 109 1009 210 HOH HOH A . 
C 2 HOH 110 1010 168 HOH HOH A . 
C 2 HOH 111 1011 411 HOH HOH A . 
C 2 HOH 112 1012 2   HOH HOH A . 
C 2 HOH 113 1013 186 HOH HOH A . 
C 2 HOH 114 1014 231 HOH HOH A . 
C 2 HOH 115 1015 190 HOH HOH A . 
C 2 HOH 116 1016 342 HOH HOH A . 
C 2 HOH 117 1017 208 HOH HOH A . 
C 2 HOH 118 1018 29  HOH HOH A . 
C 2 HOH 119 1019 421 HOH HOH A . 
C 2 HOH 120 1020 11  HOH HOH A . 
C 2 HOH 121 1021 105 HOH HOH A . 
C 2 HOH 122 1022 278 HOH HOH A . 
C 2 HOH 123 1023 5   HOH HOH A . 
C 2 HOH 124 1024 129 HOH HOH A . 
C 2 HOH 125 1025 4   HOH HOH A . 
C 2 HOH 126 1026 26  HOH HOH A . 
C 2 HOH 127 1027 545 HOH HOH A . 
C 2 HOH 128 1028 43  HOH HOH A . 
C 2 HOH 129 1029 28  HOH HOH A . 
C 2 HOH 130 1030 88  HOH HOH A . 
C 2 HOH 131 1031 167 HOH HOH A . 
C 2 HOH 132 1032 353 HOH HOH A . 
C 2 HOH 133 1033 71  HOH HOH A . 
C 2 HOH 134 1034 476 HOH HOH A . 
C 2 HOH 135 1035 472 HOH HOH A . 
C 2 HOH 136 1036 527 HOH HOH A . 
C 2 HOH 137 1037 457 HOH HOH A . 
C 2 HOH 138 1038 260 HOH HOH A . 
C 2 HOH 139 1039 46  HOH HOH A . 
C 2 HOH 140 1040 131 HOH HOH A . 
C 2 HOH 141 1041 330 HOH HOH A . 
C 2 HOH 142 1042 127 HOH HOH A . 
C 2 HOH 143 1043 44  HOH HOH A . 
C 2 HOH 144 1044 456 HOH HOH A . 
C 2 HOH 145 1045 378 HOH HOH A . 
C 2 HOH 146 1046 511 HOH HOH A . 
C 2 HOH 147 1047 38  HOH HOH A . 
C 2 HOH 148 1048 338 HOH HOH A . 
C 2 HOH 149 1049 179 HOH HOH A . 
C 2 HOH 150 1050 149 HOH HOH A . 
C 2 HOH 151 1051 42  HOH HOH A . 
C 2 HOH 152 1052 440 HOH HOH A . 
C 2 HOH 153 1053 84  HOH HOH A . 
C 2 HOH 154 1054 509 HOH HOH A . 
C 2 HOH 155 1055 362 HOH HOH A . 
C 2 HOH 156 1056 163 HOH HOH A . 
C 2 HOH 157 1057 24  HOH HOH A . 
C 2 HOH 158 1058 388 HOH HOH A . 
C 2 HOH 159 1059 316 HOH HOH A . 
C 2 HOH 160 1060 280 HOH HOH A . 
C 2 HOH 161 1061 166 HOH HOH A . 
C 2 HOH 162 1062 400 HOH HOH A . 
C 2 HOH 163 1063 120 HOH HOH A . 
C 2 HOH 164 1064 512 HOH HOH A . 
C 2 HOH 165 1065 261 HOH HOH A . 
C 2 HOH 166 1066 148 HOH HOH A . 
C 2 HOH 167 1067 409 HOH HOH A . 
C 2 HOH 168 1068 370 HOH HOH A . 
C 2 HOH 169 1069 373 HOH HOH A . 
C 2 HOH 170 1070 448 HOH HOH A . 
C 2 HOH 171 1071 324 HOH HOH A . 
C 2 HOH 172 1072 264 HOH HOH A . 
C 2 HOH 173 1073 532 HOH HOH A . 
C 2 HOH 174 1074 285 HOH HOH A . 
C 2 HOH 175 1075 314 HOH HOH A . 
C 2 HOH 176 1076 25  HOH HOH A . 
C 2 HOH 177 1077 277 HOH HOH A . 
C 2 HOH 178 1078 479 HOH HOH A . 
C 2 HOH 179 1079 49  HOH HOH A . 
C 2 HOH 180 1080 41  HOH HOH A . 
C 2 HOH 181 1081 158 HOH HOH A . 
C 2 HOH 182 1082 526 HOH HOH A . 
C 2 HOH 183 1083 502 HOH HOH A . 
C 2 HOH 184 1084 359 HOH HOH A . 
C 2 HOH 185 1085 19  HOH HOH A . 
C 2 HOH 186 1086 212 HOH HOH A . 
C 2 HOH 187 1087 313 HOH HOH A . 
C 2 HOH 188 1088 89  HOH HOH A . 
C 2 HOH 189 1089 302 HOH HOH A . 
C 2 HOH 190 1090 189 HOH HOH A . 
C 2 HOH 191 1091 519 HOH HOH A . 
C 2 HOH 192 1092 262 HOH HOH A . 
C 2 HOH 193 1093 45  HOH HOH A . 
C 2 HOH 194 1094 211 HOH HOH A . 
C 2 HOH 195 1095 52  HOH HOH A . 
C 2 HOH 196 1096 392 HOH HOH A . 
C 2 HOH 197 1097 36  HOH HOH A . 
C 2 HOH 198 1098 72  HOH HOH A . 
C 2 HOH 199 1099 422 HOH HOH A . 
C 2 HOH 200 1100 454 HOH HOH A . 
C 2 HOH 201 1101 199 HOH HOH A . 
C 2 HOH 202 1102 445 HOH HOH A . 
C 2 HOH 203 1103 374 HOH HOH A . 
C 2 HOH 204 1104 218 HOH HOH A . 
C 2 HOH 205 1105 468 HOH HOH A . 
C 2 HOH 206 1106 94  HOH HOH A . 
C 2 HOH 207 1107 315 HOH HOH A . 
C 2 HOH 208 1108 415 HOH HOH A . 
C 2 HOH 209 1109 358 HOH HOH A . 
C 2 HOH 210 1110 265 HOH HOH A . 
C 2 HOH 211 1111 399 HOH HOH A . 
C 2 HOH 212 1112 496 HOH HOH A . 
C 2 HOH 213 1113 161 HOH HOH A . 
C 2 HOH 214 1114 156 HOH HOH A . 
C 2 HOH 215 1115 174 HOH HOH A . 
C 2 HOH 216 1116 319 HOH HOH A . 
C 2 HOH 217 1117 250 HOH HOH A . 
C 2 HOH 218 1118 435 HOH HOH A . 
C 2 HOH 219 1119 224 HOH HOH A . 
C 2 HOH 220 1120 410 HOH HOH A . 
C 2 HOH 221 1121 436 HOH HOH A . 
C 2 HOH 222 1122 528 HOH HOH A . 
C 2 HOH 223 1123 529 HOH HOH A . 
C 2 HOH 224 1124 223 HOH HOH A . 
C 2 HOH 225 1125 279 HOH HOH A . 
C 2 HOH 226 1126 541 HOH HOH A . 
C 2 HOH 227 1127 428 HOH HOH A . 
C 2 HOH 228 1128 112 HOH HOH A . 
C 2 HOH 229 1129 206 HOH HOH A . 
C 2 HOH 230 1130 326 HOH HOH A . 
C 2 HOH 231 1131 193 HOH HOH A . 
C 2 HOH 232 1132 281 HOH HOH A . 
C 2 HOH 233 1133 438 HOH HOH A . 
C 2 HOH 234 1134 367 HOH HOH A . 
C 2 HOH 235 1135 56  HOH HOH A . 
C 2 HOH 236 1136 495 HOH HOH A . 
C 2 HOH 237 1137 271 HOH HOH A . 
C 2 HOH 238 1138 395 HOH HOH A . 
C 2 HOH 239 1139 286 HOH HOH A . 
C 2 HOH 240 1140 244 HOH HOH A . 
C 2 HOH 241 1141 347 HOH HOH A . 
C 2 HOH 242 1142 452 HOH HOH A . 
C 2 HOH 243 1143 37  HOH HOH A . 
C 2 HOH 244 1144 205 HOH HOH A . 
C 2 HOH 245 1145 431 HOH HOH A . 
C 2 HOH 246 1146 491 HOH HOH A . 
C 2 HOH 247 1147 521 HOH HOH A . 
C 2 HOH 248 1148 107 HOH HOH A . 
C 2 HOH 249 1149 510 HOH HOH A . 
C 2 HOH 250 1150 385 HOH HOH A . 
C 2 HOH 251 1151 266 HOH HOH A . 
C 2 HOH 252 1152 427 HOH HOH A . 
C 2 HOH 253 1153 335 HOH HOH A . 
C 2 HOH 254 1154 407 HOH HOH A . 
C 2 HOH 255 1155 331 HOH HOH A . 
C 2 HOH 256 1156 77  HOH HOH A . 
C 2 HOH 257 1157 499 HOH HOH A . 
C 2 HOH 258 1158 540 HOH HOH A . 
C 2 HOH 259 1159 506 HOH HOH A . 
C 2 HOH 260 1160 447 HOH HOH A . 
C 2 HOH 261 1161 360 HOH HOH A . 
C 2 HOH 262 1162 296 HOH HOH A . 
C 2 HOH 263 1163 113 HOH HOH A . 
C 2 HOH 264 1164 185 HOH HOH A . 
C 2 HOH 265 1165 490 HOH HOH A . 
C 2 HOH 266 1166 451 HOH HOH A . 
C 2 HOH 267 1167 372 HOH HOH A . 
C 2 HOH 268 1168 474 HOH HOH A . 
C 2 HOH 269 1169 187 HOH HOH A . 
C 2 HOH 270 1170 386 HOH HOH A . 
C 2 HOH 271 1171 402 HOH HOH A . 
C 2 HOH 272 1172 462 HOH HOH A . 
C 2 HOH 273 1173 489 HOH HOH A . 
C 2 HOH 274 1174 383 HOH HOH A . 
C 2 HOH 275 1175 482 HOH HOH A . 
C 2 HOH 276 1176 429 HOH HOH A . 
C 2 HOH 277 1177 284 HOH HOH A . 
C 2 HOH 278 1178 263 HOH HOH A . 
C 2 HOH 279 1179 403 HOH HOH A . 
C 2 HOH 280 1180 249 HOH HOH A . 
C 2 HOH 281 1181 384 HOH HOH A . 
C 2 HOH 282 1182 336 HOH HOH A . 
C 2 HOH 283 1183 349 HOH HOH A . 
C 2 HOH 284 1184 251 HOH HOH A . 
C 2 HOH 285 1185 376 HOH HOH A . 
C 2 HOH 286 1186 351 HOH HOH A . 
C 2 HOH 287 1187 380 HOH HOH A . 
C 2 HOH 288 1188 126 HOH HOH A . 
C 2 HOH 289 1189 486 HOH HOH A . 
C 2 HOH 290 1190 276 HOH HOH A . 
D 2 HOH 1   901  67  HOH HOH B . 
D 2 HOH 2   902  248 HOH HOH B . 
D 2 HOH 3   903  122 HOH HOH B . 
D 2 HOH 4   904  293 HOH HOH B . 
D 2 HOH 5   905  433 HOH HOH B . 
D 2 HOH 6   906  227 HOH HOH B . 
D 2 HOH 7   907  116 HOH HOH B . 
D 2 HOH 8   908  197 HOH HOH B . 
D 2 HOH 9   909  201 HOH HOH B . 
D 2 HOH 10  910  176 HOH HOH B . 
D 2 HOH 11  911  393 HOH HOH B . 
D 2 HOH 12  912  214 HOH HOH B . 
D 2 HOH 13  913  539 HOH HOH B . 
D 2 HOH 14  914  64  HOH HOH B . 
D 2 HOH 15  915  418 HOH HOH B . 
D 2 HOH 16  916  345 HOH HOH B . 
D 2 HOH 17  917  327 HOH HOH B . 
D 2 HOH 18  918  389 HOH HOH B . 
D 2 HOH 19  919  520 HOH HOH B . 
D 2 HOH 20  920  232 HOH HOH B . 
D 2 HOH 21  921  57  HOH HOH B . 
D 2 HOH 22  922  76  HOH HOH B . 
D 2 HOH 23  923  228 HOH HOH B . 
D 2 HOH 24  924  213 HOH HOH B . 
D 2 HOH 25  925  291 HOH HOH B . 
D 2 HOH 26  926  272 HOH HOH B . 
D 2 HOH 27  927  153 HOH HOH B . 
D 2 HOH 28  928  162 HOH HOH B . 
D 2 HOH 29  929  283 HOH HOH B . 
D 2 HOH 30  930  437 HOH HOH B . 
D 2 HOH 31  931  217 HOH HOH B . 
D 2 HOH 32  932  450 HOH HOH B . 
D 2 HOH 33  933  246 HOH HOH B . 
D 2 HOH 34  934  346 HOH HOH B . 
D 2 HOH 35  935  188 HOH HOH B . 
D 2 HOH 36  936  453 HOH HOH B . 
D 2 HOH 37  937  238 HOH HOH B . 
D 2 HOH 38  938  485 HOH HOH B . 
D 2 HOH 39  939  117 HOH HOH B . 
D 2 HOH 40  940  39  HOH HOH B . 
D 2 HOH 41  941  397 HOH HOH B . 
D 2 HOH 42  942  242 HOH HOH B . 
D 2 HOH 43  943  99  HOH HOH B . 
D 2 HOH 44  944  87  HOH HOH B . 
D 2 HOH 45  945  102 HOH HOH B . 
D 2 HOH 46  946  90  HOH HOH B . 
D 2 HOH 47  947  121 HOH HOH B . 
D 2 HOH 48  948  365 HOH HOH B . 
D 2 HOH 49  949  74  HOH HOH B . 
D 2 HOH 50  950  207 HOH HOH B . 
D 2 HOH 51  951  416 HOH HOH B . 
D 2 HOH 52  952  123 HOH HOH B . 
D 2 HOH 53  953  53  HOH HOH B . 
D 2 HOH 54  954  257 HOH HOH B . 
D 2 HOH 55  955  33  HOH HOH B . 
D 2 HOH 56  956  294 HOH HOH B . 
D 2 HOH 57  957  178 HOH HOH B . 
D 2 HOH 58  958  414 HOH HOH B . 
D 2 HOH 59  959  356 HOH HOH B . 
D 2 HOH 60  960  220 HOH HOH B . 
D 2 HOH 61  961  78  HOH HOH B . 
D 2 HOH 62  962  235 HOH HOH B . 
D 2 HOH 63  963  363 HOH HOH B . 
D 2 HOH 64  964  243 HOH HOH B . 
D 2 HOH 65  965  35  HOH HOH B . 
D 2 HOH 66  966  295 HOH HOH B . 
D 2 HOH 67  967  273 HOH HOH B . 
D 2 HOH 68  968  82  HOH HOH B . 
D 2 HOH 69  969  111 HOH HOH B . 
D 2 HOH 70  970  140 HOH HOH B . 
D 2 HOH 71  971  47  HOH HOH B . 
D 2 HOH 72  972  226 HOH HOH B . 
D 2 HOH 73  973  14  HOH HOH B . 
D 2 HOH 74  974  62  HOH HOH B . 
D 2 HOH 75  975  133 HOH HOH B . 
D 2 HOH 76  976  309 HOH HOH B . 
D 2 HOH 77  977  239 HOH HOH B . 
D 2 HOH 78  978  124 HOH HOH B . 
D 2 HOH 79  979  480 HOH HOH B . 
D 2 HOH 80  980  459 HOH HOH B . 
D 2 HOH 81  981  465 HOH HOH B . 
D 2 HOH 82  982  401 HOH HOH B . 
D 2 HOH 83  983  423 HOH HOH B . 
D 2 HOH 84  984  340 HOH HOH B . 
D 2 HOH 85  985  173 HOH HOH B . 
D 2 HOH 86  986  181 HOH HOH B . 
D 2 HOH 87  987  154 HOH HOH B . 
D 2 HOH 88  988  337 HOH HOH B . 
D 2 HOH 89  989  125 HOH HOH B . 
D 2 HOH 90  990  73  HOH HOH B . 
D 2 HOH 91  991  152 HOH HOH B . 
D 2 HOH 92  992  348 HOH HOH B . 
D 2 HOH 93  993  6   HOH HOH B . 
D 2 HOH 94  994  306 HOH HOH B . 
D 2 HOH 95  995  334 HOH HOH B . 
D 2 HOH 96  996  18  HOH HOH B . 
D 2 HOH 97  997  253 HOH HOH B . 
D 2 HOH 98  998  146 HOH HOH B . 
D 2 HOH 99  999  118 HOH HOH B . 
D 2 HOH 100 1000 504 HOH HOH B . 
D 2 HOH 101 1001 34  HOH HOH B . 
D 2 HOH 102 1002 255 HOH HOH B . 
D 2 HOH 103 1003 229 HOH HOH B . 
D 2 HOH 104 1004 288 HOH HOH B . 
D 2 HOH 105 1005 143 HOH HOH B . 
D 2 HOH 106 1006 544 HOH HOH B . 
D 2 HOH 107 1007 196 HOH HOH B . 
D 2 HOH 108 1008 516 HOH HOH B . 
D 2 HOH 109 1009 311 HOH HOH B . 
D 2 HOH 110 1010 100 HOH HOH B . 
D 2 HOH 111 1011 15  HOH HOH B . 
D 2 HOH 112 1012 68  HOH HOH B . 
D 2 HOH 113 1013 115 HOH HOH B . 
D 2 HOH 114 1014 517 HOH HOH B . 
D 2 HOH 115 1015 430 HOH HOH B . 
D 2 HOH 116 1016 547 HOH HOH B . 
D 2 HOH 117 1017 505 HOH HOH B . 
D 2 HOH 118 1018 303 HOH HOH B . 
D 2 HOH 119 1019 164 HOH HOH B . 
D 2 HOH 120 1020 518 HOH HOH B . 
D 2 HOH 121 1021 75  HOH HOH B . 
D 2 HOH 122 1022 109 HOH HOH B . 
D 2 HOH 123 1023 183 HOH HOH B . 
D 2 HOH 124 1024 361 HOH HOH B . 
D 2 HOH 125 1025 200 HOH HOH B . 
D 2 HOH 126 1026 31  HOH HOH B . 
D 2 HOH 127 1027 375 HOH HOH B . 
D 2 HOH 128 1028 138 HOH HOH B . 
D 2 HOH 129 1029 135 HOH HOH B . 
D 2 HOH 130 1030 455 HOH HOH B . 
D 2 HOH 131 1031 40  HOH HOH B . 
D 2 HOH 132 1032 147 HOH HOH B . 
D 2 HOH 133 1033 501 HOH HOH B . 
D 2 HOH 134 1034 487 HOH HOH B . 
D 2 HOH 135 1035 301 HOH HOH B . 
D 2 HOH 136 1036 439 HOH HOH B . 
D 2 HOH 137 1037 81  HOH HOH B . 
D 2 HOH 138 1038 300 HOH HOH B . 
D 2 HOH 139 1039 333 HOH HOH B . 
D 2 HOH 140 1040 144 HOH HOH B . 
D 2 HOH 141 1041 134 HOH HOH B . 
D 2 HOH 142 1042 98  HOH HOH B . 
D 2 HOH 143 1043 195 HOH HOH B . 
D 2 HOH 144 1044 307 HOH HOH B . 
D 2 HOH 145 1045 60  HOH HOH B . 
D 2 HOH 146 1046 155 HOH HOH B . 
D 2 HOH 147 1047 442 HOH HOH B . 
D 2 HOH 148 1048 292 HOH HOH B . 
D 2 HOH 149 1049 137 HOH HOH B . 
D 2 HOH 150 1050 141 HOH HOH B . 
D 2 HOH 151 1051 86  HOH HOH B . 
D 2 HOH 152 1052 298 HOH HOH B . 
D 2 HOH 153 1053 317 HOH HOH B . 
D 2 HOH 154 1054 514 HOH HOH B . 
D 2 HOH 155 1055 209 HOH HOH B . 
D 2 HOH 156 1056 391 HOH HOH B . 
D 2 HOH 157 1057 48  HOH HOH B . 
D 2 HOH 158 1058 267 HOH HOH B . 
D 2 HOH 159 1059 3   HOH HOH B . 
D 2 HOH 160 1060 110 HOH HOH B . 
D 2 HOH 161 1061 132 HOH HOH B . 
D 2 HOH 162 1062 443 HOH HOH B . 
D 2 HOH 163 1063 381 HOH HOH B . 
D 2 HOH 164 1064 268 HOH HOH B . 
D 2 HOH 165 1065 203 HOH HOH B . 
D 2 HOH 166 1066 536 HOH HOH B . 
D 2 HOH 167 1067 323 HOH HOH B . 
D 2 HOH 168 1068 50  HOH HOH B . 
D 2 HOH 169 1069 160 HOH HOH B . 
D 2 HOH 170 1070 492 HOH HOH B . 
D 2 HOH 171 1071 463 HOH HOH B . 
D 2 HOH 172 1072 542 HOH HOH B . 
D 2 HOH 173 1073 466 HOH HOH B . 
D 2 HOH 174 1074 159 HOH HOH B . 
D 2 HOH 175 1075 339 HOH HOH B . 
D 2 HOH 176 1076 79  HOH HOH B . 
D 2 HOH 177 1077 165 HOH HOH B . 
D 2 HOH 178 1078 225 HOH HOH B . 
D 2 HOH 179 1079 404 HOH HOH B . 
D 2 HOH 180 1080 305 HOH HOH B . 
D 2 HOH 181 1081 177 HOH HOH B . 
D 2 HOH 182 1082 240 HOH HOH B . 
D 2 HOH 183 1083 350 HOH HOH B . 
D 2 HOH 184 1084 287 HOH HOH B . 
D 2 HOH 185 1085 513 HOH HOH B . 
D 2 HOH 186 1086 469 HOH HOH B . 
D 2 HOH 187 1087 548 HOH HOH B . 
D 2 HOH 188 1088 299 HOH HOH B . 
D 2 HOH 189 1089 515 HOH HOH B . 
D 2 HOH 190 1090 461 HOH HOH B . 
D 2 HOH 191 1091 434 HOH HOH B . 
D 2 HOH 192 1092 417 HOH HOH B . 
D 2 HOH 193 1093 464 HOH HOH B . 
D 2 HOH 194 1094 357 HOH HOH B . 
D 2 HOH 195 1095 471 HOH HOH B . 
D 2 HOH 196 1096 546 HOH HOH B . 
D 2 HOH 197 1097 95  HOH HOH B . 
D 2 HOH 198 1098 498 HOH HOH B . 
D 2 HOH 199 1099 413 HOH HOH B . 
D 2 HOH 200 1100 221 HOH HOH B . 
D 2 HOH 201 1101 398 HOH HOH B . 
D 2 HOH 202 1102 237 HOH HOH B . 
D 2 HOH 203 1103 355 HOH HOH B . 
D 2 HOH 204 1104 329 HOH HOH B . 
D 2 HOH 205 1105 328 HOH HOH B . 
D 2 HOH 206 1106 216 HOH HOH B . 
D 2 HOH 207 1107 503 HOH HOH B . 
D 2 HOH 208 1108 446 HOH HOH B . 
D 2 HOH 209 1109 477 HOH HOH B . 
D 2 HOH 210 1110 444 HOH HOH B . 
D 2 HOH 211 1111 470 HOH HOH B . 
D 2 HOH 212 1112 497 HOH HOH B . 
D 2 HOH 213 1113 441 HOH HOH B . 
D 2 HOH 214 1114 493 HOH HOH B . 
D 2 HOH 215 1115 289 HOH HOH B . 
D 2 HOH 216 1116 354 HOH HOH B . 
D 2 HOH 217 1117 259 HOH HOH B . 
D 2 HOH 218 1118 525 HOH HOH B . 
D 2 HOH 219 1119 483 HOH HOH B . 
D 2 HOH 220 1120 533 HOH HOH B . 
D 2 HOH 221 1121 412 HOH HOH B . 
D 2 HOH 222 1122 425 HOH HOH B . 
D 2 HOH 223 1123 344 HOH HOH B . 
D 2 HOH 224 1124 128 HOH HOH B . 
D 2 HOH 225 1125 191 HOH HOH B . 
D 2 HOH 226 1126 531 HOH HOH B . 
D 2 HOH 227 1127 130 HOH HOH B . 
D 2 HOH 228 1128 275 HOH HOH B . 
D 2 HOH 229 1129 449 HOH HOH B . 
D 2 HOH 230 1130 247 HOH HOH B . 
D 2 HOH 231 1131 543 HOH HOH B . 
D 2 HOH 232 1132 408 HOH HOH B . 
D 2 HOH 233 1133 222 HOH HOH B . 
D 2 HOH 234 1134 382 HOH HOH B . 
D 2 HOH 235 1135 282 HOH HOH B . 
D 2 HOH 236 1136 524 HOH HOH B . 
D 2 HOH 237 1137 478 HOH HOH B . 
D 2 HOH 238 1138 304 HOH HOH B . 
D 2 HOH 239 1139 406 HOH HOH B . 
D 2 HOH 240 1140 96  HOH HOH B . 
D 2 HOH 241 1141 426 HOH HOH B . 
D 2 HOH 242 1142 500 HOH HOH B . 
D 2 HOH 243 1143 204 HOH HOH B . 
D 2 HOH 244 1144 458 HOH HOH B . 
D 2 HOH 245 1145 320 HOH HOH B . 
D 2 HOH 246 1146 108 HOH HOH B . 
D 2 HOH 247 1147 234 HOH HOH B . 
D 2 HOH 248 1148 364 HOH HOH B . 
D 2 HOH 249 1149 432 HOH HOH B . 
D 2 HOH 250 1150 245 HOH HOH B . 
D 2 HOH 251 1151 379 HOH HOH B . 
D 2 HOH 252 1152 325 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_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 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX     ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS      ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MR-Rosetta ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.66 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ECT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.271 
_cell.length_a_esd                 ? 
_cell.length_b                     58.550 
_cell.length_b_esd                 ? 
_cell.length_c                     76.368 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9ECT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   9ECT 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.44 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M KNO3, 25% (w/v) PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-03-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.521 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.521 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ECT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               74.21 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     40706 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          2.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.224 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.984 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.205 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.813 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4006 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.835 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.86 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.621 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                                 9ECT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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                            1.75 
_refine.ls_d_res_low                             74.21 
_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                     40700 
_refine.ls_number_reflns_R_free                  2031 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.30 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1961 
_refine.ls_R_factor_R_free                       0.2421 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1936 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_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                          1.37 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 26.06 
_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                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_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                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        74.21 
_refine_hist.number_atoms_solvent             542 
_refine_hist.number_atoms_total               3809 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3267 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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_error 
_refine_ls_shell.R_factor_R_work 
_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_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.75 1.79  . . 119 2547 99.00  . . . . 0.2865 . . . . . . . . . . . 0.3443 
'X-RAY DIFFRACTION' 1.79 1.84  . . 130 2569 99.00  . . . . 0.2622 . . . . . . . . . . . 0.3528 
'X-RAY DIFFRACTION' 1.84 1.89  . . 145 2544 99.00  . . . . 0.2340 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 1.89 1.94  . . 118 2566 99.00  . . . . 0.2386 . . . . . . . . . . . 0.2920 
'X-RAY DIFFRACTION' 1.94 2.00  . . 120 2546 99.00  . . . . 0.2092 . . . . . . . . . . . 0.2711 
'X-RAY DIFFRACTION' 2.00 2.08  . . 144 2568 99.00  . . . . 0.2105 . . . . . . . . . . . 0.2866 
'X-RAY DIFFRACTION' 2.08 2.16  . . 149 2558 99.00  . . . . 0.2085 . . . . . . . . . . . 0.2868 
'X-RAY DIFFRACTION' 2.16 2.26  . . 133 2598 100.00 . . . . 0.1999 . . . . . . . . . . . 0.2585 
'X-RAY DIFFRACTION' 2.26 2.38  . . 150 2529 99.00  . . . . 0.1948 . . . . . . . . . . . 0.2621 
'X-RAY DIFFRACTION' 2.38 2.52  . . 119 2606 99.00  . . . . 0.2006 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 2.52 2.72  . . 129 2574 100.00 . . . . 0.1993 . . . . . . . . . . . 0.2857 
'X-RAY DIFFRACTION' 2.72 2.99  . . 167 2593 100.00 . . . . 0.1971 . . . . . . . . . . . 0.2425 
'X-RAY DIFFRACTION' 2.99 3.43  . . 134 2598 100.00 . . . . 0.1770 . . . . . . . . . . . 0.2486 
'X-RAY DIFFRACTION' 3.43 4.32  . . 130 2598 99.00  . . . . 0.1466 . . . . . . . . . . . 0.1614 
'X-RAY DIFFRACTION' 4.32 74.21 . . 144 2675 100.00 . . . . 0.1660 . . . . . . . . . . . 0.1751 
# 
_struct.entry_id                     9ECT 
_struct.title                        'Crystal Structure of the Gemella haemolysans Immunoglobulin A1 Protease Trypsin-Like Domain' 
_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        9ECT 
_struct_keywords.text            'trypsin-like fold, immunoglobulin A1 protease domain, secreted protein, UNKNOWN FUNCTION' 
_struct_keywords.pdbx_keywords   'UNKNOWN FUNCTION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    C5NYF3_9BACL 
_struct_ref.pdbx_db_accession          C5NYF3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NNVPKNASALLRMNFVKGNQVLSGTGSATFIAPNVLLTVAHNFINNSADNSTGEFIGDKSKNTYEWQTPDGQKGSFTSED
IHFYNKKDYPKGFIYDLAVITLPQSTRRQHANLVENYSKVNVNDKLNVYGYPRGEYAHLKDTTVEIEQKYANNTYGVQYQ
GGKAGMSGGGIFNSKGEVIGLHQNGAENRSGGLILSPTQLDWIRSIIKGKEIT
;
_struct_ref.pdbx_align_begin           661 
# 
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 9ECT A 3 ? 215 ? C5NYF3 661 ? 873 ? 684 896 
2 1 9ECT B 3 ? 215 ? C5NYF3 661 ? 873 ? 684 896 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9ECT GLY A 1 ? UNP C5NYF3 ? ? 'expression tag' -2 1 
1 9ECT SER A 2 ? UNP C5NYF3 ? ? 'expression tag' -1 2 
2 9ECT GLY B 1 ? UNP C5NYF3 ? ? 'expression tag' -2 3 
2 9ECT SER B 2 ? UNP C5NYF3 ? ? 'expression tag' -1 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 ASN A 4   ? ALA A 9   ? ASN A 685 ALA A 690 1 ? 6  
HELX_P HELX_P2  AA2 VAL A 41  ? ASN A 44  ? VAL A 722 ASN A 725 5 ? 4  
HELX_P HELX_P3  AA3 THR A 79  ? GLU A 81  ? THR A 760 GLU A 762 5 ? 3  
HELX_P HELX_P4  AA4 ASP A 90  ? ASP A 98  ? ASP A 771 ASP A 779 5 ? 9  
HELX_P HELX_P5  AA5 TYR A 133 ? GLU A 137 ? TYR A 814 GLU A 818 5 ? 5  
HELX_P HELX_P6  AA6 SER A 198 ? LYS A 210 ? SER A 879 LYS A 891 1 ? 13 
HELX_P HELX_P7  AA7 ASN B 4   ? ALA B 9   ? ASN B 685 ALA B 690 1 ? 6  
HELX_P HELX_P8  AA8 VAL B 41  ? ASN B 44  ? VAL B 722 ASN B 725 5 ? 4  
HELX_P HELX_P9  AA9 THR B 79  ? GLU B 81  ? THR B 760 GLU B 762 5 ? 3  
HELX_P HELX_P10 AB1 ASP B 90  ? ASP B 98  ? ASP B 771 ASP B 779 5 ? 9  
HELX_P HELX_P11 AB2 TYR B 133 ? GLU B 137 ? TYR B 814 GLU B 818 5 ? 5  
HELX_P HELX_P12 AB3 GLY B 187 ? ARG B 191 ? GLY B 868 ARG B 872 5 ? 5  
HELX_P HELX_P13 AB4 SER B 198 ? GLY B 211 ? SER B 879 GLY B 892 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
AA5 ? 2 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 75  ? PHE A 78  ? LYS A 756 PHE A 759 
AA1 2 THR A 65  ? GLN A 69  ? THR A 746 GLN A 750 
AA1 3 SER A 10  ? LYS A 19  ? SER A 691 LYS A 700 
AA1 4 GLN A 22  ? ALA A 34  ? GLN A 703 ALA A 715 
AA1 5 VAL A 37  ? THR A 40  ? VAL A 718 THR A 721 
AA1 6 ALA A 100 ? THR A 103 ? ALA A 781 THR A 784 
AA1 7 ILE A 83  ? PHE A 85  ? ILE A 764 PHE A 766 
AA2 1 ILE A 46  ? ASN A 48  ? ILE A 727 ASN A 729 
AA2 2 GLY A 55  ? PHE A 57  ? GLY A 736 PHE A 738 
AA3 1 ALA A 139 ? THR A 145 ? ALA A 820 THR A 826 
AA3 2 LYS A 127 ? GLY A 132 ? LYS A 808 GLY A 813 
AA3 3 GLY A 172 ? PHE A 174 ? GLY A 853 PHE A 855 
AA3 4 VAL A 180 ? ASN A 186 ? VAL A 861 ASN A 867 
AA3 5 GLY A 193 ? ILE A 196 ? GLY A 874 ILE A 877 
AA3 6 THR A 156 ? GLN A 160 ? THR A 837 GLN A 841 
AA3 7 ILE A 148 ? ALA A 153 ? ILE A 829 ALA A 834 
AA4 1 LYS B 75  ? PHE B 78  ? LYS B 756 PHE B 759 
AA4 2 THR B 65  ? GLN B 69  ? THR B 746 GLN B 750 
AA4 3 SER B 10  ? LYS B 19  ? SER B 691 LYS B 700 
AA4 4 GLN B 22  ? ALA B 34  ? GLN B 703 ALA B 715 
AA4 5 VAL B 37  ? THR B 40  ? VAL B 718 THR B 721 
AA4 6 ALA B 100 ? THR B 103 ? ALA B 781 THR B 784 
AA4 7 ILE B 83  ? PHE B 85  ? ILE B 764 PHE B 766 
AA5 1 ILE B 46  ? ASN B 48  ? ILE B 727 ASN B 729 
AA5 2 GLY B 55  ? PHE B 57  ? GLY B 736 PHE B 738 
AA6 1 ALA B 139 ? THR B 145 ? ALA B 820 THR B 826 
AA6 2 LYS B 127 ? GLY B 132 ? LYS B 808 GLY B 813 
AA6 3 GLY B 172 ? PHE B 174 ? GLY B 853 PHE B 855 
AA6 4 VAL B 180 ? HIS B 184 ? VAL B 861 HIS B 865 
AA6 5 GLY B 193 ? ILE B 196 ? GLY B 874 ILE B 877 
AA6 6 THR B 156 ? GLN B 160 ? THR B 837 GLN B 841 
AA6 7 ILE B 148 ? ALA B 153 ? ILE B 829 ALA B 834 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLY A 76  ? O GLY A 757 N TRP A 68  ? N TRP A 749 
AA1 2 3 O GLN A 69  ? O GLN A 750 N LEU A 12  ? N LEU A 693 
AA1 3 4 N LYS A 19  ? N LYS A 700 O GLN A 22  ? O GLN A 703 
AA1 4 5 N THR A 31  ? N THR A 712 O LEU A 39  ? O LEU A 720 
AA1 5 6 N THR A 40  ? N THR A 721 O ALA A 100 ? O ALA A 781 
AA1 6 7 O VAL A 101 ? O VAL A 782 N HIS A 84  ? N HIS A 765 
AA2 1 2 N ASN A 47  ? N ASN A 728 O GLU A 56  ? O GLU A 737 
AA3 1 2 O LEU A 141 ? O LEU A 822 N VAL A 130 ? N VAL A 811 
AA3 2 3 N ASN A 129 ? N ASN A 810 O PHE A 174 ? O PHE A 855 
AA3 3 4 N ILE A 173 ? N ILE A 854 O ILE A 181 ? O ILE A 862 
AA3 4 5 N LEU A 183 ? N LEU A 864 O LEU A 195 ? O LEU A 876 
AA3 5 6 O GLY A 194 ? O GLY A 875 N VAL A 159 ? N VAL A 840 
AA3 6 7 O GLY A 158 ? O GLY A 839 N GLN A 150 ? N GLN A 831 
AA4 1 2 O GLY B 76  ? O GLY B 757 N TRP B 68  ? N TRP B 749 
AA4 2 3 O GLN B 69  ? O GLN B 750 N LEU B 12  ? N LEU B 693 
AA4 3 4 N MET B 15  ? N MET B 696 O GLY B 26  ? O GLY B 707 
AA4 4 5 N THR B 31  ? N THR B 712 O LEU B 39  ? O LEU B 720 
AA4 5 6 N LEU B 38  ? N LEU B 719 O ILE B 102 ? O ILE B 783 
AA4 6 7 O VAL B 101 ? O VAL B 782 N HIS B 84  ? N HIS B 765 
AA5 1 2 N ASN B 47  ? N ASN B 728 O GLU B 56  ? O GLU B 737 
AA6 1 2 O LEU B 141 ? O LEU B 822 N VAL B 130 ? N VAL B 811 
AA6 2 3 N ASN B 129 ? N ASN B 810 O PHE B 174 ? O PHE B 855 
AA6 3 4 N ILE B 173 ? N ILE B 854 O ILE B 181 ? O ILE B 862 
AA6 4 5 N LEU B 183 ? N LEU B 864 O LEU B 195 ? O LEU B 876 
AA6 5 6 O ILE B 196 ? O ILE B 877 N TYR B 157 ? N TYR B 838 
AA6 6 7 O GLY B 158 ? O GLY B 839 N GLN B 150 ? N GLN B 831 
# 
_pdbx_entry_details.entry_id                   9ECT 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O  B HOH 1018 ? ? O B HOH 1035 ? ? 2.05 
2  1 O  A HOH 1069 ? ? O A HOH 1171 ? ? 2.09 
3  1 O  A HOH 1025 ? ? O A HOH 1099 ? ? 2.10 
4  1 O  A HOH 902  ? ? O A HOH 1097 ? ? 2.10 
5  1 OG B SER 850  ? A O B HOH 901  ? ? 2.14 
6  1 O  A HOH 932  ? ? O A HOH 1129 ? ? 2.16 
7  1 O  A HOH 1110 ? ? O A HOH 1162 ? ? 2.16 
8  1 O  B HOH 905  ? ? O B HOH 1113 ? ? 2.17 
9  1 O  A HOH 1022 ? ? O A HOH 1125 ? ? 2.17 
10 1 O  A HOH 942  ? ? O A HOH 949  ? ? 2.17 
11 1 O  A HOH 1138 ? ? O A HOH 1166 ? ? 2.19 
12 1 O  B HOH 980  ? ? O B HOH 1121 ? ? 2.19 
13 1 O  A HOH 1011 ? ? O A HOH 1140 ? ? 2.19 
14 1 O  A HOH 1081 ? ? O A HOH 1129 ? ? 2.19 
15 1 NZ A LYS 823  ? ? O A HOH 901  ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 919 ? ? 1_555 O B HOH 1008 ? ? 2_656 2.12 
2 1 O A HOH 901 ? ? 1_555 O B HOH 1032 ? ? 1_554 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 768 ? ? -161.25 86.61  
2 1 ASN A 806 ? ? 86.41   -3.44  
3 1 ARG A 872 ? ? 74.11   116.62 
4 1 ASN B 717 ? ? -143.16 34.40  
5 1 ASN B 768 ? ? -161.07 85.61  
6 1 PHE B 776 ? ? -29.23  -51.26 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 27.4086 37.8393 5.5981  0.0679 ? -0.0161 ? -0.0249 ? 0.1113 ? -0.0092 ? 0.1396 ? 0.9538 ? 0.2693  
? 0.0091  ? 1.5867 ? -0.3378 ? 1.1345 ? 0.0118  ? 0.1028  ? 0.1031  ? 0.0869  ? -0.0424 ? 0.2006  ? 0.0640  ? -0.1598 ? 0.0412  ? 
2 'X-RAY DIFFRACTION' ? refined 35.7718 42.0518 -1.0644 0.0414 ? 0.0064  ? -0.0396 ? 0.1285 ? -0.0070 ? 0.1539 ? 0.3690 ? 0.0870  
? -0.4035 ? 0.9775 ? -0.1674 ? 0.8712 ? 0.0044  ? 0.0423  ? -0.0403 ? -0.0249 ? -0.0527 ? 0.0508  ? 0.0151  ? -0.0636 ? 0.0295  ? 
3 'X-RAY DIFFRACTION' ? refined 39.7552 45.4200 -0.2374 0.0325 ? 0.0063  ? -0.0451 ? 0.0953 ? -0.0024 ? 0.1763 ? 2.3812 ? 0.1561  
? -0.2605 ? 2.6859 ? 0.4591  ? 2.6502 ? 0.0605  ? 0.0032  ? -0.1352 ? 0.0775  ? -0.1009 ? -0.0102 ? 0.0517  ? -0.0648 ? -0.2005 ? 
4 'X-RAY DIFFRACTION' ? refined 20.7477 41.5244 41.9709 0.0835 ? 0.0050  ? -0.0266 ? 0.1290 ? 0.0076  ? 0.0825 ? 2.2686 ? -0.9475 
? -0.4654 ? 2.3021 ? 0.4354  ? 0.9456 ? -0.0957 ? -0.0311 ? -0.0824 ? 0.0492  ? 0.0511  ? 0.1790  ? 0.0292  ? -0.0839 ? 0.0331  ? 
5 'X-RAY DIFFRACTION' ? refined 30.0415 49.6706 31.0459 0.0796 ? -0.0120 ? -0.0276 ? 0.1530 ? -0.0121 ? 0.1371 ? 1.5239 ? 1.3312  
? -0.3602 ? 3.1441 ? 0.9114  ? 2.0577 ? -0.0953 ? 0.0292  ? 0.0733  ? -0.1874 ? 0.1362  ? -0.0758 ? -0.0980 ? -0.0038 ? -0.0213 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -1 through 745 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 746 through 852 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 853 through 893 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid -1 through 794 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 795 through 892 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1190 ? 6.08 . 
2 1 O ? B HOH 1152 ? 6.56 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -2  ? A GLY 1   
2 1 Y 1 A GLU 894 ? A GLU 213 
3 1 Y 1 A ILE 895 ? A ILE 214 
4 1 Y 1 A THR 896 ? A THR 215 
5 1 Y 1 B GLY -2  ? B GLY 1   
6 1 Y 1 B LYS 893 ? B LYS 212 
7 1 Y 1 B GLU 894 ? B GLU 213 
8 1 Y 1 B ILE 895 ? B ILE 214 
9 1 Y 1 B THR 896 ? B THR 215 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TRP N    N N N 307 
TRP CA   C N S 308 
TRP C    C N N 309 
TRP O    O N N 310 
TRP CB   C N N 311 
TRP CG   C Y N 312 
TRP CD1  C Y N 313 
TRP CD2  C Y N 314 
TRP NE1  N Y N 315 
TRP CE2  C Y N 316 
TRP CE3  C Y N 317 
TRP CZ2  C Y N 318 
TRP CZ3  C Y N 319 
TRP CH2  C Y N 320 
TRP OXT  O N N 321 
TRP H    H N N 322 
TRP H2   H N N 323 
TRP HA   H N N 324 
TRP HB2  H N N 325 
TRP HB3  H N N 326 
TRP HD1  H N N 327 
TRP HE1  H N N 328 
TRP HE3  H N N 329 
TRP HZ2  H N N 330 
TRP HZ3  H N N 331 
TRP HH2  H N N 332 
TRP HXT  H N N 333 
TYR N    N N N 334 
TYR CA   C N S 335 
TYR C    C N N 336 
TYR O    O N N 337 
TYR CB   C N N 338 
TYR CG   C Y N 339 
TYR CD1  C Y N 340 
TYR CD2  C Y N 341 
TYR CE1  C Y N 342 
TYR CE2  C Y N 343 
TYR CZ   C Y N 344 
TYR OH   O N N 345 
TYR OXT  O N N 346 
TYR H    H N N 347 
TYR H2   H N N 348 
TYR HA   H N N 349 
TYR HB2  H N N 350 
TYR HB3  H N N 351 
TYR HD1  H N N 352 
TYR HD2  H N N 353 
TYR HE1  H N N 354 
TYR HE2  H N N 355 
TYR HH   H N N 356 
TYR HXT  H N N 357 
VAL N    N N N 358 
VAL CA   C N S 359 
VAL C    C N N 360 
VAL O    O N N 361 
VAL CB   C N N 362 
VAL CG1  C N N 363 
VAL CG2  C N N 364 
VAL OXT  O N N 365 
VAL H    H N N 366 
VAL H2   H N N 367 
VAL HA   H N N 368 
VAL HB   H N N 369 
VAL HG11 H N N 370 
VAL HG12 H N N 371 
VAL HG13 H N N 372 
VAL HG21 H N N 373 
VAL HG22 H N N 374 
VAL HG23 H N N 375 
VAL HXT  H N N 376 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'Natural Sciences and Engineering Research Council (NSERC, Canada)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      RoseTTAFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9ECT 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021155 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005141 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017079 
_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]   0.013476 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . SER A 1 2   ? 50.786 30.675 -8.325  1.00 63.86  ? -1   SER A N   1 
ATOM   2    C CA  . SER A 1 2   ? 49.691 31.511 -7.846  1.00 56.30  ? -1   SER A CA  1 
ATOM   3    C C   . SER A 1 2   ? 48.649 31.750 -8.935  1.00 52.87  ? -1   SER A C   1 
ATOM   4    O O   . SER A 1 2   ? 47.765 32.593 -8.785  1.00 37.75  ? -1   SER A O   1 
ATOM   5    C CB  . SER A 1 2   ? 50.223 32.848 -7.325  1.00 60.28  ? -1   SER A CB  1 
ATOM   6    O OG  . SER A 1 2   ? 51.009 32.666 -6.159  1.00 53.08  ? -1   SER A OG  1 
ATOM   7    N N   . ASN A 1 3   ? 48.772 30.993 -10.028 1.00 59.96  ? 684  ASN A N   1 
ATOM   8    C CA  . ASN A 1 3   ? 47.839 31.104 -11.146 1.00 51.58  ? 684  ASN A CA  1 
ATOM   9    C C   . ASN A 1 3   ? 46.396 30.938 -10.682 1.00 47.73  ? 684  ASN A C   1 
ATOM   10   O O   . ASN A 1 3   ? 45.516 31.734 -11.034 1.00 37.48  ? 684  ASN A O   1 
ATOM   11   C CB  . ASN A 1 3   ? 48.196 30.053 -12.204 1.00 49.20  ? 684  ASN A CB  1 
ATOM   12   C CG  . ASN A 1 3   ? 47.470 30.264 -13.516 1.00 62.91  ? 684  ASN A CG  1 
ATOM   13   O OD1 . ASN A 1 3   ? 47.132 31.390 -13.880 1.00 75.19  ? 684  ASN A OD1 1 
ATOM   14   N ND2 . ASN A 1 3   ? 47.230 29.174 -14.239 1.00 58.57  ? 684  ASN A ND2 1 
ATOM   15   N N   . ASN A 1 4   ? 46.143 29.912 -9.872  1.00 36.57  ? 685  ASN A N   1 
ATOM   16   C CA  . ASN A 1 4   ? 44.808 29.567 -9.406  1.00 21.27  ? 685  ASN A CA  1 
ATOM   17   C C   . ASN A 1 4   ? 44.522 30.078 -8.007  1.00 14.99  ? 685  ASN A C   1 
ATOM   18   O O   . ASN A 1 4   ? 43.484 29.724 -7.435  1.00 18.32  ? 685  ASN A O   1 
ATOM   19   C CB  . ASN A 1 4   ? 44.611 28.050 -9.429  1.00 26.50  ? 685  ASN A CB  1 
ATOM   20   C CG  . ASN A 1 4   ? 44.938 27.441 -10.773 1.00 38.18  ? 685  ASN A CG  1 
ATOM   21   O OD1 . ASN A 1 4   ? 44.262 27.712 -11.766 1.00 30.82  ? 685  ASN A OD1 1 
ATOM   22   N ND2 . ASN A 1 4   ? 45.973 26.599 -10.812 1.00 33.35  ? 685  ASN A ND2 1 
ATOM   23   N N   . VAL A 1 5   ? 45.413 30.883 -7.435  1.00 14.78  ? 686  VAL A N   1 
ATOM   24   C CA  . VAL A 1 5   ? 45.250 31.309 -6.047  1.00 13.79  ? 686  VAL A CA  1 
ATOM   25   C C   . VAL A 1 5   ? 44.021 32.208 -5.898  1.00 12.88  ? 686  VAL A C   1 
ATOM   26   O O   . VAL A 1 5   ? 43.232 31.981 -4.970  1.00 13.68  ? 686  VAL A O   1 
ATOM   27   C CB  . VAL A 1 5   ? 46.535 31.965 -5.516  1.00 16.19  ? 686  VAL A CB  1 
ATOM   28   C CG1 . VAL A 1 5   ? 46.252 32.767 -4.270  1.00 15.06  ? 686  VAL A CG1 1 
ATOM   29   C CG2 . VAL A 1 5   ? 47.556 30.892 -5.189  1.00 22.42  ? 686  VAL A CG2 1 
ATOM   30   N N   . PRO A 1 6   ? 43.801 33.221 -6.751  1.00 12.97  ? 687  PRO A N   1 
ATOM   31   C CA  . PRO A 1 6   ? 42.557 34.012 -6.604  1.00 12.23  ? 687  PRO A CA  1 
ATOM   32   C C   . PRO A 1 6   ? 41.294 33.172 -6.686  1.00 12.07  ? 687  PRO A C   1 
ATOM   33   O O   . PRO A 1 6   ? 40.454 33.251 -5.785  1.00 12.42  ? 687  PRO A O   1 
ATOM   34   C CB  . PRO A 1 6   ? 42.663 35.027 -7.747  1.00 12.69  ? 687  PRO A CB  1 
ATOM   35   C CG  . PRO A 1 6   ? 44.130 35.245 -7.883  1.00 13.28  ? 687  PRO A CG  1 
ATOM   36   C CD  . PRO A 1 6   ? 44.708 33.848 -7.732  1.00 18.48  ? 687  PRO A CD  1 
ATOM   37   N N   . LYS A 1 7   ? 41.141 32.363 -7.736  1.00 12.83  ? 688  LYS A N   1 
ATOM   38   C CA  . LYS A 1 7   ? 39.971 31.494 -7.843  1.00 12.83  ? 688  LYS A CA  1 
ATOM   39   C C   . LYS A 1 7   ? 39.777 30.647 -6.591  1.00 12.52  ? 688  LYS A C   1 
ATOM   40   O O   . LYS A 1 7   ? 38.676 30.591 -6.026  1.00 13.45  ? 688  LYS A O   1 
ATOM   41   C CB  . LYS A 1 7   ? 40.090 30.588 -9.064  1.00 13.91  ? 688  LYS A CB  1 
ATOM   42   C CG  . LYS A 1 7   ? 38.985 29.551 -9.108  1.00 14.05  ? 688  LYS A CG  1 
ATOM   43   C CD  . LYS A 1 7   ? 39.010 28.728 -10.376 1.00 19.53  ? 688  LYS A CD  1 
ATOM   44   C CE  . LYS A 1 7   ? 37.789 27.804 -10.408 1.00 23.01  ? 688  LYS A CE  1 
ATOM   45   N NZ  . LYS A 1 7   ? 37.720 27.009 -11.664 1.00 37.16  ? 688  LYS A NZ  1 
ATOM   46   N N   . ASN A 1 8   ? 40.832 29.970 -6.144  1.00 12.59  ? 689  ASN A N   1 
ATOM   47   C CA  . ASN A 1 8   ? 40.670 29.025 -5.051  1.00 12.32  ? 689  ASN A CA  1 
ATOM   48   C C   . ASN A 1 8   ? 40.519 29.702 -3.700  1.00 11.45  ? 689  ASN A C   1 
ATOM   49   O O   . ASN A 1 8   ? 40.140 29.033 -2.736  1.00 11.13  ? 689  ASN A O   1 
ATOM   50   C CB  . ASN A 1 8   ? 41.842 28.044 -5.041  1.00 16.30  ? 689  ASN A CB  1 
ATOM   51   C CG  . ASN A 1 8   ? 41.755 27.042 -6.175  1.00 21.90  ? 689  ASN A CG  1 
ATOM   52   O OD1 . ASN A 1 8   ? 40.679 26.516 -6.469  1.00 27.68  ? 689  ASN A OD1 1 
ATOM   53   N ND2 . ASN A 1 8   ? 42.878 26.791 -6.831  1.00 26.87  ? 689  ASN A ND2 1 
ATOM   54   N N   . ALA A 1 9   ? 40.795 31.006 -3.608  1.00 11.02  ? 690  ALA A N   1 
ATOM   55   C CA  . ALA A 1 9   ? 40.499 31.774 -2.410  1.00 10.61  ? 690  ALA A CA  1 
ATOM   56   C C   . ALA A 1 9   ? 39.101 32.384 -2.421  1.00 9.76   ? 690  ALA A C   1 
ATOM   57   O O   . ALA A 1 9   ? 38.681 32.927 -1.398  1.00 10.12  ? 690  ALA A O   1 
ATOM   58   C CB  . ALA A 1 9   ? 41.531 32.888 -2.226  1.00 10.19  ? 690  ALA A CB  1 
ATOM   59   N N   . SER A 1 10  ? 38.366 32.287 -3.528  1.00 10.08  ? 691  SER A N   1 
ATOM   60   C CA  . SER A 1 10  ? 37.062 32.941 -3.663  1.00 9.80   ? 691  SER A CA  1 
ATOM   61   C C   . SER A 1 10  ? 35.971 32.035 -3.100  1.00 11.03  ? 691  SER A C   1 
ATOM   62   O O   . SER A 1 10  ? 35.642 31.003 -3.691  1.00 10.17  ? 691  SER A O   1 
ATOM   63   C CB  . SER A 1 10  ? 36.780 33.291 -5.124  1.00 10.35  ? 691  SER A CB  1 
ATOM   64   O OG  . SER A 1 10  ? 37.713 34.245 -5.617  1.00 11.76  ? 691  SER A OG  1 
ATOM   65   N N   . ALA A 1 11  ? 35.387 32.439 -1.977  1.00 14.47  ? 692  ALA A N   1 
ATOM   66   C CA  . ALA A 1 11  ? 34.373 31.651 -1.292  1.00 9.05   ? 692  ALA A CA  1 
ATOM   67   C C   . ALA A 1 11  ? 32.980 32.196 -1.572  1.00 11.49  ? 692  ALA A C   1 
ATOM   68   O O   . ALA A 1 11  ? 32.774 33.409 -1.631  1.00 8.86   ? 692  ALA A O   1 
ATOM   69   C CB  . ALA A 1 11  ? 34.616 31.640 0.218   1.00 11.36  ? 692  ALA A CB  1 
ATOM   70   N N   . LEU A 1 12  ? 32.031 31.285 -1.754  1.00 10.30  ? 693  LEU A N   1 
ATOM   71   C CA  . LEU A 1 12  ? 30.624 31.633 -1.682  1.00 13.39  ? 693  LEU A CA  1 
ATOM   72   C C   . LEU A 1 12  ? 30.222 31.772 -0.220  1.00 14.09  ? 693  LEU A C   1 
ATOM   73   O O   . LEU A 1 12  ? 30.678 31.006 0.630   1.00 12.85  ? 693  LEU A O   1 
ATOM   74   C CB  . LEU A 1 12  ? 29.792 30.552 -2.371  1.00 14.98  ? 693  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 12  ? 28.260 30.550 -2.301  1.00 14.49  ? 693  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 12  ? 27.683 31.725 -3.066  1.00 10.66  ? 693  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 12  ? 27.736 29.245 -2.882  1.00 14.22  ? 693  LEU A CD2 1 
ATOM   78   N N   . LEU A 1 13  ? 29.375 32.763 0.077   1.00 9.83   ? 694  LEU A N   1 
ATOM   79   C CA  . LEU A 1 13  ? 28.803 32.932 1.408   1.00 8.76   ? 694  LEU A CA  1 
ATOM   80   C C   . LEU A 1 13  ? 27.315 32.603 1.382   1.00 9.93   ? 694  LEU A C   1 
ATOM   81   O O   . LEU A 1 13  ? 26.609 32.982 0.448   1.00 12.71  ? 694  LEU A O   1 
ATOM   82   C CB  . LEU A 1 13  ? 28.990 34.365 1.926   1.00 8.42   ? 694  LEU A CB  1 
ATOM   83   C CG  . LEU A 1 13  ? 30.393 34.879 2.251   1.00 8.01   ? 694  LEU A CG  1 
ATOM   84   C CD1 . LEU A 1 13  ? 30.251 36.195 2.999   1.00 10.63  ? 694  LEU A CD1 1 
ATOM   85   C CD2 . LEU A 1 13  ? 31.155 33.867 3.080   1.00 7.86   ? 694  LEU A CD2 1 
ATOM   86   N N   . ARG A 1 14  ? 26.848 31.887 2.405   1.00 9.63   ? 695  ARG A N   1 
ATOM   87   C CA  . ARG A 1 14  ? 25.428 31.646 2.634   1.00 9.82   ? 695  ARG A CA  1 
ATOM   88   C C   . ARG A 1 14  ? 25.052 32.225 3.989   1.00 12.93  ? 695  ARG A C   1 
ATOM   89   O O   . ARG A 1 14  ? 25.713 31.942 4.992   1.00 14.42  ? 695  ARG A O   1 
ATOM   90   C CB  . ARG A 1 14  ? 25.103 30.143 2.587   1.00 10.82  ? 695  ARG A CB  1 
ATOM   91   C CG  . ARG A 1 14  ? 25.420 29.474 1.253   1.00 12.04  ? 695  ARG A CG  1 
ATOM   92   C CD  . ARG A 1 14  ? 24.867 28.034 1.225   1.00 12.51  ? 695  ARG A CD  1 
ATOM   93   N NE  . ARG A 1 14  ? 25.099 27.365 -0.052  1.00 19.47  ? 695  ARG A NE  1 
ATOM   94   C CZ  . ARG A 1 14  ? 26.132 26.571 -0.303  1.00 27.27  ? 695  ARG A CZ  1 
ATOM   95   N NH1 . ARG A 1 14  ? 27.073 26.354 0.601   1.00 25.38  ? 695  ARG A NH1 1 
ATOM   96   N NH2 . ARG A 1 14  ? 26.217 25.970 -1.488  1.00 21.08  ? 695  ARG A NH2 1 
ATOM   97   N N   . MET A 1 15  ? 24.012 33.055 4.020   1.00 12.51  ? 696  MET A N   1 
ATOM   98   C CA  . MET A 1 15  ? 23.596 33.725 5.244   1.00 10.05  ? 696  MET A CA  1 
ATOM   99   C C   . MET A 1 15  ? 22.182 33.290 5.597   1.00 12.34  ? 696  MET A C   1 
ATOM   100  O O   . MET A 1 15  ? 21.299 33.300 4.743   1.00 12.42  ? 696  MET A O   1 
ATOM   101  C CB  . MET A 1 15  ? 23.663 35.253 5.090   1.00 9.93   ? 696  MET A CB  1 
ATOM   102  C CG  . MET A 1 15  ? 25.061 35.802 4.779   1.00 12.06  ? 696  MET A CG  1 
ATOM   103  S SD  . MET A 1 15  ? 25.438 35.918 3.012   1.00 15.24  ? 696  MET A SD  1 
ATOM   104  C CE  . MET A 1 15  ? 24.382 37.280 2.502   1.00 13.68  ? 696  MET A CE  1 
ATOM   105  N N   . ASN A 1 16  ? 21.980 32.890 6.847   1.00 10.96  ? 697  ASN A N   1 
ATOM   106  C CA  . ASN A 1 16  ? 20.676 32.492 7.356   1.00 11.73  ? 697  ASN A CA  1 
ATOM   107  C C   . ASN A 1 16  ? 20.295 33.476 8.449   1.00 15.05  ? 697  ASN A C   1 
ATOM   108  O O   . ASN A 1 16  ? 20.784 33.378 9.577   1.00 12.95  ? 697  ASN A O   1 
ATOM   109  C CB  . ASN A 1 16  ? 20.715 31.060 7.866   1.00 15.27  ? 697  ASN A CB  1 
ATOM   110  C CG  . ASN A 1 16  ? 21.250 30.118 6.832   1.00 13.84  ? 697  ASN A CG  1 
ATOM   111  O OD1 . ASN A 1 16  ? 20.633 29.919 5.793   1.00 18.00  ? 697  ASN A OD1 1 
ATOM   112  N ND2 . ASN A 1 16  ? 22.430 29.551 7.093   1.00 20.00  ? 697  ASN A ND2 1 
ATOM   113  N N   . PHE A 1 17  ? 19.421 34.418 8.107   1.00 13.27  ? 698  PHE A N   1 
ATOM   114  C CA  . PHE A 1 17  ? 18.999 35.459 9.028   1.00 14.94  ? 698  PHE A CA  1 
ATOM   115  C C   . PHE A 1 17  ? 17.777 34.970 9.792   1.00 15.98  ? 698  PHE A C   1 
ATOM   116  O O   . PHE A 1 17  ? 16.723 34.719 9.196   1.00 14.48  ? 698  PHE A O   1 
ATOM   117  C CB  . PHE A 1 17  ? 18.689 36.755 8.281   1.00 13.64  ? 698  PHE A CB  1 
ATOM   118  C CG  . PHE A 1 17  ? 19.762 37.177 7.316   1.00 14.19  ? 698  PHE A CG  1 
ATOM   119  C CD1 . PHE A 1 17  ? 21.010 37.564 7.772   1.00 11.45  ? 698  PHE A CD1 1 
ATOM   120  C CD2 . PHE A 1 17  ? 19.514 37.197 5.951   1.00 19.59  ? 698  PHE A CD2 1 
ATOM   121  C CE1 . PHE A 1 17  ? 21.989 37.958 6.892   1.00 11.04  ? 698  PHE A CE1 1 
ATOM   122  C CE2 . PHE A 1 17  ? 20.492 37.600 5.062   1.00 13.64  ? 698  PHE A CE2 1 
ATOM   123  C CZ  . PHE A 1 17  ? 21.730 37.981 5.534   1.00 14.98  ? 698  PHE A CZ  1 
ATOM   124  N N   . VAL A 1 18  ? 17.918 34.851 11.106  1.00 16.05  ? 699  VAL A N   1 
ATOM   125  C CA  . VAL A 1 18  ? 16.881 34.301 11.967  1.00 15.47  ? 699  VAL A CA  1 
ATOM   126  C C   . VAL A 1 18  ? 16.173 35.436 12.693  1.00 19.91  ? 699  VAL A C   1 
ATOM   127  O O   . VAL A 1 18  ? 16.822 36.346 13.227  1.00 24.19  ? 699  VAL A O   1 
ATOM   128  C CB  . VAL A 1 18  ? 17.477 33.297 12.967  1.00 20.60  ? 699  VAL A CB  1 
ATOM   129  C CG1 . VAL A 1 18  ? 16.370 32.612 13.757  1.00 19.76  ? 699  VAL A CG1 1 
ATOM   130  C CG2 . VAL A 1 18  ? 18.365 32.290 12.245  1.00 24.12  ? 699  VAL A CG2 1 
ATOM   131  N N   . LYS A 1 19  ? 14.841 35.387 12.701  1.00 16.72  ? 700  LYS A N   1 
ATOM   132  C CA  . LYS A 1 19  ? 14.000 36.323 13.450  1.00 26.00  ? 700  LYS A CA  1 
ATOM   133  C C   . LYS A 1 19  ? 12.919 35.505 14.137  1.00 27.08  ? 700  LYS A C   1 
ATOM   134  O O   . LYS A 1 19  ? 12.039 34.956 13.465  1.00 26.52  ? 700  LYS A O   1 
ATOM   135  C CB  . LYS A 1 19  ? 13.373 37.378 12.538  1.00 25.46  ? 700  LYS A CB  1 
ATOM   136  C CG  . LYS A 1 19  ? 14.257 38.575 12.250  1.00 39.34  ? 700  LYS A CG  1 
ATOM   137  C CD  . LYS A 1 19  ? 14.110 39.631 13.331  1.00 44.17  ? 700  LYS A CD  1 
ATOM   138  C CE  . LYS A 1 19  ? 14.933 40.864 13.000  1.00 44.04  ? 700  LYS A CE  1 
ATOM   139  N NZ  . LYS A 1 19  ? 14.656 41.377 11.628  1.00 44.10  ? 700  LYS A NZ  1 
ATOM   140  N N   . GLY A 1 20  ? 12.969 35.434 15.460  1.00 26.44  ? 701  GLY A N   1 
ATOM   141  C CA  . GLY A 1 20  ? 12.040 34.566 16.164  1.00 26.84  ? 701  GLY A CA  1 
ATOM   142  C C   . GLY A 1 20  ? 12.299 33.130 15.751  1.00 25.49  ? 701  GLY A C   1 
ATOM   143  O O   . GLY A 1 20  ? 13.415 32.614 15.887  1.00 22.76  ? 701  GLY A O   1 
ATOM   144  N N   . ASN A 1 21  ? 11.272 32.472 15.212  1.00 21.16  ? 702  ASN A N   1 
ATOM   145  C CA  . ASN A 1 21  ? 11.405 31.116 14.696  1.00 26.35  ? 702  ASN A CA  1 
ATOM   146  C C   . ASN A 1 21  ? 11.288 31.060 13.174  1.00 20.25  ? 702  ASN A C   1 
ATOM   147  O O   . ASN A 1 21  ? 10.946 30.012 12.618  1.00 20.56  ? 702  ASN A O   1 
ATOM   148  C CB  . ASN A 1 21  ? 10.367 30.206 15.345  1.00 21.92  ? 702  ASN A CB  1 
ATOM   149  C CG  . ASN A 1 21  ? 8.976  30.783 15.268  1.00 23.35  ? 702  ASN A CG  1 
ATOM   150  O OD1 . ASN A 1 21  ? 8.671  31.559 14.367  1.00 29.46  ? 702  ASN A OD1 1 
ATOM   151  N ND2 . ASN A 1 21  ? 8.119  30.409 16.215  1.00 32.45  ? 702  ASN A ND2 1 
ATOM   152  N N   . GLN A 1 22  ? 11.549 32.171 12.493  1.00 19.75  ? 703  GLN A N   1 
ATOM   153  C CA  . GLN A 1 22  ? 11.515 32.238 11.040  1.00 21.29  ? 703  GLN A CA  1 
ATOM   154  C C   . GLN A 1 22  ? 12.890 32.639 10.521  1.00 22.96  ? 703  GLN A C   1 
ATOM   155  O O   . GLN A 1 22  ? 13.586 33.451 11.139  1.00 17.46  ? 703  GLN A O   1 
ATOM   156  C CB  . GLN A 1 22  ? 10.447 33.226 10.567  1.00 23.78  ? 703  GLN A CB  1 
ATOM   157  C CG  . GLN A 1 22  ? 9.011  32.796 10.906  1.00 23.11  ? 703  GLN A CG  1 
ATOM   158  C CD  . GLN A 1 22  ? 8.009  33.933 10.765  1.00 27.36  ? 703  GLN A CD  1 
ATOM   159  O OE1 . GLN A 1 22  ? 8.369  35.108 10.847  1.00 43.97  ? 703  GLN A OE1 1 
ATOM   160  N NE2 . GLN A 1 22  ? 6.743  33.588 10.556  1.00 37.44  ? 703  GLN A NE2 1 
ATOM   161  N N   . VAL A 1 23  ? 13.283 32.064 9.388   1.00 17.55  ? 704  VAL A N   1 
ATOM   162  C CA  A VAL A 1 23  ? 14.593 32.284 8.782   0.70 17.74  ? 704  VAL A CA  1 
ATOM   163  C CA  B VAL A 1 23  ? 14.580 32.352 8.801   0.30 17.77  ? 704  VAL A CA  1 
ATOM   164  C C   . VAL A 1 23  ? 14.397 32.686 7.326   1.00 18.71  ? 704  VAL A C   1 
ATOM   165  O O   . VAL A 1 23  ? 13.526 32.136 6.643   1.00 18.32  ? 704  VAL A O   1 
ATOM   166  C CB  A VAL A 1 23  ? 15.476 31.016 8.877   0.70 19.67  ? 704  VAL A CB  1 
ATOM   167  C CB  B VAL A 1 23  ? 15.575 31.185 9.017   0.30 19.80  ? 704  VAL A CB  1 
ATOM   168  C CG1 A VAL A 1 23  ? 16.742 31.156 8.029   0.70 17.38  ? 704  VAL A CG1 1 
ATOM   169  C CG1 B VAL A 1 23  ? 14.967 29.866 8.614   0.30 16.25  ? 704  VAL A CG1 1 
ATOM   170  C CG2 A VAL A 1 23  ? 15.841 30.733 10.315  0.70 21.70  ? 704  VAL A CG2 1 
ATOM   171  C CG2 B VAL A 1 23  ? 16.896 31.430 8.286   0.30 17.67  ? 704  VAL A CG2 1 
ATOM   172  N N   . LEU A 1 24  ? 15.181 33.654 6.860   1.00 18.08  ? 705  LEU A N   1 
ATOM   173  C CA  A LEU A 1 24  ? 15.317 33.959 5.445   0.50 16.72  ? 705  LEU A CA  1 
ATOM   174  C CA  B LEU A 1 24  ? 15.318 33.970 5.446   0.50 16.72  ? 705  LEU A CA  1 
ATOM   175  C C   . LEU A 1 24  ? 16.794 33.881 5.088   1.00 18.47  ? 705  LEU A C   1 
ATOM   176  O O   . LEU A 1 24  ? 17.653 34.222 5.903   1.00 17.34  ? 705  LEU A O   1 
ATOM   177  C CB  A LEU A 1 24  ? 14.754 35.339 5.107   0.50 20.39  ? 705  LEU A CB  1 
ATOM   178  C CB  B LEU A 1 24  ? 14.771 35.364 5.129   0.50 20.39  ? 705  LEU A CB  1 
ATOM   179  C CG  A LEU A 1 24  ? 13.245 35.509 5.291   0.50 17.33  ? 705  LEU A CG  1 
ATOM   180  C CG  B LEU A 1 24  ? 14.913 35.861 3.690   0.50 22.09  ? 705  LEU A CG  1 
ATOM   181  C CD1 A LEU A 1 24  ? 12.826 36.918 4.910   0.50 20.39  ? 705  LEU A CD1 1 
ATOM   182  C CD1 B LEU A 1 24  ? 14.293 34.865 2.724   0.50 17.58  ? 705  LEU A CD1 1 
ATOM   183  C CD2 A LEU A 1 24  ? 12.492 34.482 4.463   0.50 18.10  ? 705  LEU A CD2 1 
ATOM   184  C CD2 B LEU A 1 24  ? 14.282 37.234 3.529   0.50 19.54  ? 705  LEU A CD2 1 
ATOM   185  N N   . SER A 1 25  ? 17.088 33.413 3.877   1.00 25.84  ? 706  SER A N   1 
ATOM   186  C CA  . SER A 1 25  ? 18.465 33.181 3.468   1.00 20.27  ? 706  SER A CA  1 
ATOM   187  C C   . SER A 1 25  ? 18.857 34.072 2.297   1.00 17.59  ? 706  SER A C   1 
ATOM   188  O O   . SER A 1 25  ? 18.024 34.474 1.480   1.00 19.18  ? 706  SER A O   1 
ATOM   189  C CB  . SER A 1 25  ? 18.702 31.701 3.106   1.00 19.80  ? 706  SER A CB  1 
ATOM   190  O OG  . SER A 1 25  ? 17.822 31.242 2.094   1.00 23.33  ? 706  SER A OG  1 
ATOM   191  N N   . GLY A 1 26  ? 20.154 34.388 2.243   1.00 12.25  ? 707  GLY A N   1 
ATOM   192  C CA  . GLY A 1 26  ? 20.718 35.129 1.139   1.00 13.99  ? 707  GLY A CA  1 
ATOM   193  C C   . GLY A 1 26  ? 22.113 34.603 0.859   1.00 15.31  ? 707  GLY A C   1 
ATOM   194  O O   . GLY A 1 26  ? 22.618 33.742 1.581   1.00 13.00  ? 707  GLY A O   1 
ATOM   195  N N   . THR A 1 27  ? 22.721 35.103 -0.212  1.00 13.68  ? 708  THR A N   1 
ATOM   196  C CA  . THR A 1 27  ? 24.080 34.693 -0.525  1.00 10.70  ? 708  THR A CA  1 
ATOM   197  C C   . THR A 1 27  ? 24.948 35.907 -0.806  1.00 15.96  ? 708  THR A C   1 
ATOM   198  O O   . THR A 1 27  ? 24.467 37.000 -1.134  1.00 12.89  ? 708  THR A O   1 
ATOM   199  C CB  . THR A 1 27  ? 24.163 33.718 -1.727  1.00 13.89  ? 708  THR A CB  1 
ATOM   200  O OG1 . THR A 1 27  ? 23.841 34.404 -2.944  1.00 15.34  ? 708  THR A OG1 1 
ATOM   201  C CG2 . THR A 1 27  ? 23.216 32.533 -1.541  1.00 15.96  ? 708  THR A CG2 1 
ATOM   202  N N   . GLY A 1 28  ? 26.246 35.688 -0.652  1.00 13.20  ? 709  GLY A N   1 
ATOM   203  C CA  . GLY A 1 28  ? 27.236 36.683 -0.990  1.00 9.45   ? 709  GLY A CA  1 
ATOM   204  C C   . GLY A 1 28  ? 28.557 36.039 -1.361  1.00 10.29  ? 709  GLY A C   1 
ATOM   205  O O   . GLY A 1 28  ? 28.606 34.853 -1.714  1.00 9.40   ? 709  GLY A O   1 
ATOM   206  N N   . SER A 1 29  ? 29.641 36.813 -1.275  1.00 8.86   ? 710  SER A N   1 
ATOM   207  C CA  . SER A 1 29  ? 30.971 36.362 -1.662  1.00 8.74   ? 710  SER A CA  1 
ATOM   208  C C   . SER A 1 29  ? 31.992 36.845 -0.636  1.00 8.25   ? 710  SER A C   1 
ATOM   209  O O   . SER A 1 29  ? 31.749 37.800 0.106   1.00 8.06   ? 710  SER A O   1 
ATOM   210  C CB  . SER A 1 29  ? 31.354 36.877 -3.058  1.00 11.31  ? 710  SER A CB  1 
ATOM   211  O OG  . SER A 1 29  ? 30.331 36.610 -4.007  1.00 10.58  ? 710  SER A OG  1 
ATOM   212  N N   . ALA A 1 30  ? 33.141 36.155 -0.586  1.00 10.11  ? 711  ALA A N   1 
ATOM   213  C CA  . ALA A 1 30  ? 34.240 36.524 0.303   1.00 7.86   ? 711  ALA A CA  1 
ATOM   214  C C   . ALA A 1 30  ? 35.541 35.958 -0.258  1.00 8.05   ? 711  ALA A C   1 
ATOM   215  O O   . ALA A 1 30  ? 35.535 35.105 -1.149  1.00 10.68  ? 711  ALA A O   1 
ATOM   216  C CB  . ALA A 1 30  ? 34.003 36.021 1.735   1.00 8.53   ? 711  ALA A CB  1 
ATOM   217  N N   . THR A 1 31  ? 36.662 36.419 0.299   1.00 7.93   ? 712  THR A N   1 
ATOM   218  C CA  . THR A 1 31  ? 37.995 35.964 -0.109  1.00 8.22   ? 712  THR A CA  1 
ATOM   219  C C   . THR A 1 31  ? 38.791 35.506 1.102   1.00 9.24   ? 712  THR A C   1 
ATOM   220  O O   . THR A 1 31  ? 38.861 36.220 2.106   1.00 8.50   ? 712  THR A O   1 
ATOM   221  C CB  . THR A 1 31  ? 38.810 37.067 -0.809  1.00 8.44   ? 712  THR A CB  1 
ATOM   222  O OG1 . THR A 1 31  ? 38.097 37.582 -1.927  1.00 9.70   ? 712  THR A OG1 1 
ATOM   223  C CG2 . THR A 1 31  ? 40.157 36.498 -1.303  1.00 8.91   ? 712  THR A CG2 1 
ATOM   224  N N   . PHE A 1 32  ? 39.439 34.350 0.983   1.00 8.42   ? 713  PHE A N   1 
ATOM   225  C CA  . PHE A 1 32  ? 40.404 33.913 1.987   1.00 8.59   ? 713  PHE A CA  1 
ATOM   226  C C   . PHE A 1 32  ? 41.702 34.709 1.846   1.00 8.77   ? 713  PHE A C   1 
ATOM   227  O O   . PHE A 1 32  ? 42.331 34.692 0.782   1.00 9.20   ? 713  PHE A O   1 
ATOM   228  C CB  . PHE A 1 32  ? 40.674 32.411 1.837   1.00 8.91   ? 713  PHE A CB  1 
ATOM   229  C CG  . PHE A 1 32  ? 39.685 31.523 2.562   1.00 12.81  ? 713  PHE A CG  1 
ATOM   230  C CD1 . PHE A 1 32  ? 39.811 31.293 3.925   1.00 11.46  ? 713  PHE A CD1 1 
ATOM   231  C CD2 . PHE A 1 32  ? 38.647 30.896 1.875   1.00 12.47  ? 713  PHE A CD2 1 
ATOM   232  C CE1 . PHE A 1 32  ? 38.908 30.473 4.597   1.00 16.26  ? 713  PHE A CE1 1 
ATOM   233  C CE2 . PHE A 1 32  ? 37.742 30.073 2.541   1.00 13.97  ? 713  PHE A CE2 1 
ATOM   234  C CZ  . PHE A 1 32  ? 37.873 29.860 3.901   1.00 8.62   ? 713  PHE A CZ  1 
ATOM   235  N N   . ILE A 1 33  ? 42.088 35.416 2.911   1.00 8.62   ? 714  ILE A N   1 
ATOM   236  C CA  . ILE A 1 33  ? 43.347 36.162 2.970   1.00 9.52   ? 714  ILE A CA  1 
ATOM   237  C C   . ILE A 1 33  ? 44.257 35.660 4.078   1.00 11.58  ? 714  ILE A C   1 
ATOM   238  O O   . ILE A 1 33  ? 45.334 36.226 4.292   1.00 13.09  ? 714  ILE A O   1 
ATOM   239  C CB  . ILE A 1 33  ? 43.113 37.683 3.113   1.00 9.92   ? 714  ILE A CB  1 
ATOM   240  C CG1 . ILE A 1 33  ? 42.309 38.013 4.369   1.00 8.35   ? 714  ILE A CG1 1 
ATOM   241  C CG2 . ILE A 1 33  ? 42.429 38.235 1.887   1.00 11.94  ? 714  ILE A CG2 1 
ATOM   242  C CD1 . ILE A 1 33  ? 41.992 39.517 4.509   1.00 8.24   ? 714  ILE A CD1 1 
ATOM   243  N N   . ALA A 1 34  ? 43.854 34.596 4.762   1.00 10.35  ? 715  ALA A N   1 
ATOM   244  C CA  . ALA A 1 34  ? 44.664 33.819 5.686   1.00 9.60   ? 715  ALA A CA  1 
ATOM   245  C C   . ALA A 1 34  ? 44.036 32.437 5.713   1.00 12.28  ? 715  ALA A C   1 
ATOM   246  O O   . ALA A 1 34  ? 42.944 32.238 5.167   1.00 9.24   ? 715  ALA A O   1 
ATOM   247  C CB  . ALA A 1 34  ? 44.687 34.444 7.087   1.00 13.17  ? 715  ALA A CB  1 
ATOM   248  N N   . PRO A 1 35  ? 44.705 31.451 6.314   1.00 10.46  ? 716  PRO A N   1 
ATOM   249  C CA  . PRO A 1 35  ? 44.082 30.117 6.361   1.00 10.18  ? 716  PRO A CA  1 
ATOM   250  C C   . PRO A 1 35  ? 42.711 30.123 7.015   1.00 12.83  ? 716  PRO A C   1 
ATOM   251  O O   . PRO A 1 35  ? 41.876 29.274 6.686   1.00 9.58   ? 716  PRO A O   1 
ATOM   252  C CB  . PRO A 1 35  ? 45.092 29.279 7.156   1.00 12.24  ? 716  PRO A CB  1 
ATOM   253  C CG  . PRO A 1 35  ? 46.399 29.921 6.847   1.00 13.96  ? 716  PRO A CG  1 
ATOM   254  C CD  . PRO A 1 35  ? 46.112 31.406 6.762   1.00 11.25  ? 716  PRO A CD  1 
ATOM   255  N N   . ASN A 1 36  ? 42.430 31.094 7.885   1.00 11.18  ? 717  ASN A N   1 
ATOM   256  C CA  . ASN A 1 36  ? 41.179 31.083 8.628   1.00 14.51  ? 717  ASN A CA  1 
ATOM   257  C C   . ASN A 1 36  ? 40.585 32.485 8.736   1.00 12.51  ? 717  ASN A C   1 
ATOM   258  O O   . ASN A 1 36  ? 39.970 32.823 9.752   1.00 12.66  ? 717  ASN A O   1 
ATOM   259  C CB  . ASN A 1 36  ? 41.400 30.485 10.018  1.00 12.22  ? 717  ASN A CB  1 
ATOM   260  C CG  . ASN A 1 36  ? 42.291 31.352 10.885  1.00 21.97  ? 717  ASN A CG  1 
ATOM   261  O OD1 . ASN A 1 36  ? 43.053 32.187 10.385  1.00 19.10  ? 717  ASN A OD1 1 
ATOM   262  N ND2 . ASN A 1 36  ? 42.200 31.160 12.194  1.00 31.49  ? 717  ASN A ND2 1 
ATOM   263  N N   . VAL A 1 37  ? 40.783 33.321 7.715   1.00 9.32   ? 718  VAL A N   1 
ATOM   264  C CA  . VAL A 1 37  ? 40.310 34.706 7.738   1.00 8.00   ? 718  VAL A CA  1 
ATOM   265  C C   . VAL A 1 37  ? 39.726 35.050 6.377   1.00 7.79   ? 718  VAL A C   1 
ATOM   266  O O   . VAL A 1 37  ? 40.359 34.813 5.343   1.00 7.99   ? 718  VAL A O   1 
ATOM   267  C CB  . VAL A 1 37  ? 41.436 35.692 8.116   1.00 15.31  ? 718  VAL A CB  1 
ATOM   268  C CG1 . VAL A 1 37  ? 40.948 37.129 7.994   1.00 8.00   ? 718  VAL A CG1 1 
ATOM   269  C CG2 . VAL A 1 37  ? 41.949 35.408 9.529   1.00 11.81  ? 718  VAL A CG2 1 
ATOM   270  N N   . LEU A 1 38  ? 38.508 35.596 6.376   1.00 9.80   ? 719  LEU A N   1 
ATOM   271  C CA  . LEU A 1 38  ? 37.813 36.005 5.164   1.00 8.62   ? 719  LEU A CA  1 
ATOM   272  C C   . LEU A 1 38  ? 37.713 37.522 5.115   1.00 7.31   ? 719  LEU A C   1 
ATOM   273  O O   . LEU A 1 38  ? 37.485 38.164 6.143   1.00 10.77  ? 719  LEU A O   1 
ATOM   274  C CB  . LEU A 1 38  ? 36.395 35.428 5.113   1.00 8.59   ? 719  LEU A CB  1 
ATOM   275  C CG  . LEU A 1 38  ? 36.243 33.910 4.993   1.00 11.62  ? 719  LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 38  ? 34.786 33.503 5.197   1.00 16.90  ? 719  LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 38  ? 36.714 33.493 3.628   1.00 11.13  ? 719  LEU A CD2 1 
ATOM   278  N N   . LEU A 1 39  ? 37.836 38.083 3.915   1.00 7.39   ? 720  LEU A N   1 
ATOM   279  C CA  . LEU A 1 39  ? 37.528 39.484 3.660   1.00 8.00   ? 720  LEU A CA  1 
ATOM   280  C C   . LEU A 1 39  ? 36.194 39.562 2.933   1.00 8.46   ? 720  LEU A C   1 
ATOM   281  O O   . LEU A 1 39  ? 35.968 38.813 1.972   1.00 7.51   ? 720  LEU A O   1 
ATOM   282  C CB  . LEU A 1 39  ? 38.608 40.148 2.808   1.00 7.70   ? 720  LEU A CB  1 
ATOM   283  C CG  . LEU A 1 39  ? 38.334 41.597 2.396   1.00 7.77   ? 720  LEU A CG  1 
ATOM   284  C CD1 . LEU A 1 39  ? 38.523 42.520 3.596   1.00 12.79  ? 720  LEU A CD1 1 
ATOM   285  C CD2 . LEU A 1 39  ? 39.255 41.998 1.244   1.00 14.33  ? 720  LEU A CD2 1 
ATOM   286  N N   . THR A 1 40  ? 35.321 40.473 3.363   1.00 8.68   ? 721  THR A N   1 
ATOM   287  C CA  . THR A 1 40  ? 34.030 40.611 2.699   1.00 7.48   ? 721  THR A CA  1 
ATOM   288  C C   . THR A 1 40  ? 33.433 41.989 2.992   1.00 10.30  ? 721  THR A C   1 
ATOM   289  O O   . THR A 1 40  ? 34.072 42.858 3.599   1.00 9.35   ? 721  THR A O   1 
ATOM   290  C CB  . THR A 1 40  ? 33.079 39.486 3.126   1.00 8.31   ? 721  THR A CB  1 
ATOM   291  O OG1 . THR A 1 40  ? 31.931 39.474 2.277   1.00 7.66   ? 721  THR A OG1 1 
ATOM   292  C CG2 . THR A 1 40  ? 32.634 39.680 4.578   1.00 7.37   ? 721  THR A CG2 1 
ATOM   293  N N   . VAL A 1 41  ? 32.196 42.190 2.521   1.00 8.44   ? 722  VAL A N   1 
ATOM   294  C CA  . VAL A 1 41  ? 31.472 43.443 2.735   1.00 8.16   ? 722  VAL A CA  1 
ATOM   295  C C   . VAL A 1 41  ? 30.606 43.305 3.976   1.00 10.57  ? 722  VAL A C   1 
ATOM   296  O O   . VAL A 1 41  ? 30.071 42.227 4.283   1.00 8.74   ? 722  VAL A O   1 
ATOM   297  C CB  . VAL A 1 41  ? 30.607 43.843 1.520   1.00 10.87  ? 722  VAL A CB  1 
ATOM   298  C CG1 . VAL A 1 41  ? 31.467 44.235 0.329   1.00 12.84  ? 722  VAL A CG1 1 
ATOM   299  C CG2 . VAL A 1 41  ? 29.637 42.738 1.151   1.00 8.66   ? 722  VAL A CG2 1 
ATOM   300  N N   . ALA A 1 42  ? 30.438 44.418 4.688   1.00 8.83   ? 723  ALA A N   1 
ATOM   301  C CA  . ALA A 1 42  ? 29.634 44.380 5.896   1.00 8.66   ? 723  ALA A CA  1 
ATOM   302  C C   . ALA A 1 42  ? 28.167 44.126 5.582   1.00 10.74  ? 723  ALA A C   1 
ATOM   303  O O   . ALA A 1 42  ? 27.446 43.607 6.437   1.00 10.55  ? 723  ALA A O   1 
ATOM   304  C CB  . ALA A 1 42  ? 29.796 45.685 6.680   1.00 9.01   ? 723  ALA A CB  1 
ATOM   305  N N   . HIS A 1 43  ? 27.715 44.453 4.370   1.00 9.60   ? 724  HIS A N   1 
ATOM   306  C CA  . HIS A 1 43  ? 26.281 44.400 4.106   1.00 9.79   ? 724  HIS A CA  1 
ATOM   307  C C   . HIS A 1 43  ? 25.782 42.999 3.780   1.00 11.36  ? 724  HIS A C   1 
ATOM   308  O O   . HIS A 1 43  ? 24.577 42.825 3.569   1.00 10.25  ? 724  HIS A O   1 
ATOM   309  C CB  . HIS A 1 43  ? 25.892 45.396 3.007   1.00 10.29  ? 724  HIS A CB  1 
ATOM   310  C CG  . HIS A 1 43  ? 26.225 44.975 1.609   1.00 11.42  ? 724  HIS A CG  1 
ATOM   311  N ND1 . HIS A 1 43  ? 27.162 45.636 0.844   1.00 12.82  ? 724  HIS A ND1 1 
ATOM   312  C CD2 . HIS A 1 43  ? 25.697 44.017 0.810   1.00 21.27  ? 724  HIS A CD2 1 
ATOM   313  C CE1 . HIS A 1 43  ? 27.219 45.083 -0.355  1.00 16.60  ? 724  HIS A CE1 1 
ATOM   314  N NE2 . HIS A 1 43  ? 26.340 44.100 -0.402  1.00 22.94  ? 724  HIS A NE2 1 
ATOM   315  N N   . ASN A 1 44  ? 26.659 41.995 3.762   1.00 12.11  ? 725  ASN A N   1 
ATOM   316  C CA  . ASN A 1 44  ? 26.172 40.626 3.861   1.00 9.14   ? 725  ASN A CA  1 
ATOM   317  C C   . ASN A 1 44  ? 25.579 40.330 5.233   1.00 13.76  ? 725  ASN A C   1 
ATOM   318  O O   . ASN A 1 44  ? 24.864 39.330 5.375   1.00 10.69  ? 725  ASN A O   1 
ATOM   319  C CB  . ASN A 1 44  ? 27.299 39.631 3.549   1.00 12.88  ? 725  ASN A CB  1 
ATOM   320  C CG  . ASN A 1 44  ? 27.693 39.630 2.079   1.00 11.36  ? 725  ASN A CG  1 
ATOM   321  O OD1 . ASN A 1 44  ? 26.842 39.783 1.204   1.00 11.49  ? 725  ASN A OD1 1 
ATOM   322  N ND2 . ASN A 1 44  ? 29.003 39.475 1.801   1.00 11.62  ? 725  ASN A ND2 1 
ATOM   323  N N   . PHE A 1 45  ? 25.821 41.192 6.228   1.00 9.31   ? 726  PHE A N   1 
ATOM   324  C CA  . PHE A 1 45  ? 25.445 40.916 7.610   1.00 9.51   ? 726  PHE A CA  1 
ATOM   325  C C   . PHE A 1 45  ? 24.625 42.025 8.261   1.00 11.61  ? 726  PHE A C   1 
ATOM   326  O O   . PHE A 1 45  ? 23.835 41.755 9.174   1.00 10.60  ? 726  PHE A O   1 
ATOM   327  C CB  . PHE A 1 45  ? 26.688 40.678 8.459   1.00 11.73  ? 726  PHE A CB  1 
ATOM   328  C CG  . PHE A 1 45  ? 27.613 39.674 7.883   1.00 9.00   ? 726  PHE A CG  1 
ATOM   329  C CD1 . PHE A 1 45  ? 27.244 38.341 7.825   1.00 10.77  ? 726  PHE A CD1 1 
ATOM   330  C CD2 . PHE A 1 45  ? 28.857 40.053 7.401   1.00 12.89  ? 726  PHE A CD2 1 
ATOM   331  C CE1 . PHE A 1 45  ? 28.096 37.394 7.297   1.00 14.93  ? 726  PHE A CE1 1 
ATOM   332  C CE2 . PHE A 1 45  ? 29.713 39.118 6.867   1.00 16.87  ? 726  PHE A CE2 1 
ATOM   333  C CZ  . PHE A 1 45  ? 29.338 37.781 6.824   1.00 10.88  ? 726  PHE A CZ  1 
ATOM   334  N N   . ILE A 1 46  ? 24.825 43.273 7.834   1.00 10.28  ? 727  ILE A N   1 
ATOM   335  C CA  . ILE A 1 46  ? 24.156 44.404 8.466   1.00 10.98  ? 727  ILE A CA  1 
ATOM   336  C C   . ILE A 1 46  ? 23.480 45.276 7.418   1.00 15.00  ? 727  ILE A C   1 
ATOM   337  O O   . ILE A 1 46  ? 23.793 45.228 6.226   1.00 11.19  ? 727  ILE A O   1 
ATOM   338  C CB  . ILE A 1 46  ? 25.120 45.262 9.323   1.00 11.70  ? 727  ILE A CB  1 
ATOM   339  C CG1 . ILE A 1 46  ? 26.214 45.903 8.463   1.00 13.73  ? 727  ILE A CG1 1 
ATOM   340  C CG2 . ILE A 1 46  ? 25.735 44.429 10.437  1.00 21.46  ? 727  ILE A CG2 1 
ATOM   341  C CD1 . ILE A 1 46  ? 27.060 46.916 9.225   1.00 10.62  ? 727  ILE A CD1 1 
ATOM   342  N N   . ASN A 1 47  ? 22.522 46.071 7.898   1.00 13.13  ? 728  ASN A N   1 
ATOM   343  C CA  A ASN A 1 47  ? 21.848 47.081 7.092   0.70 16.73  ? 728  ASN A CA  1 
ATOM   344  C CA  B ASN A 1 47  ? 21.802 47.064 7.110   0.30 16.72  ? 728  ASN A CA  1 
ATOM   345  C C   . ASN A 1 47  ? 21.692 48.343 7.932   1.00 13.69  ? 728  ASN A C   1 
ATOM   346  O O   . ASN A 1 47  ? 22.103 48.395 9.096   1.00 15.07  ? 728  ASN A O   1 
ATOM   347  C CB  A ASN A 1 47  ? 20.489 46.576 6.586   0.70 16.25  ? 728  ASN A CB  1 
ATOM   348  C CB  B ASN A 1 47  ? 20.407 46.562 6.710   0.30 16.33  ? 728  ASN A CB  1 
ATOM   349  C CG  A ASN A 1 47  ? 19.617 46.035 7.704   0.70 21.07  ? 728  ASN A CG  1 
ATOM   350  C CG  B ASN A 1 47  ? 20.375 45.957 5.324   0.30 15.30  ? 728  ASN A CG  1 
ATOM   351  O OD1 A ASN A 1 47  ? 19.771 46.408 8.870   0.70 17.75  ? 728  ASN A OD1 1 
ATOM   352  O OD1 B ASN A 1 47  ? 21.035 46.440 4.408   0.30 18.77  ? 728  ASN A OD1 1 
ATOM   353  N ND2 A ASN A 1 47  ? 18.699 45.134 7.353   0.70 26.17  ? 728  ASN A ND2 1 
ATOM   354  N ND2 B ASN A 1 47  ? 19.592 44.894 5.160   0.30 17.69  ? 728  ASN A ND2 1 
ATOM   355  N N   . ASN A 1 48  ? 21.097 49.374 7.336   1.00 14.45  ? 729  ASN A N   1 
ATOM   356  C CA  . ASN A 1 48  ? 20.887 50.627 8.052   1.00 17.45  ? 729  ASN A CA  1 
ATOM   357  C C   . ASN A 1 48  ? 19.867 50.464 9.165   1.00 17.98  ? 729  ASN A C   1 
ATOM   358  O O   . ASN A 1 48  ? 18.856 49.767 9.011   1.00 18.75  ? 729  ASN A O   1 
ATOM   359  C CB  . ASN A 1 48  ? 20.406 51.719 7.103   1.00 16.06  ? 729  ASN A CB  1 
ATOM   360  C CG  . ASN A 1 48  ? 21.507 52.234 6.217   1.00 21.89  ? 729  ASN A CG  1 
ATOM   361  O OD1 . ASN A 1 48  ? 22.614 51.687 6.203   1.00 19.16  ? 729  ASN A OD1 1 
ATOM   362  N ND2 . ASN A 1 48  ? 21.217 53.285 5.465   1.00 20.74  ? 729  ASN A ND2 1 
ATOM   363  N N   . SER A 1 49  ? 20.124 51.130 10.289  1.00 16.62  ? 730  SER A N   1 
ATOM   364  C CA  . SER A 1 49  ? 19.095 51.225 11.306  1.00 17.61  ? 730  SER A CA  1 
ATOM   365  C C   . SER A 1 49  ? 17.914 52.026 10.759  1.00 18.83  ? 730  SER A C   1 
ATOM   366  O O   . SER A 1 49  ? 17.977 52.618 9.676   1.00 18.86  ? 730  SER A O   1 
ATOM   367  C CB  . SER A 1 49  ? 19.650 51.854 12.583  1.00 17.96  ? 730  SER A CB  1 
ATOM   368  O OG  . SER A 1 49  ? 20.074 53.191 12.373  1.00 18.38  ? 730  SER A OG  1 
ATOM   369  N N   . ALA A 1 50  ? 16.818 52.012 11.515  1.00 19.96  ? 731  ALA A N   1 
ATOM   370  C CA  . ALA A 1 50  ? 15.589 52.645 11.048  1.00 21.28  ? 731  ALA A CA  1 
ATOM   371  C C   . ALA A 1 50  ? 15.816 54.113 10.704  1.00 25.05  ? 731  ALA A C   1 
ATOM   372  O O   . ALA A 1 50  ? 15.246 54.628 9.733   1.00 24.39  ? 731  ALA A O   1 
ATOM   373  C CB  . ALA A 1 50  ? 14.494 52.501 12.106  1.00 22.55  ? 731  ALA A CB  1 
ATOM   374  N N   . ASP A 1 51  ? 16.653 54.800 11.477  1.00 21.86  ? 732  ASP A N   1 
ATOM   375  C CA  . ASP A 1 51  ? 16.898 56.216 11.257  1.00 22.57  ? 732  ASP A CA  1 
ATOM   376  C C   . ASP A 1 51  ? 18.220 56.484 10.547  1.00 21.44  ? 732  ASP A C   1 
ATOM   377  O O   . ASP A 1 51  ? 18.662 57.637 10.506  1.00 21.93  ? 732  ASP A O   1 
ATOM   378  C CB  . ASP A 1 51  ? 16.839 56.981 12.586  1.00 27.77  ? 732  ASP A CB  1 
ATOM   379  C CG  . ASP A 1 51  ? 17.926 56.563 13.569  1.00 22.80  ? 732  ASP A CG  1 
ATOM   380  O OD1 . ASP A 1 51  ? 18.760 55.701 13.239  1.00 21.36  ? 732  ASP A OD1 1 
ATOM   381  O OD2 . ASP A 1 51  ? 17.949 57.122 14.688  1.00 34.45  ? 732  ASP A OD2 1 
ATOM   382  N N   . ASN A 1 52  ? 18.858 55.449 9.995   1.00 20.05  ? 733  ASN A N   1 
ATOM   383  C CA  . ASN A 1 52  ? 20.149 55.521 9.310   1.00 20.17  ? 733  ASN A CA  1 
ATOM   384  C C   . ASN A 1 52  ? 21.285 55.970 10.216  1.00 18.70  ? 733  ASN A C   1 
ATOM   385  O O   . ASN A 1 52  ? 22.355 56.326 9.715   1.00 18.11  ? 733  ASN A O   1 
ATOM   386  C CB  . ASN A 1 52  ? 20.111 56.448 8.090   1.00 19.37  ? 733  ASN A CB  1 
ATOM   387  C CG  . ASN A 1 52  ? 19.110 56.004 7.055   1.00 21.91  ? 733  ASN A CG  1 
ATOM   388  O OD1 . ASN A 1 52  ? 18.930 54.808 6.828   1.00 20.03  ? 733  ASN A OD1 1 
ATOM   389  N ND2 . ASN A 1 52  ? 18.444 56.960 6.421   1.00 20.75  ? 733  ASN A ND2 1 
ATOM   390  N N   . SER A 1 53  ? 21.097 55.963 11.532  1.00 19.21  ? 734  SER A N   1 
ATOM   391  C CA  . SER A 1 53  ? 22.158 56.441 12.404  1.00 19.15  ? 734  SER A CA  1 
ATOM   392  C C   . SER A 1 53  ? 23.237 55.397 12.657  1.00 19.91  ? 734  SER A C   1 
ATOM   393  O O   . SER A 1 53  ? 24.329 55.763 13.095  1.00 20.04  ? 734  SER A O   1 
ATOM   394  C CB  . SER A 1 53  ? 21.582 56.916 13.740  1.00 20.40  ? 734  SER A CB  1 
ATOM   395  O OG  . SER A 1 53  ? 21.022 55.837 14.468  1.00 20.31  ? 734  SER A OG  1 
ATOM   396  N N   . THR A 1 54  ? 22.970 54.118 12.391  1.00 19.94  ? 735  THR A N   1 
ATOM   397  C CA  . THR A 1 54  ? 23.968 53.095 12.677  1.00 16.42  ? 735  THR A CA  1 
ATOM   398  C C   . THR A 1 54  ? 23.699 51.859 11.830  1.00 15.12  ? 735  THR A C   1 
ATOM   399  O O   . THR A 1 54  ? 22.592 51.654 11.329  1.00 15.49  ? 735  THR A O   1 
ATOM   400  C CB  . THR A 1 54  ? 23.976 52.723 14.165  1.00 22.98  ? 735  THR A CB  1 
ATOM   401  O OG1 . THR A 1 54  ? 24.998 51.746 14.413  1.00 17.45  ? 735  THR A OG1 1 
ATOM   402  C CG2 . THR A 1 54  ? 22.632 52.151 14.574  1.00 22.21  ? 735  THR A CG2 1 
ATOM   403  N N   . GLY A 1 55  ? 24.744 51.054 11.658  1.00 19.48  ? 736  GLY A N   1 
ATOM   404  C CA  . GLY A 1 55  ? 24.564 49.709 11.140  1.00 13.34  ? 736  GLY A CA  1 
ATOM   405  C C   . GLY A 1 55  ? 23.967 48.795 12.194  1.00 16.63  ? 736  GLY A C   1 
ATOM   406  O O   . GLY A 1 55  ? 24.139 48.989 13.396  1.00 13.95  ? 736  GLY A O   1 
ATOM   407  N N   . GLU A 1 56  ? 23.247 47.779 11.727  1.00 18.85  ? 737  GLU A N   1 
ATOM   408  C CA  . GLU A 1 56  ? 22.417 46.952 12.589  1.00 13.75  ? 737  GLU A CA  1 
ATOM   409  C C   . GLU A 1 56  ? 22.328 45.577 11.951  1.00 13.09  ? 737  GLU A C   1 
ATOM   410  O O   . GLU A 1 56  ? 22.168 45.471 10.735  1.00 12.83  ? 737  GLU A O   1 
ATOM   411  C CB  . GLU A 1 56  ? 21.016 47.566 12.747  1.00 15.19  ? 737  GLU A CB  1 
ATOM   412  C CG  . GLU A 1 56  ? 20.034 46.749 13.559  1.00 16.03  ? 737  GLU A CG  1 
ATOM   413  C CD  . GLU A 1 56  ? 18.696 47.458 13.769  1.00 26.40  ? 737  GLU A CD  1 
ATOM   414  O OE1 . GLU A 1 56  ? 18.667 48.710 13.783  1.00 24.30  ? 737  GLU A OE1 1 
ATOM   415  O OE2 . GLU A 1 56  ? 17.669 46.759 13.928  1.00 47.09  ? 737  GLU A OE2 1 
ATOM   416  N N   . PHE A 1 57  ? 22.438 44.532 12.766  1.00 12.92  ? 738  PHE A N   1 
ATOM   417  C CA  . PHE A 1 57  ? 22.446 43.183 12.214  1.00 14.06  ? 738  PHE A CA  1 
ATOM   418  C C   . PHE A 1 57  ? 21.140 42.868 11.497  1.00 13.43  ? 738  PHE A C   1 
ATOM   419  O O   . PHE A 1 57  ? 20.049 43.198 11.970  1.00 13.78  ? 738  PHE A O   1 
ATOM   420  C CB  . PHE A 1 57  ? 22.687 42.149 13.315  1.00 16.61  ? 738  PHE A CB  1 
ATOM   421  C CG  . PHE A 1 57  ? 24.121 41.753 13.464  1.00 14.48  ? 738  PHE A CG  1 
ATOM   422  C CD1 . PHE A 1 57  ? 24.642 40.698 12.732  1.00 15.54  ? 738  PHE A CD1 1 
ATOM   423  C CD2 . PHE A 1 57  ? 24.953 42.435 14.339  1.00 18.79  ? 738  PHE A CD2 1 
ATOM   424  C CE1 . PHE A 1 57  ? 25.969 40.332 12.868  1.00 18.94  ? 738  PHE A CE1 1 
ATOM   425  C CE2 . PHE A 1 57  ? 26.275 42.071 14.479  1.00 18.46  ? 738  PHE A CE2 1 
ATOM   426  C CZ  . PHE A 1 57  ? 26.783 41.023 13.744  1.00 15.41  ? 738  PHE A CZ  1 
ATOM   427  N N   . ILE A 1 58  ? 21.268 42.234 10.332  1.00 15.38  ? 739  ILE A N   1 
ATOM   428  C CA  . ILE A 1 58  ? 20.135 41.584 9.696   1.00 15.76  ? 739  ILE A CA  1 
ATOM   429  C C   . ILE A 1 58  ? 19.805 40.318 10.472  1.00 13.50  ? 739  ILE A C   1 
ATOM   430  O O   . ILE A 1 58  ? 20.685 39.485 10.730  1.00 14.57  ? 739  ILE A O   1 
ATOM   431  C CB  . ILE A 1 58  ? 20.450 41.268 8.227   1.00 13.15  ? 739  ILE A CB  1 
ATOM   432  C CG1 . ILE A 1 58  ? 20.868 42.534 7.483   1.00 17.18  ? 739  ILE A CG1 1 
ATOM   433  C CG2 . ILE A 1 58  ? 19.248 40.633 7.556   1.00 14.82  ? 739  ILE A CG2 1 
ATOM   434  C CD1 . ILE A 1 58  ? 21.401 42.261 6.100   1.00 20.49  ? 739  ILE A CD1 1 
ATOM   435  N N   . GLY A 1 59  ? 18.537 40.169 10.855  1.00 13.87  ? 740  GLY A N   1 
ATOM   436  C CA  . GLY A 1 59  ? 18.142 39.048 11.689  1.00 14.16  ? 740  GLY A CA  1 
ATOM   437  C C   . GLY A 1 59  ? 18.647 39.231 13.112  1.00 25.39  ? 740  GLY A C   1 
ATOM   438  O O   . GLY A 1 59  ? 19.125 40.296 13.508  1.00 25.15  ? 740  GLY A O   1 
ATOM   439  N N   . ASP A 1 60  ? 18.557 38.149 13.879  1.00 16.13  ? 741  ASP A N   1 
ATOM   440  C CA  . ASP A 1 60  ? 18.974 38.130 15.276  1.00 20.62  ? 741  ASP A CA  1 
ATOM   441  C C   . ASP A 1 60  ? 20.405 37.605 15.372  1.00 19.21  ? 741  ASP A C   1 
ATOM   442  O O   . ASP A 1 60  ? 20.653 36.421 15.113  1.00 17.93  ? 741  ASP A O   1 
ATOM   443  C CB  . ASP A 1 60  ? 18.027 37.267 16.107  1.00 19.60  ? 741  ASP A CB  1 
ATOM   444  C CG  . ASP A 1 60  ? 18.253 37.420 17.595  1.00 23.17  ? 741  ASP A CG  1 
ATOM   445  O OD1 . ASP A 1 60  ? 19.387 37.751 18.012  1.00 25.83  ? 741  ASP A OD1 1 
ATOM   446  O OD2 . ASP A 1 60  ? 17.290 37.207 18.357  1.00 24.24  ? 741  ASP A OD2 1 
ATOM   447  N N   . LYS A 1 61  ? 21.331 38.473 15.787  1.00 15.00  ? 742  LYS A N   1 
ATOM   448  C CA  . LYS A 1 61  ? 22.750 38.122 15.753  1.00 22.02  ? 742  LYS A CA  1 
ATOM   449  C C   . LYS A 1 61  ? 23.064 36.897 16.602  1.00 17.97  ? 742  LYS A C   1 
ATOM   450  O O   . LYS A 1 61  ? 24.014 36.165 16.302  1.00 26.68  ? 742  LYS A O   1 
ATOM   451  C CB  . LYS A 1 61  ? 23.599 39.312 16.203  1.00 15.51  ? 742  LYS A CB  1 
ATOM   452  C CG  . LYS A 1 61  ? 23.347 39.747 17.621  1.00 20.81  ? 742  LYS A CG  1 
ATOM   453  C CD  . LYS A 1 61  ? 24.316 40.846 18.029  1.00 31.72  ? 742  LYS A CD  1 
ATOM   454  C CE  . LYS A 1 61  ? 23.975 41.383 19.405  1.00 33.91  ? 742  LYS A CE  1 
ATOM   455  N NZ  . LYS A 1 61  ? 22.638 42.042 19.427  1.00 35.82  ? 742  LYS A NZ  1 
ATOM   456  N N   . SER A 1 62  ? 22.297 36.655 17.664  1.00 18.35  ? 743  SER A N   1 
ATOM   457  C CA  A SER A 1 62  ? 22.517 35.479 18.496  0.70 20.47  ? 743  SER A CA  1 
ATOM   458  C CA  B SER A 1 62  ? 22.516 35.480 18.497  0.30 20.51  ? 743  SER A CA  1 
ATOM   459  C C   . SER A 1 62  ? 21.976 34.202 17.873  1.00 22.96  ? 743  SER A C   1 
ATOM   460  O O   . SER A 1 62  ? 22.293 33.113 18.362  1.00 26.76  ? 743  SER A O   1 
ATOM   461  C CB  A SER A 1 62  ? 21.881 35.674 19.875  0.70 21.90  ? 743  SER A CB  1 
ATOM   462  C CB  B SER A 1 62  ? 21.874 35.677 19.872  0.30 21.91  ? 743  SER A CB  1 
ATOM   463  O OG  A SER A 1 62  ? 22.548 36.688 20.602  0.70 29.14  ? 743  SER A OG  1 
ATOM   464  O OG  B SER A 1 62  ? 20.467 35.530 19.796  0.30 16.99  ? 743  SER A OG  1 
ATOM   465  N N   . LYS A 1 63  ? 21.168 34.307 16.817  1.00 18.31  ? 744  LYS A N   1 
ATOM   466  C CA  . LYS A 1 63  ? 20.566 33.143 16.185  1.00 17.67  ? 744  LYS A CA  1 
ATOM   467  C C   . LYS A 1 63  ? 21.042 32.905 14.762  1.00 15.92  ? 744  LYS A C   1 
ATOM   468  O O   . LYS A 1 63  ? 20.984 31.762 14.298  1.00 16.47  ? 744  LYS A O   1 
ATOM   469  C CB  . LYS A 1 63  ? 19.035 33.273 16.167  1.00 14.70  ? 744  LYS A CB  1 
ATOM   470  C CG  . LYS A 1 63  ? 18.381 33.453 17.523  1.00 17.59  ? 744  LYS A CG  1 
ATOM   471  C CD  . LYS A 1 63  ? 16.865 33.426 17.376  1.00 27.79  ? 744  LYS A CD  1 
ATOM   472  C CE  . LYS A 1 63  ? 16.176 33.922 18.638  1.00 32.11  ? 744  LYS A CE  1 
ATOM   473  N NZ  . LYS A 1 63  ? 14.722 34.154 18.424  1.00 36.93  ? 744  LYS A NZ  1 
ATOM   474  N N   . ASN A 1 64  ? 21.501 33.945 14.065  1.00 12.36  ? 745  ASN A N   1 
ATOM   475  C CA  . ASN A 1 64  ? 21.942 33.797 12.686  1.00 17.47  ? 745  ASN A CA  1 
ATOM   476  C C   . ASN A 1 64  ? 23.017 32.726 12.577  1.00 16.43  ? 745  ASN A C   1 
ATOM   477  O O   . ASN A 1 64  ? 23.734 32.431 13.534  1.00 20.89  ? 745  ASN A O   1 
ATOM   478  C CB  . ASN A 1 64  ? 22.490 35.122 12.144  1.00 14.24  ? 745  ASN A CB  1 
ATOM   479  C CG  . ASN A 1 64  ? 21.444 36.218 12.101  1.00 15.59  ? 745  ASN A CG  1 
ATOM   480  O OD1 . ASN A 1 64  ? 20.248 35.946 12.014  1.00 13.01  ? 745  ASN A OD1 1 
ATOM   481  N ND2 . ASN A 1 64  ? 21.896 37.473 12.155  1.00 12.37  ? 745  ASN A ND2 1 
ATOM   482  N N   . THR A 1 65  ? 23.104 32.121 11.400  1.00 13.52  ? 746  THR A N   1 
ATOM   483  C CA  . THR A 1 65  ? 24.183 31.210 11.065  1.00 13.92  ? 746  THR A CA  1 
ATOM   484  C C   . THR A 1 65  ? 24.671 31.576 9.677   1.00 18.17  ? 746  THR A C   1 
ATOM   485  O O   . THR A 1 65  ? 23.886 32.012 8.833   1.00 12.63  ? 746  THR A O   1 
ATOM   486  C CB  . THR A 1 65  ? 23.734 29.746 11.102  1.00 17.51  ? 746  THR A CB  1 
ATOM   487  O OG1 . THR A 1 65  ? 22.677 29.554 10.158  1.00 14.51  ? 746  THR A OG1 1 
ATOM   488  C CG2 . THR A 1 65  ? 23.220 29.384 12.485  1.00 14.99  ? 746  THR A CG2 1 
ATOM   489  N N   . TYR A 1 66  ? 25.971 31.426 9.453   1.00 12.07  ? 747  TYR A N   1 
ATOM   490  C CA  . TYR A 1 66  ? 26.563 31.734 8.163   1.00 15.13  ? 747  TYR A CA  1 
ATOM   491  C C   . TYR A 1 66  ? 27.506 30.607 7.761   1.00 11.80  ? 747  TYR A C   1 
ATOM   492  O O   . TYR A 1 66  ? 27.985 29.839 8.599   1.00 15.49  ? 747  TYR A O   1 
ATOM   493  C CB  . TYR A 1 66  ? 27.307 33.067 8.188   1.00 12.80  ? 747  TYR A CB  1 
ATOM   494  C CG  . TYR A 1 66  ? 26.611 34.167 8.946   1.00 12.13  ? 747  TYR A CG  1 
ATOM   495  C CD1 . TYR A 1 66  ? 25.675 34.985 8.324   1.00 11.43  ? 747  TYR A CD1 1 
ATOM   496  C CD2 . TYR A 1 66  ? 26.910 34.406 10.279  1.00 13.95  ? 747  TYR A CD2 1 
ATOM   497  C CE1 . TYR A 1 66  ? 25.036 36.010 9.028   1.00 13.29  ? 747  TYR A CE1 1 
ATOM   498  C CE2 . TYR A 1 66  ? 26.287 35.420 10.986  1.00 12.71  ? 747  TYR A CE2 1 
ATOM   499  C CZ  . TYR A 1 66  ? 25.352 36.220 10.357  1.00 14.01  ? 747  TYR A CZ  1 
ATOM   500  O OH  . TYR A 1 66  ? 24.733 37.220 11.070  1.00 14.73  ? 747  TYR A OH  1 
ATOM   501  N N   . GLU A 1 67  ? 27.767 30.520 6.460   1.00 11.62  ? 748  GLU A N   1 
ATOM   502  C CA  A GLU A 1 67  ? 28.523 29.410 5.904   0.50 13.66  ? 748  GLU A CA  1 
ATOM   503  C CA  B GLU A 1 67  ? 28.506 29.403 5.890   0.50 13.64  ? 748  GLU A CA  1 
ATOM   504  C C   . GLU A 1 67  ? 29.357 29.913 4.733   1.00 12.79  ? 748  GLU A C   1 
ATOM   505  O O   . GLU A 1 67  ? 28.936 30.808 4.002   1.00 15.72  ? 748  GLU A O   1 
ATOM   506  C CB  A GLU A 1 67  ? 27.581 28.285 5.457   0.50 17.13  ? 748  GLU A CB  1 
ATOM   507  C CB  B GLU A 1 67  ? 27.524 28.307 5.441   0.50 17.15  ? 748  GLU A CB  1 
ATOM   508  C CG  A GLU A 1 67  ? 28.232 26.929 5.305   0.50 19.50  ? 748  GLU A CG  1 
ATOM   509  C CG  B GLU A 1 67  ? 27.992 27.319 4.380   0.50 17.03  ? 748  GLU A CG  1 
ATOM   510  C CD  A GLU A 1 67  ? 27.214 25.801 5.239   0.50 18.13  ? 748  GLU A CD  1 
ATOM   511  C CD  B GLU A 1 67  ? 26.875 26.353 3.991   0.50 19.05  ? 748  GLU A CD  1 
ATOM   512  O OE1 A GLU A 1 67  ? 26.002 26.088 5.129   0.50 24.35  ? 748  GLU A OE1 1 
ATOM   513  O OE1 B GLU A 1 67  ? 25.898 26.240 4.763   0.50 23.92  ? 748  GLU A OE1 1 
ATOM   514  O OE2 A GLU A 1 67  ? 27.630 24.629 5.307   0.50 21.93  ? 748  GLU A OE2 1 
ATOM   515  O OE2 B GLU A 1 67  ? 26.961 25.718 2.919   0.50 20.68  ? 748  GLU A OE2 1 
ATOM   516  N N   . TRP A 1 68  ? 30.556 29.352 4.583   1.00 11.52  ? 749  TRP A N   1 
ATOM   517  C CA  . TRP A 1 68  ? 31.406 29.631 3.434   1.00 11.44  ? 749  TRP A CA  1 
ATOM   518  C C   . TRP A 1 68  ? 31.635 28.338 2.663   1.00 13.23  ? 749  TRP A C   1 
ATOM   519  O O   . TRP A 1 68  ? 31.606 27.248 3.238   1.00 11.71  ? 749  TRP A O   1 
ATOM   520  C CB  . TRP A 1 68  ? 32.755 30.235 3.853   1.00 12.70  ? 749  TRP A CB  1 
ATOM   521  C CG  . TRP A 1 68  ? 33.542 29.369 4.780   1.00 12.30  ? 749  TRP A CG  1 
ATOM   522  C CD1 . TRP A 1 68  ? 33.563 29.423 6.142   1.00 13.83  ? 749  TRP A CD1 1 
ATOM   523  C CD2 . TRP A 1 68  ? 34.439 28.321 4.407   1.00 10.97  ? 749  TRP A CD2 1 
ATOM   524  N NE1 . TRP A 1 68  ? 34.415 28.462 6.641   1.00 13.71  ? 749  TRP A NE1 1 
ATOM   525  C CE2 . TRP A 1 68  ? 34.967 27.776 5.593   1.00 14.47  ? 749  TRP A CE2 1 
ATOM   526  C CE3 . TRP A 1 68  ? 34.856 27.798 3.182   1.00 12.16  ? 749  TRP A CE3 1 
ATOM   527  C CZ2 . TRP A 1 68  ? 35.891 26.726 5.590   1.00 11.42  ? 749  TRP A CZ2 1 
ATOM   528  C CZ3 . TRP A 1 68  ? 35.773 26.752 3.185   1.00 12.01  ? 749  TRP A CZ3 1 
ATOM   529  C CH2 . TRP A 1 68  ? 36.269 26.227 4.379   1.00 11.55  ? 749  TRP A CH2 1 
ATOM   530  N N   . GLN A 1 69  ? 31.868 28.458 1.355   1.00 11.38  ? 750  GLN A N   1 
ATOM   531  C CA  . GLN A 1 69  ? 32.130 27.280 0.530   1.00 11.77  ? 750  GLN A CA  1 
ATOM   532  C C   . GLN A 1 69  ? 33.114 27.645 -0.570  1.00 13.34  ? 750  GLN A C   1 
ATOM   533  O O   . GLN A 1 69  ? 32.910 28.639 -1.270  1.00 11.74  ? 750  GLN A O   1 
ATOM   534  C CB  . GLN A 1 69  ? 30.833 26.739 -0.078  1.00 12.28  ? 750  GLN A CB  1 
ATOM   535  C CG  . GLN A 1 69  ? 31.025 25.511 -0.963  1.00 21.47  ? 750  GLN A CG  1 
ATOM   536  C CD  . GLN A 1 69  ? 29.702 24.949 -1.449  1.00 18.47  ? 750  GLN A CD  1 
ATOM   537  O OE1 . GLN A 1 69  ? 28.786 24.742 -0.661  1.00 17.86  ? 750  GLN A OE1 1 
ATOM   538  N NE2 . GLN A 1 69  ? 29.592 24.716 -2.756  1.00 20.69  ? 750  GLN A NE2 1 
ATOM   539  N N   . THR A 1 70  ? 34.163 26.834 -0.736  1.00 11.73  ? 751  THR A N   1 
ATOM   540  C CA  . THR A 1 70  ? 35.185 27.102 -1.738  1.00 11.64  ? 751  THR A CA  1 
ATOM   541  C C   . THR A 1 70  ? 34.964 26.252 -2.986  1.00 13.39  ? 751  THR A C   1 
ATOM   542  O O   . THR A 1 70  ? 34.199 25.285 -2.961  1.00 18.75  ? 751  THR A O   1 
ATOM   543  C CB  . THR A 1 70  ? 36.580 26.843 -1.150  1.00 13.91  ? 751  THR A CB  1 
ATOM   544  O OG1 . THR A 1 70  ? 36.575 25.630 -0.390  1.00 17.94  ? 751  THR A OG1 1 
ATOM   545  C CG2 . THR A 1 70  ? 36.991 27.992 -0.241  1.00 16.70  ? 751  THR A CG2 1 
ATOM   546  N N   . PRO A 1 71  ? 35.614 26.591 -4.112  1.00 17.27  ? 752  PRO A N   1 
ATOM   547  C CA  . PRO A 1 71  ? 35.352 25.846 -5.359  1.00 12.66  ? 752  PRO A CA  1 
ATOM   548  C C   . PRO A 1 71  ? 35.614 24.356 -5.267  1.00 15.48  ? 752  PRO A C   1 
ATOM   549  O O   . PRO A 1 71  ? 34.961 23.585 -5.985  1.00 19.58  ? 752  PRO A O   1 
ATOM   550  C CB  . PRO A 1 71  ? 36.294 26.521 -6.364  1.00 12.50  ? 752  PRO A CB  1 
ATOM   551  C CG  . PRO A 1 71  ? 36.393 27.944 -5.863  1.00 11.94  ? 752  PRO A CG  1 
ATOM   552  C CD  . PRO A 1 71  ? 36.428 27.798 -4.364  1.00 13.84  ? 752  PRO A CD  1 
ATOM   553  N N   . ASP A 1 72  ? 36.534 23.917 -4.410  1.00 13.62  ? 753  ASP A N   1 
ATOM   554  C CA  . ASP A 1 72  ? 36.770 22.486 -4.259  1.00 14.97  ? 753  ASP A CA  1 
ATOM   555  C C   . ASP A 1 72  ? 35.687 21.787 -3.443  1.00 15.23  ? 753  ASP A C   1 
ATOM   556  O O   . ASP A 1 72  ? 35.755 20.565 -3.266  1.00 19.19  ? 753  ASP A O   1 
ATOM   557  C CB  . ASP A 1 72  ? 38.151 22.239 -3.647  1.00 19.25  ? 753  ASP A CB  1 
ATOM   558  C CG  . ASP A 1 72  ? 38.325 22.869 -2.275  1.00 21.76  ? 753  ASP A CG  1 
ATOM   559  O OD1 . ASP A 1 72  ? 37.350 23.432 -1.719  1.00 23.52  ? 753  ASP A OD1 1 
ATOM   560  O OD2 . ASP A 1 72  ? 39.461 22.799 -1.751  1.00 19.79  ? 753  ASP A OD2 1 
ATOM   561  N N   . GLY A 1 73  ? 34.681 22.517 -2.966  1.00 17.28  ? 754  GLY A N   1 
ATOM   562  C CA  . GLY A 1 73  ? 33.550 21.930 -2.280  1.00 15.93  ? 754  GLY A CA  1 
ATOM   563  C C   . GLY A 1 73  ? 33.639 21.955 -0.772  1.00 19.44  ? 754  GLY A C   1 
ATOM   564  O O   . GLY A 1 73  ? 32.658 21.602 -0.108  1.00 17.34  ? 754  GLY A O   1 
ATOM   565  N N   . GLN A 1 74  ? 34.782 22.346 -0.217  1.00 14.87  ? 755  GLN A N   1 
ATOM   566  C CA  . GLN A 1 74  ? 34.935 22.445 1.227   1.00 13.20  ? 755  GLN A CA  1 
ATOM   567  C C   . GLN A 1 74  ? 34.078 23.578 1.784   1.00 20.37  ? 755  GLN A C   1 
ATOM   568  O O   . GLN A 1 74  ? 33.843 24.592 1.123   1.00 12.85  ? 755  GLN A O   1 
ATOM   569  C CB  . GLN A 1 74  ? 36.400 22.676 1.580   1.00 18.99  ? 755  GLN A CB  1 
ATOM   570  C CG  . GLN A 1 74  ? 37.305 21.573 1.080   1.00 20.34  ? 755  GLN A CG  1 
ATOM   571  C CD  . GLN A 1 74  ? 37.048 20.272 1.800   1.00 29.41  ? 755  GLN A CD  1 
ATOM   572  O OE1 . GLN A 1 74  ? 36.387 19.376 1.270   1.00 35.75  ? 755  GLN A OE1 1 
ATOM   573  N NE2 . GLN A 1 74  ? 37.561 20.161 3.021   1.00 33.84  ? 755  GLN A NE2 1 
ATOM   574  N N   . LYS A 1 75  ? 33.625 23.411 3.024   1.00 16.16  ? 756  LYS A N   1 
ATOM   575  C CA  . LYS A 1 75  ? 32.752 24.406 3.624   1.00 12.53  ? 756  LYS A CA  1 
ATOM   576  C C   . LYS A 1 75  ? 32.978 24.450 5.126   1.00 13.56  ? 756  LYS A C   1 
ATOM   577  O O   . LYS A 1 75  ? 33.523 23.518 5.721   1.00 18.45  ? 756  LYS A O   1 
ATOM   578  C CB  . LYS A 1 75  ? 31.284 24.102 3.317   1.00 13.36  ? 756  LYS A CB  1 
ATOM   579  C CG  . LYS A 1 75  ? 30.863 22.693 3.700   1.00 19.63  ? 756  LYS A CG  1 
ATOM   580  C CD  . LYS A 1 75  ? 29.380 22.496 3.473   1.00 22.58  ? 756  LYS A CD  1 
ATOM   581  C CE  . LYS A 1 75  ? 28.994 22.860 2.048   1.00 30.88  ? 756  LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 75  ? 27.598 22.439 1.731   1.00 45.13  ? 756  LYS A NZ  1 
ATOM   583  N N   . GLY A 1 76  ? 32.538 25.545 5.737   1.00 12.13  ? 757  GLY A N   1 
ATOM   584  C CA  . GLY A 1 76  ? 32.570 25.685 7.183   1.00 12.12  ? 757  GLY A CA  1 
ATOM   585  C C   . GLY A 1 76  ? 31.588 26.753 7.609   1.00 12.48  ? 757  GLY A C   1 
ATOM   586  O O   . GLY A 1 76  ? 31.026 27.468 6.781   1.00 17.48  ? 757  GLY A O   1 
ATOM   587  N N   . SER A 1 77  ? 31.383 26.853 8.921   1.00 16.98  ? 758  SER A N   1 
ATOM   588  C CA  . SER A 1 77  ? 30.385 27.751 9.482   1.00 14.19  ? 758  SER A CA  1 
ATOM   589  C C   . SER A 1 77  ? 31.019 28.786 10.397  1.00 15.90  ? 758  SER A C   1 
ATOM   590  O O   . SER A 1 77  ? 32.135 28.620 10.897  1.00 18.72  ? 758  SER A O   1 
ATOM   591  C CB  . SER A 1 77  ? 29.313 26.988 10.280  1.00 20.05  ? 758  SER A CB  1 
ATOM   592  O OG  . SER A 1 77  ? 28.614 26.063 9.466   1.00 25.53  ? 758  SER A OG  1 
ATOM   593  N N   . PHE A 1 78  ? 30.266 29.858 10.620  1.00 11.61  ? 759  PHE A N   1 
ATOM   594  C CA  . PHE A 1 78  ? 30.650 30.884 11.573  1.00 13.88  ? 759  PHE A CA  1 
ATOM   595  C C   . PHE A 1 78  ? 29.390 31.584 12.063  1.00 15.03  ? 759  PHE A C   1 
ATOM   596  O O   . PHE A 1 78  ? 28.277 31.303 11.606  1.00 16.11  ? 759  PHE A O   1 
ATOM   597  C CB  . PHE A 1 78  ? 31.675 31.872 10.974  1.00 10.86  ? 759  PHE A CB  1 
ATOM   598  C CG  . PHE A 1 78  ? 31.191 32.636 9.757   1.00 11.96  ? 759  PHE A CG  1 
ATOM   599  C CD1 . PHE A 1 78  ? 31.307 32.092 8.484   1.00 10.70  ? 759  PHE A CD1 1 
ATOM   600  C CD2 . PHE A 1 78  ? 30.679 33.925 9.885   1.00 11.40  ? 759  PHE A CD2 1 
ATOM   601  C CE1 . PHE A 1 78  ? 30.878 32.801 7.364   1.00 10.66  ? 759  PHE A CE1 1 
ATOM   602  C CE2 . PHE A 1 78  ? 30.260 34.643 8.773   1.00 10.31  ? 759  PHE A CE2 1 
ATOM   603  C CZ  . PHE A 1 78  ? 30.366 34.085 7.510   1.00 10.28  ? 759  PHE A CZ  1 
ATOM   604  N N   . THR A 1 79  ? 29.573 32.466 13.044  1.00 14.13  ? 760  THR A N   1 
ATOM   605  C CA  . THR A 1 79  ? 28.491 33.194 13.686  1.00 12.25  ? 760  THR A CA  1 
ATOM   606  C C   . THR A 1 79  ? 28.876 34.662 13.796  1.00 13.06  ? 760  THR A C   1 
ATOM   607  O O   . THR A 1 79  ? 29.982 35.069 13.425  1.00 11.26  ? 760  THR A O   1 
ATOM   608  C CB  . THR A 1 79  ? 28.171 32.641 15.083  1.00 14.94  ? 760  THR A CB  1 
ATOM   609  O OG1 . THR A 1 79  ? 29.239 32.962 15.981  1.00 17.91  ? 760  THR A OG1 1 
ATOM   610  C CG2 . THR A 1 79  ? 27.973 31.131 15.046  1.00 25.56  ? 760  THR A CG2 1 
ATOM   611  N N   . SER A 1 80  ? 27.954 35.459 14.346  1.00 14.36  ? 761  SER A N   1 
ATOM   612  C CA  . SER A 1 80  ? 28.214 36.888 14.493  1.00 11.81  ? 761  SER A CA  1 
ATOM   613  C C   . SER A 1 80  ? 29.432 37.150 15.375  1.00 15.88  ? 761  SER A C   1 
ATOM   614  O O   . SER A 1 80  ? 30.117 38.158 15.192  1.00 12.53  ? 761  SER A O   1 
ATOM   615  C CB  . SER A 1 80  ? 26.979 37.594 15.055  1.00 14.20  ? 761  SER A CB  1 
ATOM   616  O OG  . SER A 1 80  ? 26.768 37.265 16.415  1.00 18.56  ? 761  SER A OG  1 
ATOM   617  N N   . GLU A 1 81  ? 29.736 36.247 16.315  1.00 17.58  ? 762  GLU A N   1 
ATOM   618  C CA  . GLU A 1 81  ? 30.913 36.422 17.162  1.00 12.91  ? 762  GLU A CA  1 
ATOM   619  C C   . GLU A 1 81  ? 32.211 36.448 16.360  1.00 15.90  ? 762  GLU A C   1 
ATOM   620  O O   . GLU A 1 81  ? 33.238 36.892 16.880  1.00 13.83  ? 762  GLU A O   1 
ATOM   621  C CB  . GLU A 1 81  ? 30.984 35.305 18.205  1.00 19.97  ? 762  GLU A CB  1 
ATOM   622  C CG  . GLU A 1 81  ? 29.726 35.161 19.053  1.00 37.75  ? 762  GLU A CG  1 
ATOM   623  C CD  . GLU A 1 81  ? 29.774 35.981 20.331  1.00 40.52  ? 762  GLU A CD  1 
ATOM   624  O OE1 . GLU A 1 81  ? 30.780 36.690 20.554  1.00 23.69  ? 762  GLU A OE1 1 
ATOM   625  O OE2 . GLU A 1 81  ? 28.803 35.903 21.117  1.00 37.27  ? 762  GLU A OE2 1 
ATOM   626  N N   . ASP A 1 82  ? 32.191 35.969 15.117  1.00 13.37  ? 763  ASP A N   1 
ATOM   627  C CA  . ASP A 1 82  ? 33.384 35.870 14.288  1.00 14.14  ? 763  ASP A CA  1 
ATOM   628  C C   . ASP A 1 82  ? 33.540 37.035 13.320  1.00 16.06  ? 763  ASP A C   1 
ATOM   629  O O   . ASP A 1 82  ? 34.525 37.073 12.573  1.00 13.88  ? 763  ASP A O   1 
ATOM   630  C CB  . ASP A 1 82  ? 33.356 34.550 13.514  1.00 17.59  ? 763  ASP A CB  1 
ATOM   631  C CG  . ASP A 1 82  ? 33.203 33.359 14.429  1.00 16.67  ? 763  ASP A CG  1 
ATOM   632  O OD1 . ASP A 1 82  ? 33.979 33.291 15.400  1.00 17.55  ? 763  ASP A OD1 1 
ATOM   633  O OD2 . ASP A 1 82  ? 32.298 32.514 14.202  1.00 16.64  ? 763  ASP A OD2 1 
ATOM   634  N N   . ILE A 1 83  ? 32.610 37.990 13.325  1.00 14.34  ? 764  ILE A N   1 
ATOM   635  C CA  . ILE A 1 83  ? 32.575 39.071 12.343  1.00 9.96   ? 764  ILE A CA  1 
ATOM   636  C C   . ILE A 1 83  ? 33.162 40.337 12.957  1.00 12.28  ? 764  ILE A C   1 
ATOM   637  O O   . ILE A 1 83  ? 32.777 40.745 14.061  1.00 13.55  ? 764  ILE A O   1 
ATOM   638  C CB  . ILE A 1 83  ? 31.142 39.315 11.839  1.00 11.17  ? 764  ILE A CB  1 
ATOM   639  C CG1 . ILE A 1 83  ? 30.516 38.011 11.336  1.00 10.16  ? 764  ILE A CG1 1 
ATOM   640  C CG2 . ILE A 1 83  ? 31.130 40.381 10.732  1.00 13.98  ? 764  ILE A CG2 1 
ATOM   641  C CD1 . ILE A 1 83  ? 29.109 38.184 10.824  1.00 12.57  ? 764  ILE A CD1 1 
ATOM   642  N N   . HIS A 1 84  ? 34.104 40.953 12.247  1.00 11.87  ? 765  HIS A N   1 
ATOM   643  C CA  . HIS A 1 84  ? 34.757 42.185 12.673  1.00 10.79  ? 765  HIS A CA  1 
ATOM   644  C C   . HIS A 1 84  ? 34.412 43.251 11.642  1.00 13.20  ? 765  HIS A C   1 
ATOM   645  O O   . HIS A 1 84  ? 34.829 43.152 10.486  1.00 12.63  ? 765  HIS A O   1 
ATOM   646  C CB  . HIS A 1 84  ? 36.276 41.992 12.779  1.00 11.79  ? 765  HIS A CB  1 
ATOM   647  C CG  . HIS A 1 84  ? 36.682 40.846 13.658  1.00 11.09  ? 765  HIS A CG  1 
ATOM   648  N ND1 . HIS A 1 84  ? 36.954 40.999 15.000  1.00 13.06  ? 765  HIS A ND1 1 
ATOM   649  C CD2 . HIS A 1 84  ? 36.840 39.527 13.392  1.00 11.85  ? 765  HIS A CD2 1 
ATOM   650  C CE1 . HIS A 1 84  ? 37.273 39.828 15.520  1.00 21.08  ? 765  HIS A CE1 1 
ATOM   651  N NE2 . HIS A 1 84  ? 37.209 38.917 14.566  1.00 11.55  ? 765  HIS A NE2 1 
ATOM   652  N N   . PHE A 1 85  ? 33.638 44.258 12.044  1.00 10.27  ? 766  PHE A N   1 
ATOM   653  C CA  . PHE A 1 85  ? 33.275 45.334 11.138  1.00 10.55  ? 766  PHE A CA  1 
ATOM   654  C C   . PHE A 1 85  ? 34.299 46.455 11.227  1.00 9.78   ? 766  PHE A C   1 
ATOM   655  O O   . PHE A 1 85  ? 34.731 46.828 12.319  1.00 12.59  ? 766  PHE A O   1 
ATOM   656  C CB  . PHE A 1 85  ? 31.884 45.872 11.468  1.00 12.22  ? 766  PHE A CB  1 
ATOM   657  C CG  . PHE A 1 85  ? 30.799 44.836 11.369  1.00 14.28  ? 766  PHE A CG  1 
ATOM   658  C CD1 . PHE A 1 85  ? 30.265 44.490 10.141  1.00 13.46  ? 766  PHE A CD1 1 
ATOM   659  C CD2 . PHE A 1 85  ? 30.320 44.210 12.506  1.00 12.72  ? 766  PHE A CD2 1 
ATOM   660  C CE1 . PHE A 1 85  ? 29.259 43.539 10.047  1.00 10.02  ? 766  PHE A CE1 1 
ATOM   661  C CE2 . PHE A 1 85  ? 29.319 43.264 12.421  1.00 15.77  ? 766  PHE A CE2 1 
ATOM   662  C CZ  . PHE A 1 85  ? 28.793 42.921 11.191  1.00 13.61  ? 766  PHE A CZ  1 
ATOM   663  N N   . TYR A 1 86  ? 34.699 46.976 10.066  1.00 9.37   ? 767  TYR A N   1 
ATOM   664  C CA  . TYR A 1 86  ? 35.597 48.125 10.061  1.00 10.56  ? 767  TYR A CA  1 
ATOM   665  C C   . TYR A 1 86  ? 34.972 49.302 10.795  1.00 13.71  ? 767  TYR A C   1 
ATOM   666  O O   . TYR A 1 86  ? 35.642 49.973 11.590  1.00 12.98  ? 767  TYR A O   1 
ATOM   667  C CB  . TYR A 1 86  ? 35.944 48.512 8.626   1.00 10.45  ? 767  TYR A CB  1 
ATOM   668  C CG  . TYR A 1 86  ? 36.847 49.703 8.519   1.00 10.57  ? 767  TYR A CG  1 
ATOM   669  C CD1 . TYR A 1 86  ? 38.140 49.673 9.035   1.00 13.80  ? 767  TYR A CD1 1 
ATOM   670  C CD2 . TYR A 1 86  ? 36.422 50.847 7.869   1.00 11.34  ? 767  TYR A CD2 1 
ATOM   671  C CE1 . TYR A 1 86  ? 38.973 50.769 8.925   1.00 19.34  ? 767  TYR A CE1 1 
ATOM   672  C CE2 . TYR A 1 86  ? 37.238 51.946 7.760   1.00 16.99  ? 767  TYR A CE2 1 
ATOM   673  C CZ  . TYR A 1 86  ? 38.511 51.905 8.283   1.00 16.31  ? 767  TYR A CZ  1 
ATOM   674  O OH  . TYR A 1 86  ? 39.313 53.011 8.156   1.00 14.97  ? 767  TYR A OH  1 
ATOM   675  N N   . ASN A 1 87  ? 33.687 49.563 10.540  1.00 11.45  ? 768  ASN A N   1 
ATOM   676  C CA  . ASN A 1 87  ? 32.975 50.642 11.228  1.00 10.19  ? 768  ASN A CA  1 
ATOM   677  C C   . ASN A 1 87  ? 31.470 50.387 11.083  1.00 10.34  ? 768  ASN A C   1 
ATOM   678  O O   . ASN A 1 87  ? 30.826 50.933 10.188  1.00 15.62  ? 768  ASN A O   1 
ATOM   679  C CB  . ASN A 1 87  ? 33.355 52.003 10.682  1.00 14.87  ? 768  ASN A CB  1 
ATOM   680  C CG  . ASN A 1 87  ? 32.875 53.124 11.565  1.00 16.90  ? 768  ASN A CG  1 
ATOM   681  O OD1 . ASN A 1 87  ? 31.930 52.952 12.342  1.00 17.64  ? 768  ASN A OD1 1 
ATOM   682  N ND2 . ASN A 1 87  ? 33.519 54.285 11.457  1.00 18.44  ? 768  ASN A ND2 1 
ATOM   683  N N   . LYS A 1 88  ? 30.923 49.593 12.003  1.00 11.07  ? 769  LYS A N   1 
ATOM   684  C CA  . LYS A 1 88  ? 29.492 49.303 11.979  1.00 16.40  ? 769  LYS A CA  1 
ATOM   685  C C   . LYS A 1 88  ? 28.665 50.550 12.286  1.00 14.95  ? 769  LYS A C   1 
ATOM   686  O O   . LYS A 1 88  ? 27.608 50.767 11.682  1.00 15.18  ? 769  LYS A O   1 
ATOM   687  C CB  . LYS A 1 88  ? 29.179 48.179 12.972  1.00 15.96  ? 769  LYS A CB  1 
ATOM   688  C CG  . LYS A 1 88  ? 27.697 47.870 13.123  1.00 13.30  ? 769  LYS A CG  1 
ATOM   689  C CD  . LYS A 1 88  ? 27.447 46.749 14.131  1.00 22.13  ? 769  LYS A CD  1 
ATOM   690  C CE  . LYS A 1 88  ? 25.945 46.544 14.324  1.00 27.57  ? 769  LYS A CE  1 
ATOM   691  N NZ  . LYS A 1 88  ? 25.611 45.506 15.339  1.00 37.19  ? 769  LYS A NZ  1 
ATOM   692  N N   . LYS A 1 89  ? 29.135 51.391 13.210  1.00 19.53  ? 770  LYS A N   1 
ATOM   693  C CA  . LYS A 1 89  ? 28.382 52.590 13.573  1.00 20.40  ? 770  LYS A CA  1 
ATOM   694  C C   . LYS A 1 89  ? 28.150 53.488 12.361  1.00 19.20  ? 770  LYS A C   1 
ATOM   695  O O   . LYS A 1 89  ? 27.020 53.920 12.099  1.00 15.25  ? 770  LYS A O   1 
ATOM   696  C CB  . LYS A 1 89  ? 29.118 53.349 14.683  1.00 18.27  ? 770  LYS A CB  1 
ATOM   697  C CG  . LYS A 1 89  ? 28.666 54.798 14.880  1.00 23.64  ? 770  LYS A CG  1 
ATOM   698  C CD  . LYS A 1 89  ? 27.194 54.901 15.240  1.00 28.76  ? 770  LYS A CD  1 
ATOM   699  C CE  . LYS A 1 89  ? 26.758 56.368 15.298  1.00 39.31  ? 770  LYS A CE  1 
ATOM   700  N NZ  . LYS A 1 89  ? 25.320 56.538 15.666  1.00 33.31  ? 770  LYS A NZ  1 
ATOM   701  N N   . ASP A 1 90  ? 29.207 53.775 11.607  1.00 13.95  ? 771  ASP A N   1 
ATOM   702  C CA  . ASP A 1 90  ? 29.138 54.674 10.464  1.00 11.55  ? 771  ASP A CA  1 
ATOM   703  C C   . ASP A 1 90  ? 28.893 53.945 9.153   1.00 13.38  ? 771  ASP A C   1 
ATOM   704  O O   . ASP A 1 90  ? 28.960 54.568 8.093   1.00 13.19  ? 771  ASP A O   1 
ATOM   705  C CB  . ASP A 1 90  ? 30.420 55.497 10.366  1.00 16.50  ? 771  ASP A CB  1 
ATOM   706  C CG  . ASP A 1 90  ? 30.581 56.442 11.529  1.00 18.78  ? 771  ASP A CG  1 
ATOM   707  O OD1 . ASP A 1 90  ? 29.570 57.054 11.927  1.00 28.35  ? 771  ASP A OD1 1 
ATOM   708  O OD2 . ASP A 1 90  ? 31.710 56.571 12.044  1.00 23.21  ? 771  ASP A OD2 1 
ATOM   709  N N   . TYR A 1 91  ? 28.603 52.647 9.198   1.00 12.35  ? 772  TYR A N   1 
ATOM   710  C CA  . TYR A 1 91  ? 28.208 51.934 7.986   1.00 13.18  ? 772  TYR A CA  1 
ATOM   711  C C   . TYR A 1 91  ? 27.219 52.699 7.102   1.00 16.24  ? 772  TYR A C   1 
ATOM   712  O O   . TYR A 1 91  ? 27.421 52.709 5.875   1.00 12.88  ? 772  TYR A O   1 
ATOM   713  C CB  . TYR A 1 91  ? 27.631 50.557 8.352   1.00 14.96  ? 772  TYR A CB  1 
ATOM   714  C CG  . TYR A 1 91  ? 26.907 49.911 7.196   1.00 11.55  ? 772  TYR A CG  1 
ATOM   715  C CD1 . TYR A 1 91  ? 27.606 49.202 6.216   1.00 15.77  ? 772  TYR A CD1 1 
ATOM   716  C CD2 . TYR A 1 91  ? 25.523 50.016 7.073   1.00 11.56  ? 772  TYR A CD2 1 
ATOM   717  C CE1 . TYR A 1 91  ? 26.940 48.619 5.143   1.00 12.92  ? 772  TYR A CE1 1 
ATOM   718  C CE2 . TYR A 1 91  ? 24.854 49.446 6.010   1.00 14.52  ? 772  TYR A CE2 1 
ATOM   719  C CZ  . TYR A 1 91  ? 25.561 48.751 5.052   1.00 21.51  ? 772  TYR A CZ  1 
ATOM   720  O OH  . TYR A 1 91  ? 24.877 48.194 4.002   1.00 18.61  ? 772  TYR A OH  1 
ATOM   721  N N   . PRO A 1 92  ? 26.155 53.334 7.614   1.00 13.58  ? 773  PRO A N   1 
ATOM   722  C CA  . PRO A 1 92  ? 25.216 54.003 6.697   1.00 14.10  ? 773  PRO A CA  1 
ATOM   723  C C   . PRO A 1 92  ? 25.797 55.203 5.965   1.00 15.13  ? 773  PRO A C   1 
ATOM   724  O O   . PRO A 1 92  ? 25.167 55.672 5.010   1.00 16.99  ? 773  PRO A O   1 
ATOM   725  C CB  . PRO A 1 92  ? 24.061 54.430 7.613   1.00 18.61  ? 773  PRO A CB  1 
ATOM   726  C CG  . PRO A 1 92  ? 24.170 53.572 8.817   1.00 12.66  ? 773  PRO A CG  1 
ATOM   727  C CD  . PRO A 1 92  ? 25.638 53.323 8.996   1.00 12.07  ? 773  PRO A CD  1 
ATOM   728  N N   . LYS A 1 93  ? 26.964 55.707 6.367   1.00 11.91  ? 774  LYS A N   1 
ATOM   729  C CA  . LYS A 1 93  ? 27.485 56.950 5.807   1.00 21.69  ? 774  LYS A CA  1 
ATOM   730  C C   . LYS A 1 93  ? 28.115 56.775 4.431   1.00 20.49  ? 774  LYS A C   1 
ATOM   731  O O   . LYS A 1 93  ? 28.292 57.772 3.723   1.00 14.20  ? 774  LYS A O   1 
ATOM   732  C CB  . LYS A 1 93  ? 28.511 57.574 6.758   1.00 13.11  ? 774  LYS A CB  1 
ATOM   733  C CG  . LYS A 1 93  ? 27.946 58.000 8.119   1.00 21.38  ? 774  LYS A CG  1 
ATOM   734  C CD  . LYS A 1 93  ? 27.050 59.225 8.016   1.00 27.61  ? 774  LYS A CD  1 
ATOM   735  C CE  . LYS A 1 93  ? 26.403 59.565 9.358   1.00 29.81  ? 774  LYS A CE  1 
ATOM   736  N NZ  . LYS A 1 93  ? 25.349 58.576 9.750   1.00 31.97  ? 774  LYS A NZ  1 
ATOM   737  N N   . GLY A 1 94  ? 28.464 55.559 4.033   1.00 15.61  ? 775  GLY A N   1 
ATOM   738  C CA  . GLY A 1 94  ? 29.029 55.364 2.712   1.00 15.28  ? 775  GLY A CA  1 
ATOM   739  C C   . GLY A 1 94  ? 29.770 54.053 2.590   1.00 14.25  ? 775  GLY A C   1 
ATOM   740  O O   . GLY A 1 94  ? 30.065 53.372 3.574   1.00 11.09  ? 775  GLY A O   1 
ATOM   741  N N   . PHE A 1 95  ? 30.081 53.715 1.335   1.00 10.35  ? 776  PHE A N   1 
ATOM   742  C CA  . PHE A 1 95  ? 30.734 52.462 0.987   1.00 10.68  ? 776  PHE A CA  1 
ATOM   743  C C   . PHE A 1 95  ? 32.143 52.345 1.557   1.00 15.34  ? 776  PHE A C   1 
ATOM   744  O O   . PHE A 1 95  ? 32.674 51.228 1.627   1.00 9.60   ? 776  PHE A O   1 
ATOM   745  C CB  . PHE A 1 95  ? 30.750 52.306 -0.535  1.00 9.98   ? 776  PHE A CB  1 
ATOM   746  C CG  . PHE A 1 95  ? 29.466 51.761 -1.093  1.00 17.48  ? 776  PHE A CG  1 
ATOM   747  C CD1 . PHE A 1 95  ? 29.156 50.417 -0.950  1.00 22.09  ? 776  PHE A CD1 1 
ATOM   748  C CD2 . PHE A 1 95  ? 28.569 52.586 -1.751  1.00 27.70  ? 776  PHE A CD2 1 
ATOM   749  C CE1 . PHE A 1 95  ? 27.972 49.905 -1.447  1.00 19.99  ? 776  PHE A CE1 1 
ATOM   750  C CE2 . PHE A 1 95  ? 27.381 52.080 -2.256  1.00 23.85  ? 776  PHE A CE2 1 
ATOM   751  C CZ  . PHE A 1 95  ? 27.083 50.738 -2.104  1.00 28.10  ? 776  PHE A CZ  1 
ATOM   752  N N   . ILE A 1 96  ? 32.749 53.454 1.991   1.00 9.89   ? 777  ILE A N   1 
ATOM   753  C CA  . ILE A 1 96  ? 34.052 53.373 2.645   1.00 11.32  ? 777  ILE A CA  1 
ATOM   754  C C   . ILE A 1 96  ? 33.986 52.476 3.876   1.00 11.57  ? 777  ILE A C   1 
ATOM   755  O O   . ILE A 1 96  ? 34.988 51.857 4.255   1.00 9.89   ? 777  ILE A O   1 
ATOM   756  C CB  . ILE A 1 96  ? 34.560 54.786 3.001   1.00 9.69   ? 777  ILE A CB  1 
ATOM   757  C CG1 . ILE A 1 96  ? 35.955 54.726 3.634   1.00 13.20  ? 777  ILE A CG1 1 
ATOM   758  C CG2 . ILE A 1 96  ? 33.611 55.486 3.940   1.00 10.04  ? 777  ILE A CG2 1 
ATOM   759  C CD1 . ILE A 1 96  ? 36.494 56.089 4.037   1.00 12.26  ? 777  ILE A CD1 1 
ATOM   760  N N   . TYR A 1 97  ? 32.812 52.367 4.505   1.00 10.70  ? 778  TYR A N   1 
ATOM   761  C CA  . TYR A 1 97  ? 32.653 51.583 5.720   1.00 9.57   ? 778  TYR A CA  1 
ATOM   762  C C   . TYR A 1 97  ? 32.015 50.228 5.477   1.00 9.46   ? 778  TYR A C   1 
ATOM   763  O O   . TYR A 1 97  ? 31.741 49.514 6.444   1.00 11.50  ? 778  TYR A O   1 
ATOM   764  C CB  . TYR A 1 97  ? 31.824 52.348 6.750   1.00 9.95   ? 778  TYR A CB  1 
ATOM   765  C CG  . TYR A 1 97  ? 32.407 53.697 7.073   1.00 13.58  ? 778  TYR A CG  1 
ATOM   766  C CD1 . TYR A 1 97  ? 33.674 53.807 7.636   1.00 15.76  ? 778  TYR A CD1 1 
ATOM   767  C CD2 . TYR A 1 97  ? 31.706 54.860 6.800   1.00 14.55  ? 778  TYR A CD2 1 
ATOM   768  C CE1 . TYR A 1 97  ? 34.222 55.039 7.930   1.00 19.29  ? 778  TYR A CE1 1 
ATOM   769  C CE2 . TYR A 1 97  ? 32.247 56.096 7.088   1.00 14.48  ? 778  TYR A CE2 1 
ATOM   770  C CZ  . TYR A 1 97  ? 33.502 56.180 7.651   1.00 17.73  ? 778  TYR A CZ  1 
ATOM   771  O OH  . TYR A 1 97  ? 34.031 57.425 7.934   1.00 23.96  ? 778  TYR A OH  1 
ATOM   772  N N   . ASP A 1 98  ? 31.762 49.865 4.223   1.00 9.38   ? 779  ASP A N   1 
ATOM   773  C CA  . ASP A 1 98  ? 31.100 48.598 3.911   1.00 9.37   ? 779  ASP A CA  1 
ATOM   774  C C   . ASP A 1 98  ? 32.196 47.545 3.783   1.00 9.05   ? 779  ASP A C   1 
ATOM   775  O O   . ASP A 1 98  ? 32.592 47.139 2.690   1.00 8.92   ? 779  ASP A O   1 
ATOM   776  C CB  . ASP A 1 98  ? 30.266 48.728 2.644   1.00 9.56   ? 779  ASP A CB  1 
ATOM   777  C CG  . ASP A 1 98  ? 29.397 47.511 2.389   1.00 13.47  ? 779  ASP A CG  1 
ATOM   778  O OD1 . ASP A 1 98  ? 29.349 46.618 3.256   1.00 9.63   ? 779  ASP A OD1 1 
ATOM   779  O OD2 . ASP A 1 98  ? 28.772 47.453 1.317   1.00 14.86  ? 779  ASP A OD2 1 
ATOM   780  N N   . LEU A 1 99  ? 32.690 47.105 4.937   1.00 8.98   ? 780  LEU A N   1 
ATOM   781  C CA  . LEU A 1 99  ? 33.924 46.325 5.004   1.00 8.76   ? 780  LEU A CA  1 
ATOM   782  C C   . LEU A 1 99  ? 33.907 45.462 6.259   1.00 8.82   ? 780  LEU A C   1 
ATOM   783  O O   . LEU A 1 99  ? 33.655 45.980 7.349   1.00 8.99   ? 780  LEU A O   1 
ATOM   784  C CB  . LEU A 1 99  ? 35.139 47.275 5.006   1.00 8.69   ? 780  LEU A CB  1 
ATOM   785  C CG  . LEU A 1 99  ? 36.499 46.630 5.276   1.00 8.57   ? 780  LEU A CG  1 
ATOM   786  C CD1 . LEU A 1 99  ? 36.741 45.589 4.209   1.00 8.60   ? 780  LEU A CD1 1 
ATOM   787  C CD2 . LEU A 1 99  ? 37.630 47.645 5.298   1.00 8.73   ? 780  LEU A CD2 1 
ATOM   788  N N   . ALA A 1 100 ? 34.199 44.159 6.118   1.00 8.74   ? 781  ALA A N   1 
ATOM   789  C CA  . ALA A 1 100 ? 34.199 43.271 7.273   1.00 8.86   ? 781  ALA A CA  1 
ATOM   790  C C   . ALA A 1 100 ? 35.210 42.142 7.098   1.00 13.20  ? 781  ALA A C   1 
ATOM   791  O O   . ALA A 1 100 ? 35.538 41.746 5.979   1.00 10.21  ? 781  ALA A O   1 
ATOM   792  C CB  . ALA A 1 100 ? 32.812 42.681 7.516   1.00 10.73  ? 781  ALA A CB  1 
ATOM   793  N N   . VAL A 1 101 ? 35.680 41.610 8.227   1.00 10.05  ? 782  VAL A N   1 
ATOM   794  C CA  . VAL A 1 101 ? 36.651 40.523 8.257   1.00 11.40  ? 782  VAL A CA  1 
ATOM   795  C C   . VAL A 1 101 ? 36.120 39.445 9.188   1.00 11.61  ? 782  VAL A C   1 
ATOM   796  O O   . VAL A 1 101 ? 35.625 39.749 10.279  1.00 13.22  ? 782  VAL A O   1 
ATOM   797  C CB  . VAL A 1 101 ? 38.042 41.011 8.714   1.00 8.97   ? 782  VAL A CB  1 
ATOM   798  C CG1 . VAL A 1 101 ? 38.980 39.841 8.911   1.00 9.88   ? 782  VAL A CG1 1 
ATOM   799  C CG2 . VAL A 1 101 ? 38.613 41.985 7.697   1.00 13.80  ? 782  VAL A CG2 1 
ATOM   800  N N   . ILE A 1 102 ? 36.216 38.187 8.759   1.00 10.66  ? 783  ILE A N   1 
ATOM   801  C CA  . ILE A 1 102 ? 35.697 37.052 9.512   1.00 13.86  ? 783  ILE A CA  1 
ATOM   802  C C   . ILE A 1 102 ? 36.871 36.199 9.969   1.00 12.87  ? 783  ILE A C   1 
ATOM   803  O O   . ILE A 1 102 ? 37.696 35.783 9.148   1.00 9.55   ? 783  ILE A O   1 
ATOM   804  C CB  . ILE A 1 102 ? 34.707 36.224 8.675   1.00 9.48   ? 783  ILE A CB  1 
ATOM   805  C CG1 . ILE A 1 102 ? 33.508 37.093 8.277   1.00 12.02  ? 783  ILE A CG1 1 
ATOM   806  C CG2 . ILE A 1 102 ? 34.195 35.040 9.486   1.00 9.80   ? 783  ILE A CG2 1 
ATOM   807  C CD1 . ILE A 1 102 ? 32.865 36.700 6.964   1.00 11.73  ? 783  ILE A CD1 1 
ATOM   808  N N   . THR A 1 103 ? 36.953 35.953 11.280  1.00 9.88   ? 784  THR A N   1 
ATOM   809  C CA  . THR A 1 103 ? 37.976 35.095 11.867  1.00 12.56  ? 784  THR A CA  1 
ATOM   810  C C   . THR A 1 103 ? 37.346 33.734 12.151  1.00 13.96  ? 784  THR A C   1 
ATOM   811  O O   . THR A 1 103 ? 36.502 33.600 13.043  1.00 14.28  ? 784  THR A O   1 
ATOM   812  C CB  . THR A 1 103 ? 38.561 35.704 13.136  1.00 16.98  ? 784  THR A CB  1 
ATOM   813  O OG1 . THR A 1 103 ? 37.499 36.077 14.019  1.00 12.83  ? 784  THR A OG1 1 
ATOM   814  C CG2 . THR A 1 103 ? 39.413 36.927 12.796  1.00 10.52  ? 784  THR A CG2 1 
ATOM   815  N N   . LEU A 1 104 ? 37.754 32.743 11.384  1.00 11.20  ? 785  LEU A N   1 
ATOM   816  C CA  . LEU A 1 104 ? 37.265 31.379 11.506  1.00 12.81  ? 785  LEU A CA  1 
ATOM   817  C C   . LEU A 1 104 ? 38.080 30.628 12.554  1.00 14.07  ? 785  LEU A C   1 
ATOM   818  O O   . LEU A 1 104 ? 39.126 31.102 13.013  1.00 16.18  ? 785  LEU A O   1 
ATOM   819  C CB  . LEU A 1 104 ? 37.333 30.712 10.132  1.00 11.79  ? 785  LEU A CB  1 
ATOM   820  C CG  . LEU A 1 104 ? 36.571 31.512 9.061   1.00 10.35  ? 785  LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 104 ? 36.824 30.993 7.653   1.00 17.92  ? 785  LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 104 ? 35.078 31.478 9.370   1.00 15.28  ? 785  LEU A CD2 1 
ATOM   823  N N   . PRO A 1 105 ? 37.623 29.448 12.980  1.00 17.79  ? 786  PRO A N   1 
ATOM   824  C CA  . PRO A 1 105 ? 38.393 28.680 13.967  1.00 21.77  ? 786  PRO A CA  1 
ATOM   825  C C   . PRO A 1 105 ? 39.800 28.369 13.474  1.00 21.90  ? 786  PRO A C   1 
ATOM   826  O O   . PRO A 1 105 ? 40.061 28.287 12.271  1.00 18.45  ? 786  PRO A O   1 
ATOM   827  C CB  . PRO A 1 105 ? 37.569 27.402 14.140  1.00 26.54  ? 786  PRO A CB  1 
ATOM   828  C CG  . PRO A 1 105 ? 36.176 27.830 13.854  1.00 22.14  ? 786  PRO A CG  1 
ATOM   829  C CD  . PRO A 1 105 ? 36.282 28.876 12.768  1.00 18.57  ? 786  PRO A CD  1 
ATOM   830  N N   . GLN A 1 106 ? 40.718 28.201 14.427  1.00 23.88  ? 787  GLN A N   1 
ATOM   831  C CA  . GLN A 1 106 ? 42.100 27.898 14.073  1.00 16.07  ? 787  GLN A CA  1 
ATOM   832  C C   . GLN A 1 106 ? 42.222 26.566 13.342  1.00 21.06  ? 787  GLN A C   1 
ATOM   833  O O   . GLN A 1 106 ? 43.223 26.335 12.659  1.00 24.77  ? 787  GLN A O   1 
ATOM   834  C CB  . GLN A 1 106 ? 42.976 27.895 15.327  1.00 32.15  ? 787  GLN A CB  1 
ATOM   835  C CG  . GLN A 1 106 ? 43.000 29.221 16.084  1.00 43.78  ? 787  GLN A CG  1 
ATOM   836  C CD  . GLN A 1 106 ? 43.696 30.334 15.317  1.00 43.03  ? 787  GLN A CD  1 
ATOM   837  O OE1 . GLN A 1 106 ? 44.475 30.083 14.397  1.00 41.60  ? 787  GLN A OE1 1 
ATOM   838  N NE2 . GLN A 1 106 ? 43.414 31.575 15.695  1.00 53.33  ? 787  GLN A NE2 1 
ATOM   839  N N   . SER A 1 107 ? 41.219 25.694 13.465  1.00 17.89  ? 788  SER A N   1 
ATOM   840  C CA  . SER A 1 107 ? 41.177 24.419 12.760  1.00 22.63  ? 788  SER A CA  1 
ATOM   841  C C   . SER A 1 107 ? 40.906 24.575 11.273  1.00 17.63  ? 788  SER A C   1 
ATOM   842  O O   . SER A 1 107 ? 40.970 23.581 10.544  1.00 15.52  ? 788  SER A O   1 
ATOM   843  C CB  . SER A 1 107 ? 40.107 23.529 13.379  1.00 22.36  ? 788  SER A CB  1 
ATOM   844  O OG  . SER A 1 107 ? 38.875 24.230 13.442  1.00 23.03  ? 788  SER A OG  1 
ATOM   845  N N   . THR A 1 108 ? 40.571 25.779 10.822  1.00 18.69  ? 789  THR A N   1 
ATOM   846  C CA  . THR A 1 108 ? 40.418 26.069 9.402   1.00 16.78  ? 789  THR A CA  1 
ATOM   847  C C   . THR A 1 108 ? 41.790 26.393 8.832   1.00 18.69  ? 789  THR A C   1 
ATOM   848  O O   . THR A 1 108 ? 42.463 27.317 9.303   1.00 15.87  ? 789  THR A O   1 
ATOM   849  C CB  . THR A 1 108 ? 39.459 27.238 9.193   1.00 18.20  ? 789  THR A CB  1 
ATOM   850  O OG1 . THR A 1 108 ? 38.236 26.980 9.894   1.00 23.17  ? 789  THR A OG1 1 
ATOM   851  C CG2 . THR A 1 108 ? 39.158 27.435 7.712   1.00 14.41  ? 789  THR A CG2 1 
ATOM   852  N N   . ARG A 1 109 ? 42.210 25.640 7.826   1.00 13.53  ? 790  ARG A N   1 
ATOM   853  C CA  . ARG A 1 109 ? 43.590 25.699 7.354   1.00 13.92  ? 790  ARG A CA  1 
ATOM   854  C C   . ARG A 1 109 ? 43.631 25.806 5.834   1.00 14.31  ? 790  ARG A C   1 
ATOM   855  O O   . ARG A 1 109 ? 44.372 25.093 5.150   1.00 12.73  ? 790  ARG A O   1 
ATOM   856  C CB  . ARG A 1 109 ? 44.360 24.476 7.846   1.00 13.27  ? 790  ARG A CB  1 
ATOM   857  C CG  . ARG A 1 109 ? 44.278 24.201 9.350   1.00 13.59  ? 790  ARG A CG  1 
ATOM   858  C CD  . ARG A 1 109 ? 45.019 25.261 10.170  1.00 16.26  ? 790  ARG A CD  1 
ATOM   859  N NE  . ARG A 1 109 ? 45.251 24.844 11.551  1.00 21.57  ? 790  ARG A NE  1 
ATOM   860  C CZ  . ARG A 1 109 ? 46.254 24.066 11.940  1.00 16.37  ? 790  ARG A CZ  1 
ATOM   861  N NH1 . ARG A 1 109 ? 47.130 23.580 11.073  1.00 15.00  ? 790  ARG A NH1 1 
ATOM   862  N NH2 . ARG A 1 109 ? 46.377 23.758 13.230  1.00 15.97  ? 790  ARG A NH2 1 
ATOM   863  N N   . ARG A 1 110 ? 42.828 26.718 5.289   1.00 11.86  ? 791  ARG A N   1 
ATOM   864  C CA  . ARG A 1 110 ? 42.619 26.803 3.849   1.00 11.70  ? 791  ARG A CA  1 
ATOM   865  C C   . ARG A 1 110 ? 43.794 27.464 3.141   1.00 15.75  ? 791  ARG A C   1 
ATOM   866  O O   . ARG A 1 110 ? 44.479 28.333 3.694   1.00 12.51  ? 791  ARG A O   1 
ATOM   867  C CB  . ARG A 1 110 ? 41.347 27.597 3.541   1.00 16.51  ? 791  ARG A CB  1 
ATOM   868  C CG  . ARG A 1 110 ? 40.036 26.875 3.842   1.00 14.71  ? 791  ARG A CG  1 
ATOM   869  C CD  . ARG A 1 110 ? 39.783 25.770 2.837   1.00 16.08  ? 791  ARG A CD  1 
ATOM   870  N NE  . ARG A 1 110 ? 39.824 26.258 1.464   1.00 11.58  ? 791  ARG A NE  1 
ATOM   871  C CZ  . ARG A 1 110 ? 39.732 25.481 0.391   1.00 14.87  ? 791  ARG A CZ  1 
ATOM   872  N NH1 . ARG A 1 110 ? 39.555 24.176 0.497   1.00 15.70  ? 791  ARG A NH1 1 
ATOM   873  N NH2 . ARG A 1 110 ? 39.832 26.029 -0.817  1.00 17.33  ? 791  ARG A NH2 1 
ATOM   874  N N   . GLN A 1 111 ? 44.002 27.067 1.887   1.00 11.78  ? 792  GLN A N   1 
ATOM   875  C CA  . GLN A 1 111 ? 44.834 27.870 1.009   1.00 11.65  ? 792  GLN A CA  1 
ATOM   876  C C   . GLN A 1 111 ? 44.194 29.240 0.839   1.00 12.90  ? 792  GLN A C   1 
ATOM   877  O O   . GLN A 1 111 ? 42.974 29.393 0.943   1.00 10.84  ? 792  GLN A O   1 
ATOM   878  C CB  . GLN A 1 111 ? 45.015 27.201 -0.350  1.00 11.93  ? 792  GLN A CB  1 
ATOM   879  C CG  . GLN A 1 111 ? 43.775 27.142 -1.192  1.00 18.59  ? 792  GLN A CG  1 
ATOM   880  C CD  . GLN A 1 111 ? 44.091 26.784 -2.632  1.00 20.70  ? 792  GLN A CD  1 
ATOM   881  O OE1 . GLN A 1 111 ? 44.785 27.528 -3.333  1.00 21.22  ? 792  GLN A OE1 1 
ATOM   882  N NE2 . GLN A 1 111 ? 43.592 25.634 -3.079  1.00 12.45  ? 792  GLN A NE2 1 
ATOM   883  N N   . HIS A 1 112 ? 45.022 30.244 0.582   1.00 11.39  ? 793  HIS A N   1 
ATOM   884  C CA  . HIS A 1 112 ? 44.509 31.610 0.581   1.00 10.45  ? 793  HIS A CA  1 
ATOM   885  C C   . HIS A 1 112 ? 45.361 32.501 -0.307  1.00 10.38  ? 793  HIS A C   1 
ATOM   886  O O   . HIS A 1 112 ? 46.502 32.178 -0.660  1.00 10.71  ? 793  HIS A O   1 
ATOM   887  C CB  . HIS A 1 112 ? 44.455 32.187 2.003   1.00 10.32  ? 793  HIS A CB  1 
ATOM   888  C CG  . HIS A 1 112 ? 45.795 32.306 2.664   1.00 13.01  ? 793  HIS A CG  1 
ATOM   889  N ND1 . HIS A 1 112 ? 46.562 33.451 2.597   1.00 13.17  ? 793  HIS A ND1 1 
ATOM   890  C CD2 . HIS A 1 112 ? 46.510 31.419 3.400   1.00 14.32  ? 793  HIS A CD2 1 
ATOM   891  C CE1 . HIS A 1 112 ? 47.686 33.268 3.269   1.00 11.24  ? 793  HIS A CE1 1 
ATOM   892  N NE2 . HIS A 1 112 ? 47.680 32.044 3.766   1.00 11.48  ? 793  HIS A NE2 1 
ATOM   893  N N   . ALA A 1 113 ? 44.799 33.659 -0.629  1.00 13.93  ? 794  ALA A N   1 
ATOM   894  C CA  . ALA A 1 113 ? 45.509 34.712 -1.330  1.00 9.92   ? 794  ALA A CA  1 
ATOM   895  C C   . ALA A 1 113 ? 46.142 35.664 -0.325  1.00 16.71  ? 794  ALA A C   1 
ATOM   896  O O   . ALA A 1 113 ? 45.815 35.663 0.864   1.00 13.34  ? 794  ALA A O   1 
ATOM   897  C CB  . ALA A 1 113 ? 44.557 35.479 -2.252  1.00 12.62  ? 794  ALA A CB  1 
ATOM   898  N N   . ASN A 1 114 ? 47.044 36.504 -0.822  1.00 12.41  ? 795  ASN A N   1 
ATOM   899  C CA  . ASN A 1 114 ? 47.717 37.500 -0.003  1.00 11.99  ? 795  ASN A CA  1 
ATOM   900  C C   . ASN A 1 114 ? 47.033 38.848 -0.141  1.00 9.54   ? 795  ASN A C   1 
ATOM   901  O O   . ASN A 1 114 ? 46.773 39.311 -1.256  1.00 9.68   ? 795  ASN A O   1 
ATOM   902  C CB  . ASN A 1 114 ? 49.181 37.662 -0.402  1.00 14.57  ? 795  ASN A CB  1 
ATOM   903  C CG  . ASN A 1 114 ? 49.958 36.384 -0.292  1.00 17.53  ? 795  ASN A CG  1 
ATOM   904  O OD1 . ASN A 1 114 ? 49.723 35.573 0.605   1.00 11.94  ? 795  ASN A OD1 1 
ATOM   905  N ND2 . ASN A 1 114 ? 50.910 36.198 -1.202  1.00 25.47  ? 795  ASN A ND2 1 
ATOM   906  N N   . LEU A 1 115 ? 46.770 39.479 0.992   1.00 9.71   ? 796  LEU A N   1 
ATOM   907  C CA  . LEU A 1 115 ? 46.499 40.909 0.992   1.00 11.97  ? 796  LEU A CA  1 
ATOM   908  C C   . LEU A 1 115 ? 47.740 41.654 0.510   1.00 11.90  ? 796  LEU A C   1 
ATOM   909  O O   . LEU A 1 115 ? 48.873 41.327 0.891   1.00 12.10  ? 796  LEU A O   1 
ATOM   910  C CB  . LEU A 1 115 ? 46.105 41.361 2.398   1.00 13.54  ? 796  LEU A CB  1 
ATOM   911  C CG  . LEU A 1 115 ? 45.505 42.748 2.596   1.00 9.37   ? 796  LEU A CG  1 
ATOM   912  C CD1 . LEU A 1 115 ? 44.123 42.845 1.925   1.00 13.32  ? 796  LEU A CD1 1 
ATOM   913  C CD2 . LEU A 1 115 ? 45.425 43.055 4.092   1.00 9.14   ? 796  LEU A CD2 1 
ATOM   914  N N   . VAL A 1 116 ? 47.534 42.653 -0.349  1.00 9.31   ? 797  VAL A N   1 
ATOM   915  C CA  . VAL A 1 116 ? 48.669 43.397 -0.891  1.00 9.56   ? 797  VAL A CA  1 
ATOM   916  C C   . VAL A 1 116 ? 49.479 44.006 0.248   1.00 9.83   ? 797  VAL A C   1 
ATOM   917  O O   . VAL A 1 116 ? 48.930 44.452 1.265   1.00 12.45  ? 797  VAL A O   1 
ATOM   918  C CB  . VAL A 1 116 ? 48.188 44.459 -1.896  1.00 17.56  ? 797  VAL A CB  1 
ATOM   919  C CG1 . VAL A 1 116 ? 47.366 45.547 -1.208  1.00 10.90  ? 797  VAL A CG1 1 
ATOM   920  C CG2 . VAL A 1 116 ? 49.365 45.055 -2.650  1.00 17.03  ? 797  VAL A CG2 1 
ATOM   921  N N   . GLU A 1 117 ? 50.810 43.976 0.100   1.00 10.25  ? 798  GLU A N   1 
ATOM   922  C CA  . GLU A 1 117 ? 51.693 44.480 1.145   1.00 18.13  ? 798  GLU A CA  1 
ATOM   923  C C   . GLU A 1 117 ? 51.668 46.005 1.202   1.00 15.50  ? 798  GLU A C   1 
ATOM   924  O O   . GLU A 1 117 ? 51.543 46.592 2.283   1.00 19.27  ? 798  GLU A O   1 
ATOM   925  C CB  . GLU A 1 117 ? 53.117 43.965 0.910   1.00 28.61  ? 798  GLU A CB  1 
ATOM   926  C CG  . GLU A 1 117 ? 54.071 44.109 2.089   1.00 43.88  ? 798  GLU A CG  1 
ATOM   927  C CD  . GLU A 1 117 ? 55.448 43.504 1.811   1.00 55.23  ? 798  GLU A CD  1 
ATOM   928  O OE1 . GLU A 1 117 ? 55.670 43.005 0.686   1.00 51.97  ? 798  GLU A OE1 1 
ATOM   929  O OE2 . GLU A 1 117 ? 56.311 43.527 2.716   1.00 47.07  ? 798  GLU A OE2 1 
ATOM   930  N N   . ASN A 1 118 ? 51.778 46.663 0.050   1.00 15.78  ? 799  ASN A N   1 
ATOM   931  C CA  . ASN A 1 118 ? 51.851 48.119 -0.034  1.00 18.83  ? 799  ASN A CA  1 
ATOM   932  C C   . ASN A 1 118 ? 50.666 48.669 -0.816  1.00 14.95  ? 799  ASN A C   1 
ATOM   933  O O   . ASN A 1 118 ? 50.259 48.096 -1.828  1.00 19.97  ? 799  ASN A O   1 
ATOM   934  C CB  . ASN A 1 118 ? 53.155 48.573 -0.707  1.00 17.92  ? 799  ASN A CB  1 
ATOM   935  C CG  . ASN A 1 118 ? 54.393 48.049 -0.003  1.00 21.13  ? 799  ASN A CG  1 
ATOM   936  O OD1 . ASN A 1 118 ? 55.143 47.253 -0.561  1.00 28.93  ? 799  ASN A OD1 1 
ATOM   937  N ND2 . ASN A 1 118 ? 54.603 48.485 1.229   1.00 18.24  ? 799  ASN A ND2 1 
ATOM   938  N N   . TYR A 1 119 ? 50.122 49.789 -0.352  1.00 11.14  ? 800  TYR A N   1 
ATOM   939  C CA  . TYR A 1 119 ? 49.046 50.457 -1.077  1.00 19.44  ? 800  TYR A CA  1 
ATOM   940  C C   . TYR A 1 119 ? 49.534 50.982 -2.422  1.00 19.02  ? 800  TYR A C   1 
ATOM   941  O O   . TYR A 1 119 ? 50.577 51.641 -2.505  1.00 14.36  ? 800  TYR A O   1 
ATOM   942  C CB  . TYR A 1 119 ? 48.492 51.622 -0.262  1.00 12.28  ? 800  TYR A CB  1 
ATOM   943  C CG  . TYR A 1 119 ? 47.569 52.523 -1.047  1.00 9.76   ? 800  TYR A CG  1 
ATOM   944  C CD1 . TYR A 1 119 ? 46.254 52.158 -1.279  1.00 9.59   ? 800  TYR A CD1 1 
ATOM   945  C CD2 . TYR A 1 119 ? 48.004 53.751 -1.531  1.00 12.42  ? 800  TYR A CD2 1 
ATOM   946  C CE1 . TYR A 1 119 ? 45.405 52.973 -1.986  1.00 10.32  ? 800  TYR A CE1 1 
ATOM   947  C CE2 . TYR A 1 119 ? 47.156 54.582 -2.241  1.00 10.87  ? 800  TYR A CE2 1 
ATOM   948  C CZ  . TYR A 1 119 ? 45.851 54.189 -2.456  1.00 9.61   ? 800  TYR A CZ  1 
ATOM   949  O OH  . TYR A 1 119 ? 45.000 55.014 -3.162  1.00 9.63   ? 800  TYR A OH  1 
ATOM   950  N N   . SER A 1 120 ? 48.771 50.705 -3.475  1.00 16.37  ? 801  SER A N   1 
ATOM   951  C CA  A SER A 1 120 ? 49.028 51.266 -4.796  0.50 13.42  ? 801  SER A CA  1 
ATOM   952  C CA  B SER A 1 120 ? 49.027 51.262 -4.799  0.50 13.50  ? 801  SER A CA  1 
ATOM   953  C C   . SER A 1 120 ? 47.724 51.820 -5.346  1.00 12.49  ? 801  SER A C   1 
ATOM   954  O O   . SER A 1 120 ? 46.751 51.077 -5.515  1.00 14.40  ? 801  SER A O   1 
ATOM   955  C CB  A SER A 1 120 ? 49.612 50.221 -5.748  0.50 17.84  ? 801  SER A CB  1 
ATOM   956  C CB  B SER A 1 120 ? 49.604 50.214 -5.754  0.50 17.84  ? 801  SER A CB  1 
ATOM   957  O OG  A SER A 1 120 ? 49.743 50.762 -7.049  0.50 12.68  ? 801  SER A OG  1 
ATOM   958  O OG  B SER A 1 120 ? 50.954 49.927 -5.443  0.50 13.87  ? 801  SER A OG  1 
ATOM   959  N N   . LYS A 1 121 ? 47.711 53.117 -5.619  1.00 9.87   ? 802  LYS A N   1 
ATOM   960  C CA  . LYS A 1 121 ? 46.536 53.784 -6.167  1.00 10.02  ? 802  LYS A CA  1 
ATOM   961  C C   . LYS A 1 121 ? 46.123 53.138 -7.481  1.00 12.40  ? 802  LYS A C   1 
ATOM   962  O O   . LYS A 1 121 ? 46.959 52.878 -8.354  1.00 14.66  ? 802  LYS A O   1 
ATOM   963  C CB  . LYS A 1 121 ? 46.847 55.276 -6.367  1.00 14.48  ? 802  LYS A CB  1 
ATOM   964  C CG  . LYS A 1 121 ? 45.838 56.087 -7.210  1.00 19.00  ? 802  LYS A CG  1 
ATOM   965  C CD  . LYS A 1 121 ? 44.580 56.444 -6.446  1.00 20.55  ? 802  LYS A CD  1 
ATOM   966  C CE  . LYS A 1 121 ? 43.790 57.574 -7.132  1.00 19.17  ? 802  LYS A CE  1 
ATOM   967  N NZ  . LYS A 1 121 ? 43.452 57.318 -8.565  1.00 14.01  ? 802  LYS A NZ  1 
ATOM   968  N N   . VAL A 1 122 ? 44.829 52.846 -7.597  1.00 12.40  ? 803  VAL A N   1 
ATOM   969  C CA  . VAL A 1 122 ? 44.234 52.353 -8.833  1.00 13.80  ? 803  VAL A CA  1 
ATOM   970  C C   . VAL A 1 122 ? 43.727 53.543 -9.635  1.00 12.28  ? 803  VAL A C   1 
ATOM   971  O O   . VAL A 1 122 ? 43.026 54.412 -9.099  1.00 11.73  ? 803  VAL A O   1 
ATOM   972  C CB  . VAL A 1 122 ? 43.096 51.364 -8.533  1.00 13.30  ? 803  VAL A CB  1 
ATOM   973  C CG1 . VAL A 1 122 ? 42.322 51.046 -9.794  1.00 15.44  ? 803  VAL A CG1 1 
ATOM   974  C CG2 . VAL A 1 122 ? 43.669 50.097 -7.912  1.00 9.77   ? 803  VAL A CG2 1 
ATOM   975  N N   . ASN A 1 123 ? 44.061 53.572 -10.924 1.00 12.25  ? 804  ASN A N   1 
ATOM   976  C CA  . ASN A 1 123 ? 43.729 54.677 -11.810 1.00 15.14  ? 804  ASN A CA  1 
ATOM   977  C C   . ASN A 1 123 ? 42.633 54.286 -12.792 1.00 17.17  ? 804  ASN A C   1 
ATOM   978  O O   . ASN A 1 123 ? 42.468 53.113 -13.137 1.00 12.90  ? 804  ASN A O   1 
ATOM   979  C CB  . ASN A 1 123 ? 44.953 55.133 -12.607 1.00 17.17  ? 804  ASN A CB  1 
ATOM   980  C CG  . ASN A 1 123 ? 45.959 55.867 -11.760 1.00 18.76  ? 804  ASN A CG  1 
ATOM   981  O OD1 . ASN A 1 123 ? 45.750 56.063 -10.561 1.00 19.30  ? 804  ASN A OD1 1 
ATOM   982  N ND2 . ASN A 1 123 ? 47.068 56.270 -12.374 1.00 19.06  ? 804  ASN A ND2 1 
ATOM   983  N N   . VAL A 1 124 ? 41.895 55.297 -13.256 1.00 11.51  ? 805  VAL A N   1 
ATOM   984  C CA  . VAL A 1 124 ? 40.959 55.082 -14.349 1.00 11.12  ? 805  VAL A CA  1 
ATOM   985  C C   . VAL A 1 124 ? 41.737 54.566 -15.552 1.00 19.39  ? 805  VAL A C   1 
ATOM   986  O O   . VAL A 1 124 ? 42.856 55.018 -15.830 1.00 14.24  ? 805  VAL A O   1 
ATOM   987  C CB  . VAL A 1 124 ? 40.198 56.390 -14.643 1.00 11.49  ? 805  VAL A CB  1 
ATOM   988  C CG1 . VAL A 1 124 ? 39.395 56.289 -15.929 1.00 11.94  ? 805  VAL A CG1 1 
ATOM   989  C CG2 . VAL A 1 124 ? 39.301 56.733 -13.466 1.00 11.31  ? 805  VAL A CG2 1 
ATOM   990  N N   . ASN A 1 125 ? 41.176 53.555 -16.216 1.00 11.71  ? 806  ASN A N   1 
ATOM   991  C CA  . ASN A 1 125 ? 41.703 52.787 -17.347 1.00 14.73  ? 806  ASN A CA  1 
ATOM   992  C C   . ASN A 1 125 ? 42.575 51.616 -16.890 1.00 15.07  ? 806  ASN A C   1 
ATOM   993  O O   . ASN A 1 125 ? 43.026 50.841 -17.741 1.00 15.13  ? 806  ASN A O   1 
ATOM   994  C CB  . ASN A 1 125 ? 42.489 53.640 -18.359 1.00 17.96  ? 806  ASN A CB  1 
ATOM   995  C CG  . ASN A 1 125 ? 41.617 54.676 -19.038 1.00 23.41  ? 806  ASN A CG  1 
ATOM   996  O OD1 . ASN A 1 125 ? 40.470 54.400 -19.391 1.00 24.77  ? 806  ASN A OD1 1 
ATOM   997  N ND2 . ASN A 1 125 ? 42.153 55.880 -19.216 1.00 27.45  ? 806  ASN A ND2 1 
ATOM   998  N N   . ASP A 1 126 ? 42.820 51.455 -15.591 1.00 13.99  ? 807  ASP A N   1 
ATOM   999  C CA  . ASP A 1 126 ? 43.423 50.233 -15.086 1.00 16.52  ? 807  ASP A CA  1 
ATOM   1000 C C   . ASP A 1 126 ? 42.484 49.057 -15.313 1.00 13.91  ? 807  ASP A C   1 
ATOM   1001 O O   . ASP A 1 126 ? 41.257 49.205 -15.317 1.00 12.68  ? 807  ASP A O   1 
ATOM   1002 C CB  . ASP A 1 126 ? 43.730 50.343 -13.593 1.00 12.86  ? 807  ASP A CB  1 
ATOM   1003 C CG  . ASP A 1 126 ? 44.985 51.134 -13.308 1.00 12.42  ? 807  ASP A CG  1 
ATOM   1004 O OD1 . ASP A 1 126 ? 45.625 51.599 -14.268 1.00 12.14  ? 807  ASP A OD1 1 
ATOM   1005 O OD2 . ASP A 1 126 ? 45.332 51.272 -12.119 1.00 10.25  ? 807  ASP A OD2 1 
ATOM   1006 N N   . LYS A 1 127 ? 43.076 47.884 -15.506 1.00 11.31  ? 808  LYS A N   1 
ATOM   1007 C CA  . LYS A 1 127 ? 42.334 46.637 -15.644 1.00 18.37  ? 808  LYS A CA  1 
ATOM   1008 C C   . LYS A 1 127 ? 42.449 45.839 -14.351 1.00 10.85  ? 808  LYS A C   1 
ATOM   1009 O O   . LYS A 1 127 ? 43.555 45.621 -13.844 1.00 14.58  ? 808  LYS A O   1 
ATOM   1010 C CB  . LYS A 1 127 ? 42.858 45.822 -16.826 1.00 16.70  ? 808  LYS A CB  1 
ATOM   1011 C CG  . LYS A 1 127 ? 42.541 46.451 -18.176 1.00 22.40  ? 808  LYS A CG  1 
ATOM   1012 C CD  . LYS A 1 127 ? 43.361 45.837 -19.302 1.00 32.91  ? 808  LYS A CD  1 
ATOM   1013 C CE  . LYS A 1 127 ? 42.969 46.433 -20.650 1.00 32.79  ? 808  LYS A CE  1 
ATOM   1014 N NZ  . LYS A 1 127 ? 41.569 46.074 -21.033 1.00 29.54  ? 808  LYS A NZ  1 
ATOM   1015 N N   . LEU A 1 128 ? 41.308 45.431 -13.811 1.00 10.28  ? 809  LEU A N   1 
ATOM   1016 C CA  . LEU A 1 128 ? 41.253 44.705 -12.556 1.00 11.81  ? 809  LEU A CA  1 
ATOM   1017 C C   . LEU A 1 128 ? 40.694 43.314 -12.792 1.00 10.75  ? 809  LEU A C   1 
ATOM   1018 O O   . LEU A 1 128 ? 40.051 43.039 -13.804 1.00 14.09  ? 809  LEU A O   1 
ATOM   1019 C CB  . LEU A 1 128 ? 40.379 45.419 -11.526 1.00 11.32  ? 809  LEU A CB  1 
ATOM   1020 C CG  . LEU A 1 128 ? 40.715 46.866 -11.165 1.00 12.71  ? 809  LEU A CG  1 
ATOM   1021 C CD1 . LEU A 1 128 ? 39.656 47.395 -10.215 1.00 11.56  ? 809  LEU A CD1 1 
ATOM   1022 C CD2 . LEU A 1 128 ? 42.095 46.951 -10.530 1.00 14.39  ? 809  LEU A CD2 1 
ATOM   1023 N N   . ASN A 1 129 ? 40.929 42.447 -11.821 1.00 9.89   ? 810  ASN A N   1 
ATOM   1024 C CA  . ASN A 1 129 ? 40.405 41.095 -11.840 1.00 10.04  ? 810  ASN A CA  1 
ATOM   1025 C C   . ASN A 1 129 ? 39.567 40.914 -10.590 1.00 10.27  ? 810  ASN A C   1 
ATOM   1026 O O   . ASN A 1 129 ? 40.074 41.044 -9.471  1.00 9.93   ? 810  ASN A O   1 
ATOM   1027 C CB  . ASN A 1 129 ? 41.537 40.075 -11.931 1.00 13.75  ? 810  ASN A CB  1 
ATOM   1028 C CG  . ASN A 1 129 ? 42.096 39.986 -13.333 1.00 12.59  ? 810  ASN A CG  1 
ATOM   1029 O OD1 . ASN A 1 129 ? 41.540 39.294 -14.185 1.00 14.39  ? 810  ASN A OD1 1 
ATOM   1030 N ND2 . ASN A 1 129 ? 43.176 40.717 -13.593 1.00 14.97  ? 810  ASN A ND2 1 
ATOM   1031 N N   . VAL A 1 130 ? 38.277 40.668 -10.788 1.00 11.74  ? 811  VAL A N   1 
ATOM   1032 C CA  . VAL A 1 130 ? 37.309 40.650 -9.709  1.00 9.77   ? 811  VAL A CA  1 
ATOM   1033 C C   . VAL A 1 130 ? 36.629 39.296 -9.721  1.00 10.02  ? 811  VAL A C   1 
ATOM   1034 O O   . VAL A 1 130 ? 36.194 38.819 -10.777 1.00 13.68  ? 811  VAL A O   1 
ATOM   1035 C CB  . VAL A 1 130 ? 36.289 41.791 -9.857  1.00 11.72  ? 811  VAL A CB  1 
ATOM   1036 C CG1 . VAL A 1 130 ? 35.331 41.813 -8.670  1.00 9.70   ? 811  VAL A CG1 1 
ATOM   1037 C CG2 . VAL A 1 130 ? 37.023 43.126 -9.989  1.00 9.68   ? 811  VAL A CG2 1 
ATOM   1038 N N   . TYR A 1 131 ? 36.526 38.691 -8.550  1.00 9.83   ? 812  TYR A N   1 
ATOM   1039 C CA  . TYR A 1 131 ? 35.965 37.361 -8.400  1.00 12.69  ? 812  TYR A CA  1 
ATOM   1040 C C   . TYR A 1 131 ? 34.774 37.420 -7.458  1.00 10.04  ? 812  TYR A C   1 
ATOM   1041 O O   . TYR A 1 131 ? 34.764 38.214 -6.516  1.00 13.15  ? 812  TYR A O   1 
ATOM   1042 C CB  . TYR A 1 131 ? 37.013 36.408 -7.850  1.00 10.38  ? 812  TYR A CB  1 
ATOM   1043 C CG  . TYR A 1 131 ? 38.186 36.128 -8.770  1.00 12.32  ? 812  TYR A CG  1 
ATOM   1044 C CD1 . TYR A 1 131 ? 39.154 37.095 -9.023  1.00 12.00  ? 812  TYR A CD1 1 
ATOM   1045 C CD2 . TYR A 1 131 ? 38.344 34.876 -9.353  1.00 13.78  ? 812  TYR A CD2 1 
ATOM   1046 C CE1 . TYR A 1 131 ? 40.248 36.821 -9.852  1.00 13.65  ? 812  TYR A CE1 1 
ATOM   1047 C CE2 . TYR A 1 131 ? 39.426 34.595 -10.181 1.00 14.01  ? 812  TYR A CE2 1 
ATOM   1048 C CZ  . TYR A 1 131 ? 40.375 35.568 -10.423 1.00 16.50  ? 812  TYR A CZ  1 
ATOM   1049 O OH  . TYR A 1 131 ? 41.451 35.281 -11.245 1.00 16.73  ? 812  TYR A OH  1 
ATOM   1050 N N   . GLY A 1 132 ? 33.776 36.575 -7.702  1.00 10.42  ? 813  GLY A N   1 
ATOM   1051 C CA  . GLY A 1 132 ? 32.631 36.537 -6.811  1.00 11.80  ? 813  GLY A CA  1 
ATOM   1052 C C   . GLY A 1 132 ? 31.603 35.523 -7.265  1.00 11.49  ? 813  GLY A C   1 
ATOM   1053 O O   . GLY A 1 132 ? 31.855 34.701 -8.152  1.00 11.44  ? 813  GLY A O   1 
ATOM   1054 N N   . TYR A 1 133 ? 30.421 35.597 -6.651  1.00 11.17  ? 814  TYR A N   1 
ATOM   1055 C CA  . TYR A 1 133 ? 29.345 34.639 -6.903  1.00 12.12  ? 814  TYR A CA  1 
ATOM   1056 C C   . TYR A 1 133 ? 28.034 35.357 -7.187  1.00 13.57  ? 814  TYR A C   1 
ATOM   1057 O O   . TYR A 1 133 ? 27.091 35.291 -6.390  1.00 13.74  ? 814  TYR A O   1 
ATOM   1058 C CB  . TYR A 1 133 ? 29.198 33.673 -5.728  1.00 12.11  ? 814  TYR A CB  1 
ATOM   1059 C CG  . TYR A 1 133 ? 30.411 32.792 -5.598  1.00 11.54  ? 814  TYR A CG  1 
ATOM   1060 C CD1 . TYR A 1 133 ? 31.549 33.242 -4.942  1.00 11.00  ? 814  TYR A CD1 1 
ATOM   1061 C CD2 . TYR A 1 133 ? 30.436 31.529 -6.173  1.00 11.98  ? 814  TYR A CD2 1 
ATOM   1062 C CE1 . TYR A 1 133 ? 32.666 32.450 -4.851  1.00 10.92  ? 814  TYR A CE1 1 
ATOM   1063 C CE2 . TYR A 1 133 ? 31.544 30.730 -6.082  1.00 11.88  ? 814  TYR A CE2 1 
ATOM   1064 C CZ  . TYR A 1 133 ? 32.651 31.188 -5.416  1.00 12.49  ? 814  TYR A CZ  1 
ATOM   1065 O OH  . TYR A 1 133 ? 33.764 30.397 -5.323  1.00 13.26  ? 814  TYR A OH  1 
ATOM   1066 N N   . PRO A 1 134 ? 27.931 36.028 -8.336  1.00 15.92  ? 815  PRO A N   1 
ATOM   1067 C CA  . PRO A 1 134 ? 26.638 36.605 -8.737  1.00 16.09  ? 815  PRO A CA  1 
ATOM   1068 C C   . PRO A 1 134 ? 25.586 35.515 -8.858  1.00 15.91  ? 815  PRO A C   1 
ATOM   1069 O O   . PRO A 1 134 ? 25.764 34.530 -9.581  1.00 16.17  ? 815  PRO A O   1 
ATOM   1070 C CB  . PRO A 1 134 ? 26.943 37.261 -10.090 1.00 14.59  ? 815  PRO A CB  1 
ATOM   1071 C CG  . PRO A 1 134 ? 28.165 36.539 -10.593 1.00 15.94  ? 815  PRO A CG  1 
ATOM   1072 C CD  . PRO A 1 134 ? 28.964 36.210 -9.370  1.00 12.63  ? 815  PRO A CD  1 
ATOM   1073 N N   . ARG A 1 135 ? 24.490 35.687 -8.118  1.00 13.83  ? 816  ARG A N   1 
ATOM   1074 C CA  . ARG A 1 135 ? 23.419 34.688 -8.051  1.00 17.71  ? 816  ARG A CA  1 
ATOM   1075 C C   . ARG A 1 135 ? 23.934 33.346 -7.534  1.00 19.58  ? 816  ARG A C   1 
ATOM   1076 O O   . ARG A 1 135 ? 23.378 32.285 -7.848  1.00 23.76  ? 816  ARG A O   1 
ATOM   1077 C CB  . ARG A 1 135 ? 22.736 34.530 -9.410  1.00 23.63  ? 816  ARG A CB  1 
ATOM   1078 C CG  . ARG A 1 135 ? 21.999 35.791 -9.846  1.00 40.50  ? 816  ARG A CG  1 
ATOM   1079 C CD  . ARG A 1 135 ? 21.263 35.604 -11.157 1.00 39.14  ? 816  ARG A CD  1 
ATOM   1080 N NE  . ARG A 1 135 ? 20.203 34.611 -11.044 1.00 59.96  ? 816  ARG A NE  1 
ATOM   1081 C CZ  . ARG A 1 135 ? 20.303 33.359 -11.467 1.00 50.96  ? 816  ARG A CZ  1 
ATOM   1082 N NH1 . ARG A 1 135 ? 21.405 32.916 -12.052 1.00 41.38  ? 816  ARG A NH1 1 
ATOM   1083 N NH2 . ARG A 1 135 ? 19.272 32.534 -11.305 1.00 49.05  ? 816  ARG A NH2 1 
ATOM   1084 N N   . GLY A 1 136 ? 24.990 33.394 -6.727  1.00 13.65  ? 817  GLY A N   1 
ATOM   1085 C CA  . GLY A 1 136 ? 25.607 32.220 -6.154  1.00 13.50  ? 817  GLY A CA  1 
ATOM   1086 C C   . GLY A 1 136 ? 26.439 31.402 -7.111  1.00 14.65  ? 817  GLY A C   1 
ATOM   1087 O O   . GLY A 1 136 ? 26.911 30.326 -6.724  1.00 16.86  ? 817  GLY A O   1 
ATOM   1088 N N   . GLU A 1 137 ? 26.631 31.870 -8.342  1.00 13.79  ? 818  GLU A N   1 
ATOM   1089 C CA  . GLU A 1 137 ? 27.397 31.165 -9.359  1.00 15.21  ? 818  GLU A CA  1 
ATOM   1090 C C   . GLU A 1 137 ? 28.770 31.811 -9.503  1.00 16.49  ? 818  GLU A C   1 
ATOM   1091 O O   . GLU A 1 137 ? 28.890 33.040 -9.487  1.00 12.99  ? 818  GLU A O   1 
ATOM   1092 C CB  . GLU A 1 137 ? 26.665 31.186 -10.704 1.00 15.56  ? 818  GLU A CB  1 
ATOM   1093 C CG  . GLU A 1 137 ? 25.226 30.671 -10.636 1.00 19.79  ? 818  GLU A CG  1 
ATOM   1094 C CD  . GLU A 1 137 ? 24.489 30.751 -11.963 1.00 20.96  ? 818  GLU A CD  1 
ATOM   1095 O OE1 . GLU A 1 137 ? 25.041 31.305 -12.935 1.00 22.86  ? 818  GLU A OE1 1 
ATOM   1096 O OE2 . GLU A 1 137 ? 23.348 30.253 -12.035 1.00 20.14  ? 818  GLU A OE2 1 
ATOM   1097 N N   . TYR A 1 138 ? 29.799 30.979 -9.661  1.00 15.39  ? 819  TYR A N   1 
ATOM   1098 C CA  . TYR A 1 138 ? 31.168 31.485 -9.714  1.00 12.80  ? 819  TYR A CA  1 
ATOM   1099 C C   . TYR A 1 138 ? 31.391 32.339 -10.958 1.00 12.84  ? 819  TYR A C   1 
ATOM   1100 O O   . TYR A 1 138 ? 31.040 31.947 -12.073 1.00 13.44  ? 819  TYR A O   1 
ATOM   1101 C CB  . TYR A 1 138 ? 32.166 30.325 -9.701  1.00 17.14  ? 819  TYR A CB  1 
ATOM   1102 C CG  . TYR A 1 138 ? 33.596 30.755 -9.970  1.00 14.67  ? 819  TYR A CG  1 
ATOM   1103 C CD1 . TYR A 1 138 ? 34.383 31.288 -8.954  1.00 12.66  ? 819  TYR A CD1 1 
ATOM   1104 C CD2 . TYR A 1 138 ? 34.150 30.656 -11.244 1.00 16.26  ? 819  TYR A CD2 1 
ATOM   1105 C CE1 . TYR A 1 138 ? 35.688 31.687 -9.191  1.00 15.75  ? 819  TYR A CE1 1 
ATOM   1106 C CE2 . TYR A 1 138 ? 35.454 31.061 -11.491 1.00 15.86  ? 819  TYR A CE2 1 
ATOM   1107 C CZ  . TYR A 1 138 ? 36.213 31.579 -10.461 1.00 16.71  ? 819  TYR A CZ  1 
ATOM   1108 O OH  . TYR A 1 138 ? 37.509 31.975 -10.696 1.00 13.46  ? 819  TYR A OH  1 
ATOM   1109 N N   . ALA A 1 139 ? 32.035 33.490 -10.773 1.00 13.75  ? 820  ALA A N   1 
ATOM   1110 C CA  . ALA A 1 139 ? 32.304 34.377 -11.895 1.00 12.40  ? 820  ALA A CA  1 
ATOM   1111 C C   . ALA A 1 139 ? 33.629 35.089 -11.685 1.00 11.85  ? 820  ALA A C   1 
ATOM   1112 O O   . ALA A 1 139 ? 33.977 35.452 -10.560 1.00 11.35  ? 820  ALA A O   1 
ATOM   1113 C CB  . ALA A 1 139 ? 31.188 35.412 -12.088 1.00 14.91  ? 820  ALA A CB  1 
ATOM   1114 N N   . HIS A 1 140 ? 34.349 35.284 -12.785 1.00 12.01  ? 821  HIS A N   1 
ATOM   1115 C CA  . HIS A 1 140 ? 35.616 36.010 -12.806 1.00 14.33  ? 821  HIS A CA  1 
ATOM   1116 C C   . HIS A 1 140 ? 35.483 37.116 -13.839 1.00 11.79  ? 821  HIS A C   1 
ATOM   1117 O O   . HIS A 1 140 ? 35.335 36.839 -15.032 1.00 13.92  ? 821  HIS A O   1 
ATOM   1118 C CB  . HIS A 1 140 ? 36.783 35.069 -13.142 1.00 11.75  ? 821  HIS A CB  1 
ATOM   1119 C CG  . HIS A 1 140 ? 38.087 35.771 -13.379 1.00 11.57  ? 821  HIS A CG  1 
ATOM   1120 N ND1 . HIS A 1 140 ? 39.129 35.186 -14.066 1.00 14.81  ? 821  HIS A ND1 1 
ATOM   1121 C CD2 . HIS A 1 140 ? 38.515 37.011 -13.034 1.00 11.11  ? 821  HIS A CD2 1 
ATOM   1122 C CE1 . HIS A 1 140 ? 40.145 36.030 -14.127 1.00 18.03  ? 821  HIS A CE1 1 
ATOM   1123 N NE2 . HIS A 1 140 ? 39.798 37.146 -13.508 1.00 11.13  ? 821  HIS A NE2 1 
ATOM   1124 N N   . LEU A 1 141 ? 35.511 38.365 -13.383 1.00 11.41  ? 822  LEU A N   1 
ATOM   1125 C CA  . LEU A 1 141 ? 35.569 39.514 -14.282 1.00 11.54  ? 822  LEU A CA  1 
ATOM   1126 C C   . LEU A 1 141 ? 37.039 39.748 -14.612 1.00 11.38  ? 822  LEU A C   1 
ATOM   1127 O O   . LEU A 1 141 ? 37.776 40.333 -13.819 1.00 14.01  ? 822  LEU A O   1 
ATOM   1128 C CB  . LEU A 1 141 ? 34.942 40.743 -13.634 1.00 13.41  ? 822  LEU A CB  1 
ATOM   1129 C CG  . LEU A 1 141 ? 33.523 40.599 -13.078 1.00 13.19  ? 822  LEU A CG  1 
ATOM   1130 C CD1 . LEU A 1 141 ? 33.043 41.943 -12.510 1.00 19.95  ? 822  LEU A CD1 1 
ATOM   1131 C CD2 . LEU A 1 141 ? 32.597 40.122 -14.166 1.00 12.13  ? 822  LEU A CD2 1 
ATOM   1132 N N   . LYS A 1 142 ? 37.470 39.284 -15.784 1.00 11.80  ? 823  LYS A N   1 
ATOM   1133 C CA  . LYS A 1 142 ? 38.882 39.311 -16.154 1.00 13.87  ? 823  LYS A CA  1 
ATOM   1134 C C   . LYS A 1 142 ? 39.216 40.643 -16.817 1.00 14.51  ? 823  LYS A C   1 
ATOM   1135 O O   . LYS A 1 142 ? 38.595 41.013 -17.818 1.00 12.21  ? 823  LYS A O   1 
ATOM   1136 C CB  . LYS A 1 142 ? 39.218 38.146 -17.088 1.00 18.85  ? 823  LYS A CB  1 
ATOM   1137 C CG  . LYS A 1 142 ? 40.702 38.040 -17.444 1.00 21.06  ? 823  LYS A CG  1 
ATOM   1138 C CD  . LYS A 1 142 ? 41.025 36.760 -18.218 1.00 18.23  ? 823  LYS A CD  1 
ATOM   1139 C CE  . LYS A 1 142 ? 40.478 36.819 -19.629 1.00 27.38  ? 823  LYS A CE  1 
ATOM   1140 N NZ  . LYS A 1 142 ? 40.833 35.605 -20.425 1.00 29.38  ? 823  LYS A NZ  1 
ATOM   1141 N N   . ASP A 1 143 ? 40.201 41.352 -16.260 1.00 11.41  ? 824  ASP A N   1 
ATOM   1142 C CA  . ASP A 1 143 ? 40.706 42.603 -16.818 1.00 11.46  ? 824  ASP A CA  1 
ATOM   1143 C C   . ASP A 1 143 ? 39.572 43.581 -17.122 1.00 17.23  ? 824  ASP A C   1 
ATOM   1144 O O   . ASP A 1 143 ? 39.494 44.157 -18.210 1.00 13.20  ? 824  ASP A O   1 
ATOM   1145 C CB  . ASP A 1 143 ? 41.551 42.345 -18.069 1.00 16.39  ? 824  ASP A CB  1 
ATOM   1146 C CG  . ASP A 1 143 ? 42.823 41.569 -17.768 1.00 16.45  ? 824  ASP A CG  1 
ATOM   1147 O OD1 . ASP A 1 143 ? 43.304 41.630 -16.619 1.00 17.19  ? 824  ASP A OD1 1 
ATOM   1148 O OD2 . ASP A 1 143 ? 43.343 40.891 -18.679 1.00 19.45  ? 824  ASP A OD2 1 
ATOM   1149 N N   . THR A 1 144 ? 38.670 43.759 -16.158 1.00 15.01  ? 825  THR A N   1 
ATOM   1150 C CA  . THR A 1 144 ? 37.611 44.745 -16.331 1.00 16.03  ? 825  THR A CA  1 
ATOM   1151 C C   . THR A 1 144 ? 38.188 46.135 -16.079 1.00 13.57  ? 825  THR A C   1 
ATOM   1152 O O   . THR A 1 144 ? 38.990 46.338 -15.164 1.00 15.11  ? 825  THR A O   1 
ATOM   1153 C CB  . THR A 1 144 ? 36.405 44.462 -15.423 1.00 16.92  ? 825  THR A CB  1 
ATOM   1154 O OG1 . THR A 1 144 ? 35.390 45.451 -15.655 1.00 20.21  ? 825  THR A OG1 1 
ATOM   1155 C CG2 . THR A 1 144 ? 36.771 44.465 -13.945 1.00 11.63  ? 825  THR A CG2 1 
ATOM   1156 N N   . THR A 1 145 ? 37.802 47.082 -16.923 1.00 16.57  ? 826  THR A N   1 
ATOM   1157 C CA  A THR A 1 145 ? 38.427 48.398 -16.927 0.70 13.48  ? 826  THR A CA  1 
ATOM   1158 C CA  B THR A 1 145 ? 38.419 48.403 -16.937 0.30 12.99  ? 826  THR A CA  1 
ATOM   1159 C C   . THR A 1 145 ? 37.773 49.321 -15.908 1.00 11.74  ? 826  THR A C   1 
ATOM   1160 O O   . THR A 1 145 ? 36.549 49.351 -15.769 1.00 12.30  ? 826  THR A O   1 
ATOM   1161 C CB  A THR A 1 145 ? 38.348 49.019 -18.322 0.70 15.14  ? 826  THR A CB  1 
ATOM   1162 C CB  B THR A 1 145 ? 38.292 49.029 -18.328 0.30 15.24  ? 826  THR A CB  1 
ATOM   1163 O OG1 A THR A 1 145 ? 36.980 49.120 -18.725 0.70 20.83  ? 826  THR A OG1 1 
ATOM   1164 O OG1 B THR A 1 145 ? 38.756 48.102 -19.319 0.30 15.21  ? 826  THR A OG1 1 
ATOM   1165 C CG2 A THR A 1 145 ? 39.099 48.159 -19.330 0.70 15.51  ? 826  THR A CG2 1 
ATOM   1166 C CG2 B THR A 1 145 ? 39.102 50.319 -18.419 0.30 12.12  ? 826  THR A CG2 1 
ATOM   1167 N N   . VAL A 1 146 ? 38.600 50.084 -15.197 1.00 11.01  ? 827  VAL A N   1 
ATOM   1168 C CA  . VAL A 1 146 ? 38.085 51.108 -14.293 1.00 12.51  ? 827  VAL A CA  1 
ATOM   1169 C C   . VAL A 1 146 ? 37.667 52.314 -15.126 1.00 12.53  ? 827  VAL A C   1 
ATOM   1170 O O   . VAL A 1 146 ? 38.468 52.867 -15.886 1.00 13.55  ? 827  VAL A O   1 
ATOM   1171 C CB  . VAL A 1 146 ? 39.125 51.497 -13.234 1.00 15.96  ? 827  VAL A CB  1 
ATOM   1172 C CG1 . VAL A 1 146 ? 38.623 52.670 -12.412 1.00 12.00  ? 827  VAL A CG1 1 
ATOM   1173 C CG2 . VAL A 1 146 ? 39.408 50.312 -12.334 1.00 14.19  ? 827  VAL A CG2 1 
ATOM   1174 N N   . GLU A 1 147 ? 36.405 52.711 -15.003 1.00 12.17  ? 828  GLU A N   1 
ATOM   1175 C CA  . GLU A 1 147 ? 35.877 53.815 -15.795 1.00 17.20  ? 828  GLU A CA  1 
ATOM   1176 C C   . GLU A 1 147 ? 35.699 55.098 -14.998 1.00 16.73  ? 828  GLU A C   1 
ATOM   1177 O O   . GLU A 1 147 ? 35.820 56.186 -15.568 1.00 15.70  ? 828  GLU A O   1 
ATOM   1178 C CB  . GLU A 1 147 ? 34.536 53.419 -16.417 1.00 14.32  ? 828  GLU A CB  1 
ATOM   1179 C CG  . GLU A 1 147 ? 34.655 52.259 -17.389 1.00 21.34  ? 828  GLU A CG  1 
ATOM   1180 C CD  . GLU A 1 147 ? 33.311 51.722 -17.816 1.00 34.87  ? 828  GLU A CD  1 
ATOM   1181 O OE1 . GLU A 1 147 ? 32.281 52.298 -17.400 1.00 26.59  ? 828  GLU A OE1 1 
ATOM   1182 O OE2 . GLU A 1 147 ? 33.284 50.721 -18.564 1.00 26.68  ? 828  GLU A OE2 1 
ATOM   1183 N N   . ILE A 1 148 ? 35.433 54.992 -13.699 1.00 15.37  ? 829  ILE A N   1 
ATOM   1184 C CA  . ILE A 1 148 ? 35.114 56.126 -12.841 1.00 12.73  ? 829  ILE A CA  1 
ATOM   1185 C C   . ILE A 1 148 ? 35.745 55.870 -11.483 1.00 14.28  ? 829  ILE A C   1 
ATOM   1186 O O   . ILE A 1 148 ? 35.774 54.728 -11.018 1.00 13.89  ? 829  ILE A O   1 
ATOM   1187 C CB  . ILE A 1 148 ? 33.583 56.299 -12.701 1.00 14.96  ? 829  ILE A CB  1 
ATOM   1188 C CG1 . ILE A 1 148 ? 32.947 56.660 -14.037 1.00 19.83  ? 829  ILE A CG1 1 
ATOM   1189 C CG2 . ILE A 1 148 ? 33.251 57.336 -11.655 1.00 21.54  ? 829  ILE A CG2 1 
ATOM   1190 C CD1 . ILE A 1 148 ? 33.276 58.038 -14.507 1.00 24.07  ? 829  ILE A CD1 1 
ATOM   1191 N N   . GLU A 1 149 ? 36.256 56.918 -10.840 1.00 12.10  ? 830  GLU A N   1 
ATOM   1192 C CA  . GLU A 1 149 ? 36.758 56.776 -9.482  1.00 12.31  ? 830  GLU A CA  1 
ATOM   1193 C C   . GLU A 1 149 ? 36.101 57.806 -8.574  1.00 12.33  ? 830  GLU A C   1 
ATOM   1194 O O   . GLU A 1 149 ? 35.742 58.903 -9.010  1.00 12.76  ? 830  GLU A O   1 
ATOM   1195 C CB  . GLU A 1 149 ? 38.291 56.920 -9.420  1.00 13.80  ? 830  GLU A CB  1 
ATOM   1196 C CG  . GLU A 1 149 ? 38.784 58.315 -9.775  1.00 14.38  ? 830  GLU A CG  1 
ATOM   1197 C CD  . GLU A 1 149 ? 40.295 58.463 -9.668  1.00 18.83  ? 830  GLU A CD  1 
ATOM   1198 O OE1 . GLU A 1 149 ? 40.961 57.572 -9.102  1.00 17.18  ? 830  GLU A OE1 1 
ATOM   1199 O OE2 . GLU A 1 149 ? 40.806 59.489 -10.149 1.00 28.71  ? 830  GLU A OE2 1 
ATOM   1200 N N   . GLN A 1 150 ? 35.971 57.452 -7.299  1.00 10.61  ? 831  GLN A N   1 
ATOM   1201 C CA  . GLN A 1 150 ? 35.336 58.312 -6.307  1.00 10.79  ? 831  GLN A CA  1 
ATOM   1202 C C   . GLN A 1 150 ? 36.214 58.382 -5.072  1.00 11.89  ? 831  GLN A C   1 
ATOM   1203 O O   . GLN A 1 150 ? 36.426 57.367 -4.404  1.00 12.25  ? 831  GLN A O   1 
ATOM   1204 C CB  . GLN A 1 150 ? 33.942 57.788 -5.933  1.00 12.25  ? 831  GLN A CB  1 
ATOM   1205 C CG  . GLN A 1 150 ? 33.240 58.641 -4.891  1.00 13.69  ? 831  GLN A CG  1 
ATOM   1206 C CD  . GLN A 1 150 ? 31.770 58.297 -4.739  1.00 16.71  ? 831  GLN A CD  1 
ATOM   1207 O OE1 . GLN A 1 150 ? 31.239 57.441 -5.452  1.00 20.73  ? 831  GLN A OE1 1 
ATOM   1208 N NE2 . GLN A 1 150 ? 31.109 58.959 -3.809  1.00 17.00  ? 831  GLN A NE2 1 
ATOM   1209 N N   . LYS A 1 151 ? 36.724 59.570 -4.759  1.00 10.75  ? 832  LYS A N   1 
ATOM   1210 C CA  . LYS A 1 151 ? 37.530 59.728 -3.552  1.00 10.62  ? 832  LYS A CA  1 
ATOM   1211 C C   . LYS A 1 151 ? 36.612 59.807 -2.339  1.00 10.68  ? 832  LYS A C   1 
ATOM   1212 O O   . LYS A 1 151 ? 35.881 60.791 -2.162  1.00 16.76  ? 832  LYS A O   1 
ATOM   1213 C CB  . LYS A 1 151 ? 38.420 60.967 -3.641  1.00 13.69  ? 832  LYS A CB  1 
ATOM   1214 C CG  . LYS A 1 151 ? 39.285 61.177 -2.401  1.00 14.38  ? 832  LYS A CG  1 
ATOM   1215 C CD  . LYS A 1 151 ? 40.246 62.358 -2.583  1.00 18.66  ? 832  LYS A CD  1 
ATOM   1216 C CE  . LYS A 1 151 ? 41.173 62.525 -1.388  1.00 19.53  ? 832  LYS A CE  1 
ATOM   1217 N NZ  . LYS A 1 151 ? 42.367 63.342 -1.741  1.00 28.03  ? 832  LYS A NZ  1 
ATOM   1218 N N   . TYR A 1 152 ? 36.642 58.763 -1.507  1.00 10.55  ? 833  TYR A N   1 
ATOM   1219 C CA  . TYR A 1 152 ? 35.874 58.740 -0.267  1.00 14.20  ? 833  TYR A CA  1 
ATOM   1220 C C   . TYR A 1 152 ? 36.621 59.441 0.855   1.00 14.79  ? 833  TYR A C   1 
ATOM   1221 O O   . TYR A 1 152 ? 36.001 60.028 1.748   1.00 21.58  ? 833  TYR A O   1 
ATOM   1222 C CB  . TYR A 1 152 ? 35.581 57.300 0.160   1.00 13.07  ? 833  TYR A CB  1 
ATOM   1223 C CG  . TYR A 1 152 ? 34.678 56.475 -0.743  1.00 10.70  ? 833  TYR A CG  1 
ATOM   1224 C CD1 . TYR A 1 152 ? 33.532 57.012 -1.311  1.00 13.19  ? 833  TYR A CD1 1 
ATOM   1225 C CD2 . TYR A 1 152 ? 34.963 55.139 -0.986  1.00 10.05  ? 833  TYR A CD2 1 
ATOM   1226 C CE1 . TYR A 1 152 ? 32.691 56.241 -2.116  1.00 14.49  ? 833  TYR A CE1 1 
ATOM   1227 C CE2 . TYR A 1 152 ? 34.141 54.360 -1.794  1.00 13.73  ? 833  TYR A CE2 1 
ATOM   1228 C CZ  . TYR A 1 152 ? 33.001 54.916 -2.354  1.00 11.94  ? 833  TYR A CZ  1 
ATOM   1229 O OH  . TYR A 1 152 ? 32.172 54.142 -3.155  1.00 11.21  ? 833  TYR A OH  1 
ATOM   1230 N N   . ALA A 1 153 ? 37.948 59.353 0.839   1.00 13.23  ? 834  ALA A N   1 
ATOM   1231 C CA  . ALA A 1 153 ? 38.812 59.957 1.843   1.00 11.74  ? 834  ALA A CA  1 
ATOM   1232 C C   . ALA A 1 153 ? 40.232 59.873 1.301   1.00 12.51  ? 834  ALA A C   1 
ATOM   1233 O O   . ALA A 1 153 ? 40.468 59.355 0.204   1.00 13.01  ? 834  ALA A O   1 
ATOM   1234 C CB  . ALA A 1 153 ? 38.684 59.267 3.205   1.00 10.81  ? 834  ALA A CB  1 
ATOM   1235 N N   . ASN A 1 154 ? 41.174 60.387 2.077   1.00 10.83  ? 835  ASN A N   1 
ATOM   1236 C CA  . ASN A 1 154 ? 42.566 60.359 1.653   1.00 10.91  ? 835  ASN A CA  1 
ATOM   1237 C C   . ASN A 1 154 ? 42.990 58.927 1.348   1.00 10.47  ? 835  ASN A C   1 
ATOM   1238 O O   . ASN A 1 154 ? 42.852 58.040 2.193   1.00 11.87  ? 835  ASN A O   1 
ATOM   1239 C CB  . ASN A 1 154 ? 43.449 60.974 2.727   1.00 11.28  ? 835  ASN A CB  1 
ATOM   1240 C CG  . ASN A 1 154 ? 43.325 62.481 2.773   1.00 18.76  ? 835  ASN A CG  1 
ATOM   1241 O OD1 . ASN A 1 154 ? 42.861 63.103 1.817   1.00 17.72  ? 835  ASN A OD1 1 
ATOM   1242 N ND2 . ASN A 1 154 ? 43.745 63.078 3.878   1.00 19.85  ? 835  ASN A ND2 1 
ATOM   1243 N N   . ASN A 1 155 ? 43.462 58.713 0.116   1.00 10.37  ? 836  ASN A N   1 
ATOM   1244 C CA  . ASN A 1 155 ? 43.959 57.418 -0.359  1.00 10.07  ? 836  ASN A CA  1 
ATOM   1245 C C   . ASN A 1 155 ? 42.907 56.317 -0.228  1.00 14.06  ? 836  ASN A C   1 
ATOM   1246 O O   . ASN A 1 155 ? 43.246 55.136 -0.096  1.00 9.49   ? 836  ASN A O   1 
ATOM   1247 C CB  . ASN A 1 155 ? 45.254 57.027 0.366   1.00 10.20  ? 836  ASN A CB  1 
ATOM   1248 C CG  . ASN A 1 155 ? 46.269 58.143 0.363   1.00 10.66  ? 836  ASN A CG  1 
ATOM   1249 O OD1 . ASN A 1 155 ? 46.605 58.692 1.410   1.00 12.27  ? 836  ASN A OD1 1 
ATOM   1250 N ND2 . ASN A 1 155 ? 46.726 58.520 -0.818  1.00 10.77  ? 836  ASN A ND2 1 
ATOM   1251 N N   . THR A 1 156 ? 41.625 56.694 -0.283  1.00 9.70   ? 837  THR A N   1 
ATOM   1252 C CA  . THR A 1 156 ? 40.500 55.769 -0.126  1.00 9.45   ? 837  THR A CA  1 
ATOM   1253 C C   . THR A 1 156 ? 39.523 56.022 -1.272  1.00 12.20  ? 837  THR A C   1 
ATOM   1254 O O   . THR A 1 156 ? 38.767 57.004 -1.244  1.00 15.76  ? 837  THR A O   1 
ATOM   1255 C CB  . THR A 1 156 ? 39.808 55.954 1.223   1.00 10.89  ? 837  THR A CB  1 
ATOM   1256 O OG1 . THR A 1 156 ? 40.789 56.019 2.268   1.00 9.64   ? 837  THR A OG1 1 
ATOM   1257 C CG2 . THR A 1 156 ? 38.860 54.787 1.492   1.00 12.94  ? 837  THR A CG2 1 
ATOM   1258 N N   . TYR A 1 157 ? 39.531 55.139 -2.269  1.00 9.32   ? 838  TYR A N   1 
ATOM   1259 C CA  . TYR A 1 157 ? 38.812 55.342 -3.518  1.00 9.44   ? 838  TYR A CA  1 
ATOM   1260 C C   . TYR A 1 157 ? 37.832 54.211 -3.796  1.00 9.31   ? 838  TYR A C   1 
ATOM   1261 O O   . TYR A 1 157 ? 38.184 53.030 -3.699  1.00 9.35   ? 838  TYR A O   1 
ATOM   1262 C CB  . TYR A 1 157 ? 39.786 55.451 -4.688  1.00 9.56   ? 838  TYR A CB  1 
ATOM   1263 C CG  . TYR A 1 157 ? 40.493 56.779 -4.733  1.00 10.94  ? 838  TYR A CG  1 
ATOM   1264 C CD1 . TYR A 1 157 ? 41.666 56.990 -4.026  1.00 9.80   ? 838  TYR A CD1 1 
ATOM   1265 C CD2 . TYR A 1 157 ? 39.967 57.831 -5.475  1.00 10.35  ? 838  TYR A CD2 1 
ATOM   1266 C CE1 . TYR A 1 157 ? 42.303 58.233 -4.060  1.00 10.12  ? 838  TYR A CE1 1 
ATOM   1267 C CE2 . TYR A 1 157 ? 40.594 59.061 -5.526  1.00 14.84  ? 838  TYR A CE2 1 
ATOM   1268 C CZ  . TYR A 1 157 ? 41.758 59.260 -4.818  1.00 19.19  ? 838  TYR A CZ  1 
ATOM   1269 O OH  . TYR A 1 157 ? 42.370 60.499 -4.880  1.00 14.94  ? 838  TYR A OH  1 
ATOM   1270 N N   . GLY A 1 158 ? 36.608 54.579 -4.158  1.00 9.52   ? 839  GLY A N   1 
ATOM   1271 C CA  . GLY A 1 158 ? 35.748 53.678 -4.884  1.00 10.10  ? 839  GLY A CA  1 
ATOM   1272 C C   . GLY A 1 158 ? 36.068 53.720 -6.368  1.00 9.70   ? 839  GLY A C   1 
ATOM   1273 O O   . GLY A 1 158 ? 36.470 54.747 -6.907  1.00 11.14  ? 839  GLY A O   1 
ATOM   1274 N N   . VAL A 1 159 ? 35.891 52.578 -7.030  1.00 9.65   ? 840  VAL A N   1 
ATOM   1275 C CA  . VAL A 1 159 ? 36.077 52.475 -8.471  1.00 9.86   ? 840  VAL A CA  1 
ATOM   1276 C C   . VAL A 1 159 ? 34.848 51.804 -9.058  1.00 11.80  ? 840  VAL A C   1 
ATOM   1277 O O   . VAL A 1 159 ? 34.177 51.007 -8.395  1.00 12.14  ? 840  VAL A O   1 
ATOM   1278 C CB  . VAL A 1 159 ? 37.350 51.686 -8.849  1.00 9.66   ? 840  VAL A CB  1 
ATOM   1279 C CG1 . VAL A 1 159 ? 38.573 52.397 -8.323  1.00 9.52   ? 840  VAL A CG1 1 
ATOM   1280 C CG2 . VAL A 1 159 ? 37.268 50.289 -8.290  1.00 9.41   ? 840  VAL A CG2 1 
ATOM   1281 N N   . GLN A 1 160 ? 34.541 52.153 -10.303 1.00 15.88  ? 841  GLN A N   1 
ATOM   1282 C CA  . GLN A 1 160 ? 33.433 51.561 -11.036 1.00 17.74  ? 841  GLN A CA  1 
ATOM   1283 C C   . GLN A 1 160 ? 33.976 50.845 -12.263 1.00 19.27  ? 841  GLN A C   1 
ATOM   1284 O O   . GLN A 1 160 ? 34.836 51.381 -12.974 1.00 13.66  ? 841  GLN A O   1 
ATOM   1285 C CB  . GLN A 1 160 ? 32.399 52.620 -11.437 1.00 16.42  ? 841  GLN A CB  1 
ATOM   1286 C CG  . GLN A 1 160 ? 31.736 53.301 -10.247 1.00 21.69  ? 841  GLN A CG  1 
ATOM   1287 C CD  . GLN A 1 160 ? 30.633 54.269 -10.656 1.00 31.88  ? 841  GLN A CD  1 
ATOM   1288 O OE1 . GLN A 1 160 ? 30.233 54.319 -11.818 1.00 43.80  ? 841  GLN A OE1 1 
ATOM   1289 N NE2 . GLN A 1 160 ? 30.140 55.043 -9.696  1.00 33.42  ? 841  GLN A NE2 1 
ATOM   1290 N N   . TYR A 1 161 ? 33.476 49.632 -12.488 1.00 14.99  ? 842  TYR A N   1 
ATOM   1291 C CA  . TYR A 1 161 ? 33.863 48.767 -13.592 1.00 11.30  ? 842  TYR A CA  1 
ATOM   1292 C C   . TYR A 1 161 ? 32.651 47.912 -13.925 1.00 14.47  ? 842  TYR A C   1 
ATOM   1293 O O   . TYR A 1 161 ? 31.825 47.627 -13.055 1.00 18.77  ? 842  TYR A O   1 
ATOM   1294 C CB  . TYR A 1 161 ? 35.076 47.885 -13.230 1.00 10.99  ? 842  TYR A CB  1 
ATOM   1295 C CG  . TYR A 1 161 ? 34.929 47.220 -11.876 1.00 10.47  ? 842  TYR A CG  1 
ATOM   1296 C CD1 . TYR A 1 161 ? 34.213 46.033 -11.739 1.00 11.73  ? 842  TYR A CD1 1 
ATOM   1297 C CD2 . TYR A 1 161 ? 35.464 47.800 -10.729 1.00 10.07  ? 842  TYR A CD2 1 
ATOM   1298 C CE1 . TYR A 1 161 ? 34.051 45.425 -10.505 1.00 10.26  ? 842  TYR A CE1 1 
ATOM   1299 C CE2 . TYR A 1 161 ? 35.307 47.199 -9.482  1.00 11.45  ? 842  TYR A CE2 1 
ATOM   1300 C CZ  . TYR A 1 161 ? 34.597 46.013 -9.381  1.00 13.74  ? 842  TYR A CZ  1 
ATOM   1301 O OH  . TYR A 1 161 ? 34.427 45.395 -8.159  1.00 13.73  ? 842  TYR A OH  1 
ATOM   1302 N N   . GLN A 1 162 ? 32.549 47.490 -15.178 1.00 14.97  ? 843  GLN A N   1 
ATOM   1303 C CA  . GLN A 1 162 ? 31.375 46.738 -15.593 1.00 14.56  ? 843  GLN A CA  1 
ATOM   1304 C C   . GLN A 1 162 ? 31.498 45.265 -15.216 1.00 18.86  ? 843  GLN A C   1 
ATOM   1305 O O   . GLN A 1 162 ? 32.600 44.709 -15.141 1.00 16.97  ? 843  GLN A O   1 
ATOM   1306 C CB  . GLN A 1 162 ? 31.157 46.892 -17.097 1.00 27.60  ? 843  GLN A CB  1 
ATOM   1307 C CG  . GLN A 1 162 ? 30.873 48.332 -17.508 1.00 33.81  ? 843  GLN A CG  1 
ATOM   1308 C CD  . GLN A 1 162 ? 30.585 48.477 -18.985 1.00 31.68  ? 843  GLN A CD  1 
ATOM   1309 O OE1 . GLN A 1 162 ? 29.704 47.813 -19.523 1.00 43.04  ? 843  GLN A OE1 1 
ATOM   1310 N NE2 . GLN A 1 162 ? 31.329 49.349 -19.650 1.00 32.86  ? 843  GLN A NE2 1 
ATOM   1311 N N   . GLY A 1 163 ? 30.346 44.644 -14.945 1.00 17.19  ? 844  GLY A N   1 
ATOM   1312 C CA  . GLY A 1 163 ? 30.269 43.204 -14.767 1.00 18.03  ? 844  GLY A CA  1 
ATOM   1313 C C   . GLY A 1 163 ? 29.532 42.690 -13.541 1.00 21.41  ? 844  GLY A C   1 
ATOM   1314 O O   . GLY A 1 163 ? 28.986 41.581 -13.559 1.00 25.36  ? 844  GLY A O   1 
ATOM   1315 N N   . GLY A 1 164 ? 29.506 43.475 -12.469 1.00 19.56  ? 845  GLY A N   1 
ATOM   1316 C CA  . GLY A 1 164 ? 28.970 42.979 -11.214 1.00 18.64  ? 845  GLY A CA  1 
ATOM   1317 C C   . GLY A 1 164 ? 27.463 42.791 -11.267 1.00 18.78  ? 845  GLY A C   1 
ATOM   1318 O O   . GLY A 1 164 ? 26.737 43.561 -11.897 1.00 27.50  ? 845  GLY A O   1 
ATOM   1319 N N   . LYS A 1 165 ? 26.993 41.740 -10.598 1.00 23.80  ? 846  LYS A N   1 
ATOM   1320 C CA  . LYS A 1 165 ? 25.569 41.512 -10.394 1.00 22.23  ? 846  LYS A CA  1 
ATOM   1321 C C   . LYS A 1 165 ? 25.350 41.089 -8.949  1.00 20.99  ? 846  LYS A C   1 
ATOM   1322 O O   . LYS A 1 165 ? 26.300 40.843 -8.201  1.00 20.11  ? 846  LYS A O   1 
ATOM   1323 C CB  . LYS A 1 165 ? 25.007 40.457 -11.358 1.00 21.05  ? 846  LYS A CB  1 
ATOM   1324 C CG  . LYS A 1 165 ? 25.254 40.741 -12.836 1.00 26.07  ? 846  LYS A CG  1 
ATOM   1325 C CD  . LYS A 1 165 ? 24.354 41.837 -13.381 1.00 40.58  ? 846  LYS A CD  1 
ATOM   1326 C CE  . LYS A 1 165 ? 22.968 41.307 -13.695 1.00 48.03  ? 846  LYS A CE  1 
ATOM   1327 N NZ  . LYS A 1 165 ? 22.097 42.360 -14.284 1.00 58.62  ? 846  LYS A NZ  1 
ATOM   1328 N N   . ALA A 1 166 ? 24.076 41.004 -8.564  1.00 18.95  ? 847  ALA A N   1 
ATOM   1329 C CA  . ALA A 1 166 ? 23.719 40.702 -7.183  1.00 20.47  ? 847  ALA A CA  1 
ATOM   1330 C C   . ALA A 1 166 ? 24.337 39.378 -6.747  1.00 24.07  ? 847  ALA A C   1 
ATOM   1331 O O   . ALA A 1 166 ? 24.396 38.417 -7.520  1.00 21.20  ? 847  ALA A O   1 
ATOM   1332 C CB  . ALA A 1 166 ? 22.196 40.651 -7.027  1.00 21.13  ? 847  ALA A CB  1 
ATOM   1333 N N   . GLY A 1 167 ? 24.815 39.338 -5.502  1.00 16.84  ? 848  GLY A N   1 
ATOM   1334 C CA  . GLY A 1 167 ? 25.501 38.187 -4.960  1.00 12.16  ? 848  GLY A CA  1 
ATOM   1335 C C   . GLY A 1 167 ? 27.014 38.280 -5.009  1.00 11.54  ? 848  GLY A C   1 
ATOM   1336 O O   . GLY A 1 167 ? 27.690 37.569 -4.256  1.00 15.77  ? 848  GLY A O   1 
ATOM   1337 N N   . MET A 1 168 ? 27.557 39.141 -5.869  1.00 11.82  ? 849  MET A N   1 
ATOM   1338 C CA  . MET A 1 168 ? 29.003 39.270 -6.016  1.00 10.93  ? 849  MET A CA  1 
ATOM   1339 C C   . MET A 1 168 ? 29.632 40.144 -4.945  1.00 10.42  ? 849  MET A C   1 
ATOM   1340 O O   . MET A 1 168 ? 30.853 40.093 -4.759  1.00 11.89  ? 849  MET A O   1 
ATOM   1341 C CB  . MET A 1 168 ? 29.342 39.842 -7.395  1.00 11.07  ? 849  MET A CB  1 
ATOM   1342 C CG  . MET A 1 168 ? 30.834 39.809 -7.734  1.00 17.93  ? 849  MET A CG  1 
ATOM   1343 S SD  . MET A 1 168 ? 31.157 39.999 -9.496  1.00 28.81  ? 849  MET A SD  1 
ATOM   1344 C CE  . MET A 1 168 ? 32.789 39.269 -9.609  1.00 20.87  ? 849  MET A CE  1 
ATOM   1345 N N   . SER A 1 169 ? 28.842 40.955 -4.250  1.00 10.77  ? 850  SER A N   1 
ATOM   1346 C CA  . SER A 1 169 ? 29.410 41.865 -3.264  1.00 11.68  ? 850  SER A CA  1 
ATOM   1347 C C   . SER A 1 169 ? 30.162 41.089 -2.191  1.00 14.94  ? 850  SER A C   1 
ATOM   1348 O O   . SER A 1 169 ? 29.677 40.082 -1.667  1.00 11.81  ? 850  SER A O   1 
ATOM   1349 C CB  . SER A 1 169 ? 28.310 42.721 -2.648  1.00 20.04  ? 850  SER A CB  1 
ATOM   1350 O OG  . SER A 1 169 ? 27.715 43.514 -3.659  1.00 21.47  ? 850  SER A OG  1 
ATOM   1351 N N   . GLY A 1 170 ? 31.363 41.560 -1.877  1.00 11.46  ? 851  GLY A N   1 
ATOM   1352 C CA  . GLY A 1 170 ? 32.245 40.881 -0.971  1.00 12.77  ? 851  GLY A CA  1 
ATOM   1353 C C   . GLY A 1 170 ? 33.341 40.098 -1.657  1.00 9.05   ? 851  GLY A C   1 
ATOM   1354 O O   . GLY A 1 170 ? 34.333 39.758 -1.010  1.00 11.59  ? 851  GLY A O   1 
ATOM   1355 N N   . GLY A 1 171 ? 33.194 39.830 -2.955  1.00 9.24   ? 852  GLY A N   1 
ATOM   1356 C CA  . GLY A 1 171 ? 34.258 39.200 -3.699  1.00 9.22   ? 852  GLY A CA  1 
ATOM   1357 C C   . GLY A 1 171 ? 35.477 40.094 -3.830  1.00 10.42  ? 852  GLY A C   1 
ATOM   1358 O O   . GLY A 1 171 ? 35.415 41.320 -3.699  1.00 13.94  ? 852  GLY A O   1 
ATOM   1359 N N   . GLY A 1 172 ? 36.609 39.467 -4.108  1.00 11.21  ? 853  GLY A N   1 
ATOM   1360 C CA  . GLY A 1 172 ? 37.876 40.164 -4.072  1.00 10.46  ? 853  GLY A CA  1 
ATOM   1361 C C   . GLY A 1 172 ? 38.221 40.879 -5.365  1.00 10.35  ? 853  GLY A C   1 
ATOM   1362 O O   . GLY A 1 172 ? 37.900 40.432 -6.461  1.00 11.05  ? 853  GLY A O   1 
ATOM   1363 N N   . ILE A 1 173 ? 38.903 42.016 -5.218  1.00 9.68   ? 854  ILE A N   1 
ATOM   1364 C CA  . ILE A 1 173 ? 39.544 42.689 -6.334  1.00 9.76   ? 854  ILE A CA  1 
ATOM   1365 C C   . ILE A 1 173 ? 41.040 42.413 -6.241  1.00 9.79   ? 854  ILE A C   1 
ATOM   1366 O O   . ILE A 1 173 ? 41.638 42.581 -5.173  1.00 9.39   ? 854  ILE A O   1 
ATOM   1367 C CB  . ILE A 1 173 ? 39.264 44.200 -6.318  1.00 9.35   ? 854  ILE A CB  1 
ATOM   1368 C CG1 . ILE A 1 173 ? 37.757 44.480 -6.297  1.00 9.55   ? 854  ILE A CG1 1 
ATOM   1369 C CG2 . ILE A 1 173 ? 39.871 44.840 -7.545  1.00 9.74   ? 854  ILE A CG2 1 
ATOM   1370 C CD1 . ILE A 1 173 ? 37.420 45.967 -6.254  1.00 9.42   ? 854  ILE A CD1 1 
ATOM   1371 N N   . PHE A 1 174 ? 41.640 41.995 -7.353  1.00 10.47  ? 855  PHE A N   1 
ATOM   1372 C CA  . PHE A 1 174 ? 43.019 41.512 -7.379  1.00 10.89  ? 855  PHE A CA  1 
ATOM   1373 C C   . PHE A 1 174 ? 43.843 42.330 -8.356  1.00 11.26  ? 855  PHE A C   1 
ATOM   1374 O O   . PHE A 1 174 ? 43.351 42.718 -9.421  1.00 16.99  ? 855  PHE A O   1 
ATOM   1375 C CB  . PHE A 1 174 ? 43.095 40.042 -7.793  1.00 11.84  ? 855  PHE A CB  1 
ATOM   1376 C CG  . PHE A 1 174 ? 42.456 39.099 -6.824  1.00 12.78  ? 855  PHE A CG  1 
ATOM   1377 C CD1 . PHE A 1 174 ? 41.080 38.942 -6.795  1.00 11.79  ? 855  PHE A CD1 1 
ATOM   1378 C CD2 . PHE A 1 174 ? 43.230 38.326 -5.975  1.00 13.14  ? 855  PHE A CD2 1 
ATOM   1379 C CE1 . PHE A 1 174 ? 40.492 38.073 -5.911  1.00 12.04  ? 855  PHE A CE1 1 
ATOM   1380 C CE2 . PHE A 1 174 ? 42.647 37.452 -5.090  1.00 12.48  ? 855  PHE A CE2 1 
ATOM   1381 C CZ  . PHE A 1 174 ? 41.270 37.325 -5.058  1.00 12.38  ? 855  PHE A CZ  1 
ATOM   1382 N N   . ASN A 1 175 ? 45.105 42.568 -8.005  1.00 14.32  ? 856  ASN A N   1 
ATOM   1383 C CA  . ASN A 1 175 ? 46.031 43.206 -8.928  1.00 18.30  ? 856  ASN A CA  1 
ATOM   1384 C C   . ASN A 1 175 ? 46.619 42.143 -9.856  1.00 19.57  ? 856  ASN A C   1 
ATOM   1385 O O   . ASN A 1 175 ? 46.242 40.968 -9.821  1.00 16.54  ? 856  ASN A O   1 
ATOM   1386 C CB  . ASN A 1 175 ? 47.106 43.986 -8.169  1.00 12.53  ? 856  ASN A CB  1 
ATOM   1387 C CG  . ASN A 1 175 ? 48.027 43.095 -7.337  1.00 12.48  ? 856  ASN A CG  1 
ATOM   1388 O OD1 . ASN A 1 175 ? 48.041 41.881 -7.477  1.00 15.64  ? 856  ASN A OD1 1 
ATOM   1389 N ND2 . ASN A 1 175 ? 48.813 43.718 -6.467  1.00 13.58  ? 856  ASN A ND2 1 
ATOM   1390 N N   . SER A 1 176 ? 47.579 42.547 -10.686 1.00 19.30  ? 857  SER A N   1 
ATOM   1391 C CA  . SER A 1 176 ? 48.128 41.633 -11.677 1.00 19.39  ? 857  SER A CA  1 
ATOM   1392 C C   . SER A 1 176 ? 48.937 40.504 -11.049 1.00 24.72  ? 857  SER A C   1 
ATOM   1393 O O   . SER A 1 176 ? 49.099 39.455 -11.680 1.00 24.48  ? 857  SER A O   1 
ATOM   1394 C CB  . SER A 1 176 ? 48.990 42.406 -12.672 1.00 26.00  ? 857  SER A CB  1 
ATOM   1395 O OG  . SER A 1 176 ? 50.084 43.009 -12.007 1.00 24.20  ? 857  SER A OG  1 
ATOM   1396 N N   . LYS A 1 177 ? 49.446 40.688 -9.831  1.00 18.74  ? 858  LYS A N   1 
ATOM   1397 C CA  . LYS A 1 177 ? 50.133 39.615 -9.121  1.00 21.27  ? 858  LYS A CA  1 
ATOM   1398 C C   . LYS A 1 177 ? 49.180 38.662 -8.405  1.00 16.64  ? 858  LYS A C   1 
ATOM   1399 O O   . LYS A 1 177 ? 49.643 37.697 -7.791  1.00 18.69  ? 858  LYS A O   1 
ATOM   1400 C CB  . LYS A 1 177 ? 51.120 40.194 -8.101  1.00 16.40  ? 858  LYS A CB  1 
ATOM   1401 C CG  . LYS A 1 177 ? 52.281 40.959 -8.708  1.00 24.54  ? 858  LYS A CG  1 
ATOM   1402 C CD  . LYS A 1 177 ? 53.280 41.379 -7.639  1.00 26.52  ? 858  LYS A CD  1 
ATOM   1403 C CE  . LYS A 1 177 ? 52.888 42.703 -6.996  1.00 39.55  ? 858  LYS A CE  1 
ATOM   1404 N NZ  . LYS A 1 177 ? 52.950 43.839 -7.962  1.00 33.69  ? 858  LYS A NZ  1 
ATOM   1405 N N   . GLY A 1 178 ? 47.871 38.892 -8.460  1.00 14.90  ? 859  GLY A N   1 
ATOM   1406 C CA  . GLY A 1 178 ? 46.972 38.022 -7.727  1.00 14.61  ? 859  GLY A CA  1 
ATOM   1407 C C   . GLY A 1 178 ? 46.895 38.311 -6.245  1.00 13.77  ? 859  GLY A C   1 
ATOM   1408 O O   . GLY A 1 178 ? 46.429 37.462 -5.480  1.00 13.93  ? 859  GLY A O   1 
ATOM   1409 N N   . GLU A 1 179 ? 47.334 39.490 -5.817  1.00 13.09  ? 860  GLU A N   1 
ATOM   1410 C CA  . GLU A 1 179 ? 47.153 39.951 -4.449  1.00 12.35  ? 860  GLU A CA  1 
ATOM   1411 C C   . GLU A 1 179 ? 45.836 40.710 -4.322  1.00 11.21  ? 860  GLU A C   1 
ATOM   1412 O O   . GLU A 1 179 ? 45.367 41.331 -5.275  1.00 10.92  ? 860  GLU A O   1 
ATOM   1413 C CB  . GLU A 1 179 ? 48.311 40.858 -4.028  1.00 12.49  ? 860  GLU A CB  1 
ATOM   1414 C CG  . GLU A 1 179 ? 49.688 40.210 -4.172  1.00 19.36  ? 860  GLU A CG  1 
ATOM   1415 C CD  . GLU A 1 179 ? 50.835 41.207 -4.104  1.00 30.68  ? 860  GLU A CD  1 
ATOM   1416 O OE1 . GLU A 1 179 ? 50.677 42.354 -4.583  1.00 15.82  ? 860  GLU A OE1 1 
ATOM   1417 O OE2 . GLU A 1 179 ? 51.908 40.832 -3.581  1.00 19.95  ? 860  GLU A OE2 1 
ATOM   1418 N N   . VAL A 1 180 ? 45.252 40.661 -3.127  1.00 10.79  ? 861  VAL A N   1 
ATOM   1419 C CA  . VAL A 1 180 ? 43.965 41.296 -2.866  1.00 9.96   ? 861  VAL A CA  1 
ATOM   1420 C C   . VAL A 1 180 ? 44.206 42.775 -2.601  1.00 9.37   ? 861  VAL A C   1 
ATOM   1421 O O   . VAL A 1 180 ? 44.948 43.134 -1.683  1.00 9.46   ? 861  VAL A O   1 
ATOM   1422 C CB  . VAL A 1 180 ? 43.248 40.644 -1.675  1.00 10.04  ? 861  VAL A CB  1 
ATOM   1423 C CG1 . VAL A 1 180 ? 42.001 41.433 -1.313  1.00 9.38   ? 861  VAL A CG1 1 
ATOM   1424 C CG2 . VAL A 1 180 ? 42.892 39.187 -1.985  1.00 10.85  ? 861  VAL A CG2 1 
ATOM   1425 N N   . ILE A 1 181 ? 43.568 43.631 -3.394  1.00 9.05   ? 862  ILE A N   1 
ATOM   1426 C CA  . ILE A 1 181 ? 43.701 45.077 -3.235  1.00 8.64   ? 862  ILE A CA  1 
ATOM   1427 C C   . ILE A 1 181 ? 42.380 45.744 -2.889  1.00 11.73  ? 862  ILE A C   1 
ATOM   1428 O O   . ILE A 1 181 ? 42.369 46.945 -2.582  1.00 8.05   ? 862  ILE A O   1 
ATOM   1429 C CB  . ILE A 1 181 ? 44.307 45.731 -4.497  1.00 9.21   ? 862  ILE A CB  1 
ATOM   1430 C CG1 . ILE A 1 181 ? 43.414 45.501 -5.719  1.00 15.77  ? 862  ILE A CG1 1 
ATOM   1431 C CG2 . ILE A 1 181 ? 45.705 45.187 -4.765  1.00 11.13  ? 862  ILE A CG2 1 
ATOM   1432 C CD1 . ILE A 1 181 ? 43.847 46.282 -6.947  1.00 14.12  ? 862  ILE A CD1 1 
ATOM   1433 N N   . GLY A 1 182 ? 41.280 45.010 -2.911  1.00 8.61   ? 863  GLY A N   1 
ATOM   1434 C CA  . GLY A 1 182 ? 39.980 45.629 -2.739  1.00 9.16   ? 863  GLY A CA  1 
ATOM   1435 C C   . GLY A 1 182 ? 38.898 44.578 -2.733  1.00 8.48   ? 863  GLY A C   1 
ATOM   1436 O O   . GLY A 1 182 ? 39.173 43.375 -2.722  1.00 9.94   ? 863  GLY A O   1 
ATOM   1437 N N   . LEU A 1 183 ? 37.650 45.042 -2.735  1.00 11.15  ? 864  LEU A N   1 
ATOM   1438 C CA  . LEU A 1 183 ? 36.532 44.117 -2.742  1.00 11.14  ? 864  LEU A CA  1 
ATOM   1439 C C   . LEU A 1 183 ? 35.356 44.733 -3.482  1.00 9.43   ? 864  LEU A C   1 
ATOM   1440 O O   . LEU A 1 183 ? 35.152 45.951 -3.460  1.00 10.30  ? 864  LEU A O   1 
ATOM   1441 C CB  . LEU A 1 183 ? 36.113 43.713 -1.324  1.00 14.77  ? 864  LEU A CB  1 
ATOM   1442 C CG  . LEU A 1 183 ? 35.407 44.727 -0.428  1.00 12.95  ? 864  LEU A CG  1 
ATOM   1443 C CD1 . LEU A 1 183 ? 35.005 44.017 0.842   1.00 15.63  ? 864  LEU A CD1 1 
ATOM   1444 C CD2 . LEU A 1 183 ? 36.295 45.925 -0.105  1.00 12.92  ? 864  LEU A CD2 1 
ATOM   1445 N N   . HIS A 1 184 ? 34.605 43.869 -4.151  1.00 10.13  ? 865  HIS A N   1 
ATOM   1446 C CA  . HIS A 1 184 ? 33.403 44.270 -4.864  1.00 12.56  ? 865  HIS A CA  1 
ATOM   1447 C C   . HIS A 1 184 ? 32.296 44.634 -3.883  1.00 11.85  ? 865  HIS A C   1 
ATOM   1448 O O   . HIS A 1 184 ? 32.081 43.942 -2.885  1.00 11.38  ? 865  HIS A O   1 
ATOM   1449 C CB  . HIS A 1 184 ? 32.945 43.128 -5.769  1.00 11.82  ? 865  HIS A CB  1 
ATOM   1450 C CG  . HIS A 1 184 ? 31.884 43.518 -6.742  1.00 15.45  ? 865  HIS A CG  1 
ATOM   1451 N ND1 . HIS A 1 184 ? 32.168 44.122 -7.948  1.00 13.17  ? 865  HIS A ND1 1 
ATOM   1452 C CD2 . HIS A 1 184 ? 30.540 43.374 -6.699  1.00 13.98  ? 865  HIS A CD2 1 
ATOM   1453 C CE1 . HIS A 1 184 ? 31.043 44.348 -8.598  1.00 14.40  ? 865  HIS A CE1 1 
ATOM   1454 N NE2 . HIS A 1 184 ? 30.042 43.895 -7.866  1.00 15.83  ? 865  HIS A NE2 1 
ATOM   1455 N N   . GLN A 1 185 ? 31.582 45.725 -4.169  1.00 15.60  ? 866  GLN A N   1 
ATOM   1456 C CA  . GLN A 1 185 ? 30.586 46.195 -3.211  1.00 15.05  ? 866  GLN A CA  1 
ATOM   1457 C C   . GLN A 1 185 ? 29.200 46.407 -3.802  1.00 23.30  ? 866  GLN A C   1 
ATOM   1458 O O   . GLN A 1 185 ? 28.200 46.309 -3.084  1.00 27.49  ? 866  GLN A O   1 
ATOM   1459 C CB  . GLN A 1 185 ? 31.031 47.503 -2.570  1.00 13.96  ? 866  GLN A CB  1 
ATOM   1460 C CG  . GLN A 1 185 ? 32.161 47.373 -1.574  1.00 12.92  ? 866  GLN A CG  1 
ATOM   1461 C CD  . GLN A 1 185 ? 32.634 48.733 -1.116  1.00 11.35  ? 866  GLN A CD  1 
ATOM   1462 O OE1 . GLN A 1 185 ? 32.719 49.665 -1.917  1.00 10.65  ? 866  GLN A OE1 1 
ATOM   1463 N NE2 . GLN A 1 185 ? 32.924 48.863 0.172   1.00 10.36  ? 866  GLN A NE2 1 
ATOM   1464 N N   . ASN A 1 186 ? 29.116 46.739 -5.084  1.00 21.17  ? 867  ASN A N   1 
ATOM   1465 C CA  . ASN A 1 186 ? 27.815 46.964 -5.691  1.00 27.71  ? 867  ASN A CA  1 
ATOM   1466 C C   . ASN A 1 186 ? 27.762 46.292 -7.050  1.00 33.35  ? 867  ASN A C   1 
ATOM   1467 O O   . ASN A 1 186 ? 28.681 46.445 -7.859  1.00 35.25  ? 867  ASN A O   1 
ATOM   1468 C CB  . ASN A 1 186 ? 27.514 48.459 -5.818  1.00 30.98  ? 867  ASN A CB  1 
ATOM   1469 C CG  . ASN A 1 186 ? 26.059 48.726 -6.142  1.00 45.12  ? 867  ASN A CG  1 
ATOM   1470 O OD1 . ASN A 1 186 ? 25.159 48.200 -5.493  1.00 56.33  ? 867  ASN A OD1 1 
ATOM   1471 N ND2 . ASN A 1 186 ? 25.822 49.566 -7.144  1.00 53.73  ? 867  ASN A ND2 1 
ATOM   1472 N N   . GLY A 1 187 ? 26.700 45.529 -7.285  1.00 40.12  ? 868  GLY A N   1 
ATOM   1473 C CA  . GLY A 1 187 ? 26.472 44.932 -8.584  1.00 35.91  ? 868  GLY A CA  1 
ATOM   1474 C C   . GLY A 1 187 ? 25.048 45.187 -9.017  1.00 44.09  ? 868  GLY A C   1 
ATOM   1475 O O   . GLY A 1 187 ? 24.583 44.656 -10.029 1.00 47.71  ? 868  GLY A O   1 
ATOM   1476 N N   . ALA A 1 188 ? 24.350 46.011 -8.240  1.00 53.73  ? 869  ALA A N   1 
ATOM   1477 C CA  . ALA A 1 188 ? 22.963 46.333 -8.523  1.00 59.99  ? 869  ALA A CA  1 
ATOM   1478 C C   . ALA A 1 188 ? 22.877 47.253 -9.739  1.00 61.38  ? 869  ALA A C   1 
ATOM   1479 O O   . ALA A 1 188 ? 23.881 47.622 -10.356 1.00 55.51  ? 869  ALA A O   1 
ATOM   1480 C CB  . ALA A 1 188 ? 22.310 46.967 -7.296  1.00 57.68  ? 869  ALA A CB  1 
ATOM   1481 N N   . GLU A 1 189 ? 21.646 47.628 -10.082 1.00 72.83  ? 870  GLU A N   1 
ATOM   1482 C CA  . GLU A 1 189 ? 21.404 48.486 -11.233 1.00 71.25  ? 870  GLU A CA  1 
ATOM   1483 C C   . GLU A 1 189 ? 22.056 49.856 -11.095 1.00 76.13  ? 870  GLU A C   1 
ATOM   1484 O O   . GLU A 1 189 ? 22.179 50.567 -12.098 1.00 72.95  ? 870  GLU A O   1 
ATOM   1485 C CB  . GLU A 1 189 ? 19.894 48.636 -11.446 1.00 84.41  ? 870  GLU A CB  1 
ATOM   1486 C CG  . GLU A 1 189 ? 19.129 47.321 -11.297 1.00 76.93  ? 870  GLU A CG  1 
ATOM   1487 C CD  . GLU A 1 189 ? 17.694 47.406 -11.784 1.00 77.57  ? 870  GLU A CD  1 
ATOM   1488 O OE1 . GLU A 1 189 ? 16.982 48.361 -11.404 1.00 79.94  ? 870  GLU A OE1 1 
ATOM   1489 O OE2 . GLU A 1 189 ? 17.279 46.515 -12.556 1.00 81.86  ? 870  GLU A OE2 1 
ATOM   1490 N N   . ASN A 1 190 ? 22.488 50.236 -9.895  1.00 84.33  ? 871  ASN A N   1 
ATOM   1491 C CA  . ASN A 1 190 ? 23.115 51.539 -9.662  1.00 84.54  ? 871  ASN A CA  1 
ATOM   1492 C C   . ASN A 1 190 ? 24.643 51.421 -9.663  1.00 80.93  ? 871  ASN A C   1 
ATOM   1493 O O   . ASN A 1 190 ? 25.322 51.713 -8.677  1.00 78.96  ? 871  ASN A O   1 
ATOM   1494 C CB  . ASN A 1 190 ? 22.593 52.158 -8.362  1.00 69.51  ? 871  ASN A CB  1 
ATOM   1495 C CG  . ASN A 1 190 ? 22.919 51.326 -7.127  1.00 79.02  ? 871  ASN A CG  1 
ATOM   1496 O OD1 . ASN A 1 190 ? 22.980 50.100 -7.186  1.00 83.35  ? 871  ASN A OD1 1 
ATOM   1497 N ND2 . ASN A 1 190 ? 23.133 52.002 -5.998  1.00 64.84  ? 871  ASN A ND2 1 
ATOM   1498 N N   . ARG A 1 191 ? 25.172 50.978 -10.810 1.00 74.43  ? 872  ARG A N   1 
ATOM   1499 C CA  . ARG A 1 191 ? 26.604 50.984 -11.118 1.00 58.93  ? 872  ARG A CA  1 
ATOM   1500 C C   . ARG A 1 191 ? 27.400 49.912 -10.376 1.00 55.63  ? 872  ARG A C   1 
ATOM   1501 O O   . ARG A 1 191 ? 27.502 49.926 -9.144  1.00 44.64  ? 872  ARG A O   1 
ATOM   1502 C CB  . ARG A 1 191 ? 27.211 52.366 -10.844 1.00 60.11  ? 872  ARG A CB  1 
ATOM   1503 C CG  . ARG A 1 191 ? 26.792 53.444 -11.834 1.00 73.97  ? 872  ARG A CG  1 
ATOM   1504 C CD  . ARG A 1 191 ? 27.206 53.064 -13.248 1.00 86.22  ? 872  ARG A CD  1 
ATOM   1505 N NE  . ARG A 1 191 ? 26.871 54.097 -14.221 1.00 106.05 ? 872  ARG A NE  1 
ATOM   1506 C CZ  . ARG A 1 191 ? 27.005 53.962 -15.534 1.00 107.75 ? 872  ARG A CZ  1 
ATOM   1507 N NH1 . ARG A 1 191 ? 27.462 52.841 -16.072 1.00 94.66  ? 872  ARG A NH1 1 
ATOM   1508 N NH2 . ARG A 1 191 ? 26.667 54.976 -16.329 1.00 93.42  ? 872  ARG A NH2 1 
ATOM   1509 N N   . SER A 1 192 ? 27.984 48.987 -11.134 1.00 34.56  ? 873  SER A N   1 
ATOM   1510 C CA  . SER A 1 192 ? 28.881 47.988 -10.575 1.00 28.65  ? 873  SER A CA  1 
ATOM   1511 C C   . SER A 1 192 ? 30.212 48.628 -10.183 1.00 23.36  ? 873  SER A C   1 
ATOM   1512 O O   . SER A 1 192 ? 30.734 49.486 -10.898 1.00 16.61  ? 873  SER A O   1 
ATOM   1513 C CB  . SER A 1 192 ? 29.093 46.873 -11.606 1.00 19.61  ? 873  SER A CB  1 
ATOM   1514 O OG  . SER A 1 192 ? 30.216 46.057 -11.322 1.00 22.17  ? 873  SER A OG  1 
ATOM   1515 N N   . GLY A 1 193 ? 30.756 48.218 -9.042  1.00 21.99  ? 874  GLY A N   1 
ATOM   1516 C CA  . GLY A 1 193 ? 32.050 48.736 -8.623  1.00 17.01  ? 874  GLY A CA  1 
ATOM   1517 C C   . GLY A 1 193 ? 32.477 48.181 -7.279  1.00 15.68  ? 874  GLY A C   1 
ATOM   1518 O O   . GLY A 1 193 ? 31.879 47.240 -6.752  1.00 12.49  ? 874  GLY A O   1 
ATOM   1519 N N   . GLY A 1 194 ? 33.532 48.774 -6.726  1.00 11.50  ? 875  GLY A N   1 
ATOM   1520 C CA  . GLY A 1 194 ? 34.083 48.280 -5.477  1.00 10.53  ? 875  GLY A CA  1 
ATOM   1521 C C   . GLY A 1 194 ? 35.006 49.291 -4.833  1.00 11.18  ? 875  GLY A C   1 
ATOM   1522 O O   . GLY A 1 194 ? 35.143 50.423 -5.296  1.00 13.30  ? 875  GLY A O   1 
ATOM   1523 N N   . LEU A 1 195 ? 35.629 48.862 -3.741  1.00 9.27   ? 876  LEU A N   1 
ATOM   1524 C CA  . LEU A 1 195 ? 36.474 49.705 -2.904  1.00 10.07  ? 876  LEU A CA  1 
ATOM   1525 C C   . LEU A 1 195 ? 37.919 49.246 -3.002  1.00 10.98  ? 876  LEU A C   1 
ATOM   1526 O O   . LEU A 1 195 ? 38.208 48.059 -2.796  1.00 9.56   ? 876  LEU A O   1 
ATOM   1527 C CB  . LEU A 1 195 ? 36.013 49.631 -1.444  1.00 8.85   ? 876  LEU A CB  1 
ATOM   1528 C CG  . LEU A 1 195 ? 36.945 50.195 -0.376  1.00 8.61   ? 876  LEU A CG  1 
ATOM   1529 C CD1 . LEU A 1 195 ? 37.005 51.736 -0.466  1.00 9.73   ? 876  LEU A CD1 1 
ATOM   1530 C CD2 . LEU A 1 195 ? 36.481 49.758 1.005   1.00 10.08  ? 876  LEU A CD2 1 
ATOM   1531 N N   . ILE A 1 196 ? 38.825 50.173 -3.304  1.00 8.53   ? 877  ILE A N   1 
ATOM   1532 C CA  . ILE A 1 196 ? 40.254 49.901 -3.210  1.00 8.27   ? 877  ILE A CA  1 
ATOM   1533 C C   . ILE A 1 196 ? 40.687 50.264 -1.799  1.00 8.14   ? 877  ILE A C   1 
ATOM   1534 O O   . ILE A 1 196 ? 40.522 51.410 -1.368  1.00 8.73   ? 877  ILE A O   1 
ATOM   1535 C CB  . ILE A 1 196 ? 41.046 50.677 -4.268  1.00 8.72   ? 877  ILE A CB  1 
ATOM   1536 C CG1 . ILE A 1 196 ? 40.557 50.301 -5.675  1.00 9.11   ? 877  ILE A CG1 1 
ATOM   1537 C CG2 . ILE A 1 196 ? 42.552 50.435 -4.083  1.00 8.75   ? 877  ILE A CG2 1 
ATOM   1538 C CD1 . ILE A 1 196 ? 40.589 48.779 -5.984  1.00 10.17  ? 877  ILE A CD1 1 
ATOM   1539 N N   . LEU A 1 197 ? 41.192 49.274 -1.063  1.00 7.93   ? 878  LEU A N   1 
ATOM   1540 C CA  . LEU A 1 197 ? 41.503 49.455 0.350   1.00 8.10   ? 878  LEU A CA  1 
ATOM   1541 C C   . LEU A 1 197 ? 42.619 50.489 0.543   1.00 8.65   ? 878  LEU A C   1 
ATOM   1542 O O   . LEU A 1 197 ? 43.627 50.483 -0.165  1.00 11.05  ? 878  LEU A O   1 
ATOM   1543 C CB  . LEU A 1 197 ? 41.896 48.105 0.966   1.00 9.10   ? 878  LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 197 ? 40.765 47.068 0.958   1.00 7.95   ? 878  LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 197 ? 41.336 45.645 1.132   1.00 8.17   ? 878  LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 197 ? 39.730 47.364 2.035   1.00 10.47  ? 878  LEU A CD2 1 
ATOM   1547 N N   . SER A 1 198 ? 42.424 51.377 1.517   1.00 8.73   ? 879  SER A N   1 
ATOM   1548 C CA  . SER A 1 198 ? 43.379 52.419 1.876   1.00 10.43  ? 879  SER A CA  1 
ATOM   1549 C C   . SER A 1 198 ? 44.513 51.851 2.728   1.00 9.70   ? 879  SER A C   1 
ATOM   1550 O O   . SER A 1 198 ? 44.368 50.786 3.327   1.00 9.76   ? 879  SER A O   1 
ATOM   1551 C CB  . SER A 1 198 ? 42.673 53.507 2.669   1.00 9.81   ? 879  SER A CB  1 
ATOM   1552 O OG  . SER A 1 198 ? 42.445 53.079 4.003   1.00 10.82  ? 879  SER A OG  1 
ATOM   1553 N N   . PRO A 1 199 ? 45.642 52.570 2.830   1.00 10.42  ? 880  PRO A N   1 
ATOM   1554 C CA  . PRO A 1 199 ? 46.670 52.185 3.813   1.00 11.13  ? 880  PRO A CA  1 
ATOM   1555 C C   . PRO A 1 199 ? 46.115 51.922 5.209   1.00 11.82  ? 880  PRO A C   1 
ATOM   1556 O O   . PRO A 1 199 ? 46.536 50.958 5.866   1.00 11.67  ? 880  PRO A O   1 
ATOM   1557 C CB  . PRO A 1 199 ? 47.619 53.393 3.807   1.00 13.83  ? 880  PRO A CB  1 
ATOM   1558 C CG  . PRO A 1 199 ? 47.502 53.958 2.430   1.00 11.88  ? 880  PRO A CG  1 
ATOM   1559 C CD  . PRO A 1 199 ? 46.027 53.776 2.070   1.00 13.13  ? 880  PRO A CD  1 
ATOM   1560 N N   . THR A 1 200 ? 45.174 52.753 5.680   1.00 13.15  ? 881  THR A N   1 
ATOM   1561 C CA  A THR A 1 200 ? 44.581 52.524 6.996   0.70 11.87  ? 881  THR A CA  1 
ATOM   1562 C CA  B THR A 1 200 ? 44.581 52.526 6.995   0.30 11.87  ? 881  THR A CA  1 
ATOM   1563 C C   . THR A 1 200 ? 43.783 51.228 7.023   1.00 11.25  ? 881  THR A C   1 
ATOM   1564 O O   . THR A 1 200 ? 43.878 50.454 7.980   1.00 11.77  ? 881  THR A O   1 
ATOM   1565 C CB  A THR A 1 200 ? 43.678 53.691 7.390   0.70 18.34  ? 881  THR A CB  1 
ATOM   1566 C CB  B THR A 1 200 ? 43.690 53.708 7.383   0.30 18.22  ? 881  THR A CB  1 
ATOM   1567 O OG1 A THR A 1 200 ? 42.806 54.011 6.295   0.70 24.51  ? 881  THR A OG1 1 
ATOM   1568 O OG1 B THR A 1 200 ? 44.478 54.903 7.470   0.30 15.00  ? 881  THR A OG1 1 
ATOM   1569 C CG2 A THR A 1 200 ? 44.503 54.916 7.774   0.70 14.84  ? 881  THR A CG2 1 
ATOM   1570 C CG2 B THR A 1 200 ? 43.007 53.459 8.727   0.30 12.92  ? 881  THR A CG2 1 
ATOM   1571 N N   . GLN A 1 201 ? 42.980 50.983 5.991   1.00 11.15  ? 882  GLN A N   1 
ATOM   1572 C CA  . GLN A 1 201 ? 42.152 49.782 5.972   1.00 10.83  ? 882  GLN A CA  1 
ATOM   1573 C C   . GLN A 1 201 ? 43.006 48.526 5.840   1.00 11.77  ? 882  GLN A C   1 
ATOM   1574 O O   . GLN A 1 201 ? 42.704 47.499 6.459   1.00 10.29  ? 882  GLN A O   1 
ATOM   1575 C CB  . GLN A 1 201 ? 41.140 49.884 4.841   1.00 10.30  ? 882  GLN A CB  1 
ATOM   1576 C CG  . GLN A 1 201 ? 40.069 50.932 5.113   1.00 9.58   ? 882  GLN A CG  1 
ATOM   1577 C CD  . GLN A 1 201 ? 39.204 51.195 3.902   1.00 11.64  ? 882  GLN A CD  1 
ATOM   1578 O OE1 . GLN A 1 201 ? 39.699 51.252 2.769   1.00 8.82   ? 882  GLN A OE1 1 
ATOM   1579 N NE2 . GLN A 1 201 ? 37.897 51.354 4.128   1.00 9.84   ? 882  GLN A NE2 1 
ATOM   1580 N N   . LEU A 1 202 ? 44.093 48.599 5.066   1.00 12.81  ? 883  LEU A N   1 
ATOM   1581 C CA  . LEU A 1 202 ? 45.003 47.459 4.970   1.00 11.55  ? 883  LEU A CA  1 
ATOM   1582 C C   . LEU A 1 202 ? 45.612 47.134 6.326   1.00 11.40  ? 883  LEU A C   1 
ATOM   1583 O O   . LEU A 1 202 ? 45.643 45.967 6.746   1.00 13.43  ? 883  LEU A O   1 
ATOM   1584 C CB  . LEU A 1 202 ? 46.097 47.742 3.939   1.00 10.22  ? 883  LEU A CB  1 
ATOM   1585 C CG  . LEU A 1 202 ? 45.660 47.775 2.472   1.00 9.48   ? 883  LEU A CG  1 
ATOM   1586 C CD1 . LEU A 1 202 ? 46.831 48.205 1.577   1.00 12.48  ? 883  LEU A CD1 1 
ATOM   1587 C CD2 . LEU A 1 202 ? 45.094 46.426 2.030   1.00 9.21   ? 883  LEU A CD2 1 
ATOM   1588 N N   . ASP A 1 203 ? 46.128 48.160 7.013   1.00 12.11  ? 884  ASP A N   1 
ATOM   1589 C CA  . ASP A 1 203 ? 46.677 47.974 8.351   1.00 13.15  ? 884  ASP A CA  1 
ATOM   1590 C C   . ASP A 1 203 ? 45.647 47.388 9.296   1.00 13.42  ? 884  ASP A C   1 
ATOM   1591 O O   . ASP A 1 203 ? 45.976 46.548 10.139  1.00 14.45  ? 884  ASP A O   1 
ATOM   1592 C CB  . ASP A 1 203 ? 47.181 49.302 8.909   1.00 13.90  ? 884  ASP A CB  1 
ATOM   1593 C CG  . ASP A 1 203 ? 48.500 49.714 8.318   1.00 22.19  ? 884  ASP A CG  1 
ATOM   1594 O OD1 . ASP A 1 203 ? 49.138 48.869 7.660   1.00 20.94  ? 884  ASP A OD1 1 
ATOM   1595 O OD2 . ASP A 1 203 ? 48.895 50.884 8.507   1.00 21.31  ? 884  ASP A OD2 1 
ATOM   1596 N N   . TRP A 1 204 ? 44.397 47.834 9.191   1.00 12.75  ? 885  TRP A N   1 
ATOM   1597 C CA  . TRP A 1 204 ? 43.374 47.288 10.073  1.00 13.56  ? 885  TRP A CA  1 
ATOM   1598 C C   . TRP A 1 204 ? 43.141 45.809 9.793   1.00 13.14  ? 885  TRP A C   1 
ATOM   1599 O O   . TRP A 1 204 ? 43.056 45.006 10.729  1.00 14.20  ? 885  TRP A O   1 
ATOM   1600 C CB  . TRP A 1 204 ? 42.068 48.067 9.941   1.00 12.73  ? 885  TRP A CB  1 
ATOM   1601 C CG  . TRP A 1 204 ? 40.959 47.402 10.704  1.00 13.32  ? 885  TRP A CG  1 
ATOM   1602 C CD1 . TRP A 1 204 ? 40.787 47.388 12.061  1.00 14.67  ? 885  TRP A CD1 1 
ATOM   1603 C CD2 . TRP A 1 204 ? 39.888 46.632 10.157  1.00 12.86  ? 885  TRP A CD2 1 
ATOM   1604 N NE1 . TRP A 1 204 ? 39.665 46.667 12.388  1.00 15.07  ? 885  TRP A NE1 1 
ATOM   1605 C CE2 . TRP A 1 204 ? 39.097 46.188 11.237  1.00 13.98  ? 885  TRP A CE2 1 
ATOM   1606 C CE3 . TRP A 1 204 ? 39.517 46.275 8.857   1.00 11.81  ? 885  TRP A CE3 1 
ATOM   1607 C CZ2 . TRP A 1 204 ? 37.948 45.416 11.055  1.00 14.10  ? 885  TRP A CZ2 1 
ATOM   1608 C CZ3 . TRP A 1 204 ? 38.376 45.499 8.683   1.00 11.92  ? 885  TRP A CZ3 1 
ATOM   1609 C CH2 . TRP A 1 204 ? 37.611 45.080 9.777   1.00 13.06  ? 885  TRP A CH2 1 
ATOM   1610 N N   . ILE A 1 205 ? 43.061 45.424 8.517   1.00 12.13  ? 886  ILE A N   1 
ATOM   1611 C CA  . ILE A 1 205 ? 42.873 44.007 8.201   1.00 12.26  ? 886  ILE A CA  1 
ATOM   1612 C C   . ILE A 1 205 ? 44.047 43.187 8.717   1.00 13.36  ? 886  ILE A C   1 
ATOM   1613 O O   . ILE A 1 205 ? 43.865 42.110 9.295   1.00 15.51  ? 886  ILE A O   1 
ATOM   1614 C CB  . ILE A 1 205 ? 42.671 43.803 6.689   1.00 11.20  ? 886  ILE A CB  1 
ATOM   1615 C CG1 . ILE A 1 205 ? 41.365 44.440 6.214   1.00 10.46  ? 886  ILE A CG1 1 
ATOM   1616 C CG2 . ILE A 1 205 ? 42.650 42.317 6.365   1.00 11.61  ? 886  ILE A CG2 1 
ATOM   1617 C CD1 . ILE A 1 205 ? 41.323 44.688 4.702   1.00 11.94  ? 886  ILE A CD1 1 
ATOM   1618 N N   . ARG A 1 206 ? 45.270 43.680 8.525   1.00 16.36  ? 887  ARG A N   1 
ATOM   1619 C CA  . ARG A 1 206 ? 46.427 42.939 9.013   1.00 16.12  ? 887  ARG A CA  1 
ATOM   1620 C C   . ARG A 1 206 ? 46.422 42.818 10.530  1.00 19.22  ? 887  ARG A C   1 
ATOM   1621 O O   . ARG A 1 206 ? 46.898 41.814 11.069  1.00 23.60  ? 887  ARG A O   1 
ATOM   1622 C CB  . ARG A 1 206 ? 47.713 43.596 8.529   1.00 14.93  ? 887  ARG A CB  1 
ATOM   1623 C CG  . ARG A 1 206 ? 48.002 43.284 7.085   1.00 15.97  ? 887  ARG A CG  1 
ATOM   1624 C CD  . ARG A 1 206 ? 49.399 43.726 6.701   1.00 19.50  ? 887  ARG A CD  1 
ATOM   1625 N NE  . ARG A 1 206 ? 49.397 45.136 6.342   1.00 14.51  ? 887  ARG A NE  1 
ATOM   1626 C CZ  . ARG A 1 206 ? 49.235 45.584 5.108   1.00 13.47  ? 887  ARG A CZ  1 
ATOM   1627 N NH1 . ARG A 1 206 ? 49.083 44.756 4.090   1.00 14.13  ? 887  ARG A NH1 1 
ATOM   1628 N NH2 . ARG A 1 206 ? 49.202 46.897 4.893   1.00 19.61  ? 887  ARG A NH2 1 
ATOM   1629 N N   . SER A 1 207 ? 45.865 43.804 11.232  1.00 17.15  ? 888  SER A N   1 
ATOM   1630 C CA  . SER A 1 207 ? 45.791 43.704 12.687  1.00 22.60  ? 888  SER A CA  1 
ATOM   1631 C C   . SER A 1 207 ? 44.868 42.569 13.108  1.00 24.67  ? 888  SER A C   1 
ATOM   1632 O O   . SER A 1 207 ? 45.115 41.904 14.121  1.00 27.67  ? 888  SER A O   1 
ATOM   1633 C CB  . SER A 1 207 ? 45.314 45.026 13.284  1.00 17.83  ? 888  SER A CB  1 
ATOM   1634 O OG  . SER A 1 207 ? 43.922 45.203 13.077  1.00 20.40  ? 888  SER A OG  1 
ATOM   1635 N N   . ILE A 1 208 ? 43.799 42.340 12.342  1.00 19.66  ? 889  ILE A N   1 
ATOM   1636 C CA  . ILE A 1 208 ? 42.908 41.215 12.604  1.00 27.72  ? 889  ILE A CA  1 
ATOM   1637 C C   . ILE A 1 208 ? 43.599 39.899 12.270  1.00 28.11  ? 889  ILE A C   1 
ATOM   1638 O O   . ILE A 1 208 ? 43.503 38.923 13.023  1.00 35.53  ? 889  ILE A O   1 
ATOM   1639 C CB  . ILE A 1 208 ? 41.603 41.378 11.808  1.00 20.41  ? 889  ILE A CB  1 
ATOM   1640 C CG1 . ILE A 1 208 ? 40.993 42.763 12.043  1.00 16.84  ? 889  ILE A CG1 1 
ATOM   1641 C CG2 . ILE A 1 208 ? 40.626 40.273 12.159  1.00 21.88  ? 889  ILE A CG2 1 
ATOM   1642 C CD1 . ILE A 1 208 ? 40.652 43.043 13.490  1.00 20.80  ? 889  ILE A CD1 1 
ATOM   1643 N N   . ILE A 1 209 ? 44.298 39.848 11.133  1.00 25.92  ? 890  ILE A N   1 
ATOM   1644 C CA  . ILE A 1 209 ? 45.028 38.641 10.755  1.00 25.61  ? 890  ILE A CA  1 
ATOM   1645 C C   . ILE A 1 209 ? 46.068 38.301 11.810  1.00 32.88  ? 890  ILE A C   1 
ATOM   1646 O O   . ILE A 1 209 ? 46.206 37.144 12.222  1.00 44.50  ? 890  ILE A O   1 
ATOM   1647 C CB  . ILE A 1 209 ? 45.678 38.814 9.371   1.00 22.36  ? 890  ILE A CB  1 
ATOM   1648 C CG1 . ILE A 1 209 ? 44.614 38.893 8.280   1.00 16.93  ? 890  ILE A CG1 1 
ATOM   1649 C CG2 . ILE A 1 209 ? 46.654 37.677 9.098   1.00 22.59  ? 890  ILE A CG2 1 
ATOM   1650 C CD1 . ILE A 1 209 ? 45.172 39.227 6.919   1.00 16.48  ? 890  ILE A CD1 1 
ATOM   1651 N N   . LYS A 1 210 ? 46.816 39.306 12.268  1.00 31.54  ? 891  LYS A N   1 
ATOM   1652 C CA  . LYS A 1 210 ? 47.882 39.049 13.230  1.00 37.20  ? 891  LYS A CA  1 
ATOM   1653 C C   . LYS A 1 210 ? 47.364 38.784 14.635  1.00 37.22  ? 891  LYS A C   1 
ATOM   1654 O O   . LYS A 1 210 ? 48.168 38.478 15.522  1.00 55.06  ? 891  LYS A O   1 
ATOM   1655 C CB  . LYS A 1 210 ? 48.886 40.205 13.232  1.00 33.60  ? 891  LYS A CB  1 
ATOM   1656 C CG  . LYS A 1 210 ? 50.032 39.978 12.247  1.00 40.12  ? 891  LYS A CG  1 
ATOM   1657 C CD  . LYS A 1 210 ? 51.038 41.116 12.239  1.00 45.76  ? 891  LYS A CD  1 
ATOM   1658 C CE  . LYS A 1 210 ? 50.506 42.317 11.485  1.00 27.11  ? 891  LYS A CE  1 
ATOM   1659 N NZ  . LYS A 1 210 ? 51.558 43.345 11.269  1.00 54.32  ? 891  LYS A NZ  1 
ATOM   1660 N N   . GLY A 1 211 ? 46.054 38.893 14.864  1.00 39.02  ? 892  GLY A N   1 
ATOM   1661 C CA  . GLY A 1 211 ? 45.466 38.248 16.022  1.00 48.89  ? 892  GLY A CA  1 
ATOM   1662 C C   . GLY A 1 211 ? 45.304 36.754 15.856  1.00 57.07  ? 892  GLY A C   1 
ATOM   1663 O O   . GLY A 1 211 ? 45.231 36.030 16.855  1.00 56.00  ? 892  GLY A O   1 
ATOM   1664 N N   . LYS A 1 212 ? 45.257 36.280 14.613  1.00 54.63  ? 893  LYS A N   1 
ATOM   1665 C CA  . LYS A 1 212 ? 45.164 34.858 14.311  1.00 52.99  ? 893  LYS A CA  1 
ATOM   1666 C C   . LYS A 1 212 ? 46.553 34.279 14.053  1.00 58.69  ? 893  LYS A C   1 
ATOM   1667 O O   . LYS A 1 212 ? 46.699 33.089 13.770  1.00 63.12  ? 893  LYS A O   1 
ATOM   1668 C CB  . LYS A 1 212 ? 44.260 34.627 13.099  1.00 45.24  ? 893  LYS A CB  1 
ATOM   1669 C CG  . LYS A 1 212 ? 42.968 35.434 13.128  1.00 41.88  ? 893  LYS A CG  1 
ATOM   1670 C CD  . LYS A 1 212 ? 42.062 34.999 14.270  1.00 44.57  ? 893  LYS A CD  1 
ATOM   1671 C CE  . LYS A 1 212 ? 41.420 33.654 13.982  1.00 50.35  ? 893  LYS A CE  1 
ATOM   1672 N NZ  . LYS A 1 212 ? 40.503 33.202 15.073  1.00 53.85  ? 893  LYS A NZ  1 
ATOM   1673 N N   . SER B 1 2   ? 41.326 32.190 28.264  1.00 57.09  ? -1   SER B N   1 
ATOM   1674 C CA  . SER B 1 2   ? 40.631 33.291 28.918  1.00 47.99  ? -1   SER B CA  1 
ATOM   1675 C C   . SER B 1 2   ? 39.674 33.979 27.950  1.00 55.96  ? -1   SER B C   1 
ATOM   1676 O O   . SER B 1 2   ? 38.926 34.879 28.335  1.00 36.64  ? -1   SER B O   1 
ATOM   1677 C CB  . SER B 1 2   ? 41.633 34.302 29.482  1.00 58.79  ? -1   SER B CB  1 
ATOM   1678 O OG  . SER B 1 2   ? 42.372 33.742 30.554  1.00 59.12  ? -1   SER B OG  1 
ATOM   1679 N N   . ASN B 1 3   ? 39.708 33.538 26.688  1.00 80.09  ? 684  ASN B N   1 
ATOM   1680 C CA  . ASN B 1 3   ? 38.799 34.065 25.675  1.00 68.84  ? 684  ASN B CA  1 
ATOM   1681 C C   . ASN B 1 3   ? 37.343 33.918 26.100  1.00 67.36  ? 684  ASN B C   1 
ATOM   1682 O O   . ASN B 1 3   ? 36.495 34.739 25.726  1.00 58.66  ? 684  ASN B O   1 
ATOM   1683 C CB  . ASN B 1 3   ? 39.041 33.345 24.346  1.00 73.44  ? 684  ASN B CB  1 
ATOM   1684 C CG  . ASN B 1 3   ? 38.505 34.111 23.155  1.00 81.75  ? 684  ASN B CG  1 
ATOM   1685 O OD1 . ASN B 1 3   ? 37.295 34.290 23.011  1.00 84.71  ? 684  ASN B OD1 1 
ATOM   1686 N ND2 . ASN B 1 3   ? 39.405 34.551 22.281  1.00 72.48  ? 684  ASN B ND2 1 
ATOM   1687 N N   . ASN B 1 4   ? 37.044 32.895 26.896  1.00 48.52  ? 685  ASN B N   1 
ATOM   1688 C CA  . ASN B 1 4   ? 35.694 32.549 27.313  1.00 29.94  ? 685  ASN B CA  1 
ATOM   1689 C C   . ASN B 1 4   ? 35.334 33.086 28.690  1.00 23.23  ? 685  ASN B C   1 
ATOM   1690 O O   . ASN B 1 4   ? 34.224 32.824 29.172  1.00 21.25  ? 685  ASN B O   1 
ATOM   1691 C CB  . ASN B 1 4   ? 35.541 31.027 27.310  1.00 41.56  ? 685  ASN B CB  1 
ATOM   1692 C CG  . ASN B 1 4   ? 36.684 30.331 28.033  1.00 47.66  ? 685  ASN B CG  1 
ATOM   1693 O OD1 . ASN B 1 4   ? 37.767 30.900 28.192  1.00 47.81  ? 685  ASN B OD1 1 
ATOM   1694 N ND2 . ASN B 1 4   ? 36.451 29.098 28.470  1.00 45.80  ? 685  ASN B ND2 1 
ATOM   1695 N N   . VAL B 1 5   ? 36.242 33.814 29.341  1.00 14.38  ? 686  VAL B N   1 
ATOM   1696 C CA  . VAL B 1 5   ? 35.987 34.255 30.713  1.00 14.70  ? 686  VAL B CA  1 
ATOM   1697 C C   . VAL B 1 5   ? 34.835 35.252 30.797  1.00 16.12  ? 686  VAL B C   1 
ATOM   1698 O O   . VAL B 1 5   ? 33.956 35.072 31.658  1.00 17.03  ? 686  VAL B O   1 
ATOM   1699 C CB  . VAL B 1 5   ? 37.285 34.791 31.345  1.00 19.30  ? 686  VAL B CB  1 
ATOM   1700 C CG1 . VAL B 1 5   ? 36.972 35.575 32.620  1.00 15.90  ? 686  VAL B CG1 1 
ATOM   1701 C CG2 . VAL B 1 5   ? 38.237 33.631 31.636  1.00 27.54  ? 686  VAL B CG2 1 
ATOM   1702 N N   . PRO B 1 6   ? 34.776 36.313 29.981  1.00 20.07  ? 687  PRO B N   1 
ATOM   1703 C CA  . PRO B 1 6   ? 33.607 37.203 30.073  1.00 12.03  ? 687  PRO B CA  1 
ATOM   1704 C C   . PRO B 1 6   ? 32.283 36.487 29.848  1.00 14.87  ? 687  PRO B C   1 
ATOM   1705 O O   . PRO B 1 6   ? 31.310 36.767 30.560  1.00 14.56  ? 687  PRO B O   1 
ATOM   1706 C CB  . PRO B 1 6   ? 33.884 38.256 28.985  1.00 15.12  ? 687  PRO B CB  1 
ATOM   1707 C CG  . PRO B 1 6   ? 35.363 38.249 28.827  1.00 13.84  ? 687  PRO B CG  1 
ATOM   1708 C CD  . PRO B 1 6   ? 35.778 36.830 29.029  1.00 20.95  ? 687  PRO B CD  1 
ATOM   1709 N N   . LYS B 1 7   ? 32.215 35.563 28.883  1.00 13.00  ? 688  LYS B N   1 
ATOM   1710 C CA  . LYS B 1 7   ? 30.968 34.840 28.642  1.00 16.36  ? 688  LYS B CA  1 
ATOM   1711 C C   . LYS B 1 7   ? 30.575 34.002 29.850  1.00 14.36  ? 688  LYS B C   1 
ATOM   1712 O O   . LYS B 1 7   ? 29.429 34.047 30.310  1.00 13.84  ? 688  LYS B O   1 
ATOM   1713 C CB  . LYS B 1 7   ? 31.096 33.946 27.409  1.00 15.88  ? 688  LYS B CB  1 
ATOM   1714 C CG  . LYS B 1 7   ? 29.870 33.061 27.210  1.00 25.78  ? 688  LYS B CG  1 
ATOM   1715 C CD  . LYS B 1 7   ? 29.936 32.259 25.927  1.00 31.30  ? 688  LYS B CD  1 
ATOM   1716 C CE  . LYS B 1 7   ? 28.667 31.434 25.740  1.00 31.49  ? 688  LYS B CE  1 
ATOM   1717 N NZ  . LYS B 1 7   ? 28.667 30.706 24.440  1.00 42.32  ? 688  LYS B NZ  1 
ATOM   1718 N N   . ASN B 1 8   ? 31.516 33.218 30.377  1.00 11.92  ? 689  ASN B N   1 
ATOM   1719 C CA  . ASN B 1 8   ? 31.195 32.341 31.493  1.00 11.50  ? 689  ASN B CA  1 
ATOM   1720 C C   . ASN B 1 8   ? 30.995 33.090 32.803  1.00 12.65  ? 689  ASN B C   1 
ATOM   1721 O O   . ASN B 1 8   ? 30.567 32.479 33.786  1.00 15.21  ? 689  ASN B O   1 
ATOM   1722 C CB  . ASN B 1 8   ? 32.283 31.274 31.632  1.00 16.37  ? 689  ASN B CB  1 
ATOM   1723 C CG  . ASN B 1 8   ? 32.215 30.247 30.529  1.00 19.28  ? 689  ASN B CG  1 
ATOM   1724 O OD1 . ASN B 1 8   ? 33.187 30.024 29.805  1.00 21.54  ? 689  ASN B OD1 1 
ATOM   1725 N ND2 . ASN B 1 8   ? 31.053 29.615 30.389  1.00 24.03  ? 689  ASN B ND2 1 
ATOM   1726 N N   . ALA B 1 9   ? 31.269 34.393 32.845  1.00 11.55  ? 690  ALA B N   1 
ATOM   1727 C CA  . ALA B 1 9   ? 30.962 35.195 34.018  1.00 10.11  ? 690  ALA B CA  1 
ATOM   1728 C C   . ALA B 1 9   ? 29.641 35.943 33.885  1.00 11.06  ? 690  ALA B C   1 
ATOM   1729 O O   . ALA B 1 9   ? 29.179 36.536 34.866  1.00 12.50  ? 690  ALA B O   1 
ATOM   1730 C CB  . ALA B 1 9   ? 32.096 36.196 34.291  1.00 11.96  ? 690  ALA B CB  1 
ATOM   1731 N N   . SER B 1 10  ? 29.028 35.920 32.707  1.00 12.28  ? 691  SER B N   1 
ATOM   1732 C CA  . SER B 1 10  ? 27.809 36.674 32.437  1.00 12.03  ? 691  SER B CA  1 
ATOM   1733 C C   . SER B 1 10  ? 26.603 35.858 32.880  1.00 15.07  ? 691  SER B C   1 
ATOM   1734 O O   . SER B 1 10  ? 26.218 34.890 32.215  1.00 16.71  ? 691  SER B O   1 
ATOM   1735 C CB  . SER B 1 10  ? 27.733 37.033 30.960  1.00 12.13  ? 691  SER B CB  1 
ATOM   1736 O OG  . SER B 1 10  ? 28.869 37.804 30.621  1.00 14.40  ? 691  SER B OG  1 
ATOM   1737 N N   . ALA B 1 11  ? 26.008 36.262 34.000  1.00 9.35   ? 692  ALA B N   1 
ATOM   1738 C CA  . ALA B 1 11  ? 24.888 35.571 34.619  1.00 10.16  ? 692  ALA B CA  1 
ATOM   1739 C C   . ALA B 1 11  ? 23.561 36.228 34.255  1.00 12.23  ? 692  ALA B C   1 
ATOM   1740 O O   . ALA B 1 11  ? 23.469 37.457 34.144  1.00 12.26  ? 692  ALA B O   1 
ATOM   1741 C CB  . ALA B 1 11  ? 25.050 35.558 36.143  1.00 12.62  ? 692  ALA B CB  1 
ATOM   1742 N N   . LEU B 1 12  ? 22.537 35.394 34.068  1.00 11.71  ? 693  LEU B N   1 
ATOM   1743 C CA  . LEU B 1 12  ? 21.156 35.863 34.006  1.00 12.03  ? 693  LEU B CA  1 
ATOM   1744 C C   . LEU B 1 12  ? 20.616 36.028 35.420  1.00 11.45  ? 693  LEU B C   1 
ATOM   1745 O O   . LEU B 1 12  ? 20.897 35.208 36.297  1.00 15.70  ? 693  LEU B O   1 
ATOM   1746 C CB  . LEU B 1 12  ? 20.293 34.867 33.223  1.00 13.59  ? 693  LEU B CB  1 
ATOM   1747 C CG  . LEU B 1 12  ? 18.756 34.943 33.297  1.00 12.35  ? 693  LEU B CG  1 
ATOM   1748 C CD1 . LEU B 1 12  ? 18.211 36.007 32.367  1.00 12.59  ? 693  LEU B CD1 1 
ATOM   1749 C CD2 . LEU B 1 12  ? 18.146 33.586 32.967  1.00 17.34  ? 693  LEU B CD2 1 
ATOM   1750 N N   . LEU B 1 13  ? 19.844 37.093 35.647  1.00 13.31  ? 694  LEU B N   1 
ATOM   1751 C CA  . LEU B 1 13  ? 19.129 37.277 36.906  1.00 9.70   ? 694  LEU B CA  1 
ATOM   1752 C C   . LEU B 1 13  ? 17.645 37.051 36.681  1.00 10.54  ? 694  LEU B C   1 
ATOM   1753 O O   . LEU B 1 13  ? 17.086 37.539 35.696  1.00 12.50  ? 694  LEU B O   1 
ATOM   1754 C CB  . LEU B 1 13  ? 19.352 38.676 37.491  1.00 10.09  ? 694  LEU B CB  1 
ATOM   1755 C CG  . LEU B 1 13  ? 20.779 39.074 37.858  1.00 10.31  ? 694  LEU B CG  1 
ATOM   1756 C CD1 . LEU B 1 13  ? 20.737 40.458 38.512  1.00 10.76  ? 694  LEU B CD1 1 
ATOM   1757 C CD2 . LEU B 1 13  ? 21.453 38.063 38.770  1.00 12.94  ? 694  LEU B CD2 1 
ATOM   1758 N N   . ARG B 1 14  ? 17.018 36.292 37.584  1.00 10.91  ? 695  ARG B N   1 
ATOM   1759 C CA  . ARG B 1 14  ? 15.569 36.102 37.627  1.00 11.83  ? 695  ARG B CA  1 
ATOM   1760 C C   . ARG B 1 14  ? 15.040 36.703 38.916  1.00 14.15  ? 695  ARG B C   1 
ATOM   1761 O O   . ARG B 1 14  ? 15.604 36.466 39.989  1.00 15.87  ? 695  ARG B O   1 
ATOM   1762 C CB  . ARG B 1 14  ? 15.183 34.618 37.564  1.00 15.78  ? 695  ARG B CB  1 
ATOM   1763 C CG  . ARG B 1 14  ? 15.365 34.002 36.213  1.00 13.38  ? 695  ARG B CG  1 
ATOM   1764 C CD  . ARG B 1 14  ? 14.727 32.616 36.147  1.00 18.33  ? 695  ARG B CD  1 
ATOM   1765 N NE  . ARG B 1 14  ? 14.769 32.127 34.778  1.00 23.88  ? 695  ARG B NE  1 
ATOM   1766 C CZ  . ARG B 1 14  ? 15.783 31.446 34.266  1.00 27.69  ? 695  ARG B CZ  1 
ATOM   1767 N NH1 . ARG B 1 14  ? 16.823 31.094 35.007  1.00 21.68  ? 695  ARG B NH1 1 
ATOM   1768 N NH2 . ARG B 1 14  ? 15.750 31.103 32.981  1.00 25.27  ? 695  ARG B NH2 1 
ATOM   1769 N N   . MET B 1 15  ? 13.967 37.485 38.811  1.00 14.65  ? 696  MET B N   1 
ATOM   1770 C CA  . MET B 1 15  ? 13.380 38.150 39.964  1.00 13.06  ? 696  MET B CA  1 
ATOM   1771 C C   . MET B 1 15  ? 11.893 37.840 40.027  1.00 17.59  ? 696  MET B C   1 
ATOM   1772 O O   . MET B 1 15  ? 11.177 38.006 39.035  1.00 15.46  ? 696  MET B O   1 
ATOM   1773 C CB  . MET B 1 15  ? 13.606 39.659 39.905  1.00 15.33  ? 696  MET B CB  1 
ATOM   1774 C CG  . MET B 1 15  ? 15.094 40.061 39.898  1.00 11.86  ? 696  MET B CG  1 
ATOM   1775 S SD  . MET B 1 15  ? 15.761 40.195 38.226  1.00 14.60  ? 696  MET B SD  1 
ATOM   1776 C CE  . MET B 1 15  ? 15.005 41.719 37.657  1.00 24.52  ? 696  MET B CE  1 
ATOM   1777 N N   . ASN B 1 16  ? 11.446 37.371 41.183  1.00 17.61  ? 697  ASN B N   1 
ATOM   1778 C CA  . ASN B 1 16  ? 10.033 37.134 41.466  1.00 22.22  ? 697  ASN B CA  1 
ATOM   1779 C C   . ASN B 1 16  ? 9.613  38.164 42.505  1.00 20.02  ? 697  ASN B C   1 
ATOM   1780 O O   . ASN B 1 16  ? 9.821  37.968 43.706  1.00 19.54  ? 697  ASN B O   1 
ATOM   1781 C CB  . ASN B 1 16  ? 9.805  35.709 41.955  1.00 23.74  ? 697  ASN B CB  1 
ATOM   1782 C CG  . ASN B 1 16  ? 10.073 34.681 40.879  1.00 39.31  ? 697  ASN B CG  1 
ATOM   1783 O OD1 . ASN B 1 16  ? 9.505  34.749 39.789  1.00 40.97  ? 697  ASN B OD1 1 
ATOM   1784 N ND2 . ASN B 1 16  ? 10.960 33.736 41.168  1.00 41.99  ? 697  ASN B ND2 1 
ATOM   1785 N N   . PHE B 1 17  ? 9.052  39.275 42.038  1.00 19.21  ? 698  PHE B N   1 
ATOM   1786 C CA  . PHE B 1 17  ? 8.612  40.337 42.929  1.00 16.01  ? 698  PHE B CA  1 
ATOM   1787 C C   . PHE B 1 17  ? 7.235  39.989 43.466  1.00 16.37  ? 698  PHE B C   1 
ATOM   1788 O O   . PHE B 1 17  ? 6.296  39.793 42.689  1.00 23.19  ? 698  PHE B O   1 
ATOM   1789 C CB  . PHE B 1 17  ? 8.586  41.674 42.193  1.00 19.28  ? 698  PHE B CB  1 
ATOM   1790 C CG  . PHE B 1 17  ? 9.881  42.016 41.523  1.00 15.18  ? 698  PHE B CG  1 
ATOM   1791 C CD1 . PHE B 1 17  ? 11.011 42.279 42.273  1.00 12.41  ? 698  PHE B CD1 1 
ATOM   1792 C CD2 . PHE B 1 17  ? 9.965  42.084 40.142  1.00 21.53  ? 698  PHE B CD2 1 
ATOM   1793 C CE1 . PHE B 1 17  ? 12.211 42.596 41.655  1.00 24.46  ? 698  PHE B CE1 1 
ATOM   1794 C CE2 . PHE B 1 17  ? 11.158 42.402 39.522  1.00 16.68  ? 698  PHE B CE2 1 
ATOM   1795 C CZ  . PHE B 1 17  ? 12.279 42.667 40.278  1.00 22.32  ? 698  PHE B CZ  1 
ATOM   1796 N N   . VAL B 1 18  ? 7.114  39.898 44.784  1.00 16.71  ? 699  VAL B N   1 
ATOM   1797 C CA  . VAL B 1 18  ? 5.868  39.500 45.424  1.00 19.21  ? 699  VAL B CA  1 
ATOM   1798 C C   . VAL B 1 18  ? 5.173  40.738 45.971  1.00 25.97  ? 699  VAL B C   1 
ATOM   1799 O O   . VAL B 1 18  ? 5.790  41.565 46.654  1.00 21.75  ? 699  VAL B O   1 
ATOM   1800 C CB  . VAL B 1 18  ? 6.113  38.462 46.532  1.00 28.12  ? 699  VAL B CB  1 
ATOM   1801 C CG1 . VAL B 1 18  ? 4.799  38.083 47.203  1.00 34.19  ? 699  VAL B CG1 1 
ATOM   1802 C CG2 . VAL B 1 18  ? 6.780  37.236 45.952  1.00 23.47  ? 699  VAL B CG2 1 
ATOM   1803 N N   . LYS B 1 19  ? 3.885  40.865 45.667  1.00 29.95  ? 700  LYS B N   1 
ATOM   1804 C CA  . LYS B 1 19  ? 3.072  42.001 46.097  1.00 28.18  ? 700  LYS B CA  1 
ATOM   1805 C C   . LYS B 1 19  ? 1.724  41.422 46.514  1.00 22.27  ? 700  LYS B C   1 
ATOM   1806 O O   . LYS B 1 19  ? 0.876  41.140 45.663  1.00 25.10  ? 700  LYS B O   1 
ATOM   1807 C CB  . LYS B 1 19  ? 2.935  43.021 44.974  1.00 36.35  ? 700  LYS B CB  1 
ATOM   1808 C CG  . LYS B 1 19  ? 3.088  42.387 43.594  1.00 35.19  ? 700  LYS B CG  1 
ATOM   1809 C CD  . LYS B 1 19  ? 2.723  43.333 42.469  1.00 51.33  ? 700  LYS B CD  1 
ATOM   1810 C CE  . LYS B 1 19  ? 2.885  42.641 41.122  1.00 41.56  ? 700  LYS B CE  1 
ATOM   1811 N NZ  . LYS B 1 19  ? 2.484  43.526 39.991  1.00 54.98  ? 700  LYS B NZ  1 
ATOM   1812 N N   . GLY B 1 20  ? 1.539  41.234 47.818  1.00 28.85  ? 701  GLY B N   1 
ATOM   1813 C CA  . GLY B 1 20  ? 0.449  40.415 48.304  1.00 36.35  ? 701  GLY B CA  1 
ATOM   1814 C C   . GLY B 1 20  ? 0.707  38.956 47.982  1.00 33.45  ? 701  GLY B C   1 
ATOM   1815 O O   . GLY B 1 20  ? 1.744  38.410 48.372  1.00 37.00  ? 701  GLY B O   1 
ATOM   1816 N N   . ASN B 1 21  ? -0.225 38.312 47.273  1.00 39.13  ? 702  ASN B N   1 
ATOM   1817 C CA  . ASN B 1 21  ? -0.010 36.975 46.729  1.00 31.57  ? 702  ASN B CA  1 
ATOM   1818 C C   . ASN B 1 21  ? 0.198  37.002 45.217  1.00 32.35  ? 702  ASN B C   1 
ATOM   1819 O O   . ASN B 1 21  ? 0.039  35.975 44.548  1.00 33.87  ? 702  ASN B O   1 
ATOM   1820 C CB  . ASN B 1 21  ? -1.170 36.046 47.096  1.00 33.61  ? 702  ASN B CB  1 
ATOM   1821 C CG  . ASN B 1 21  ? -2.528 36.574 46.652  1.00 35.16  ? 702  ASN B CG  1 
ATOM   1822 O OD1 . ASN B 1 21  ? -2.625 37.518 45.868  1.00 43.29  ? 702  ASN B OD1 1 
ATOM   1823 N ND2 . ASN B 1 21  ? -3.588 35.952 47.153  1.00 33.12  ? 702  ASN B ND2 1 
ATOM   1824 N N   . GLN B 1 22  ? 0.554  38.161 44.672  1.00 25.05  ? 703  GLN B N   1 
ATOM   1825 C CA  . GLN B 1 22  ? 0.720  38.356 43.239  1.00 24.58  ? 703  GLN B CA  1 
ATOM   1826 C C   . GLN B 1 22  ? 2.202  38.303 42.900  1.00 31.46  ? 703  GLN B C   1 
ATOM   1827 O O   . GLN B 1 22  ? 3.006  39.012 43.513  1.00 30.28  ? 703  GLN B O   1 
ATOM   1828 C CB  . GLN B 1 22  ? 0.129  39.700 42.808  1.00 37.28  ? 703  GLN B CB  1 
ATOM   1829 C CG  . GLN B 1 22  ? 0.071  39.915 41.309  1.00 40.62  ? 703  GLN B CG  1 
ATOM   1830 C CD  . GLN B 1 22  ? -1.081 39.169 40.671  1.00 44.73  ? 703  GLN B CD  1 
ATOM   1831 O OE1 . GLN B 1 22  ? -2.220 39.260 41.132  1.00 48.42  ? 703  GLN B OE1 1 
ATOM   1832 N NE2 . GLN B 1 22  ? -0.792 38.417 39.611  1.00 48.66  ? 703  GLN B NE2 1 
ATOM   1833 N N   . VAL B 1 23  ? 2.561  37.469 41.930  1.00 22.73  ? 704  VAL B N   1 
ATOM   1834 C CA  . VAL B 1 23  ? 3.936  37.383 41.450  1.00 21.13  ? 704  VAL B CA  1 
ATOM   1835 C C   . VAL B 1 23  ? 4.061  38.180 40.163  1.00 21.34  ? 704  VAL B C   1 
ATOM   1836 O O   . VAL B 1 23  ? 3.201  38.091 39.277  1.00 33.93  ? 704  VAL B O   1 
ATOM   1837 C CB  . VAL B 1 23  ? 4.371  35.926 41.228  1.00 21.80  ? 704  VAL B CB  1 
ATOM   1838 C CG1 . VAL B 1 23  ? 5.855  35.873 40.853  1.00 27.09  ? 704  VAL B CG1 1 
ATOM   1839 C CG2 . VAL B 1 23  ? 4.084  35.088 42.465  1.00 30.40  ? 704  VAL B CG2 1 
ATOM   1840 N N   . LEU B 1 24  ? 5.130  38.962 40.062  1.00 20.60  ? 705  LEU B N   1 
ATOM   1841 C CA  . LEU B 1 24  ? 5.531  39.619 38.823  1.00 24.95  ? 705  LEU B CA  1 
ATOM   1842 C C   . LEU B 1 24  ? 6.965  39.193 38.541  1.00 22.19  ? 705  LEU B C   1 
ATOM   1843 O O   . LEU B 1 24  ? 7.867  39.491 39.329  1.00 20.26  ? 705  LEU B O   1 
ATOM   1844 C CB  . LEU B 1 24  ? 5.417  41.140 38.931  1.00 28.08  ? 705  LEU B CB  1 
ATOM   1845 C CG  . LEU B 1 24  ? 5.894  41.927 37.706  1.00 32.13  ? 705  LEU B CG  1 
ATOM   1846 C CD1 . LEU B 1 24  ? 5.033  41.609 36.490  1.00 28.43  ? 705  LEU B CD1 1 
ATOM   1847 C CD2 . LEU B 1 24  ? 5.894  43.420 37.987  1.00 39.21  ? 705  LEU B CD2 1 
ATOM   1848 N N   . SER B 1 25  ? 7.172  38.470 37.444  1.00 18.21  ? 706  SER B N   1 
ATOM   1849 C CA  . SER B 1 25  ? 8.496  37.968 37.114  1.00 22.61  ? 706  SER B CA  1 
ATOM   1850 C C   . SER B 1 25  ? 9.238  38.961 36.232  1.00 21.93  ? 706  SER B C   1 
ATOM   1851 O O   . SER B 1 25  ? 8.651  39.588 35.345  1.00 24.71  ? 706  SER B O   1 
ATOM   1852 C CB  . SER B 1 25  ? 8.405  36.616 36.409  1.00 23.64  ? 706  SER B CB  1 
ATOM   1853 O OG  . SER B 1 25  ? 8.011  35.601 37.312  1.00 44.32  ? 706  SER B OG  1 
ATOM   1854 N N   . GLY B 1 26  ? 10.532 39.109 36.494  1.00 22.79  ? 707  GLY B N   1 
ATOM   1855 C CA  . GLY B 1 26  ? 11.388 39.893 35.629  1.00 15.92  ? 707  GLY B CA  1 
ATOM   1856 C C   . GLY B 1 26  ? 12.758 39.261 35.550  1.00 14.14  ? 707  GLY B C   1 
ATOM   1857 O O   . GLY B 1 26  ? 13.120 38.402 36.362  1.00 13.74  ? 707  GLY B O   1 
ATOM   1858 N N   . THR B 1 27  ? 13.526 39.700 34.557  1.00 13.11  ? 708  THR B N   1 
ATOM   1859 C CA  . THR B 1 27  ? 14.888 39.219 34.389  1.00 12.41  ? 708  THR B CA  1 
ATOM   1860 C C   . THR B 1 27  ? 15.827 40.404 34.225  1.00 14.18  ? 708  THR B C   1 
ATOM   1861 O O   . THR B 1 27  ? 15.429 41.494 33.805  1.00 11.95  ? 708  THR B O   1 
ATOM   1862 C CB  . THR B 1 27  ? 15.041 38.258 33.187  1.00 13.24  ? 708  THR B CB  1 
ATOM   1863 O OG1 . THR B 1 27  ? 14.843 38.967 31.956  1.00 13.96  ? 708  THR B OG1 1 
ATOM   1864 C CG2 . THR B 1 27  ? 14.044 37.100 33.273  1.00 17.11  ? 708  THR B CG2 1 
ATOM   1865 N N   . GLY B 1 28  ? 17.083 40.171 34.578  1.00 10.85  ? 709  GLY B N   1 
ATOM   1866 C CA  . GLY B 1 28  ? 18.119 41.164 34.402  1.00 10.55  ? 709  GLY B CA  1 
ATOM   1867 C C   . GLY B 1 28  ? 19.438 40.489 34.087  1.00 15.47  ? 709  GLY B C   1 
ATOM   1868 O O   . GLY B 1 28  ? 19.461 39.319 33.687  1.00 12.18  ? 709  GLY B O   1 
ATOM   1869 N N   . SER B 1 29  ? 20.542 41.207 34.261  1.00 9.83   ? 710  SER B N   1 
ATOM   1870 C CA  . SER B 1 29  ? 21.855 40.656 33.964  1.00 13.31  ? 710  SER B CA  1 
ATOM   1871 C C   . SER B 1 29  ? 22.810 40.993 35.097  1.00 11.75  ? 710  SER B C   1 
ATOM   1872 O O   . SER B 1 29  ? 22.579 41.923 35.873  1.00 9.74   ? 710  SER B O   1 
ATOM   1873 C CB  . SER B 1 29  ? 22.389 41.189 32.629  1.00 12.05  ? 710  SER B CB  1 
ATOM   1874 O OG  . SER B 1 29  ? 21.462 40.955 31.582  1.00 14.02  ? 710  SER B OG  1 
ATOM   1875 N N   . ALA B 1 30  ? 23.896 40.220 35.182  1.00 10.33  ? 711  ALA B N   1 
ATOM   1876 C CA  . ALA B 1 30  ? 24.913 40.410 36.206  1.00 9.25   ? 711  ALA B CA  1 
ATOM   1877 C C   . ALA B 1 30  ? 26.191 39.697 35.774  1.00 11.91  ? 711  ALA B C   1 
ATOM   1878 O O   . ALA B 1 30  ? 26.166 38.828 34.897  1.00 11.84  ? 711  ALA B O   1 
ATOM   1879 C CB  . ALA B 1 30  ? 24.437 39.904 37.573  1.00 7.58   ? 711  ALA B CB  1 
ATOM   1880 N N   . THR B 1 31  ? 27.309 40.080 36.398  1.00 8.37   ? 712  THR B N   1 
ATOM   1881 C CA  . THR B 1 31  ? 28.629 39.528 36.089  1.00 8.16   ? 712  THR B CA  1 
ATOM   1882 C C   . THR B 1 31  ? 29.279 38.987 37.358  1.00 11.24  ? 712  THR B C   1 
ATOM   1883 O O   . THR B 1 31  ? 29.289 39.667 38.388  1.00 11.65  ? 712  THR B O   1 
ATOM   1884 C CB  . THR B 1 31  ? 29.554 40.587 35.459  1.00 9.26   ? 712  THR B CB  1 
ATOM   1885 O OG1 . THR B 1 31  ? 28.928 41.168 34.313  1.00 15.75  ? 712  THR B OG1 1 
ATOM   1886 C CG2 . THR B 1 31  ? 30.882 39.965 35.035  1.00 10.43  ? 712  THR B CG2 1 
ATOM   1887 N N   . PHE B 1 32  ? 29.830 37.774 37.289  1.00 9.63   ? 713  PHE B N   1 
ATOM   1888 C CA  . PHE B 1 32  ? 30.627 37.259 38.399  1.00 8.38   ? 713  PHE B CA  1 
ATOM   1889 C C   . PHE B 1 32  ? 31.976 37.971 38.413  1.00 12.16  ? 713  PHE B C   1 
ATOM   1890 O O   . PHE B 1 32  ? 32.728 37.899 37.437  1.00 12.93  ? 713  PHE B O   1 
ATOM   1891 C CB  . PHE B 1 32  ? 30.820 35.740 38.282  1.00 10.84  ? 713  PHE B CB  1 
ATOM   1892 C CG  . PHE B 1 32  ? 29.739 34.933 38.957  1.00 13.30  ? 713  PHE B CG  1 
ATOM   1893 C CD1 . PHE B 1 32  ? 29.770 34.714 40.326  1.00 16.15  ? 713  PHE B CD1 1 
ATOM   1894 C CD2 . PHE B 1 32  ? 28.696 34.389 38.222  1.00 13.41  ? 713  PHE B CD2 1 
ATOM   1895 C CE1 . PHE B 1 32  ? 28.774 33.981 40.957  1.00 17.01  ? 713  PHE B CE1 1 
ATOM   1896 C CE2 . PHE B 1 32  ? 27.701 33.655 38.840  1.00 11.91  ? 713  PHE B CE2 1 
ATOM   1897 C CZ  . PHE B 1 32  ? 27.738 33.449 40.211  1.00 13.79  ? 713  PHE B CZ  1 
ATOM   1898 N N   . ILE B 1 33  ? 32.273 38.678 39.506  1.00 9.60   ? 714  ILE B N   1 
ATOM   1899 C CA  . ILE B 1 33  ? 33.563 39.341 39.672  1.00 9.68   ? 714  ILE B CA  1 
ATOM   1900 C C   . ILE B 1 33  ? 34.356 38.778 40.836  1.00 15.06  ? 714  ILE B C   1 
ATOM   1901 O O   . ILE B 1 33  ? 35.441 39.293 41.150  1.00 15.89  ? 714  ILE B O   1 
ATOM   1902 C CB  . ILE B 1 33  ? 33.392 40.866 39.806  1.00 8.62   ? 714  ILE B CB  1 
ATOM   1903 C CG1 . ILE B 1 33  ? 32.499 41.213 41.005  1.00 8.38   ? 714  ILE B CG1 1 
ATOM   1904 C CG2 . ILE B 1 33  ? 32.836 41.412 38.507  1.00 10.20  ? 714  ILE B CG2 1 
ATOM   1905 C CD1 . ILE B 1 33  ? 32.391 42.713 41.280  1.00 13.27  ? 714  ILE B CD1 1 
ATOM   1906 N N   . ALA B 1 34  ? 33.854 37.727 41.469  1.00 10.31  ? 715  ALA B N   1 
ATOM   1907 C CA  . ALA B 1 34  ? 34.540 36.969 42.504  1.00 14.89  ? 715  ALA B CA  1 
ATOM   1908 C C   . ALA B 1 34  ? 33.922 35.584 42.483  1.00 9.55   ? 715  ALA B C   1 
ATOM   1909 O O   . ALA B 1 34  ? 32.892 35.371 41.830  1.00 14.91  ? 715  ALA B O   1 
ATOM   1910 C CB  . ALA B 1 34  ? 34.382 37.629 43.881  1.00 12.12  ? 715  ALA B CB  1 
ATOM   1911 N N   . PRO B 1 35  ? 34.530 34.608 43.163  1.00 11.75  ? 716  PRO B N   1 
ATOM   1912 C CA  . PRO B 1 35  ? 33.910 33.270 43.183  1.00 12.68  ? 716  PRO B CA  1 
ATOM   1913 C C   . PRO B 1 35  ? 32.465 33.272 43.676  1.00 14.03  ? 716  PRO B C   1 
ATOM   1914 O O   . PRO B 1 35  ? 31.699 32.371 43.305  1.00 13.78  ? 716  PRO B O   1 
ATOM   1915 C CB  . PRO B 1 35  ? 34.824 32.466 44.117  1.00 15.26  ? 716  PRO B CB  1 
ATOM   1916 C CG  . PRO B 1 35  ? 36.161 33.105 43.974  1.00 16.63  ? 716  PRO B CG  1 
ATOM   1917 C CD  . PRO B 1 35  ? 35.903 34.587 43.711  1.00 10.96  ? 716  PRO B CD  1 
ATOM   1918 N N   . ASN B 1 36  ? 32.061 34.266 44.481  1.00 12.05  ? 717  ASN B N   1 
ATOM   1919 C CA  . ASN B 1 36  ? 30.721 34.300 45.065  1.00 14.72  ? 717  ASN B CA  1 
ATOM   1920 C C   . ASN B 1 36  ? 30.159 35.721 45.140  1.00 10.89  ? 717  ASN B C   1 
ATOM   1921 O O   . ASN B 1 36  ? 29.429 36.050 46.079  1.00 12.86  ? 717  ASN B O   1 
ATOM   1922 C CB  . ASN B 1 36  ? 30.717 33.683 46.468  1.00 14.39  ? 717  ASN B CB  1 
ATOM   1923 C CG  . ASN B 1 36  ? 31.580 34.448 47.439  1.00 19.24  ? 717  ASN B CG  1 
ATOM   1924 O OD1 . ASN B 1 36  ? 32.505 35.161 47.034  1.00 20.80  ? 717  ASN B OD1 1 
ATOM   1925 N ND2 . ASN B 1 36  ? 31.284 34.320 48.730  1.00 22.28  ? 717  ASN B ND2 1 
ATOM   1926 N N   . VAL B 1 37  ? 30.479 36.570 44.168  1.00 12.21  ? 718  VAL B N   1 
ATOM   1927 C CA  . VAL B 1 37  ? 30.049 37.967 44.182  1.00 9.62   ? 718  VAL B CA  1 
ATOM   1928 C C   . VAL B 1 37  ? 29.616 38.361 42.780  1.00 11.39  ? 718  VAL B C   1 
ATOM   1929 O O   . VAL B 1 37  ? 30.336 38.110 41.807  1.00 8.65   ? 718  VAL B O   1 
ATOM   1930 C CB  . VAL B 1 37  ? 31.158 38.911 44.684  1.00 12.84  ? 718  VAL B CB  1 
ATOM   1931 C CG1 . VAL B 1 37  ? 30.730 40.354 44.533  1.00 15.30  ? 718  VAL B CG1 1 
ATOM   1932 C CG2 . VAL B 1 37  ? 31.511 38.612 46.136  1.00 14.72  ? 718  VAL B CG2 1 
ATOM   1933 N N   . LEU B 1 38  ? 28.447 38.987 42.674  1.00 8.64   ? 719  LEU B N   1 
ATOM   1934 C CA  . LEU B 1 38  ? 27.905 39.439 41.402  1.00 8.78   ? 719  LEU B CA  1 
ATOM   1935 C C   . LEU B 1 38  ? 27.832 40.957 41.377  1.00 7.38   ? 719  LEU B C   1 
ATOM   1936 O O   . LEU B 1 38  ? 27.510 41.586 42.390  1.00 12.31  ? 719  LEU B O   1 
ATOM   1937 C CB  . LEU B 1 38  ? 26.510 38.852 41.166  1.00 10.67  ? 719  LEU B CB  1 
ATOM   1938 C CG  . LEU B 1 38  ? 26.407 37.352 40.904  1.00 11.62  ? 719  LEU B CG  1 
ATOM   1939 C CD1 . LEU B 1 38  ? 24.955 36.895 41.077  1.00 11.24  ? 719  LEU B CD1 1 
ATOM   1940 C CD2 . LEU B 1 38  ? 26.885 37.061 39.496  1.00 11.40  ? 719  LEU B CD2 1 
ATOM   1941 N N   . LEU B 1 39  ? 28.121 41.535 40.217  1.00 7.28   ? 720  LEU B N   1 
ATOM   1942 C CA  . LEU B 1 39  ? 27.971 42.967 39.976  1.00 9.69   ? 720  LEU B CA  1 
ATOM   1943 C C   . LEU B 1 39  ? 26.784 43.191 39.047  1.00 10.92  ? 720  LEU B C   1 
ATOM   1944 O O   . LEU B 1 39  ? 26.677 42.541 38.001  1.00 9.37   ? 720  LEU B O   1 
ATOM   1945 C CB  . LEU B 1 39  ? 29.242 43.559 39.363  1.00 10.74  ? 720  LEU B CB  1 
ATOM   1946 C CG  . LEU B 1 39  ? 29.212 45.062 39.066  1.00 14.87  ? 720  LEU B CG  1 
ATOM   1947 C CD1 . LEU B 1 39  ? 29.287 45.857 40.366  1.00 13.09  ? 720  LEU B CD1 1 
ATOM   1948 C CD2 . LEU B 1 39  ? 30.335 45.460 38.117  1.00 17.77  ? 720  LEU B CD2 1 
ATOM   1949 N N   . THR B 1 40  ? 25.893 44.102 39.428  1.00 9.23   ? 721  THR B N   1 
ATOM   1950 C CA  . THR B 1 40  ? 24.710 44.388 38.616  1.00 9.73   ? 721  THR B CA  1 
ATOM   1951 C C   . THR B 1 40  ? 24.268 45.820 38.898  1.00 8.67   ? 721  THR B C   1 
ATOM   1952 O O   . THR B 1 40  ? 24.968 46.579 39.576  1.00 8.58   ? 721  THR B O   1 
ATOM   1953 C CB  . THR B 1 40  ? 23.593 43.367 38.885  1.00 8.61   ? 721  THR B CB  1 
ATOM   1954 O OG1 . THR B 1 40  ? 22.513 43.583 37.969  1.00 12.68  ? 721  THR B OG1 1 
ATOM   1955 C CG2 . THR B 1 40  ? 23.075 43.468 40.316  1.00 8.59   ? 721  THR B CG2 1 
ATOM   1956 N N   . VAL B 1 41  ? 23.097 46.194 38.366  1.00 10.24  ? 722  VAL B N   1 
ATOM   1957 C CA  . VAL B 1 41  ? 22.524 47.517 38.604  1.00 13.97  ? 722  VAL B CA  1 
ATOM   1958 C C   . VAL B 1 41  ? 21.511 47.420 39.733  1.00 9.24   ? 722  VAL B C   1 
ATOM   1959 O O   . VAL B 1 41  ? 20.844 46.393 39.926  1.00 8.25   ? 722  VAL B O   1 
ATOM   1960 C CB  . VAL B 1 41  ? 21.870 48.114 37.341  1.00 11.30  ? 722  VAL B CB  1 
ATOM   1961 C CG1 . VAL B 1 41  ? 22.936 48.479 36.317  1.00 18.24  ? 722  VAL B CG1 1 
ATOM   1962 C CG2 . VAL B 1 41  ? 20.843 47.146 36.755  1.00 12.74  ? 722  VAL B CG2 1 
ATOM   1963 N N   . ALA B 1 42  ? 21.400 48.515 40.492  1.00 9.06   ? 723  ALA B N   1 
ATOM   1964 C CA  . ALA B 1 42  ? 20.452 48.566 41.595  1.00 10.04  ? 723  ALA B CA  1 
ATOM   1965 C C   . ALA B 1 42  ? 19.014 48.450 41.111  1.00 12.28  ? 723  ALA B C   1 
ATOM   1966 O O   . ALA B 1 42  ? 18.165 47.918 41.833  1.00 14.29  ? 723  ALA B O   1 
ATOM   1967 C CB  . ALA B 1 42  ? 20.633 49.866 42.382  1.00 17.61  ? 723  ALA B CB  1 
ATOM   1968 N N   . HIS B 1 43  ? 18.715 48.927 39.900  1.00 14.56  ? 724  HIS B N   1 
ATOM   1969 C CA  . HIS B 1 43  ? 17.320 48.995 39.484  1.00 13.49  ? 724  HIS B CA  1 
ATOM   1970 C C   . HIS B 1 43  ? 16.758 47.643 39.070  1.00 14.92  ? 724  HIS B C   1 
ATOM   1971 O O   . HIS B 1 43  ? 15.558 47.551 38.781  1.00 15.04  ? 724  HIS B O   1 
ATOM   1972 C CB  . HIS B 1 43  ? 17.135 50.050 38.376  1.00 17.19  ? 724  HIS B CB  1 
ATOM   1973 C CG  . HIS B 1 43  ? 17.523 49.609 36.997  1.00 15.46  ? 724  HIS B CG  1 
ATOM   1974 N ND1 . HIS B 1 43  ? 18.561 50.191 36.301  1.00 20.23  ? 724  HIS B ND1 1 
ATOM   1975 C CD2 . HIS B 1 43  ? 16.963 48.712 36.150  1.00 21.51  ? 724  HIS B CD2 1 
ATOM   1976 C CE1 . HIS B 1 43  ? 18.654 49.640 35.104  1.00 20.94  ? 724  HIS B CE1 1 
ATOM   1977 N NE2 . HIS B 1 43  ? 17.695 48.741 34.986  1.00 19.82  ? 724  HIS B NE2 1 
ATOM   1978 N N   . ASN B 1 44  ? 17.573 46.584 39.075  1.00 15.90  ? 725  ASN B N   1 
ATOM   1979 C CA  . ASN B 1 44  ? 17.012 45.245 38.995  1.00 19.50  ? 725  ASN B CA  1 
ATOM   1980 C C   . ASN B 1 44  ? 16.228 44.880 40.252  1.00 18.16  ? 725  ASN B C   1 
ATOM   1981 O O   . ASN B 1 44  ? 15.424 43.939 40.215  1.00 12.77  ? 725  ASN B O   1 
ATOM   1982 C CB  . ASN B 1 44  ? 18.130 44.224 38.731  1.00 14.91  ? 725  ASN B CB  1 
ATOM   1983 C CG  . ASN B 1 44  ? 18.603 44.237 37.284  1.00 15.34  ? 725  ASN B CG  1 
ATOM   1984 O OD1 . ASN B 1 44  ? 17.810 44.451 36.367  1.00 14.51  ? 725  ASN B OD1 1 
ATOM   1985 N ND2 . ASN B 1 44  ? 19.900 43.999 37.072  1.00 12.61  ? 725  ASN B ND2 1 
ATOM   1986 N N   . PHE B 1 45  ? 16.400 45.629 41.344  1.00 13.09  ? 726  PHE B N   1 
ATOM   1987 C CA  . PHE B 1 45  ? 15.773 45.256 42.602  1.00 12.09  ? 726  PHE B CA  1 
ATOM   1988 C C   . PHE B 1 45  ? 14.972 46.384 43.254  1.00 10.85  ? 726  PHE B C   1 
ATOM   1989 O O   . PHE B 1 45  ? 14.030 46.105 44.004  1.00 13.23  ? 726  PHE B O   1 
ATOM   1990 C CB  . PHE B 1 45  ? 16.841 44.749 43.564  1.00 15.20  ? 726  PHE B CB  1 
ATOM   1991 C CG  . PHE B 1 45  ? 17.674 43.642 42.988  1.00 10.81  ? 726  PHE B CG  1 
ATOM   1992 C CD1 . PHE B 1 45  ? 17.131 42.384 42.793  1.00 13.13  ? 726  PHE B CD1 1 
ATOM   1993 C CD2 . PHE B 1 45  ? 18.993 43.864 42.629  1.00 12.34  ? 726  PHE B CD2 1 
ATOM   1994 C CE1 . PHE B 1 45  ? 17.897 41.361 42.255  1.00 15.16  ? 726  PHE B CE1 1 
ATOM   1995 C CE2 . PHE B 1 45  ? 19.762 42.846 42.088  1.00 13.95  ? 726  PHE B CE2 1 
ATOM   1996 C CZ  . PHE B 1 45  ? 19.213 41.595 41.905  1.00 15.72  ? 726  PHE B CZ  1 
ATOM   1997 N N   . ILE B 1 46  ? 15.319 47.650 42.998  1.00 11.73  ? 727  ILE B N   1 
ATOM   1998 C CA  . ILE B 1 46  ? 14.678 48.752 43.706  1.00 17.23  ? 727  ILE B CA  1 
ATOM   1999 C C   . ILE B 1 46  ? 14.144 49.798 42.738  1.00 19.94  ? 727  ILE B C   1 
ATOM   2000 O O   . ILE B 1 46  ? 14.654 49.980 41.629  1.00 16.88  ? 727  ILE B O   1 
ATOM   2001 C CB  . ILE B 1 46  ? 15.625 49.423 44.729  1.00 16.14  ? 727  ILE B CB  1 
ATOM   2002 C CG1 . ILE B 1 46  ? 16.844 50.039 44.030  1.00 12.91  ? 727  ILE B CG1 1 
ATOM   2003 C CG2 . ILE B 1 46  ? 16.016 48.420 45.823  1.00 14.52  ? 727  ILE B CG2 1 
ATOM   2004 C CD1 . ILE B 1 46  ? 17.745 50.839 44.960  1.00 11.59  ? 727  ILE B CD1 1 
ATOM   2005 N N   . ASN B 1 47  ? 13.106 50.498 43.186  1.00 13.94  ? 728  ASN B N   1 
ATOM   2006 C CA  . ASN B 1 47  ? 12.497 51.618 42.483  1.00 19.99  ? 728  ASN B CA  1 
ATOM   2007 C C   . ASN B 1 47  ? 12.481 52.830 43.401  1.00 12.23  ? 728  ASN B C   1 
ATOM   2008 O O   . ASN B 1 47  ? 12.800 52.742 44.588  1.00 13.75  ? 728  ASN B O   1 
ATOM   2009 C CB  . ASN B 1 47  ? 11.066 51.282 42.041  1.00 15.18  ? 728  ASN B CB  1 
ATOM   2010 C CG  . ASN B 1 47  ? 11.024 50.470 40.768  1.00 24.43  ? 728  ASN B CG  1 
ATOM   2011 O OD1 . ASN B 1 47  ? 11.940 50.534 39.947  1.00 43.80  ? 728  ASN B OD1 1 
ATOM   2012 N ND2 . ASN B 1 47  ? 9.950  49.708 40.588  1.00 28.56  ? 728  ASN B ND2 1 
ATOM   2013 N N   . ASN B 1 48  ? 12.082 53.973 42.857  1.00 14.92  ? 729  ASN B N   1 
ATOM   2014 C CA  . ASN B 1 48  ? 11.901 55.143 43.700  1.00 14.02  ? 729  ASN B CA  1 
ATOM   2015 C C   . ASN B 1 48  ? 10.644 54.989 44.554  1.00 16.65  ? 729  ASN B C   1 
ATOM   2016 O O   . ASN B 1 48  ? 9.590  54.563 44.072  1.00 14.48  ? 729  ASN B O   1 
ATOM   2017 C CB  . ASN B 1 48  ? 11.813 56.415 42.847  1.00 15.31  ? 729  ASN B CB  1 
ATOM   2018 C CG  . ASN B 1 48  ? 13.051 56.629 41.979  1.00 19.39  ? 729  ASN B CG  1 
ATOM   2019 O OD1 . ASN B 1 48  ? 14.133 56.136 42.294  1.00 28.99  ? 729  ASN B OD1 1 
ATOM   2020 N ND2 . ASN B 1 48  ? 12.894 57.371 40.888  1.00 23.79  ? 729  ASN B ND2 1 
ATOM   2021 N N   . SER B 1 49  ? 10.765 55.337 45.833  1.00 19.15  ? 730  SER B N   1 
ATOM   2022 C CA  . SER B 1 49  ? 9.624  55.324 46.736  1.00 18.21  ? 730  SER B CA  1 
ATOM   2023 C C   . SER B 1 49  ? 8.595  56.372 46.317  1.00 18.47  ? 730  SER B C   1 
ATOM   2024 O O   . SER B 1 49  ? 8.869  57.268 45.513  1.00 16.26  ? 730  SER B O   1 
ATOM   2025 C CB  . SER B 1 49  ? 10.078 55.589 48.169  1.00 19.64  ? 730  SER B CB  1 
ATOM   2026 O OG  . SER B 1 49  ? 10.607 56.897 48.281  1.00 17.27  ? 730  SER B OG  1 
ATOM   2027 N N   . ALA B 1 50  ? 7.394  56.255 46.893  1.00 18.83  ? 731  ALA B N   1 
ATOM   2028 C CA  . ALA B 1 50  ? 6.292  57.137 46.515  1.00 18.05  ? 731  ALA B CA  1 
ATOM   2029 C C   . ALA B 1 50  ? 6.661  58.605 46.692  1.00 18.55  ? 731  ALA B C   1 
ATOM   2030 O O   . ALA B 1 50  ? 6.303  59.444 45.857  1.00 19.12  ? 731  ALA B O   1 
ATOM   2031 C CB  . ALA B 1 50  ? 5.043  56.807 47.335  1.00 19.03  ? 731  ALA B CB  1 
ATOM   2032 N N   . ASP B 1 51  ? 7.365  58.937 47.773  1.00 18.89  ? 732  ASP B N   1 
ATOM   2033 C CA  . ASP B 1 51  ? 7.761  60.313 48.037  1.00 19.17  ? 732  ASP B CA  1 
ATOM   2034 C C   . ASP B 1 51  ? 9.148  60.652 47.494  1.00 18.47  ? 732  ASP B C   1 
ATOM   2035 O O   . ASP B 1 51  ? 9.641  61.758 47.746  1.00 19.07  ? 732  ASP B O   1 
ATOM   2036 C CB  . ASP B 1 51  ? 7.682  60.612 49.540  1.00 20.25  ? 732  ASP B CB  1 
ATOM   2037 C CG  . ASP B 1 51  ? 8.719  59.866 50.366  1.00 19.79  ? 732  ASP B CG  1 
ATOM   2038 O OD1 . ASP B 1 51  ? 9.535  59.095 49.815  1.00 18.12  ? 732  ASP B OD1 1 
ATOM   2039 O OD2 . ASP B 1 51  ? 8.722  60.072 51.596  1.00 30.96  ? 732  ASP B OD2 1 
ATOM   2040 N N   . ASN B 1 52  ? 9.777  59.733 46.761  1.00 17.38  ? 733  ASN B N   1 
ATOM   2041 C CA  . ASN B 1 52  ? 11.059 59.932 46.087  1.00 16.78  ? 733  ASN B CA  1 
ATOM   2042 C C   . ASN B 1 52  ? 12.217 60.138 47.061  1.00 18.07  ? 733  ASN B C   1 
ATOM   2043 O O   . ASN B 1 52  ? 13.304 60.546 46.643  1.00 16.49  ? 733  ASN B O   1 
ATOM   2044 C CB  . ASN B 1 52  ? 10.984 61.106 45.090  1.00 21.44  ? 733  ASN B CB  1 
ATOM   2045 C CG  . ASN B 1 52  ? 12.119 61.094 44.073  1.00 18.78  ? 733  ASN B CG  1 
ATOM   2046 O OD1 . ASN B 1 52  ? 12.244 60.169 43.280  1.00 22.71  ? 733  ASN B OD1 1 
ATOM   2047 N ND2 . ASN B 1 52  ? 12.947 62.143 44.091  1.00 20.27  ? 733  ASN B ND2 1 
ATOM   2048 N N   . SER B 1 53  ? 12.021 59.849 48.350  1.00 16.93  ? 734  SER B N   1 
ATOM   2049 C CA  . SER B 1 53  ? 13.054 60.105 49.345  1.00 17.45  ? 734  SER B CA  1 
ATOM   2050 C C   . SER B 1 53  ? 14.127 59.024 49.377  1.00 18.11  ? 734  SER B C   1 
ATOM   2051 O O   . SER B 1 53  ? 15.225 59.266 49.893  1.00 17.93  ? 734  SER B O   1 
ATOM   2052 C CB  . SER B 1 53  ? 12.427 60.233 50.737  1.00 18.62  ? 734  SER B CB  1 
ATOM   2053 O OG  . SER B 1 53  ? 11.910 58.989 51.184  1.00 18.78  ? 734  SER B OG  1 
ATOM   2054 N N   . THR B 1 54  ? 13.846 57.845 48.836  1.00 17.16  ? 735  THR B N   1 
ATOM   2055 C CA  . THR B 1 54  ? 14.782 56.740 48.944  1.00 14.40  ? 735  THR B CA  1 
ATOM   2056 C C   . THR B 1 54  ? 14.444 55.709 47.883  1.00 17.84  ? 735  THR B C   1 
ATOM   2057 O O   . THR B 1 54  ? 13.328 55.677 47.354  1.00 13.73  ? 735  THR B O   1 
ATOM   2058 C CB  . THR B 1 54  ? 14.740 56.100 50.342  1.00 15.18  ? 735  THR B CB  1 
ATOM   2059 O OG1 . THR B 1 54  ? 15.642 54.983 50.397  1.00 14.33  ? 735  THR B OG1 1 
ATOM   2060 C CG2 . THR B 1 54  ? 13.327 55.623 50.675  1.00 15.53  ? 735  THR B CG2 1 
ATOM   2061 N N   . GLY B 1 55  ? 15.436 54.880 47.567  1.00 17.76  ? 736  GLY B N   1 
ATOM   2062 C CA  . GLY B 1 55  ? 15.153 53.647 46.868  1.00 18.08  ? 736  GLY B CA  1 
ATOM   2063 C C   . GLY B 1 55  ? 14.408 52.680 47.769  1.00 13.64  ? 736  GLY B C   1 
ATOM   2064 O O   . GLY B 1 55  ? 14.547 52.696 48.991  1.00 16.73  ? 736  GLY B O   1 
ATOM   2065 N N   . GLU B 1 56  ? 13.588 51.840 47.147  1.00 15.34  ? 737  GLU B N   1 
ATOM   2066 C CA  . GLU B 1 56  ? 12.714 50.922 47.863  1.00 12.69  ? 737  GLU B CA  1 
ATOM   2067 C C   . GLU B 1 56  ? 12.596 49.649 47.038  1.00 12.04  ? 737  GLU B C   1 
ATOM   2068 O O   . GLU B 1 56  ? 12.562 49.712 45.808  1.00 14.13  ? 737  GLU B O   1 
ATOM   2069 C CB  . GLU B 1 56  ? 11.334 51.555 48.098  1.00 14.16  ? 737  GLU B CB  1 
ATOM   2070 C CG  . GLU B 1 56  ? 10.318 50.625 48.757  1.00 28.71  ? 737  GLU B CG  1 
ATOM   2071 C CD  . GLU B 1 56  ? 8.936  51.244 48.901  1.00 27.16  ? 737  GLU B CD  1 
ATOM   2072 O OE1 . GLU B 1 56  ? 8.839  52.481 49.000  1.00 22.24  ? 737  GLU B OE1 1 
ATOM   2073 O OE2 . GLU B 1 56  ? 7.944  50.486 48.921  1.00 49.95  ? 737  GLU B OE2 1 
ATOM   2074 N N   . PHE B 1 57  ? 12.529 48.499 47.713  1.00 13.03  ? 738  PHE B N   1 
ATOM   2075 C CA  . PHE B 1 57  ? 12.484 47.219 47.008  1.00 17.18  ? 738  PHE B CA  1 
ATOM   2076 C C   . PHE B 1 57  ? 11.191 47.069 46.209  1.00 12.87  ? 738  PHE B C   1 
ATOM   2077 O O   . PHE B 1 57  ? 10.098 47.389 46.692  1.00 16.77  ? 738  PHE B O   1 
ATOM   2078 C CB  . PHE B 1 57  ? 12.630 46.048 47.995  1.00 16.82  ? 738  PHE B CB  1 
ATOM   2079 C CG  . PHE B 1 57  ? 14.058 45.598 48.205  1.00 17.45  ? 738  PHE B CG  1 
ATOM   2080 C CD1 . PHE B 1 57  ? 14.843 46.161 49.200  1.00 20.90  ? 738  PHE B CD1 1 
ATOM   2081 C CD2 . PHE B 1 57  ? 14.611 44.599 47.409  1.00 14.85  ? 738  PHE B CD2 1 
ATOM   2082 C CE1 . PHE B 1 57  ? 16.162 45.749 49.394  1.00 16.18  ? 738  PHE B CE1 1 
ATOM   2083 C CE2 . PHE B 1 57  ? 15.930 44.188 47.595  1.00 22.94  ? 738  PHE B CE2 1 
ATOM   2084 C CZ  . PHE B 1 57  ? 16.705 44.764 48.590  1.00 14.72  ? 738  PHE B CZ  1 
ATOM   2085 N N   . ILE B 1 58  ? 11.330 46.612 44.964  1.00 12.00  ? 739  ILE B N   1 
ATOM   2086 C CA  . ILE B 1 58  ? 10.182 46.189 44.179  1.00 17.54  ? 739  ILE B CA  1 
ATOM   2087 C C   . ILE B 1 58  ? 9.602  44.937 44.817  1.00 15.34  ? 739  ILE B C   1 
ATOM   2088 O O   . ILE B 1 58  ? 10.330 43.989 45.135  1.00 14.80  ? 739  ILE B O   1 
ATOM   2089 C CB  . ILE B 1 58  ? 10.595 45.936 42.721  1.00 16.96  ? 739  ILE B CB  1 
ATOM   2090 C CG1 . ILE B 1 58  ? 11.367 47.138 42.171  1.00 12.51  ? 739  ILE B CG1 1 
ATOM   2091 C CG2 . ILE B 1 58  ? 9.377  45.617 41.863  1.00 16.99  ? 739  ILE B CG2 1 
ATOM   2092 C CD1 . ILE B 1 58  ? 11.941 46.915 40.786  1.00 19.04  ? 739  ILE B CD1 1 
ATOM   2093 N N   . GLY B 1 59  ? 8.295  44.938 45.038  1.00 20.38  ? 740  GLY B N   1 
ATOM   2094 C CA  . GLY B 1 59  ? 7.687  43.832 45.749  1.00 19.85  ? 740  GLY B CA  1 
ATOM   2095 C C   . GLY B 1 59  ? 7.936  43.902 47.247  1.00 18.76  ? 740  GLY B C   1 
ATOM   2096 O O   . GLY B 1 59  ? 8.255  44.949 47.817  1.00 32.33  ? 740  GLY B O   1 
ATOM   2097 N N   . ASP B 1 60  ? 7.782  42.754 47.889  1.00 21.72  ? 741  ASP B N   1 
ATOM   2098 C CA  . ASP B 1 60  ? 7.947  42.614 49.332  1.00 21.61  ? 741  ASP B CA  1 
ATOM   2099 C C   . ASP B 1 60  ? 9.274  41.898 49.565  1.00 24.20  ? 741  ASP B C   1 
ATOM   2100 O O   . ASP B 1 60  ? 9.412  40.717 49.230  1.00 24.72  ? 741  ASP B O   1 
ATOM   2101 C CB  . ASP B 1 60  ? 6.771  41.837 49.923  1.00 24.20  ? 741  ASP B CB  1 
ATOM   2102 C CG  . ASP B 1 60  ? 6.787  41.786 51.445  1.00 30.31  ? 741  ASP B CG  1 
ATOM   2103 O OD1 . ASP B 1 60  ? 7.863  41.945 52.060  1.00 29.90  ? 741  ASP B OD1 1 
ATOM   2104 O OD2 . ASP B 1 60  ? 5.705  41.563 52.032  1.00 37.76  ? 741  ASP B OD2 1 
ATOM   2105 N N   . LYS B 1 61  ? 10.252 42.610 50.137  1.00 22.68  ? 742  LYS B N   1 
ATOM   2106 C CA  . LYS B 1 61  ? 11.608 42.067 50.217  1.00 25.82  ? 742  LYS B CA  1 
ATOM   2107 C C   . LYS B 1 61  ? 11.699 40.823 51.091  1.00 29.08  ? 742  LYS B C   1 
ATOM   2108 O O   . LYS B 1 61  ? 12.680 40.079 50.987  1.00 31.41  ? 742  LYS B O   1 
ATOM   2109 C CB  . LYS B 1 61  ? 12.582 43.124 50.738  1.00 28.58  ? 742  LYS B CB  1 
ATOM   2110 C CG  . LYS B 1 61  ? 12.324 43.522 52.170  1.00 34.60  ? 742  LYS B CG  1 
ATOM   2111 C CD  . LYS B 1 61  ? 13.385 44.453 52.698  1.00 33.87  ? 742  LYS B CD  1 
ATOM   2112 C CE  . LYS B 1 61  ? 13.046 44.861 54.119  1.00 48.66  ? 742  LYS B CE  1 
ATOM   2113 N NZ  . LYS B 1 61  ? 11.688 45.483 54.190  1.00 56.34  ? 742  LYS B NZ  1 
ATOM   2114 N N   . SER B 1 62  ? 10.718 40.579 51.957  1.00 31.04  ? 743  SER B N   1 
ATOM   2115 C CA  . SER B 1 62  ? 10.732 39.346 52.729  1.00 31.39  ? 743  SER B CA  1 
ATOM   2116 C C   . SER B 1 62  ? 10.118 38.181 51.968  1.00 30.59  ? 743  SER B C   1 
ATOM   2117 O O   . SER B 1 62  ? 10.317 37.028 52.365  1.00 44.98  ? 743  SER B O   1 
ATOM   2118 C CB  . SER B 1 62  ? 10.002 39.540 54.060  1.00 40.92  ? 743  SER B CB  1 
ATOM   2119 O OG  . SER B 1 62  ? 8.603  39.657 53.872  1.00 31.10  ? 743  SER B OG  1 
ATOM   2120 N N   . LYS B 1 63  ? 9.386  38.455 50.882  1.00 24.01  ? 744  LYS B N   1 
ATOM   2121 C CA  . LYS B 1 63  ? 8.770  37.418 50.065  1.00 24.75  ? 744  LYS B CA  1 
ATOM   2122 C C   . LYS B 1 63  ? 9.421  37.245 48.700  1.00 20.69  ? 744  LYS B C   1 
ATOM   2123 O O   . LYS B 1 63  ? 9.299  36.162 48.116  1.00 19.95  ? 744  LYS B O   1 
ATOM   2124 C CB  . LYS B 1 63  ? 7.275  37.712 49.858  1.00 23.99  ? 744  LYS B CB  1 
ATOM   2125 C CG  . LYS B 1 63  ? 6.449  37.740 51.132  1.00 29.45  ? 744  LYS B CG  1 
ATOM   2126 C CD  . LYS B 1 63  ? 5.009  38.051 50.807  1.00 40.21  ? 744  LYS B CD  1 
ATOM   2127 C CE  . LYS B 1 63  ? 4.273  38.595 52.013  1.00 45.00  ? 744  LYS B CE  1 
ATOM   2128 N NZ  . LYS B 1 63  ? 2.942  39.136 51.630  1.00 34.12  ? 744  LYS B NZ  1 
ATOM   2129 N N   . ASN B 1 64  ? 10.090 38.274 48.180  1.00 15.94  ? 745  ASN B N   1 
ATOM   2130 C CA  . ASN B 1 64  ? 10.783 38.173 46.898  1.00 14.90  ? 745  ASN B CA  1 
ATOM   2131 C C   . ASN B 1 64  ? 11.830 37.067 46.932  1.00 17.72  ? 745  ASN B C   1 
ATOM   2132 O O   . ASN B 1 64  ? 12.489 36.840 47.949  1.00 19.47  ? 745  ASN B O   1 
ATOM   2133 C CB  . ASN B 1 64  ? 11.488 39.487 46.539  1.00 18.12  ? 745  ASN B CB  1 
ATOM   2134 C CG  . ASN B 1 64  ? 10.544 40.666 46.398  1.00 21.60  ? 745  ASN B CG  1 
ATOM   2135 O OD1 . ASN B 1 64  ? 9.333  40.511 46.233  1.00 16.16  ? 745  ASN B OD1 1 
ATOM   2136 N ND2 . ASN B 1 64  ? 11.112 41.868 46.448  1.00 17.20  ? 745  ASN B ND2 1 
ATOM   2137 N N   . THR B 1 65  ? 11.996 36.395 45.799  1.00 18.84  ? 746  THR B N   1 
ATOM   2138 C CA  . THR B 1 65  ? 13.066 35.427 45.615  1.00 16.66  ? 746  THR B CA  1 
ATOM   2139 C C   . THR B 1 65  ? 13.806 35.733 44.325  1.00 18.52  ? 746  THR B C   1 
ATOM   2140 O O   . THR B 1 65  ? 13.216 36.196 43.345  1.00 13.09  ? 746  THR B O   1 
ATOM   2141 C CB  . THR B 1 65  ? 12.538 33.985 45.583  1.00 19.72  ? 746  THR B CB  1 
ATOM   2142 O OG1 . THR B 1 65  ? 11.532 33.861 44.574  1.00 27.15  ? 746  THR B OG1 1 
ATOM   2143 C CG2 . THR B 1 65  ? 11.963 33.587 46.930  1.00 22.26  ? 746  THR B CG2 1 
ATOM   2144 N N   . TYR B 1 66  ? 15.109 35.486 44.337  1.00 16.63  ? 747  TYR B N   1 
ATOM   2145 C CA  . TYR B 1 66  ? 15.953 35.787 43.199  1.00 16.18  ? 747  TYR B CA  1 
ATOM   2146 C C   . TYR B 1 66  ? 16.853 34.595 42.911  1.00 14.34  ? 747  TYR B C   1 
ATOM   2147 O O   . TYR B 1 66  ? 17.133 33.764 43.781  1.00 15.01  ? 747  TYR B O   1 
ATOM   2148 C CB  . TYR B 1 66  ? 16.807 37.042 43.440  1.00 16.22  ? 747  TYR B CB  1 
ATOM   2149 C CG  . TYR B 1 66  ? 16.090 38.194 44.118  1.00 16.32  ? 747  TYR B CG  1 
ATOM   2150 C CD1 . TYR B 1 66  ? 15.266 39.051 43.400  1.00 19.69  ? 747  TYR B CD1 1 
ATOM   2151 C CD2 . TYR B 1 66  ? 16.264 38.441 45.475  1.00 18.20  ? 747  TYR B CD2 1 
ATOM   2152 C CE1 . TYR B 1 66  ? 14.622 40.122 44.021  1.00 17.90  ? 747  TYR B CE1 1 
ATOM   2153 C CE2 . TYR B 1 66  ? 15.621 39.501 46.105  1.00 20.48  ? 747  TYR B CE2 1 
ATOM   2154 C CZ  . TYR B 1 66  ? 14.804 40.336 45.372  1.00 18.51  ? 747  TYR B CZ  1 
ATOM   2155 O OH  . TYR B 1 66  ? 14.172 41.392 45.993  1.00 17.90  ? 747  TYR B OH  1 
ATOM   2156 N N   . GLU B 1 67  ? 17.305 34.528 41.666  1.00 12.49  ? 748  GLU B N   1 
ATOM   2157 C CA  . GLU B 1 67  ? 18.128 33.431 41.197  1.00 13.89  ? 748  GLU B CA  1 
ATOM   2158 C C   . GLU B 1 67  ? 19.084 33.969 40.146  1.00 18.42  ? 748  GLU B C   1 
ATOM   2159 O O   . GLU B 1 67  ? 18.740 34.891 39.402  1.00 16.95  ? 748  GLU B O   1 
ATOM   2160 C CB  . GLU B 1 67  ? 17.257 32.305 40.621  1.00 15.67  ? 748  GLU B CB  1 
ATOM   2161 C CG  . GLU B 1 67  ? 18.012 31.203 39.908  1.00 25.58  ? 748  GLU B CG  1 
ATOM   2162 C CD  . GLU B 1 67  ? 17.086 30.169 39.305  1.00 35.94  ? 748  GLU B CD  1 
ATOM   2163 O OE1 . GLU B 1 67  ? 16.613 29.293 40.056  1.00 33.04  ? 748  GLU B OE1 1 
ATOM   2164 O OE2 . GLU B 1 67  ? 16.826 30.242 38.084  1.00 38.13  ? 748  GLU B OE2 1 
ATOM   2165 N N   . TRP B 1 68  ? 20.292 33.420 40.122  1.00 12.40  ? 749  TRP B N   1 
ATOM   2166 C CA  . TRP B 1 68  ? 21.246 33.647 39.051  1.00 11.51  ? 749  TRP B CA  1 
ATOM   2167 C C   . TRP B 1 68  ? 21.435 32.357 38.266  1.00 13.97  ? 749  TRP B C   1 
ATOM   2168 O O   . TRP B 1 68  ? 21.245 31.263 38.795  1.00 11.23  ? 749  TRP B O   1 
ATOM   2169 C CB  . TRP B 1 68  ? 22.596 34.125 39.597  1.00 12.20  ? 749  TRP B CB  1 
ATOM   2170 C CG  . TRP B 1 68  ? 23.223 33.152 40.561  1.00 11.96  ? 749  TRP B CG  1 
ATOM   2171 C CD1 . TRP B 1 68  ? 23.075 33.142 41.916  1.00 13.79  ? 749  TRP B CD1 1 
ATOM   2172 C CD2 . TRP B 1 68  ? 24.087 32.049 40.245  1.00 11.45  ? 749  TRP B CD2 1 
ATOM   2173 N NE1 . TRP B 1 68  ? 23.798 32.114 42.465  1.00 10.17  ? 749  TRP B NE1 1 
ATOM   2174 C CE2 . TRP B 1 68  ? 24.428 31.427 41.462  1.00 12.89  ? 749  TRP B CE2 1 
ATOM   2175 C CE3 . TRP B 1 68  ? 24.611 31.533 39.055  1.00 10.23  ? 749  TRP B CE3 1 
ATOM   2176 C CZ2 . TRP B 1 68  ? 25.252 30.306 41.523  1.00 10.75  ? 749  TRP B CZ2 1 
ATOM   2177 C CZ3 . TRP B 1 68  ? 25.435 30.414 39.122  1.00 14.18  ? 749  TRP B CZ3 1 
ATOM   2178 C CH2 . TRP B 1 68  ? 25.748 29.822 40.348  1.00 10.83  ? 749  TRP B CH2 1 
ATOM   2179 N N   . GLN B 1 69  ? 21.844 32.502 37.004  1.00 15.03  ? 750  GLN B N   1 
ATOM   2180 C CA  . GLN B 1 69  ? 22.064 31.375 36.104  1.00 15.26  ? 750  GLN B CA  1 
ATOM   2181 C C   . GLN B 1 69  ? 23.169 31.730 35.121  1.00 12.94  ? 750  GLN B C   1 
ATOM   2182 O O   . GLN B 1 69  ? 23.116 32.792 34.496  1.00 10.79  ? 750  GLN B O   1 
ATOM   2183 C CB  . GLN B 1 69  ? 20.779 31.022 35.349  1.00 19.13  ? 750  GLN B CB  1 
ATOM   2184 C CG  . GLN B 1 69  ? 20.912 29.934 34.287  1.00 14.06  ? 750  GLN B CG  1 
ATOM   2185 C CD  . GLN B 1 69  ? 19.608 29.742 33.528  1.00 17.68  ? 750  GLN B CD  1 
ATOM   2186 O OE1 . GLN B 1 69  ? 18.559 29.559 34.132  1.00 21.92  ? 750  GLN B OE1 1 
ATOM   2187 N NE2 . GLN B 1 69  ? 19.668 29.813 32.202  1.00 19.09  ? 750  GLN B NE2 1 
ATOM   2188 N N   . THR B 1 70  ? 24.156 30.850 34.984  1.00 11.75  ? 751  THR B N   1 
ATOM   2189 C CA  . THR B 1 70  ? 25.302 31.077 34.110  1.00 11.21  ? 751  THR B CA  1 
ATOM   2190 C C   . THR B 1 70  ? 25.259 30.170 32.875  1.00 12.58  ? 751  THR B C   1 
ATOM   2191 O O   . THR B 1 70  ? 24.515 29.180 32.838  1.00 13.05  ? 751  THR B O   1 
ATOM   2192 C CB  . THR B 1 70  ? 26.616 30.862 34.880  1.00 13.44  ? 751  THR B CB  1 
ATOM   2193 O OG1 . THR B 1 70  ? 26.541 29.663 35.661  1.00 15.53  ? 751  THR B OG1 1 
ATOM   2194 C CG2 . THR B 1 70  ? 26.907 32.064 35.788  1.00 13.65  ? 751  THR B CG2 1 
ATOM   2195 N N   . PRO B 1 71  ? 26.033 30.497 31.830  1.00 12.43  ? 752  PRO B N   1 
ATOM   2196 C CA  . PRO B 1 71  ? 25.960 29.708 30.588  1.00 14.07  ? 752  PRO B CA  1 
ATOM   2197 C C   . PRO B 1 71  ? 26.336 28.241 30.752  1.00 19.95  ? 752  PRO B C   1 
ATOM   2198 O O   . PRO B 1 71  ? 25.848 27.404 29.980  1.00 17.00  ? 752  PRO B O   1 
ATOM   2199 C CB  . PRO B 1 71  ? 26.937 30.439 29.657  1.00 15.17  ? 752  PRO B CB  1 
ATOM   2200 C CG  . PRO B 1 71  ? 26.913 31.868 30.149  1.00 13.90  ? 752  PRO B CG  1 
ATOM   2201 C CD  . PRO B 1 71  ? 26.784 31.757 31.637  1.00 14.35  ? 752  PRO B CD  1 
ATOM   2202 N N   . ASP B 1 72  ? 27.184 27.898 31.722  1.00 15.26  ? 753  ASP B N   1 
ATOM   2203 C CA  . ASP B 1 72  ? 27.484 26.485 31.957  1.00 16.53  ? 753  ASP B CA  1 
ATOM   2204 C C   . ASP B 1 72  ? 26.316 25.718 32.564  1.00 15.12  ? 753  ASP B C   1 
ATOM   2205 O O   . ASP B 1 72  ? 26.446 24.511 32.803  1.00 16.29  ? 753  ASP B O   1 
ATOM   2206 C CB  . ASP B 1 72  ? 28.713 26.344 32.857  1.00 15.85  ? 753  ASP B CB  1 
ATOM   2207 C CG  . ASP B 1 72  ? 28.524 26.979 34.222  1.00 18.10  ? 753  ASP B CG  1 
ATOM   2208 O OD1 . ASP B 1 72  ? 27.416 27.456 34.529  1.00 17.47  ? 753  ASP B OD1 1 
ATOM   2209 O OD2 . ASP B 1 72  ? 29.505 27.020 34.994  1.00 22.74  ? 753  ASP B OD2 1 
ATOM   2210 N N   . GLY B 1 73  ? 25.191 26.374 32.828  1.00 18.52  ? 754  GLY B N   1 
ATOM   2211 C CA  . GLY B 1 73  ? 24.022 25.719 33.366  1.00 19.05  ? 754  GLY B CA  1 
ATOM   2212 C C   . GLY B 1 73  ? 23.883 25.793 34.872  1.00 22.53  ? 754  GLY B C   1 
ATOM   2213 O O   . GLY B 1 73  ? 22.830 25.403 35.396  1.00 25.60  ? 754  GLY B O   1 
ATOM   2214 N N   . GLN B 1 74  ? 24.900 26.281 35.579  1.00 15.15  ? 755  GLN B N   1 
ATOM   2215 C CA  . GLN B 1 74  ? 24.819 26.378 37.028  1.00 18.13  ? 755  GLN B CA  1 
ATOM   2216 C C   . GLN B 1 74  ? 23.860 27.496 37.428  1.00 17.93  ? 755  GLN B C   1 
ATOM   2217 O O   . GLN B 1 74  ? 23.734 28.513 36.741  1.00 13.43  ? 755  GLN B O   1 
ATOM   2218 C CB  . GLN B 1 74  ? 26.206 26.631 37.624  1.00 16.78  ? 755  GLN B CB  1 
ATOM   2219 C CG  . GLN B 1 74  ? 26.268 26.567 39.153  1.00 36.48  ? 755  GLN B CG  1 
ATOM   2220 C CD  . GLN B 1 74  ? 27.699 26.551 39.697  1.00 25.40  ? 755  GLN B CD  1 
ATOM   2221 O OE1 . GLN B 1 74  ? 28.658 26.336 38.955  1.00 38.18  ? 755  GLN B OE1 1 
ATOM   2222 N NE2 . GLN B 1 74  ? 27.839 26.768 41.001  1.00 30.79  ? 755  GLN B NE2 1 
ATOM   2223 N N   . LYS B 1 75  ? 23.169 27.293 38.546  1.00 16.28  ? 756  LYS B N   1 
ATOM   2224 C CA  . LYS B 1 75  ? 22.267 28.313 39.058  1.00 21.31  ? 756  LYS B CA  1 
ATOM   2225 C C   . LYS B 1 75  ? 22.319 28.305 40.579  1.00 24.27  ? 756  LYS B C   1 
ATOM   2226 O O   . LYS B 1 75  ? 22.771 27.342 41.200  1.00 17.89  ? 756  LYS B O   1 
ATOM   2227 C CB  . LYS B 1 75  ? 20.830 28.095 38.555  1.00 19.37  ? 756  LYS B CB  1 
ATOM   2228 C CG  . LYS B 1 75  ? 20.248 26.738 38.879  1.00 30.84  ? 756  LYS B CG  1 
ATOM   2229 C CD  . LYS B 1 75  ? 18.839 26.587 38.305  1.00 35.73  ? 756  LYS B CD  1 
ATOM   2230 C CE  . LYS B 1 75  ? 18.812 26.959 36.829  1.00 36.92  ? 756  LYS B CE  1 
ATOM   2231 N NZ  . LYS B 1 75  ? 17.543 26.565 36.156  1.00 29.84  ? 756  LYS B NZ  1 
ATOM   2232 N N   . GLY B 1 76  ? 21.862 29.404 41.171  1.00 12.72  ? 757  GLY B N   1 
ATOM   2233 C CA  . GLY B 1 76  ? 21.777 29.510 42.616  1.00 17.08  ? 757  GLY B CA  1 
ATOM   2234 C C   . GLY B 1 76  ? 20.815 30.614 42.986  1.00 19.74  ? 757  GLY B C   1 
ATOM   2235 O O   . GLY B 1 76  ? 20.453 31.449 42.151  1.00 14.99  ? 757  GLY B O   1 
ATOM   2236 N N   . SER B 1 77  ? 20.393 30.607 44.248  1.00 22.31  ? 758  SER B N   1 
ATOM   2237 C CA  . SER B 1 77  ? 19.427 31.572 44.758  1.00 15.52  ? 758  SER B CA  1 
ATOM   2238 C C   . SER B 1 77  ? 20.095 32.578 45.688  1.00 18.21  ? 758  SER B C   1 
ATOM   2239 O O   . SER B 1 77  ? 21.197 32.356 46.198  1.00 14.89  ? 758  SER B O   1 
ATOM   2240 C CB  . SER B 1 77  ? 18.292 30.869 45.510  1.00 22.37  ? 758  SER B CB  1 
ATOM   2241 O OG  . SER B 1 77  ? 17.571 29.998 44.662  1.00 27.78  ? 758  SER B OG  1 
ATOM   2242 N N   . PHE B 1 78  ? 19.402 33.700 45.891  1.00 14.54  ? 759  PHE B N   1 
ATOM   2243 C CA  . PHE B 1 78  ? 19.760 34.686 46.904  1.00 13.74  ? 759  PHE B CA  1 
ATOM   2244 C C   . PHE B 1 78  ? 18.506 35.474 47.264  1.00 18.09  ? 759  PHE B C   1 
ATOM   2245 O O   . PHE B 1 78  ? 17.476 35.387 46.591  1.00 12.54  ? 759  PHE B O   1 
ATOM   2246 C CB  . PHE B 1 78  ? 20.902 35.609 46.441  1.00 13.65  ? 759  PHE B CB  1 
ATOM   2247 C CG  . PHE B 1 78  ? 20.610 36.393 45.180  1.00 11.66  ? 759  PHE B CG  1 
ATOM   2248 C CD1 . PHE B 1 78  ? 20.753 35.807 43.929  1.00 11.87  ? 759  PHE B CD1 1 
ATOM   2249 C CD2 . PHE B 1 78  ? 20.238 37.734 45.244  1.00 12.57  ? 759  PHE B CD2 1 
ATOM   2250 C CE1 . PHE B 1 78  ? 20.510 36.537 42.769  1.00 13.90  ? 759  PHE B CE1 1 
ATOM   2251 C CE2 . PHE B 1 78  ? 19.996 38.465 44.092  1.00 9.38   ? 759  PHE B CE2 1 
ATOM   2252 C CZ  . PHE B 1 78  ? 20.127 37.870 42.855  1.00 12.28  ? 759  PHE B CZ  1 
ATOM   2253 N N   . THR B 1 79  ? 18.590 36.222 48.356  1.00 17.90  ? 760  THR B N   1 
ATOM   2254 C CA  . THR B 1 79  ? 17.472 37.033 48.816  1.00 18.25  ? 760  THR B CA  1 
ATOM   2255 C C   . THR B 1 79  ? 17.908 38.490 48.908  1.00 16.62  ? 760  THR B C   1 
ATOM   2256 O O   . THR B 1 79  ? 19.044 38.846 48.583  1.00 15.11  ? 760  THR B O   1 
ATOM   2257 C CB  . THR B 1 79  ? 16.940 36.536 50.164  1.00 20.74  ? 760  THR B CB  1 
ATOM   2258 O OG1 . THR B 1 79  ? 17.906 36.802 51.188  1.00 26.00  ? 760  THR B OG1 1 
ATOM   2259 C CG2 . THR B 1 79  ? 16.652 35.049 50.111  1.00 27.27  ? 760  THR B CG2 1 
ATOM   2260 N N   . SER B 1 80  ? 16.985 39.342 49.360  1.00 19.77  ? 761  SER B N   1 
ATOM   2261 C CA  . SER B 1 80  ? 17.294 40.764 49.454  1.00 19.70  ? 761  SER B CA  1 
ATOM   2262 C C   . SER B 1 80  ? 18.427 41.025 50.442  1.00 15.39  ? 761  SER B C   1 
ATOM   2263 O O   . SER B 1 80  ? 19.189 41.990 50.278  1.00 11.17  ? 761  SER B O   1 
ATOM   2264 C CB  . SER B 1 80  ? 16.032 41.544 49.837  1.00 18.61  ? 761  SER B CB  1 
ATOM   2265 O OG  . SER B 1 80  ? 15.519 41.138 51.093  1.00 30.36  ? 761  SER B OG  1 
ATOM   2266 N N   . GLU B 1 81  ? 18.580 40.154 51.445  1.00 14.31  ? 762  GLU B N   1 
ATOM   2267 C CA  . GLU B 1 81  ? 19.638 40.304 52.440  1.00 16.45  ? 762  GLU B CA  1 
ATOM   2268 C C   . GLU B 1 81  ? 21.032 40.191 51.845  1.00 16.17  ? 762  GLU B C   1 
ATOM   2269 O O   . GLU B 1 81  ? 21.999 40.610 52.489  1.00 20.08  ? 762  GLU B O   1 
ATOM   2270 C CB  . GLU B 1 81  ? 19.472 39.254 53.531  1.00 14.34  ? 762  GLU B CB  1 
ATOM   2271 C CG  . GLU B 1 81  ? 18.096 39.296 54.160  1.00 21.73  ? 762  GLU B CG  1 
ATOM   2272 C CD  . GLU B 1 81  ? 17.935 38.311 55.289  1.00 31.79  ? 762  GLU B CD  1 
ATOM   2273 O OE1 . GLU B 1 81  ? 18.519 37.202 55.213  1.00 28.41  ? 762  GLU B OE1 1 
ATOM   2274 O OE2 . GLU B 1 81  ? 17.221 38.658 56.253  1.00 22.36  ? 762  GLU B OE2 1 
ATOM   2275 N N   . ASP B 1 82  ? 21.161 39.604 50.657  1.00 17.24  ? 763  ASP B N   1 
ATOM   2276 C CA  . ASP B 1 82  ? 22.451 39.401 50.011  1.00 13.21  ? 763  ASP B CA  1 
ATOM   2277 C C   . ASP B 1 82  ? 22.826 40.535 49.074  1.00 17.04  ? 763  ASP B C   1 
ATOM   2278 O O   . ASP B 1 82  ? 23.892 40.472 48.453  1.00 11.24  ? 763  ASP B O   1 
ATOM   2279 C CB  . ASP B 1 82  ? 22.448 38.091 49.217  1.00 13.39  ? 763  ASP B CB  1 
ATOM   2280 C CG  . ASP B 1 82  ? 22.142 36.889 50.078  1.00 20.36  ? 763  ASP B CG  1 
ATOM   2281 O OD1 . ASP B 1 82  ? 22.743 36.768 51.164  1.00 19.09  ? 763  ASP B OD1 1 
ATOM   2282 O OD2 . ASP B 1 82  ? 21.295 36.066 49.667  1.00 17.05  ? 763  ASP B OD2 1 
ATOM   2283 N N   . ILE B 1 83  ? 21.979 41.556 48.947  1.00 11.12  ? 764  ILE B N   1 
ATOM   2284 C CA  . ILE B 1 83  ? 22.174 42.627 47.977  1.00 16.33  ? 764  ILE B CA  1 
ATOM   2285 C C   . ILE B 1 83  ? 22.684 43.861 48.701  1.00 15.18  ? 764  ILE B C   1 
ATOM   2286 O O   . ILE B 1 83  ? 22.130 44.266 49.732  1.00 12.78  ? 764  ILE B O   1 
ATOM   2287 C CB  . ILE B 1 83  ? 20.876 42.936 47.214  1.00 13.21  ? 764  ILE B CB  1 
ATOM   2288 C CG1 . ILE B 1 83  ? 20.244 41.640 46.702  1.00 13.76  ? 764  ILE B CG1 1 
ATOM   2289 C CG2 . ILE B 1 83  ? 21.163 43.865 46.052  1.00 13.26  ? 764  ILE B CG2 1 
ATOM   2290 C CD1 . ILE B 1 83  ? 18.909 41.842 46.023  1.00 12.32  ? 764  ILE B CD1 1 
ATOM   2291 N N   . HIS B 1 84  ? 23.745 44.453 48.166  1.00 14.41  ? 765  HIS B N   1 
ATOM   2292 C CA  . HIS B 1 84  ? 24.381 45.626 48.748  1.00 16.43  ? 765  HIS B CA  1 
ATOM   2293 C C   . HIS B 1 84  ? 24.326 46.745 47.727  1.00 14.08  ? 765  HIS B C   1 
ATOM   2294 O O   . HIS B 1 84  ? 24.913 46.633 46.645  1.00 15.90  ? 765  HIS B O   1 
ATOM   2295 C CB  . HIS B 1 84  ? 25.827 45.319 49.148  1.00 13.15  ? 765  HIS B CB  1 
ATOM   2296 C CG  . HIS B 1 84  ? 25.951 44.119 50.027  1.00 16.41  ? 765  HIS B CG  1 
ATOM   2297 N ND1 . HIS B 1 84  ? 25.878 44.194 51.401  1.00 19.96  ? 765  HIS B ND1 1 
ATOM   2298 C CD2 . HIS B 1 84  ? 26.111 42.807 49.729  1.00 17.54  ? 765  HIS B CD2 1 
ATOM   2299 C CE1 . HIS B 1 84  ? 26.001 42.982 51.913  1.00 24.53  ? 765  HIS B CE1 1 
ATOM   2300 N NE2 . HIS B 1 84  ? 26.141 42.123 50.919  1.00 19.89  ? 765  HIS B NE2 1 
ATOM   2301 N N   . PHE B 1 85  ? 23.614 47.815 48.063  1.00 14.22  ? 766  PHE B N   1 
ATOM   2302 C CA  . PHE B 1 85  ? 23.432 48.921 47.144  1.00 15.07  ? 766  PHE B CA  1 
ATOM   2303 C C   . PHE B 1 85  ? 24.511 49.967 47.377  1.00 13.91  ? 766  PHE B C   1 
ATOM   2304 O O   . PHE B 1 85  ? 24.889 50.248 48.519  1.00 13.85  ? 766  PHE B O   1 
ATOM   2305 C CB  . PHE B 1 85  ? 22.037 49.523 47.314  1.00 11.61  ? 766  PHE B CB  1 
ATOM   2306 C CG  . PHE B 1 85  ? 20.936 48.524 47.090  1.00 10.57  ? 766  PHE B CG  1 
ATOM   2307 C CD1 . PHE B 1 85  ? 20.540 48.187 45.804  1.00 12.42  ? 766  PHE B CD1 1 
ATOM   2308 C CD2 . PHE B 1 85  ? 20.340 47.878 48.158  1.00 11.00  ? 766  PHE B CD2 1 
ATOM   2309 C CE1 . PHE B 1 85  ? 19.548 47.242 45.591  1.00 16.53  ? 766  PHE B CE1 1 
ATOM   2310 C CE2 . PHE B 1 85  ? 19.340 46.935 47.950  1.00 18.17  ? 766  PHE B CE2 1 
ATOM   2311 C CZ  . PHE B 1 85  ? 18.947 46.618 46.666  1.00 15.43  ? 766  PHE B CZ  1 
ATOM   2312 N N   . TYR B 1 86  ? 25.030 50.513 46.279  1.00 13.56  ? 767  TYR B N   1 
ATOM   2313 C CA  . TYR B 1 86  ? 26.028 51.574 46.386  1.00 18.48  ? 767  TYR B CA  1 
ATOM   2314 C C   . TYR B 1 86  ? 25.498 52.727 47.233  1.00 14.02  ? 767  TYR B C   1 
ATOM   2315 O O   . TYR B 1 86  ? 26.185 53.224 48.131  1.00 12.11  ? 767  TYR B O   1 
ATOM   2316 C CB  . TYR B 1 86  ? 26.426 52.049 44.984  1.00 13.95  ? 767  TYR B CB  1 
ATOM   2317 C CG  . TYR B 1 86  ? 27.444 53.179 44.946  1.00 12.48  ? 767  TYR B CG  1 
ATOM   2318 C CD1 . TYR B 1 86  ? 28.711 53.020 45.498  1.00 15.27  ? 767  TYR B CD1 1 
ATOM   2319 C CD2 . TYR B 1 86  ? 27.142 54.388 44.330  1.00 16.20  ? 767  TYR B CD2 1 
ATOM   2320 C CE1 . TYR B 1 86  ? 29.643 54.042 45.449  1.00 13.35  ? 767  TYR B CE1 1 
ATOM   2321 C CE2 . TYR B 1 86  ? 28.068 55.420 44.278  1.00 23.62  ? 767  TYR B CE2 1 
ATOM   2322 C CZ  . TYR B 1 86  ? 29.317 55.242 44.840  1.00 17.61  ? 767  TYR B CZ  1 
ATOM   2323 O OH  . TYR B 1 86  ? 30.238 56.266 44.788  1.00 24.63  ? 767  TYR B OH  1 
ATOM   2324 N N   . ASN B 1 87  ? 24.250 53.132 46.993  1.00 17.40  ? 768  ASN B N   1 
ATOM   2325 C CA  . ASN B 1 87  ? 23.653 54.215 47.770  1.00 11.96  ? 768  ASN B CA  1 
ATOM   2326 C C   . ASN B 1 87  ? 22.135 54.102 47.589  1.00 13.69  ? 768  ASN B C   1 
ATOM   2327 O O   . ASN B 1 87  ? 21.563 54.748 46.712  1.00 15.17  ? 768  ASN B O   1 
ATOM   2328 C CB  . ASN B 1 87  ? 24.172 55.571 47.330  1.00 17.57  ? 768  ASN B CB  1 
ATOM   2329 C CG  . ASN B 1 87  ? 23.813 56.676 48.306  1.00 22.69  ? 768  ASN B CG  1 
ATOM   2330 O OD1 . ASN B 1 87  ? 22.837 56.577 49.055  1.00 21.90  ? 768  ASN B OD1 1 
ATOM   2331 N ND2 . ASN B 1 87  ? 24.601 57.749 48.293  1.00 22.59  ? 768  ASN B ND2 1 
ATOM   2332 N N   . LYS B 1 88  ? 21.507 53.266 48.422  1.00 16.20  ? 769  LYS B N   1 
ATOM   2333 C CA  . LYS B 1 88  ? 20.069 53.043 48.299  1.00 15.80  ? 769  LYS B CA  1 
ATOM   2334 C C   . LYS B 1 88  ? 19.280 54.309 48.596  1.00 14.11  ? 769  LYS B C   1 
ATOM   2335 O O   . LYS B 1 88  ? 18.253 54.570 47.961  1.00 16.18  ? 769  LYS B O   1 
ATOM   2336 C CB  . LYS B 1 88  ? 19.630 51.921 49.235  1.00 18.41  ? 769  LYS B CB  1 
ATOM   2337 C CG  . LYS B 1 88  ? 18.134 51.633 49.194  1.00 19.85  ? 769  LYS B CG  1 
ATOM   2338 C CD  . LYS B 1 88  ? 17.786 50.446 50.083  1.00 25.87  ? 769  LYS B CD  1 
ATOM   2339 C CE  . LYS B 1 88  ? 16.288 50.180 50.108  1.00 31.99  ? 769  LYS B CE  1 
ATOM   2340 N NZ  . LYS B 1 88  ? 15.950 49.079 51.056  1.00 44.42  ? 769  LYS B NZ  1 
ATOM   2341 N N   . LYS B 1 89  ? 19.732 55.089 49.579  1.00 18.52  ? 770  LYS B N   1 
ATOM   2342 C CA  . LYS B 1 89  ? 19.019 56.307 49.952  1.00 17.04  ? 770  LYS B CA  1 
ATOM   2343 C C   . LYS B 1 89  ? 19.021 57.322 48.818  1.00 21.57  ? 770  LYS B C   1 
ATOM   2344 O O   . LYS B 1 89  ? 18.001 57.973 48.552  1.00 21.02  ? 770  LYS B O   1 
ATOM   2345 C CB  . LYS B 1 89  ? 19.643 56.909 51.212  1.00 18.61  ? 770  LYS B CB  1 
ATOM   2346 C CG  . LYS B 1 89  ? 19.059 58.257 51.622  1.00 23.47  ? 770  LYS B CG  1 
ATOM   2347 C CD  . LYS B 1 89  ? 17.596 58.142 52.018  1.00 29.15  ? 770  LYS B CD  1 
ATOM   2348 C CE  . LYS B 1 89  ? 17.016 59.488 52.448  1.00 27.02  ? 770  LYS B CE  1 
ATOM   2349 N NZ  . LYS B 1 89  ? 16.944 60.460 51.318  1.00 28.87  ? 770  LYS B NZ  1 
ATOM   2350 N N   . ASP B 1 90  ? 20.155 57.477 48.139  1.00 17.68  ? 771  ASP B N   1 
ATOM   2351 C CA  . ASP B 1 90  ? 20.276 58.442 47.055  1.00 16.42  ? 771  ASP B CA  1 
ATOM   2352 C C   . ASP B 1 90  ? 19.991 57.828 45.696  1.00 19.26  ? 771  ASP B C   1 
ATOM   2353 O O   . ASP B 1 90  ? 20.209 58.487 44.673  1.00 16.21  ? 771  ASP B O   1 
ATOM   2354 C CB  . ASP B 1 90  ? 21.672 59.076 47.054  1.00 22.07  ? 771  ASP B CB  1 
ATOM   2355 C CG  . ASP B 1 90  ? 21.867 60.069 48.184  1.00 22.33  ? 771  ASP B CG  1 
ATOM   2356 O OD1 . ASP B 1 90  ? 20.881 60.713 48.603  1.00 24.64  ? 771  ASP B OD1 1 
ATOM   2357 O OD2 . ASP B 1 90  ? 23.017 60.213 48.646  1.00 35.68  ? 771  ASP B OD2 1 
ATOM   2358 N N   . TYR B 1 91  ? 19.509 56.586 45.665  1.00 17.67  ? 772  TYR B N   1 
ATOM   2359 C CA  . TYR B 1 91  ? 19.128 55.961 44.402  1.00 16.92  ? 772  TYR B CA  1 
ATOM   2360 C C   . TYR B 1 91  ? 18.222 56.830 43.534  1.00 19.09  ? 772  TYR B C   1 
ATOM   2361 O O   . TYR B 1 91  ? 18.428 56.839 42.308  1.00 15.78  ? 772  TYR B O   1 
ATOM   2362 C CB  . TYR B 1 91  ? 18.469 54.596 44.663  1.00 19.22  ? 772  TYR B CB  1 
ATOM   2363 C CG  . TYR B 1 91  ? 17.841 54.031 43.412  1.00 16.87  ? 772  TYR B CG  1 
ATOM   2364 C CD1 . TYR B 1 91  ? 18.624 53.438 42.428  1.00 17.77  ? 772  TYR B CD1 1 
ATOM   2365 C CD2 . TYR B 1 91  ? 16.467 54.110 43.203  1.00 16.96  ? 772  TYR B CD2 1 
ATOM   2366 C CE1 . TYR B 1 91  ? 18.065 52.949 41.266  1.00 15.81  ? 772  TYR B CE1 1 
ATOM   2367 C CE2 . TYR B 1 91  ? 15.897 53.611 42.051  1.00 19.04  ? 772  TYR B CE2 1 
ATOM   2368 C CZ  . TYR B 1 91  ? 16.697 53.032 41.085  1.00 19.46  ? 772  TYR B CZ  1 
ATOM   2369 O OH  . TYR B 1 91  ? 16.125 52.545 39.933  1.00 20.79  ? 772  TYR B OH  1 
ATOM   2370 N N   . PRO B 1 92  ? 17.232 57.567 44.064  1.00 16.11  ? 773  PRO B N   1 
ATOM   2371 C CA  . PRO B 1 92  ? 16.407 58.416 43.185  1.00 21.89  ? 773  PRO B CA  1 
ATOM   2372 C C   . PRO B 1 92  ? 17.171 59.538 42.501  1.00 25.65  ? 773  PRO B C   1 
ATOM   2373 O O   . PRO B 1 92  ? 16.678 60.072 41.497  1.00 18.67  ? 773  PRO B O   1 
ATOM   2374 C CB  . PRO B 1 92  ? 15.346 58.985 44.137  1.00 14.44  ? 773  PRO B CB  1 
ATOM   2375 C CG  . PRO B 1 92  ? 15.272 58.016 45.248  1.00 15.52  ? 773  PRO B CG  1 
ATOM   2376 C CD  . PRO B 1 92  ? 16.683 57.538 45.434  1.00 18.60  ? 773  PRO B CD  1 
ATOM   2377 N N   . LYS B 1 93  ? 18.348 59.922 43.010  1.00 23.30  ? 774  LYS B N   1 
ATOM   2378 C CA  . LYS B 1 93  ? 19.055 61.074 42.459  1.00 18.37  ? 774  LYS B CA  1 
ATOM   2379 C C   . LYS B 1 93  ? 19.652 60.789 41.084  1.00 31.58  ? 774  LYS B C   1 
ATOM   2380 O O   . LYS B 1 93  ? 19.951 61.736 40.350  1.00 38.96  ? 774  LYS B O   1 
ATOM   2381 C CB  . LYS B 1 93  ? 20.139 61.543 43.429  1.00 26.01  ? 774  LYS B CB  1 
ATOM   2382 C CG  . LYS B 1 93  ? 19.582 62.095 44.733  1.00 17.48  ? 774  LYS B CG  1 
ATOM   2383 C CD  . LYS B 1 93  ? 20.665 62.716 45.596  1.00 30.12  ? 774  LYS B CD  1 
ATOM   2384 C CE  . LYS B 1 93  ? 20.083 63.285 46.881  1.00 27.52  ? 774  LYS B CE  1 
ATOM   2385 N NZ  . LYS B 1 93  ? 19.233 62.290 47.597  1.00 31.22  ? 774  LYS B NZ  1 
ATOM   2386 N N   . GLY B 1 94  ? 19.846 59.521 40.720  1.00 28.32  ? 775  GLY B N   1 
ATOM   2387 C CA  . GLY B 1 94  ? 19.957 59.191 39.318  1.00 29.13  ? 775  GLY B CA  1 
ATOM   2388 C C   . GLY B 1 94  ? 21.057 58.192 39.017  1.00 25.21  ? 775  GLY B C   1 
ATOM   2389 O O   . GLY B 1 94  ? 21.525 57.453 39.883  1.00 20.19  ? 775  GLY B O   1 
ATOM   2390 N N   . PHE B 1 95  ? 21.423 58.204 37.737  1.00 18.71  ? 776  PHE B N   1 
ATOM   2391 C CA  . PHE B 1 95  ? 22.413 57.369 37.065  1.00 24.97  ? 776  PHE B CA  1 
ATOM   2392 C C   . PHE B 1 95  ? 23.569 56.879 37.939  1.00 26.25  ? 776  PHE B C   1 
ATOM   2393 O O   . PHE B 1 95  ? 23.861 55.677 37.967  1.00 25.72  ? 776  PHE B O   1 
ATOM   2394 C CB  . PHE B 1 95  ? 22.948 58.177 35.878  1.00 33.60  ? 776  PHE B CB  1 
ATOM   2395 C CG  . PHE B 1 95  ? 23.862 57.422 34.974  1.00 39.97  ? 776  PHE B CG  1 
ATOM   2396 C CD1 . PHE B 1 95  ? 23.353 56.662 33.936  1.00 39.38  ? 776  PHE B CD1 1 
ATOM   2397 C CD2 . PHE B 1 95  ? 25.236 57.504 35.134  1.00 38.94  ? 776  PHE B CD2 1 
ATOM   2398 C CE1 . PHE B 1 95  ? 24.195 55.985 33.085  1.00 32.24  ? 776  PHE B CE1 1 
ATOM   2399 C CE2 . PHE B 1 95  ? 26.084 56.818 34.293  1.00 32.58  ? 776  PHE B CE2 1 
ATOM   2400 C CZ  . PHE B 1 95  ? 25.562 56.055 33.269  1.00 27.93  ? 776  PHE B CZ  1 
ATOM   2401 N N   . ILE B 1 96  ? 24.234 57.791 38.654  1.00 18.18  ? 777  ILE B N   1 
ATOM   2402 C CA  . ILE B 1 96  ? 25.495 57.436 39.299  1.00 25.50  ? 777  ILE B CA  1 
ATOM   2403 C C   . ILE B 1 96  ? 25.320 56.459 40.455  1.00 27.45  ? 777  ILE B C   1 
ATOM   2404 O O   . ILE B 1 96  ? 26.299 55.831 40.875  1.00 23.97  ? 777  ILE B O   1 
ATOM   2405 C CB  . ILE B 1 96  ? 26.234 58.693 39.785  1.00 27.06  ? 777  ILE B CB  1 
ATOM   2406 C CG1 . ILE B 1 96  ? 25.435 59.414 40.868  1.00 25.20  ? 777  ILE B CG1 1 
ATOM   2407 C CG2 . ILE B 1 96  ? 26.481 59.635 38.630  1.00 25.37  ? 777  ILE B CG2 1 
ATOM   2408 C CD1 . ILE B 1 96  ? 26.233 60.470 41.580  1.00 35.19  ? 777  ILE B CD1 1 
ATOM   2409 N N   . TYR B 1 97  ? 24.109 56.305 40.986  1.00 18.19  ? 778  TYR B N   1 
ATOM   2410 C CA  . TYR B 1 97  ? 23.880 55.423 42.123  1.00 19.91  ? 778  TYR B CA  1 
ATOM   2411 C C   . TYR B 1 97  ? 23.238 54.096 41.732  1.00 18.12  ? 778  TYR B C   1 
ATOM   2412 O O   . TYR B 1 97  ? 22.876 53.310 42.614  1.00 18.64  ? 778  TYR B O   1 
ATOM   2413 C CB  . TYR B 1 97  ? 23.028 56.143 43.173  1.00 13.97  ? 778  TYR B CB  1 
ATOM   2414 C CG  . TYR B 1 97  ? 23.659 57.422 43.680  1.00 21.59  ? 778  TYR B CG  1 
ATOM   2415 C CD1 . TYR B 1 97  ? 24.856 57.394 44.389  1.00 21.74  ? 778  TYR B CD1 1 
ATOM   2416 C CD2 . TYR B 1 97  ? 23.065 58.657 43.444  1.00 22.56  ? 778  TYR B CD2 1 
ATOM   2417 C CE1 . TYR B 1 97  ? 25.440 58.555 44.854  1.00 27.14  ? 778  TYR B CE1 1 
ATOM   2418 C CE2 . TYR B 1 97  ? 23.646 59.832 43.906  1.00 29.94  ? 778  TYR B CE2 1 
ATOM   2419 C CZ  . TYR B 1 97  ? 24.833 59.772 44.610  1.00 21.67  ? 778  TYR B CZ  1 
ATOM   2420 O OH  . TYR B 1 97  ? 25.413 60.931 45.074  1.00 33.40  ? 778  TYR B OH  1 
ATOM   2421 N N   . ASP B 1 98  ? 23.108 53.811 40.436  1.00 12.56  ? 779  ASP B N   1 
ATOM   2422 C CA  . ASP B 1 98  ? 22.382 52.625 39.989  1.00 18.22  ? 779  ASP B CA  1 
ATOM   2423 C C   . ASP B 1 98  ? 23.362 51.456 39.912  1.00 12.02  ? 779  ASP B C   1 
ATOM   2424 O O   . ASP B 1 98  ? 23.808 51.034 38.845  1.00 13.80  ? 779  ASP B O   1 
ATOM   2425 C CB  . ASP B 1 98  ? 21.697 52.883 38.656  1.00 16.77  ? 779  ASP B CB  1 
ATOM   2426 C CG  . ASP B 1 98  ? 20.781 51.744 38.249  1.00 20.11  ? 779  ASP B CG  1 
ATOM   2427 O OD1 . ASP B 1 98  ? 20.585 50.821 39.066  1.00 15.12  ? 779  ASP B OD1 1 
ATOM   2428 O OD2 . ASP B 1 98  ? 20.255 51.779 37.118  1.00 23.70  ? 779  ASP B OD2 1 
ATOM   2429 N N   . LEU B 1 99  ? 23.669 50.902 41.079  1.00 11.04  ? 780  LEU B N   1 
ATOM   2430 C CA  . LEU B 1 99  ? 24.815 50.015 41.187  1.00 11.07  ? 780  LEU B CA  1 
ATOM   2431 C C   . LEU B 1 99  ? 24.674 49.164 42.437  1.00 9.27   ? 780  LEU B C   1 
ATOM   2432 O O   . LEU B 1 99  ? 24.413 49.696 43.521  1.00 13.62  ? 780  LEU B O   1 
ATOM   2433 C CB  . LEU B 1 99  ? 26.103 50.843 41.232  1.00 12.10  ? 780  LEU B CB  1 
ATOM   2434 C CG  . LEU B 1 99  ? 27.369 50.088 41.615  1.00 15.74  ? 780  LEU B CG  1 
ATOM   2435 C CD1 . LEU B 1 99  ? 27.613 48.984 40.611  1.00 15.16  ? 780  LEU B CD1 1 
ATOM   2436 C CD2 . LEU B 1 99  ? 28.557 51.034 41.667  1.00 10.05  ? 780  LEU B CD2 1 
ATOM   2437 N N   . ALA B 1 100 ? 24.861 47.853 42.292  1.00 8.01   ? 781  ALA B N   1 
ATOM   2438 C CA  . ALA B 1 100 ? 24.671 46.956 43.420  1.00 12.09  ? 781  ALA B CA  1 
ATOM   2439 C C   . ALA B 1 100 ? 25.618 45.766 43.317  1.00 8.78   ? 781  ALA B C   1 
ATOM   2440 O O   . ALA B 1 100 ? 26.088 45.401 42.236  1.00 11.00  ? 781  ALA B O   1 
ATOM   2441 C CB  . ALA B 1 100 ? 23.217 46.470 43.506  1.00 9.87   ? 781  ALA B CB  1 
ATOM   2442 N N   . VAL B 1 101 ? 25.886 45.159 44.466  1.00 7.91   ? 782  VAL B N   1 
ATOM   2443 C CA  . VAL B 1 101 ? 26.726 43.971 44.552  1.00 13.41  ? 782  VAL B CA  1 
ATOM   2444 C C   . VAL B 1 101 ? 25.970 42.912 45.343  1.00 15.24  ? 782  VAL B C   1 
ATOM   2445 O O   . VAL B 1 101 ? 25.357 43.222 46.371  1.00 16.47  ? 782  VAL B O   1 
ATOM   2446 C CB  . VAL B 1 101 ? 28.089 44.294 45.199  1.00 13.35  ? 782  VAL B CB  1 
ATOM   2447 C CG1 . VAL B 1 101 ? 28.840 43.037 45.535  1.00 15.94  ? 782  VAL B CG1 1 
ATOM   2448 C CG2 . VAL B 1 101 ? 28.925 45.163 44.263  1.00 19.89  ? 782  VAL B CG2 1 
ATOM   2449 N N   . ILE B 1 102 ? 25.999 41.669 44.854  1.00 10.66  ? 783  ILE B N   1 
ATOM   2450 C CA  . ILE B 1 102 ? 25.315 40.539 45.476  1.00 12.87  ? 783  ILE B CA  1 
ATOM   2451 C C   . ILE B 1 102 ? 26.372 39.583 46.011  1.00 12.35  ? 783  ILE B C   1 
ATOM   2452 O O   . ILE B 1 102 ? 27.199 39.074 45.246  1.00 11.07  ? 783  ILE B O   1 
ATOM   2453 C CB  . ILE B 1 102 ? 24.395 39.812 44.481  1.00 14.20  ? 783  ILE B CB  1 
ATOM   2454 C CG1 . ILE B 1 102 ? 23.373 40.773 43.881  1.00 16.13  ? 783  ILE B CG1 1 
ATOM   2455 C CG2 . ILE B 1 102 ? 23.709 38.600 45.147  1.00 14.49  ? 783  ILE B CG2 1 
ATOM   2456 C CD1 . ILE B 1 102 ? 22.832 40.312 42.554  1.00 14.58  ? 783  ILE B CD1 1 
ATOM   2457 N N   . THR B 1 103 ? 26.332 39.313 47.311  1.00 11.91  ? 784  THR B N   1 
ATOM   2458 C CA  . THR B 1 103 ? 27.275 38.402 47.943  1.00 15.24  ? 784  THR B CA  1 
ATOM   2459 C C   . THR B 1 103 ? 26.600 37.049 48.159  1.00 17.75  ? 784  THR B C   1 
ATOM   2460 O O   . THR B 1 103 ? 25.581 36.961 48.854  1.00 16.17  ? 784  THR B O   1 
ATOM   2461 C CB  . THR B 1 103 ? 27.791 38.986 49.258  1.00 12.47  ? 784  THR B CB  1 
ATOM   2462 O OG1 . THR B 1 103 ? 26.688 39.308 50.105  1.00 16.49  ? 784  THR B OG1 1 
ATOM   2463 C CG2 . THR B 1 103 ? 28.600 40.256 48.989  1.00 19.76  ? 784  THR B CG2 1 
ATOM   2464 N N   . LEU B 1 104 ? 27.161 36.006 47.554  1.00 14.20  ? 785  LEU B N   1 
ATOM   2465 C CA  . LEU B 1 104 ? 26.620 34.651 47.574  1.00 16.82  ? 785  LEU B CA  1 
ATOM   2466 C C   . LEU B 1 104 ? 27.322 33.797 48.629  1.00 16.29  ? 785  LEU B C   1 
ATOM   2467 O O   . LEU B 1 104 ? 28.367 34.179 49.166  1.00 17.39  ? 785  LEU B O   1 
ATOM   2468 C CB  . LEU B 1 104 ? 26.770 34.025 46.185  1.00 12.34  ? 785  LEU B CB  1 
ATOM   2469 C CG  . LEU B 1 104 ? 26.032 34.791 45.088  1.00 15.71  ? 785  LEU B CG  1 
ATOM   2470 C CD1 . LEU B 1 104 ? 26.404 34.261 43.717  1.00 13.40  ? 785  LEU B CD1 1 
ATOM   2471 C CD2 . LEU B 1 104 ? 24.517 34.720 45.318  1.00 17.71  ? 785  LEU B CD2 1 
ATOM   2472 N N   . PRO B 1 105 ? 26.774 32.616 48.954  1.00 20.83  ? 786  PRO B N   1 
ATOM   2473 C CA  . PRO B 1 105 ? 27.411 31.774 49.972  1.00 19.64  ? 786  PRO B CA  1 
ATOM   2474 C C   . PRO B 1 105 ? 28.847 31.427 49.617  1.00 16.16  ? 786  PRO B C   1 
ATOM   2475 O O   . PRO B 1 105 ? 29.225 31.349 48.444  1.00 17.81  ? 786  PRO B O   1 
ATOM   2476 C CB  . PRO B 1 105 ? 26.530 30.521 49.996  1.00 20.04  ? 786  PRO B CB  1 
ATOM   2477 C CG  . PRO B 1 105 ? 25.201 31.015 49.574  1.00 18.80  ? 786  PRO B CG  1 
ATOM   2478 C CD  . PRO B 1 105 ? 25.478 32.052 48.534  1.00 20.18  ? 786  PRO B CD  1 
ATOM   2479 N N   . GLN B 1 106 ? 29.644 31.211 50.664  1.00 18.63  ? 787  GLN B N   1 
ATOM   2480 C CA  . GLN B 1 106 ? 31.050 30.851 50.499  1.00 23.72  ? 787  GLN B CA  1 
ATOM   2481 C C   . GLN B 1 106 ? 31.247 29.577 49.678  1.00 24.25  ? 787  GLN B C   1 
ATOM   2482 O O   . GLN B 1 106 ? 32.345 29.357 49.154  1.00 26.50  ? 787  GLN B O   1 
ATOM   2483 C CB  . GLN B 1 106 ? 31.701 30.683 51.873  1.00 30.92  ? 787  GLN B CB  1 
ATOM   2484 C CG  . GLN B 1 106 ? 33.208 30.879 51.876  1.00 36.10  ? 787  GLN B CG  1 
ATOM   2485 C CD  . GLN B 1 106 ? 33.591 32.336 51.775  1.00 42.70  ? 787  GLN B CD  1 
ATOM   2486 O OE1 . GLN B 1 106 ? 32.893 33.205 52.295  1.00 40.09  ? 787  GLN B OE1 1 
ATOM   2487 N NE2 . GLN B 1 106 ? 34.698 32.615 51.096  1.00 49.20  ? 787  GLN B NE2 1 
ATOM   2488 N N   . SER B 1 107 ? 30.219 28.741 49.550  1.00 20.23  ? 788  SER B N   1 
ATOM   2489 C CA  . SER B 1 107 ? 30.308 27.492 48.806  1.00 19.09  ? 788  SER B CA  1 
ATOM   2490 C C   . SER B 1 107 ? 30.168 27.672 47.299  1.00 24.61  ? 788  SER B C   1 
ATOM   2491 O O   . SER B 1 107 ? 30.248 26.679 46.573  1.00 21.44  ? 788  SER B O   1 
ATOM   2492 C CB  . SER B 1 107 ? 29.236 26.515 49.297  1.00 23.59  ? 788  SER B CB  1 
ATOM   2493 O OG  . SER B 1 107 ? 27.934 27.068 49.147  1.00 26.71  ? 788  SER B OG  1 
ATOM   2494 N N   . THR B 1 108 ? 29.958 28.895 46.808  1.00 19.50  ? 789  THR B N   1 
ATOM   2495 C CA  . THR B 1 108 ? 29.742 29.091 45.375  1.00 20.76  ? 789  THR B CA  1 
ATOM   2496 C C   . THR B 1 108 ? 30.968 28.676 44.563  1.00 19.02  ? 789  THR B C   1 
ATOM   2497 O O   . THR B 1 108 ? 30.888 27.785 43.710  1.00 28.67  ? 789  THR B O   1 
ATOM   2498 C CB  . THR B 1 108 ? 29.363 30.546 45.105  1.00 16.09  ? 789  THR B CB  1 
ATOM   2499 O OG1 . THR B 1 108 ? 28.313 30.920 46.002  1.00 23.84  ? 789  THR B OG1 1 
ATOM   2500 C CG2 . THR B 1 108 ? 28.878 30.707 43.677  1.00 13.80  ? 789  THR B CG2 1 
ATOM   2501 N N   . ARG B 1 109 ? 32.110 29.323 44.809  1.00 16.04  ? 790  ARG B N   1 
ATOM   2502 C CA  . ARG B 1 109 ? 33.420 28.878 44.302  1.00 19.60  ? 790  ARG B CA  1 
ATOM   2503 C C   . ARG B 1 109 ? 33.497 28.855 42.772  1.00 21.72  ? 790  ARG B C   1 
ATOM   2504 O O   . ARG B 1 109 ? 34.083 27.945 42.180  1.00 14.81  ? 790  ARG B O   1 
ATOM   2505 C CB  . ARG B 1 109 ? 33.788 27.497 44.856  1.00 19.22  ? 790  ARG B CB  1 
ATOM   2506 C CG  . ARG B 1 109 ? 33.616 27.300 46.361  1.00 24.93  ? 790  ARG B CG  1 
ATOM   2507 C CD  . ARG B 1 109 ? 34.661 28.041 47.191  1.00 28.08  ? 790  ARG B CD  1 
ATOM   2508 N NE  . ARG B 1 109 ? 34.701 27.541 48.563  1.00 31.80  ? 790  ARG B NE  1 
ATOM   2509 C CZ  . ARG B 1 109 ? 35.506 26.574 48.986  1.00 28.51  ? 790  ARG B CZ  1 
ATOM   2510 N NH1 . ARG B 1 109 ? 36.381 25.997 48.176  1.00 19.95  ? 790  ARG B NH1 1 
ATOM   2511 N NH2 . ARG B 1 109 ? 35.435 26.175 50.253  1.00 30.10  ? 790  ARG B NH2 1 
ATOM   2512 N N   . ARG B 1 110 ? 32.939 29.862 42.111  1.00 17.46  ? 791  ARG B N   1 
ATOM   2513 C CA  . ARG B 1 110 ? 32.897 29.810 40.653  1.00 15.81  ? 791  ARG B CA  1 
ATOM   2514 C C   . ARG B 1 110 ? 34.103 30.497 40.021  1.00 11.29  ? 791  ARG B C   1 
ATOM   2515 O O   . ARG B 1 110 ? 34.777 31.324 40.638  1.00 13.11  ? 791  ARG B O   1 
ATOM   2516 C CB  . ARG B 1 110 ? 31.617 30.452 40.121  1.00 17.11  ? 791  ARG B CB  1 
ATOM   2517 C CG  . ARG B 1 110 ? 30.395 29.592 40.294  1.00 18.99  ? 791  ARG B CG  1 
ATOM   2518 C CD  . ARG B 1 110 ? 29.220 30.221 39.606  1.00 16.89  ? 791  ARG B CD  1 
ATOM   2519 N NE  . ARG B 1 110 ? 29.513 30.504 38.209  1.00 17.42  ? 791  ARG B NE  1 
ATOM   2520 C CZ  . ARG B 1 110 ? 29.494 29.593 37.248  1.00 17.81  ? 791  ARG B CZ  1 
ATOM   2521 N NH1 . ARG B 1 110 ? 29.239 28.323 37.509  1.00 22.64  ? 791  ARG B NH1 1 
ATOM   2522 N NH2 . ARG B 1 110 ? 29.736 29.965 35.994  1.00 16.17  ? 791  ARG B NH2 1 
ATOM   2523 N N   . GLN B 1 111 ? 34.369 30.139 38.766  1.00 11.01  ? 792  GLN B N   1 
ATOM   2524 C CA  . GLN B 1 111 ? 35.230 30.974 37.940  1.00 12.38  ? 792  GLN B CA  1 
ATOM   2525 C C   . GLN B 1 111 ? 34.558 32.325 37.720  1.00 13.50  ? 792  GLN B C   1 
ATOM   2526 O O   . GLN B 1 111 ? 33.332 32.443 37.762  1.00 13.55  ? 792  GLN B O   1 
ATOM   2527 C CB  . GLN B 1 111 ? 35.515 30.301 36.595  1.00 15.24  ? 792  GLN B CB  1 
ATOM   2528 C CG  . GLN B 1 111 ? 34.283 30.121 35.713  1.00 19.18  ? 792  GLN B CG  1 
ATOM   2529 C CD  . GLN B 1 111 ? 34.638 29.844 34.261  1.00 25.06  ? 792  GLN B CD  1 
ATOM   2530 O OE1 . GLN B 1 111 ? 35.309 30.647 33.612  1.00 27.09  ? 792  GLN B OE1 1 
ATOM   2531 N NE2 . GLN B 1 111 ? 34.196 28.699 33.747  1.00 21.22  ? 792  GLN B NE2 1 
ATOM   2532 N N   . HIS B 1 112 ? 35.357 33.359 37.484  1.00 11.62  ? 793  HIS B N   1 
ATOM   2533 C CA  . HIS B 1 112 ? 34.773 34.688 37.380  1.00 9.68   ? 793  HIS B CA  1 
ATOM   2534 C C   . HIS B 1 112 ? 35.663 35.571 36.519  1.00 11.95  ? 793  HIS B C   1 
ATOM   2535 O O   . HIS B 1 112 ? 36.769 35.190 36.132  1.00 15.75  ? 793  HIS B O   1 
ATOM   2536 C CB  . HIS B 1 112 ? 34.572 35.296 38.774  1.00 9.45   ? 793  HIS B CB  1 
ATOM   2537 C CG  . HIS B 1 112 ? 35.847 35.448 39.542  1.00 17.60  ? 793  HIS B CG  1 
ATOM   2538 N ND1 . HIS B 1 112 ? 36.615 36.592 39.490  1.00 15.65  ? 793  HIS B ND1 1 
ATOM   2539 C CD2 . HIS B 1 112 ? 36.509 34.587 40.350  1.00 12.09  ? 793  HIS B CD2 1 
ATOM   2540 C CE1 . HIS B 1 112 ? 37.685 36.436 40.248  1.00 15.05  ? 793  HIS B CE1 1 
ATOM   2541 N NE2 . HIS B 1 112 ? 37.644 35.228 40.781  1.00 18.99  ? 793  HIS B NE2 1 
ATOM   2542 N N   . ALA B 1 113 ? 35.156 36.763 36.213  1.00 11.16  ? 794  ALA B N   1 
ATOM   2543 C CA  . ALA B 1 113 ? 35.942 37.797 35.562  1.00 11.47  ? 794  ALA B CA  1 
ATOM   2544 C C   . ALA B 1 113 ? 36.576 38.707 36.612  1.00 13.41  ? 794  ALA B C   1 
ATOM   2545 O O   . ALA B 1 113 ? 36.159 38.737 37.772  1.00 11.59  ? 794  ALA B O   1 
ATOM   2546 C CB  . ALA B 1 113 ? 35.065 38.616 34.613  1.00 13.08  ? 794  ALA B CB  1 
ATOM   2547 N N   . ASN B 1 114 ? 37.601 39.451 36.196  1.00 17.82  ? 795  ASN B N   1 
ATOM   2548 C CA  . ASN B 1 114 ? 38.289 40.392 37.073  1.00 17.02  ? 795  ASN B CA  1 
ATOM   2549 C C   . ASN B 1 114 ? 37.740 41.802 36.896  1.00 15.59  ? 795  ASN B C   1 
ATOM   2550 O O   . ASN B 1 114 ? 37.619 42.293 35.769  1.00 16.17  ? 795  ASN B O   1 
ATOM   2551 C CB  . ASN B 1 114 ? 39.796 40.405 36.803  1.00 18.48  ? 795  ASN B CB  1 
ATOM   2552 C CG  . ASN B 1 114 ? 40.455 39.096 37.141  1.00 24.09  ? 795  ASN B CG  1 
ATOM   2553 O OD1 . ASN B 1 114 ? 40.099 38.452 38.119  1.00 24.58  ? 795  ASN B OD1 1 
ATOM   2554 N ND2 . ASN B 1 114 ? 41.426 38.696 36.334  1.00 33.87  ? 795  ASN B ND2 1 
ATOM   2555 N N   . LEU B 1 115 ? 37.436 42.452 38.012  1.00 15.46  ? 796  LEU B N   1 
ATOM   2556 C CA  . LEU B 1 115 ? 37.164 43.881 37.989  1.00 14.54  ? 796  LEU B CA  1 
ATOM   2557 C C   . LEU B 1 115 ? 38.446 44.645 37.673  1.00 16.89  ? 796  LEU B C   1 
ATOM   2558 O O   . LEU B 1 115 ? 39.525 44.302 38.165  1.00 16.60  ? 796  LEU B O   1 
ATOM   2559 C CB  . LEU B 1 115 ? 36.600 44.324 39.335  1.00 14.86  ? 796  LEU B CB  1 
ATOM   2560 C CG  . LEU B 1 115 ? 36.172 45.784 39.464  1.00 13.78  ? 796  LEU B CG  1 
ATOM   2561 C CD1 . LEU B 1 115 ? 34.943 46.075 38.639  1.00 14.15  ? 796  LEU B CD1 1 
ATOM   2562 C CD2 . LEU B 1 115 ? 35.933 46.117 40.938  1.00 15.60  ? 796  LEU B CD2 1 
ATOM   2563 N N   . VAL B 1 116 ? 38.326 45.675 36.830  1.00 14.39  ? 797  VAL B N   1 
ATOM   2564 C CA  . VAL B 1 116 ? 39.500 46.429 36.409  1.00 17.14  ? 797  VAL B CA  1 
ATOM   2565 C C   . VAL B 1 116 ? 40.189 47.020 37.629  1.00 16.00  ? 797  VAL B C   1 
ATOM   2566 O O   . VAL B 1 116 ? 39.540 47.436 38.596  1.00 16.48  ? 797  VAL B O   1 
ATOM   2567 C CB  . VAL B 1 116 ? 39.114 47.512 35.385  1.00 14.18  ? 797  VAL B CB  1 
ATOM   2568 C CG1 . VAL B 1 116 ? 38.200 48.575 36.001  1.00 20.79  ? 797  VAL B CG1 1 
ATOM   2569 C CG2 . VAL B 1 116 ? 40.355 48.150 34.786  1.00 26.81  ? 797  VAL B CG2 1 
ATOM   2570 N N   . GLU B 1 117 ? 41.525 47.025 37.602  1.00 17.41  ? 798  GLU B N   1 
ATOM   2571 C CA  . GLU B 1 117 ? 42.282 47.422 38.785  1.00 26.11  ? 798  GLU B CA  1 
ATOM   2572 C C   . GLU B 1 117 ? 42.187 48.924 39.017  1.00 28.73  ? 798  GLU B C   1 
ATOM   2573 O O   . GLU B 1 117 ? 41.873 49.372 40.127  1.00 28.22  ? 798  GLU B O   1 
ATOM   2574 C CB  . GLU B 1 117 ? 43.738 46.978 38.646  1.00 28.15  ? 798  GLU B CB  1 
ATOM   2575 C CG  . GLU B 1 117 ? 44.569 47.131 39.909  1.00 39.90  ? 798  GLU B CG  1 
ATOM   2576 C CD  . GLU B 1 117 ? 46.002 46.642 39.731  1.00 58.11  ? 798  GLU B CD  1 
ATOM   2577 O OE1 . GLU B 1 117 ? 46.399 46.352 38.580  1.00 57.96  ? 798  GLU B OE1 1 
ATOM   2578 O OE2 . GLU B 1 117 ? 46.732 46.546 40.743  1.00 42.16  ? 798  GLU B OE2 1 
ATOM   2579 N N   . ASN B 1 118 ? 42.454 49.722 37.988  1.00 26.95  ? 799  ASN B N   1 
ATOM   2580 C CA  A ASN B 1 118 ? 42.365 51.171 38.079  0.70 28.05  ? 799  ASN B CA  1 
ATOM   2581 C CA  B ASN B 1 118 ? 42.339 51.167 38.100  0.30 28.00  ? 799  ASN B CA  1 
ATOM   2582 C C   . ASN B 1 118 ? 41.444 51.701 36.991  1.00 25.60  ? 799  ASN B C   1 
ATOM   2583 O O   . ASN B 1 118 ? 41.290 51.089 35.930  1.00 24.64  ? 799  ASN B O   1 
ATOM   2584 C CB  A ASN B 1 118 ? 43.747 51.838 37.957  0.70 28.72  ? 799  ASN B CB  1 
ATOM   2585 C CB  B ASN B 1 118 ? 43.715 51.867 38.071  0.30 28.67  ? 799  ASN B CB  1 
ATOM   2586 C CG  A ASN B 1 118 ? 44.681 51.460 39.091  0.70 28.41  ? 799  ASN B CG  1 
ATOM   2587 C CG  B ASN B 1 118 ? 44.547 51.501 36.852  0.30 26.56  ? 799  ASN B CG  1 
ATOM   2588 O OD1 A ASN B 1 118 ? 44.524 51.923 40.219  0.70 28.85  ? 799  ASN B OD1 1 
ATOM   2589 O OD1 B ASN B 1 118 ? 44.049 51.442 35.729  0.30 26.17  ? 799  ASN B OD1 1 
ATOM   2590 N ND2 A ASN B 1 118 ? 45.666 50.623 38.792  0.70 32.15  ? 799  ASN B ND2 1 
ATOM   2591 N ND2 B ASN B 1 118 ? 45.834 51.257 37.075  0.30 33.39  ? 799  ASN B ND2 1 
ATOM   2592 N N   . TYR B 1 119 ? 40.841 52.849 37.267  1.00 27.10  ? 800  TYR B N   1 
ATOM   2593 C CA  . TYR B 1 119 ? 39.975 53.508 36.306  1.00 20.02  ? 800  TYR B CA  1 
ATOM   2594 C C   . TYR B 1 119 ? 40.768 53.993 35.099  1.00 18.79  ? 800  TYR B C   1 
ATOM   2595 O O   . TYR B 1 119 ? 41.851 54.573 35.235  1.00 28.36  ? 800  TYR B O   1 
ATOM   2596 C CB  . TYR B 1 119 ? 39.276 54.688 36.978  1.00 21.78  ? 800  TYR B CB  1 
ATOM   2597 C CG  . TYR B 1 119 ? 38.674 55.698 36.027  1.00 18.81  ? 800  TYR B CG  1 
ATOM   2598 C CD1 . TYR B 1 119 ? 37.367 55.562 35.584  1.00 13.12  ? 800  TYR B CD1 1 
ATOM   2599 C CD2 . TYR B 1 119 ? 39.405 56.808 35.595  1.00 14.80  ? 800  TYR B CD2 1 
ATOM   2600 C CE1 . TYR B 1 119 ? 36.801 56.483 34.722  1.00 16.99  ? 800  TYR B CE1 1 
ATOM   2601 C CE2 . TYR B 1 119 ? 38.851 57.730 34.734  1.00 15.55  ? 800  TYR B CE2 1 
ATOM   2602 C CZ  . TYR B 1 119 ? 37.541 57.569 34.306  1.00 15.96  ? 800  TYR B CZ  1 
ATOM   2603 O OH  . TYR B 1 119 ? 36.976 58.490 33.448  1.00 19.25  ? 800  TYR B OH  1 
ATOM   2604 N N   . SER B 1 120 ? 40.225 53.740 33.911  1.00 14.69  ? 801  SER B N   1 
ATOM   2605 C CA  A SER B 1 120 ? 40.762 54.280 32.668  0.70 19.09  ? 801  SER B CA  1 
ATOM   2606 C CA  B SER B 1 120 ? 40.764 54.270 32.666  0.30 19.14  ? 801  SER B CA  1 
ATOM   2607 C C   . SER B 1 120 ? 39.641 54.963 31.909  1.00 22.76  ? 801  SER B C   1 
ATOM   2608 O O   . SER B 1 120 ? 38.572 54.374 31.704  1.00 22.39  ? 801  SER B O   1 
ATOM   2609 C CB  A SER B 1 120 ? 41.393 53.199 31.793  0.70 21.36  ? 801  SER B CB  1 
ATOM   2610 C CB  B SER B 1 120 ? 41.387 53.162 31.810  0.30 21.35  ? 801  SER B CB  1 
ATOM   2611 O OG  A SER B 1 120 ? 42.690 52.883 32.250  0.70 20.82  ? 801  SER B OG  1 
ATOM   2612 O OG  B SER B 1 120 ? 41.965 53.683 30.627  0.30 18.38  ? 801  SER B OG  1 
ATOM   2613 N N   . LYS B 1 121 ? 39.886 56.204 31.503  1.00 16.65  ? 802  LYS B N   1 
ATOM   2614 C CA  . LYS B 1 121 ? 38.882 56.962 30.775  1.00 21.02  ? 802  LYS B CA  1 
ATOM   2615 C C   . LYS B 1 121 ? 38.505 56.247 29.489  1.00 17.00  ? 802  LYS B C   1 
ATOM   2616 O O   . LYS B 1 121 ? 39.372 55.808 28.730  1.00 17.31  ? 802  LYS B O   1 
ATOM   2617 C CB  . LYS B 1 121 ? 39.407 58.359 30.464  1.00 18.84  ? 802  LYS B CB  1 
ATOM   2618 C CG  . LYS B 1 121 ? 38.535 59.162 29.513  1.00 22.68  ? 802  LYS B CG  1 
ATOM   2619 C CD  . LYS B 1 121 ? 37.312 59.694 30.218  1.00 27.13  ? 802  LYS B CD  1 
ATOM   2620 C CE  . LYS B 1 121 ? 36.736 60.901 29.496  1.00 16.42  ? 802  LYS B CE  1 
ATOM   2621 N NZ  . LYS B 1 121 ? 36.600 60.664 28.033  1.00 22.54  ? 802  LYS B NZ  1 
ATOM   2622 N N   . VAL B 1 122 ? 37.203 56.126 29.255  1.00 15.56  ? 803  VAL B N   1 
ATOM   2623 C CA  . VAL B 1 122 ? 36.662 55.604 28.010  1.00 17.68  ? 803  VAL B CA  1 
ATOM   2624 C C   . VAL B 1 122 ? 36.318 56.784 27.116  1.00 16.93  ? 803  VAL B C   1 
ATOM   2625 O O   . VAL B 1 122 ? 35.689 57.750 27.571  1.00 18.42  ? 803  VAL B O   1 
ATOM   2626 C CB  . VAL B 1 122 ? 35.425 54.729 28.272  1.00 13.51  ? 803  VAL B CB  1 
ATOM   2627 C CG1 . VAL B 1 122 ? 34.809 54.284 26.961  1.00 15.09  ? 803  VAL B CG1 1 
ATOM   2628 C CG2 . VAL B 1 122 ? 35.817 53.538 29.130  1.00 18.36  ? 803  VAL B CG2 1 
ATOM   2629 N N   . ASN B 1 123 ? 36.724 56.711 25.851  1.00 15.94  ? 804  ASN B N   1 
ATOM   2630 C CA  . ASN B 1 123 ? 36.553 57.803 24.904  1.00 21.53  ? 804  ASN B CA  1 
ATOM   2631 C C   . ASN B 1 123 ? 35.493 57.466 23.861  1.00 26.62  ? 804  ASN B C   1 
ATOM   2632 O O   . ASN B 1 123 ? 35.189 56.297 23.598  1.00 21.02  ? 804  ASN B O   1 
ATOM   2633 C CB  . ASN B 1 123 ? 37.874 58.132 24.193  1.00 18.44  ? 804  ASN B CB  1 
ATOM   2634 C CG  . ASN B 1 123 ? 38.869 58.828 25.094  1.00 30.13  ? 804  ASN B CG  1 
ATOM   2635 O OD1 . ASN B 1 123 ? 38.537 59.250 26.199  1.00 27.12  ? 804  ASN B OD1 1 
ATOM   2636 N ND2 . ASN B 1 123 ? 40.100 58.970 24.615  1.00 32.32  ? 804  ASN B ND2 1 
ATOM   2637 N N   . VAL B 1 124 ? 34.927 58.524 23.273  1.00 18.96  ? 805  VAL B N   1 
ATOM   2638 C CA  . VAL B 1 124 ? 34.095 58.367 22.088  1.00 23.03  ? 805  VAL B CA  1 
ATOM   2639 C C   . VAL B 1 124 ? 34.888 57.635 21.018  1.00 20.03  ? 805  VAL B C   1 
ATOM   2640 O O   . VAL B 1 124 ? 36.093 57.858 20.847  1.00 28.20  ? 805  VAL B O   1 
ATOM   2641 C CB  . VAL B 1 124 ? 33.611 59.737 21.583  1.00 26.25  ? 805  VAL B CB  1 
ATOM   2642 C CG1 . VAL B 1 124 ? 32.829 59.597 20.278  1.00 26.93  ? 805  VAL B CG1 1 
ATOM   2643 C CG2 . VAL B 1 124 ? 32.768 60.425 22.636  1.00 21.41  ? 805  VAL B CG2 1 
ATOM   2644 N N   . ASN B 1 125 ? 34.209 56.735 20.309  1.00 20.42  ? 806  ASN B N   1 
ATOM   2645 C CA  . ASN B 1 125 ? 34.720 55.854 19.263  1.00 28.47  ? 806  ASN B CA  1 
ATOM   2646 C C   . ASN B 1 125 ? 35.513 54.691 19.834  1.00 19.67  ? 806  ASN B C   1 
ATOM   2647 O O   . ASN B 1 125 ? 36.025 53.885 19.053  1.00 26.15  ? 806  ASN B O   1 
ATOM   2648 C CB  . ASN B 1 125 ? 35.585 56.581 18.225  1.00 24.56  ? 806  ASN B CB  1 
ATOM   2649 C CG  . ASN B 1 125 ? 34.786 57.544 17.399  1.00 27.86  ? 806  ASN B CG  1 
ATOM   2650 O OD1 . ASN B 1 125 ? 33.646 57.254 17.031  1.00 31.96  ? 806  ASN B OD1 1 
ATOM   2651 N ND2 . ASN B 1 125 ? 35.363 58.705 17.113  1.00 34.01  ? 806  ASN B ND2 1 
ATOM   2652 N N   . ASP B 1 126 ? 35.649 54.579 21.151  1.00 20.91  ? 807  ASP B N   1 
ATOM   2653 C CA  . ASP B 1 126 ? 36.168 53.350 21.722  1.00 20.44  ? 807  ASP B CA  1 
ATOM   2654 C C   . ASP B 1 126 ? 35.216 52.212 21.393  1.00 17.31  ? 807  ASP B C   1 
ATOM   2655 O O   . ASP B 1 126 ? 34.004 52.405 21.260  1.00 22.91  ? 807  ASP B O   1 
ATOM   2656 C CB  . ASP B 1 126 ? 36.310 53.454 23.242  1.00 18.81  ? 807  ASP B CB  1 
ATOM   2657 C CG  . ASP B 1 126 ? 37.514 54.262 23.677  1.00 23.40  ? 807  ASP B CG  1 
ATOM   2658 O OD1 . ASP B 1 126 ? 38.198 54.851 22.811  1.00 23.22  ? 807  ASP B OD1 1 
ATOM   2659 O OD2 . ASP B 1 126 ? 37.764 54.308 24.901  1.00 17.61  ? 807  ASP B OD2 1 
ATOM   2660 N N   . LYS B 1 127 ? 35.764 51.016 21.274  1.00 24.79  ? 808  LYS B N   1 
ATOM   2661 C CA  . LYS B 1 127 ? 34.954 49.829 21.063  1.00 22.45  ? 808  LYS B CA  1 
ATOM   2662 C C   . LYS B 1 127 ? 34.903 49.037 22.360  1.00 18.55  ? 808  LYS B C   1 
ATOM   2663 O O   . LYS B 1 127 ? 35.942 48.773 22.977  1.00 22.92  ? 808  LYS B O   1 
ATOM   2664 C CB  . LYS B 1 127 ? 35.503 49.004 19.899  1.00 23.10  ? 808  LYS B CB  1 
ATOM   2665 C CG  . LYS B 1 127 ? 35.319 49.740 18.569  1.00 23.69  ? 808  LYS B CG  1 
ATOM   2666 C CD  . LYS B 1 127 ? 35.968 49.045 17.395  1.00 33.73  ? 808  LYS B CD  1 
ATOM   2667 C CE  . LYS B 1 127 ? 35.768 49.858 16.122  1.00 30.76  ? 808  LYS B CE  1 
ATOM   2668 N NZ  . LYS B 1 127 ? 36.207 49.118 14.908  1.00 44.79  ? 808  LYS B NZ  1 
ATOM   2669 N N   . LEU B 1 128 ? 33.687 48.700 22.787  1.00 17.60  ? 809  LEU B N   1 
ATOM   2670 C CA  . LEU B 1 128 ? 33.440 48.005 24.039  1.00 13.30  ? 809  LEU B CA  1 
ATOM   2671 C C   . LEU B 1 128 ? 32.823 46.644 23.766  1.00 13.84  ? 809  LEU B C   1 
ATOM   2672 O O   . LEU B 1 128 ? 32.284 46.385 22.689  1.00 14.40  ? 809  LEU B O   1 
ATOM   2673 C CB  . LEU B 1 128 ? 32.508 48.811 24.951  1.00 14.85  ? 809  LEU B CB  1 
ATOM   2674 C CG  . LEU B 1 128 ? 33.016 50.184 25.384  1.00 14.02  ? 809  LEU B CG  1 
ATOM   2675 C CD1 . LEU B 1 128 ? 31.967 50.923 26.207  1.00 14.69  ? 809  LEU B CD1 1 
ATOM   2676 C CD2 . LEU B 1 128 ? 34.307 50.024 26.164  1.00 18.37  ? 809  LEU B CD2 1 
ATOM   2677 N N   . ASN B 1 129 ? 32.903 45.773 24.763  1.00 12.71  ? 810  ASN B N   1 
ATOM   2678 C CA  . ASN B 1 129 ? 32.325 44.436 24.677  1.00 12.53  ? 810  ASN B CA  1 
ATOM   2679 C C   . ASN B 1 129 ? 31.357 44.276 25.837  1.00 12.37  ? 810  ASN B C   1 
ATOM   2680 O O   . ASN B 1 129 ? 31.771 44.272 27.002  1.00 14.95  ? 810  ASN B O   1 
ATOM   2681 C CB  . ASN B 1 129 ? 33.409 43.362 24.686  1.00 17.61  ? 810  ASN B CB  1 
ATOM   2682 C CG  . ASN B 1 129 ? 34.122 43.265 23.352  1.00 21.42  ? 810  ASN B CG  1 
ATOM   2683 O OD1 . ASN B 1 129 ? 33.626 42.632 22.422  1.00 16.90  ? 810  ASN B OD1 1 
ATOM   2684 N ND2 . ASN B 1 129 ? 35.269 43.935 23.236  1.00 16.32  ? 810  ASN B ND2 1 
ATOM   2685 N N   . VAL B 1 130 ? 30.071 44.152 25.517  1.00 17.06  ? 811  VAL B N   1 
ATOM   2686 C CA  . VAL B 1 130 ? 29.003 44.149 26.506  1.00 12.73  ? 811  VAL B CA  1 
ATOM   2687 C C   . VAL B 1 130 ? 28.284 42.807 26.445  1.00 13.33  ? 811  VAL B C   1 
ATOM   2688 O O   . VAL B 1 130 ? 28.009 42.280 25.360  1.00 11.71  ? 811  VAL B O   1 
ATOM   2689 C CB  . VAL B 1 130 ? 28.021 45.318 26.273  1.00 11.45  ? 811  VAL B CB  1 
ATOM   2690 C CG1 . VAL B 1 130 ? 27.071 45.464 27.450  1.00 13.99  ? 811  VAL B CG1 1 
ATOM   2691 C CG2 . VAL B 1 130 ? 28.789 46.618 26.033  1.00 15.91  ? 811  VAL B CG2 1 
ATOM   2692 N N   . TYR B 1 131 ? 27.999 42.253 27.615  1.00 10.65  ? 812  TYR B N   1 
ATOM   2693 C CA  . TYR B 1 131 ? 27.366 40.949 27.739  1.00 14.67  ? 812  TYR B CA  1 
ATOM   2694 C C   . TYR B 1 131 ? 26.106 41.084 28.581  1.00 11.59  ? 812  TYR B C   1 
ATOM   2695 O O   . TYR B 1 131 ? 26.052 41.891 29.517  1.00 11.17  ? 812  TYR B O   1 
ATOM   2696 C CB  . TYR B 1 131 ? 28.321 39.938 28.374  1.00 13.30  ? 812  TYR B CB  1 
ATOM   2697 C CG  . TYR B 1 131 ? 29.556 39.621 27.546  1.00 12.41  ? 812  TYR B CG  1 
ATOM   2698 C CD1 . TYR B 1 131 ? 30.609 40.528 27.444  1.00 12.62  ? 812  TYR B CD1 1 
ATOM   2699 C CD2 . TYR B 1 131 ? 29.676 38.408 26.886  1.00 16.86  ? 812  TYR B CD2 1 
ATOM   2700 C CE1 . TYR B 1 131 ? 31.742 40.240 26.700  1.00 14.63  ? 812  TYR B CE1 1 
ATOM   2701 C CE2 . TYR B 1 131 ? 30.810 38.103 26.142  1.00 16.23  ? 812  TYR B CE2 1 
ATOM   2702 C CZ  . TYR B 1 131 ? 31.837 39.024 26.050  1.00 16.30  ? 812  TYR B CZ  1 
ATOM   2703 O OH  . TYR B 1 131 ? 32.961 38.726 25.305  1.00 19.09  ? 812  TYR B OH  1 
ATOM   2704 N N   . GLY B 1 132 ? 25.091 40.294 28.256  1.00 13.12  ? 813  GLY B N   1 
ATOM   2705 C CA  . GLY B 1 132 ? 23.843 40.411 28.984  1.00 14.35  ? 813  GLY B CA  1 
ATOM   2706 C C   . GLY B 1 132 ? 22.794 39.474 28.430  1.00 13.14  ? 813  GLY B C   1 
ATOM   2707 O O   . GLY B 1 132 ? 23.065 38.648 27.557  1.00 12.14  ? 813  GLY B O   1 
ATOM   2708 N N   . TYR B 1 133 ? 21.575 39.629 28.948  1.00 12.03  ? 814  TYR B N   1 
ATOM   2709 C CA  . TYR B 1 133 ? 20.436 38.806 28.556  1.00 16.29  ? 814  TYR B CA  1 
ATOM   2710 C C   . TYR B 1 133 ? 19.276 39.706 28.144  1.00 19.67  ? 814  TYR B C   1 
ATOM   2711 O O   . TYR B 1 133 ? 18.254 39.782 28.838  1.00 14.22  ? 814  TYR B O   1 
ATOM   2712 C CB  . TYR B 1 133 ? 20.046 37.848 29.685  1.00 13.05  ? 814  TYR B CB  1 
ATOM   2713 C CG  . TYR B 1 133 ? 21.108 36.797 29.933  1.00 12.86  ? 814  TYR B CG  1 
ATOM   2714 C CD1 . TYR B 1 133 ? 22.228 37.082 30.702  1.00 12.25  ? 814  TYR B CD1 1 
ATOM   2715 C CD2 . TYR B 1 133 ? 21.009 35.528 29.364  1.00 15.44  ? 814  TYR B CD2 1 
ATOM   2716 C CE1 . TYR B 1 133 ? 23.214 36.129 30.913  1.00 16.70  ? 814  TYR B CE1 1 
ATOM   2717 C CE2 . TYR B 1 133 ? 21.988 34.570 29.569  1.00 17.28  ? 814  TYR B CE2 1 
ATOM   2718 C CZ  . TYR B 1 133 ? 23.091 34.878 30.342  1.00 17.68  ? 814  TYR B CZ  1 
ATOM   2719 O OH  . TYR B 1 133 ? 24.070 33.932 30.558  1.00 15.96  ? 814  TYR B OH  1 
ATOM   2720 N N   . PRO B 1 134 ? 19.399 40.399 27.009  1.00 18.95  ? 815  PRO B N   1 
ATOM   2721 C CA  . PRO B 1 134 ? 18.245 41.137 26.478  1.00 20.32  ? 815  PRO B CA  1 
ATOM   2722 C C   . PRO B 1 134 ? 17.100 40.181 26.183  1.00 23.43  ? 815  PRO B C   1 
ATOM   2723 O O   . PRO B 1 134 ? 17.293 39.119 25.580  1.00 24.30  ? 815  PRO B O   1 
ATOM   2724 C CB  . PRO B 1 134 ? 18.793 41.786 25.201  1.00 18.93  ? 815  PRO B CB  1 
ATOM   2725 C CG  . PRO B 1 134 ? 19.920 40.892 24.790  1.00 17.23  ? 815  PRO B CG  1 
ATOM   2726 C CD  . PRO B 1 134 ? 20.542 40.429 26.078  1.00 13.65  ? 815  PRO B CD  1 
ATOM   2727 N N   . ARG B 1 135 ? 15.903 40.551 26.643  1.00 17.53  ? 816  ARG B N   1 
ATOM   2728 C CA  . ARG B 1 135 ? 14.699 39.723 26.551  1.00 22.62  ? 816  ARG B CA  1 
ATOM   2729 C C   . ARG B 1 135 ? 14.883 38.365 27.215  1.00 21.61  ? 816  ARG B C   1 
ATOM   2730 O O   . ARG B 1 135 ? 14.193 37.404 26.869  1.00 28.19  ? 816  ARG B O   1 
ATOM   2731 C CB  . ARG B 1 135 ? 14.246 39.537 25.098  1.00 22.38  ? 816  ARG B CB  1 
ATOM   2732 C CG  . ARG B 1 135 ? 14.200 40.830 24.291  1.00 46.04  ? 816  ARG B CG  1 
ATOM   2733 C CD  . ARG B 1 135 ? 13.157 41.802 24.823  1.00 48.85  ? 816  ARG B CD  1 
ATOM   2734 N NE  . ARG B 1 135 ? 13.193 43.076 24.112  1.00 52.58  ? 816  ARG B NE  1 
ATOM   2735 C CZ  . ARG B 1 135 ? 12.239 43.996 24.172  1.00 52.92  ? 816  ARG B CZ  1 
ATOM   2736 N NH1 . ARG B 1 135 ? 11.138 43.806 24.880  1.00 65.18  ? 816  ARG B NH1 1 
ATOM   2737 N NH2 . ARG B 1 135 ? 12.395 45.135 23.503  1.00 53.71  ? 816  ARG B NH2 1 
ATOM   2738 N N   . GLY B 1 136 ? 15.808 38.272 28.168  1.00 17.96  ? 817  GLY B N   1 
ATOM   2739 C CA  . GLY B 1 136 ? 16.068 37.028 28.858  1.00 20.51  ? 817  GLY B CA  1 
ATOM   2740 C C   . GLY B 1 136 ? 16.954 36.047 28.125  1.00 22.80  ? 817  GLY B C   1 
ATOM   2741 O O   . GLY B 1 136 ? 17.094 34.908 28.587  1.00 25.09  ? 817  GLY B O   1 
ATOM   2742 N N   . GLU B 1 137 ? 17.560 36.439 27.004  1.00 15.74  ? 818  GLU B N   1 
ATOM   2743 C CA  . GLU B 1 137 ? 18.383 35.537 26.211  1.00 18.27  ? 818  GLU B CA  1 
ATOM   2744 C C   . GLU B 1 137 ? 19.776 36.132 26.021  1.00 16.11  ? 818  GLU B C   1 
ATOM   2745 O O   . GLU B 1 137 ? 19.924 37.343 25.829  1.00 15.22  ? 818  GLU B O   1 
ATOM   2746 C CB  . GLU B 1 137 ? 17.725 35.243 24.855  1.00 20.96  ? 818  GLU B CB  1 
ATOM   2747 C CG  . GLU B 1 137 ? 16.336 34.590 24.982  1.00 18.27  ? 818  GLU B CG  1 
ATOM   2748 C CD  . GLU B 1 137 ? 15.697 34.275 23.644  1.00 19.90  ? 818  GLU B CD  1 
ATOM   2749 O OE1 . GLU B 1 137 ? 16.381 34.417 22.610  1.00 30.49  ? 818  GLU B OE1 1 
ATOM   2750 O OE2 . GLU B 1 137 ? 14.507 33.886 23.628  1.00 30.41  ? 818  GLU B OE2 1 
ATOM   2751 N N   . TYR B 1 138 ? 20.789 35.267 26.076  1.00 17.05  ? 819  TYR B N   1 
ATOM   2752 C CA  . TYR B 1 138 ? 22.182 35.707 26.043  1.00 13.98  ? 819  TYR B CA  1 
ATOM   2753 C C   . TYR B 1 138 ? 22.500 36.493 24.778  1.00 15.71  ? 819  TYR B C   1 
ATOM   2754 O O   . TYR B 1 138 ? 22.063 36.140 23.679  1.00 16.82  ? 819  TYR B O   1 
ATOM   2755 C CB  . TYR B 1 138 ? 23.111 34.495 26.136  1.00 14.24  ? 819  TYR B CB  1 
ATOM   2756 C CG  . TYR B 1 138 ? 24.591 34.822 26.019  1.00 13.89  ? 819  TYR B CG  1 
ATOM   2757 C CD1 . TYR B 1 138 ? 25.339 35.139 27.142  1.00 15.09  ? 819  TYR B CD1 1 
ATOM   2758 C CD2 . TYR B 1 138 ? 25.240 34.786 24.790  1.00 14.39  ? 819  TYR B CD2 1 
ATOM   2759 C CE1 . TYR B 1 138 ? 26.696 35.431 27.045  1.00 14.55  ? 819  TYR B CE1 1 
ATOM   2760 C CE2 . TYR B 1 138 ? 26.595 35.062 24.684  1.00 15.08  ? 819  TYR B CE2 1 
ATOM   2761 C CZ  . TYR B 1 138 ? 27.314 35.390 25.814  1.00 16.68  ? 819  TYR B CZ  1 
ATOM   2762 O OH  . TYR B 1 138 ? 28.658 35.678 25.708  1.00 17.98  ? 819  TYR B OH  1 
ATOM   2763 N N   . ALA B 1 139 ? 23.300 37.549 24.936  1.00 16.27  ? 820  ALA B N   1 
ATOM   2764 C CA  . ALA B 1 139 ? 23.825 38.294 23.803  1.00 16.25  ? 820  ALA B CA  1 
ATOM   2765 C C   . ALA B 1 139 ? 25.201 38.847 24.153  1.00 13.18  ? 820  ALA B C   1 
ATOM   2766 O O   . ALA B 1 139 ? 25.490 39.141 25.315  1.00 12.43  ? 820  ALA B O   1 
ATOM   2767 C CB  . ALA B 1 139 ? 22.894 39.439 23.391  1.00 16.71  ? 820  ALA B CB  1 
ATOM   2768 N N   . HIS B 1 140 ? 26.045 38.983 23.133  1.00 13.68  ? 821  HIS B N   1 
ATOM   2769 C CA  . HIS B 1 140 ? 27.346 39.648 23.238  1.00 13.40  ? 821  HIS B CA  1 
ATOM   2770 C C   . HIS B 1 140 ? 27.351 40.785 22.231  1.00 15.48  ? 821  HIS B C   1 
ATOM   2771 O O   . HIS B 1 140 ? 27.276 40.539 21.021  1.00 17.02  ? 821  HIS B O   1 
ATOM   2772 C CB  . HIS B 1 140 ? 28.501 38.677 22.961  1.00 13.93  ? 821  HIS B CB  1 
ATOM   2773 C CG  . HIS B 1 140 ? 29.854 39.336 22.891  1.00 15.41  ? 821  HIS B CG  1 
ATOM   2774 N ND1 . HIS B 1 140 ? 30.898 38.814 22.157  1.00 18.61  ? 821  HIS B ND1 1 
ATOM   2775 C CD2 . HIS B 1 140 ? 30.332 40.467 23.468  1.00 17.56  ? 821  HIS B CD2 1 
ATOM   2776 C CE1 . HIS B 1 140 ? 31.959 39.594 22.283  1.00 15.78  ? 821  HIS B CE1 1 
ATOM   2777 N NE2 . HIS B 1 140 ? 31.645 40.601 23.080  1.00 14.75  ? 821  HIS B NE2 1 
ATOM   2778 N N   . LEU B 1 141 ? 27.424 42.025 22.720  1.00 13.33  ? 822  LEU B N   1 
ATOM   2779 C CA  . LEU B 1 141 ? 27.622 43.172 21.842  1.00 17.83  ? 822  LEU B CA  1 
ATOM   2780 C C   . LEU B 1 141 ? 29.118 43.252 21.572  1.00 15.57  ? 822  LEU B C   1 
ATOM   2781 O O   . LEU B 1 141 ? 29.903 43.612 22.452  1.00 13.52  ? 822  LEU B O   1 
ATOM   2782 C CB  . LEU B 1 141 ? 27.095 44.451 22.483  1.00 15.72  ? 822  LEU B CB  1 
ATOM   2783 C CG  . LEU B 1 141 ? 25.657 44.422 23.014  1.00 16.54  ? 822  LEU B CG  1 
ATOM   2784 C CD1 . LEU B 1 141 ? 25.263 45.801 23.538  1.00 23.91  ? 822  LEU B CD1 1 
ATOM   2785 C CD2 . LEU B 1 141 ? 24.670 43.934 21.962  1.00 17.52  ? 822  LEU B CD2 1 
ATOM   2786 N N   . LYS B 1 142 ? 29.519 42.877 20.363  1.00 15.25  ? 823  LYS B N   1 
ATOM   2787 C CA  . LYS B 1 142 ? 30.925 42.688 20.034  1.00 15.80  ? 823  LYS B CA  1 
ATOM   2788 C C   . LYS B 1 142 ? 31.475 43.989 19.474  1.00 16.37  ? 823  LYS B C   1 
ATOM   2789 O O   . LYS B 1 142 ? 31.052 44.434 18.402  1.00 17.37  ? 823  LYS B O   1 
ATOM   2790 C CB  . LYS B 1 142 ? 31.088 41.553 19.027  1.00 21.07  ? 823  LYS B CB  1 
ATOM   2791 C CG  . LYS B 1 142 ? 32.525 41.247 18.639  1.00 17.83  ? 823  LYS B CG  1 
ATOM   2792 C CD  . LYS B 1 142 ? 32.586 40.202 17.523  1.00 19.23  ? 823  LYS B CD  1 
ATOM   2793 C CE  . LYS B 1 142 ? 34.013 39.980 17.030  1.00 20.47  ? 823  LYS B CE  1 
ATOM   2794 N NZ  . LYS B 1 142 ? 34.864 39.300 18.046  1.00 30.60  ? 823  LYS B NZ  1 
ATOM   2795 N N   . ASP B 1 143 ? 32.424 44.586 20.193  1.00 15.93  ? 824  ASP B N   1 
ATOM   2796 C CA  . ASP B 1 143 ? 33.092 45.815 19.777  1.00 17.53  ? 824  ASP B CA  1 
ATOM   2797 C C   . ASP B 1 143 ? 32.081 46.867 19.311  1.00 18.23  ? 824  ASP B C   1 
ATOM   2798 O O   . ASP B 1 143 ? 32.134 47.364 18.186  1.00 21.31  ? 824  ASP B O   1 
ATOM   2799 C CB  . ASP B 1 143 ? 34.129 45.530 18.685  1.00 20.59  ? 824  ASP B CB  1 
ATOM   2800 C CG  . ASP B 1 143 ? 35.257 44.634 19.166  1.00 19.84  ? 824  ASP B CG  1 
ATOM   2801 O OD1 . ASP B 1 143 ? 35.573 44.663 20.375  1.00 20.05  ? 824  ASP B OD1 1 
ATOM   2802 O OD2 . ASP B 1 143 ? 35.823 43.899 18.333  1.00 22.77  ? 824  ASP B OD2 1 
ATOM   2803 N N   . THR B 1 144 ? 31.146 47.201 20.199  1.00 18.82  ? 825  THR B N   1 
ATOM   2804 C CA  . THR B 1 144 ? 30.201 48.276 19.912  1.00 16.21  ? 825  THR B CA  1 
ATOM   2805 C C   . THR B 1 144 ? 30.832 49.636 20.222  1.00 16.73  ? 825  THR B C   1 
ATOM   2806 O O   . THR B 1 144 ? 31.588 49.780 21.186  1.00 22.46  ? 825  THR B O   1 
ATOM   2807 C CB  . THR B 1 144 ? 28.908 48.087 20.708  1.00 17.77  ? 825  THR B CB  1 
ATOM   2808 O OG1 . THR B 1 144 ? 27.982 49.126 20.370  1.00 17.79  ? 825  THR B OG1 1 
ATOM   2809 C CG2 . THR B 1 144 ? 29.171 48.089 22.210  1.00 14.02  ? 825  THR B CG2 1 
ATOM   2810 N N   . THR B 1 145 ? 30.504 50.638 19.401  1.00 17.46  ? 826  THR B N   1 
ATOM   2811 C CA  . THR B 1 145 ? 31.184 51.934 19.425  1.00 17.98  ? 826  THR B CA  1 
ATOM   2812 C C   . THR B 1 145 ? 30.514 52.898 20.397  1.00 17.72  ? 826  THR B C   1 
ATOM   2813 O O   . THR B 1 145 ? 29.294 53.088 20.354  1.00 19.92  ? 826  THR B O   1 
ATOM   2814 C CB  . THR B 1 145 ? 31.202 52.561 18.026  1.00 19.88  ? 826  THR B CB  1 
ATOM   2815 O OG1 . THR B 1 145 ? 32.057 51.799 17.166  1.00 27.85  ? 826  THR B OG1 1 
ATOM   2816 C CG2 . THR B 1 145 ? 31.693 54.004 18.078  1.00 27.12  ? 826  THR B CG2 1 
ATOM   2817 N N   . VAL B 1 146 ? 31.321 53.526 21.252  1.00 18.42  ? 827  VAL B N   1 
ATOM   2818 C CA  . VAL B 1 146 ? 30.838 54.606 22.108  1.00 21.36  ? 827  VAL B CA  1 
ATOM   2819 C C   . VAL B 1 146 ? 30.501 55.797 21.213  1.00 19.39  ? 827  VAL B C   1 
ATOM   2820 O O   . VAL B 1 146 ? 31.389 56.396 20.601  1.00 19.16  ? 827  VAL B O   1 
ATOM   2821 C CB  . VAL B 1 146 ? 31.875 54.985 23.169  1.00 21.50  ? 827  VAL B CB  1 
ATOM   2822 C CG1 . VAL B 1 146 ? 31.344 56.107 24.066  1.00 16.80  ? 827  VAL B CG1 1 
ATOM   2823 C CG2 . VAL B 1 146 ? 32.252 53.780 23.999  1.00 14.61  ? 827  VAL B CG2 1 
ATOM   2824 N N   . GLU B 1 147 ? 29.220 56.146 21.131  1.00 19.79  ? 828  GLU B N   1 
ATOM   2825 C CA  . GLU B 1 147 ? 28.821 57.263 20.283  1.00 22.90  ? 828  GLU B CA  1 
ATOM   2826 C C   . GLU B 1 147 ? 28.778 58.588 21.033  1.00 22.21  ? 828  GLU B C   1 
ATOM   2827 O O   . GLU B 1 147 ? 29.102 59.633 20.461  1.00 29.69  ? 828  GLU B O   1 
ATOM   2828 C CB  . GLU B 1 147 ? 27.452 56.984 19.662  1.00 28.83  ? 828  GLU B CB  1 
ATOM   2829 C CG  . GLU B 1 147 ? 27.386 55.679 18.910  1.00 33.00  ? 828  GLU B CG  1 
ATOM   2830 C CD  . GLU B 1 147 ? 25.969 55.278 18.564  1.00 39.81  ? 828  GLU B CD  1 
ATOM   2831 O OE1 . GLU B 1 147 ? 25.045 56.094 18.761  1.00 47.75  ? 828  GLU B OE1 1 
ATOM   2832 O OE2 . GLU B 1 147 ? 25.785 54.141 18.093  1.00 39.82  ? 828  GLU B OE2 1 
ATOM   2833 N N   . ILE B 1 148 ? 28.375 58.560 22.300  1.00 25.58  ? 829  ILE B N   1 
ATOM   2834 C CA  . ILE B 1 148 ? 28.192 59.751 23.119  1.00 19.83  ? 829  ILE B CA  1 
ATOM   2835 C C   . ILE B 1 148 ? 28.691 59.426 24.518  1.00 19.19  ? 829  ILE B C   1 
ATOM   2836 O O   . ILE B 1 148 ? 28.566 58.287 24.978  1.00 23.06  ? 829  ILE B O   1 
ATOM   2837 C CB  . ILE B 1 148 ? 26.708 60.197 23.150  1.00 26.50  ? 829  ILE B CB  1 
ATOM   2838 C CG1 . ILE B 1 148 ? 26.229 60.648 21.767  1.00 28.35  ? 829  ILE B CG1 1 
ATOM   2839 C CG2 . ILE B 1 148 ? 26.477 61.305 24.168  1.00 31.97  ? 829  ILE B CG2 1 
ATOM   2840 C CD1 . ILE B 1 148 ? 25.346 59.635 21.059  1.00 31.34  ? 829  ILE B CD1 1 
ATOM   2841 N N   . GLU B 1 149 ? 29.279 60.412 25.189  1.00 18.27  ? 830  GLU B N   1 
ATOM   2842 C CA  . GLU B 1 149 ? 29.625 60.279 26.594  1.00 21.24  ? 830  GLU B CA  1 
ATOM   2843 C C   . GLU B 1 149 ? 28.947 61.386 27.389  1.00 21.44  ? 830  GLU B C   1 
ATOM   2844 O O   . GLU B 1 149 ? 28.744 62.499 26.891  1.00 25.25  ? 830  GLU B O   1 
ATOM   2845 C CB  . GLU B 1 149 ? 31.140 60.328 26.813  1.00 23.61  ? 830  GLU B CB  1 
ATOM   2846 C CG  . GLU B 1 149 ? 31.774 61.641 26.394  1.00 25.20  ? 830  GLU B CG  1 
ATOM   2847 C CD  . GLU B 1 149 ? 33.265 61.685 26.644  1.00 26.09  ? 830  GLU B CD  1 
ATOM   2848 O OE1 . GLU B 1 149 ? 33.780 60.803 27.360  1.00 30.93  ? 830  GLU B OE1 1 
ATOM   2849 O OE2 . GLU B 1 149 ? 33.921 62.609 26.126  1.00 33.94  ? 830  GLU B OE2 1 
ATOM   2850 N N   . GLN B 1 150 ? 28.589 61.068 28.629  1.00 16.72  ? 831  GLN B N   1 
ATOM   2851 C CA  . GLN B 1 150 ? 27.915 62.010 29.511  1.00 28.38  ? 831  GLN B CA  1 
ATOM   2852 C C   . GLN B 1 150 ? 28.642 62.024 30.846  1.00 21.38  ? 831  GLN B C   1 
ATOM   2853 O O   . GLN B 1 150 ? 28.732 60.991 31.517  1.00 15.74  ? 831  GLN B O   1 
ATOM   2854 C CB  . GLN B 1 150 ? 26.441 61.635 29.692  1.00 23.37  ? 831  GLN B CB  1 
ATOM   2855 C CG  . GLN B 1 150 ? 25.646 61.528 28.392  1.00 34.56  ? 831  GLN B CG  1 
ATOM   2856 C CD  . GLN B 1 150 ? 25.237 62.875 27.814  1.00 39.58  ? 831  GLN B CD  1 
ATOM   2857 O OE1 . GLN B 1 150 ? 26.079 63.672 27.380  1.00 40.26  ? 831  GLN B OE1 1 
ATOM   2858 N NE2 . GLN B 1 150 ? 23.933 63.131 27.796  1.00 39.75  ? 831  GLN B NE2 1 
ATOM   2859 N N   . LYS B 1 151 ? 29.156 63.188 31.228  1.00 19.21  ? 832  LYS B N   1 
ATOM   2860 C CA  . LYS B 1 151 ? 29.886 63.343 32.481  1.00 21.21  ? 832  LYS B CA  1 
ATOM   2861 C C   . LYS B 1 151 ? 28.892 63.697 33.578  1.00 22.00  ? 832  LYS B C   1 
ATOM   2862 O O   . LYS B 1 151 ? 28.323 64.795 33.582  1.00 20.44  ? 832  LYS B O   1 
ATOM   2863 C CB  . LYS B 1 151 ? 30.960 64.420 32.356  1.00 19.98  ? 832  LYS B CB  1 
ATOM   2864 C CG  . LYS B 1 151 ? 31.766 64.640 33.618  1.00 22.61  ? 832  LYS B CG  1 
ATOM   2865 C CD  . LYS B 1 151 ? 32.919 65.581 33.346  1.00 25.26  ? 832  LYS B CD  1 
ATOM   2866 C CE  . LYS B 1 151 ? 33.739 65.849 34.589  1.00 26.64  ? 832  LYS B CE  1 
ATOM   2867 N NZ  . LYS B 1 151 ? 35.000 66.577 34.268  1.00 28.14  ? 832  LYS B NZ  1 
ATOM   2868 N N   . TYR B 1 152 ? 28.687 62.773 34.510  1.00 18.79  ? 833  TYR B N   1 
ATOM   2869 C CA  . TYR B 1 152 ? 27.749 62.998 35.600  1.00 24.92  ? 833  TYR B CA  1 
ATOM   2870 C C   . TYR B 1 152 ? 28.426 63.523 36.856  1.00 27.18  ? 833  TYR B C   1 
ATOM   2871 O O   . TYR B 1 152 ? 27.782 64.202 37.663  1.00 22.71  ? 833  TYR B O   1 
ATOM   2872 C CB  . TYR B 1 152 ? 27.011 61.702 35.923  1.00 22.62  ? 833  TYR B CB  1 
ATOM   2873 C CG  . TYR B 1 152 ? 26.068 61.250 34.840  1.00 31.37  ? 833  TYR B CG  1 
ATOM   2874 C CD1 . TYR B 1 152 ? 26.517 60.474 33.784  1.00 27.92  ? 833  TYR B CD1 1 
ATOM   2875 C CD2 . TYR B 1 152 ? 24.724 61.598 34.876  1.00 32.19  ? 833  TYR B CD2 1 
ATOM   2876 C CE1 . TYR B 1 152 ? 25.653 60.055 32.789  1.00 36.56  ? 833  TYR B CE1 1 
ATOM   2877 C CE2 . TYR B 1 152 ? 23.851 61.183 33.887  1.00 33.67  ? 833  TYR B CE2 1 
ATOM   2878 C CZ  . TYR B 1 152 ? 24.320 60.412 32.846  1.00 37.49  ? 833  TYR B CZ  1 
ATOM   2879 O OH  . TYR B 1 152 ? 23.456 59.996 31.856  1.00 38.70  ? 833  TYR B OH  1 
ATOM   2880 N N   . ALA B 1 153 ? 29.705 63.212 37.036  1.00 18.17  ? 834  ALA B N   1 
ATOM   2881 C CA  . ALA B 1 153 ? 30.496 63.656 38.176  1.00 21.83  ? 834  ALA B CA  1 
ATOM   2882 C C   . ALA B 1 153 ? 31.952 63.459 37.785  1.00 16.15  ? 834  ALA B C   1 
ATOM   2883 O O   . ALA B 1 153 ? 32.244 62.874 36.740  1.00 17.49  ? 834  ALA B O   1 
ATOM   2884 C CB  . ALA B 1 153 ? 30.121 62.888 39.447  1.00 20.20  ? 834  ALA B CB  1 
ATOM   2885 N N   . ASN B 1 154 ? 32.873 63.965 38.610  1.00 22.66  ? 835  ASN B N   1 
ATOM   2886 C CA  . ASN B 1 154 ? 34.286 63.824 38.268  1.00 17.28  ? 835  ASN B CA  1 
ATOM   2887 C C   . ASN B 1 154 ? 34.633 62.352 38.071  1.00 19.25  ? 835  ASN B C   1 
ATOM   2888 O O   . ASN B 1 154 ? 34.371 61.514 38.941  1.00 17.50  ? 835  ASN B O   1 
ATOM   2889 C CB  . ASN B 1 154 ? 35.194 64.459 39.324  1.00 27.87  ? 835  ASN B CB  1 
ATOM   2890 C CG  . ASN B 1 154 ? 34.779 64.135 40.739  1.00 31.06  ? 835  ASN B CG  1 
ATOM   2891 O OD1 . ASN B 1 154 ? 33.930 63.277 40.976  1.00 41.15  ? 835  ASN B OD1 1 
ATOM   2892 N ND2 . ASN B 1 154 ? 35.383 64.831 41.699  1.00 42.27  ? 835  ASN B ND2 1 
ATOM   2893 N N   . ASN B 1 155 ? 35.175 62.047 36.890  1.00 16.72  ? 836  ASN B N   1 
ATOM   2894 C CA  . ASN B 1 155 ? 35.596 60.711 36.494  1.00 14.63  ? 836  ASN B CA  1 
ATOM   2895 C C   . ASN B 1 155 ? 34.458 59.708 36.551  1.00 13.73  ? 836  ASN B C   1 
ATOM   2896 O O   . ASN B 1 155 ? 34.701 58.511 36.674  1.00 13.19  ? 836  ASN B O   1 
ATOM   2897 C CB  . ASN B 1 155 ? 36.766 60.224 37.352  1.00 14.91  ? 836  ASN B CB  1 
ATOM   2898 C CG  . ASN B 1 155 ? 37.834 61.273 37.504  1.00 16.01  ? 836  ASN B CG  1 
ATOM   2899 O OD1 . ASN B 1 155 ? 38.151 61.691 38.618  1.00 16.63  ? 836  ASN B OD1 1 
ATOM   2900 N ND2 . ASN B 1 155 ? 38.384 61.718 36.385  1.00 16.42  ? 836  ASN B ND2 1 
ATOM   2901 N N   . THR B 1 156 ? 33.211 60.171 36.471  1.00 14.08  ? 837  THR B N   1 
ATOM   2902 C CA  . THR B 1 156 ? 32.039 59.292 36.511  1.00 13.96  ? 837  THR B CA  1 
ATOM   2903 C C   . THR B 1 156 ? 31.231 59.544 35.242  1.00 16.19  ? 837  THR B C   1 
ATOM   2904 O O   . THR B 1 156 ? 30.531 60.556 35.140  1.00 16.43  ? 837  THR B O   1 
ATOM   2905 C CB  . THR B 1 156 ? 31.203 59.556 37.758  1.00 16.26  ? 837  THR B CB  1 
ATOM   2906 O OG1 . THR B 1 156 ? 32.049 59.532 38.913  1.00 17.52  ? 837  THR B OG1 1 
ATOM   2907 C CG2 . THR B 1 156 ? 30.114 58.506 37.909  1.00 17.68  ? 837  THR B CG2 1 
ATOM   2908 N N   . TYR B 1 157 ? 31.329 58.629 34.281  1.00 13.57  ? 838  TYR B N   1 
ATOM   2909 C CA  . TYR B 1 157 ? 30.785 58.824 32.945  1.00 13.01  ? 838  TYR B CA  1 
ATOM   2910 C C   . TYR B 1 157 ? 29.739 57.777 32.600  1.00 19.07  ? 838  TYR B C   1 
ATOM   2911 O O   . TYR B 1 157 ? 29.890 56.594 32.926  1.00 13.65  ? 838  TYR B O   1 
ATOM   2912 C CB  . TYR B 1 157 ? 31.895 58.768 31.891  1.00 13.20  ? 838  TYR B CB  1 
ATOM   2913 C CG  . TYR B 1 157 ? 32.720 60.026 31.818  1.00 15.43  ? 838  TYR B CG  1 
ATOM   2914 C CD1 . TYR B 1 157 ? 33.850 60.188 32.606  1.00 14.86  ? 838  TYR B CD1 1 
ATOM   2915 C CD2 . TYR B 1 157 ? 32.371 61.048 30.952  1.00 17.72  ? 838  TYR B CD2 1 
ATOM   2916 C CE1 . TYR B 1 157 ? 34.607 61.344 32.537  1.00 19.35  ? 838  TYR B CE1 1 
ATOM   2917 C CE2 . TYR B 1 157 ? 33.121 62.203 30.877  1.00 26.83  ? 838  TYR B CE2 1 
ATOM   2918 C CZ  . TYR B 1 157 ? 34.232 62.345 31.672  1.00 20.07  ? 838  TYR B CZ  1 
ATOM   2919 O OH  . TYR B 1 157 ? 34.970 63.494 31.586  1.00 23.69  ? 838  TYR B OH  1 
ATOM   2920 N N   . GLY B 1 158 ? 28.700 58.213 31.901  1.00 14.65  ? 839  GLY B N   1 
ATOM   2921 C CA  . GLY B 1 158 ? 27.840 57.312 31.169  1.00 12.98  ? 839  GLY B CA  1 
ATOM   2922 C C   . GLY B 1 158 ? 28.221 57.345 29.703  1.00 13.44  ? 839  GLY B C   1 
ATOM   2923 O O   . GLY B 1 158 ? 28.701 58.353 29.193  1.00 15.35  ? 839  GLY B O   1 
ATOM   2924 N N   . VAL B 1 159 ? 28.030 56.222 29.030  1.00 13.08  ? 840  VAL B N   1 
ATOM   2925 C CA  . VAL B 1 159 ? 28.360 56.120 27.618  1.00 14.90  ? 840  VAL B CA  1 
ATOM   2926 C C   . VAL B 1 159 ? 27.151 55.554 26.894  1.00 21.06  ? 840  VAL B C   1 
ATOM   2927 O O   . VAL B 1 159 ? 26.343 54.826 27.474  1.00 15.82  ? 840  VAL B O   1 
ATOM   2928 C CB  . VAL B 1 159 ? 29.614 55.249 27.368  1.00 15.51  ? 840  VAL B CB  1 
ATOM   2929 C CG1 . VAL B 1 159 ? 30.858 55.930 27.928  1.00 13.07  ? 840  VAL B CG1 1 
ATOM   2930 C CG2 . VAL B 1 159 ? 29.441 53.857 27.963  1.00 12.35  ? 840  VAL B CG2 1 
ATOM   2931 N N   . GLN B 1 160 ? 27.016 55.914 25.625  1.00 23.30  ? 841  GLN B N   1 
ATOM   2932 C CA  . GLN B 1 160 ? 25.920 55.440 24.797  1.00 20.63  ? 841  GLN B CA  1 
ATOM   2933 C C   . GLN B 1 160 ? 26.497 54.660 23.627  1.00 17.99  ? 841  GLN B C   1 
ATOM   2934 O O   . GLN B 1 160 ? 27.475 55.092 23.008  1.00 22.00  ? 841  GLN B O   1 
ATOM   2935 C CB  . GLN B 1 160 ? 25.048 56.605 24.316  1.00 21.09  ? 841  GLN B CB  1 
ATOM   2936 C CG  . GLN B 1 160 ? 24.329 57.310 25.455  1.00 29.07  ? 841  GLN B CG  1 
ATOM   2937 C CD  . GLN B 1 160 ? 23.237 58.251 24.982  1.00 42.34  ? 841  GLN B CD  1 
ATOM   2938 O OE1 . GLN B 1 160 ? 22.938 58.331 23.790  1.00 44.89  ? 841  GLN B OE1 1 
ATOM   2939 N NE2 . GLN B 1 160 ? 22.632 58.969 25.922  1.00 43.20  ? 841  GLN B NE2 1 
ATOM   2940 N N   . TYR B 1 161 ? 25.906 53.499 23.355  1.00 15.89  ? 842  TYR B N   1 
ATOM   2941 C CA  . TYR B 1 161 ? 26.331 52.615 22.280  1.00 17.51  ? 842  TYR B CA  1 
ATOM   2942 C C   . TYR B 1 161 ? 25.122 51.795 21.852  1.00 19.24  ? 842  TYR B C   1 
ATOM   2943 O O   . TYR B 1 161 ? 24.149 51.666 22.597  1.00 18.42  ? 842  TYR B O   1 
ATOM   2944 C CB  . TYR B 1 161 ? 27.484 51.705 22.725  1.00 15.00  ? 842  TYR B CB  1 
ATOM   2945 C CG  . TYR B 1 161 ? 27.233 51.045 24.060  1.00 15.97  ? 842  TYR B CG  1 
ATOM   2946 C CD1 . TYR B 1 161 ? 26.446 49.910 24.154  1.00 13.40  ? 842  TYR B CD1 1 
ATOM   2947 C CD2 . TYR B 1 161 ? 27.764 51.571 25.232  1.00 15.34  ? 842  TYR B CD2 1 
ATOM   2948 C CE1 . TYR B 1 161 ? 26.203 49.307 25.368  1.00 12.44  ? 842  TYR B CE1 1 
ATOM   2949 C CE2 . TYR B 1 161 ? 27.525 50.972 26.457  1.00 12.09  ? 842  TYR B CE2 1 
ATOM   2950 C CZ  . TYR B 1 161 ? 26.738 49.842 26.514  1.00 11.77  ? 842  TYR B CZ  1 
ATOM   2951 O OH  . TYR B 1 161 ? 26.495 49.227 27.724  1.00 12.85  ? 842  TYR B OH  1 
ATOM   2952 N N   . GLN B 1 162 ? 25.187 51.241 20.647  1.00 19.58  ? 843  GLN B N   1 
ATOM   2953 C CA  . GLN B 1 162 ? 24.055 50.485 20.126  1.00 25.14  ? 843  GLN B CA  1 
ATOM   2954 C C   . GLN B 1 162 ? 24.087 49.040 20.609  1.00 21.00  ? 843  GLN B C   1 
ATOM   2955 O O   . GLN B 1 162 ? 25.151 48.464 20.854  1.00 27.01  ? 843  GLN B O   1 
ATOM   2956 C CB  . GLN B 1 162 ? 24.044 50.505 18.596  1.00 25.40  ? 843  GLN B CB  1 
ATOM   2957 C CG  . GLN B 1 162 ? 23.821 51.872 17.975  1.00 41.64  ? 843  GLN B CG  1 
ATOM   2958 C CD  . GLN B 1 162 ? 22.433 52.447 18.230  1.00 49.73  ? 843  GLN B CD  1 
ATOM   2959 O OE1 . GLN B 1 162 ? 21.536 51.759 18.726  1.00 64.48  ? 843  GLN B OE1 1 
ATOM   2960 N NE2 . GLN B 1 162 ? 22.250 53.717 17.881  1.00 41.51  ? 843  GLN B NE2 1 
ATOM   2961 N N   . GLY B 1 163 ? 22.901 48.449 20.742  1.00 23.68  ? 844  GLY B N   1 
ATOM   2962 C CA  . GLY B 1 163 ? 22.832 47.026 21.013  1.00 26.41  ? 844  GLY B CA  1 
ATOM   2963 C C   . GLY B 1 163 ? 21.930 46.586 22.147  1.00 22.10  ? 844  GLY B C   1 
ATOM   2964 O O   . GLY B 1 163 ? 21.346 45.499 22.084  1.00 23.95  ? 844  GLY B O   1 
ATOM   2965 N N   . GLY B 1 164 ? 21.800 47.407 23.185  1.00 24.38  ? 845  GLY B N   1 
ATOM   2966 C CA  . GLY B 1 164 ? 21.075 46.981 24.367  1.00 22.67  ? 845  GLY B CA  1 
ATOM   2967 C C   . GLY B 1 164 ? 19.571 46.937 24.158  1.00 25.83  ? 845  GLY B C   1 
ATOM   2968 O O   . GLY B 1 164 ? 18.994 47.703 23.387  1.00 23.72  ? 845  GLY B O   1 
ATOM   2969 N N   . LYS B 1 165 ? 18.934 45.997 24.856  1.00 22.60  ? 846  LYS B N   1 
ATOM   2970 C CA  . LYS B 1 165 ? 17.485 45.918 24.952  1.00 16.99  ? 846  LYS B CA  1 
ATOM   2971 C C   . LYS B 1 165 ? 17.121 45.613 26.397  1.00 20.96  ? 846  LYS B C   1 
ATOM   2972 O O   . LYS B 1 165 ? 17.990 45.363 27.237  1.00 19.36  ? 846  LYS B O   1 
ATOM   2973 C CB  . LYS B 1 165 ? 16.907 44.863 24.001  1.00 29.59  ? 846  LYS B CB  1 
ATOM   2974 C CG  . LYS B 1 165 ? 17.105 45.189 22.532  1.00 33.01  ? 846  LYS B CG  1 
ATOM   2975 C CD  . LYS B 1 165 ? 16.259 44.296 21.645  1.00 44.99  ? 846  LYS B CD  1 
ATOM   2976 C CE  . LYS B 1 165 ? 16.561 44.541 20.173  1.00 57.69  ? 846  LYS B CE  1 
ATOM   2977 N NZ  . LYS B 1 165 ? 17.975 44.202 19.832  1.00 56.75  ? 846  LYS B NZ  1 
ATOM   2978 N N   . ALA B 1 166 ? 15.821 45.644 26.686  1.00 23.72  ? 847  ALA B N   1 
ATOM   2979 C CA  . ALA B 1 166 ? 15.339 45.355 28.032  1.00 28.03  ? 847  ALA B CA  1 
ATOM   2980 C C   . ALA B 1 166 ? 15.876 44.015 28.523  1.00 19.57  ? 847  ALA B C   1 
ATOM   2981 O O   . ALA B 1 166 ? 15.949 43.044 27.766  1.00 23.39  ? 847  ALA B O   1 
ATOM   2982 C CB  . ALA B 1 166 ? 13.810 45.344 28.051  1.00 32.90  ? 847  ALA B CB  1 
ATOM   2983 N N   . GLY B 1 167 ? 16.260 43.972 29.800  1.00 15.40  ? 848  GLY B N   1 
ATOM   2984 C CA  . GLY B 1 167 ? 16.839 42.799 30.412  1.00 14.59  ? 848  GLY B CA  1 
ATOM   2985 C C   . GLY B 1 167 ? 18.354 42.788 30.444  1.00 14.63  ? 848  GLY B C   1 
ATOM   2986 O O   . GLY B 1 167 ? 18.939 42.063 31.256  1.00 12.77  ? 848  GLY B O   1 
ATOM   2987 N N   . MET B 1 168 ? 19.004 43.572 29.589  1.00 13.08  ? 849  MET B N   1 
ATOM   2988 C CA  . MET B 1 168 ? 20.461 43.603 29.573  1.00 12.11  ? 849  MET B CA  1 
ATOM   2989 C C   . MET B 1 168 ? 21.056 44.474 30.669  1.00 13.40  ? 849  MET B C   1 
ATOM   2990 O O   . MET B 1 168 ? 22.267 44.378 30.922  1.00 13.50  ? 849  MET B O   1 
ATOM   2991 C CB  . MET B 1 168 ? 20.958 44.091 28.213  1.00 15.37  ? 849  MET B CB  1 
ATOM   2992 C CG  . MET B 1 168 ? 22.406 43.730 27.919  1.00 18.33  ? 849  MET B CG  1 
ATOM   2993 S SD  . MET B 1 168 ? 22.751 43.825 26.154  1.00 26.92  ? 849  MET B SD  1 
ATOM   2994 C CE  . MET B 1 168 ? 24.385 43.092 26.141  1.00 22.80  ? 849  MET B CE  1 
ATOM   2995 N N   . SER B 1 169 ? 20.263 45.327 31.319  1.00 12.08  ? 850  SER B N   1 
ATOM   2996 C CA  A SER B 1 169 ? 20.825 46.206 32.335  0.70 15.86  ? 850  SER B CA  1 
ATOM   2997 C CA  B SER B 1 169 ? 20.812 46.205 32.343  0.30 15.90  ? 850  SER B CA  1 
ATOM   2998 C C   . SER B 1 169 ? 21.429 45.377 33.462  1.00 15.16  ? 850  SER B C   1 
ATOM   2999 O O   . SER B 1 169 ? 20.835 44.392 33.926  1.00 13.54  ? 850  SER B O   1 
ATOM   3000 C CB  A SER B 1 169 ? 19.763 47.166 32.871  0.70 21.28  ? 850  SER B CB  1 
ATOM   3001 C CB  B SER B 1 169 ? 19.728 47.128 32.894  0.30 21.22  ? 850  SER B CB  1 
ATOM   3002 O OG  A SER B 1 169 ? 18.702 46.466 33.488  0.70 27.08  ? 850  SER B OG  1 
ATOM   3003 O OG  B SER B 1 169 ? 19.249 48.005 31.890  0.30 20.14  ? 850  SER B OG  1 
ATOM   3004 N N   . GLY B 1 170 ? 22.623 45.774 33.884  1.00 11.90  ? 851  GLY B N   1 
ATOM   3005 C CA  . GLY B 1 170 ? 23.400 45.016 34.831  1.00 10.25  ? 851  GLY B CA  1 
ATOM   3006 C C   . GLY B 1 170 ? 24.425 44.107 34.189  1.00 9.92   ? 851  GLY B C   1 
ATOM   3007 O O   . GLY B 1 170 ? 25.257 43.549 34.902  1.00 9.88   ? 851  GLY B O   1 
ATOM   3008 N N   . GLY B 1 171 ? 24.383 43.944 32.871  1.00 9.89   ? 852  GLY B N   1 
ATOM   3009 C CA  . GLY B 1 171 ? 25.409 43.190 32.192  1.00 10.80  ? 852  GLY B CA  1 
ATOM   3010 C C   . GLY B 1 171 ? 26.744 43.911 32.190  1.00 11.09  ? 852  GLY B C   1 
ATOM   3011 O O   . GLY B 1 171 ? 26.828 45.139 32.276  1.00 12.90  ? 852  GLY B O   1 
ATOM   3012 N N   . GLY B 1 172 ? 27.810 43.125 32.079  1.00 11.15  ? 853  GLY B N   1 
ATOM   3013 C CA  . GLY B 1 172 ? 29.152 43.674 32.228  1.00 9.59   ? 853  GLY B CA  1 
ATOM   3014 C C   . GLY B 1 172 ? 29.658 44.324 30.951  1.00 12.34  ? 853  GLY B C   1 
ATOM   3015 O O   . GLY B 1 172 ? 29.443 43.828 29.845  1.00 9.88   ? 853  GLY B O   1 
ATOM   3016 N N   . ILE B 1 173 ? 30.310 45.476 31.121  1.00 10.03  ? 854  ILE B N   1 
ATOM   3017 C CA  . ILE B 1 173 ? 31.104 46.100 30.072  1.00 15.27  ? 854  ILE B CA  1 
ATOM   3018 C C   . ILE B 1 173 ? 32.558 45.739 30.323  1.00 10.68  ? 854  ILE B C   1 
ATOM   3019 O O   . ILE B 1 173 ? 33.058 45.917 31.440  1.00 10.72  ? 854  ILE B O   1 
ATOM   3020 C CB  . ILE B 1 173 ? 30.929 47.628 30.049  1.00 9.86   ? 854  ILE B CB  1 
ATOM   3021 C CG1 . ILE B 1 173 ? 29.457 48.013 29.929  1.00 11.21  ? 854  ILE B CG1 1 
ATOM   3022 C CG2 . ILE B 1 173 ? 31.729 48.210 28.893  1.00 10.38  ? 854  ILE B CG2 1 
ATOM   3023 C CD1 . ILE B 1 173 ? 29.237 49.516 29.934  1.00 12.23  ? 854  ILE B CD1 1 
ATOM   3024 N N   . PHE B 1 174 ? 33.235 45.236 29.292  1.00 11.89  ? 855  PHE B N   1 
ATOM   3025 C CA  . PHE B 1 174 ? 34.580 44.689 29.418  1.00 13.77  ? 855  PHE B CA  1 
ATOM   3026 C C   . PHE B 1 174 ? 35.551 45.440 28.513  1.00 13.60  ? 855  PHE B C   1 
ATOM   3027 O O   . PHE B 1 174 ? 35.197 45.843 27.402  1.00 16.50  ? 855  PHE B O   1 
ATOM   3028 C CB  . PHE B 1 174 ? 34.623 43.191 29.043  1.00 15.09  ? 855  PHE B CB  1 
ATOM   3029 C CG  . PHE B 1 174 ? 33.822 42.292 29.948  1.00 11.69  ? 855  PHE B CG  1 
ATOM   3030 C CD1 . PHE B 1 174 ? 32.432 42.273 29.884  1.00 11.05  ? 855  PHE B CD1 1 
ATOM   3031 C CD2 . PHE B 1 174 ? 34.451 41.440 30.831  1.00 12.27  ? 855  PHE B CD2 1 
ATOM   3032 C CE1 . PHE B 1 174 ? 31.694 41.412 30.700  1.00 16.24  ? 855  PHE B CE1 1 
ATOM   3033 C CE2 . PHE B 1 174 ? 33.723 40.590 31.651  1.00 14.25  ? 855  PHE B CE2 1 
ATOM   3034 C CZ  . PHE B 1 174 ? 32.338 40.575 31.581  1.00 12.01  ? 855  PHE B CZ  1 
ATOM   3035 N N   . ASN B 1 175 ? 36.791 45.597 28.980  1.00 18.59  ? 856  ASN B N   1 
ATOM   3036 C CA  . ASN B 1 175 ? 37.852 46.128 28.137  1.00 17.51  ? 856  ASN B CA  1 
ATOM   3037 C C   . ASN B 1 175 ? 38.464 45.008 27.289  1.00 20.49  ? 856  ASN B C   1 
ATOM   3038 O O   . ASN B 1 175 ? 38.024 43.855 27.320  1.00 18.49  ? 856  ASN B O   1 
ATOM   3039 C CB  . ASN B 1 175 ? 38.915 46.839 28.980  1.00 18.75  ? 856  ASN B CB  1 
ATOM   3040 C CG  . ASN B 1 175 ? 39.604 45.915 29.975  1.00 25.58  ? 856  ASN B CG  1 
ATOM   3041 O OD1 . ASN B 1 175 ? 39.533 44.686 29.867  1.00 17.24  ? 856  ASN B OD1 1 
ATOM   3042 N ND2 . ASN B 1 175 ? 40.268 46.508 30.962  1.00 16.53  ? 856  ASN B ND2 1 
ATOM   3043 N N   . SER B 1 176 ? 39.509 45.358 26.530  1.00 20.16  ? 857  SER B N   1 
ATOM   3044 C CA  A SER B 1 176 ? 40.164 44.414 25.628  0.70 25.32  ? 857  SER B CA  1 
ATOM   3045 C CA  B SER B 1 176 ? 40.136 44.399 25.627  0.30 25.25  ? 857  SER B CA  1 
ATOM   3046 C C   . SER B 1 176 ? 40.798 43.241 26.363  1.00 25.78  ? 857  SER B C   1 
ATOM   3047 O O   . SER B 1 176 ? 41.073 42.206 25.742  1.00 22.10  ? 857  SER B O   1 
ATOM   3048 C CB  A SER B 1 176 ? 41.239 45.132 24.809  0.70 27.86  ? 857  SER B CB  1 
ATOM   3049 C CB  B SER B 1 176 ? 41.165 45.106 24.743  0.30 27.77  ? 857  SER B CB  1 
ATOM   3050 O OG  A SER B 1 176 ? 40.737 46.327 24.239  0.70 35.07  ? 857  SER B OG  1 
ATOM   3051 O OG  B SER B 1 176 ? 42.161 45.736 25.527  0.30 19.03  ? 857  SER B OG  1 
ATOM   3052 N N   . LYS B 1 177 ? 41.056 43.382 27.658  1.00 25.46  ? 858  LYS B N   1 
ATOM   3053 C CA  . LYS B 1 177 ? 41.688 42.330 28.439  1.00 29.20  ? 858  LYS B CA  1 
ATOM   3054 C C   . LYS B 1 177 ? 40.686 41.399 29.112  1.00 23.46  ? 858  LYS B C   1 
ATOM   3055 O O   . LYS B 1 177 ? 41.098 40.480 29.831  1.00 20.98  ? 858  LYS B O   1 
ATOM   3056 C CB  . LYS B 1 177 ? 42.614 42.952 29.487  1.00 21.89  ? 858  LYS B CB  1 
ATOM   3057 C CG  . LYS B 1 177 ? 43.847 43.593 28.884  1.00 40.41  ? 858  LYS B CG  1 
ATOM   3058 C CD  . LYS B 1 177 ? 44.745 44.205 29.943  1.00 32.04  ? 858  LYS B CD  1 
ATOM   3059 C CE  . LYS B 1 177 ? 44.279 45.597 30.332  1.00 41.99  ? 858  LYS B CE  1 
ATOM   3060 N NZ  . LYS B 1 177 ? 44.355 46.555 29.193  1.00 40.80  ? 858  LYS B NZ  1 
ATOM   3061 N N   . GLY B 1 178 ? 39.390 41.592 28.879  1.00 21.49  ? 859  GLY B N   1 
ATOM   3062 C CA  . GLY B 1 178 ? 38.389 40.783 29.539  1.00 24.50  ? 859  GLY B CA  1 
ATOM   3063 C C   . GLY B 1 178 ? 38.102 41.188 30.963  1.00 17.55  ? 859  GLY B C   1 
ATOM   3064 O O   . GLY B 1 178 ? 37.491 40.410 31.701  1.00 18.21  ? 859  GLY B O   1 
ATOM   3065 N N   . GLU B 1 179 ? 38.531 42.376 31.375  1.00 14.99  ? 860  GLU B N   1 
ATOM   3066 C CA  . GLU B 1 179 ? 38.255 42.898 32.706  1.00 14.92  ? 860  GLU B CA  1 
ATOM   3067 C C   . GLU B 1 179 ? 36.982 43.740 32.687  1.00 15.91  ? 860  GLU B C   1 
ATOM   3068 O O   . GLU B 1 179 ? 36.698 44.421 31.698  1.00 15.31  ? 860  GLU B O   1 
ATOM   3069 C CB  . GLU B 1 179 ? 39.430 43.745 33.193  1.00 15.33  ? 860  GLU B CB  1 
ATOM   3070 C CG  . GLU B 1 179 ? 40.749 42.996 33.264  1.00 17.07  ? 860  GLU B CG  1 
ATOM   3071 C CD  . GLU B 1 179 ? 41.913 43.927 33.507  1.00 21.94  ? 860  GLU B CD  1 
ATOM   3072 O OE1 . GLU B 1 179 ? 41.911 45.033 32.935  1.00 23.25  ? 860  GLU B OE1 1 
ATOM   3073 O OE2 . GLU B 1 179 ? 42.828 43.554 34.270  1.00 36.39  ? 860  GLU B OE2 1 
ATOM   3074 N N   . VAL B 1 180 ? 36.224 43.695 33.783  1.00 13.03  ? 861  VAL B N   1 
ATOM   3075 C CA  . VAL B 1 180 ? 34.986 44.469 33.900  1.00 11.62  ? 861  VAL B CA  1 
ATOM   3076 C C   . VAL B 1 180 ? 35.331 45.924 34.200  1.00 11.49  ? 861  VAL B C   1 
ATOM   3077 O O   . VAL B 1 180 ? 36.004 46.217 35.191  1.00 12.08  ? 861  VAL B O   1 
ATOM   3078 C CB  . VAL B 1 180 ? 34.068 43.907 34.994  1.00 11.62  ? 861  VAL B CB  1 
ATOM   3079 C CG1 . VAL B 1 180 ? 32.882 44.847 35.225  1.00 10.64  ? 861  VAL B CG1 1 
ATOM   3080 C CG2 . VAL B 1 180 ? 33.574 42.516 34.631  1.00 11.58  ? 861  VAL B CG2 1 
ATOM   3081 N N   . ILE B 1 181 ? 34.841 46.834 33.364  1.00 10.98  ? 862  ILE B N   1 
ATOM   3082 C CA  . ILE B 1 181 ? 35.048 48.265 33.569  1.00 10.95  ? 862  ILE B CA  1 
ATOM   3083 C C   . ILE B 1 181 ? 33.750 49.018 33.823  1.00 13.34  ? 862  ILE B C   1 
ATOM   3084 O O   . ILE B 1 181 ? 33.801 50.207 34.181  1.00 13.13  ? 862  ILE B O   1 
ATOM   3085 C CB  . ILE B 1 181 ? 35.798 48.899 32.378  1.00 11.34  ? 862  ILE B CB  1 
ATOM   3086 C CG1 . ILE B 1 181 ? 35.001 48.710 31.087  1.00 11.05  ? 862  ILE B CG1 1 
ATOM   3087 C CG2 . ILE B 1 181 ? 37.199 48.290 32.238  1.00 12.27  ? 862  ILE B CG2 1 
ATOM   3088 C CD1 . ILE B 1 181 ? 35.570 49.449 29.897  1.00 16.75  ? 862  ILE B CD1 1 
ATOM   3089 N N   . GLY B 1 182 ? 32.602 48.377 33.661  1.00 9.91   ? 863  GLY B N   1 
ATOM   3090 C CA  . GLY B 1 182 ? 31.337 49.067 33.783  1.00 12.54  ? 863  GLY B CA  1 
ATOM   3091 C C   . GLY B 1 182 ? 30.175 48.110 33.645  1.00 17.30  ? 863  GLY B C   1 
ATOM   3092 O O   . GLY B 1 182 ? 30.349 46.889 33.621  1.00 11.07  ? 863  GLY B O   1 
ATOM   3093 N N   . LEU B 1 183 ? 28.981 48.694 33.538  1.00 13.56  ? 864  LEU B N   1 
ATOM   3094 C CA  . LEU B 1 183 ? 27.716 47.970 33.531  1.00 12.43  ? 864  LEU B CA  1 
ATOM   3095 C C   . LEU B 1 183 ? 26.788 48.542 32.475  1.00 15.21  ? 864  LEU B C   1 
ATOM   3096 O O   . LEU B 1 183 ? 26.673 49.761 32.350  1.00 14.20  ? 864  LEU B O   1 
ATOM   3097 C CB  . LEU B 1 183 ? 26.976 48.086 34.864  1.00 18.51  ? 864  LEU B CB  1 
ATOM   3098 C CG  . LEU B 1 183 ? 27.542 47.581 36.173  1.00 24.27  ? 864  LEU B CG  1 
ATOM   3099 C CD1 . LEU B 1 183 ? 27.011 48.477 37.259  1.00 31.59  ? 864  LEU B CD1 1 
ATOM   3100 C CD2 . LEU B 1 183 ? 27.059 46.190 36.393  1.00 22.95  ? 864  LEU B CD2 1 
ATOM   3101 N N   . HIS B 1 184 ? 26.091 47.668 31.757  1.00 17.25  ? 865  HIS B N   1 
ATOM   3102 C CA  . HIS B 1 184 ? 25.035 48.120 30.862  1.00 16.95  ? 865  HIS B CA  1 
ATOM   3103 C C   . HIS B 1 184 ? 23.886 48.717 31.660  1.00 14.54  ? 865  HIS B C   1 
ATOM   3104 O O   . HIS B 1 184 ? 23.507 48.195 32.713  1.00 14.40  ? 865  HIS B O   1 
ATOM   3105 C CB  . HIS B 1 184 ? 24.512 46.967 30.003  1.00 12.46  ? 865  HIS B CB  1 
ATOM   3106 C CG  . HIS B 1 184 ? 23.569 47.414 28.931  1.00 14.52  ? 865  HIS B CG  1 
ATOM   3107 N ND1 . HIS B 1 184 ? 24.008 47.927 27.729  1.00 14.51  ? 865  HIS B ND1 1 
ATOM   3108 C CD2 . HIS B 1 184 ? 22.214 47.451 28.885  1.00 12.64  ? 865  HIS B CD2 1 
ATOM   3109 C CE1 . HIS B 1 184 ? 22.963 48.244 26.983  1.00 18.02  ? 865  HIS B CE1 1 
ATOM   3110 N NE2 . HIS B 1 184 ? 21.864 47.969 27.663  1.00 12.86  ? 865  HIS B NE2 1 
ATOM   3111 N N   . GLN B 1 185 ? 23.327 49.819 31.153  1.00 17.86  ? 866  GLN B N   1 
ATOM   3112 C CA  . GLN B 1 185 ? 22.162 50.460 31.763  1.00 22.76  ? 866  GLN B CA  1 
ATOM   3113 C C   . GLN B 1 185 ? 21.230 50.943 30.661  1.00 27.35  ? 866  GLN B C   1 
ATOM   3114 O O   . GLN B 1 185 ? 21.525 51.938 29.992  1.00 42.93  ? 866  GLN B O   1 
ATOM   3115 C CB  . GLN B 1 185 ? 22.574 51.622 32.667  1.00 30.65  ? 866  GLN B CB  1 
ATOM   3116 C CG  . GLN B 1 185 ? 23.113 51.188 34.012  1.00 31.43  ? 866  GLN B CG  1 
ATOM   3117 C CD  . GLN B 1 185 ? 23.635 52.343 34.839  1.00 36.92  ? 866  GLN B CD  1 
ATOM   3118 O OE1 . GLN B 1 185 ? 24.096 53.345 34.301  1.00 41.98  ? 866  GLN B OE1 1 
ATOM   3119 N NE2 . GLN B 1 185 ? 23.573 52.203 36.159  1.00 34.47  ? 866  GLN B NE2 1 
ATOM   3120 N N   . ASN B 1 186 ? 20.110 50.251 30.472  1.00 37.80  ? 867  ASN B N   1 
ATOM   3121 C CA  . ASN B 1 186 ? 19.082 50.734 29.558  1.00 51.82  ? 867  ASN B CA  1 
ATOM   3122 C C   . ASN B 1 186 ? 18.438 51.990 30.131  1.00 62.11  ? 867  ASN B C   1 
ATOM   3123 O O   . ASN B 1 186 ? 17.878 51.961 31.232  1.00 69.70  ? 867  ASN B O   1 
ATOM   3124 C CB  . ASN B 1 186 ? 18.019 49.664 29.321  1.00 49.74  ? 867  ASN B CB  1 
ATOM   3125 C CG  . ASN B 1 186 ? 18.498 48.553 28.413  1.00 51.89  ? 867  ASN B CG  1 
ATOM   3126 O OD1 . ASN B 1 186 ? 19.181 48.794 27.414  1.00 45.88  ? 867  ASN B OD1 1 
ATOM   3127 N ND2 . ASN B 1 186 ? 18.137 47.322 28.756  1.00 42.21  ? 867  ASN B ND2 1 
ATOM   3128 N N   . GLY B 1 187 ? 18.514 53.090 29.388  1.00 50.14  ? 868  GLY B N   1 
ATOM   3129 C CA  . GLY B 1 187 ? 17.871 54.318 29.795  1.00 59.21  ? 868  GLY B CA  1 
ATOM   3130 C C   . GLY B 1 187 ? 16.399 54.344 29.431  1.00 63.21  ? 868  GLY B C   1 
ATOM   3131 O O   . GLY B 1 187 ? 15.826 53.378 28.926  1.00 55.94  ? 868  GLY B O   1 
ATOM   3132 N N   . ALA B 1 188 ? 15.778 55.489 29.704  1.00 75.58  ? 869  ALA B N   1 
ATOM   3133 C CA  . ALA B 1 188 ? 14.386 55.697 29.335  1.00 63.41  ? 869  ALA B CA  1 
ATOM   3134 C C   . ALA B 1 188 ? 14.237 55.730 27.819  1.00 61.00  ? 869  ALA B C   1 
ATOM   3135 O O   . ALA B 1 188 ? 15.154 56.121 27.090  1.00 61.40  ? 869  ALA B O   1 
ATOM   3136 C CB  . ALA B 1 188 ? 13.859 56.996 29.944  1.00 55.96  ? 869  ALA B CB  1 
ATOM   3137 N N   . GLU B 1 189 ? 13.059 55.313 27.348  1.00 62.30  ? 870  GLU B N   1 
ATOM   3138 C CA  . GLU B 1 189 ? 12.772 55.178 25.919  1.00 65.35  ? 870  GLU B CA  1 
ATOM   3139 C C   . GLU B 1 189 ? 13.736 54.209 25.240  1.00 69.49  ? 870  GLU B C   1 
ATOM   3140 O O   . GLU B 1 189 ? 14.084 54.385 24.069  1.00 73.70  ? 870  GLU B O   1 
ATOM   3141 C CB  . GLU B 1 189 ? 12.785 56.536 25.209  1.00 59.31  ? 870  GLU B CB  1 
ATOM   3142 C CG  . GLU B 1 189 ? 11.596 57.424 25.539  1.00 56.79  ? 870  GLU B CG  1 
ATOM   3143 C CD  . GLU B 1 189 ? 10.275 56.840 25.064  1.00 74.21  ? 870  GLU B CD  1 
ATOM   3144 O OE1 . GLU B 1 189 ? 10.283 56.002 24.134  1.00 70.07  ? 870  GLU B OE1 1 
ATOM   3145 O OE2 . GLU B 1 189 ? 9.224  57.219 25.624  1.00 77.34  ? 870  GLU B OE2 1 
ATOM   3146 N N   . ASN B 1 190 ? 14.169 53.184 25.978  1.00 76.12  ? 871  ASN B N   1 
ATOM   3147 C CA  . ASN B 1 190 ? 15.069 52.150 25.463  1.00 78.44  ? 871  ASN B CA  1 
ATOM   3148 C C   . ASN B 1 190 ? 16.359 52.751 24.906  1.00 79.73  ? 871  ASN B C   1 
ATOM   3149 O O   . ASN B 1 190 ? 16.836 52.366 23.836  1.00 75.33  ? 871  ASN B O   1 
ATOM   3150 C CB  . ASN B 1 190 ? 14.369 51.285 24.414  1.00 80.19  ? 871  ASN B CB  1 
ATOM   3151 C CG  . ASN B 1 190 ? 13.312 50.385 25.018  1.00 88.54  ? 871  ASN B CG  1 
ATOM   3152 O OD1 . ASN B 1 190 ? 13.624 49.329 25.571  1.00 93.42  ? 871  ASN B OD1 1 
ATOM   3153 N ND2 . ASN B 1 190 ? 12.053 50.797 24.916  1.00 70.01  ? 871  ASN B ND2 1 
ATOM   3154 N N   . ARG B 1 191 ? 16.928 53.702 25.640  1.00 55.43  ? 872  ARG B N   1 
ATOM   3155 C CA  . ARG B 1 191 ? 18.191 54.323 25.256  1.00 55.17  ? 872  ARG B CA  1 
ATOM   3156 C C   . ARG B 1 191 ? 19.332 53.410 25.692  1.00 42.41  ? 872  ARG B C   1 
ATOM   3157 O O   . ARG B 1 191 ? 19.598 53.260 26.889  1.00 43.18  ? 872  ARG B O   1 
ATOM   3158 C CB  . ARG B 1 191 ? 18.305 55.708 25.884  1.00 57.94  ? 872  ARG B CB  1 
ATOM   3159 C CG  . ARG B 1 191 ? 19.378 56.606 25.290  1.00 59.69  ? 872  ARG B CG  1 
ATOM   3160 C CD  . ARG B 1 191 ? 19.305 58.010 25.893  1.00 68.19  ? 872  ARG B CD  1 
ATOM   3161 N NE  . ARG B 1 191 ? 18.020 58.658 25.645  1.00 76.07  ? 872  ARG B NE  1 
ATOM   3162 C CZ  . ARG B 1 191 ? 17.026 58.726 26.521  1.00 74.07  ? 872  ARG B CZ  1 
ATOM   3163 N NH1 . ARG B 1 191 ? 17.131 58.198 27.730  1.00 70.30  ? 872  ARG B NH1 1 
ATOM   3164 N NH2 . ARG B 1 191 ? 15.896 59.338 26.175  1.00 64.45  ? 872  ARG B NH2 1 
ATOM   3165 N N   . SER B 1 192 ? 20.002 52.794 24.724  1.00 28.35  ? 873  SER B N   1 
ATOM   3166 C CA  . SER B 1 192 ? 21.071 51.848 25.014  1.00 27.16  ? 873  SER B CA  1 
ATOM   3167 C C   . SER B 1 192 ? 22.323 52.573 25.506  1.00 18.32  ? 873  SER B C   1 
ATOM   3168 O O   . SER B 1 192 ? 22.780 53.537 24.883  1.00 21.13  ? 873  SER B O   1 
ATOM   3169 C CB  . SER B 1 192 ? 21.379 51.024 23.763  1.00 17.73  ? 873  SER B CB  1 
ATOM   3170 O OG  . SER B 1 192 ? 22.428 50.099 23.984  1.00 22.79  ? 873  SER B OG  1 
ATOM   3171 N N   . GLY B 1 193 ? 22.869 52.113 26.625  1.00 16.10  ? 874  GLY B N   1 
ATOM   3172 C CA  . GLY B 1 193 ? 24.145 52.622 27.092  1.00 21.02  ? 874  GLY B CA  1 
ATOM   3173 C C   . GLY B 1 193 ? 24.554 51.959 28.388  1.00 18.06  ? 874  GLY B C   1 
ATOM   3174 O O   . GLY B 1 193 ? 23.975 50.952 28.803  1.00 20.33  ? 874  GLY B O   1 
ATOM   3175 N N   . GLY B 1 194 ? 25.558 52.549 29.034  1.00 16.76  ? 875  GLY B N   1 
ATOM   3176 C CA  . GLY B 1 194 ? 26.076 51.981 30.263  1.00 17.04  ? 875  GLY B CA  1 
ATOM   3177 C C   . GLY B 1 194 ? 26.802 53.002 31.110  1.00 14.31  ? 875  GLY B C   1 
ATOM   3178 O O   . GLY B 1 194 ? 26.936 54.173 30.744  1.00 14.10  ? 875  GLY B O   1 
ATOM   3179 N N   . LEU B 1 195 ? 27.239 52.541 32.278  1.00 10.48  ? 876  LEU B N   1 
ATOM   3180 C CA  . LEU B 1 195 ? 28.021 53.336 33.217  1.00 11.79  ? 876  LEU B CA  1 
ATOM   3181 C C   . LEU B 1 195 ? 29.455 52.822 33.226  1.00 13.38  ? 876  LEU B C   1 
ATOM   3182 O O   . LEU B 1 195 ? 29.678 51.608 33.266  1.00 15.36  ? 876  LEU B O   1 
ATOM   3183 C CB  . LEU B 1 195 ? 27.427 53.256 34.623  1.00 10.50  ? 876  LEU B CB  1 
ATOM   3184 C CG  . LEU B 1 195 ? 28.347 53.587 35.800  1.00 23.34  ? 876  LEU B CG  1 
ATOM   3185 C CD1 . LEU B 1 195 ? 28.675 55.080 35.849  1.00 31.14  ? 876  LEU B CD1 1 
ATOM   3186 C CD2 . LEU B 1 195 ? 27.722 53.127 37.105  1.00 27.74  ? 876  LEU B CD2 1 
ATOM   3187 N N   . ILE B 1 196 ? 30.421 53.732 33.181  1.00 12.62  ? 877  ILE B N   1 
ATOM   3188 C CA  . ILE B 1 196 ? 31.824 53.381 33.359  1.00 10.56  ? 877  ILE B CA  1 
ATOM   3189 C C   . ILE B 1 196 ? 32.173 53.645 34.818  1.00 12.88  ? 877  ILE B C   1 
ATOM   3190 O O   . ILE B 1 196 ? 32.048 54.776 35.299  1.00 16.10  ? 877  ILE B O   1 
ATOM   3191 C CB  . ILE B 1 196 ? 32.727 54.175 32.402  1.00 12.32  ? 877  ILE B CB  1 
ATOM   3192 C CG1 . ILE B 1 196 ? 32.317 53.906 30.950  1.00 12.65  ? 877  ILE B CG1 1 
ATOM   3193 C CG2 . ILE B 1 196 ? 34.183 53.821 32.623  1.00 11.22  ? 877  ILE B CG2 1 
ATOM   3194 C CD1 . ILE B 1 196 ? 32.278 52.418 30.580  1.00 15.99  ? 877  ILE B CD1 1 
ATOM   3195 N N   . LEU B 1 197 ? 32.595 52.603 35.527  1.00 10.45  ? 878  LEU B N   1 
ATOM   3196 C CA  . LEU B 1 197 ? 32.800 52.708 36.968  1.00 10.76  ? 878  LEU B CA  1 
ATOM   3197 C C   . LEU B 1 197 ? 33.915 53.696 37.303  1.00 14.56  ? 878  LEU B C   1 
ATOM   3198 O O   . LEU B 1 197 ? 35.015 53.630 36.746  1.00 16.68  ? 878  LEU B O   1 
ATOM   3199 C CB  . LEU B 1 197 ? 33.105 51.323 37.540  1.00 13.56  ? 878  LEU B CB  1 
ATOM   3200 C CG  . LEU B 1 197 ? 31.905 50.373 37.452  1.00 13.08  ? 878  LEU B CG  1 
ATOM   3201 C CD1 . LEU B 1 197 ? 32.360 48.918 37.601  1.00 10.66  ? 878  LEU B CD1 1 
ATOM   3202 C CD2 . LEU B 1 197 ? 30.864 50.734 38.497  1.00 12.43  ? 878  LEU B CD2 1 
ATOM   3203 N N   . SER B 1 198 ? 33.613 54.627 38.209  1.00 11.73  ? 879  SER B N   1 
ATOM   3204 C CA  . SER B 1 198 ? 34.562 55.633 38.658  1.00 15.75  ? 879  SER B CA  1 
ATOM   3205 C C   . SER B 1 198 ? 35.590 55.017 39.600  1.00 15.51  ? 879  SER B C   1 
ATOM   3206 O O   . SER B 1 198 ? 35.396 53.910 40.118  1.00 14.80  ? 879  SER B O   1 
ATOM   3207 C CB  . SER B 1 198 ? 33.810 56.753 39.367  1.00 13.84  ? 879  SER B CB  1 
ATOM   3208 O OG  . SER B 1 198 ? 33.318 56.286 40.611  1.00 16.57  ? 879  SER B OG  1 
ATOM   3209 N N   . PRO B 1 199 ? 36.703 55.719 39.857  1.00 13.87  ? 880  PRO B N   1 
ATOM   3210 C CA  . PRO B 1 199 ? 37.623 55.263 40.916  1.00 15.51  ? 880  PRO B CA  1 
ATOM   3211 C C   . PRO B 1 199 ? 36.934 55.012 42.249  1.00 20.65  ? 880  PRO B C   1 
ATOM   3212 O O   . PRO B 1 199 ? 37.221 54.008 42.914  1.00 20.97  ? 880  PRO B O   1 
ATOM   3213 C CB  . PRO B 1 199 ? 38.636 56.418 41.010  1.00 19.21  ? 880  PRO B CB  1 
ATOM   3214 C CG  . PRO B 1 199 ? 38.650 57.018 39.646  1.00 15.30  ? 880  PRO B CG  1 
ATOM   3215 C CD  . PRO B 1 199 ? 37.200 56.938 39.188  1.00 14.22  ? 880  PRO B CD  1 
ATOM   3216 N N   . THR B 1 200 ? 36.026 55.903 42.657  1.00 15.00  ? 881  THR B N   1 
ATOM   3217 C CA  . THR B 1 200 ? 35.304 55.717 43.911  1.00 19.28  ? 881  THR B CA  1 
ATOM   3218 C C   . THR B 1 200 ? 34.417 54.480 43.857  1.00 16.68  ? 881  THR B C   1 
ATOM   3219 O O   . THR B 1 200 ? 34.343 53.715 44.827  1.00 15.51  ? 881  THR B O   1 
ATOM   3220 C CB  . THR B 1 200 ? 34.469 56.964 44.220  1.00 19.60  ? 881  THR B CB  1 
ATOM   3221 O OG1 . THR B 1 200 ? 35.342 58.069 44.477  1.00 21.59  ? 881  THR B OG1 1 
ATOM   3222 C CG2 . THR B 1 200 ? 33.582 56.742 45.435  1.00 22.20  ? 881  THR B CG2 1 
ATOM   3223 N N   . GLN B 1 201 ? 33.735 54.273 42.734  1.00 15.13  ? 882  GLN B N   1 
ATOM   3224 C CA  . GLN B 1 201 ? 32.840 53.125 42.614  1.00 14.31  ? 882  GLN B CA  1 
ATOM   3225 C C   . GLN B 1 201 ? 33.626 51.818 42.584  1.00 19.07  ? 882  GLN B C   1 
ATOM   3226 O O   . GLN B 1 201 ? 33.219 50.828 43.203  1.00 14.77  ? 882  GLN B O   1 
ATOM   3227 C CB  . GLN B 1 201 ? 31.976 53.282 41.369  1.00 15.74  ? 882  GLN B CB  1 
ATOM   3228 C CG  . GLN B 1 201 ? 30.840 54.279 41.553  1.00 12.45  ? 882  GLN B CG  1 
ATOM   3229 C CD  . GLN B 1 201 ? 30.200 54.672 40.246  1.00 14.28  ? 882  GLN B CD  1 
ATOM   3230 O OE1 . GLN B 1 201 ? 30.821 54.587 39.189  1.00 14.03  ? 882  GLN B OE1 1 
ATOM   3231 N NE2 . GLN B 1 201 ? 28.946 55.105 40.306  1.00 16.88  ? 882  GLN B NE2 1 
ATOM   3232 N N   . LEU B 1 202 ? 34.763 51.802 41.886  1.00 18.40  ? 883  LEU B N   1 
ATOM   3233 C CA  . LEU B 1 202 ? 35.635 50.632 41.932  1.00 15.02  ? 883  LEU B CA  1 
ATOM   3234 C C   . LEU B 1 202 ? 36.072 50.325 43.359  1.00 15.21  ? 883  LEU B C   1 
ATOM   3235 O O   . LEU B 1 202 ? 36.078 49.163 43.777  1.00 15.71  ? 883  LEU B O   1 
ATOM   3236 C CB  . LEU B 1 202 ? 36.850 50.850 41.032  1.00 14.23  ? 883  LEU B CB  1 
ATOM   3237 C CG  . LEU B 1 202 ? 36.568 50.931 39.531  1.00 14.45  ? 883  LEU B CG  1 
ATOM   3238 C CD1 . LEU B 1 202 ? 37.826 51.381 38.790  1.00 19.55  ? 883  LEU B CD1 1 
ATOM   3239 C CD2 . LEU B 1 202 ? 36.055 49.591 38.992  1.00 15.02  ? 883  LEU B CD2 1 
ATOM   3240 N N   . ASP B 1 203 ? 36.434 51.353 44.124  1.00 15.93  ? 884  ASP B N   1 
ATOM   3241 C CA  . ASP B 1 203 ? 36.893 51.130 45.490  1.00 19.64  ? 884  ASP B CA  1 
ATOM   3242 C C   . ASP B 1 203 ? 35.788 50.536 46.352  1.00 17.57  ? 884  ASP B C   1 
ATOM   3243 O O   . ASP B 1 203 ? 36.037 49.628 47.156  1.00 18.70  ? 884  ASP B O   1 
ATOM   3244 C CB  . ASP B 1 203 ? 37.405 52.440 46.093  1.00 20.48  ? 884  ASP B CB  1 
ATOM   3245 C CG  . ASP B 1 203 ? 38.829 52.764 45.665  1.00 26.12  ? 884  ASP B CG  1 
ATOM   3246 O OD1 . ASP B 1 203 ? 39.489 51.887 45.058  1.00 25.80  ? 884  ASP B OD1 1 
ATOM   3247 O OD2 . ASP B 1 203 ? 39.286 53.900 45.934  1.00 33.47  ? 884  ASP B OD2 1 
ATOM   3248 N N   . TRP B 1 204 ? 34.558 51.032 46.193  1.00 16.68  ? 885  TRP B N   1 
ATOM   3249 C CA  . TRP B 1 204 ? 33.433 50.502 46.957  1.00 16.95  ? 885  TRP B CA  1 
ATOM   3250 C C   . TRP B 1 204 ? 33.182 49.035 46.639  1.00 16.73  ? 885  TRP B C   1 
ATOM   3251 O O   . TRP B 1 204 ? 32.958 48.224 47.548  1.00 18.04  ? 885  TRP B O   1 
ATOM   3252 C CB  . TRP B 1 204 ? 32.174 51.320 46.678  1.00 16.17  ? 885  TRP B CB  1 
ATOM   3253 C CG  . TRP B 1 204 ? 30.957 50.740 47.331  1.00 16.52  ? 885  TRP B CG  1 
ATOM   3254 C CD1 . TRP B 1 204 ? 30.586 50.868 48.640  1.00 18.42  ? 885  TRP B CD1 1 
ATOM   3255 C CD2 . TRP B 1 204 ? 29.952 49.935 46.706  1.00 19.09  ? 885  TRP B CD2 1 
ATOM   3256 N NE1 . TRP B 1 204 ? 29.410 50.194 48.866  1.00 18.35  ? 885  TRP B NE1 1 
ATOM   3257 C CE2 . TRP B 1 204 ? 29.003 49.609 47.697  1.00 17.63  ? 885  TRP B CE2 1 
ATOM   3258 C CE3 . TRP B 1 204 ? 29.761 49.459 45.402  1.00 16.05  ? 885  TRP B CE3 1 
ATOM   3259 C CZ2 . TRP B 1 204 ? 27.882 48.827 47.429  1.00 18.51  ? 885  TRP B CZ2 1 
ATOM   3260 C CZ3 . TRP B 1 204 ? 28.644 48.683 45.137  1.00 18.10  ? 885  TRP B CZ3 1 
ATOM   3261 C CH2 . TRP B 1 204 ? 27.720 48.373 46.148  1.00 17.84  ? 885  TRP B CH2 1 
ATOM   3262 N N   . ILE B 1 205 ? 33.187 48.679 45.354  1.00 15.57  ? 886  ILE B N   1 
ATOM   3263 C CA  . ILE B 1 205 ? 32.980 47.281 44.978  1.00 15.43  ? 886  ILE B CA  1 
ATOM   3264 C C   . ILE B 1 205 ? 34.013 46.389 45.657  1.00 20.36  ? 886  ILE B C   1 
ATOM   3265 O O   . ILE B 1 205 ? 33.679 45.355 46.247  1.00 17.61  ? 886  ILE B O   1 
ATOM   3266 C CB  . ILE B 1 205 ? 33.028 47.122 43.453  1.00 14.21  ? 886  ILE B CB  1 
ATOM   3267 C CG1 . ILE B 1 205 ? 31.881 47.895 42.788  1.00 13.12  ? 886  ILE B CG1 1 
ATOM   3268 C CG2 . ILE B 1 205 ? 32.997 45.641 43.090  1.00 14.92  ? 886  ILE B CG2 1 
ATOM   3269 C CD1 . ILE B 1 205 ? 32.060 48.061 41.291  1.00 12.17  ? 886  ILE B CD1 1 
ATOM   3270 N N   . ARG B 1 206 ? 35.289 46.777 45.581  1.00 17.71  ? 887  ARG B N   1 
ATOM   3271 C CA  . ARG B 1 206 ? 36.327 45.969 46.214  1.00 19.06  ? 887  ARG B CA  1 
ATOM   3272 C C   . ARG B 1 206 ? 36.139 45.900 47.726  1.00 23.51  ? 887  ARG B C   1 
ATOM   3273 O O   . ARG B 1 206 ? 36.484 44.886 48.347  1.00 30.26  ? 887  ARG B O   1 
ATOM   3274 C CB  . ARG B 1 206 ? 37.704 46.520 45.852  1.00 24.00  ? 887  ARG B CB  1 
ATOM   3275 C CG  . ARG B 1 206 ? 38.170 46.102 44.464  1.00 24.17  ? 887  ARG B CG  1 
ATOM   3276 C CD  . ARG B 1 206 ? 39.598 46.544 44.189  1.00 22.58  ? 887  ARG B CD  1 
ATOM   3277 N NE  . ARG B 1 206 ? 39.658 47.970 43.901  1.00 32.52  ? 887  ARG B NE  1 
ATOM   3278 C CZ  . ARG B 1 206 ? 39.650 48.489 42.682  1.00 22.87  ? 887  ARG B CZ  1 
ATOM   3279 N NH1 . ARG B 1 206 ? 39.628 47.721 41.603  1.00 21.15  ? 887  ARG B NH1 1 
ATOM   3280 N NH2 . ARG B 1 206 ? 39.681 49.811 42.541  1.00 27.77  ? 887  ARG B NH2 1 
ATOM   3281 N N   . SER B 1 207 ? 35.567 46.949 48.329  1.00 27.70  ? 888  SER B N   1 
ATOM   3282 C CA  . SER B 1 207 ? 35.299 46.924 49.765  1.00 32.00  ? 888  SER B CA  1 
ATOM   3283 C C   . SER B 1 207 ? 34.232 45.897 50.125  1.00 27.44  ? 888  SER B C   1 
ATOM   3284 O O   . SER B 1 207 ? 34.291 45.300 51.207  1.00 32.86  ? 888  SER B O   1 
ATOM   3285 C CB  . SER B 1 207 ? 34.872 48.309 50.248  1.00 23.93  ? 888  SER B CB  1 
ATOM   3286 O OG  . SER B 1 207 ? 33.580 48.636 49.763  1.00 28.71  ? 888  SER B OG  1 
ATOM   3287 N N   . ILE B 1 208 ? 33.245 45.688 49.249  1.00 29.78  ? 889  ILE B N   1 
ATOM   3288 C CA  . ILE B 1 208 ? 32.248 44.652 49.502  1.00 28.04  ? 889  ILE B CA  1 
ATOM   3289 C C   . ILE B 1 208 ? 32.868 43.269 49.335  1.00 31.91  ? 889  ILE B C   1 
ATOM   3290 O O   . ILE B 1 208 ? 32.603 42.356 50.125  1.00 34.54  ? 889  ILE B O   1 
ATOM   3291 C CB  . ILE B 1 208 ? 31.025 44.841 48.584  1.00 24.64  ? 889  ILE B CB  1 
ATOM   3292 C CG1 . ILE B 1 208 ? 30.473 46.269 48.689  1.00 25.66  ? 889  ILE B CG1 1 
ATOM   3293 C CG2 . ILE B 1 208 ? 29.932 43.841 48.934  1.00 26.12  ? 889  ILE B CG2 1 
ATOM   3294 C CD1 . ILE B 1 208 ? 29.934 46.625 50.061  1.00 29.00  ? 889  ILE B CD1 1 
ATOM   3295 N N   . ILE B 1 209 ? 33.712 43.098 48.313  1.00 27.75  ? 890  ILE B N   1 
ATOM   3296 C CA  . ILE B 1 209 ? 34.365 41.813 48.073  1.00 28.40  ? 890  ILE B CA  1 
ATOM   3297 C C   . ILE B 1 209 ? 35.213 41.408 49.272  1.00 41.13  ? 890  ILE B C   1 
ATOM   3298 O O   . ILE B 1 209 ? 35.195 40.247 49.701  1.00 43.04  ? 890  ILE B O   1 
ATOM   3299 C CB  . ILE B 1 209 ? 35.212 41.875 46.787  1.00 26.68  ? 890  ILE B CB  1 
ATOM   3300 C CG1 . ILE B 1 209 ? 34.322 42.110 45.570  1.00 29.91  ? 890  ILE B CG1 1 
ATOM   3301 C CG2 . ILE B 1 209 ? 36.034 40.601 46.617  1.00 29.41  ? 890  ILE B CG2 1 
ATOM   3302 C CD1 . ILE B 1 209 ? 35.085 42.256 44.283  1.00 23.73  ? 890  ILE B CD1 1 
ATOM   3303 N N   . LYS B 1 210 ? 35.970 42.356 49.829  1.00 31.93  ? 891  LYS B N   1 
ATOM   3304 C CA  . LYS B 1 210 ? 36.838 42.037 50.957  1.00 35.94  ? 891  LYS B CA  1 
ATOM   3305 C C   . LYS B 1 210 ? 36.037 41.593 52.177  1.00 51.60  ? 891  LYS B C   1 
ATOM   3306 O O   . LYS B 1 210 ? 36.512 40.763 52.962  1.00 48.38  ? 891  LYS B O   1 
ATOM   3307 C CB  . LYS B 1 210 ? 37.718 43.242 51.296  1.00 36.88  ? 891  LYS B CB  1 
ATOM   3308 C CG  . LYS B 1 210 ? 38.906 42.912 52.190  1.00 47.99  ? 891  LYS B CG  1 
ATOM   3309 C CD  . LYS B 1 210 ? 39.745 44.144 52.486  1.00 57.20  ? 891  LYS B CD  1 
ATOM   3310 C CE  . LYS B 1 210 ? 40.958 43.790 53.338  1.00 57.82  ? 891  LYS B CE  1 
ATOM   3311 N NZ  . LYS B 1 210 ? 41.748 44.994 53.714  1.00 41.73  ? 891  LYS B NZ  1 
ATOM   3312 N N   . GLY B 1 211 ? 34.826 42.116 52.348  1.00 46.78  ? 892  GLY B N   1 
ATOM   3313 C CA  . GLY B 1 211 ? 33.971 41.710 53.450  1.00 47.15  ? 892  GLY B CA  1 
ATOM   3314 C C   . GLY B 1 211 ? 33.239 40.406 53.189  1.00 55.99  ? 892  GLY B C   1 
ATOM   3315 O O   . GLY B 1 211 ? 33.142 39.544 54.065  1.00 54.14  ? 892  GLY B O   1 
HETATM 3316 O O   . HOH C 2 .   ? 39.774 34.431 -21.945 1.00 32.81  ? 901  HOH A O   1 
HETATM 3317 O O   . HOH C 2 .   ? 32.038 55.391 -5.155  1.00 32.66  ? 902  HOH A O   1 
HETATM 3318 O O   . HOH C 2 .   ? 43.139 24.109 -1.471  1.00 25.22  ? 903  HOH A O   1 
HETATM 3319 O O   . HOH C 2 .   ? 50.393 43.468 -9.813  1.00 28.36  ? 904  HOH A O   1 
HETATM 3320 O O   . HOH C 2 .   ? 30.962 31.504 16.311  1.00 32.81  ? 905  HOH A O   1 
HETATM 3321 O O   . HOH C 2 .   ? 37.582 24.255 11.557  1.00 34.39  ? 906  HOH A O   1 
HETATM 3322 O O   . HOH C 2 .   ? 54.769 41.729 -0.989  1.00 36.85  ? 907  HOH A O   1 
HETATM 3323 O O   . HOH C 2 .   ? 16.173 33.926 0.201   1.00 36.11  ? 908  HOH A O   1 
HETATM 3324 O O   . HOH C 2 .   ? 37.378 28.251 -13.597 1.00 32.59  ? 909  HOH A O   1 
HETATM 3325 O O   . HOH C 2 .   ? 22.589 48.554 3.740   1.00 29.07  ? 910  HOH A O   1 
HETATM 3326 O O   . HOH C 2 .   ? 16.612 41.915 10.471  1.00 34.55  ? 911  HOH A O   1 
HETATM 3327 O O   . HOH C 2 .   ? 29.126 51.262 3.941   1.00 22.12  ? 912  HOH A O   1 
HETATM 3328 O O   . HOH C 2 .   ? 15.118 37.012 17.441  1.00 29.34  ? 913  HOH A O   1 
HETATM 3329 O O   . HOH C 2 .   ? 41.623 62.327 -6.234  1.00 24.46  ? 914  HOH A O   1 
HETATM 3330 O O   . HOH C 2 .   ? 32.567 59.291 7.502   1.00 33.04  ? 915  HOH A O   1 
HETATM 3331 O O   . HOH C 2 .   ? 16.662 56.233 4.969   1.00 28.60  ? 916  HOH A O   1 
HETATM 3332 O O   . HOH C 2 .   ? 37.461 24.269 15.398  1.00 38.17  ? 917  HOH A O   1 
HETATM 3333 O O   . HOH C 2 .   ? 48.049 34.841 -9.626  1.00 38.91  ? 918  HOH A O   1 
HETATM 3334 O O   . HOH C 2 .   ? 26.953 22.341 -0.608  1.00 36.44  ? 919  HOH A O   1 
HETATM 3335 O O   . HOH C 2 .   ? 36.142 19.159 -1.139  1.00 29.95  ? 920  HOH A O   1 
HETATM 3336 O O   . HOH C 2 .   ? 35.985 56.568 -17.973 1.00 25.75  ? 921  HOH A O   1 
HETATM 3337 O O   . HOH C 2 .   ? 45.729 44.694 -13.222 1.00 28.23  ? 922  HOH A O   1 
HETATM 3338 O O   . HOH C 2 .   ? 26.853 44.757 -14.033 1.00 36.27  ? 923  HOH A O   1 
HETATM 3339 O O   . HOH C 2 .   ? 33.139 37.270 20.102  1.00 28.53  ? 924  HOH A O   1 
HETATM 3340 O O   . HOH C 2 .   ? 25.220 34.775 14.644  1.00 18.02  ? 925  HOH A O   1 
HETATM 3341 O O   . HOH C 2 .   ? 42.854 37.180 -12.043 1.00 23.59  ? 926  HOH A O   1 
HETATM 3342 O O   . HOH C 2 .   ? 16.925 52.749 7.408   1.00 36.11  ? 927  HOH A O   1 
HETATM 3343 O O   . HOH C 2 .   ? 49.608 36.262 3.011   1.00 17.76  ? 928  HOH A O   1 
HETATM 3344 O O   . HOH C 2 .   ? 23.871 58.145 7.767   1.00 22.61  ? 929  HOH A O   1 
HETATM 3345 O O   . HOH C 2 .   ? 41.141 54.819 -7.483  1.00 19.91  ? 930  HOH A O   1 
HETATM 3346 O O   . HOH C 2 .   ? 16.675 43.848 8.137   1.00 31.21  ? 931  HOH A O   1 
HETATM 3347 O O   . HOH C 2 .   ? 32.760 21.611 7.189   1.00 27.75  ? 932  HOH A O   1 
HETATM 3348 O O   . HOH C 2 .   ? 19.244 43.016 14.358  1.00 25.92  ? 933  HOH A O   1 
HETATM 3349 O O   . HOH C 2 .   ? 38.716 31.762 -12.930 1.00 25.17  ? 934  HOH A O   1 
HETATM 3350 O O   . HOH C 2 .   ? 35.062 50.639 -20.404 1.00 32.16  ? 935  HOH A O   1 
HETATM 3351 O O   . HOH C 2 .   ? 32.833 51.607 -3.596  1.00 19.15  ? 936  HOH A O   1 
HETATM 3352 O O   . HOH C 2 .   ? 49.291 32.787 -13.661 1.00 41.03  ? 937  HOH A O   1 
HETATM 3353 O O   . HOH C 2 .   ? 36.078 34.692 15.973  1.00 21.85  ? 938  HOH A O   1 
HETATM 3354 O O   . HOH C 2 .   ? 31.530 51.220 -15.169 1.00 34.01  ? 939  HOH A O   1 
HETATM 3355 O O   . HOH C 2 .   ? 23.212 51.838 3.672   1.00 23.61  ? 940  HOH A O   1 
HETATM 3356 O O   . HOH C 2 .   ? 9.908  36.588 12.340  1.00 30.52  ? 941  HOH A O   1 
HETATM 3357 O O   . HOH C 2 .   ? 24.938 39.523 -1.653  1.00 25.07  ? 942  HOH A O   1 
HETATM 3358 O O   . HOH C 2 .   ? 40.974 55.161 4.818   1.00 13.44  ? 943  HOH A O   1 
HETATM 3359 O O   . HOH C 2 .   ? 38.801 54.936 6.442   1.00 22.51  ? 944  HOH A O   1 
HETATM 3360 O O   . HOH C 2 .   ? 44.943 59.963 -4.954  1.00 14.77  ? 945  HOH A O   1 
HETATM 3361 O O   . HOH C 2 .   ? 32.407 60.829 -2.489  1.00 21.52  ? 946  HOH A O   1 
HETATM 3362 O O   . HOH C 2 .   ? 14.781 30.804 17.222  1.00 34.30  ? 947  HOH A O   1 
HETATM 3363 O O   . HOH C 2 .   ? 35.849 25.871 9.825   1.00 33.32  ? 948  HOH A O   1 
HETATM 3364 O O   . HOH C 2 .   ? 27.060 39.906 -1.899  1.00 23.27  ? 949  HOH A O   1 
HETATM 3365 O O   . HOH C 2 .   ? 36.116 25.069 -10.864 1.00 30.74  ? 950  HOH A O   1 
HETATM 3366 O O   . HOH C 2 .   ? 20.267 29.266 11.203  1.00 34.74  ? 951  HOH A O   1 
HETATM 3367 O O   . HOH C 2 .   ? 33.984 32.224 17.823  1.00 28.74  ? 952  HOH A O   1 
HETATM 3368 O O   . HOH C 2 .   ? 18.335 55.778 16.939  1.00 37.77  ? 953  HOH A O   1 
HETATM 3369 O O   . HOH C 2 .   ? 25.764 45.282 -3.985  1.00 29.88  ? 954  HOH A O   1 
HETATM 3370 O O   . HOH C 2 .   ? 45.932 57.697 -3.213  1.00 10.25  ? 955  HOH A O   1 
HETATM 3371 O O   . HOH C 2 .   ? 32.923 28.184 -3.885  1.00 16.62  ? 956  HOH A O   1 
HETATM 3372 O O   . HOH C 2 .   ? 36.978 39.774 -0.774  1.00 9.68   ? 957  HOH A O   1 
HETATM 3373 O O   . HOH C 2 .   ? 26.281 27.323 9.632   1.00 22.30  ? 958  HOH A O   1 
HETATM 3374 O O   . HOH C 2 .   ? 50.449 46.254 8.512   1.00 30.32  ? 959  HOH A O   1 
HETATM 3375 O O   . HOH C 2 .   ? 23.441 39.203 9.856   1.00 13.29  ? 960  HOH A O   1 
HETATM 3376 O O   . HOH C 2 .   ? 32.485 27.988 13.461  1.00 20.15  ? 961  HOH A O   1 
HETATM 3377 O O   . HOH C 2 .   ? 29.331 58.535 14.130  1.00 31.26  ? 962  HOH A O   1 
HETATM 3378 O O   . HOH C 2 .   ? 19.094 31.314 -13.669 1.00 39.91  ? 963  HOH A O   1 
HETATM 3379 O O   . HOH C 2 .   ? 40.912 23.531 6.835   1.00 15.28  ? 964  HOH A O   1 
HETATM 3380 O O   . HOH C 2 .   ? 52.753 51.442 -4.040  1.00 20.11  ? 965  HOH A O   1 
HETATM 3381 O O   . HOH C 2 .   ? 20.608 49.256 4.713   1.00 25.26  ? 966  HOH A O   1 
HETATM 3382 O O   . HOH C 2 .   ? 32.008 24.333 -4.165  1.00 22.77  ? 967  HOH A O   1 
HETATM 3383 O O   . HOH C 2 .   ? 33.559 30.177 14.580  1.00 30.16  ? 968  HOH A O   1 
HETATM 3384 O O   . HOH C 2 .   ? 53.175 50.328 2.567   1.00 26.78  ? 969  HOH A O   1 
HETATM 3385 O O   . HOH C 2 .   ? 27.347 43.108 -6.292  1.00 25.84  ? 970  HOH A O   1 
HETATM 3386 O O   . HOH C 2 .   ? 49.438 53.368 7.621   1.00 41.01  ? 971  HOH A O   1 
HETATM 3387 O O   . HOH C 2 .   ? 52.588 42.915 -2.015  1.00 36.80  ? 972  HOH A O   1 
HETATM 3388 O O   . HOH C 2 .   ? 26.952 28.965 11.785  1.00 23.21  ? 973  HOH A O   1 
HETATM 3389 O O   . HOH C 2 .   ? 32.079 48.026 8.666   1.00 8.71   ? 974  HOH A O   1 
HETATM 3390 O O   . HOH C 2 .   ? 35.821 31.379 14.898  1.00 30.47  ? 975  HOH A O   1 
HETATM 3391 O O   . HOH C 2 .   ? 37.872 53.939 -18.777 1.00 29.06  ? 976  HOH A O   1 
HETATM 3392 O O   . HOH C 2 .   ? 26.438 34.872 -3.793  1.00 13.33  ? 977  HOH A O   1 
HETATM 3393 O O   . HOH C 2 .   ? 44.467 42.583 -12.104 1.00 16.52  ? 978  HOH A O   1 
HETATM 3394 O O   . HOH C 2 .   ? 34.497 27.871 9.290   1.00 23.15  ? 979  HOH A O   1 
HETATM 3395 O O   . HOH C 2 .   ? 34.460 48.327 -17.171 1.00 18.51  ? 980  HOH A O   1 
HETATM 3396 O O   . HOH C 2 .   ? 16.266 49.916 13.153  1.00 30.32  ? 981  HOH A O   1 
HETATM 3397 O O   . HOH C 2 .   ? 44.619 48.399 -1.605  1.00 8.92   ? 982  HOH A O   1 
HETATM 3398 O O   . HOH C 2 .   ? 40.426 28.773 -0.040  1.00 10.73  ? 983  HOH A O   1 
HETATM 3399 O O   . HOH C 2 .   ? 22.175 31.053 1.571   1.00 18.96  ? 984  HOH A O   1 
HETATM 3400 O O   . HOH C 2 .   ? 53.474 49.029 -4.910  1.00 27.25  ? 985  HOH A O   1 
HETATM 3401 O O   . HOH C 2 .   ? 44.273 60.704 -1.567  1.00 19.93  ? 986  HOH A O   1 
HETATM 3402 O O   . HOH C 2 .   ? 35.702 62.003 3.610   1.00 34.50  ? 987  HOH A O   1 
HETATM 3403 O O   . HOH C 2 .   ? 47.155 38.146 3.615   1.00 17.90  ? 988  HOH A O   1 
HETATM 3404 O O   . HOH C 2 .   ? 45.397 54.025 -16.007 1.00 26.25  ? 989  HOH A O   1 
HETATM 3405 O O   . HOH C 2 .   ? 28.764 57.801 -3.003  1.00 26.35  ? 990  HOH A O   1 
HETATM 3406 O O   . HOH C 2 .   ? 42.733 60.949 -8.858  1.00 21.06  ? 991  HOH A O   1 
HETATM 3407 O O   . HOH C 2 .   ? 44.046 30.101 -2.730  1.00 15.04  ? 992  HOH A O   1 
HETATM 3408 O O   . HOH C 2 .   ? 47.914 36.182 -3.553  1.00 10.45  ? 993  HOH A O   1 
HETATM 3409 O O   . HOH C 2 .   ? 30.480 20.611 -1.474  1.00 24.79  ? 994  HOH A O   1 
HETATM 3410 O O   . HOH C 2 .   ? 49.107 32.840 0.002   1.00 16.09  ? 995  HOH A O   1 
HETATM 3411 O O   . HOH C 2 .   ? 10.781 32.502 6.634   1.00 15.46  ? 996  HOH A O   1 
HETATM 3412 O O   . HOH C 2 .   ? 30.170 50.062 -13.548 1.00 29.93  ? 997  HOH A O   1 
HETATM 3413 O O   . HOH C 2 .   ? 20.500 39.323 20.003  1.00 24.40  ? 998  HOH A O   1 
HETATM 3414 O O   . HOH C 2 .   ? 48.550 46.236 11.116  1.00 22.00  ? 999  HOH A O   1 
HETATM 3415 O O   . HOH C 2 .   ? 28.974 33.035 -13.572 1.00 22.28  ? 1000 HOH A O   1 
HETATM 3416 O O   . HOH C 2 .   ? 51.697 53.762 -1.106  1.00 12.61  ? 1001 HOH A O   1 
HETATM 3417 O O   . HOH C 2 .   ? 32.434 30.901 -14.243 1.00 32.34  ? 1002 HOH A O   1 
HETATM 3418 O O   . HOH C 2 .   ? 47.719 35.878 5.684   1.00 18.34  ? 1003 HOH A O   1 
HETATM 3419 O O   . HOH C 2 .   ? 25.116 28.689 -5.362  1.00 20.26  ? 1004 HOH A O   1 
HETATM 3420 O O   . HOH C 2 .   ? 45.122 38.791 -11.151 1.00 20.09  ? 1005 HOH A O   1 
HETATM 3421 O O   . HOH C 2 .   ? 38.690 22.580 9.273   1.00 32.06  ? 1006 HOH A O   1 
HETATM 3422 O O   . HOH C 2 .   ? 36.884 36.546 -4.230  1.00 8.07   ? 1007 HOH A O   1 
HETATM 3423 O O   . HOH C 2 .   ? 51.390 40.436 0.027   1.00 27.08  ? 1008 HOH A O   1 
HETATM 3424 O O   . HOH C 2 .   ? 26.779 56.750 11.333  1.00 26.42  ? 1009 HOH A O   1 
HETATM 3425 O O   . HOH C 2 .   ? 43.760 63.638 -4.162  1.00 27.74  ? 1010 HOH A O   1 
HETATM 3426 O O   . HOH C 2 .   ? 44.407 27.949 -14.562 1.00 40.08  ? 1011 HOH A O   1 
HETATM 3427 O O   . HOH C 2 .   ? 41.936 53.590 -2.441  1.00 8.38   ? 1012 HOH A O   1 
HETATM 3428 O O   . HOH C 2 .   ? 49.472 41.795 3.606   1.00 19.86  ? 1013 HOH A O   1 
HETATM 3429 O O   . HOH C 2 .   ? 50.971 47.225 -4.630  1.00 23.51  ? 1014 HOH A O   1 
HETATM 3430 O O   . HOH C 2 .   ? 45.824 48.876 -10.704 1.00 23.95  ? 1015 HOH A O   1 
HETATM 3431 O O   . HOH C 2 .   ? 45.713 42.608 -15.495 1.00 27.04  ? 1016 HOH A O   1 
HETATM 3432 O O   . HOH C 2 .   ? 18.641 28.130 6.724   1.00 31.93  ? 1017 HOH A O   1 
HETATM 3433 O O   . HOH C 2 .   ? 25.145 37.827 20.577  1.00 20.92  ? 1018 HOH A O   1 
HETATM 3434 O O   . HOH C 2 .   ? 23.916 30.881 15.906  1.00 28.26  ? 1019 HOH A O   1 
HETATM 3435 O O   . HOH C 2 .   ? 47.757 45.309 -11.337 1.00 17.16  ? 1020 HOH A O   1 
HETATM 3436 O O   . HOH C 2 .   ? 44.574 51.022 10.678  1.00 20.44  ? 1021 HOH A O   1 
HETATM 3437 O O   . HOH C 2 .   ? 36.520 63.499 -1.562  1.00 31.28  ? 1022 HOH A O   1 
HETATM 3438 O O   . HOH C 2 .   ? 30.039 41.004 15.262  1.00 15.53  ? 1023 HOH A O   1 
HETATM 3439 O O   . HOH C 2 .   ? 48.023 57.698 -9.986  1.00 28.41  ? 1024 HOH A O   1 
HETATM 3440 O O   . HOH C 2 .   ? 44.666 55.484 4.676   1.00 15.36  ? 1025 HOH A O   1 
HETATM 3441 O O   . HOH C 2 .   ? 47.421 55.950 -15.200 1.00 20.08  ? 1026 HOH A O   1 
HETATM 3442 O O   . HOH C 2 .   ? 25.072 33.292 17.652  1.00 28.63  ? 1027 HOH A O   1 
HETATM 3443 O O   . HOH C 2 .   ? 47.635 50.127 -8.897  1.00 18.50  ? 1028 HOH A O   1 
HETATM 3444 O O   . HOH C 2 .   ? 42.767 57.802 -12.140 1.00 17.29  ? 1029 HOH A O   1 
HETATM 3445 O O   . HOH C 2 .   ? 42.830 32.107 -10.052 1.00 22.62  ? 1030 HOH A O   1 
HETATM 3446 O O   . HOH C 2 .   ? 36.330 35.036 -17.050 1.00 24.63  ? 1031 HOH A O   1 
HETATM 3447 O O   . HOH C 2 .   ? 27.655 39.067 18.490  1.00 31.70  ? 1032 HOH A O   1 
HETATM 3448 O O   . HOH C 2 .   ? 52.831 45.226 -2.228  1.00 24.89  ? 1033 HOH A O   1 
HETATM 3449 O O   . HOH C 2 .   ? 25.411 41.533 -3.712  1.00 31.40  ? 1034 HOH A O   1 
HETATM 3450 O O   . HOH C 2 .   ? 22.772 45.033 15.663  1.00 26.48  ? 1035 HOH A O   1 
HETATM 3451 O O   . HOH C 2 .   ? 48.716 28.454 -8.622  1.00 39.94  ? 1036 HOH A O   1 
HETATM 3452 O O   . HOH C 2 .   ? 46.682 27.322 -5.526  1.00 27.25  ? 1037 HOH A O   1 
HETATM 3453 O O   . HOH C 2 .   ? 49.061 35.874 -5.602  1.00 34.76  ? 1038 HOH A O   1 
HETATM 3454 O O   . HOH C 2 .   ? 45.967 47.817 -15.810 1.00 19.42  ? 1039 HOH A O   1 
HETATM 3455 O O   . HOH C 2 .   ? 52.344 49.867 -8.006  1.00 21.22  ? 1040 HOH A O   1 
HETATM 3456 O O   . HOH C 2 .   ? 21.292 29.005 3.105   1.00 23.48  ? 1041 HOH A O   1 
HETATM 3457 O O   . HOH C 2 .   ? 14.642 56.657 7.726   1.00 22.54  ? 1042 HOH A O   1 
HETATM 3458 O O   . HOH C 2 .   ? 48.926 46.634 -6.445  1.00 15.80  ? 1043 HOH A O   1 
HETATM 3459 O O   . HOH C 2 .   ? 48.469 38.612 -14.405 1.00 31.87  ? 1044 HOH A O   1 
HETATM 3460 O O   . HOH C 2 .   ? 53.691 31.497 -6.138  1.00 42.56  ? 1045 HOH A O   1 
HETATM 3461 O O   . HOH C 2 .   ? 24.875 26.524 -4.036  1.00 24.57  ? 1046 HOH A O   1 
HETATM 3462 O O   . HOH C 2 .   ? 20.630 41.244 16.450  1.00 24.59  ? 1047 HOH A O   1 
HETATM 3463 O O   . HOH C 2 .   ? 26.356 59.980 3.669   1.00 36.15  ? 1048 HOH A O   1 
HETATM 3464 O O   . HOH C 2 .   ? 44.939 28.541 11.756  1.00 24.62  ? 1049 HOH A O   1 
HETATM 3465 O O   . HOH C 2 .   ? 50.131 50.524 2.492   1.00 25.38  ? 1050 HOH A O   1 
HETATM 3466 O O   . HOH C 2 .   ? 39.885 29.093 17.104  1.00 26.66  ? 1051 HOH A O   1 
HETATM 3467 O O   . HOH C 2 .   ? 29.450 55.614 -3.989  1.00 28.73  ? 1052 HOH A O   1 
HETATM 3468 O O   . HOH C 2 .   ? 46.373 48.894 -3.573  1.00 18.81  ? 1053 HOH A O   1 
HETATM 3469 O O   . HOH C 2 .   ? 39.317 22.528 3.070   1.00 24.30  ? 1054 HOH A O   1 
HETATM 3470 O O   . HOH C 2 .   ? 35.639 24.361 7.600   1.00 35.31  ? 1055 HOH A O   1 
HETATM 3471 O O   . HOH C 2 .   ? 27.599 23.804 11.079  1.00 41.53  ? 1056 HOH A O   1 
HETATM 3472 O O   . HOH C 2 .   ? 34.417 35.430 -3.868  1.00 10.76  ? 1057 HOH A O   1 
HETATM 3473 O O   . HOH C 2 .   ? 45.775 47.559 -13.511 1.00 23.21  ? 1058 HOH A O   1 
HETATM 3474 O O   . HOH C 2 .   ? 37.124 45.699 -19.921 1.00 30.17  ? 1059 HOH A O   1 
HETATM 3475 O O   . HOH C 2 .   ? 21.969 42.634 -9.878  1.00 26.32  ? 1060 HOH A O   1 
HETATM 3476 O O   . HOH C 2 .   ? 38.168 33.418 16.900  1.00 26.61  ? 1061 HOH A O   1 
HETATM 3477 O O   . HOH C 2 .   ? 57.217 45.952 1.247   1.00 37.08  ? 1062 HOH A O   1 
HETATM 3478 O O   . HOH C 2 .   ? 32.165 51.996 -6.437  1.00 18.29  ? 1063 HOH A O   1 
HETATM 3479 O O   . HOH C 2 .   ? 31.992 24.615 10.789  1.00 24.95  ? 1064 HOH A O   1 
HETATM 3480 O O   . HOH C 2 .   ? 40.450 62.129 4.384   1.00 20.29  ? 1065 HOH A O   1 
HETATM 3481 O O   . HOH C 2 .   ? 33.384 58.634 2.104   1.00 22.18  ? 1066 HOH A O   1 
HETATM 3482 O O   . HOH C 2 .   ? 32.747 19.634 2.139   1.00 33.06  ? 1067 HOH A O   1 
HETATM 3483 O O   . HOH C 2 .   ? 45.093 56.276 -18.842 1.00 38.23  ? 1068 HOH A O   1 
HETATM 3484 O O   . HOH C 2 .   ? 22.514 40.966 2.439   1.00 27.45  ? 1069 HOH A O   1 
HETATM 3485 O O   . HOH C 2 .   ? 16.757 53.631 14.240  1.00 20.82  ? 1070 HOH A O   1 
HETATM 3486 O O   . HOH C 2 .   ? 36.324 45.331 14.378  1.00 28.11  ? 1071 HOH A O   1 
HETATM 3487 O O   . HOH C 2 .   ? 42.997 53.720 -5.383  1.00 13.88  ? 1072 HOH A O   1 
HETATM 3488 O O   . HOH C 2 .   ? 42.366 36.956 16.705  1.00 41.88  ? 1073 HOH A O   1 
HETATM 3489 O O   . HOH C 2 .   ? 43.627 66.053 4.377   1.00 21.79  ? 1074 HOH A O   1 
HETATM 3490 O O   . HOH C 2 .   ? 35.176 46.366 -18.524 1.00 29.90  ? 1075 HOH A O   1 
HETATM 3491 O O   . HOH C 2 .   ? 33.095 44.259 15.019  1.00 22.44  ? 1076 HOH A O   1 
HETATM 3492 O O   . HOH C 2 .   ? 45.545 49.638 -18.916 1.00 32.23  ? 1077 HOH A O   1 
HETATM 3493 O O   . HOH C 2 .   ? 28.044 57.232 -9.767  1.00 26.33  ? 1078 HOH A O   1 
HETATM 3494 O O   . HOH C 2 .   ? 32.860 48.468 14.056  1.00 19.87  ? 1079 HOH A O   1 
HETATM 3495 O O   . HOH C 2 .   ? 46.800 48.195 -6.469  1.00 21.78  ? 1080 HOH A O   1 
HETATM 3496 O O   . HOH C 2 .   ? 33.946 20.644 4.249   1.00 20.82  ? 1081 HOH A O   1 
HETATM 3497 O O   . HOH C 2 .   ? 48.939 36.482 -10.996 1.00 32.76  ? 1082 HOH A O   1 
HETATM 3498 O O   . HOH C 2 .   ? 41.070 58.256 -20.804 1.00 33.53  ? 1083 HOH A O   1 
HETATM 3499 O O   . HOH C 2 .   ? 41.839 39.335 15.558  1.00 33.91  ? 1084 HOH A O   1 
HETATM 3500 O O   . HOH C 2 .   ? 32.007 56.332 1.262   1.00 14.24  ? 1085 HOH A O   1 
HETATM 3501 O O   . HOH C 2 .   ? 38.330 33.658 -16.598 1.00 29.83  ? 1086 HOH A O   1 
HETATM 3502 O O   . HOH C 2 .   ? 27.630 30.914 -14.534 1.00 25.16  ? 1087 HOH A O   1 
HETATM 3503 O O   . HOH C 2 .   ? 29.330 55.869 -0.741  1.00 18.77  ? 1088 HOH A O   1 
HETATM 3504 O O   . HOH C 2 .   ? 43.463 23.810 -5.567  1.00 19.21  ? 1089 HOH A O   1 
HETATM 3505 O O   . HOH C 2 .   ? 27.243 22.696 -2.779  1.00 32.94  ? 1090 HOH A O   1 
HETATM 3506 O O   . HOH C 2 .   ? 39.322 24.938 16.425  1.00 37.19  ? 1091 HOH A O   1 
HETATM 3507 O O   . HOH C 2 .   ? 8.731  29.395 19.079  1.00 30.28  ? 1092 HOH A O   1 
HETATM 3508 O O   . HOH C 2 .   ? 39.268 25.580 -3.871  1.00 17.23  ? 1093 HOH A O   1 
HETATM 3509 O O   . HOH C 2 .   ? 29.334 58.665 0.939   1.00 25.71  ? 1094 HOH A O   1 
HETATM 3510 O O   . HOH C 2 .   ? 44.874 38.950 -16.487 1.00 28.82  ? 1095 HOH A O   1 
HETATM 3511 O O   . HOH C 2 .   ? 45.846 59.149 -10.067 1.00 29.82  ? 1096 HOH A O   1 
HETATM 3512 O O   . HOH C 2 .   ? 32.397 55.125 -7.210  1.00 16.62  ? 1097 HOH A O   1 
HETATM 3513 O O   . HOH C 2 .   ? 20.542 36.498 -1.991  1.00 29.34  ? 1098 HOH A O   1 
HETATM 3514 O O   . HOH C 2 .   ? 45.717 57.188 4.033   1.00 24.20  ? 1099 HOH A O   1 
HETATM 3515 O O   . HOH C 2 .   ? 28.063 48.964 -14.303 1.00 36.99  ? 1100 HOH A O   1 
HETATM 3516 O O   . HOH C 2 .   ? 16.305 51.480 -11.198 1.00 50.91  ? 1101 HOH A O   1 
HETATM 3517 O O   . HOH C 2 .   ? 42.527 57.519 5.336   1.00 28.29  ? 1102 HOH A O   1 
HETATM 3518 O O   . HOH C 2 .   ? 19.557 31.225 -0.598  1.00 28.36  ? 1103 HOH A O   1 
HETATM 3519 O O   . HOH C 2 .   ? 49.418 50.223 4.627   1.00 20.56  ? 1104 HOH A O   1 
HETATM 3520 O O   . HOH C 2 .   ? 46.138 51.661 -17.963 1.00 37.73  ? 1105 HOH A O   1 
HETATM 3521 O O   . HOH C 2 .   ? 43.532 36.837 -14.826 1.00 20.70  ? 1106 HOH A O   1 
HETATM 3522 O O   . HOH C 2 .   ? 24.521 43.496 -3.155  1.00 29.27  ? 1107 HOH A O   1 
HETATM 3523 O O   . HOH C 2 .   ? 34.200 32.732 -14.773 1.00 21.79  ? 1108 HOH A O   1 
HETATM 3524 O O   . HOH C 2 .   ? 27.987 32.818 21.754  1.00 35.99  ? 1109 HOH A O   1 
HETATM 3525 O O   . HOH C 2 .   ? 14.854 37.356 8.812   1.00 25.77  ? 1110 HOH A O   1 
HETATM 3526 O O   . HOH C 2 .   ? 25.919 34.923 -12.829 1.00 30.05  ? 1111 HOH A O   1 
HETATM 3527 O O   . HOH C 2 .   ? 23.504 44.792 17.762  1.00 31.57  ? 1112 HOH A O   1 
HETATM 3528 O O   . HOH C 2 .   ? 22.321 38.532 -3.159  1.00 27.66  ? 1113 HOH A O   1 
HETATM 3529 O O   . HOH C 2 .   ? 27.667 46.553 -15.573 1.00 40.01  ? 1114 HOH A O   1 
HETATM 3530 O O   . HOH C 2 .   ? 25.539 55.064 1.731   1.00 31.39  ? 1115 HOH A O   1 
HETATM 3531 O O   . HOH C 2 .   ? 25.606 43.963 18.358  1.00 35.36  ? 1116 HOH A O   1 
HETATM 3532 O O   . HOH C 2 .   ? 46.212 39.398 -14.364 1.00 35.25  ? 1117 HOH A O   1 
HETATM 3533 O O   . HOH C 2 .   ? 16.886 42.521 14.780  1.00 40.10  ? 1118 HOH A O   1 
HETATM 3534 O O   . HOH C 2 .   ? 26.046 52.496 2.749   1.00 33.19  ? 1119 HOH A O   1 
HETATM 3535 O O   . HOH C 2 .   ? 30.969 31.578 18.600  1.00 31.40  ? 1120 HOH A O   1 
HETATM 3536 O O   . HOH C 2 .   ? 49.344 27.254 -10.633 1.00 41.94  ? 1121 HOH A O   1 
HETATM 3537 O O   . HOH C 2 .   ? 52.037 27.832 -9.818  1.00 31.98  ? 1122 HOH A O   1 
HETATM 3538 O O   . HOH C 2 .   ? 53.738 31.938 -9.662  1.00 38.49  ? 1123 HOH A O   1 
HETATM 3539 O O   . HOH C 2 .   ? 15.250 30.966 -0.247  1.00 30.24  ? 1124 HOH A O   1 
HETATM 3540 O O   . HOH C 2 .   ? 36.168 63.310 0.570   1.00 33.28  ? 1125 HOH A O   1 
HETATM 3541 O O   . HOH C 2 .   ? 36.909 54.673 10.072  1.00 34.21  ? 1126 HOH A O   1 
HETATM 3542 O O   . HOH C 2 .   ? 47.261 34.243 10.513  1.00 30.97  ? 1127 HOH A O   1 
HETATM 3543 O O   . HOH C 2 .   ? 21.908 36.734 -4.752  1.00 31.31  ? 1128 HOH A O   1 
HETATM 3544 O O   . HOH C 2 .   ? 32.301 20.196 5.628   1.00 32.76  ? 1129 HOH A O   1 
HETATM 3545 O O   . HOH C 2 .   ? 13.251 56.407 12.058  1.00 28.45  ? 1130 HOH A O   1 
HETATM 3546 O O   . HOH C 2 .   ? 48.020 23.696 -10.860 1.00 30.02  ? 1131 HOH A O   1 
HETATM 3547 O O   . HOH C 2 .   ? 24.603 59.199 4.820   1.00 27.87  ? 1132 HOH A O   1 
HETATM 3548 O O   . HOH C 2 .   ? 49.533 49.122 -10.251 1.00 33.78  ? 1133 HOH A O   1 
HETATM 3549 O O   . HOH C 2 .   ? 48.528 49.398 -13.794 1.00 34.50  ? 1134 HOH A O   1 
HETATM 3550 O O   . HOH C 2 .   ? 37.692 57.120 7.825   1.00 28.31  ? 1135 HOH A O   1 
HETATM 3551 O O   . HOH C 2 .   ? 36.726 22.077 11.316  1.00 44.92  ? 1136 HOH A O   1 
HETATM 3552 O O   . HOH C 2 .   ? 17.460 37.172 -1.051  1.00 35.18  ? 1137 HOH A O   1 
HETATM 3553 O O   . HOH C 2 .   ? 20.587 40.701 -9.937  1.00 37.34  ? 1138 HOH A O   1 
HETATM 3554 O O   . HOH C 2 .   ? 29.986 51.666 -6.828  1.00 26.71  ? 1139 HOH A O   1 
HETATM 3555 O O   . HOH C 2 .   ? 44.409 28.054 -16.751 1.00 40.00  ? 1140 HOH A O   1 
HETATM 3556 O O   . HOH C 2 .   ? 26.101 58.852 0.628   1.00 32.74  ? 1141 HOH A O   1 
HETATM 3557 O O   . HOH C 2 .   ? 24.229 48.027 -0.301  1.00 31.12  ? 1142 HOH A O   1 
HETATM 3558 O O   . HOH C 2 .   ? 45.113 60.909 -7.718  1.00 17.82  ? 1143 HOH A O   1 
HETATM 3559 O O   . HOH C 2 .   ? 37.956 30.944 17.146  1.00 32.08  ? 1144 HOH A O   1 
HETATM 3560 O O   . HOH C 2 .   ? 36.383 60.365 6.594   1.00 32.26  ? 1145 HOH A O   1 
HETATM 3561 O O   . HOH C 2 .   ? 38.067 20.442 7.035   1.00 43.51  ? 1146 HOH A O   1 
HETATM 3562 O O   . HOH C 2 .   ? 22.411 45.875 0.627   1.00 31.49  ? 1147 HOH A O   1 
HETATM 3563 O O   . HOH C 2 .   ? 34.957 24.729 12.450  1.00 31.23  ? 1148 HOH A O   1 
HETATM 3564 O O   . HOH C 2 .   ? 19.500 32.967 -2.049  1.00 31.30  ? 1149 HOH A O   1 
HETATM 3565 O O   . HOH C 2 .   ? 20.710 35.973 -6.498  1.00 30.61  ? 1150 HOH A O   1 
HETATM 3566 O O   . HOH C 2 .   ? 12.660 36.746 8.740   1.00 29.38  ? 1151 HOH A O   1 
HETATM 3567 O O   . HOH C 2 .   ? 49.558 35.505 10.189  1.00 34.44  ? 1152 HOH A O   1 
HETATM 3568 O O   . HOH C 2 .   ? 46.348 36.028 -11.207 1.00 40.47  ? 1153 HOH A O   1 
HETATM 3569 O O   . HOH C 2 .   ? 15.235 36.523 -1.020  1.00 49.94  ? 1154 HOH A O   1 
HETATM 3570 O O   . HOH C 2 .   ? 34.728 19.853 7.578   1.00 34.26  ? 1155 HOH A O   1 
HETATM 3571 O O   . HOH C 2 .   ? 48.354 40.135 5.044   1.00 23.50  ? 1156 HOH A O   1 
HETATM 3572 O O   . HOH C 2 .   ? 11.205 41.351 8.967   1.00 41.75  ? 1157 HOH A O   1 
HETATM 3573 O O   . HOH C 2 .   ? 36.717 60.617 9.253   1.00 42.03  ? 1158 HOH A O   1 
HETATM 3574 O O   . HOH C 2 .   ? 52.038 41.589 4.772   1.00 33.25  ? 1159 HOH A O   1 
HETATM 3575 O O   . HOH C 2 .   ? 38.249 20.347 9.242   1.00 37.41  ? 1160 HOH A O   1 
HETATM 3576 O O   . HOH C 2 .   ? 46.161 53.688 -19.115 1.00 34.70  ? 1161 HOH A O   1 
HETATM 3577 O O   . HOH C 2 .   ? 15.415 39.160 7.765   1.00 26.86  ? 1162 HOH A O   1 
HETATM 3578 O O   . HOH C 2 .   ? 21.075 40.681 -3.364  1.00 29.99  ? 1163 HOH A O   1 
HETATM 3579 O O   . HOH C 2 .   ? 13.692 48.876 13.669  1.00 34.76  ? 1164 HOH A O   1 
HETATM 3580 O O   . HOH C 2 .   ? 27.207 27.858 14.338  1.00 32.65  ? 1165 HOH A O   1 
HETATM 3581 O O   . HOH C 2 .   ? 20.074 38.724 -9.151  1.00 29.53  ? 1166 HOH A O   1 
HETATM 3582 O O   . HOH C 2 .   ? 14.802 32.261 -10.612 1.00 35.24  ? 1167 HOH A O   1 
HETATM 3583 O O   . HOH C 2 .   ? 30.831 17.668 -1.530  1.00 34.49  ? 1168 HOH A O   1 
HETATM 3584 O O   . HOH C 2 .   ? 25.009 28.544 15.642  1.00 41.84  ? 1169 HOH A O   1 
HETATM 3585 O O   . HOH C 2 .   ? 45.890 46.829 -9.885  1.00 31.24  ? 1170 HOH A O   1 
HETATM 3586 O O   . HOH C 2 .   ? 21.414 39.854 1.060   1.00 35.48  ? 1171 HOH A O   1 
HETATM 3587 O O   . HOH C 2 .   ? 22.366 42.686 -3.200  1.00 39.87  ? 1172 HOH A O   1 
HETATM 3588 O O   . HOH C 2 .   ? 30.758 60.717 6.514   1.00 31.48  ? 1173 HOH A O   1 
HETATM 3589 O O   . HOH C 2 .   ? 19.451 42.197 -8.229  1.00 26.37  ? 1174 HOH A O   1 
HETATM 3590 O O   . HOH C 2 .   ? 57.787 40.865 6.543   1.00 36.01  ? 1175 HOH A O   1 
HETATM 3591 O O   . HOH C 2 .   ? 48.196 34.205 8.361   1.00 27.76  ? 1176 HOH A O   1 
HETATM 3592 O O   . HOH C 2 .   ? 37.998 62.792 5.281   1.00 30.59  ? 1177 HOH A O   1 
HETATM 3593 O O   . HOH C 2 .   ? 49.181 39.806 7.174   1.00 31.09  ? 1178 HOH A O   1 
HETATM 3594 O O   . HOH C 2 .   ? 28.124 28.168 16.593  1.00 39.15  ? 1179 HOH A O   1 
HETATM 3595 O O   . HOH C 2 .   ? 46.314 47.402 16.830  1.00 42.13  ? 1180 HOH A O   1 
HETATM 3596 O O   . HOH C 2 .   ? 26.510 37.215 -13.867 1.00 30.37  ? 1181 HOH A O   1 
HETATM 3597 O O   . HOH C 2 .   ? 34.595 24.957 16.069  1.00 36.08  ? 1182 HOH A O   1 
HETATM 3598 O O   . HOH C 2 .   ? 49.821 37.393 6.668   1.00 35.38  ? 1183 HOH A O   1 
HETATM 3599 O O   . HOH C 2 .   ? 48.252 46.804 15.516  1.00 28.26  ? 1184 HOH A O   1 
HETATM 3600 O O   . HOH C 2 .   ? 34.680 62.697 7.180   1.00 30.68  ? 1185 HOH A O   1 
HETATM 3601 O O   . HOH C 2 .   ? 32.139 62.693 4.413   1.00 40.43  ? 1186 HOH A O   1 
HETATM 3602 O O   . HOH C 2 .   ? 17.452 34.647 -4.031  1.00 27.98  ? 1187 HOH A O   1 
HETATM 3603 O O   . HOH C 2 .   ? 12.490 51.210 14.984  1.00 39.08  ? 1188 HOH A O   1 
HETATM 3604 O O   . HOH C 2 .   ? 14.410 35.339 -10.225 1.00 29.76  ? 1189 HOH A O   1 
HETATM 3605 O O   . HOH C 2 .   ? 37.421 62.462 7.622   1.00 33.42  ? 1190 HOH A O   1 
HETATM 3606 O O   . HOH D 2 .   ? 18.048 44.438 33.627  1.00 17.47  ? 901  HOH B O   1 
HETATM 3607 O O   . HOH D 2 .   ? 35.245 63.879 27.362  1.00 31.96  ? 902  HOH B O   1 
HETATM 3608 O O   . HOH D 2 .   ? 38.513 56.082 20.963  1.00 25.31  ? 903  HOH B O   1 
HETATM 3609 O O   . HOH D 2 .   ? 9.174  48.563 38.818  1.00 31.15  ? 904  HOH B O   1 
HETATM 3610 O O   . HOH D 2 .   ? 24.313 58.313 30.612  1.00 34.64  ? 905  HOH B O   1 
HETATM 3611 O O   . HOH D 2 .   ? 46.393 49.053 37.020  1.00 37.08  ? 906  HOH B O   1 
HETATM 3612 O O   . HOH D 2 .   ? 23.693 26.857 43.228  1.00 30.67  ? 907  HOH B O   1 
HETATM 3613 O O   . HOH D 2 .   ? 34.874 64.933 29.791  1.00 36.46  ? 908  HOH B O   1 
HETATM 3614 O O   . HOH D 2 .   ? 26.671 27.015 47.190  1.00 29.71  ? 909  HOH B O   1 
HETATM 3615 O O   . HOH D 2 .   ? 43.143 41.284 34.708  1.00 34.05  ? 910  HOH B O   1 
HETATM 3616 O O   . HOH D 2 .   ? 15.029 40.523 53.294  1.00 34.36  ? 911  HOH B O   1 
HETATM 3617 O O   . HOH D 2 .   ? 18.356 33.984 21.410  1.00 30.96  ? 912  HOH B O   1 
HETATM 3618 O O   . HOH D 2 .   ? 45.414 51.883 33.862  1.00 33.15  ? 913  HOH B O   1 
HETATM 3619 O O   . HOH D 2 .   ? 37.319 63.262 31.754  1.00 19.20  ? 914  HOH B O   1 
HETATM 3620 O O   . HOH D 2 .   ? 17.620 60.567 47.844  1.00 28.19  ? 915  HOH B O   1 
HETATM 3621 O O   . HOH D 2 .   ? 21.197 63.757 40.158  1.00 37.89  ? 916  HOH B O   1 
HETATM 3622 O O   . HOH D 2 .   ? 42.365 46.583 27.883  1.00 25.25  ? 917  HOH B O   1 
HETATM 3623 O O   . HOH D 2 .   ? 20.932 43.151 22.005  1.00 28.74  ? 918  HOH B O   1 
HETATM 3624 O O   . HOH D 2 .   ? 7.886  55.593 42.741  1.00 29.20  ? 919  HOH B O   1 
HETATM 3625 O O   . HOH D 2 .   ? 30.946 25.753 42.442  1.00 34.09  ? 920  HOH B O   1 
HETATM 3626 O O   . HOH D 2 .   ? 30.827 32.393 36.178  1.00 19.59  ? 921  HOH B O   1 
HETATM 3627 O O   . HOH D 2 .   ? 26.275 29.629 45.871  1.00 29.97  ? 922  HOH B O   1 
HETATM 3628 O O   . HOH D 2 .   ? 37.787 49.282 13.075  1.00 26.89  ? 923  HOH B O   1 
HETATM 3629 O O   . HOH D 2 .   ? -1.143 42.448 45.310  1.00 30.05  ? 924  HOH B O   1 
HETATM 3630 O O   . HOH D 2 .   ? 5.472  41.210 54.430  1.00 31.33  ? 925  HOH B O   1 
HETATM 3631 O O   . HOH D 2 .   ? 14.094 46.948 25.200  1.00 39.75  ? 926  HOH B O   1 
HETATM 3632 O O   . HOH D 2 .   ? 13.754 49.802 38.461  1.00 28.96  ? 927  HOH B O   1 
HETATM 3633 O O   . HOH D 2 .   ? 27.562 51.960 19.018  1.00 21.95  ? 928  HOH B O   1 
HETATM 3634 O O   . HOH D 2 .   ? 44.086 53.094 29.523  1.00 30.21  ? 929  HOH B O   1 
HETATM 3635 O O   . HOH D 2 .   ? 7.792  33.434 38.582  1.00 35.61  ? 930  HOH B O   1 
HETATM 3636 O O   . HOH D 2 .   ? 39.841 39.488 40.372  1.00 25.71  ? 931  HOH B O   1 
HETATM 3637 O O   . HOH D 2 .   ? 29.799 58.106 46.435  1.00 26.86  ? 932  HOH B O   1 
HETATM 3638 O O   . HOH D 2 .   ? 14.120 38.840 49.346  1.00 19.28  ? 933  HOH B O   1 
HETATM 3639 O O   . HOH D 2 .   ? 25.956 27.137 50.694  1.00 38.98  ? 934  HOH B O   1 
HETATM 3640 O O   . HOH D 2 .   ? 36.055 66.641 31.985  1.00 30.16  ? 935  HOH B O   1 
HETATM 3641 O O   . HOH D 2 .   ? 21.916 54.405 29.638  1.00 34.60  ? 936  HOH B O   1 
HETATM 3642 O O   . HOH D 2 .   ? 21.623 23.727 36.854  1.00 31.59  ? 937  HOH B O   1 
HETATM 3643 O O   . HOH D 2 .   ? 13.821 52.523 38.886  1.00 26.17  ? 938  HOH B O   1 
HETATM 3644 O O   . HOH D 2 .   ? 39.897 48.006 25.952  1.00 21.87  ? 939  HOH B O   1 
HETATM 3645 O O   . HOH D 2 .   ? 17.250 39.466 31.299  1.00 12.17  ? 940  HOH B O   1 
HETATM 3646 O O   . HOH D 2 .   ? 15.271 62.083 47.140  1.00 26.25  ? 941  HOH B O   1 
HETATM 3647 O O   . HOH D 2 .   ? 30.991 50.633 15.170  1.00 28.72  ? 942  HOH B O   1 
HETATM 3648 O O   . HOH D 2 .   ? 37.780 60.897 33.653  1.00 22.11  ? 943  HOH B O   1 
HETATM 3649 O O   . HOH D 2 .   ? 18.308 24.737 34.551  1.00 29.76  ? 944  HOH B O   1 
HETATM 3650 O O   . HOH D 2 .   ? 29.915 35.232 23.533  1.00 22.28  ? 945  HOH B O   1 
HETATM 3651 O O   . HOH D 2 .   ? 22.460 52.230 44.890  1.00 15.59  ? 946  HOH B O   1 
HETATM 3652 O O   . HOH D 2 .   ? 33.743 58.320 29.129  1.00 17.65  ? 947  HOH B O   1 
HETATM 3653 O O   . HOH D 2 .   ? 13.991 52.018 51.395  1.00 34.25  ? 948  HOH B O   1 
HETATM 3654 O O   . HOH D 2 .   ? 24.391 40.001 53.186  1.00 21.19  ? 949  HOH B O   1 
HETATM 3655 O O   . HOH D 2 .   ? 34.098 35.290 26.458  1.00 23.03  ? 950  HOH B O   1 
HETATM 3656 O O   . HOH D 2 .   ? 7.525  58.846 24.579  1.00 38.98  ? 951  HOH B O   1 
HETATM 3657 O O   . HOH D 2 .   ? 15.431 31.309 44.076  1.00 33.03  ? 952  HOH B O   1 
HETATM 3658 O O   . HOH D 2 .   ? 6.951  54.235 48.902  1.00 21.91  ? 953  HOH B O   1 
HETATM 3659 O O   . HOH D 2 .   ? 15.207 37.410 57.287  1.00 31.67  ? 954  HOH B O   1 
HETATM 3660 O O   . HOH D 2 .   ? 31.933 58.787 41.389  1.00 18.36  ? 955  HOH B O   1 
HETATM 3661 O O   . HOH D 2 .   ? 44.840 34.522 30.575  1.00 37.87  ? 956  HOH B O   1 
HETATM 3662 O O   . HOH D 2 .   ? 37.186 26.962 29.734  1.00 25.14  ? 957  HOH B O   1 
HETATM 3663 O O   . HOH D 2 .   ? 28.270 36.054 50.948  1.00 26.58  ? 958  HOH B O   1 
HETATM 3664 O O   . HOH D 2 .   ? 16.454 54.375 52.779  1.00 30.49  ? 959  HOH B O   1 
HETATM 3665 O O   . HOH D 2 .   ? 42.197 50.589 33.551  1.00 28.81  ? 960  HOH B O   1 
HETATM 3666 O O   . HOH D 2 .   ? 39.700 45.122 41.352  1.00 23.76  ? 961  HOH B O   1 
HETATM 3667 O O   . HOH D 2 .   ? 9.273  47.350 49.175  1.00 29.73  ? 962  HOH B O   1 
HETATM 3668 O O   . HOH D 2 .   ? 13.860 33.097 21.210  1.00 29.99  ? 963  HOH B O   1 
HETATM 3669 O O   . HOH D 2 .   ? 7.280  53.452 44.637  1.00 33.84  ? 964  HOH B O   1 
HETATM 3670 O O   . HOH D 2 .   ? 34.622 54.381 47.355  1.00 23.66  ? 965  HOH B O   1 
HETATM 3671 O O   . HOH D 2 .   ? 16.669 47.502 31.684  1.00 30.03  ? 966  HOH B O   1 
HETATM 3672 O O   . HOH D 2 .   ? 17.110 49.747 24.018  1.00 42.22  ? 967  HOH B O   1 
HETATM 3673 O O   . HOH D 2 .   ? 34.882 40.529 25.102  1.00 27.68  ? 968  HOH B O   1 
HETATM 3674 O O   . HOH D 2 .   ? 36.696 45.367 24.941  1.00 20.27  ? 969  HOH B O   1 
HETATM 3675 O O   . HOH D 2 .   ? 29.285 59.878 17.831  1.00 37.42  ? 970  HOH B O   1 
HETATM 3676 O O   . HOH D 2 .   ? 27.848 43.413 35.448  1.00 10.28  ? 971  HOH B O   1 
HETATM 3677 O O   . HOH D 2 .   ? 32.603 63.765 24.127  1.00 32.68  ? 972  HOH B O   1 
HETATM 3678 O O   . HOH D 2 .   ? 35.928 51.479 35.162  1.00 13.20  ? 973  HOH B O   1 
HETATM 3679 O O   . HOH D 2 .   ? 33.545 56.891 34.671  1.00 11.10  ? 974  HOH B O   1 
HETATM 3680 O O   . HOH D 2 .   ? 35.415 61.220 24.401  1.00 25.16  ? 975  HOH B O   1 
HETATM 3681 O O   . HOH D 2 .   ? 10.195 53.477 51.082  1.00 26.21  ? 976  HOH B O   1 
HETATM 3682 O O   . HOH D 2 .   ? 41.300 54.583 44.303  1.00 37.63  ? 977  HOH B O   1 
HETATM 3683 O O   . HOH D 2 .   ? 20.976 33.874 22.743  1.00 24.70  ? 978  HOH B O   1 
HETATM 3684 O O   . HOH D 2 .   ? 20.271 55.221 40.685  1.00 23.49  ? 979  HOH B O   1 
HETATM 3685 O O   . HOH D 2 .   ? 26.308 25.027 28.815  1.00 31.27  ? 980  HOH B O   1 
HETATM 3686 O O   . HOH D 2 .   ? 43.601 47.128 32.971  1.00 33.22  ? 981  HOH B O   1 
HETATM 3687 O O   . HOH D 2 .   ? 25.558 61.321 47.741  1.00 35.44  ? 982  HOH B O   1 
HETATM 3688 O O   . HOH D 2 .   ? 11.562 34.320 38.094  1.00 29.38  ? 983  HOH B O   1 
HETATM 3689 O O   . HOH D 2 .   ? 33.650 38.034 49.544  1.00 32.78  ? 984  HOH B O   1 
HETATM 3690 O O   . HOH D 2 .   ? 23.747 31.435 45.086  1.00 19.76  ? 985  HOH B O   1 
HETATM 3691 O O   . HOH D 2 .   ? 21.376 25.303 42.309  1.00 28.38  ? 986  HOH B O   1 
HETATM 3692 O O   . HOH D 2 .   ? 25.324 65.021 36.865  1.00 24.47  ? 987  HOH B O   1 
HETATM 3693 O O   . HOH D 2 .   ? 43.269 38.964 30.425  1.00 36.97  ? 988  HOH B O   1 
HETATM 3694 O O   . HOH D 2 .   ? 43.904 48.718 35.756  1.00 33.36  ? 989  HOH B O   1 
HETATM 3695 O O   . HOH D 2 .   ? 43.120 45.927 35.667  1.00 28.80  ? 990  HOH B O   1 
HETATM 3696 O O   . HOH D 2 .   ? 18.705 28.386 42.762  1.00 33.57  ? 991  HOH B O   1 
HETATM 3697 O O   . HOH D 2 .   ? 17.457 38.313 22.968  1.00 25.97  ? 992  HOH B O   1 
HETATM 3698 O O   . HOH D 2 .   ? 37.393 41.083 40.434  1.00 17.41  ? 993  HOH B O   1 
HETATM 3699 O O   . HOH D 2 .   ? 20.423 60.204 36.145  1.00 29.45  ? 994  HOH B O   1 
HETATM 3700 O O   . HOH D 2 .   ? 34.976 28.274 30.946  1.00 39.34  ? 995  HOH B O   1 
HETATM 3701 O O   . HOH D 2 .   ? 25.277 37.898 52.005  1.00 17.48  ? 996  HOH B O   1 
HETATM 3702 O O   . HOH D 2 .   ? 36.729 30.244 31.274  1.00 29.33  ? 997  HOH B O   1 
HETATM 3703 O O   . HOH D 2 .   ? 33.106 30.978 47.043  1.00 28.78  ? 998  HOH B O   1 
HETATM 3704 O O   . HOH D 2 .   ? 5.138  38.029 35.615  1.00 25.03  ? 999  HOH B O   1 
HETATM 3705 O O   . HOH D 2 .   ? 12.694 32.024 42.488  1.00 39.52  ? 1000 HOH B O   1 
HETATM 3706 O O   . HOH D 2 .   ? 27.890 40.148 31.951  1.00 7.78   ? 1001 HOH B O   1 
HETATM 3707 O O   . HOH D 2 .   ? 13.120 43.523 44.481  1.00 19.23  ? 1002 HOH B O   1 
HETATM 3708 O O   . HOH D 2 .   ? 45.872 45.220 36.096  1.00 40.03  ? 1003 HOH B O   1 
HETATM 3709 O O   . HOH D 2 .   ? 40.806 60.696 26.922  1.00 31.57  ? 1004 HOH B O   1 
HETATM 3710 O O   . HOH D 2 .   ? 37.236 41.636 25.830  1.00 22.23  ? 1005 HOH B O   1 
HETATM 3711 O O   . HOH D 2 .   ? 28.330 29.304 22.054  1.00 34.20  ? 1006 HOH B O   1 
HETATM 3712 O O   . HOH D 2 .   ? 19.546 44.695 50.894  1.00 19.61  ? 1007 HOH B O   1 
HETATM 3713 O O   . HOH D 2 .   ? 22.431 28.130 31.290  1.00 22.98  ? 1008 HOH B O   1 
HETATM 3714 O O   . HOH D 2 .   ? 29.948 43.256 16.109  1.00 27.61  ? 1009 HOH B O   1 
HETATM 3715 O O   . HOH D 2 .   ? 34.211 33.502 33.987  1.00 17.63  ? 1010 HOH B O   1 
HETATM 3716 O O   . HOH D 2 .   ? 38.734 38.694 33.721  1.00 19.14  ? 1011 HOH B O   1 
HETATM 3717 O O   . HOH D 2 .   ? 43.342 56.789 36.169  1.00 19.43  ? 1012 HOH B O   1 
HETATM 3718 O O   . HOH D 2 .   ? 31.846 46.695 15.450  1.00 22.15  ? 1013 HOH B O   1 
HETATM 3719 O O   . HOH D 2 .   ? 6.769  47.261 44.495  1.00 29.14  ? 1014 HOH B O   1 
HETATM 3720 O O   . HOH D 2 .   ? 14.627 30.226 41.848  1.00 36.13  ? 1015 HOH B O   1 
HETATM 3721 O O   . HOH D 2 .   ? 38.042 52.029 33.298  1.00 20.07  ? 1016 HOH B O   1 
HETATM 3722 O O   . HOH D 2 .   ? 23.225 60.408 38.187  1.00 29.58  ? 1017 HOH B O   1 
HETATM 3723 O O   . HOH D 2 .   ? 35.734 58.864 41.772  1.00 24.48  ? 1018 HOH B O   1 
HETATM 3724 O O   . HOH D 2 .   ? 36.809 37.365 17.274  1.00 24.54  ? 1019 HOH B O   1 
HETATM 3725 O O   . HOH D 2 .   ? 36.259 64.326 35.560  1.00 24.51  ? 1020 HOH B O   1 
HETATM 3726 O O   . HOH D 2 .   ? 23.346 51.728 50.411  1.00 20.18  ? 1021 HOH B O   1 
HETATM 3727 O O   . HOH D 2 .   ? 24.214 25.080 29.691  1.00 24.10  ? 1022 HOH B O   1 
HETATM 3728 O O   . HOH D 2 .   ? 33.520 28.019 27.797  1.00 35.22  ? 1023 HOH B O   1 
HETATM 3729 O O   . HOH D 2 .   ? 33.397 56.089 14.425  1.00 32.02  ? 1024 HOH B O   1 
HETATM 3730 O O   . HOH D 2 .   ? 38.557 62.538 27.063  1.00 26.60  ? 1025 HOH B O   1 
HETATM 3731 O O   . HOH D 2 .   ? 11.948 35.751 36.376  1.00 18.43  ? 1026 HOH B O   1 
HETATM 3732 O O   . HOH D 2 .   ? 37.887 51.752 26.269  1.00 21.97  ? 1027 HOH B O   1 
HETATM 3733 O O   . HOH D 2 .   ? 21.771 43.472 52.910  1.00 24.28  ? 1028 HOH B O   1 
HETATM 3734 O O   . HOH D 2 .   ? 39.982 53.148 42.490  1.00 26.80  ? 1029 HOH B O   1 
HETATM 3735 O O   . HOH D 2 .   ? 9.428  56.516 51.152  1.00 29.55  ? 1030 HOH B O   1 
HETATM 3736 O O   . HOH D 2 .   ? 29.563 58.043 42.586  1.00 26.90  ? 1031 HOH B O   1 
HETATM 3737 O O   . HOH D 2 .   ? 22.516 33.536 50.425  1.00 25.91  ? 1032 HOH B O   1 
HETATM 3738 O O   . HOH D 2 .   ? 19.436 34.420 51.864  1.00 32.77  ? 1033 HOH B O   1 
HETATM 3739 O O   . HOH D 2 .   ? 15.087 58.173 39.140  1.00 29.19  ? 1034 HOH B O   1 
HETATM 3740 O O   . HOH D 2 .   ? 36.921 60.262 40.850  1.00 24.35  ? 1035 HOH B O   1 
HETATM 3741 O O   . HOH D 2 .   ? 27.957 55.412 48.934  1.00 36.92  ? 1036 HOH B O   1 
HETATM 3742 O O   . HOH D 2 .   ? 40.642 49.413 31.126  1.00 21.10  ? 1037 HOH B O   1 
HETATM 3743 O O   . HOH D 2 .   ? 33.378 35.740 50.895  1.00 37.29  ? 1038 HOH B O   1 
HETATM 3744 O O   . HOH D 2 .   ? 16.507 43.076 53.075  1.00 23.89  ? 1039 HOH B O   1 
HETATM 3745 O O   . HOH D 2 .   ? 37.615 38.680 43.037  1.00 20.14  ? 1040 HOH B O   1 
HETATM 3746 O O   . HOH D 2 .   ? 40.634 53.957 39.991  1.00 25.64  ? 1041 HOH B O   1 
HETATM 3747 O O   . HOH D 2 .   ? 8.088  49.331 45.739  1.00 29.74  ? 1042 HOH B O   1 
HETATM 3748 O O   . HOH D 2 .   ? 35.247 57.174 31.448  1.00 15.59  ? 1043 HOH B O   1 
HETATM 3749 O O   . HOH D 2 .   ? 13.600 45.918 37.284  1.00 26.20  ? 1044 HOH B O   1 
HETATM 3750 O O   . HOH D 2 .   ? 21.961 31.776 48.997  1.00 32.38  ? 1045 HOH B O   1 
HETATM 3751 O O   . HOH D 2 .   ? 31.316 25.519 39.986  1.00 33.33  ? 1046 HOH B O   1 
HETATM 3752 O O   . HOH D 2 .   ? 14.326 28.862 37.276  1.00 33.63  ? 1047 HOH B O   1 
HETATM 3753 O O   . HOH D 2 .   ? 41.923 39.510 32.513  1.00 28.64  ? 1048 HOH B O   1 
HETATM 3754 O O   . HOH D 2 .   ? 13.126 57.704 53.579  1.00 27.68  ? 1049 HOH B O   1 
HETATM 3755 O O   . HOH D 2 .   ? 22.020 28.829 46.002  1.00 35.70  ? 1050 HOH B O   1 
HETATM 3756 O O   . HOH D 2 .   ? 22.870 48.000 50.947  1.00 20.58  ? 1051 HOH B O   1 
HETATM 3757 O O   . HOH D 2 .   ? 39.779 52.844 28.656  1.00 17.96  ? 1052 HOH B O   1 
HETATM 3758 O O   . HOH D 2 .   ? 21.224 53.869 51.874  1.00 30.07  ? 1053 HOH B O   1 
HETATM 3759 O O   . HOH D 2 .   ? 13.091 43.371 33.868  1.00 29.08  ? 1054 HOH B O   1 
HETATM 3760 O O   . HOH D 2 .   ? 38.615 48.963 48.553  1.00 24.40  ? 1055 HOH B O   1 
HETATM 3761 O O   . HOH D 2 .   ? 13.963 33.730 40.907  1.00 29.24  ? 1056 HOH B O   1 
HETATM 3762 O O   . HOH D 2 .   ? 25.088 34.600 50.662  1.00 20.15  ? 1057 HOH B O   1 
HETATM 3763 O O   . HOH D 2 .   ? 27.595 41.759 18.281  1.00 22.98  ? 1058 HOH B O   1 
HETATM 3764 O O   . HOH D 2 .   ? 29.425 29.812 32.950  1.00 14.49  ? 1059 HOH B O   1 
HETATM 3765 O O   . HOH D 2 .   ? 38.738 50.695 20.761  1.00 20.89  ? 1060 HOH B O   1 
HETATM 3766 O O   . HOH D 2 .   ? 30.055 62.936 23.659  1.00 22.28  ? 1061 HOH B O   1 
HETATM 3767 O O   . HOH D 2 .   ? -4.898 39.275 42.628  1.00 30.52  ? 1062 HOH B O   1 
HETATM 3768 O O   . HOH D 2 .   ? 17.928 64.045 40.308  1.00 28.91  ? 1063 HOH B O   1 
HETATM 3769 O O   . HOH D 2 .   ? 35.376 40.169 21.864  1.00 26.82  ? 1064 HOH B O   1 
HETATM 3770 O O   . HOH D 2 .   ? 24.291 56.082 29.388  1.00 24.75  ? 1065 HOH B O   1 
HETATM 3771 O O   . HOH D 2 .   ? 9.915  33.148 37.195  1.00 36.57  ? 1066 HOH B O   1 
HETATM 3772 O O   . HOH D 2 .   ? 25.592 30.805 24.644  1.00 33.54  ? 1067 HOH B O   1 
HETATM 3773 O O   . HOH D 2 .   ? 25.286 39.193 31.961  1.00 10.86  ? 1068 HOH B O   1 
HETATM 3774 O O   . HOH D 2 .   ? 32.511 25.538 51.030  1.00 29.79  ? 1069 HOH B O   1 
HETATM 3775 O O   . HOH D 2 .   ? 18.644 63.057 51.607  1.00 37.29  ? 1070 HOH B O   1 
HETATM 3776 O O   . HOH D 2 .   ? 3.441  42.496 49.963  1.00 36.29  ? 1071 HOH B O   1 
HETATM 3777 O O   . HOH D 2 .   ? 31.551 29.487 24.566  1.00 34.99  ? 1072 HOH B O   1 
HETATM 3778 O O   . HOH D 2 .   ? 5.712  33.633 36.483  1.00 27.25  ? 1073 HOH B O   1 
HETATM 3779 O O   . HOH D 2 .   ? 37.119 55.639 47.405  1.00 30.95  ? 1074 HOH B O   1 
HETATM 3780 O O   . HOH D 2 .   ? 31.461 23.815 47.056  1.00 38.93  ? 1075 HOH B O   1 
HETATM 3781 O O   . HOH D 2 .   ? 7.333  56.821 50.113  1.00 21.10  ? 1076 HOH B O   1 
HETATM 3782 O O   . HOH D 2 .   ? 29.992 62.636 20.962  1.00 29.28  ? 1077 HOH B O   1 
HETATM 3783 O O   . HOH D 2 .   ? 9.662  45.682 50.693  1.00 27.03  ? 1078 HOH B O   1 
HETATM 3784 O O   . HOH D 2 .   ? 25.798 48.474 51.000  1.00 29.16  ? 1079 HOH B O   1 
HETATM 3785 O O   . HOH D 2 .   ? 22.920 24.212 39.358  1.00 27.39  ? 1080 HOH B O   1 
HETATM 3786 O O   . HOH D 2 .   ? 22.465 54.466 21.824  1.00 29.93  ? 1081 HOH B O   1 
HETATM 3787 O O   . HOH D 2 .   ? 42.530 50.535 43.855  1.00 40.56  ? 1082 HOH B O   1 
HETATM 3788 O O   . HOH D 2 .   ? 13.447 36.255 52.399  1.00 36.26  ? 1083 HOH B O   1 
HETATM 3789 O O   . HOH D 2 .   ? 23.793 63.350 43.677  1.00 29.91  ? 1084 HOH B O   1 
HETATM 3790 O O   . HOH D 2 .   ? 11.666 41.705 32.825  1.00 22.47  ? 1085 HOH B O   1 
HETATM 3791 O O   . HOH D 2 .   ? 19.559 37.698 22.266  1.00 28.15  ? 1086 HOH B O   1 
HETATM 3792 O O   . HOH D 2 .   ? 38.261 42.805 22.495  1.00 33.02  ? 1087 HOH B O   1 
HETATM 3793 O O   . HOH D 2 .   ? 12.675 48.770 50.982  1.00 16.31  ? 1088 HOH B O   1 
HETATM 3794 O O   . HOH D 2 .   ? 20.325 26.764 33.738  1.00 21.01  ? 1089 HOH B O   1 
HETATM 3795 O O   . HOH D 2 .   ? 27.320 25.584 45.481  1.00 41.37  ? 1090 HOH B O   1 
HETATM 3796 O O   . HOH D 2 .   ? 28.081 49.941 51.899  1.00 30.65  ? 1091 HOH B O   1 
HETATM 3797 O O   . HOH D 2 .   ? 15.754 35.703 54.127  1.00 32.15  ? 1092 HOH B O   1 
HETATM 3798 O O   . HOH D 2 .   ? 33.371 33.919 24.881  1.00 30.17  ? 1093 HOH B O   1 
HETATM 3799 O O   . HOH D 2 .   ? 19.184 41.374 21.160  1.00 29.45  ? 1094 HOH B O   1 
HETATM 3800 O O   . HOH D 2 .   ? 37.629 38.081 50.491  1.00 39.34  ? 1095 HOH B O   1 
HETATM 3801 O O   . HOH D 2 .   ? -6.189 37.359 48.761  1.00 38.18  ? 1096 HOH B O   1 
HETATM 3802 O O   . HOH D 2 .   ? 7.583  49.180 42.939  1.00 31.64  ? 1097 HOH B O   1 
HETATM 3803 O O   . HOH D 2 .   ? 19.541 52.638 21.313  1.00 32.26  ? 1098 HOH B O   1 
HETATM 3804 O O   . HOH D 2 .   ? 26.606 27.342 44.110  1.00 34.96  ? 1099 HOH B O   1 
HETATM 3805 O O   . HOH D 2 .   ? 28.773 49.747 16.570  1.00 18.43  ? 1100 HOH B O   1 
HETATM 3806 O O   . HOH D 2 .   ? 8.910  31.048 40.434  1.00 24.90  ? 1101 HOH B O   1 
HETATM 3807 O O   . HOH D 2 .   ? 13.349 43.207 31.552  1.00 32.60  ? 1102 HOH B O   1 
HETATM 3808 O O   . HOH D 2 .   ? 18.802 47.121 51.586  1.00 27.93  ? 1103 HOH B O   1 
HETATM 3809 O O   . HOH D 2 .   ? 8.006  50.718 37.844  1.00 40.45  ? 1104 HOH B O   1 
HETATM 3810 O O   . HOH D 2 .   ? 31.361 29.373 26.876  1.00 37.92  ? 1105 HOH B O   1 
HETATM 3811 O O   . HOH D 2 .   ? 10.125 52.518 37.641  1.00 28.51  ? 1106 HOH B O   1 
HETATM 3812 O O   . HOH D 2 .   ? 0.103  35.729 50.007  1.00 33.81  ? 1107 HOH B O   1 
HETATM 3813 O O   . HOH D 2 .   ? 27.540 59.732 48.083  1.00 35.89  ? 1108 HOH B O   1 
HETATM 3814 O O   . HOH D 2 .   ? 35.799 36.439 47.588  1.00 31.32  ? 1109 HOH B O   1 
HETATM 3815 O O   . HOH D 2 .   ? 8.302  42.750 33.701  1.00 30.57  ? 1110 HOH B O   1 
HETATM 3816 O O   . HOH D 2 .   ? 35.336 57.018 13.871  1.00 39.85  ? 1111 HOH B O   1 
HETATM 3817 O O   . HOH D 2 .   ? 14.021 56.790 21.393  1.00 36.53  ? 1112 HOH B O   1 
HETATM 3818 O O   . HOH D 2 .   ? 25.027 58.498 28.574  1.00 38.80  ? 1113 HOH B O   1 
HETATM 3819 O O   . HOH D 2 .   ? 18.144 55.431 38.921  1.00 30.01  ? 1114 HOH B O   1 
HETATM 3820 O O   . HOH D 2 .   ? 44.594 36.468 29.478  1.00 47.13  ? 1115 HOH B O   1 
HETATM 3821 O O   . HOH D 2 .   ? 28.991 60.331 44.312  1.00 42.37  ? 1116 HOH B O   1 
HETATM 3822 O O   . HOH D 2 .   ? 39.272 55.597 18.478  1.00 28.24  ? 1117 HOH B O   1 
HETATM 3823 O O   . HOH D 2 .   ? 43.463 47.686 43.054  1.00 34.68  ? 1118 HOH B O   1 
HETATM 3824 O O   . HOH D 2 .   ? 35.784 36.724 50.832  1.00 47.03  ? 1119 HOH B O   1 
HETATM 3825 O O   . HOH D 2 .   ? 5.524  44.639 41.887  1.00 31.09  ? 1120 HOH B O   1 
HETATM 3826 O O   . HOH D 2 .   ? 27.342 23.186 29.395  1.00 32.25  ? 1121 HOH B O   1 
HETATM 3827 O O   . HOH D 2 .   ? 11.455 41.369 27.775  1.00 33.71  ? 1122 HOH B O   1 
HETATM 3828 O O   . HOH D 2 .   ? 46.020 32.659 30.567  1.00 41.61  ? 1123 HOH B O   1 
HETATM 3829 O O   . HOH D 2 .   ? 40.267 44.453 48.664  1.00 32.22  ? 1124 HOH B O   1 
HETATM 3830 O O   . HOH D 2 .   ? 40.836 46.811 47.368  1.00 29.18  ? 1125 HOH B O   1 
HETATM 3831 O O   . HOH D 2 .   ? 42.852 35.768 26.684  1.00 33.22  ? 1126 HOH B O   1 
HETATM 3832 O O   . HOH D 2 .   ? 37.731 64.414 28.908  1.00 31.20  ? 1127 HOH B O   1 
HETATM 3833 O O   . HOH D 2 .   ? 8.252  37.894 31.785  1.00 39.17  ? 1128 HOH B O   1 
HETATM 3834 O O   . HOH D 2 .   ? 16.660 40.648 21.962  1.00 36.83  ? 1129 HOH B O   1 
HETATM 3835 O O   . HOH D 2 .   ? 12.551 41.334 29.687  1.00 31.46  ? 1130 HOH B O   1 
HETATM 3836 O O   . HOH D 2 .   ? 30.314 27.532 22.454  1.00 43.71  ? 1131 HOH B O   1 
HETATM 3837 O O   . HOH D 2 .   ? 19.350 65.311 42.286  1.00 28.82  ? 1132 HOH B O   1 
HETATM 3838 O O   . HOH D 2 .   ? 4.804  57.631 50.851  1.00 24.26  ? 1133 HOH B O   1 
HETATM 3839 O O   . HOH D 2 .   ? 13.057 38.763 57.029  1.00 35.39  ? 1134 HOH B O   1 
HETATM 3840 O O   . HOH D 2 .   ? 23.838 64.289 47.574  1.00 42.29  ? 1135 HOH B O   1 
HETATM 3841 O O   . HOH D 2 .   ? 4.209  46.182 45.917  1.00 30.95  ? 1136 HOH B O   1 
HETATM 3842 O O   . HOH D 2 .   ? 13.685 41.178 55.808  1.00 41.40  ? 1137 HOH B O   1 
HETATM 3843 O O   . HOH D 2 .   ? 6.136  38.699 31.841  1.00 34.85  ? 1138 HOH B O   1 
HETATM 3844 O O   . HOH D 2 .   ? 23.867 65.164 45.052  1.00 46.17  ? 1139 HOH B O   1 
HETATM 3845 O O   . HOH D 2 .   ? 8.293  40.740 30.948  1.00 27.85  ? 1140 HOH B O   1 
HETATM 3846 O O   . HOH D 2 .   ? 38.921 48.043 51.349  1.00 32.39  ? 1141 HOH B O   1 
HETATM 3847 O O   . HOH D 2 .   ? 21.775 66.108 46.519  1.00 44.54  ? 1142 HOH B O   1 
HETATM 3848 O O   . HOH D 2 .   ? 38.422 43.116 42.616  1.00 25.29  ? 1143 HOH B O   1 
HETATM 3849 O O   . HOH D 2 .   ? 39.840 48.970 19.708  1.00 39.95  ? 1144 HOH B O   1 
HETATM 3850 O O   . HOH D 2 .   ? 12.300 44.509 36.096  1.00 37.12  ? 1145 HOH B O   1 
HETATM 3851 O O   . HOH D 2 .   ? 37.744 37.744 45.244  1.00 33.16  ? 1146 HOH B O   1 
HETATM 3852 O O   . HOH D 2 .   ? 39.218 38.670 47.248  1.00 31.37  ? 1147 HOH B O   1 
HETATM 3853 O O   . HOH D 2 .   ? 39.317 42.343 44.905  1.00 33.09  ? 1148 HOH B O   1 
HETATM 3854 O O   . HOH D 2 .   ? 8.785  44.738 34.735  1.00 35.23  ? 1149 HOH B O   1 
HETATM 3855 O O   . HOH D 2 .   ? 27.947 65.551 42.794  1.00 43.89  ? 1150 HOH B O   1 
HETATM 3856 O O   . HOH D 2 .   ? 28.151 65.424 45.780  1.00 42.12  ? 1151 HOH B O   1 
HETATM 3857 O O   . HOH D 2 .   ? 26.101 67.258 43.489  1.00 32.62  ? 1152 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 2   ? 0.7464 0.8506 0.8293 0.0790  0.0759  0.0329  -1  SER A N   
2    C CA  . SER A 2   ? 0.6542 0.7552 0.7297 0.0688  0.0625  0.0335  -1  SER A CA  
3    C C   . SER A 2   ? 0.6223 0.7157 0.6707 0.0638  0.0637  0.0282  -1  SER A C   
4    O O   . SER A 2   ? 0.4328 0.5260 0.4757 0.0559  0.0543  0.0297  -1  SER A O   
5    C CB  . SER A 2   ? 0.6918 0.8098 0.7887 0.0639  0.0564  0.0445  -1  SER A CB  
6    O OG  . SER A 2   ? 0.5909 0.7145 0.7112 0.0666  0.0515  0.0493  -1  SER A OG  
7    N N   . ASN A 3   ? 0.7200 0.8067 0.7515 0.0686  0.0753  0.0220  684 ASN A N   
8    C CA  . ASN A 3   ? 0.6260 0.7045 0.6292 0.0639  0.0764  0.0167  684 ASN A CA  
9    C C   . ASN A 3   ? 0.5861 0.6516 0.5758 0.0569  0.0636  0.0107  684 ASN A C   
10   O O   . ASN A 3   ? 0.4592 0.5259 0.4388 0.0496  0.0566  0.0121  684 ASN A O   
11   C CB  . ASN A 3   ? 0.6052 0.6739 0.5902 0.0707  0.0906  0.0088  684 ASN A CB  
12   C CG  . ASN A 3   ? 0.7911 0.8533 0.7460 0.0657  0.0930  0.0047  684 ASN A CG  
13   O OD1 . ASN A 3   ? 0.9445 1.0156 0.8968 0.0591  0.0881  0.0111  684 ASN A OD1 
14   N ND2 . ASN A 3   ? 0.7497 0.7952 0.6805 0.0687  0.1001  -0.0060 684 ASN A ND2 
15   N N   . ASN A 4   ? 0.4484 0.5018 0.4392 0.0592  0.0604  0.0046  685 ASN A N   
16   C CA  . ASN A 4   ? 0.2629 0.3036 0.2418 0.0529  0.0499  -0.0015 685 ASN A CA  
17   C C   . ASN A 4   ? 0.1760 0.2210 0.1727 0.0492  0.0388  0.0032  685 ASN A C   
18   O O   . ASN A 4   ? 0.2236 0.2587 0.2137 0.0446  0.0310  -0.0015 685 ASN A O   
19   C CB  . ASN A 4   ? 0.3398 0.3616 0.3054 0.0567  0.0537  -0.0117 685 ASN A CB  
20   C CG  . ASN A 4   ? 0.4968 0.5113 0.4426 0.0610  0.0658  -0.0179 685 ASN A CG  
21   O OD1 . ASN A 4   ? 0.4114 0.4232 0.3364 0.0558  0.0653  -0.0209 685 ASN A OD1 
22   N ND2 . ASN A 4   ? 0.4350 0.4456 0.3865 0.0707  0.0767  -0.0198 685 ASN A ND2 
23   N N   . VAL A 5   ? 0.1614 0.2203 0.1798 0.0507  0.0381  0.0122  686 VAL A N   
24   C CA  . VAL A 5   ? 0.1432 0.2041 0.1765 0.0474  0.0280  0.0161  686 VAL A CA  
25   C C   . VAL A 5   ? 0.1338 0.1947 0.1609 0.0390  0.0187  0.0163  686 VAL A C   
26   O O   . VAL A 5   ? 0.1467 0.2000 0.1730 0.0355  0.0114  0.0133  686 VAL A O   
27   C CB  . VAL A 5   ? 0.1607 0.2363 0.2181 0.0502  0.0287  0.0256  686 VAL A CB  
28   C CG1 . VAL A 5   ? 0.1418 0.2199 0.2104 0.0445  0.0174  0.0300  686 VAL A CG1 
29   C CG2 . VAL A 5   ? 0.2368 0.3106 0.3044 0.0586  0.0346  0.0252  686 VAL A CG2 
30   N N   . PRO A 6   ? 0.1336 0.2025 0.1567 0.0357  0.0188  0.0199  687 PRO A N   
31   C CA  . PRO A 6   ? 0.1261 0.1942 0.1444 0.0287  0.0098  0.0200  687 PRO A CA  
32   C C   . PRO A 6   ? 0.1334 0.1894 0.1357 0.0258  0.0064  0.0113  687 PRO A C   
33   O O   . PRO A 6   ? 0.1380 0.1904 0.1436 0.0219  -0.0008 0.0097  687 PRO A O   
34   C CB  . PRO A 6   ? 0.1303 0.2074 0.1444 0.0270  0.0121  0.0255  687 PRO A CB  
35   C CG  . PRO A 6   ? 0.1302 0.2171 0.1574 0.0315  0.0197  0.0318  687 PRO A CG  
36   C CD  . PRO A 6   ? 0.1986 0.2788 0.2245 0.0379  0.0264  0.0259  687 PRO A CD  
37   N N   . LYS A 7   ? 0.1511 0.2004 0.1359 0.0270  0.0116  0.0055  688 LYS A N   
38   C CA  . LYS A 7   ? 0.1601 0.1974 0.1298 0.0233  0.0078  -0.0030 688 LYS A CA  
39   C C   . LYS A 7   ? 0.1572 0.1854 0.1331 0.0235  0.0052  -0.0067 688 LYS A C   
40   O O   . LYS A 7   ? 0.1706 0.1949 0.1455 0.0181  -0.0018 -0.0093 688 LYS A O   
41   C CB  . LYS A 7   ? 0.1836 0.2123 0.1328 0.0253  0.0149  -0.0095 688 LYS A CB  
42   C CG  . LYS A 7   ? 0.1952 0.2096 0.1292 0.0209  0.0108  -0.0187 688 LYS A CG  
43   C CD  . LYS A 7   ? 0.2760 0.2798 0.1863 0.0216  0.0168  -0.0259 688 LYS A CD  
44   C CE  . LYS A 7   ? 0.3295 0.3195 0.2252 0.0152  0.0106  -0.0346 688 LYS A CE  
45   N NZ  . LYS A 7   ? 0.5218 0.4991 0.3912 0.0145  0.0152  -0.0427 688 LYS A NZ  
46   N N   . ASN A 8   ? 0.1570 0.1818 0.1397 0.0297  0.0107  -0.0066 689 ASN A N   
47   C CA  . ASN A 8   ? 0.1563 0.1701 0.1417 0.0301  0.0084  -0.0100 689 ASN A CA  
48   C C   . ASN A 8   ? 0.1388 0.1574 0.1389 0.0272  0.0013  -0.0049 689 ASN A C   
49   O O   . ASN A 8   ? 0.1378 0.1470 0.1380 0.0256  -0.0018 -0.0074 689 ASN A O   
50   C CB  . ASN A 8   ? 0.2077 0.2156 0.1959 0.0384  0.0163  -0.0110 689 ASN A CB  
51   C CG  . ASN A 8   ? 0.2890 0.2850 0.2582 0.0409  0.0234  -0.0191 689 ASN A CG  
52   O OD1 . ASN A 8   ? 0.3710 0.3562 0.3245 0.0354  0.0202  -0.0260 689 ASN A OD1 
53   N ND2 . ASN A 8   ? 0.3506 0.3489 0.3213 0.0487  0.0333  -0.0184 689 ASN A ND2 
54   N N   . ALA A 9   ? 0.1253 0.1569 0.1364 0.0260  -0.0011 0.0020  690 ALA A N   
55   C CA  . ALA A 9   ? 0.1157 0.1502 0.1374 0.0223  -0.0080 0.0058  690 ALA A CA  
56   C C   . ALA A 9   ? 0.1062 0.1413 0.1233 0.0159  -0.0135 0.0039  690 ALA A C   
57   O O   . ALA A 9   ? 0.1085 0.1439 0.1322 0.0128  -0.0183 0.0055  690 ALA A O   
58   C CB  . ALA A 9   ? 0.1013 0.1479 0.1379 0.0239  -0.0083 0.0140  690 ALA A CB  
59   N N   . SER A 10  ? 0.1140 0.1492 0.1198 0.0139  -0.0129 0.0005  691 SER A N   
60   C CA  . SER A 10  ? 0.1099 0.1483 0.1141 0.0084  -0.0186 0.0000  691 SER A CA  
61   C C   . SER A 10  ? 0.1303 0.1596 0.1292 0.0043  -0.0212 -0.0064 691 SER A C   
62   O O   . SER A 10  ? 0.1260 0.1477 0.1129 0.0033  -0.0198 -0.0121 691 SER A O   
63   C CB  . SER A 10  ? 0.1183 0.1618 0.1130 0.0076  -0.0182 0.0004  691 SER A CB  
64   O OG  . SER A 10  ? 0.1314 0.1839 0.1315 0.0105  -0.0156 0.0073  691 SER A OG  
65   N N   . ALA A 11  ? 0.1710 0.2007 0.1783 0.0014  -0.0248 -0.0055 692 ALA A N   
66   C CA  . ALA A 11  ? 0.1058 0.1280 0.1102 -0.0030 -0.0265 -0.0104 692 ALA A CA  
67   C C   . ALA A 11  ? 0.1337 0.1626 0.1404 -0.0079 -0.0308 -0.0112 692 ALA A C   
68   O O   . ALA A 11  ? 0.0946 0.1327 0.1096 -0.0076 -0.0331 -0.0068 692 ALA A O   
69   C CB  . ALA A 11  ? 0.1344 0.1518 0.1452 -0.0031 -0.0266 -0.0091 692 ALA A CB  
70   N N   . LEU A 12  ? 0.1223 0.1464 0.1226 -0.0126 -0.0321 -0.0165 693 LEU A N   
71   C CA  . LEU A 12  ? 0.1572 0.1879 0.1635 -0.0178 -0.0362 -0.0171 693 LEU A CA  
72   C C   . LEU A 12  ? 0.1637 0.1927 0.1789 -0.0195 -0.0350 -0.0168 693 LEU A C   
73   O O   . LEU A 12  ? 0.1527 0.1714 0.1640 -0.0193 -0.0322 -0.0185 693 LEU A O   
74   C CB  . LEU A 12  ? 0.1822 0.2083 0.1788 -0.0233 -0.0384 -0.0227 693 LEU A CB  
75   C CG  . LEU A 12  ? 0.1714 0.2041 0.1749 -0.0301 -0.0429 -0.0242 693 LEU A CG  
76   C CD1 . LEU A 12  ? 0.1154 0.1627 0.1268 -0.0298 -0.0480 -0.0198 693 LEU A CD1 
77   C CD2 . LEU A 12  ? 0.1748 0.1990 0.1664 -0.0361 -0.0448 -0.0303 693 LEU A CD2 
78   N N   . LEU A 13  ? 0.1029 0.1413 0.1294 -0.0207 -0.0370 -0.0145 694 LEU A N   
79   C CA  . LEU A 13  ? 0.0872 0.1244 0.1212 -0.0227 -0.0349 -0.0149 694 LEU A CA  
80   C C   . LEU A 13  ? 0.0983 0.1410 0.1381 -0.0284 -0.0363 -0.0175 694 LEU A C   
81   O O   . LEU A 13  ? 0.1283 0.1812 0.1733 -0.0295 -0.0405 -0.0165 694 LEU A O   
82   C CB  . LEU A 13  ? 0.0779 0.1205 0.1216 -0.0191 -0.0346 -0.0107 694 LEU A CB  
83   C CG  . LEU A 13  ? 0.0749 0.1131 0.1163 -0.0146 -0.0336 -0.0074 694 LEU A CG  
84   C CD1 . LEU A 13  ? 0.1042 0.1450 0.1546 -0.0132 -0.0333 -0.0048 694 LEU A CD1 
85   C CD2 . LEU A 13  ? 0.0798 0.1062 0.1129 -0.0150 -0.0312 -0.0093 694 LEU A CD2 
86   N N   . ARG A 14  ? 0.0967 0.1331 0.1361 -0.0324 -0.0330 -0.0201 695 ARG A N   
87   C CA  . ARG A 14  ? 0.0941 0.1369 0.1422 -0.0383 -0.0329 -0.0219 695 ARG A CA  
88   C C   . ARG A 14  ? 0.1307 0.1740 0.1867 -0.0380 -0.0276 -0.0210 695 ARG A C   
89   O O   . ARG A 14  ? 0.1561 0.1879 0.2039 -0.0374 -0.0238 -0.0214 695 ARG A O   
90   C CB  . ARG A 14  ? 0.1127 0.1465 0.1520 -0.0448 -0.0328 -0.0260 695 ARG A CB  
91   C CG  . ARG A 14  ? 0.1327 0.1633 0.1614 -0.0456 -0.0374 -0.0283 695 ARG A CG  
92   C CD  . ARG A 14  ? 0.1443 0.1654 0.1655 -0.0533 -0.0378 -0.0329 695 ARG A CD  
93   N NE  . ARG A 14  ? 0.2384 0.2542 0.2471 -0.0547 -0.0419 -0.0362 695 ARG A NE  
94   C CZ  . ARG A 14  ? 0.3473 0.3480 0.3410 -0.0518 -0.0399 -0.0389 695 ARG A CZ  
95   N NH1 . ARG A 14  ? 0.3278 0.3183 0.3182 -0.0472 -0.0349 -0.0377 695 ARG A NH1 
96   N NH2 . ARG A 14  ? 0.2749 0.2700 0.2561 -0.0535 -0.0430 -0.0428 695 ARG A NH2 
97   N N   . MET A 15  ? 0.1160 0.1721 0.1872 -0.0381 -0.0274 -0.0197 696 MET A N   
98   C CA  . MET A 15  ? 0.0823 0.1389 0.1608 -0.0370 -0.0211 -0.0195 696 MET A CA  
99   C C   . MET A 15  ? 0.1048 0.1695 0.1947 -0.0428 -0.0179 -0.0211 696 MET A C   
100  O O   . MET A 15  ? 0.0975 0.1752 0.1992 -0.0449 -0.0222 -0.0203 696 MET A O   
101  C CB  . MET A 15  ? 0.0749 0.1390 0.1636 -0.0306 -0.0219 -0.0164 696 MET A CB  
102  C CG  . MET A 15  ? 0.1071 0.1644 0.1868 -0.0255 -0.0248 -0.0141 696 MET A CG  
103  S SD  . MET A 15  ? 0.1450 0.2100 0.2239 -0.0236 -0.0327 -0.0111 696 MET A SD  
104  C CE  . MET A 15  ? 0.1138 0.1941 0.2119 -0.0204 -0.0355 -0.0072 696 MET A CE  
105  N N   . ASN A 16  ? 0.0911 0.1482 0.1771 -0.0459 -0.0107 -0.0229 697 ASN A N   
106  C CA  . ASN A 16  ? 0.0947 0.1592 0.1918 -0.0517 -0.0056 -0.0240 697 ASN A CA  
107  C C   . ASN A 16  ? 0.1337 0.2001 0.2379 -0.0482 0.0029  -0.0239 697 ASN A C   
108  O O   . ASN A 16  ? 0.1159 0.1689 0.2071 -0.0485 0.0088  -0.0252 697 ASN A O   
109  C CB  . ASN A 16  ? 0.1478 0.2002 0.2322 -0.0592 -0.0033 -0.0260 697 ASN A CB  
110  C CG  . ASN A 16  ? 0.1350 0.1815 0.2094 -0.0615 -0.0108 -0.0269 697 ASN A CG  
111  O OD1 . ASN A 16  ? 0.1816 0.2383 0.2641 -0.0643 -0.0165 -0.0271 697 ASN A OD1 
112  N ND2 . ASN A 16  ? 0.2246 0.2543 0.2811 -0.0599 -0.0112 -0.0274 697 ASN A ND2 
113  N N   . PHE A 17  ? 0.0992 0.1815 0.2236 -0.0448 0.0033  -0.0225 698 PHE A N   
114  C CA  . PHE A 17  ? 0.1168 0.2011 0.2496 -0.0403 0.0119  -0.0230 698 PHE A CA  
115  C C   . PHE A 17  ? 0.1241 0.2156 0.2676 -0.0457 0.0211  -0.0243 698 PHE A C   
116  O O   . PHE A 17  ? 0.0931 0.2015 0.2557 -0.0488 0.0192  -0.0229 698 PHE A O   
117  C CB  . PHE A 17  ? 0.0902 0.1872 0.2407 -0.0328 0.0082  -0.0203 698 PHE A CB  
118  C CG  . PHE A 17  ? 0.1013 0.1943 0.2436 -0.0287 -0.0013 -0.0179 698 PHE A CG  
119  C CD1 . PHE A 17  ? 0.0773 0.1548 0.2029 -0.0256 -0.0010 -0.0185 698 PHE A CD1 
120  C CD2 . PHE A 17  ? 0.1627 0.2677 0.3140 -0.0285 -0.0106 -0.0147 698 PHE A CD2 
121  C CE1 . PHE A 17  ? 0.0749 0.1500 0.1947 -0.0222 -0.0087 -0.0158 698 PHE A CE1 
122  C CE2 . PHE A 17  ? 0.0913 0.1927 0.2342 -0.0249 -0.0181 -0.0122 698 PHE A CE2 
123  C CZ  . PHE A 17  ? 0.1181 0.2050 0.2462 -0.0217 -0.0166 -0.0127 698 PHE A CZ  
124  N N   . VAL A 18  ? 0.1333 0.2123 0.2643 -0.0472 0.0308  -0.0267 699 VAL A N   
125  C CA  . VAL A 18  ? 0.1225 0.2057 0.2597 -0.0531 0.0413  -0.0278 699 VAL A CA  
126  C C   . VAL A 18  ? 0.1722 0.2618 0.3224 -0.0473 0.0522  -0.0291 699 VAL A C   
127  O O   . VAL A 18  ? 0.2338 0.3119 0.3734 -0.0412 0.0549  -0.0308 699 VAL A O   
128  C CB  . VAL A 18  ? 0.2023 0.2659 0.3144 -0.0594 0.0454  -0.0292 699 VAL A CB  
129  C CG1 . VAL A 18  ? 0.1880 0.2564 0.3062 -0.0670 0.0562  -0.0296 699 VAL A CG1 
130  C CG2 . VAL A 18  ? 0.2546 0.3090 0.3528 -0.0628 0.0347  -0.0283 699 VAL A CG2 
131  N N   . LYS A 19  ? 0.1179 0.2257 0.2918 -0.0493 0.0584  -0.0283 700 LYS A N   
132  C CA  . LYS A 19  ? 0.2279 0.3432 0.4168 -0.0440 0.0713  -0.0297 700 LYS A CA  
133  C C   . LYS A 19  ? 0.2367 0.3594 0.4327 -0.0513 0.0816  -0.0295 700 LYS A C   
134  O O   . LYS A 19  ? 0.2200 0.3574 0.4304 -0.0544 0.0755  -0.0254 700 LYS A O   
135  C CB  . LYS A 19  ? 0.2059 0.3396 0.4220 -0.0355 0.0665  -0.0269 700 LYS A CB  
136  C CG  . LYS A 19  ? 0.3864 0.5113 0.5970 -0.0263 0.0618  -0.0274 700 LYS A CG  
137  C CD  . LYS A 19  ? 0.4508 0.5674 0.6600 -0.0193 0.0751  -0.0311 700 LYS A CD  
138  C CE  . LYS A 19  ? 0.4541 0.5608 0.6582 -0.0105 0.0693  -0.0311 700 LYS A CE  
139  N NZ  . LYS A 19  ? 0.4419 0.5653 0.6685 -0.0056 0.0580  -0.0258 700 LYS A NZ  
140  N N   . GLY A 20  ? 0.2378 0.3479 0.4191 -0.0536 0.0956  -0.0328 701 GLY A N   
141  C CA  . GLY A 20  ? 0.2419 0.3548 0.4229 -0.0604 0.1037  -0.0314 701 GLY A CA  
142  C C   . GLY A 20  ? 0.2295 0.3383 0.4008 -0.0709 0.0950  -0.0291 701 GLY A C   
143  O O   . GLY A 20  ? 0.2083 0.2995 0.3571 -0.0752 0.0916  -0.0307 701 GLY A O   
144  N N   . ASN A 21  ? 0.1638 0.2882 0.3518 -0.0750 0.0906  -0.0249 702 ASN A N   
145  C CA  . ASN A 21  ? 0.2335 0.3538 0.4140 -0.0846 0.0814  -0.0227 702 ASN A CA  
146  C C   . ASN A 21  ? 0.1473 0.2804 0.3417 -0.0837 0.0656  -0.0200 702 ASN A C   
147  O O   . ASN A 21  ? 0.1503 0.2855 0.3455 -0.0913 0.0582  -0.0174 702 ASN A O   
148  C CB  . ASN A 21  ? 0.1747 0.2993 0.3589 -0.0925 0.0887  -0.0199 702 ASN A CB  
149  C CG  . ASN A 21  ? 0.1754 0.3239 0.3878 -0.0890 0.0932  -0.0168 702 ASN A CG  
150  O OD1 . ASN A 21  ? 0.2417 0.4054 0.4724 -0.0826 0.0860  -0.0153 702 ASN A OD1 
151  N ND2 . ASN A 21  ? 0.2886 0.4404 0.5039 -0.0931 0.1049  -0.0153 702 ASN A ND2 
152  N N   . GLN A 22  ? 0.1355 0.2757 0.3391 -0.0747 0.0604  -0.0202 703 GLN A N   
153  C CA  . GLN A 22  ? 0.1486 0.2991 0.3613 -0.0733 0.0453  -0.0173 703 GLN A CA  
154  C C   . GLN A 22  ? 0.1786 0.3169 0.3769 -0.0688 0.0380  -0.0199 703 GLN A C   
155  O O   . GLN A 22  ? 0.1137 0.2437 0.3061 -0.0631 0.0443  -0.0229 703 GLN A O   
156  C CB  . GLN A 22  ? 0.1646 0.3368 0.4023 -0.0665 0.0443  -0.0136 703 GLN A CB  
157  C CG  . GLN A 22  ? 0.1450 0.3333 0.3999 -0.0714 0.0497  -0.0103 703 GLN A CG  
158  C CD  . GLN A 22  ? 0.1843 0.3922 0.4629 -0.0630 0.0524  -0.0079 703 GLN A CD  
159  O OE1 . GLN A 22  ? 0.3950 0.6002 0.6756 -0.0528 0.0549  -0.0094 703 GLN A OE1 
160  N NE2 . GLN A 22  ? 0.2994 0.5266 0.5963 -0.0674 0.0517  -0.0040 703 GLN A NE2 
161  N N   . VAL A 23  ? 0.1125 0.2494 0.3048 -0.0717 0.0251  -0.0187 704 VAL A N   
162  C CA  A VAL A 23  ? 0.1235 0.2493 0.3014 -0.0682 0.0174  -0.0206 704 VAL A CA  
163  C CA  B VAL A 23  ? 0.1235 0.2497 0.3020 -0.0677 0.0177  -0.0206 704 VAL A CA  
164  C C   . VAL A 23  ? 0.1293 0.2667 0.3151 -0.0648 0.0048  -0.0169 704 VAL A C   
165  O O   . VAL A 23  ? 0.1185 0.2660 0.3115 -0.0699 -0.0012 -0.0139 704 VAL A O   
166  C CB  A VAL A 23  ? 0.1618 0.2688 0.3167 -0.0753 0.0150  -0.0234 704 VAL A CB  
167  C CB  B VAL A 23  ? 0.1638 0.2701 0.3184 -0.0743 0.0163  -0.0237 704 VAL A CB  
168  C CG1 A VAL A 23  ? 0.1404 0.2385 0.2817 -0.0714 0.0058  -0.0246 704 VAL A CG1 
169  C CG1 B VAL A 23  ? 0.1198 0.2255 0.2723 -0.0830 0.0117  -0.0223 704 VAL A CG1 
170  C CG2 A VAL A 23  ? 0.1968 0.2893 0.3382 -0.0780 0.0266  -0.0259 704 VAL A CG2 
171  C CG2 B VAL A 23  ? 0.1452 0.2414 0.2850 -0.0693 0.0078  -0.0246 704 VAL A CG2 
172  N N   . LEU A 24  ? 0.1227 0.2583 0.3061 -0.0569 0.0007  -0.0168 705 LEU A N   
173  C CA  A LEU A 24  ? 0.1037 0.2453 0.2863 -0.0542 -0.0112 -0.0135 705 LEU A CA  
174  C CA  B LEU A 24  ? 0.1037 0.2453 0.2863 -0.0542 -0.0112 -0.0135 705 LEU A CA  
175  C C   . LEU A 24  ? 0.1371 0.2638 0.3010 -0.0523 -0.0158 -0.0158 705 LEU A C   
176  O O   . LEU A 24  ? 0.1283 0.2446 0.2859 -0.0493 -0.0101 -0.0187 705 LEU A O   
177  C CB  A LEU A 24  ? 0.1405 0.2953 0.3387 -0.0456 -0.0119 -0.0099 705 LEU A CB  
178  C CB  B LEU A 24  ? 0.1406 0.2952 0.3389 -0.0454 -0.0117 -0.0099 705 LEU A CB  
179  C CG  A LEU A 24  ? 0.0893 0.2614 0.3079 -0.0462 -0.0084 -0.0074 705 LEU A CG  
180  C CG  B LEU A 24  ? 0.1613 0.3214 0.3567 -0.0419 -0.0228 -0.0068 705 LEU A CG  
181  C CD1 A LEU A 24  ? 0.1202 0.3021 0.3524 -0.0364 -0.0096 -0.0042 705 LEU A CD1 
182  C CD1 B LEU A 24  ? 0.1026 0.2699 0.2955 -0.0499 -0.0304 -0.0073 705 LEU A CD1 
183  C CD2 A LEU A 24  ? 0.0957 0.2771 0.3149 -0.0551 -0.0158 -0.0065 705 LEU A CD2 
184  C CD2 B LEU A 24  ? 0.1201 0.2909 0.3314 -0.0331 -0.0222 -0.0033 705 LEU A CD2 
185  N N   . SER A 25  ? 0.2340 0.3597 0.3882 -0.0545 -0.0255 -0.0148 706 SER A N   
186  C CA  . SER A 25  ? 0.1740 0.2860 0.3100 -0.0530 -0.0294 -0.0170 706 SER A CA  
187  C C   . SER A 25  ? 0.1390 0.2561 0.2730 -0.0468 -0.0365 -0.0136 706 SER A C   
188  O O   . SER A 25  ? 0.1523 0.2821 0.2944 -0.0458 -0.0406 -0.0114 706 SER A O   
189  C CB  . SER A 25  ? 0.1767 0.2777 0.2978 -0.0607 -0.0329 -0.0201 706 SER A CB  
190  O OG  . SER A 25  ? 0.2177 0.3248 0.3441 -0.0645 -0.0406 -0.0183 706 SER A OG  
191  N N   . GLY A 26  ? 0.0785 0.1853 0.2015 -0.0423 -0.0373 -0.0141 707 GLY A N   
192  C CA  . GLY A 26  ? 0.1018 0.2104 0.2194 -0.0370 -0.0429 -0.0109 707 GLY A CA  
193  C C   . GLY A 26  ? 0.1286 0.2241 0.2289 -0.0368 -0.0450 -0.0126 707 GLY A C   
194  O O   . GLY A 26  ? 0.1073 0.1904 0.1965 -0.0391 -0.0403 -0.0162 707 GLY A O   
195  N N   . THR A 27  ? 0.1102 0.2063 0.2033 -0.0329 -0.0495 -0.0099 708 THR A N   
196  C CA  . THR A 27  ? 0.0819 0.1665 0.1581 -0.0315 -0.0496 -0.0108 708 THR A CA  
197  C C   . THR A 27  ? 0.1482 0.2336 0.2248 -0.0248 -0.0500 -0.0059 708 THR A C   
198  O O   . THR A 27  ? 0.1034 0.1969 0.1893 -0.0212 -0.0514 -0.0020 708 THR A O   
199  C CB  . THR A 27  ? 0.1278 0.2097 0.1902 -0.0357 -0.0547 -0.0132 708 THR A CB  
200  O OG1 . THR A 27  ? 0.1430 0.2334 0.2066 -0.0337 -0.0604 -0.0097 708 THR A OG1 
201  C CG2 . THR A 27  ? 0.1544 0.2352 0.2170 -0.0437 -0.0555 -0.0178 708 THR A CG2 
202  N N   . GLY A 28  ? 0.1206 0.1956 0.1852 -0.0222 -0.0469 -0.0064 709 GLY A N   
203  C CA  . GLY A 28  ? 0.0736 0.1485 0.1370 -0.0170 -0.0472 -0.0017 709 GLY A CA  
204  C C   . GLY A 28  ? 0.0918 0.1583 0.1408 -0.0156 -0.0453 -0.0026 709 GLY A C   
205  O O   . GLY A 28  ? 0.0859 0.1470 0.1243 -0.0183 -0.0449 -0.0068 709 GLY A O   
206  N N   . SER A 29  ? 0.0740 0.1391 0.1233 -0.0114 -0.0437 0.0014  710 SER A N   
207  C CA  . SER A 29  ? 0.0777 0.1374 0.1169 -0.0092 -0.0413 0.0019  710 SER A CA  
208  C C   . SER A 29  ? 0.0717 0.1268 0.1151 -0.0065 -0.0385 0.0041  710 SER A C   
209  O O   . SER A 29  ? 0.0660 0.1222 0.1182 -0.0061 -0.0391 0.0061  710 SER A O   
210  C CB  . SER A 29  ? 0.1098 0.1754 0.1446 -0.0075 -0.0432 0.0061  710 SER A CB  
211  O OG  . SER A 29  ? 0.1003 0.1706 0.1311 -0.0106 -0.0476 0.0048  710 SER A OG  
212  N N   . ALA A 30  ? 0.0991 0.1488 0.1363 -0.0046 -0.0357 0.0037  711 ALA A N   
213  C CA  . ALA A 30  ? 0.0704 0.1167 0.1115 -0.0026 -0.0343 0.0065  711 ALA A CA  
214  C C   . ALA A 30  ? 0.0745 0.1201 0.1114 0.0007  -0.0316 0.0080  711 ALA A C   
215  O O   . ALA A 30  ? 0.1108 0.1554 0.1394 0.0014  -0.0296 0.0053  711 ALA A O   
216  C CB  . ALA A 30  ? 0.0818 0.1197 0.1226 -0.0046 -0.0337 0.0033  711 ALA A CB  
217  N N   . THR A 31  ? 0.0709 0.1167 0.1138 0.0026  -0.0313 0.0122  712 THR A N   
218  C CA  . THR A 31  ? 0.0740 0.1213 0.1171 0.0064  -0.0282 0.0147  712 THR A CA  
219  C C   . THR A 31  ? 0.0876 0.1292 0.1343 0.0072  -0.0288 0.0153  712 THR A C   
220  O O   . THR A 31  ? 0.0770 0.1171 0.1288 0.0050  -0.0322 0.0173  712 THR A O   
221  C CB  . THR A 31  ? 0.0713 0.1280 0.1214 0.0078  -0.0277 0.0214  712 THR A CB  
222  O OG1 . THR A 31  ? 0.0869 0.1485 0.1330 0.0068  -0.0280 0.0221  712 THR A OG1 
223  C CG2 . THR A 31  ? 0.0756 0.1355 0.1274 0.0120  -0.0229 0.0239  712 THR A CG2 
224  N N   . PHE A 32  ? 0.0796 0.1173 0.1232 0.0105  -0.0257 0.0138  713 PHE A N   
225  C CA  . PHE A 32  ? 0.0813 0.1152 0.1299 0.0123  -0.0269 0.0161  713 PHE A CA  
226  C C   . PHE A 32  ? 0.0762 0.1200 0.1372 0.0146  -0.0272 0.0233  713 PHE A C   
227  O O   . PHE A 32  ? 0.0781 0.1295 0.1420 0.0181  -0.0225 0.0254  713 PHE A O   
228  C CB  . PHE A 32  ? 0.0899 0.1160 0.1326 0.0161  -0.0232 0.0127  713 PHE A CB  
229  C CG  . PHE A 32  ? 0.1467 0.1603 0.1797 0.0128  -0.0246 0.0073  713 PHE A CG  
230  C CD1 . PHE A 32  ? 0.1319 0.1382 0.1653 0.0111  -0.0282 0.0086  713 PHE A CD1 
231  C CD2 . PHE A 32  ? 0.1473 0.1564 0.1702 0.0108  -0.0224 0.0012  713 PHE A CD2 
232  C CE1 . PHE A 32  ? 0.1997 0.1944 0.2237 0.0076  -0.0286 0.0044  713 PHE A CE1 
233  C CE2 . PHE A 32  ? 0.1724 0.1706 0.1877 0.0070  -0.0234 -0.0031 713 PHE A CE2 
234  C CZ  . PHE A 32  ? 0.1068 0.0978 0.1227 0.0054  -0.0259 -0.0014 713 PHE A CZ  
235  N N   . ILE A 33  ? 0.0721 0.1159 0.1398 0.0119  -0.0325 0.0270  714 ILE A N   
236  C CA  . ILE A 33  ? 0.0759 0.1288 0.1569 0.0125  -0.0343 0.0342  714 ILE A CA  
237  C C   . ILE A 33  ? 0.1011 0.1511 0.1878 0.0133  -0.0386 0.0372  714 ILE A C   
238  O O   . ILE A 33  ? 0.1167 0.1709 0.2099 0.0120  -0.0390 0.0410  714 ILE A O   
239  C CB  . ILE A 33  ? 0.0799 0.1344 0.1626 0.0075  -0.0372 0.0362  714 ILE A CB  
240  C CG1 . ILE A 33  ? 0.0660 0.1096 0.1415 0.0029  -0.0417 0.0326  714 ILE A CG1 
241  C CG2 . ILE A 33  ? 0.1038 0.1646 0.1854 0.0079  -0.0345 0.0364  714 ILE A CG2 
242  C CD1 . ILE A 33  ? 0.0656 0.1071 0.1403 -0.0013 -0.0426 0.0330  714 ILE A CD1 
243  N N   . ALA A 34  ? 0.0920 0.1312 0.1701 0.0138  -0.0393 0.0333  715 ALA A N   
244  C CA  . ALA A 34  ? 0.0827 0.1176 0.1643 0.0157  -0.0431 0.0361  715 ALA A CA  
245  C C   . ALA A 34  ? 0.1243 0.1477 0.1946 0.0182  -0.0397 0.0307  715 ALA A C   
246  O O   . ALA A 34  ? 0.0906 0.1097 0.1507 0.0168  -0.0358 0.0247  715 ALA A O   
247  C CB  . ALA A 34  ? 0.1314 0.1598 0.2091 0.0094  -0.0503 0.0373  715 ALA A CB  
248  N N   . PRO A 35  ? 0.1024 0.1203 0.1746 0.0216  -0.0416 0.0330  716 PRO A N   
249  C CA  . PRO A 35  ? 0.1072 0.1117 0.1679 0.0234  -0.0385 0.0279  716 PRO A CA  
250  C C   . PRO A 35  ? 0.1494 0.1429 0.1951 0.0165  -0.0400 0.0227  716 PRO A C   
251  O O   . PRO A 35  ? 0.1144 0.0993 0.1503 0.0162  -0.0360 0.0171  716 PRO A O   
252  C CB  . PRO A 35  ? 0.1328 0.1330 0.1995 0.0276  -0.0424 0.0331  716 PRO A CB  
253  C CG  . PRO A 35  ? 0.1430 0.1591 0.2285 0.0312  -0.0436 0.0401  716 PRO A CG  
254  C CD  . PRO A 35  ? 0.1052 0.1299 0.1922 0.0250  -0.0459 0.0407  716 PRO A CD  
255  N N   . ASN A 36  ? 0.1290 0.1226 0.1730 0.0107  -0.0450 0.0240  717 ASN A N   
256  C CA  . ASN A 36  ? 0.1790 0.1624 0.2098 0.0046  -0.0453 0.0194  717 ASN A CA  
257  C C   . ASN A 36  ? 0.1518 0.1403 0.1830 0.0000  -0.0463 0.0183  717 ASN A C   
258  O O   . ASN A 36  ? 0.1590 0.1401 0.1819 -0.0050 -0.0482 0.0168  717 ASN A O   
259  C CB  . ASN A 36  ? 0.1567 0.1279 0.1798 0.0024  -0.0503 0.0219  717 ASN A CB  
260  C CG  . ASN A 36  ? 0.2777 0.2518 0.3053 0.0003  -0.0578 0.0276  717 ASN A CG  
261  O OD1 . ASN A 36  ? 0.2332 0.2192 0.2733 0.0020  -0.0594 0.0310  717 ASN A OD1 
262  N ND2 . ASN A 36  ? 0.4058 0.3684 0.4224 -0.0040 -0.0627 0.0289  717 ASN A ND2 
263  N N   . VAL A 37  ? 0.1045 0.1048 0.1447 0.0018  -0.0445 0.0193  718 VAL A N   
264  C CA  . VAL A 37  ? 0.0857 0.0904 0.1279 -0.0017 -0.0457 0.0190  718 VAL A CA  
265  C C   . VAL A 37  ? 0.0791 0.0924 0.1245 0.0000  -0.0412 0.0171  718 VAL A C   
266  O O   . VAL A 37  ? 0.0773 0.0980 0.1282 0.0041  -0.0387 0.0190  718 VAL A O   
267  C CB  . VAL A 37  ? 0.1737 0.1834 0.2247 -0.0025 -0.0510 0.0250  718 VAL A CB  
268  C CG1 . VAL A 37  ? 0.0794 0.0920 0.1325 -0.0057 -0.0516 0.0245  718 VAL A CG1 
269  C CG2 . VAL A 37  ? 0.1341 0.1346 0.1800 -0.0053 -0.0571 0.0271  718 VAL A CG2 
270  N N   . LEU A 38  ? 0.1060 0.1183 0.1479 -0.0030 -0.0400 0.0134  719 LEU A N   
271  C CA  . LEU A 38  ? 0.0877 0.1079 0.1321 -0.0021 -0.0373 0.0121  719 LEU A CA  
272  C C   . LEU A 38  ? 0.0674 0.0924 0.1182 -0.0034 -0.0393 0.0147  719 LEU A C   
273  O O   . LEU A 38  ? 0.1135 0.1327 0.1632 -0.0061 -0.0413 0.0141  719 LEU A O   
274  C CB  . LEU A 38  ? 0.0906 0.1073 0.1286 -0.0044 -0.0350 0.0064  719 LEU A CB  
275  C CG  . LEU A 38  ? 0.1335 0.1439 0.1640 -0.0041 -0.0328 0.0029  719 LEU A CG  
276  C CD1 . LEU A 38  ? 0.2030 0.2101 0.2290 -0.0082 -0.0312 -0.0021 719 LEU A CD1 
277  C CD2 . LEU A 38  ? 0.1254 0.1412 0.1563 -0.0004 -0.0308 0.0033  719 LEU A CD2 
278  N N   . LEU A 39  ? 0.0636 0.0977 0.1196 -0.0015 -0.0385 0.0175  720 LEU A N   
279  C CA  . LEU A 39  ? 0.0681 0.1060 0.1298 -0.0024 -0.0400 0.0201  720 LEU A CA  
280  C C   . LEU A 39  ? 0.0733 0.1145 0.1337 -0.0024 -0.0387 0.0173  720 LEU A C   
281  O O   . LEU A 39  ? 0.0612 0.1064 0.1179 -0.0011 -0.0370 0.0161  720 LEU A O   
282  C CB  . LEU A 39  ? 0.0599 0.1051 0.1275 -0.0009 -0.0398 0.0261  720 LEU A CB  
283  C CG  . LEU A 39  ? 0.0598 0.1056 0.1297 -0.0018 -0.0396 0.0286  720 LEU A CG  
284  C CD1 . LEU A 39  ? 0.1256 0.1633 0.1971 -0.0047 -0.0422 0.0288  720 LEU A CD1 
285  C CD2 . LEU A 39  ? 0.1394 0.1927 0.2125 -0.0006 -0.0377 0.0341  720 LEU A CD2 
286  N N   . THR A 40  ? 0.0756 0.1151 0.1392 -0.0036 -0.0396 0.0164  721 THR A N   
287  C CA  . THR A 40  ? 0.0580 0.1025 0.1236 -0.0033 -0.0392 0.0148  721 THR A CA  
288  C C   . THR A 40  ? 0.0915 0.1354 0.1645 -0.0029 -0.0404 0.0163  721 THR A C   
289  O O   . THR A 40  ? 0.0805 0.1192 0.1556 -0.0033 -0.0415 0.0184  721 THR A O   
290  C CB  . THR A 40  ? 0.0711 0.1128 0.1318 -0.0051 -0.0372 0.0088  721 THR A CB  
291  O OG1 . THR A 40  ? 0.0594 0.1084 0.1232 -0.0053 -0.0378 0.0080  721 THR A OG1 
292  C CG2 . THR A 40  ? 0.0620 0.0956 0.1222 -0.0070 -0.0355 0.0056  721 THR A CG2 
293  N N   . VAL A 41  ? 0.0647 0.1138 0.1423 -0.0022 -0.0405 0.0154  722 VAL A N   
294  C CA  . VAL A 41  ? 0.0583 0.1071 0.1447 -0.0006 -0.0410 0.0167  722 VAL A CA  
295  C C   . VAL A 41  ? 0.0905 0.1336 0.1775 -0.0015 -0.0373 0.0109  722 VAL A C   
296  O O   . VAL A 41  ? 0.0683 0.1120 0.1517 -0.0035 -0.0350 0.0066  722 VAL A O   
297  C CB  . VAL A 41  ? 0.0893 0.1456 0.1781 0.0014  -0.0416 0.0191  722 VAL A CB  
298  C CG1 . VAL A 41  ? 0.1157 0.1734 0.1988 0.0021  -0.0425 0.0242  722 VAL A CG1 
299  C CG2 . VAL A 41  ? 0.0593 0.1223 0.1474 -0.0001 -0.0416 0.0156  722 VAL A CG2 
300  N N   . ALA A 42  ? 0.0692 0.1058 0.1604 -0.0002 -0.0361 0.0107  723 ALA A N   
301  C CA  . ALA A 42  ? 0.0695 0.0996 0.1600 -0.0007 -0.0311 0.0049  723 ALA A CA  
302  C C   . ALA A 42  ? 0.0892 0.1291 0.1896 0.0007  -0.0287 0.0032  723 ALA A C   
303  O O   . ALA A 42  ? 0.0879 0.1258 0.1871 -0.0009 -0.0236 -0.0017 723 ALA A O   
304  C CB  . ALA A 42  ? 0.0773 0.0964 0.1687 0.0006  -0.0299 0.0044  723 ALA A CB  
305  N N   . HIS A 43  ? 0.0679 0.1188 0.1780 0.0031  -0.0326 0.0077  724 HIS A N   
306  C CA  . HIS A 43  ? 0.0627 0.1240 0.1854 0.0045  -0.0315 0.0070  724 HIS A CA  
307  C C   . HIS A 43  ? 0.0808 0.1498 0.2010 0.0005  -0.0319 0.0045  724 HIS A C   
308  O O   . HIS A 43  ? 0.0595 0.1387 0.1911 0.0005  -0.0315 0.0040  724 HIS A O   
309  C CB  . HIS A 43  ? 0.0627 0.1318 0.1964 0.0086  -0.0363 0.0132  724 HIS A CB  
310  C CG  . HIS A 43  ? 0.0796 0.1528 0.2016 0.0069  -0.0403 0.0167  724 HIS A CG  
311  N ND1 . HIS A 43  ? 0.1010 0.1703 0.2157 0.0078  -0.0427 0.0215  724 HIS A ND1 
312  C CD2 . HIS A 43  ? 0.2031 0.2842 0.3210 0.0045  -0.0421 0.0159  724 HIS A CD2 
313  C CE1 . HIS A 43  ? 0.1499 0.2245 0.2565 0.0064  -0.0453 0.0230  724 HIS A CE1 
314  N NE2 . HIS A 43  ? 0.2274 0.3088 0.3355 0.0044  -0.0455 0.0195  724 HIS A NE2 
315  N N   . ASN A 44  ? 0.0966 0.1607 0.2030 -0.0030 -0.0325 0.0030  725 ASN A N   
316  C CA  . ASN A 44  ? 0.0596 0.1259 0.1618 -0.0073 -0.0311 -0.0009 725 ASN A CA  
317  C C   . ASN A 44  ? 0.1199 0.1807 0.2222 -0.0093 -0.0241 -0.0057 725 ASN A C   
318  O O   . ASN A 44  ? 0.0799 0.1438 0.1824 -0.0133 -0.0222 -0.0085 725 ASN A O   
319  C CB  . ASN A 44  ? 0.1138 0.1742 0.2014 -0.0096 -0.0328 -0.0013 725 ASN A CB  
320  C CG  . ASN A 44  ? 0.0930 0.1599 0.1788 -0.0085 -0.0383 0.0025  725 ASN A CG  
321  O OD1 . ASN A 44  ? 0.0889 0.1658 0.1818 -0.0086 -0.0418 0.0042  725 ASN A OD1 
322  N ND2 . ASN A 44  ? 0.1010 0.1628 0.1775 -0.0076 -0.0390 0.0042  725 ASN A ND2 
323  N N   . PHE A 45  ? 0.0669 0.1189 0.1681 -0.0072 -0.0202 -0.0067 726 PHE A N   
324  C CA  . PHE A 45  ? 0.0737 0.1176 0.1700 -0.0094 -0.0128 -0.0115 726 PHE A CA  
325  C C   . PHE A 45  ? 0.0970 0.1406 0.2034 -0.0058 -0.0070 -0.0131 726 PHE A C   
326  O O   . PHE A 45  ? 0.0844 0.1266 0.1916 -0.0074 0.0005  -0.0170 726 PHE A O   
327  C CB  . PHE A 45  ? 0.1126 0.1415 0.1917 -0.0114 -0.0128 -0.0126 726 PHE A CB  
328  C CG  . PHE A 45  ? 0.0812 0.1094 0.1515 -0.0135 -0.0177 -0.0109 726 PHE A CG  
329  C CD1 . PHE A 45  ? 0.1044 0.1339 0.1708 -0.0173 -0.0167 -0.0128 726 PHE A CD1 
330  C CD2 . PHE A 45  ? 0.1323 0.1582 0.1991 -0.0116 -0.0227 -0.0073 726 PHE A CD2 
331  C CE1 . PHE A 45  ? 0.1607 0.1877 0.2188 -0.0184 -0.0204 -0.0118 726 PHE A CE1 
332  C CE2 . PHE A 45  ? 0.1852 0.2107 0.2451 -0.0126 -0.0259 -0.0059 726 PHE A CE2 
333  C CZ  . PHE A 45  ? 0.1109 0.1363 0.1661 -0.0156 -0.0246 -0.0084 726 PHE A CZ  
334  N N   . ILE A 46  ? 0.0777 0.1215 0.1913 -0.0009 -0.0097 -0.0101 727 ILE A N   
335  C CA  . ILE A 46  ? 0.0847 0.1253 0.2071 0.0036  -0.0039 -0.0119 727 ILE A CA  
336  C C   . ILE A 46  ? 0.1251 0.1778 0.2670 0.0092  -0.0075 -0.0071 727 ILE A C   
337  O O   . ILE A 46  ? 0.0734 0.1339 0.2181 0.0093  -0.0155 -0.0019 727 ILE A O   
338  C CB  . ILE A 46  ? 0.1042 0.1267 0.2137 0.0042  -0.0028 -0.0137 727 ILE A CB  
339  C CG1 . ILE A 46  ? 0.1309 0.1517 0.2392 0.0054  -0.0113 -0.0082 727 ILE A CG1 
340  C CG2 . ILE A 46  ? 0.2383 0.2487 0.3283 -0.0013 0.0000  -0.0178 727 ILE A CG2 
341  C CD1 . ILE A 46  ? 0.1003 0.1041 0.1992 0.0057  -0.0112 -0.0095 727 ILE A CD1 
342  N N   . ASN A 47  ? 0.0968 0.1505 0.2516 0.0139  -0.0012 -0.0088 728 ASN A N   
343  C CA  A ASN A 47  ? 0.1326 0.1957 0.3073 0.0205  -0.0040 -0.0040 728 ASN A CA  
344  C CA  B ASN A 47  ? 0.1322 0.1957 0.3074 0.0206  -0.0038 -0.0041 728 ASN A CA  
345  C C   . ASN A 47  ? 0.0974 0.1478 0.2751 0.0264  0.0029  -0.0068 728 ASN A C   
346  O O   . ASN A 47  ? 0.1250 0.1598 0.2879 0.0245  0.0094  -0.0128 728 ASN A O   
347  C CB  A ASN A 47  ? 0.1132 0.1964 0.3078 0.0212  -0.0037 -0.0024 728 ASN A CB  
348  C CB  B ASN A 47  ? 0.1141 0.1972 0.3092 0.0212  -0.0026 -0.0030 728 ASN A CB  
349  C CG  A ASN A 47  ? 0.1726 0.2572 0.3706 0.0195  0.0074  -0.0084 728 ASN A CG  
350  C CG  B ASN A 47  ? 0.0956 0.1923 0.2934 0.0184  -0.0131 0.0027  728 ASN A CG  
351  O OD1 A ASN A 47  ? 0.1383 0.2089 0.3274 0.0206  0.0163  -0.0138 728 ASN A OD1 
352  O OD1 B ASN A 47  ? 0.1434 0.2367 0.3331 0.0193  -0.0206 0.0077  728 ASN A OD1 
353  N ND2 A ASN A 47  ? 0.2277 0.3290 0.4375 0.0162  0.0069  -0.0077 728 ASN A ND2 
354  N ND2 B ASN A 47  ? 0.1217 0.2291 0.3214 0.0136  -0.0129 0.0016  728 ASN A ND2 
355  N N   . ASN A 48  ? 0.0990 0.1550 0.2951 0.0335  0.0011  -0.0024 729 ASN A N   
356  C CA  . ASN A 48  ? 0.1399 0.1827 0.3403 0.0400  0.0079  -0.0052 729 ASN A CA  
357  C C   . ASN A 48  ? 0.1446 0.1877 0.3508 0.0421  0.0210  -0.0122 729 ASN A C   
358  O O   . ASN A 48  ? 0.1436 0.2043 0.3646 0.0418  0.0237  -0.0118 729 ASN A O   
359  C CB  . ASN A 48  ? 0.1135 0.1627 0.3342 0.0479  0.0028  0.0020  729 ASN A CB  
360  C CG  . ASN A 48  ? 0.1922 0.2350 0.4044 0.0466  -0.0078 0.0085  729 ASN A CG  
361  O OD1 . ASN A 48  ? 0.1658 0.2027 0.3595 0.0399  -0.0116 0.0080  729 ASN A OD1 
362  N ND2 . ASN A 48  ? 0.1763 0.2185 0.3931 0.0504  -0.0118 0.0146  729 ASN A ND2 
363  N N   . SER A 49  ? 0.1380 0.1611 0.3323 0.0438  0.0294  -0.0187 730 SER A N   
364  C CA  . SER A 49  ? 0.1487 0.1708 0.3497 0.0475  0.0435  -0.0253 730 SER A CA  
365  C C   . SER A 49  ? 0.1494 0.1849 0.3813 0.0576  0.0459  -0.0215 730 SER A C   
366  O O   . SER A 49  ? 0.1453 0.1862 0.3849 0.0602  0.0354  -0.0136 730 SER A O   
367  C CB  . SER A 49  ? 0.1694 0.1648 0.3483 0.0472  0.0516  -0.0334 730 SER A CB  
368  O OG  . SER A 49  ? 0.1792 0.1601 0.3591 0.0527  0.0484  -0.0322 730 SER A OG  
369  N N   . ALA A 50  ? 0.1599 0.1995 0.3988 0.0602  0.0581  -0.0257 731 ALA A N   
370  C CA  . ALA A 50  ? 0.1658 0.2185 0.4244 0.0665  0.0582  -0.0207 731 ALA A CA  
371  C C   . ALA A 50  ? 0.2173 0.2571 0.4772 0.0737  0.0544  -0.0179 731 ALA A C   
372  O O   . ALA A 50  ? 0.2004 0.2515 0.4748 0.0776  0.0469  -0.0102 731 ALA A O   
373  C CB  . ALA A 50  ? 0.1792 0.2347 0.4427 0.0684  0.0733  -0.0265 731 ALA A CB  
374  N N   . ASP A 51  ? 0.1908 0.2057 0.4340 0.0748  0.0589  -0.0239 732 ASP A N   
375  C CA  . ASP A 51  ? 0.2051 0.2049 0.4476 0.0809  0.0559  -0.0219 732 ASP A CA  
376  C C   . ASP A 51  ? 0.1976 0.1874 0.4296 0.0773  0.0434  -0.0173 732 ASP A C   
377  O O   . ASP A 51  ? 0.2112 0.1840 0.4379 0.0805  0.0411  -0.0166 732 ASP A O   
378  C CB  . ASP A 51  ? 0.2831 0.2598 0.5123 0.0843  0.0689  -0.0317 732 ASP A CB  
379  C CG  . ASP A 51  ? 0.2363 0.1919 0.4380 0.0773  0.0726  -0.0401 732 ASP A CG  
380  O OD1 . ASP A 51  ? 0.2192 0.1780 0.4144 0.0705  0.0654  -0.0385 732 ASP A OD1 
381  O OD2 . ASP A 51  ? 0.3963 0.3312 0.5814 0.0783  0.0823  -0.0485 732 ASP A OD2 
382  N N   . ASN A 52  ? 0.1776 0.1776 0.4065 0.0706  0.0354  -0.0142 733 ASN A N   
383  C CA  . ASN A 52  ? 0.1848 0.1779 0.4038 0.0663  0.0236  -0.0094 733 ASN A CA  
384  C C   . ASN A 52  ? 0.1826 0.1482 0.3796 0.0630  0.0257  -0.0158 733 ASN A C   
385  O O   . ASN A 52  ? 0.1811 0.1386 0.3685 0.0592  0.0161  -0.0113 733 ASN A O   
386  C CB  . ASN A 52  ? 0.1705 0.1679 0.3975 0.0693  0.0137  0.0006  733 ASN A CB  
387  C CG  . ASN A 52  ? 0.1894 0.2117 0.4314 0.0700  0.0087  0.0076  733 ASN A CG  
388  O OD1 . ASN A 52  ? 0.1601 0.1978 0.4029 0.0652  0.0069  0.0077  733 ASN A OD1 
389  N ND2 . ASN A 52  ? 0.1702 0.1954 0.4228 0.0757  0.0061  0.0131  733 ASN A ND2 
390  N N   . SER A 53  ? 0.1981 0.1494 0.3824 0.0626  0.0373  -0.0259 734 SER A N   
391  C CA  . SER A 53  ? 0.2150 0.1394 0.3732 0.0575  0.0376  -0.0319 734 SER A CA  
392  C C   . SER A 53  ? 0.2323 0.1560 0.3681 0.0462  0.0315  -0.0325 734 SER A C   
393  O O   . SER A 53  ? 0.2469 0.1517 0.3630 0.0406  0.0271  -0.0345 734 SER A O   
394  C CB  . SER A 53  ? 0.2398 0.1459 0.3894 0.0612  0.0523  -0.0428 734 SER A CB  
395  O OG  . SER A 53  ? 0.2375 0.1524 0.3818 0.0581  0.0614  -0.0481 734 SER A OG  
396  N N   . THR A 54  ? 0.2252 0.1685 0.3640 0.0425  0.0307  -0.0306 735 THR A N   
397  C CA  . THR A 54  ? 0.1880 0.1297 0.3063 0.0328  0.0255  -0.0312 735 THR A CA  
398  C C   . THR A 54  ? 0.1602 0.1258 0.2883 0.0304  0.0211  -0.0259 735 THR A C   
399  O O   . THR A 54  ? 0.1526 0.1353 0.3006 0.0350  0.0241  -0.0239 735 THR A O   
400  C CB  . THR A 54  ? 0.2834 0.2098 0.3801 0.0285  0.0348  -0.0406 735 THR A CB  
401  O OG1 . THR A 54  ? 0.2202 0.1448 0.2980 0.0194  0.0283  -0.0400 735 THR A OG1 
402  C CG2 . THR A 54  ? 0.2664 0.2043 0.3733 0.0318  0.0468  -0.0444 735 THR A CG2 
403  N N   . GLY A 55  ? 0.2199 0.1862 0.3342 0.0231  0.0136  -0.0237 736 GLY A N   
404  C CA  . GLY A 55  ? 0.1353 0.1191 0.2526 0.0196  0.0111  -0.0211 736 GLY A CA  
405  C C   . GLY A 55  ? 0.1800 0.1629 0.2891 0.0164  0.0203  -0.0275 736 GLY A C   
406  O O   . GLY A 55  ? 0.1569 0.1231 0.2499 0.0145  0.0266  -0.0337 736 GLY A O   
407  N N   . GLU A 56  ? 0.1988 0.1992 0.3180 0.0152  0.0210  -0.0258 737 GLU A N   
408  C CA  . GLU A 56  ? 0.1342 0.1371 0.2510 0.0126  0.0307  -0.0307 737 GLU A CA  
409  C C   . GLU A 56  ? 0.1202 0.1377 0.2393 0.0076  0.0261  -0.0276 737 GLU A C   
410  O O   . GLU A 56  ? 0.1074 0.1394 0.2405 0.0090  0.0188  -0.0223 737 GLU A O   
411  C CB  . GLU A 56  ? 0.1431 0.1540 0.2802 0.0193  0.0406  -0.0326 737 GLU A CB  
412  C CG  . GLU A 56  ? 0.1513 0.1678 0.2898 0.0168  0.0520  -0.0369 737 GLU A CG  
413  C CD  . GLU A 56  ? 0.2725 0.2974 0.4333 0.0243  0.0630  -0.0388 737 GLU A CD  
414  O OE1 . GLU A 56  ? 0.2466 0.2635 0.4133 0.0317  0.0648  -0.0396 737 GLU A OE1 
415  O OE2 . GLU A 56  ? 0.5253 0.5649 0.6988 0.0229  0.0702  -0.0393 737 GLU A OE2 
416  N N   . PHE A 57  ? 0.1249 0.1370 0.2289 0.0013  0.0300  -0.0308 738 PHE A N   
417  C CA  . PHE A 57  ? 0.1360 0.1583 0.2397 -0.0039 0.0255  -0.0283 738 PHE A CA  
418  C C   . PHE A 57  ? 0.1136 0.1564 0.2404 -0.0027 0.0271  -0.0264 738 PHE A C   
419  O O   . PHE A 57  ? 0.1119 0.1603 0.2514 -0.0002 0.0363  -0.0287 738 PHE A O   
420  C CB  . PHE A 57  ? 0.1786 0.1900 0.2625 -0.0106 0.0303  -0.0317 738 PHE A CB  
421  C CG  . PHE A 57  ? 0.1625 0.1612 0.2264 -0.0142 0.0227  -0.0305 738 PHE A CG  
422  C CD1 . PHE A 57  ? 0.1749 0.1788 0.2367 -0.0173 0.0154  -0.0272 738 PHE A CD1 
423  C CD2 . PHE A 57  ? 0.2284 0.2097 0.2759 -0.0143 0.0227  -0.0326 738 PHE A CD2 
424  C CE1 . PHE A 57  ? 0.2267 0.2202 0.2729 -0.0196 0.0089  -0.0255 738 PHE A CE1 
425  C CE2 . PHE A 57  ? 0.2326 0.2044 0.2645 -0.0176 0.0150  -0.0306 738 PHE A CE2 
426  C CZ  . PHE A 57  ? 0.1915 0.1701 0.2239 -0.0198 0.0083  -0.0268 738 PHE A CZ  
427  N N   . ILE A 58  ? 0.1326 0.1866 0.2650 -0.0046 0.0181  -0.0222 739 ILE A N   
428  C CA  . ILE A 58  ? 0.1255 0.1979 0.2755 -0.0065 0.0177  -0.0206 739 ILE A CA  
429  C C   . ILE A 58  ? 0.1005 0.1706 0.2418 -0.0139 0.0238  -0.0238 739 ILE A C   
430  O O   . ILE A 58  ? 0.1244 0.1830 0.2462 -0.0186 0.0213  -0.0247 739 ILE A O   
431  C CB  . ILE A 58  ? 0.0879 0.1699 0.2417 -0.0072 0.0058  -0.0158 739 ILE A CB  
432  C CG1 . ILE A 58  ? 0.1367 0.2193 0.2968 -0.0005 -0.0001 -0.0117 739 ILE A CG1 
433  C CG2 . ILE A 58  ? 0.0969 0.1976 0.2685 -0.0100 0.0040  -0.0142 739 ILE A CG2 
434  C CD1 . ILE A 58  ? 0.1772 0.2659 0.3353 -0.0015 -0.0111 -0.0070 739 ILE A CD1 
435  N N   . GLY A 59  ? 0.0964 0.1774 0.2531 -0.0147 0.0319  -0.0251 740 GLY A N   
436  C CA  . GLY A 59  ? 0.1037 0.1819 0.2526 -0.0222 0.0392  -0.0277 740 GLY A CA  
437  C C   . GLY A 59  ? 0.2594 0.3182 0.3872 -0.0227 0.0482  -0.0319 740 GLY A C   
438  O O   . GLY A 59  ? 0.2617 0.3103 0.3836 -0.0173 0.0499  -0.0335 740 GLY A O   
439  N N   . ASP A 60  ? 0.1485 0.2008 0.2634 -0.0301 0.0534  -0.0335 741 ASP A N   
440  C CA  . ASP A 60  ? 0.2194 0.2527 0.3113 -0.0323 0.0617  -0.0370 741 ASP A CA  
441  C C   . ASP A 60  ? 0.2153 0.2319 0.2827 -0.0352 0.0528  -0.0360 741 ASP A C   
442  O O   . ASP A 60  ? 0.2015 0.2172 0.2627 -0.0407 0.0481  -0.0341 741 ASP A O   
443  C CB  . ASP A 60  ? 0.2058 0.2414 0.2974 -0.0389 0.0730  -0.0383 741 ASP A CB  
444  C CG  . ASP A 60  ? 0.2651 0.2820 0.3334 -0.0407 0.0835  -0.0421 741 ASP A CG  
445  O OD1 . ASP A 60  ? 0.3120 0.3110 0.3583 -0.0397 0.0788  -0.0431 741 ASP A OD1 
446  O OD2 . ASP A 60  ? 0.2764 0.2966 0.3479 -0.0435 0.0964  -0.0438 741 ASP A OD2 
447  N N   . LYS A 61  ? 0.1710 0.1738 0.2249 -0.0315 0.0507  -0.0373 742 LYS A N   
448  C CA  . LYS A 61  ? 0.2705 0.2605 0.3058 -0.0332 0.0409  -0.0353 742 LYS A CA  
449  C C   . LYS A 61  ? 0.2299 0.2078 0.2450 -0.0404 0.0424  -0.0351 742 LYS A C   
450  O O   . LYS A 61  ? 0.3451 0.3176 0.3510 -0.0423 0.0338  -0.0323 742 LYS A O   
451  C CB  . LYS A 61  ? 0.1957 0.1730 0.2206 -0.0293 0.0389  -0.0368 742 LYS A CB  
452  C CG  . LYS A 61  ? 0.2729 0.2357 0.2821 -0.0307 0.0490  -0.0415 742 LYS A CG  
453  C CD  . LYS A 61  ? 0.4203 0.3682 0.4166 -0.0283 0.0449  -0.0431 742 LYS A CD  
454  C CE  . LYS A 61  ? 0.4590 0.3912 0.4383 -0.0295 0.0557  -0.0489 742 LYS A CE  
455  N NZ  . LYS A 61  ? 0.4745 0.4156 0.4710 -0.0246 0.0681  -0.0526 742 LYS A NZ  
456  N N   . SER A 62  ? 0.2387 0.2118 0.2468 -0.0442 0.0535  -0.0377 743 SER A N   
457  C CA  A SER A 62  ? 0.2762 0.2371 0.2644 -0.0515 0.0553  -0.0367 743 SER A CA  
458  C CA  B SER A 62  ? 0.2767 0.2375 0.2649 -0.0515 0.0553  -0.0367 743 SER A CA  
459  C C   . SER A 62  ? 0.3013 0.2717 0.2992 -0.0563 0.0541  -0.0341 743 SER A C   
460  O O   . SER A 62  ? 0.3583 0.3178 0.3405 -0.0622 0.0532  -0.0322 743 SER A O   
461  C CB  A SER A 62  ? 0.3020 0.2533 0.2768 -0.0546 0.0686  -0.0401 743 SER A CB  
462  C CB  B SER A 62  ? 0.3020 0.2534 0.2770 -0.0546 0.0686  -0.0401 743 SER A CB  
463  O OG  A SER A 62  ? 0.4039 0.3407 0.3625 -0.0518 0.0687  -0.0429 743 SER A OG  
464  O OG  B SER A 62  ? 0.2287 0.1948 0.2221 -0.0557 0.0794  -0.0412 743 SER A OG  
465  N N   . LYS A 63  ? 0.2279 0.2174 0.2505 -0.0544 0.0533  -0.0338 744 LYS A N   
466  C CA  . LYS A 63  ? 0.2135 0.2120 0.2457 -0.0598 0.0517  -0.0319 744 LYS A CA  
467  C C   . LYS A 63  ? 0.1858 0.1920 0.2272 -0.0575 0.0397  -0.0300 744 LYS A C   
468  O O   . LYS A 63  ? 0.1930 0.1992 0.2336 -0.0625 0.0359  -0.0288 744 LYS A O   
469  C CB  . LYS A 63  ? 0.1630 0.1788 0.2169 -0.0616 0.0612  -0.0330 744 LYS A CB  
470  C CG  . LYS A 63  ? 0.2037 0.2141 0.2506 -0.0641 0.0756  -0.0351 744 LYS A CG  
471  C CD  . LYS A 63  ? 0.3175 0.3482 0.3902 -0.0661 0.0847  -0.0352 744 LYS A CD  
472  C CE  . LYS A 63  ? 0.3744 0.4022 0.4435 -0.0661 0.1012  -0.0380 744 LYS A CE  
473  N NZ  . LYS A 63  ? 0.4176 0.4684 0.5172 -0.0657 0.1104  -0.0379 744 LYS A NZ  
474  N N   . ASN A 64  ? 0.1363 0.1479 0.1853 -0.0503 0.0341  -0.0298 745 ASN A N   
475  C CA  . ASN A 64  ? 0.1962 0.2152 0.2525 -0.0480 0.0236  -0.0278 745 ASN A CA  
476  C C   . ASN A 64  ? 0.1930 0.1990 0.2324 -0.0505 0.0174  -0.0266 745 ASN A C   
477  O O   . ASN A 64  ? 0.2605 0.2511 0.2822 -0.0519 0.0187  -0.0263 745 ASN A O   
478  C CB  . ASN A 64  ? 0.1519 0.1747 0.2143 -0.0402 0.0191  -0.0270 745 ASN A CB  
479  C CG  . ASN A 64  ? 0.1585 0.1940 0.2399 -0.0363 0.0244  -0.0278 745 ASN A CG  
480  O OD1 . ASN A 64  ? 0.1167 0.1646 0.2130 -0.0388 0.0289  -0.0281 745 ASN A OD1 
481  N ND2 . ASN A 64  ? 0.1183 0.1511 0.2006 -0.0300 0.0237  -0.0278 745 ASN A ND2 
482  N N   . THR A 65  ? 0.1010 0.1648 0.2479 -0.0346 0.0230  -0.0255 746 THR A N   
483  C CA  . THR A 65  ? 0.1117 0.1674 0.2498 -0.0347 0.0208  -0.0245 746 THR A CA  
484  C C   . THR A 65  ? 0.1616 0.2256 0.3032 -0.0329 0.0132  -0.0253 746 THR A C   
485  O O   . THR A 65  ? 0.0839 0.1598 0.2361 -0.0338 0.0104  -0.0278 746 THR A O   
486  C CB  . THR A 65  ? 0.1589 0.2089 0.2974 -0.0399 0.0261  -0.0266 746 THR A CB  
487  O OG1 . THR A 65  ? 0.1127 0.1743 0.2644 -0.0442 0.0251  -0.0309 746 THR A OG1 
488  C CG2 . THR A 65  ? 0.1314 0.1723 0.2658 -0.0418 0.0344  -0.0257 746 THR A CG2 
489  N N   . TYR A 66  ? 0.0894 0.1473 0.2220 -0.0301 0.0099  -0.0228 747 TYR A N   
490  C CA  . TYR A 66  ? 0.1256 0.1894 0.2598 -0.0281 0.0035  -0.0233 747 TYR A CA  
491  C C   . TYR A 66  ? 0.0887 0.1440 0.2159 -0.0283 0.0037  -0.0225 747 TYR A C   
492  O O   . TYR A 66  ? 0.1413 0.1860 0.2611 -0.0282 0.0077  -0.0203 747 TYR A O   
493  C CB  . TYR A 66  ? 0.0962 0.1626 0.2275 -0.0233 -0.0010 -0.0205 747 TYR A CB  
494  C CG  . TYR A 66  ? 0.0856 0.1554 0.2198 -0.0222 0.0005  -0.0201 747 TYR A CG  
495  C CD1 . TYR A 66  ? 0.0697 0.1507 0.2139 -0.0218 -0.0013 -0.0220 747 TYR A CD1 
496  C CD2 . TYR A 66  ? 0.1141 0.1755 0.2402 -0.0214 0.0038  -0.0175 747 TYR A CD2 
497  C CE1 . TYR A 66  ? 0.0916 0.1748 0.2384 -0.0201 0.0011  -0.0214 747 TYR A CE1 
498  C CE2 . TYR A 66  ? 0.0977 0.1603 0.2249 -0.0204 0.0062  -0.0173 747 TYR A CE2 
499  C CZ  . TYR A 66  ? 0.1071 0.1804 0.2449 -0.0196 0.0052  -0.0192 747 TYR A CZ  
500  O OH  . TYR A 66  ? 0.1157 0.1892 0.2546 -0.0180 0.0086  -0.0188 747 TYR A OH  
501  N N   . GLU A 67  ? 0.0843 0.1437 0.2134 -0.0283 -0.0003 -0.0243 748 GLU A N   
502  C CA  A GLU A 67  ? 0.1148 0.1662 0.2382 -0.0287 0.0008  -0.0242 748 GLU A CA  
503  C CA  B GLU A 67  ? 0.1145 0.1659 0.2379 -0.0288 0.0008  -0.0243 748 GLU A CA  
504  C C   . GLU A 67  ? 0.1029 0.1579 0.2252 -0.0256 -0.0046 -0.0238 748 GLU A C   
505  O O   . GLU A 67  ? 0.1350 0.1996 0.2625 -0.0253 -0.0090 -0.0254 748 GLU A O   
506  C CB  A GLU A 67  ? 0.1583 0.2080 0.2846 -0.0349 0.0042  -0.0288 748 GLU A CB  
507  C CB  B GLU A 67  ? 0.1582 0.2084 0.2849 -0.0350 0.0042  -0.0290 748 GLU A CB  
508  C CG  A GLU A 67  ? 0.1953 0.2322 0.3136 -0.0358 0.0084  -0.0286 748 GLU A CG  
509  C CG  B GLU A 67  ? 0.1603 0.2043 0.2823 -0.0366 0.0045  -0.0309 748 GLU A CG  
510  C CD  A GLU A 67  ? 0.1787 0.2115 0.2988 -0.0428 0.0134  -0.0329 748 GLU A CD  
511  C CD  B GLU A 67  ? 0.1850 0.2284 0.3104 -0.0441 0.0075  -0.0361 748 GLU A CD  
512  O OE1 A GLU A 67  ? 0.2512 0.2936 0.3803 -0.0473 0.0126  -0.0365 748 GLU A OE1 
513  O OE1 B GLU A 67  ? 0.2441 0.2897 0.3749 -0.0476 0.0108  -0.0374 748 GLU A OE1 
514  O OE2 A GLU A 67  ? 0.2334 0.2535 0.3462 -0.0439 0.0184  -0.0327 748 GLU A OE2 
515  O OE2 B GLU A 67  ? 0.2076 0.2480 0.3300 -0.0469 0.0068  -0.0392 748 GLU A OE2 
516  N N   . TRP A 68  ? 0.0917 0.1388 0.2072 -0.0228 -0.0038 -0.0211 749 TRP A N   
517  C CA  . TRP A 68  ? 0.0906 0.1393 0.2045 -0.0201 -0.0074 -0.0207 749 TRP A CA  
518  C C   . TRP A 68  ? 0.1177 0.1579 0.2271 -0.0220 -0.0041 -0.0226 749 TRP A C   
519  O O   . TRP A 68  ? 0.1027 0.1336 0.2086 -0.0236 0.0012  -0.0223 749 TRP A O   
520  C CB  . TRP A 68  ? 0.1081 0.1557 0.2187 -0.0146 -0.0093 -0.0154 749 TRP A CB  
521  C CG  . TRP A 68  ? 0.1079 0.1463 0.2133 -0.0127 -0.0054 -0.0114 749 TRP A CG  
522  C CD1 . TRP A 68  ? 0.1289 0.1646 0.2321 -0.0122 -0.0040 -0.0085 749 TRP A CD1 
523  C CD2 . TRP A 68  ? 0.0952 0.1254 0.1963 -0.0107 -0.0024 -0.0096 749 TRP A CD2 
524  N NE1 . TRP A 68  ? 0.1321 0.1589 0.2300 -0.0098 -0.0009 -0.0047 749 TRP A NE1 
525  C CE2 . TRP A 68  ? 0.1430 0.1665 0.2402 -0.0086 0.0004  -0.0051 749 TRP A CE2 
526  C CE3 . TRP A 68  ? 0.1118 0.1390 0.2114 -0.0102 -0.0015 -0.0110 749 TRP A CE3 
527  C CZ2 . TRP A 68  ? 0.1088 0.1235 0.2017 -0.0054 0.0041  -0.0017 749 TRP A CZ2 
528  C CZ3 . TRP A 68  ? 0.1145 0.1321 0.2096 -0.0073 0.0029  -0.0080 749 TRP A CZ3 
529  C CH2 . TRP A 68  ? 0.1115 0.1234 0.2039 -0.0047 0.0057  -0.0033 749 TRP A CH2 
530  N N   . GLN A 69  ? 0.0939 0.1359 0.2024 -0.0219 -0.0068 -0.0245 750 GLN A N   
531  C CA  . GLN A 69  ? 0.1041 0.1366 0.2067 -0.0237 -0.0033 -0.0267 750 GLN A CA  
532  C C   . GLN A 69  ? 0.1251 0.1573 0.2244 -0.0200 -0.0055 -0.0256 750 GLN A C   
533  O O   . GLN A 69  ? 0.1012 0.1420 0.2030 -0.0196 -0.0107 -0.0267 750 GLN A O   
534  C CB  . GLN A 69  ? 0.1096 0.1434 0.2138 -0.0309 -0.0031 -0.0328 750 GLN A CB  
535  C CG  . GLN A 69  ? 0.2324 0.2546 0.3287 -0.0339 0.0008  -0.0359 750 GLN A CG  
536  C CD  . GLN A 69  ? 0.1934 0.2172 0.2913 -0.0423 0.0007  -0.0422 750 GLN A CD  
537  O OE1 . GLN A 69  ? 0.1828 0.2094 0.2862 -0.0462 0.0023  -0.0435 750 GLN A OE1 
538  N NE2 . GLN A 69  ? 0.2237 0.2458 0.3167 -0.0454 -0.0014 -0.0461 750 GLN A NE2 
539  N N   . THR A 70  ? 0.1101 0.1321 0.2036 -0.0171 -0.0011 -0.0232 751 THR A N   
540  C CA  . THR A 70  ? 0.1105 0.1311 0.2008 -0.0133 -0.0018 -0.0217 751 THR A CA  
541  C C   . THR A 70  ? 0.1378 0.1500 0.2211 -0.0168 0.0008  -0.0264 751 THR A C   
542  O O   . THR A 70  ? 0.2088 0.2145 0.2891 -0.0219 0.0040  -0.0301 751 THR A O   
543  C CB  . THR A 70  ? 0.1410 0.1569 0.2306 -0.0071 0.0014  -0.0155 751 THR A CB  
544  O OG1 . THR A 70  ? 0.1964 0.2024 0.2831 -0.0075 0.0073  -0.0143 751 THR A OG1 
545  C CG2 . THR A 70  ? 0.1712 0.1968 0.2666 -0.0038 -0.0030 -0.0112 751 THR A CG2 
546  N N   . PRO A 71  ? 0.1885 0.1997 0.2679 -0.0145 -0.0002 -0.0264 752 PRO A N   
547  C CA  . PRO A 71  ? 0.1360 0.1383 0.2066 -0.0184 0.0021  -0.0313 752 PRO A CA  
548  C C   . PRO A 71  ? 0.1792 0.1661 0.2430 -0.0195 0.0103  -0.0320 752 PRO A C   
549  O O   . PRO A 71  ? 0.2361 0.2151 0.2927 -0.0254 0.0122  -0.0375 752 PRO A O   
550  C CB  . PRO A 71  ? 0.1350 0.1377 0.2024 -0.0140 0.0009  -0.0296 752 PRO A CB  
551  C CG  . PRO A 71  ? 0.1204 0.1370 0.1964 -0.0108 -0.0052 -0.0263 752 PRO A CG  
552  C CD  . PRO A 71  ? 0.1415 0.1604 0.2240 -0.0095 -0.0040 -0.0229 752 PRO A CD  
553  N N   . ASP A 72  ? 0.1568 0.1387 0.2221 -0.0142 0.0151  -0.0266 753 ASP A N   
554  C CA  . ASP A 72  ? 0.1815 0.1476 0.2399 -0.0145 0.0236  -0.0266 753 ASP A CA  
555  C C   . ASP A 72  ? 0.1855 0.1486 0.2444 -0.0203 0.0254  -0.0294 753 ASP A C   
556  O O   . ASP A 72  ? 0.2426 0.1915 0.2951 -0.0213 0.0329  -0.0298 753 ASP A O   
557  C CB  . ASP A 72  ? 0.2362 0.1985 0.2966 -0.0061 0.0282  -0.0191 753 ASP A CB  
558  C CG  . ASP A 72  ? 0.2617 0.2344 0.3309 -0.0028 0.0244  -0.0139 753 ASP A CG  
559  O OD1 . ASP A 72  ? 0.2797 0.2609 0.3531 -0.0069 0.0195  -0.0161 753 ASP A OD1 
560  O OD2 . ASP A 72  ? 0.2359 0.2082 0.3078 0.0040  0.0264  -0.0073 753 ASP A OD2 
561  N N   . GLY A 73  ? 0.2050 0.1805 0.2709 -0.0241 0.0194  -0.0314 754 GLY A N   
562  C CA  . GLY A 73  ? 0.1881 0.1620 0.2553 -0.0304 0.0211  -0.0346 754 GLY A CA  
563  C C   . GLY A 73  ? 0.2304 0.2059 0.3024 -0.0274 0.0226  -0.0298 754 GLY A C   
564  O O   . GLY A 73  ? 0.2032 0.1785 0.2773 -0.0325 0.0241  -0.0321 754 GLY A O   
565  N N   . GLN A 74  ? 0.1715 0.1484 0.2451 -0.0197 0.0224  -0.0232 755 GLN A N   
566  C CA  . GLN A 74  ? 0.1488 0.1272 0.2255 -0.0168 0.0229  -0.0183 755 GLN A CA  
567  C C   . GLN A 74  ? 0.2326 0.2248 0.3167 -0.0192 0.0167  -0.0196 755 GLN A C   
568  O O   . GLN A 74  ? 0.1323 0.1352 0.2206 -0.0198 0.0109  -0.0215 755 GLN A O   
569  C CB  . GLN A 74  ? 0.2219 0.2006 0.2991 -0.0083 0.0228  -0.0110 755 GLN A CB  
570  C CG  . GLN A 74  ? 0.2456 0.2109 0.3165 -0.0046 0.0297  -0.0089 755 GLN A CG  
571  C CD  . GLN A 74  ? 0.3671 0.3183 0.4322 -0.0057 0.0372  -0.0082 755 GLN A CD  
572  O OE1 . GLN A 74  ? 0.4528 0.3935 0.5121 -0.0110 0.0422  -0.0133 755 GLN A OE1 
573  N NE2 . GLN A 74  ? 0.4231 0.3737 0.4891 -0.0009 0.0379  -0.0019 755 GLN A NE2 
574  N N   . LYS A 75  ? 0.1793 0.1704 0.2644 -0.0202 0.0186  -0.0180 756 LYS A N   
575  C CA  . LYS A 75  ? 0.1274 0.1297 0.2189 -0.0225 0.0143  -0.0192 756 LYS A CA  
576  C C   . LYS A 75  ? 0.1416 0.1415 0.2319 -0.0199 0.0160  -0.0144 756 LYS A C   
577  O O   . LYS A 75  ? 0.2092 0.1980 0.2937 -0.0176 0.0209  -0.0110 756 LYS A O   
578  C CB  . LYS A 75  ? 0.1362 0.1406 0.2310 -0.0303 0.0153  -0.0257 756 LYS A CB  
579  C CG  . LYS A 75  ? 0.2216 0.2128 0.3114 -0.0344 0.0231  -0.0273 756 LYS A CG  
580  C CD  . LYS A 75  ? 0.2558 0.2514 0.3507 -0.0429 0.0235  -0.0336 756 LYS A CD  
581  C CE  . LYS A 75  ? 0.3574 0.3610 0.4551 -0.0462 0.0182  -0.0384 756 LYS A CE  
582  N NZ  . LYS A 75  ? 0.5350 0.5423 0.6374 -0.0552 0.0188  -0.0447 756 LYS A NZ  
583  N N   . GLY A 76  ? 0.1188 0.1282 0.2137 -0.0200 0.0120  -0.0141 757 GLY A N   
584  C CA  . GLY A 76  ? 0.1205 0.1273 0.2129 -0.0186 0.0134  -0.0104 757 GLY A CA  
585  C C   . GLY A 76  ? 0.1200 0.1362 0.2180 -0.0212 0.0108  -0.0126 757 GLY A C   
586  O O   . GLY A 76  ? 0.1780 0.2038 0.2824 -0.0229 0.0071  -0.0161 757 GLY A O   
587  N N   . SER A 77  ? 0.1792 0.1920 0.2741 -0.0211 0.0130  -0.0103 758 SER A N   
588  C CA  . SER A 77  ? 0.1402 0.1595 0.2395 -0.0234 0.0125  -0.0122 758 SER A CA  
589  C C   . SER A 77  ? 0.1627 0.1833 0.2580 -0.0198 0.0093  -0.0081 758 SER A C   
590  O O   . SER A 77  ? 0.2023 0.2179 0.2909 -0.0162 0.0081  -0.0034 758 SER A O   
591  C CB  . SER A 77  ? 0.2168 0.2297 0.3154 -0.0278 0.0194  -0.0141 758 SER A CB  
592  O OG  . SER A 77  ? 0.2851 0.2971 0.3877 -0.0325 0.0224  -0.0186 758 SER A OG  
593  N N   . PHE A 78  ? 0.1045 0.1323 0.2042 -0.0209 0.0079  -0.0099 759 PHE A N   
594  C CA  . PHE A 78  ? 0.1349 0.1625 0.2298 -0.0187 0.0059  -0.0069 759 PHE A CA  
595  C C   . PHE A 78  ? 0.1471 0.1780 0.2460 -0.0211 0.0087  -0.0097 759 PHE A C   
596  O O   . PHE A 78  ? 0.1566 0.1919 0.2637 -0.0242 0.0114  -0.0135 759 PHE A O   
597  C CB  . PHE A 78  ? 0.0945 0.1284 0.1899 -0.0153 -0.0009 -0.0051 759 PHE A CB  
598  C CG  . PHE A 78  ? 0.1020 0.1462 0.2062 -0.0156 -0.0040 -0.0085 759 PHE A CG  
599  C CD1 . PHE A 78  ? 0.0837 0.1308 0.1920 -0.0157 -0.0053 -0.0104 759 PHE A CD1 
600  C CD2 . PHE A 78  ? 0.0922 0.1421 0.1991 -0.0153 -0.0056 -0.0095 759 PHE A CD2 
601  C CE1 . PHE A 78  ? 0.0779 0.1341 0.1929 -0.0158 -0.0087 -0.0132 759 PHE A CE1 
602  C CE2 . PHE A 78  ? 0.0727 0.1318 0.1871 -0.0148 -0.0087 -0.0120 759 PHE A CE2 
603  C CZ  . PHE A 78  ? 0.0699 0.1324 0.1882 -0.0150 -0.0106 -0.0137 759 PHE A CZ  
604  N N   . THR A 79  ? 0.1385 0.1669 0.2314 -0.0199 0.0083  -0.0076 760 THR A N   
605  C CA  . THR A 79  ? 0.1138 0.1432 0.2086 -0.0214 0.0120  -0.0094 760 THR A CA  
606  C C   . THR A 79  ? 0.1237 0.1563 0.2163 -0.0191 0.0080  -0.0084 760 THR A C   
607  O O   . THR A 79  ? 0.1014 0.1355 0.1910 -0.0169 0.0023  -0.0063 760 THR A O   
608  C CB  . THR A 79  ? 0.1546 0.1726 0.2406 -0.0231 0.0184  -0.0080 760 THR A CB  
609  O OG1 . THR A 79  ? 0.1991 0.2094 0.2721 -0.0212 0.0158  -0.0039 760 THR A OG1 
610  C CG2 . THR A 79  ? 0.2910 0.3032 0.3769 -0.0253 0.0227  -0.0084 760 THR A CG2 
611  N N   . SER A 80  ? 0.1396 0.1726 0.2336 -0.0197 0.0116  -0.0098 761 SER A N   
612  C CA  . SER A 80  ? 0.1079 0.1420 0.1988 -0.0178 0.0090  -0.0092 761 SER A CA  
613  C C   . SER A 80  ? 0.1671 0.1925 0.2438 -0.0173 0.0063  -0.0057 761 SER A C   
614  O O   . SER A 80  ? 0.1251 0.1521 0.1989 -0.0160 0.0018  -0.0048 761 SER A O   
615  C CB  . SER A 80  ? 0.1372 0.1712 0.2311 -0.0182 0.0150  -0.0110 761 SER A CB  
616  O OG  . SER A 80  ? 0.1997 0.2222 0.2834 -0.0200 0.0209  -0.0101 761 SER A OG  
617  N N   . GLU A 81  ? 0.1948 0.2109 0.2624 -0.0185 0.0086  -0.0036 762 GLU A N   
618  C CA  . GLU A 81  ? 0.1426 0.1513 0.1967 -0.0183 0.0049  0.0001  762 GLU A CA  
619  C C   . GLU A 81  ? 0.1777 0.1926 0.2340 -0.0163 -0.0027 0.0023  762 GLU A C   
620  O O   . GLU A 81  ? 0.1552 0.1674 0.2029 -0.0162 -0.0071 0.0053  762 GLU A O   
621  C CB  . GLU A 81  ? 0.2387 0.2368 0.2832 -0.0193 0.0086  0.0025  762 GLU A CB  
622  C CG  . GLU A 81  ? 0.4673 0.4582 0.5090 -0.0215 0.0172  0.0005  762 GLU A CG  
623  C CD  . GLU A 81  ? 0.5106 0.4913 0.5377 -0.0226 0.0189  0.0015  762 GLU A CD  
624  O OE1 . GLU A 81  ? 0.3004 0.2802 0.3195 -0.0222 0.0128  0.0036  762 GLU A OE1 
625  O OE2 . GLU A 81  ? 0.4732 0.4465 0.4965 -0.0242 0.0266  0.0002  762 GLU A OE2 
626  N N   . ASP A 82  ? 0.1393 0.1621 0.2066 -0.0151 -0.0041 0.0011  763 ASP A N   
627  C CA  . ASP A 82  ? 0.1464 0.1745 0.2164 -0.0130 -0.0099 0.0032  763 ASP A CA  
628  C C   . ASP A 82  ? 0.1659 0.2023 0.2420 -0.0121 -0.0138 0.0016  763 ASP A C   
629  O O   . ASP A 82  ? 0.1359 0.1769 0.2147 -0.0104 -0.0182 0.0032  763 ASP A O   
630  C CB  . ASP A 82  ? 0.1876 0.2169 0.2636 -0.0123 -0.0084 0.0029  763 ASP A CB  
631  C CG  . ASP A 82  ? 0.1813 0.2012 0.2509 -0.0131 -0.0039 0.0046  763 ASP A CG  
632  O OD1 . ASP A 82  ? 0.1976 0.2117 0.2576 -0.0123 -0.0055 0.0086  763 ASP A OD1 
633  O OD2 . ASP A 82  ? 0.1802 0.1983 0.2538 -0.0147 0.0012  0.0021  763 ASP A OD2 
634  N N   . ILE A 83  ? 0.1430 0.1808 0.2212 -0.0127 -0.0117 -0.0012 764 ILE A N   
635  C CA  . ILE A 83  ? 0.0831 0.1281 0.1673 -0.0113 -0.0145 -0.0027 764 ILE A CA  
636  C C   . ILE A 83  ? 0.1164 0.1578 0.1924 -0.0118 -0.0166 -0.0015 764 ILE A C   
637  O O   . ILE A 83  ? 0.1375 0.1717 0.2057 -0.0133 -0.0135 -0.0016 764 ILE A O   
638  C CB  . ILE A 83  ? 0.0939 0.1437 0.1868 -0.0111 -0.0109 -0.0062 764 ILE A CB  
639  C CG1 . ILE A 83  ? 0.0778 0.1305 0.1779 -0.0121 -0.0088 -0.0078 764 ILE A CG1 
640  C CG2 . ILE A 83  ? 0.1253 0.1823 0.2238 -0.0090 -0.0141 -0.0072 764 ILE A CG2 
641  C CD1 . ILE A 83  ? 0.1026 0.1620 0.2128 -0.0124 -0.0061 -0.0111 764 ILE A CD1 
642  N N   . HIS A 84  ? 0.1094 0.1551 0.1866 -0.0108 -0.0214 -0.0004 765 HIS A N   
643  C CA  . HIS A 84  ? 0.0991 0.1418 0.1691 -0.0119 -0.0237 0.0004  765 HIS A CA  
644  C C   . HIS A 84  ? 0.1262 0.1735 0.2018 -0.0101 -0.0240 -0.0015 765 HIS A C   
645  O O   . HIS A 84  ? 0.1146 0.1685 0.1969 -0.0084 -0.0268 -0.0013 765 HIS A O   
646  C CB  . HIS A 84  ? 0.1124 0.1562 0.1792 -0.0127 -0.0291 0.0039  765 HIS A CB  
647  C CG  . HIS A 84  ? 0.1064 0.1466 0.1685 -0.0133 -0.0294 0.0066  765 HIS A CG  
648  N ND1 . HIS A 84  ? 0.1377 0.1704 0.1881 -0.0159 -0.0299 0.0082  765 HIS A ND1 
649  C CD2 . HIS A 84  ? 0.1139 0.1559 0.1803 -0.0117 -0.0290 0.0081  765 HIS A CD2 
650  C CE1 . HIS A 84  ? 0.2407 0.2714 0.2888 -0.0154 -0.0301 0.0110  765 HIS A CE1 
651  N NE2 . HIS A 84  ? 0.1151 0.1510 0.1729 -0.0127 -0.0293 0.0110  765 HIS A NE2 
652  N N   . PHE A 85  ? 0.0915 0.1348 0.1640 -0.0102 -0.0206 -0.0031 766 PHE A N   
653  C CA  . PHE A 85  ? 0.0925 0.1390 0.1693 -0.0079 -0.0205 -0.0044 766 PHE A CA  
654  C C   . PHE A 85  ? 0.0865 0.1291 0.1559 -0.0094 -0.0232 -0.0034 766 PHE A C   
655  O O   . PHE A 85  ? 0.1282 0.1630 0.1872 -0.0125 -0.0229 -0.0028 766 PHE A O   
656  C CB  . PHE A 85  ? 0.1139 0.1581 0.1921 -0.0065 -0.0148 -0.0063 766 PHE A CB  
657  C CG  . PHE A 85  ? 0.1355 0.1846 0.2224 -0.0058 -0.0119 -0.0075 766 PHE A CG  
658  C CD1 . PHE A 85  ? 0.1180 0.1770 0.2165 -0.0035 -0.0134 -0.0085 766 PHE A CD1 
659  C CD2 . PHE A 85  ? 0.1190 0.1624 0.2019 -0.0078 -0.0076 -0.0078 766 PHE A CD2 
660  C CE1 . PHE A 85  ? 0.0700 0.1339 0.1767 -0.0038 -0.0109 -0.0100 766 PHE A CE1 
661  C CE2 . PHE A 85  ? 0.1533 0.2010 0.2447 -0.0077 -0.0044 -0.0091 766 PHE A CE2 
662  C CZ  . PHE A 85  ? 0.1184 0.1767 0.2220 -0.0060 -0.0063 -0.0103 766 PHE A CZ  
663  N N   . TYR A 86  ? 0.0781 0.1257 0.1522 -0.0075 -0.0257 -0.0032 767 TYR A N   
664  C CA  . TYR A 86  ? 0.0966 0.1404 0.1643 -0.0092 -0.0275 -0.0025 767 TYR A CA  
665  C C   . TYR A 86  ? 0.1423 0.1768 0.2019 -0.0099 -0.0231 -0.0039 767 TYR A C   
666  O O   . TYR A 86  ? 0.1390 0.1659 0.1883 -0.0137 -0.0236 -0.0037 767 TYR A O   
667  C CB  . TYR A 86  ? 0.0911 0.1408 0.1652 -0.0066 -0.0296 -0.0023 767 TYR A CB  
668  C CG  . TYR A 86  ? 0.0959 0.1416 0.1641 -0.0085 -0.0308 -0.0017 767 TYR A CG  
669  C CD1 . TYR A 86  ? 0.1386 0.1834 0.2025 -0.0128 -0.0343 -0.0001 767 TYR A CD1 
670  C CD2 . TYR A 86  ? 0.1067 0.1497 0.1743 -0.0062 -0.0285 -0.0025 767 TYR A CD2 
671  C CE1 . TYR A 86  ? 0.2113 0.2528 0.2705 -0.0154 -0.0353 0.0002  767 TYR A CE1 
672  C CE2 . TYR A 86  ? 0.1820 0.2201 0.2436 -0.0083 -0.0289 -0.0021 767 TYR A CE2 
673  C CZ  . TYR A 86  ? 0.1749 0.2123 0.2324 -0.0134 -0.0323 -0.0010 767 TYR A CZ  
674  O OH  . TYR A 86  ? 0.1612 0.1940 0.2135 -0.0163 -0.0325 -0.0008 767 TYR A OH  
675  N N   . ASN A 87  ? 0.1119 0.1469 0.1761 -0.0063 -0.0187 -0.0053 768 ASN A N   
676  C CA  . ASN A 87  ? 0.1015 0.1271 0.1586 -0.0059 -0.0131 -0.0064 768 ASN A CA  
677  C C   . ASN A 87  ? 0.0992 0.1287 0.1650 -0.0018 -0.0084 -0.0073 768 ASN A C   
678  O O   . ASN A 87  ? 0.1621 0.1962 0.2350 0.0026  -0.0074 -0.0073 768 ASN A O   
679  C CB  . ASN A 87  ? 0.1636 0.1849 0.2166 -0.0051 -0.0129 -0.0063 768 ASN A CB  
680  C CG  . ASN A 87  ? 0.1970 0.2055 0.2395 -0.0057 -0.0068 -0.0074 768 ASN A CG  
681  O OD1 . ASN A 87  ? 0.2081 0.2127 0.2494 -0.0049 -0.0017 -0.0082 768 ASN A OD1 
682  N ND2 . ASN A 87  ? 0.2217 0.2227 0.2561 -0.0073 -0.0066 -0.0075 768 ASN A ND2 
683  N N   . LYS A 88  ? 0.1093 0.1370 0.1744 -0.0033 -0.0055 -0.0079 769 LYS A N   
684  C CA  . LYS A 88  ? 0.1722 0.2043 0.2466 -0.0001 -0.0006 -0.0087 769 LYS A CA  
685  C C   . LYS A 88  ? 0.1570 0.1825 0.2287 0.0028  0.0059  -0.0091 769 LYS A C   
686  O O   . LYS A 88  ? 0.1539 0.1865 0.2366 0.0074  0.0084  -0.0091 769 LYS A O   
687  C CB  . LYS A 88  ? 0.1679 0.1978 0.2408 -0.0029 0.0018  -0.0092 769 LYS A CB  
688  C CG  . LYS A 88  ? 0.1298 0.1636 0.2121 -0.0006 0.0079  -0.0102 769 LYS A CG  
689  C CD  . LYS A 88  ? 0.2437 0.2738 0.3233 -0.0038 0.0109  -0.0106 769 LYS A CD  
690  C CE  . LYS A 88  ? 0.3079 0.3419 0.3976 -0.0019 0.0179  -0.0116 769 LYS A CE  
691  N NZ  . LYS A 88  ? 0.4325 0.4615 0.5190 -0.0051 0.0223  -0.0120 769 LYS A NZ  
692  N N   . LYS A 89  ? 0.2244 0.2363 0.2816 0.0003  0.0087  -0.0094 770 LYS A N   
693  C CA  . LYS A 89  ? 0.2397 0.2428 0.2926 0.0031  0.0160  -0.0098 770 LYS A CA  
694  C C   . LYS A 89  ? 0.2203 0.2287 0.2805 0.0084  0.0153  -0.0088 770 LYS A C   
695  O O   . LYS A 89  ? 0.1667 0.1780 0.2349 0.0138  0.0203  -0.0084 770 LYS A O   
696  C CB  . LYS A 89  ? 0.2248 0.2110 0.2585 -0.0017 0.0183  -0.0106 770 LYS A CB  
697  C CG  . LYS A 89  ? 0.2991 0.2736 0.3254 0.0009  0.0254  -0.0110 770 LYS A CG  
698  C CD  . LYS A 89  ? 0.3622 0.3359 0.3947 0.0057  0.0344  -0.0111 770 LYS A CD  
699  C CE  . LYS A 89  ? 0.5018 0.4639 0.5279 0.0095  0.0420  -0.0110 770 LYS A CE  
700  N NZ  . LYS A 89  ? 0.4236 0.3851 0.4568 0.0149  0.0516  -0.0107 770 LYS A NZ  
701  N N   . ASP A 90  ? 0.1542 0.1639 0.2119 0.0072  0.0094  -0.0083 771 ASP A N   
702  C CA  . ASP A 90  ? 0.1214 0.1340 0.1833 0.0119  0.0086  -0.0071 771 ASP A CA  
703  C C   . ASP A 90  ? 0.1345 0.1629 0.2109 0.0152  0.0031  -0.0062 771 ASP A C   
704  O O   . ASP A 90  ? 0.1302 0.1616 0.2094 0.0188  0.0012  -0.0050 771 ASP A O   
705  C CB  . ASP A 90  ? 0.1910 0.1948 0.2412 0.0084  0.0061  -0.0071 771 ASP A CB  
706  C CG  . ASP A 90  ? 0.2308 0.2175 0.2653 0.0051  0.0119  -0.0082 771 ASP A CG  
707  O OD1 . ASP A 90  ? 0.3545 0.3349 0.3879 0.0088  0.0193  -0.0084 771 ASP A OD1 
708  O OD2 . ASP A 90  ? 0.2929 0.2727 0.3164 -0.0012 0.0090  -0.0089 771 ASP A OD2 
709  N N   . TYR A 91  ? 0.1158 0.1533 0.2003 0.0138  0.0008  -0.0068 772 TYR A N   
710  C CA  . TYR A 91  ? 0.1172 0.1689 0.2148 0.0165  -0.0038 -0.0064 772 TYR A CA  
711  C C   . TYR A 91  ? 0.1512 0.2088 0.2571 0.0231  -0.0025 -0.0052 772 TYR A C   
712  O O   . TYR A 91  ? 0.1049 0.1695 0.2150 0.0253  -0.0075 -0.0043 772 TYR A O   
713  C CB  . TYR A 91  ? 0.1347 0.1936 0.2401 0.0144  -0.0039 -0.0076 772 TYR A CB  
714  C CG  . TYR A 91  ? 0.0822 0.1553 0.2014 0.0170  -0.0075 -0.0077 772 TYR A CG  
715  C CD1 . TYR A 91  ? 0.1331 0.2120 0.2541 0.0156  -0.0138 -0.0079 772 TYR A CD1 
716  C CD2 . TYR A 91  ? 0.0761 0.1568 0.2064 0.0206  -0.0044 -0.0076 772 TYR A CD2 
717  C CE1 . TYR A 91  ? 0.0894 0.1802 0.2212 0.0173  -0.0173 -0.0083 772 TYR A CE1 
718  C CE2 . TYR A 91  ? 0.1048 0.1993 0.2475 0.0223  -0.0085 -0.0077 772 TYR A CE2 
719  C CZ  . TYR A 91  ? 0.1919 0.2908 0.3344 0.0203  -0.0150 -0.0083 772 TYR A CZ  
720  O OH  . TYR A 91  ? 0.1510 0.2589 0.2974 0.0206  -0.0183 -0.0080 772 TYR A OH  
721  N N   . PRO A 92  ? 0.1174 0.1727 0.2259 0.0267  0.0039  -0.0047 773 PRO A N   
722  C CA  . PRO A 92  ? 0.1182 0.1812 0.2362 0.0338  0.0044  -0.0027 773 PRO A CA  
723  C C   . PRO A 92  ? 0.1358 0.1924 0.2465 0.0371  0.0035  -0.0010 773 PRO A C   
724  O O   . PRO A 92  ? 0.1547 0.2183 0.2726 0.0431  0.0023  0.0011  773 PRO A O   
725  C CB  . PRO A 92  ? 0.1751 0.2352 0.2966 0.0368  0.0129  -0.0024 773 PRO A CB  
726  C CG  . PRO A 92  ? 0.1027 0.1581 0.2203 0.0310  0.0156  -0.0045 773 PRO A CG  
727  C CD  . PRO A 92  ? 0.1021 0.1497 0.2069 0.0251  0.0111  -0.0056 773 PRO A CD  
728  N N   . LYS A 93  ? 0.1040 0.1477 0.2007 0.0331  0.0040  -0.0016 774 LYS A N   
729  C CA  . LYS A 93  ? 0.2334 0.2687 0.3220 0.0357  0.0048  -0.0001 774 LYS A CA  
730  C C   . LYS A 93  ? 0.2151 0.2574 0.3060 0.0365  -0.0022 0.0009  774 LYS A C   
731  O O   . LYS A 93  ? 0.1384 0.1760 0.2251 0.0403  -0.0016 0.0027  774 LYS A O   
732  C CB  . LYS A 93  ? 0.1355 0.1545 0.2082 0.0302  0.0078  -0.0015 774 LYS A CB  
733  C CG  . LYS A 93  ? 0.2461 0.2539 0.3123 0.0294  0.0159  -0.0025 774 LYS A CG  
734  C CD  . LYS A 93  ? 0.3274 0.3286 0.3931 0.0365  0.0231  -0.0007 774 LYS A CD  
735  C CE  . LYS A 93  ? 0.3611 0.3510 0.4208 0.0362  0.0322  -0.0017 774 LYS A CE  
736  N NZ  . LYS A 93  ? 0.3804 0.3815 0.4529 0.0376  0.0335  -0.0019 774 LYS A NZ  
737  N N   . GLY A 94  ? 0.1483 0.2003 0.2447 0.0333  -0.0082 -0.0002 775 GLY A N   
738  C CA  . GLY A 94  ? 0.1417 0.1995 0.2395 0.0342  -0.0141 0.0006  775 GLY A CA  
739  C C   . GLY A 94  ? 0.1260 0.1895 0.2258 0.0290  -0.0191 -0.0010 775 GLY A C   
740  O O   . GLY A 94  ? 0.0871 0.1487 0.1855 0.0243  -0.0183 -0.0025 775 GLY A O   
741  N N   . PHE A 95  ? 0.0738 0.1434 0.1760 0.0302  -0.0239 -0.0004 776 PHE A N   
742  C CA  . PHE A 95  ? 0.0755 0.1504 0.1798 0.0263  -0.0283 -0.0017 776 PHE A CA  
743  C C   . PHE A 95  ? 0.1392 0.2072 0.2362 0.0211  -0.0282 -0.0020 776 PHE A C   
744  O O   . PHE A 95  ? 0.0647 0.1361 0.1637 0.0178  -0.0306 -0.0028 776 PHE A O   
745  C CB  . PHE A 95  ? 0.0641 0.1449 0.1704 0.0290  -0.0327 -0.0010 776 PHE A CB  
746  C CG  . PHE A 95  ? 0.1549 0.2439 0.2653 0.0306  -0.0333 -0.0006 776 PHE A CG  
747  C CD1 . PHE A 95  ? 0.2117 0.3046 0.3230 0.0262  -0.0335 -0.0019 776 PHE A CD1 
748  C CD2 . PHE A 95  ? 0.2827 0.3747 0.3950 0.0360  -0.0334 0.0014  776 PHE A CD2 
749  C CE1 . PHE A 95  ? 0.1816 0.2817 0.2964 0.0265  -0.0341 -0.0014 776 PHE A CE1 
750  C CE2 . PHE A 95  ? 0.2300 0.3303 0.3460 0.0364  -0.0342 0.0024  776 PHE A CE2 
751  C CZ  . PHE A 95  ? 0.2819 0.3864 0.3995 0.0314  -0.0348 0.0008  776 PHE A CZ  
752  N N   . ILE A 96  ? 0.0763 0.1346 0.1650 0.0203  -0.0255 -0.0012 777 ILE A N   
753  C CA  . ILE A 96  ? 0.0981 0.1511 0.1808 0.0148  -0.0259 -0.0014 777 ILE A CA  
754  C C   . ILE A 96  ? 0.1009 0.1545 0.1844 0.0110  -0.0257 -0.0026 777 ILE A C   
755  O O   . ILE A 96  ? 0.0800 0.1338 0.1619 0.0068  -0.0279 -0.0024 777 ILE A O   
756  C CB  . ILE A 96  ? 0.0844 0.1262 0.1576 0.0137  -0.0227 -0.0009 777 ILE A CB  
757  C CG1 . ILE A 96  ? 0.1320 0.1699 0.1997 0.0073  -0.0241 -0.0010 777 ILE A CG1 
758  C CG2 . ILE A 96  ? 0.0922 0.1273 0.1620 0.0151  -0.0177 -0.0014 777 ILE A CG2 
759  C CD1 . ILE A 96  ? 0.1272 0.1536 0.1849 0.0047  -0.0210 -0.0010 777 ILE A CD1 
760  N N   . TYR A 97  ? 0.0887 0.1428 0.1750 0.0126  -0.0228 -0.0034 778 TYR A N   
761  C CA  . TYR A 97  ? 0.0749 0.1279 0.1607 0.0092  -0.0215 -0.0044 778 TYR A CA  
762  C C   . TYR A 97  ? 0.0673 0.1297 0.1624 0.0096  -0.0232 -0.0052 778 TYR A C   
763  O O   . TYR A 97  ? 0.0935 0.1548 0.1885 0.0073  -0.0215 -0.0059 778 TYR A O   
764  C CB  . TYR A 97  ? 0.0837 0.1291 0.1651 0.0098  -0.0158 -0.0049 778 TYR A CB  
765  C CG  . TYR A 97  ? 0.1371 0.1711 0.2076 0.0087  -0.0134 -0.0046 778 TYR A CG  
766  C CD1 . TYR A 97  ? 0.1696 0.1977 0.2315 0.0031  -0.0154 -0.0046 778 TYR A CD1 
767  C CD2 . TYR A 97  ? 0.1514 0.1807 0.2206 0.0131  -0.0092 -0.0041 778 TYR A CD2 
768  C CE1 . TYR A 97  ? 0.2214 0.2388 0.2729 0.0010  -0.0132 -0.0047 778 TYR A CE1 
769  C CE2 . TYR A 97  ? 0.1583 0.1755 0.2164 0.0117  -0.0063 -0.0040 778 TYR A CE2 
770  C CZ  . TYR A 97  ? 0.2045 0.2156 0.2536 0.0051  -0.0083 -0.0046 778 TYR A CZ  
771  O OH  . TYR A 97  ? 0.2912 0.2899 0.3290 0.0028  -0.0054 -0.0049 778 TYR A OH  
772  N N   . ASP A 98  ? 0.0614 0.1318 0.1633 0.0123  -0.0261 -0.0051 779 ASP A N   
773  C CA  . ASP A 98  ? 0.0557 0.1343 0.1659 0.0121  -0.0276 -0.0063 779 ASP A CA  
774  C C   . ASP A 98  ? 0.0520 0.1310 0.1607 0.0089  -0.0305 -0.0062 779 ASP A C   
775  O O   . ASP A 98  ? 0.0512 0.1312 0.1565 0.0092  -0.0318 -0.0056 779 ASP A O   
776  C CB  . ASP A 98  ? 0.0538 0.1397 0.1695 0.0159  -0.0293 -0.0063 779 ASP A CB  
777  C CG  . ASP A 98  ? 0.1012 0.1919 0.2187 0.0141  -0.0288 -0.0070 779 ASP A CG  
778  O OD1 . ASP A 98  ? 0.0520 0.1423 0.1716 0.0111  -0.0275 -0.0082 779 ASP A OD1 
779  O OD2 . ASP A 98  ? 0.1175 0.2124 0.2348 0.0156  -0.0300 -0.0063 779 ASP A OD2 
780  N N   . LEU A 99  ? 0.0541 0.1285 0.1587 0.0056  -0.0292 -0.0060 780 LEU A N   
781  C CA  . LEU A 99  ? 0.0523 0.1259 0.1546 0.0031  -0.0316 -0.0049 780 LEU A CA  
782  C C   . LEU A 99  ? 0.0549 0.1254 0.1550 0.0003  -0.0300 -0.0048 780 LEU A C   
783  O O   . LEU A 99  ? 0.0606 0.1255 0.1556 -0.0010 -0.0275 -0.0049 780 LEU A O   
784  C CB  . LEU A 99  ? 0.0548 0.1242 0.1510 0.0022  -0.0330 -0.0032 780 LEU A CB  
785  C CG  . LEU A 99  ? 0.0540 0.1233 0.1485 -0.0004 -0.0353 -0.0014 780 LEU A CG  
786  C CD1 . LEU A 99  ? 0.0531 0.1253 0.1483 0.0010  -0.0350 -0.0012 780 LEU A CD1 
787  C CD2 . LEU A 99  ? 0.0585 0.1249 0.1483 -0.0021 -0.0367 0.0001  780 LEU A CD2 
788  N N   . ALA A 100 ? 0.0521 0.1250 0.1551 -0.0006 -0.0310 -0.0047 781 ALA A N   
789  C CA  . ALA A 100 ? 0.0557 0.1249 0.1559 -0.0029 -0.0294 -0.0042 781 ALA A CA  
790  C C   . ALA A 100 ? 0.1103 0.1803 0.2110 -0.0034 -0.0313 -0.0024 781 ALA A C   
791  O O   . ALA A 100 ? 0.0702 0.1436 0.1742 -0.0020 -0.0325 -0.0025 781 ALA A O   
792  C CB  . ALA A 100 ? 0.0774 0.1479 0.1822 -0.0031 -0.0259 -0.0063 781 ALA A CB  
793  N N   . VAL A 101 ? 0.0735 0.1391 0.1693 -0.0051 -0.0309 -0.0005 782 VAL A N   
794  C CA  . VAL A 101 ? 0.0906 0.1561 0.1864 -0.0050 -0.0322 0.0020  782 VAL A CA  
795  C C   . VAL A 101 ? 0.0955 0.1565 0.1890 -0.0061 -0.0292 0.0021  782 VAL A C   
796  O O   . VAL A 101 ? 0.1192 0.1755 0.2074 -0.0077 -0.0274 0.0019  782 VAL A O   
797  C CB  . VAL A 101 ? 0.0612 0.1266 0.1531 -0.0057 -0.0358 0.0054  782 VAL A CB  
798  C CG1 . VAL A 101 ? 0.0722 0.1380 0.1649 -0.0048 -0.0368 0.0087  782 VAL A CG1 
799  C CG2 . VAL A 101 ? 0.1200 0.1895 0.2147 -0.0049 -0.0379 0.0053  782 VAL A CG2 
800  N N   . ILE A 102 ? 0.0825 0.1437 0.1791 -0.0052 -0.0281 0.0024  783 ILE A N   
801  C CA  . ILE A 102 ? 0.1254 0.1813 0.2198 -0.0063 -0.0245 0.0025  783 ILE A CA  
802  C C   . ILE A 102 ? 0.1149 0.1680 0.2060 -0.0050 -0.0256 0.0068  783 ILE A C   
803  O O   . ILE A 102 ? 0.0708 0.1266 0.1654 -0.0029 -0.0270 0.0083  783 ILE A O   
804  C CB  . ILE A 102 ? 0.0675 0.1249 0.1678 -0.0067 -0.0215 -0.0009 783 ILE A CB  
805  C CG1 . ILE A 102 ? 0.0966 0.1585 0.2014 -0.0075 -0.0210 -0.0046 783 ILE A CG1 
806  C CG2 . ILE A 102 ? 0.0746 0.1255 0.1722 -0.0083 -0.0171 -0.0009 783 ILE A CG2 
807  C CD1 . ILE A 102 ? 0.0889 0.1561 0.2007 -0.0077 -0.0211 -0.0077 783 ILE A CD1 
808  N N   . THR A 103 ? 0.0815 0.1287 0.1653 -0.0060 -0.0249 0.0090  784 THR A N   
809  C CA  . THR A 103 ? 0.1176 0.1618 0.1977 -0.0044 -0.0260 0.0138  784 THR A CA  
810  C C   . THR A 103 ? 0.1382 0.1755 0.2167 -0.0043 -0.0208 0.0135  784 THR A C   
811  O O   . THR A 103 ? 0.1459 0.1773 0.2192 -0.0064 -0.0174 0.0124  784 THR A O   
812  C CB  . THR A 103 ? 0.1772 0.2190 0.2489 -0.0057 -0.0293 0.0169  784 THR A CB  
813  O OG1 . THR A 103 ? 0.1289 0.1645 0.1941 -0.0084 -0.0261 0.0145  784 THR A OG1 
814  C CG2 . THR A 103 ? 0.0926 0.1410 0.1661 -0.0061 -0.0345 0.0177  784 THR A CG2 
815  N N   . LEU A 104 ? 0.1019 0.1393 0.1844 -0.0021 -0.0194 0.0145  785 LEU A N   
816  C CA  . LEU A 104 ? 0.1254 0.1552 0.2062 -0.0020 -0.0140 0.0142  785 LEU A CA  
817  C C   . LEU A 104 ? 0.1457 0.1693 0.2196 0.0003  -0.0139 0.0200  785 LEU A C   
818  O O   . LEU A 104 ? 0.1719 0.1989 0.2439 0.0021  -0.0188 0.0244  785 LEU A O   
819  C CB  . LEU A 104 ? 0.1099 0.1412 0.1969 -0.0009 -0.0122 0.0123  785 LEU A CB  
820  C CG  . LEU A 104 ? 0.0873 0.1254 0.1804 -0.0030 -0.0133 0.0070  785 LEU A CG  
821  C CD1 . LEU A 104 ? 0.1813 0.2208 0.2787 -0.0018 -0.0126 0.0054  785 LEU A CD1 
822  C CD2 . LEU A 104 ? 0.1502 0.1866 0.2437 -0.0068 -0.0099 0.0026  785 LEU A CD2 
823  N N   . PRO A 105 ? 0.1973 0.2116 0.2670 0.0003  -0.0084 0.0204  786 PRO A N   
824  C CA  . PRO A 105 ? 0.2523 0.2601 0.3147 0.0033  -0.0082 0.0266  786 PRO A CA  
825  C C   . PRO A 105 ? 0.2512 0.2634 0.3176 0.0083  -0.0114 0.0317  786 PRO A C   
826  O O   . PRO A 105 ? 0.2035 0.2201 0.2774 0.0095  -0.0110 0.0301  786 PRO A O   
827  C CB  . PRO A 105 ? 0.3177 0.3143 0.3765 0.0023  -0.0004 0.0252  786 PRO A CB  
828  C CG  . PRO A 105 ? 0.2604 0.2582 0.3224 -0.0028 0.0024  0.0184  786 PRO A CG  
829  C CD  . PRO A 105 ? 0.2085 0.2179 0.2791 -0.0031 -0.0023 0.0154  786 PRO A CD  
830  N N   . GLN A 106 ? 0.2783 0.2895 0.3396 0.0112  -0.0145 0.0382  787 GLN A N   
831  C CA  . GLN A 106 ? 0.1757 0.1925 0.2422 0.0164  -0.0176 0.0440  787 GLN A CA  
832  C C   . GLN A 106 ? 0.2403 0.2506 0.3094 0.0202  -0.0112 0.0450  787 GLN A C   
833  O O   . GLN A 106 ? 0.2834 0.2987 0.3592 0.0246  -0.0120 0.0483  787 GLN A O   
834  C CB  . GLN A 106 ? 0.3814 0.3985 0.4416 0.0187  -0.0226 0.0511  787 GLN A CB  
835  C CG  . GLN A 106 ? 0.5283 0.5507 0.5843 0.0145  -0.0292 0.0504  787 GLN A CG  
836  C CD  . GLN A 106 ? 0.5114 0.5467 0.5766 0.0136  -0.0348 0.0494  787 GLN A CD  
837  O OE1 . GLN A 106 ? 0.4880 0.5297 0.5628 0.0172  -0.0350 0.0514  787 GLN A OE1 
838  N NE2 . GLN A 106 ? 0.6422 0.6802 0.7040 0.0089  -0.0386 0.0464  787 GLN A NE2 
839  N N   . SER A 107 ? 0.2056 0.2045 0.2694 0.0184  -0.0043 0.0420  788 SER A N   
840  C CA  . SER A 107 ? 0.2684 0.2587 0.3329 0.0208  0.0029  0.0418  788 SER A CA  
841  C C   . SER A 107 ? 0.2012 0.1955 0.2732 0.0191  0.0045  0.0361  788 SER A C   
842  O O   . SER A 107 ? 0.1767 0.1638 0.2490 0.0209  0.0103  0.0355  788 SER A O   
843  C CB  . SER A 107 ? 0.2723 0.2491 0.3284 0.0180  0.0098  0.0397  788 SER A CB  
844  O OG  . SER A 107 ? 0.2801 0.2587 0.3362 0.0115  0.0099  0.0330  788 SER A OG  
845  N N   . THR A 108 ? 0.2098 0.2138 0.2865 0.0156  -0.0001 0.0318  789 THR A N   
846  C CA  . THR A 108 ? 0.1820 0.1906 0.2651 0.0143  0.0002  0.0270  789 THR A CA  
847  C C   . THR A 108 ? 0.2016 0.2178 0.2906 0.0191  -0.0031 0.0314  789 THR A C   
848  O O   . THR A 108 ? 0.1622 0.1873 0.2536 0.0200  -0.0092 0.0346  789 THR A O   
849  C CB  . THR A 108 ? 0.1969 0.2123 0.2822 0.0091  -0.0031 0.0212  789 THR A CB  
850  O OG1 . THR A 108 ? 0.2633 0.2728 0.3443 0.0050  0.0001  0.0181  789 THR A OG1 
851  C CG2 . THR A 108 ? 0.1460 0.1649 0.2364 0.0077  -0.0026 0.0162  789 THR A CG2 
852  N N   . ARG A 109 ? 0.1367 0.1492 0.2280 0.0220  0.0012  0.0315  790 ARG A N   
853  C CA  . ARG A 109 ? 0.1378 0.1561 0.2351 0.0275  -0.0001 0.0366  790 ARG A CA  
854  C C   . ARG A 109 ? 0.1413 0.1604 0.2421 0.0272  0.0022  0.0326  790 ARG A C   
855  O O   . ARG A 109 ? 0.1220 0.1373 0.2245 0.0315  0.0067  0.0349  790 ARG A O   
856  C CB  . ARG A 109 ? 0.1326 0.1435 0.2280 0.0336  0.0042  0.0433  790 ARG A CB  
857  C CG  . ARG A 109 ? 0.1397 0.1474 0.2293 0.0342  0.0026  0.0477  790 ARG A CG  
858  C CD  . ARG A 109 ? 0.1683 0.1884 0.2611 0.0347  -0.0061 0.0522  790 ARG A CD  
859  N NE  . ARG A 109 ? 0.2388 0.2553 0.3254 0.0369  -0.0078 0.0580  790 ARG A NE  
860  C CZ  . ARG A 109 ? 0.1728 0.1885 0.2605 0.0436  -0.0072 0.0660  790 ARG A CZ  
861  N NH1 . ARG A 109 ? 0.1522 0.1700 0.2476 0.0491  -0.0041 0.0691  790 ARG A NH1 
862  N NH2 . ARG A 109 ? 0.1713 0.1836 0.2518 0.0451  -0.0094 0.0712  790 ARG A NH2 
863  N N   . ARG A 110 ? 0.1085 0.1322 0.2099 0.0222  -0.0007 0.0265  791 ARG A N   
864  C CA  . ARG A 110 ? 0.1064 0.1294 0.2088 0.0209  0.0013  0.0218  791 ARG A CA  
865  C C   . ARG A 110 ? 0.1530 0.1838 0.2615 0.0245  -0.0008 0.0248  791 ARG A C   
866  O O   . ARG A 110 ? 0.1072 0.1476 0.2204 0.0257  -0.0059 0.0285  791 ARG A O   
867  C CB  . ARG A 110 ? 0.1666 0.1928 0.2679 0.0149  -0.0016 0.0150  791 ARG A CB  
868  C CG  . ARG A 110 ? 0.1480 0.1665 0.2445 0.0104  0.0016  0.0105  791 ARG A CG  
869  C CD  . ARG A 110 ? 0.1698 0.1784 0.2625 0.0094  0.0076  0.0072  791 ARG A CD  
870  N NE  . ARG A 110 ? 0.1116 0.1233 0.2052 0.0086  0.0063  0.0037  791 ARG A NE  
871  C CZ  . ARG A 110 ? 0.1574 0.1609 0.2467 0.0076  0.0108  0.0005  791 ARG A CZ  
872  N NH1 . ARG A 110 ? 0.1738 0.1649 0.2577 0.0070  0.0173  -0.0001 791 ARG A NH1 
873  N NH2 . ARG A 110 ? 0.1877 0.1941 0.2768 0.0071  0.0091  -0.0022 791 ARG A NH2 
874  N N   . GLN A 111 ? 0.1044 0.1308 0.2123 0.0257  0.0036  0.0227  792 GLN A N   
875  C CA  . GLN A 111 ? 0.0987 0.1322 0.2116 0.0276  0.0019  0.0237  792 GLN A CA  
876  C C   . GLN A 111 ? 0.1117 0.1532 0.2253 0.0232  -0.0042 0.0197  792 GLN A C   
877  O O   . GLN A 111 ? 0.0875 0.1273 0.1972 0.0187  -0.0056 0.0148  792 GLN A O   
878  C CB  . GLN A 111 ? 0.1062 0.1312 0.2159 0.0290  0.0083  0.0214  792 GLN A CB  
879  C CG  . GLN A 111 ? 0.1949 0.2140 0.2974 0.0236  0.0089  0.0137  792 GLN A CG  
880  C CD  . GLN A 111 ? 0.2254 0.2373 0.3237 0.0246  0.0140  0.0114  792 GLN A CD  
881  O OE1 . GLN A 111 ? 0.2293 0.2463 0.3306 0.0265  0.0130  0.0125  792 GLN A OE1 
882  N NE2 . GLN A 111 ? 0.1279 0.1269 0.2184 0.0229  0.0198  0.0080  792 GLN A NE2 
883  N N   . HIS A 112 ? 0.0878 0.1380 0.2068 0.0246  -0.0074 0.0221  793 HIS A N   
884  C CA  . HIS A 112 ? 0.0735 0.1307 0.1929 0.0210  -0.0130 0.0192  793 HIS A CA  
885  C C   . HIS A 112 ? 0.0694 0.1323 0.1928 0.0224  -0.0139 0.0203  793 HIS A C   
886  O O   . HIS A 112 ? 0.0718 0.1357 0.1996 0.0262  -0.0110 0.0243  793 HIS A O   
887  C CB  . HIS A 112 ? 0.0695 0.1323 0.1903 0.0195  -0.0180 0.0216  793 HIS A CB  
888  C CG  . HIS A 112 ? 0.0996 0.1687 0.2262 0.0226  -0.0199 0.0283  793 HIS A CG  
889  N ND1 . HIS A 112 ? 0.0982 0.1749 0.2272 0.0218  -0.0234 0.0295  793 HIS A ND1 
890  C CD2 . HIS A 112 ? 0.1157 0.1841 0.2443 0.0261  -0.0186 0.0337  793 HIS A CD2 
891  C CE1 . HIS A 112 ? 0.0726 0.1521 0.2025 0.0236  -0.0242 0.0342  793 HIS A CE1 
892  N NE2 . HIS A 112 ? 0.0755 0.1523 0.2085 0.0271  -0.0221 0.0380  793 HIS A NE2 
893  N N   . ALA A 113 ? 0.1136 0.1802 0.2356 0.0194  -0.0176 0.0170  794 ALA A N   
894  C CA  . ALA A 113 ? 0.0600 0.1318 0.1850 0.0199  -0.0189 0.0179  794 ALA A CA  
895  C C   . ALA A 113 ? 0.1443 0.2216 0.2689 0.0184  -0.0226 0.0204  794 ALA A C   
896  O O   . ALA A 113 ? 0.1023 0.1800 0.2246 0.0167  -0.0251 0.0208  794 ALA A O   
897  C CB  . ALA A 113 ? 0.0964 0.1666 0.2163 0.0174  -0.0202 0.0126  794 ALA A CB  
898  N N   . ASN A 114 ? 0.0891 0.1690 0.2133 0.0185  -0.0224 0.0212  795 ASN A N   
899  C CA  . ASN A 114 ? 0.0837 0.1670 0.2050 0.0161  -0.0252 0.0223  795 ASN A CA  
900  C C   . ASN A 114 ? 0.0547 0.1375 0.1703 0.0130  -0.0273 0.0187  795 ASN A C   
901  O O   . ASN A 114 ? 0.0569 0.1387 0.1722 0.0133  -0.0263 0.0168  795 ASN A O   
902  C CB  . ASN A 114 ? 0.1136 0.2006 0.2396 0.0177  -0.0235 0.0256  795 ASN A CB  
903  C CG  . ASN A 114 ? 0.1488 0.2365 0.2807 0.0216  -0.0208 0.0298  795 ASN A CG  
904  O OD1 . ASN A 114 ? 0.0783 0.1650 0.2102 0.0225  -0.0216 0.0315  795 ASN A OD1 
905  N ND2 . ASN A 114 ? 0.2471 0.3361 0.3843 0.0243  -0.0169 0.0321  795 ASN A ND2 
906  N N   . LEU A 115 ? 0.0582 0.1413 0.1696 0.0102  -0.0301 0.0181  796 LEU A N   
907  C CA  . LEU A 115 ? 0.0882 0.1712 0.1954 0.0076  -0.0316 0.0159  796 LEU A CA  
908  C C   . LEU A 115 ? 0.0852 0.1714 0.1954 0.0072  -0.0313 0.0176  796 LEU A C   
909  O O   . LEU A 115 ? 0.0852 0.1748 0.1995 0.0076  -0.0314 0.0207  796 LEU A O   
910  C CB  . LEU A 115 ? 0.1095 0.1921 0.2129 0.0048  -0.0343 0.0155  796 LEU A CB  
911  C CG  . LEU A 115 ? 0.0586 0.1397 0.1576 0.0022  -0.0356 0.0132  796 LEU A CG  
912  C CD1 . LEU A 115 ? 0.1103 0.1887 0.2071 0.0031  -0.0345 0.0101  796 LEU A CD1 
913  C CD2 . LEU A 115 ? 0.0565 0.1375 0.1531 -0.0006 -0.0384 0.0139  796 LEU A CD2 
914  N N   . VAL A 116 ? 0.0532 0.1385 0.1622 0.0066  -0.0308 0.0160  797 VAL A N   
915  C CA  . VAL A 116 ? 0.0539 0.1423 0.1670 0.0060  -0.0301 0.0178  797 VAL A CA  
916  C C   . VAL A 116 ? 0.0560 0.1477 0.1697 0.0027  -0.0326 0.0193  797 VAL A C   
917  O O   . VAL A 116 ? 0.0912 0.1815 0.2004 0.0003  -0.0351 0.0180  797 VAL A O   
918  C CB  . VAL A 116 ? 0.1562 0.2428 0.2681 0.0057  -0.0296 0.0161  797 VAL A CB  
919  C CG1 . VAL A 116 ? 0.0744 0.1588 0.1810 0.0030  -0.0321 0.0141  797 VAL A CG1 
920  C CG2 . VAL A 116 ? 0.1464 0.2363 0.2644 0.0054  -0.0280 0.0185  797 VAL A CG2 
921  N N   . GLU A 117 ? 0.0577 0.1542 0.1777 0.0027  -0.0320 0.0222  798 GLU A N   
922  C CA  . GLU A 117 ? 0.1554 0.2563 0.2771 -0.0007 -0.0349 0.0239  798 GLU A CA  
923  C C   . GLU A 117 ? 0.1229 0.2234 0.2428 -0.0051 -0.0364 0.0225  798 GLU A C   
924  O O   . GLU A 117 ? 0.1719 0.2722 0.2882 -0.0087 -0.0396 0.0219  798 GLU A O   
925  C CB  . GLU A 117 ? 0.2833 0.3904 0.4134 0.0007  -0.0337 0.0276  798 GLU A CB  
926  C CG  . GLU A 117 ? 0.4739 0.5867 0.6066 -0.0020 -0.0373 0.0298  798 GLU A CG  
927  C CD  . GLU A 117 ? 0.6121 0.7320 0.7545 0.0000  -0.0359 0.0339  798 GLU A CD  
928  O OE1 . GLU A 117 ? 0.5694 0.6891 0.7163 0.0035  -0.0316 0.0350  798 GLU A OE1 
929  O OE2 . GLU A 117 ? 0.5056 0.6315 0.6514 -0.0018 -0.0392 0.0362  798 GLU A OE2 
930  N N   . ASN A 118 ? 0.1256 0.2259 0.2482 -0.0049 -0.0341 0.0224  799 ASN A N   
931  C CA  . ASN A 118 ? 0.1642 0.2644 0.2867 -0.0092 -0.0351 0.0218  799 ASN A CA  
932  C C   . ASN A 118 ? 0.1182 0.2128 0.2369 -0.0079 -0.0341 0.0197  799 ASN A C   
933  O O   . ASN A 118 ? 0.1822 0.2752 0.3016 -0.0038 -0.0317 0.0194  799 ASN A O   
934  C CB  . ASN A 118 ? 0.1481 0.2538 0.2791 -0.0107 -0.0333 0.0243  799 ASN A CB  
935  C CG  . ASN A 118 ? 0.1846 0.2972 0.3209 -0.0116 -0.0345 0.0268  799 ASN A CG  
936  O OD1 . ASN A 118 ? 0.2800 0.3964 0.4228 -0.0085 -0.0319 0.0292  799 ASN A OD1 
937  N ND2 . ASN A 118 ? 0.1484 0.2625 0.2821 -0.0159 -0.0386 0.0264  799 ASN A ND2 
938  N N   . TYR A 119 ? 0.0721 0.1639 0.1872 -0.0114 -0.0363 0.0184  800 TYR A N   
939  C CA  . TYR A 119 ? 0.1794 0.2667 0.2924 -0.0099 -0.0358 0.0169  800 TYR A CA  
940  C C   . TYR A 119 ? 0.1727 0.2601 0.2900 -0.0089 -0.0329 0.0183  800 TYR A C   
941  O O   . TYR A 119 ? 0.1116 0.2013 0.2326 -0.0126 -0.0317 0.0198  800 TYR A O   
942  C CB  . TYR A 119 ? 0.0914 0.1750 0.2003 -0.0142 -0.0385 0.0157  800 TYR A CB  
943  C CG  . TYR A 119 ? 0.0653 0.1396 0.1658 -0.0117 -0.0353 0.0134  800 TYR A CG  
944  C CD1 . TYR A 119 ? 0.0657 0.1367 0.1622 -0.0072 -0.0352 0.0115  800 TYR A CD1 
945  C CD2 . TYR A 119 ? 0.1021 0.1710 0.1987 -0.0140 -0.0326 0.0133  800 TYR A CD2 
946  C CE1 . TYR A 119 ? 0.0796 0.1433 0.1691 -0.0043 -0.0329 0.0101  800 TYR A CE1 
947  C CE2 . TYR A 119 ? 0.0883 0.1481 0.1766 -0.0109 -0.0296 0.0118  800 TYR A CE2 
948  C CZ  . TYR A 119 ? 0.0742 0.1319 0.1592 -0.0058 -0.0301 0.0104  800 TYR A CZ  
949  O OH  . TYR A 119 ? 0.0795 0.1294 0.1571 -0.0022 -0.0278 0.0095  800 TYR A OH  
950  N N   . SER A 120 ? 0.1422 0.2248 0.2552 -0.0040 -0.0305 0.0169  801 SER A N   
951  C CA  A SER A 120 ? 0.1075 0.1851 0.2173 -0.0022 -0.0262 0.0170  801 SER A CA  
952  C CA  B SER A 120 ? 0.1085 0.1861 0.2183 -0.0022 -0.0262 0.0170  801 SER A CA  
953  C C   . SER A 120 ? 0.1020 0.1711 0.2015 0.0009  -0.0258 0.0145  801 SER A C   
954  O O   . SER A 120 ? 0.1269 0.1958 0.2244 0.0043  -0.0272 0.0130  801 SER A O   
955  C CB  A SER A 120 ? 0.1608 0.2413 0.2757 0.0012  -0.0233 0.0185  801 SER A CB  
956  C CB  B SER A 120 ? 0.1608 0.2413 0.2756 0.0012  -0.0233 0.0185  801 SER A CB  
957  O OG  A SER A 120 ? 0.0994 0.1734 0.2089 0.0031  -0.0189 0.0184  801 SER A OG  
958  O OG  B SER A 120 ? 0.1044 0.1929 0.2298 -0.0011 -0.0225 0.0216  801 SER A OG  
959  N N   . LYS A 121 ? 0.0731 0.1355 0.1663 -0.0003 -0.0237 0.0142  802 LYS A N   
960  C CA  . LYS A 121 ? 0.0808 0.1352 0.1645 0.0033  -0.0232 0.0127  802 LYS A CA  
961  C C   . LYS A 121 ? 0.1124 0.1654 0.1932 0.0084  -0.0221 0.0125  802 LYS A C   
962  O O   . LYS A 121 ? 0.1409 0.1935 0.2227 0.0089  -0.0191 0.0138  802 LYS A O   
963  C CB  . LYS A 121 ? 0.1422 0.1885 0.2195 0.0013  -0.0199 0.0131  802 LYS A CB  
964  C CG  . LYS A 121 ? 0.2060 0.2430 0.2730 0.0060  -0.0183 0.0126  802 LYS A CG  
965  C CD  . LYS A 121 ? 0.2275 0.2624 0.2910 0.0076  -0.0205 0.0112  802 LYS A CD  
966  C CE  . LYS A 121 ? 0.2165 0.2416 0.2702 0.0118  -0.0181 0.0116  802 LYS A CE  
967  N NZ  . LYS A 121 ? 0.1531 0.1766 0.2026 0.0172  -0.0178 0.0124  802 LYS A NZ  
968  N N   . VAL A 122 ? 0.1139 0.1661 0.1910 0.0119  -0.0246 0.0108  803 VAL A N   
969  C CA  . VAL A 122 ? 0.1340 0.1841 0.2063 0.0162  -0.0246 0.0102  803 VAL A CA  
970  C C   . VAL A 122 ? 0.1206 0.1626 0.1833 0.0192  -0.0233 0.0107  803 VAL A C   
971  O O   . VAL A 122 ? 0.1153 0.1549 0.1755 0.0197  -0.0241 0.0105  803 VAL A O   
972  C CB  . VAL A 122 ? 0.1254 0.1802 0.1998 0.0179  -0.0285 0.0082  803 VAL A CB  
973  C CG1 . VAL A 122 ? 0.1554 0.2077 0.2234 0.0217  -0.0295 0.0073  803 VAL A CG1 
974  C CG2 . VAL A 122 ? 0.0759 0.1369 0.1583 0.0156  -0.0290 0.0081  803 VAL A CG2 
975  N N   . ASN A 123 ? 0.1239 0.1611 0.1806 0.0214  -0.0208 0.0115  804 ASN A N   
976  C CA  . ASN A 123 ? 0.1667 0.1952 0.2132 0.0245  -0.0190 0.0126  804 ASN A CA  
977  C C   . ASN A 123 ? 0.1950 0.2225 0.2347 0.0293  -0.0221 0.0119  804 ASN A C   
978  O O   . ASN A 123 ? 0.1391 0.1707 0.1804 0.0295  -0.0241 0.0105  804 ASN A O   
979  C CB  . ASN A 123 ? 0.1957 0.2179 0.2386 0.0234  -0.0134 0.0144  804 ASN A CB  
980  C CG  . ASN A 123 ? 0.2142 0.2364 0.2624 0.0184  -0.0104 0.0153  804 ASN A CG  
981  O OD1 . ASN A 123 ? 0.2181 0.2441 0.2712 0.0157  -0.0127 0.0146  804 ASN A OD1 
982  N ND2 . ASN A 123 ? 0.2197 0.2376 0.2667 0.0167  -0.0052 0.0169  804 ASN A ND2 
983  N N   . VAL A 124 ? 0.1280 0.1499 0.1596 0.0330  -0.0225 0.0131  805 VAL A N   
984  C CA  . VAL A 124 ? 0.1260 0.1466 0.1498 0.0376  -0.0257 0.0131  805 VAL A CA  
985  C C   . VAL A 124 ? 0.2348 0.2502 0.2517 0.0376  -0.0230 0.0133  805 VAL A C   
986  O O   . VAL A 124 ? 0.1724 0.1816 0.1870 0.0361  -0.0175 0.0147  805 VAL A O   
987  C CB  . VAL A 124 ? 0.1352 0.1498 0.1514 0.0423  -0.0259 0.0153  805 VAL A CB  
988  C CG1 . VAL A 124 ? 0.1448 0.1574 0.1514 0.0472  -0.0294 0.0161  805 VAL A CG1 
989  C CG2 . VAL A 124 ? 0.1289 0.1488 0.1521 0.0428  -0.0282 0.0149  805 VAL A CG2 
990  N N   . ASN A 125 ? 0.1376 0.1556 0.1517 0.0387  -0.0266 0.0116  806 ASN A N   
991  C CA  . ASN A 125 ? 0.1800 0.1931 0.1867 0.0386  -0.0246 0.0109  806 ASN A CA  
992  C C   . ASN A 125 ? 0.1800 0.1971 0.1954 0.0348  -0.0220 0.0094  806 ASN A C   
993  O O   . ASN A 125 ? 0.1840 0.1969 0.1940 0.0346  -0.0196 0.0086  806 ASN A O   
994  C CB  . ASN A 125 ? 0.2285 0.2300 0.2240 0.0402  -0.0191 0.0134  806 ASN A CB  
995  C CG  . ASN A 125 ? 0.3031 0.2990 0.2873 0.0450  -0.0216 0.0153  806 ASN A CG  
996  O OD1 . ASN A 125 ? 0.3204 0.3197 0.3010 0.0475  -0.0278 0.0146  806 ASN A OD1 
997  N ND2 . ASN A 125 ? 0.3589 0.3462 0.3378 0.0461  -0.0167 0.0180  806 ASN A ND2 
998  N N   . ASP A 126 ? 0.1597 0.1843 0.1876 0.0320  -0.0223 0.0091  807 ASP A N   
999  C CA  . ASP A 126 ? 0.1872 0.2168 0.2238 0.0292  -0.0210 0.0080  807 ASP A CA  
1000 C C   . ASP A 126 ? 0.1536 0.1861 0.1888 0.0294  -0.0252 0.0052  807 ASP A C   
1001 O O   . ASP A 126 ? 0.1379 0.1731 0.1709 0.0307  -0.0305 0.0040  807 ASP A O   
1002 C CB  . ASP A 126 ? 0.1342 0.1712 0.1831 0.0264  -0.0216 0.0085  807 ASP A CB  
1003 C CG  . ASP A 126 ? 0.1281 0.1634 0.1805 0.0243  -0.0169 0.0108  807 ASP A CG  
1004 O OD1 . ASP A 126 ? 0.1289 0.1573 0.1750 0.0253  -0.0125 0.0122  807 ASP A OD1 
1005 O OD2 . ASP A 126 ? 0.0957 0.1366 0.1570 0.0214  -0.0176 0.0113  807 ASP A OD2 
1006 N N   . LYS A 127 ? 0.1203 0.1522 0.1571 0.0281  -0.0225 0.0041  808 LYS A N   
1007 C CA  . LYS A 127 ? 0.2096 0.2431 0.2452 0.0272  -0.0254 0.0011  808 LYS A CA  
1008 C C   . LYS A 127 ? 0.1078 0.1487 0.1558 0.0249  -0.0258 0.0007  808 LYS A C   
1009 O O   . LYS A 127 ? 0.1522 0.1943 0.2073 0.0241  -0.0217 0.0025  808 LYS A O   
1010 C CB  . LYS A 127 ? 0.1944 0.2194 0.2207 0.0275  -0.0213 0.0001  808 LYS A CB  
1011 C CG  . LYS A 127 ? 0.2743 0.2910 0.2856 0.0296  -0.0218 0.0002  808 LYS A CG  
1012 C CD  . LYS A 127 ? 0.4143 0.4205 0.4156 0.0299  -0.0157 -0.0002 808 LYS A CD  
1013 C CE  . LYS A 127 ? 0.4216 0.4185 0.4058 0.0319  -0.0167 -0.0002 808 LYS A CE  
1014 N NZ  . LYS A 127 ? 0.3822 0.3811 0.3592 0.0313  -0.0247 -0.0031 808 LYS A NZ  
1015 N N   . LEU A 128 ? 0.0977 0.1440 0.1487 0.0239  -0.0308 -0.0015 809 LEU A N   
1016 C CA  . LEU A 128 ? 0.1117 0.1642 0.1730 0.0218  -0.0314 -0.0020 809 LEU A CA  
1017 C C   . LEU A 128 ? 0.0990 0.1508 0.1586 0.0202  -0.0321 -0.0051 809 LEU A C   
1018 O O   . LEU A 128 ? 0.1454 0.1936 0.1964 0.0202  -0.0340 -0.0073 809 LEU A O   
1019 C CB  . LEU A 128 ? 0.1014 0.1604 0.1684 0.0215  -0.0354 -0.0019 809 LEU A CB  
1020 C CG  . LEU A 128 ? 0.1188 0.1776 0.1865 0.0226  -0.0349 0.0006  809 LEU A CG  
1021 C CD1 . LEU A 128 ? 0.1010 0.1650 0.1730 0.0226  -0.0384 0.0001  809 LEU A CD1 
1022 C CD2 . LEU A 128 ? 0.1381 0.1971 0.2114 0.0211  -0.0310 0.0029  809 LEU A CD2 
1023 N N   . ASN A 129 ? 0.0846 0.1393 0.1520 0.0186  -0.0309 -0.0051 810 ASN A N   
1024 C CA  . ASN A 129 ? 0.0871 0.1406 0.1537 0.0167  -0.0309 -0.0080 810 ASN A CA  
1025 C C   . ASN A 129 ? 0.0850 0.1455 0.1596 0.0149  -0.0341 -0.0088 810 ASN A C   
1026 O O   . ASN A 129 ? 0.0771 0.1410 0.1592 0.0149  -0.0331 -0.0065 810 ASN A O   
1027 C CB  . ASN A 129 ? 0.1358 0.1839 0.2029 0.0170  -0.0249 -0.0070 810 ASN A CB  
1028 C CG  . ASN A 129 ? 0.1274 0.1667 0.1843 0.0183  -0.0212 -0.0073 810 ASN A CG  
1029 O OD1 . ASN A 129 ? 0.1551 0.1885 0.2030 0.0170  -0.0214 -0.0105 810 ASN A OD1 
1030 N ND2 . ASN A 129 ? 0.1577 0.1957 0.2154 0.0205  -0.0177 -0.0041 810 ASN A ND2 
1031 N N   . VAL A 130 ? 0.1033 0.1663 0.1763 0.0132  -0.0380 -0.0119 811 VAL A N   
1032 C CA  . VAL A 130 ? 0.0737 0.1436 0.1541 0.0116  -0.0409 -0.0128 811 VAL A CA  
1033 C C   . VAL A 130 ? 0.0771 0.1461 0.1574 0.0083  -0.0409 -0.0162 811 VAL A C   
1034 O O   . VAL A 130 ? 0.1268 0.1927 0.2002 0.0068  -0.0421 -0.0190 811 VAL A O   
1035 C CB  . VAL A 130 ? 0.0963 0.1718 0.1773 0.0129  -0.0455 -0.0128 811 VAL A CB  
1036 C CG1 . VAL A 130 ? 0.0661 0.1479 0.1547 0.0115  -0.0468 -0.0132 811 VAL A CG1 
1037 C CG2 . VAL A 130 ? 0.0716 0.1455 0.1507 0.0161  -0.0446 -0.0096 811 VAL A CG2 
1038 N N   . TYR A 131 ? 0.0719 0.1429 0.1588 0.0067  -0.0395 -0.0161 812 TYR A N   
1039 C CA  . TYR A 131 ? 0.1088 0.1777 0.1958 0.0032  -0.0383 -0.0191 812 TYR A CA  
1040 C C   . TYR A 131 ? 0.0703 0.1465 0.1646 0.0011  -0.0409 -0.0204 812 TYR A C   
1041 O O   . TYR A 131 ? 0.1064 0.1870 0.2061 0.0026  -0.0414 -0.0181 812 TYR A O   
1042 C CB  . TYR A 131 ? 0.0813 0.1442 0.1690 0.0036  -0.0330 -0.0174 812 TYR A CB  
1043 C CG  . TYR A 131 ? 0.1105 0.1657 0.1919 0.0057  -0.0291 -0.0161 812 TYR A CG  
1044 C CD1 . TYR A 131 ? 0.1061 0.1620 0.1877 0.0090  -0.0285 -0.0128 812 TYR A CD1 
1045 C CD2 . TYR A 131 ? 0.1338 0.1805 0.2094 0.0042  -0.0251 -0.0183 812 TYR A CD2 
1046 C CE1 . TYR A 131 ? 0.1309 0.1800 0.2077 0.0110  -0.0239 -0.0115 812 TYR A CE1 
1047 C CE2 . TYR A 131 ? 0.1413 0.1801 0.2111 0.0065  -0.0204 -0.0170 812 TYR A CE2 
1048 C CZ  . TYR A 131 ? 0.1718 0.2123 0.2428 0.0101  -0.0198 -0.0135 812 TYR A CZ  
1049 O OH  . TYR A 131 ? 0.1789 0.2119 0.2451 0.0124  -0.0143 -0.0121 812 TYR A OH  
1050 N N   . GLY A 132 ? 0.0748 0.1520 0.1691 -0.0028 -0.0420 -0.0241 813 GLY A N   
1051 C CA  . GLY A 132 ? 0.0873 0.1716 0.1895 -0.0051 -0.0435 -0.0254 813 GLY A CA  
1052 C C   . GLY A 132 ? 0.0832 0.1683 0.1851 -0.0103 -0.0447 -0.0299 813 GLY A C   
1053 O O   . GLY A 132 ? 0.0874 0.1656 0.1817 -0.0125 -0.0437 -0.0322 813 GLY A O   
1054 N N   . TYR A 133 ? 0.0747 0.1668 0.1831 -0.0125 -0.0458 -0.0306 814 TYR A N   
1055 C CA  . TYR A 133 ? 0.0853 0.1797 0.1955 -0.0183 -0.0468 -0.0348 814 TYR A CA  
1056 C C   . TYR A 133 ? 0.1010 0.2029 0.2116 -0.0185 -0.0498 -0.0329 814 TYR A C   
1057 O O   . TYR A 133 ? 0.1001 0.2061 0.2160 -0.0202 -0.0481 -0.0319 814 TYR A O   
1058 C CB  . TYR A 133 ? 0.0841 0.1763 0.1999 -0.0215 -0.0423 -0.0361 814 TYR A CB  
1059 C CG  . TYR A 133 ? 0.0834 0.1630 0.1920 -0.0209 -0.0370 -0.0352 814 TYR A CG  
1060 C CD1 . TYR A 133 ? 0.0780 0.1540 0.1858 -0.0160 -0.0344 -0.0308 814 TYR A CD1 
1061 C CD2 . TYR A 133 ? 0.0940 0.1650 0.1961 -0.0252 -0.0343 -0.0386 814 TYR A CD2 
1062 C CE1 . TYR A 133 ? 0.0822 0.1480 0.1845 -0.0147 -0.0297 -0.0292 814 TYR A CE1 
1063 C CE2 . TYR A 133 ? 0.0990 0.1580 0.1945 -0.0237 -0.0287 -0.0372 814 TYR A CE2 
1064 C CZ  . TYR A 133 ? 0.1070 0.1642 0.2033 -0.0182 -0.0265 -0.0322 814 TYR A CZ  
1065 O OH  . TYR A 133 ? 0.1220 0.1687 0.2133 -0.0161 -0.0211 -0.0302 814 TYR A OH  
1066 N N   . PRO A 134 ? 0.1316 0.2359 0.2374 -0.0169 -0.0542 -0.0323 815 PRO A N   
1067 C CA  . PRO A 134 ? 0.1304 0.2428 0.2380 -0.0174 -0.0577 -0.0304 815 PRO A CA  
1068 C C   . PRO A 134 ? 0.1259 0.2418 0.2367 -0.0242 -0.0590 -0.0340 815 PRO A C   
1069 O O   . PRO A 134 ? 0.1319 0.2441 0.2383 -0.0289 -0.0607 -0.0389 815 PRO A O   
1070 C CB  . PRO A 134 ? 0.1139 0.2262 0.2142 -0.0150 -0.0625 -0.0301 815 PRO A CB  
1071 C CG  . PRO A 134 ? 0.1357 0.2399 0.2302 -0.0158 -0.0622 -0.0342 815 PRO A CG  
1072 C CD  . PRO A 134 ? 0.0937 0.1935 0.1927 -0.0147 -0.0565 -0.0336 815 PRO A CD  
1073 N N   . ARG A 135 ? 0.0947 0.2175 0.2132 -0.0250 -0.0580 -0.0319 816 ARG A N   
1074 C CA  . ARG A 135 ? 0.1409 0.2678 0.2642 -0.0317 -0.0586 -0.0348 816 ARG A CA  
1075 C C   . ARG A 135 ? 0.1674 0.2863 0.2901 -0.0363 -0.0543 -0.0394 816 ARG A C   
1076 O O   . ARG A 135 ? 0.2204 0.3388 0.3433 -0.0431 -0.0550 -0.0435 816 ARG A O   
1077 C CB  . ARG A 135 ? 0.2153 0.3468 0.3356 -0.0355 -0.0654 -0.0363 816 ARG A CB  
1078 C CG  . ARG A 135 ? 0.4249 0.5659 0.5481 -0.0313 -0.0696 -0.0313 816 ARG A CG  
1079 C CD  . ARG A 135 ? 0.4069 0.5530 0.5274 -0.0354 -0.0771 -0.0324 816 ARG A CD  
1080 N NE  . ARG A 135 ? 0.6670 0.8177 0.7937 -0.0428 -0.0785 -0.0348 816 ARG A NE  
1081 C CZ  . ARG A 135 ? 0.5568 0.7013 0.6783 -0.0499 -0.0793 -0.0405 816 ARG A CZ  
1082 N NH1 . ARG A 135 ? 0.4429 0.5766 0.5528 -0.0506 -0.0787 -0.0444 816 ARG A NH1 
1083 N NH2 . ARG A 135 ? 0.5289 0.6778 0.6569 -0.0566 -0.0803 -0.0424 816 ARG A NH2 
1084 N N   . GLY A 136 ? 0.0948 0.2071 0.2169 -0.0329 -0.0498 -0.0387 817 GLY A N   
1085 C CA  . GLY A 136 ? 0.0955 0.1999 0.2178 -0.0362 -0.0452 -0.0424 817 GLY A CA  
1086 C C   . GLY A 136 ? 0.1149 0.2115 0.2303 -0.0392 -0.0459 -0.0473 817 GLY A C   
1087 O O   . GLY A 136 ? 0.1462 0.2341 0.2603 -0.0425 -0.0411 -0.0502 817 GLY A O   
1088 N N   . GLU A 137 ? 0.1058 0.2034 0.2148 -0.0380 -0.0509 -0.0478 818 GLU A N   
1089 C CA  . GLU A 137 ? 0.1309 0.2181 0.2288 -0.0403 -0.0506 -0.0516 818 GLU A CA  
1090 C C   . GLU A 137 ? 0.1517 0.2318 0.2430 -0.0330 -0.0483 -0.0473 818 GLU A C   
1091 O O   . GLU A 137 ? 0.1039 0.1910 0.1987 -0.0277 -0.0516 -0.0439 818 GLU A O   
1092 C CB  . GLU A 137 ? 0.1355 0.2273 0.2284 -0.0445 -0.0577 -0.0552 818 GLU A CB  
1093 C CG  . GLU A 137 ? 0.1858 0.2836 0.2826 -0.0509 -0.0594 -0.0561 818 GLU A CG  
1094 C CD  . GLU A 137 ? 0.2018 0.3029 0.2918 -0.0545 -0.0666 -0.0574 818 GLU A CD  
1095 O OE1 . GLU A 137 ? 0.2293 0.3284 0.3108 -0.0516 -0.0703 -0.0575 818 GLU A OE1 
1096 O OE2 . GLU A 137 ? 0.1889 0.2944 0.2820 -0.0603 -0.0688 -0.0582 818 GLU A OE2 
1097 N N   . TYR A 138 ? 0.1456 0.2115 0.2276 -0.0327 -0.0424 -0.0474 819 TYR A N   
1098 C CA  . TYR A 138 ? 0.1165 0.1761 0.1939 -0.0261 -0.0394 -0.0431 819 TYR A CA  
1099 C C   . TYR A 138 ? 0.1191 0.1795 0.1894 -0.0236 -0.0438 -0.0428 819 TYR A C   
1100 O O   . TYR A 138 ? 0.1308 0.1876 0.1921 -0.0273 -0.0461 -0.0464 819 TYR A O   
1101 C CB  . TYR A 138 ? 0.1789 0.2235 0.2486 -0.0262 -0.0317 -0.0432 819 TYR A CB  
1102 C CG  . TYR A 138 ? 0.1512 0.1897 0.2164 -0.0198 -0.0285 -0.0390 819 TYR A CG  
1103 C CD1 . TYR A 138 ? 0.1223 0.1639 0.1947 -0.0147 -0.0265 -0.0340 819 TYR A CD1 
1104 C CD2 . TYR A 138 ? 0.1779 0.2080 0.2317 -0.0193 -0.0274 -0.0402 819 TYR A CD2 
1105 C CE1 . TYR A 138 ? 0.1637 0.2012 0.2336 -0.0094 -0.0237 -0.0301 819 TYR A CE1 
1106 C CE2 . TYR A 138 ? 0.1755 0.2007 0.2264 -0.0136 -0.0238 -0.0362 819 TYR A CE2 
1107 C CZ  . TYR A 138 ? 0.1817 0.2115 0.2416 -0.0088 -0.0222 -0.0312 819 TYR A CZ  
1108 O OH  . TYR A 138 ? 0.1421 0.1685 0.2008 -0.0036 -0.0187 -0.0272 819 TYR A OH  
1109 N N   . ALA A 139 ? 0.1285 0.1925 0.2014 -0.0175 -0.0445 -0.0384 820 ALA A N   
1110 C CA  . ALA A 139 ? 0.1139 0.1778 0.1796 -0.0146 -0.0479 -0.0374 820 ALA A CA  
1111 C C   . ALA A 139 ? 0.1083 0.1684 0.1735 -0.0085 -0.0442 -0.0327 820 ALA A C   
1112 O O   . ALA A 139 ? 0.0979 0.1616 0.1716 -0.0061 -0.0424 -0.0296 820 ALA A O   
1113 C CB  . ALA A 139 ? 0.1395 0.2162 0.2106 -0.0141 -0.0555 -0.0373 820 ALA A CB  
1114 N N   . HIS A 140 ? 0.1163 0.1690 0.1711 -0.0066 -0.0431 -0.0323 821 HIS A N   
1115 C CA  . HIS A 140 ? 0.1471 0.1964 0.2010 -0.0014 -0.0397 -0.0281 821 HIS A CA  
1116 C C   . HIS A 140 ? 0.1166 0.1672 0.1640 0.0009  -0.0438 -0.0273 821 HIS A C   
1117 O O   . HIS A 140 ? 0.1495 0.1940 0.1855 -0.0006 -0.0448 -0.0298 821 HIS A O   
1118 C CB  . HIS A 140 ? 0.1205 0.1577 0.1680 -0.0008 -0.0323 -0.0278 821 HIS A CB  
1119 C CG  . HIS A 140 ? 0.1197 0.1538 0.1662 0.0041  -0.0286 -0.0236 821 HIS A CG  
1120 N ND1 . HIS A 140 ? 0.1667 0.1899 0.2059 0.0055  -0.0221 -0.0231 821 HIS A ND1 
1121 C CD2 . HIS A 140 ? 0.1100 0.1501 0.1619 0.0076  -0.0300 -0.0199 821 HIS A CD2 
1122 C CE1 . HIS A 140 ? 0.2067 0.2305 0.2480 0.0096  -0.0198 -0.0191 821 HIS A CE1 
1123 N NE2 . HIS A 140 ? 0.1135 0.1473 0.1622 0.0106  -0.0246 -0.0172 821 HIS A NE2 
1124 N N   . LEU A 141 ? 0.1075 0.1651 0.1610 0.0045  -0.0459 -0.0240 822 LEU A N   
1125 C CA  . LEU A 141 ? 0.1114 0.1687 0.1585 0.0077  -0.0486 -0.0223 822 LEU A CA  
1126 C C   . LEU A 141 ? 0.1136 0.1625 0.1561 0.0106  -0.0426 -0.0195 822 LEU A C   
1127 O O   . LEU A 141 ? 0.1439 0.1949 0.1935 0.0129  -0.0400 -0.0162 822 LEU A O   
1128 C CB  . LEU A 141 ? 0.1290 0.1962 0.1844 0.0102  -0.0526 -0.0200 822 LEU A CB  
1129 C CG  . LEU A 141 ? 0.1200 0.1975 0.1835 0.0079  -0.0576 -0.0219 822 LEU A CG  
1130 C CD1 . LEU A 141 ? 0.2007 0.2860 0.2713 0.0117  -0.0601 -0.0189 822 LEU A CD1 
1131 C CD2 . LEU A 141 ? 0.1085 0.1870 0.1653 0.0051  -0.0627 -0.0252 822 LEU A CD2 
1132 N N   . LYS A 142 ? 0.1263 0.1654 0.1567 0.0102  -0.0401 -0.0209 823 LYS A N   
1133 C CA  . LYS A 142 ? 0.1568 0.1873 0.1832 0.0127  -0.0331 -0.0185 823 LYS A CA  
1134 C C   . LYS A 142 ? 0.1669 0.1962 0.1882 0.0162  -0.0338 -0.0158 823 LYS A C   
1135 O O   . LYS A 142 ? 0.1421 0.1690 0.1530 0.0163  -0.0376 -0.0170 823 LYS A O   
1136 C CB  . LYS A 142 ? 0.2276 0.2462 0.2425 0.0108  -0.0287 -0.0213 823 LYS A CB  
1137 C CG  . LYS A 142 ? 0.2594 0.2692 0.2716 0.0137  -0.0201 -0.0187 823 LYS A CG  
1138 C CD  . LYS A 142 ? 0.2314 0.2284 0.2329 0.0120  -0.0144 -0.0215 823 LYS A CD  
1139 C CE  . LYS A 142 ? 0.3561 0.3445 0.3398 0.0102  -0.0168 -0.0247 823 LYS A CE  
1140 N NZ  . LYS A 142 ? 0.3906 0.3643 0.3616 0.0082  -0.0104 -0.0278 823 LYS A NZ  
1141 N N   . ASP A 143 ? 0.1249 0.1557 0.1530 0.0187  -0.0301 -0.0120 824 ASP A N   
1142 C CA  . ASP A 143 ? 0.1279 0.1560 0.1515 0.0217  -0.0290 -0.0092 824 ASP A CA  
1143 C C   . ASP A 143 ? 0.2009 0.2330 0.2207 0.0228  -0.0358 -0.0093 824 ASP A C   
1144 O O   . ASP A 143 ? 0.1556 0.1820 0.1639 0.0246  -0.0366 -0.0089 824 ASP A O   
1145 C CB  . ASP A 143 ? 0.1983 0.2146 0.2097 0.0227  -0.0233 -0.0091 824 ASP A CB  
1146 C CG  . ASP A 143 ? 0.1984 0.2114 0.2153 0.0229  -0.0155 -0.0078 824 ASP A CG  
1147 O OD1 . ASP A 143 ? 0.2009 0.2212 0.2312 0.0230  -0.0146 -0.0056 824 ASP A OD1 
1148 O OD2 . ASP A 143 ? 0.2429 0.2457 0.2505 0.0230  -0.0102 -0.0088 824 ASP A OD2 
1149 N N   . THR A 144 ? 0.1664 0.2082 0.1956 0.0221  -0.0406 -0.0097 825 THR A N   
1150 C CA  . THR A 144 ? 0.1781 0.2249 0.2061 0.0241  -0.0465 -0.0091 825 THR A CA  
1151 C C   . THR A 144 ? 0.1469 0.1925 0.1762 0.0273  -0.0443 -0.0053 825 THR A C   
1152 O O   . THR A 144 ? 0.1634 0.2102 0.2006 0.0269  -0.0405 -0.0037 825 THR A O   
1153 C CB  . THR A 144 ? 0.1825 0.2398 0.2205 0.0224  -0.0515 -0.0107 825 THR A CB  
1154 O OG1 . THR A 144 ? 0.2226 0.2851 0.2601 0.0251  -0.0568 -0.0096 825 THR A OG1 
1155 C CG2 . THR A 144 ? 0.1098 0.1717 0.1602 0.0216  -0.0488 -0.0096 825 THR A CG2 
1156 N N   . THR A 145 ? 0.1887 0.2315 0.2094 0.0304  -0.0466 -0.0038 826 THR A N   
1157 C CA  A THR A 145 ? 0.1516 0.1903 0.1704 0.0333  -0.0434 -0.0003 826 THR A CA  
1158 C CA  B THR A 145 ? 0.1454 0.1840 0.1641 0.0333  -0.0434 -0.0003 826 THR A CA  
1159 C C   . THR A 145 ? 0.1244 0.1698 0.1518 0.0348  -0.0457 0.0012  826 THR A C   
1160 O O   . THR A 145 ? 0.1283 0.1805 0.1585 0.0359  -0.0511 0.0005  826 THR A O   
1161 C CB  A THR A 145 ? 0.1803 0.2108 0.1843 0.0364  -0.0440 0.0010  826 THR A CB  
1162 C CB  B THR A 145 ? 0.1814 0.2122 0.1854 0.0365  -0.0443 0.0010  826 THR A CB  
1163 O OG1 A THR A 145 ? 0.2516 0.2873 0.2526 0.0380  -0.0514 0.0004  826 THR A OG1 
1164 O OG1 B THR A 145 ? 0.1868 0.2103 0.1809 0.0348  -0.0422 -0.0009 826 THR A OG1 
1165 C CG2 A THR A 145 ? 0.1912 0.2129 0.1851 0.0348  -0.0403 -0.0005 826 THR A CG2 
1166 C CG2 B THR A 145 ? 0.1453 0.1693 0.1458 0.0390  -0.0395 0.0045  826 THR A CG2 
1167 N N   . VAL A 146 ? 0.1145 0.1578 0.1460 0.0348  -0.0414 0.0033  827 VAL A N   
1168 C CA  . VAL A 146 ? 0.1306 0.1773 0.1676 0.0363  -0.0423 0.0048  827 VAL A CA  
1169 C C   . VAL A 146 ? 0.1357 0.1771 0.1633 0.0410  -0.0430 0.0073  827 VAL A C   
1170 O O   . VAL A 146 ? 0.1545 0.1870 0.1734 0.0420  -0.0393 0.0090  827 VAL A O   
1171 C CB  . VAL A 146 ? 0.1725 0.2181 0.2158 0.0338  -0.0377 0.0058  827 VAL A CB  
1172 C CG1 . VAL A 146 ? 0.1214 0.1673 0.1671 0.0352  -0.0378 0.0072  827 VAL A CG1 
1173 C CG2 . VAL A 146 ? 0.1451 0.1966 0.1976 0.0299  -0.0377 0.0039  827 VAL A CG2 
1174 N N   . GLU A 147 ? 0.1287 0.1754 0.1582 0.0440  -0.0475 0.0078  828 GLU A N   
1175 C CA  . GLU A 147 ? 0.1968 0.2391 0.2177 0.0494  -0.0488 0.0108  828 GLU A CA  
1176 C C   . GLU A 147 ? 0.1906 0.2308 0.2143 0.0521  -0.0461 0.0133  828 GLU A C   
1177 O O   . GLU A 147 ? 0.1832 0.2151 0.1982 0.0560  -0.0439 0.0162  828 GLU A O   
1178 C CB  . GLU A 147 ? 0.1579 0.2079 0.1783 0.0519  -0.0561 0.0103  828 GLU A CB  
1179 C CG  . GLU A 147 ? 0.2491 0.2987 0.2630 0.0492  -0.0588 0.0077  828 GLU A CG  
1180 C CD  . GLU A 147 ? 0.4167 0.4760 0.4322 0.0498  -0.0668 0.0065  828 GLU A CD  
1181 O OE1 . GLU A 147 ? 0.3069 0.3740 0.3294 0.0532  -0.0701 0.0082  828 GLU A OE1 
1182 O OE2 . GLU A 147 ? 0.3150 0.3739 0.3248 0.0468  -0.0695 0.0039  828 GLU A OE2 
1183 N N   . ILE A 148 ? 0.1678 0.2139 0.2023 0.0501  -0.0456 0.0121  829 ILE A N   
1184 C CA  . ILE A 148 ? 0.1344 0.1781 0.1713 0.0523  -0.0430 0.0139  829 ILE A CA  
1185 C C   . ILE A 148 ? 0.1511 0.1958 0.1956 0.0470  -0.0398 0.0120  829 ILE A C   
1186 O O   . ILE A 148 ? 0.1416 0.1932 0.1930 0.0433  -0.0417 0.0095  829 ILE A O   
1187 C CB  . ILE A 148 ? 0.1580 0.2100 0.2003 0.0570  -0.0472 0.0148  829 ILE A CB  
1188 C CG1 . ILE A 148 ? 0.2225 0.2740 0.2570 0.0627  -0.0511 0.0174  829 ILE A CG1 
1189 C CG2 . ILE A 148 ? 0.2412 0.2904 0.2868 0.0590  -0.0433 0.0163  829 ILE A CG2 
1190 C CD1 . ILE A 148 ? 0.2836 0.3233 0.3077 0.0674  -0.0471 0.0212  829 ILE A CD1 
1191 N N   . GLU A 149 ? 0.1268 0.1639 0.1691 0.0464  -0.0351 0.0133  830 GLU A N   
1192 C CA  . GLU A 149 ? 0.1271 0.1651 0.1755 0.0413  -0.0328 0.0116  830 GLU A CA  
1193 C C   . GLU A 149 ? 0.1285 0.1629 0.1771 0.0432  -0.0303 0.0125  830 GLU A C   
1194 O O   . GLU A 149 ? 0.1383 0.1658 0.1806 0.0479  -0.0282 0.0149  830 GLU A O   
1195 C CB  . GLU A 149 ? 0.1490 0.1809 0.1946 0.0364  -0.0290 0.0116  830 GLU A CB  
1196 C CG  . GLU A 149 ? 0.1631 0.1835 0.1999 0.0377  -0.0244 0.0138  830 GLU A CG  
1197 C CD  . GLU A 149 ? 0.2212 0.2371 0.2570 0.0320  -0.0206 0.0138  830 GLU A CD  
1198 O OE1 . GLU A 149 ? 0.1958 0.2181 0.2388 0.0274  -0.0217 0.0123  830 GLU A OE1 
1199 O OE2 . GLU A 149 ? 0.3521 0.3583 0.3803 0.0324  -0.0165 0.0154  830 GLU A OE2 
1200 N N   . GLN A 150 ? 0.1034 0.1413 0.1583 0.0398  -0.0300 0.0107  831 GLN A N   
1201 C CA  . GLN A 150 ? 0.1070 0.1409 0.1619 0.0411  -0.0269 0.0111  831 GLN A CA  
1202 C C   . GLN A 150 ? 0.1225 0.1522 0.1771 0.0344  -0.0242 0.0094  831 GLN A C   
1203 O O   . GLN A 150 ? 0.1229 0.1591 0.1835 0.0303  -0.0264 0.0076  831 GLN A O   
1204 C CB  . GLN A 150 ? 0.1198 0.1629 0.1828 0.0442  -0.0295 0.0105  831 GLN A CB  
1205 C CG  . GLN A 150 ? 0.1395 0.1781 0.2027 0.0460  -0.0254 0.0110  831 GLN A CG  
1206 C CD  . GLN A 150 ? 0.1715 0.2197 0.2435 0.0505  -0.0272 0.0112  831 GLN A CD  
1207 O OE1 . GLN A 150 ? 0.2170 0.2757 0.2949 0.0519  -0.0323 0.0110  831 GLN A OE1 
1208 N NE2 . GLN A 150 ? 0.1763 0.2206 0.2491 0.0524  -0.0229 0.0117  831 GLN A NE2 
1209 N N   . LYS A 151 ? 0.1143 0.1327 0.1614 0.0331  -0.0196 0.0102  832 LYS A N   
1210 C CA  . LYS A 151 ? 0.1145 0.1287 0.1603 0.0262  -0.0176 0.0085  832 LYS A CA  
1211 C C   . LYS A 151 ? 0.1150 0.1286 0.1622 0.0264  -0.0162 0.0074  832 LYS A C   
1212 O O   . LYS A 151 ? 0.1960 0.2020 0.2387 0.0303  -0.0123 0.0083  832 LYS A O   
1213 C CB  . LYS A 151 ? 0.1606 0.1623 0.1972 0.0235  -0.0130 0.0093  832 LYS A CB  
1214 C CG  . LYS A 151 ? 0.1714 0.1689 0.2059 0.0154  -0.0116 0.0075  832 LYS A CG  
1215 C CD  . LYS A 151 ? 0.2325 0.2182 0.2584 0.0116  -0.0073 0.0079  832 LYS A CD  
1216 C CE  . LYS A 151 ? 0.2451 0.2279 0.2690 0.0024  -0.0070 0.0060  832 LYS A CE  
1217 N NZ  . LYS A 151 ? 0.3568 0.3324 0.3757 -0.0028 -0.0041 0.0063  832 LYS A NZ  
1218 N N   . TYR A 152 ? 0.1089 0.1298 0.1621 0.0227  -0.0189 0.0056  833 TYR A N   
1219 C CA  . TYR A 152 ? 0.1552 0.1750 0.2092 0.0220  -0.0171 0.0043  833 TYR A CA  
1220 C C   . TYR A 152 ? 0.1689 0.1783 0.2149 0.0158  -0.0140 0.0032  833 TYR A C   
1221 O O   . TYR A 152 ? 0.2588 0.2609 0.3003 0.0160  -0.0101 0.0025  833 TYR A O   
1222 C CB  . TYR A 152 ? 0.1344 0.1653 0.1971 0.0205  -0.0210 0.0030  833 TYR A CB  
1223 C CG  . TYR A 152 ? 0.0982 0.1396 0.1690 0.0254  -0.0242 0.0034  833 TYR A CG  
1224 C CD1 . TYR A 152 ? 0.1287 0.1712 0.2012 0.0320  -0.0233 0.0047  833 TYR A CD1 
1225 C CD2 . TYR A 152 ? 0.0849 0.1352 0.1618 0.0233  -0.0282 0.0025  833 TYR A CD2 
1226 C CE1 . TYR A 152 ? 0.1391 0.1923 0.2192 0.0356  -0.0271 0.0049  833 TYR A CE1 
1227 C CE2 . TYR A 152 ? 0.1264 0.1856 0.2097 0.0267  -0.0313 0.0023  833 TYR A CE2 
1228 C CZ  . TYR A 152 ? 0.1025 0.1636 0.1875 0.0325  -0.0311 0.0034  833 TYR A CZ  
1229 O OH  . TYR A 152 ? 0.0878 0.1588 0.1793 0.0351  -0.0350 0.0031  833 TYR A OH  
1230 N N   . ALA A 153 ? 0.1498 0.1589 0.1941 0.0099  -0.0157 0.0029  834 ALA A N   
1231 C CA  . ALA A 153 ? 0.1362 0.1368 0.1730 0.0026  -0.0140 0.0018  834 ALA A CA  
1232 C C   . ALA A 153 ? 0.1447 0.1481 0.1828 -0.0020 -0.0162 0.0024  834 ALA A C   
1233 O O   . ALA A 153 ? 0.1468 0.1571 0.1905 0.0010  -0.0182 0.0037  834 ALA A O   
1234 C CB  . ALA A 153 ? 0.1234 0.1263 0.1609 -0.0015 -0.0156 0.0002  834 ALA A CB  
1235 N N   . ASN A 154 ? 0.1270 0.1249 0.1597 -0.0095 -0.0157 0.0015  835 ASN A N   
1236 C CA  . ASN A 154 ? 0.1260 0.1274 0.1613 -0.0145 -0.0176 0.0023  835 ASN A CA  
1237 C C   . ASN A 154 ? 0.1119 0.1276 0.1584 -0.0138 -0.0225 0.0034  835 ASN A C   
1238 O O   . ASN A 154 ? 0.1265 0.1481 0.1765 -0.0152 -0.0257 0.0029  835 ASN A O   
1239 C CB  . ASN A 154 ? 0.1347 0.1302 0.1637 -0.0236 -0.0175 0.0010  835 ASN A CB  
1240 C CG  . ASN A 154 ? 0.2387 0.2182 0.2557 -0.0252 -0.0116 0.0000  835 ASN A CG  
1241 O OD1 . ASN A 154 ? 0.2283 0.2020 0.2428 -0.0196 -0.0077 0.0010  835 ASN A OD1 
1242 N ND2 . ASN A 154 ? 0.2580 0.2295 0.2666 -0.0330 -0.0110 -0.0020 835 ASN A ND2 
1243 N N   . ASN A 155 ? 0.1077 0.1277 0.1588 -0.0112 -0.0225 0.0050  836 ASN A N   
1244 C CA  . ASN A 155 ? 0.0966 0.1285 0.1575 -0.0101 -0.0260 0.0061  836 ASN A CA  
1245 C C   . ASN A 155 ? 0.1437 0.1816 0.2089 -0.0055 -0.0283 0.0056  836 ASN A C   
1246 O O   . ASN A 155 ? 0.0807 0.1271 0.1529 -0.0060 -0.0313 0.0061  836 ASN A O   
1247 C CB  . ASN A 155 ? 0.0946 0.1327 0.1604 -0.0170 -0.0288 0.0068  836 ASN A CB  
1248 C CG  . ASN A 155 ? 0.1033 0.1362 0.1655 -0.0229 -0.0267 0.0070  836 ASN A CG  
1249 O OD1 . ASN A 155 ? 0.1265 0.1557 0.1842 -0.0292 -0.0275 0.0060  836 ASN A OD1 
1250 N ND2 . ASN A 155 ? 0.1049 0.1363 0.1679 -0.0212 -0.0238 0.0082  836 ASN A ND2 
1251 N N   . THR A 156 ? 0.0912 0.1246 0.1526 -0.0010 -0.0266 0.0047  837 THR A N   
1252 C CA  . THR A 156 ? 0.0849 0.1237 0.1505 0.0029  -0.0283 0.0039  837 THR A CA  
1253 C C   . THR A 156 ? 0.1200 0.1582 0.1852 0.0096  -0.0274 0.0043  837 THR A C   
1254 O O   . THR A 156 ? 0.1690 0.2005 0.2291 0.0124  -0.0246 0.0044  837 THR A O   
1255 C CB  . THR A 156 ? 0.1054 0.1405 0.1679 0.0012  -0.0274 0.0026  837 THR A CB  
1256 O OG1 . THR A 156 ? 0.0910 0.1244 0.1510 -0.0056 -0.0285 0.0024  837 THR A OG1 
1257 C CG2 . THR A 156 ? 0.1269 0.1692 0.1956 0.0038  -0.0293 0.0018  837 THR A CG2 
1258 N N   . TYR A 157 ? 0.0798 0.1247 0.1496 0.0122  -0.0296 0.0047  838 TYR A N   
1259 C CA  . TYR A 157 ? 0.0819 0.1266 0.1502 0.0179  -0.0296 0.0054  838 TYR A CA  
1260 C C   . TYR A 157 ? 0.0754 0.1285 0.1496 0.0207  -0.0327 0.0044  838 TYR A C   
1261 O O   . TYR A 157 ? 0.0724 0.1312 0.1514 0.0185  -0.0347 0.0036  838 TYR A O   
1262 C CB  . TYR A 157 ? 0.0848 0.1278 0.1508 0.0180  -0.0289 0.0067  838 TYR A CB  
1263 C CG  . TYR A 157 ? 0.1076 0.1413 0.1668 0.0163  -0.0252 0.0078  838 TYR A CG  
1264 C CD1 . TYR A 157 ? 0.0934 0.1257 0.1531 0.0102  -0.0241 0.0078  838 TYR A CD1 
1265 C CD2 . TYR A 157 ? 0.1049 0.1312 0.1572 0.0208  -0.0229 0.0090  838 TYR A CD2 
1266 C CE1 . TYR A 157 ? 0.1027 0.1259 0.1560 0.0077  -0.0204 0.0084  838 TYR A CE1 
1267 C CE2 . TYR A 157 ? 0.1675 0.1837 0.2127 0.0191  -0.0187 0.0100  838 TYR A CE2 
1268 C CZ  . TYR A 157 ? 0.2229 0.2374 0.2687 0.0122  -0.0174 0.0094  838 TYR A CZ  
1269 O OH  . TYR A 157 ? 0.1751 0.1791 0.2136 0.0097  -0.0130 0.0100  838 TYR A OH  
1270 N N   . GLY A 158 ? 0.0780 0.1318 0.1520 0.0255  -0.0331 0.0046  839 GLY A N   
1271 C CA  . GLY A 158 ? 0.0813 0.1428 0.1598 0.0282  -0.0365 0.0039  839 GLY A CA  
1272 C C   . GLY A 158 ? 0.0781 0.1384 0.1521 0.0307  -0.0377 0.0049  839 GLY A C   
1273 O O   . GLY A 158 ? 0.1009 0.1542 0.1683 0.0325  -0.0356 0.0066  839 GLY A O   
1274 N N   . VAL A 159 ? 0.0746 0.1408 0.1512 0.0305  -0.0408 0.0036  840 VAL A N   
1275 C CA  . VAL A 159 ? 0.0796 0.1444 0.1507 0.0327  -0.0422 0.0042  840 VAL A CA  
1276 C C   . VAL A 159 ? 0.1008 0.1729 0.1745 0.0348  -0.0467 0.0030  840 VAL A C   
1277 O O   . VAL A 159 ? 0.1020 0.1788 0.1803 0.0318  -0.0464 0.0019  840 VAL A O   
1278 C CB  . VAL A 159 ? 0.0781 0.1409 0.1479 0.0295  -0.0409 0.0038  840 VAL A CB  
1279 C CG1 . VAL A 159 ? 0.0787 0.1360 0.1472 0.0270  -0.0370 0.0052  840 VAL A CG1 
1280 C CG2 . VAL A 159 ? 0.0708 0.1396 0.1473 0.0263  -0.0423 0.0016  840 VAL A CG2 
1281 N N   . GLN A 160 ? 0.1552 0.2258 0.2225 0.0384  -0.0487 0.0042  841 GLN A N   
1282 C CA  . GLN A 160 ? 0.1766 0.2533 0.2442 0.0392  -0.0529 0.0035  841 GLN A CA  
1283 C C   . GLN A 160 ? 0.1989 0.2734 0.2597 0.0388  -0.0553 0.0021  841 GLN A C   
1284 O O   . GLN A 160 ? 0.1336 0.1998 0.1857 0.0400  -0.0528 0.0037  841 GLN A O   
1285 C CB  . GLN A 160 ? 0.1601 0.2378 0.2260 0.0442  -0.0543 0.0063  841 GLN A CB  
1286 C CG  . GLN A 160 ? 0.2240 0.3035 0.2966 0.0451  -0.0514 0.0076  841 GLN A CG  
1287 C CD  . GLN A 160 ? 0.3526 0.4337 0.4251 0.0506  -0.0525 0.0108  841 GLN A CD  
1288 O OE1 . GLN A 160 ? 0.5046 0.5869 0.5726 0.0528  -0.0561 0.0122  841 GLN A OE1 
1289 N NE2 . GLN A 160 ? 0.3704 0.4515 0.4479 0.0531  -0.0495 0.0121  841 GLN A NE2 
1290 N N   . TYR A 161 ? 0.1424 0.2219 0.2053 0.0355  -0.0579 -0.0004 842 TYR A N   
1291 C CA  . TYR A 161 ? 0.0989 0.1757 0.1546 0.0342  -0.0598 -0.0024 842 TYR A CA  
1292 C C   . TYR A 161 ? 0.1358 0.2201 0.1938 0.0320  -0.0647 -0.0046 842 TYR A C   
1293 O O   . TYR A 161 ? 0.1861 0.2755 0.2518 0.0290  -0.0632 -0.0044 842 TYR A O   
1294 C CB  . TYR A 161 ? 0.0963 0.1684 0.1526 0.0302  -0.0552 -0.0038 842 TYR A CB  
1295 C CG  . TYR A 161 ? 0.0843 0.1619 0.1515 0.0271  -0.0542 -0.0052 842 TYR A CG  
1296 C CD1 . TYR A 161 ? 0.0973 0.1798 0.1684 0.0238  -0.0562 -0.0081 842 TYR A CD1 
1297 C CD2 . TYR A 161 ? 0.0777 0.1547 0.1502 0.0270  -0.0509 -0.0036 842 TYR A CD2 
1298 C CE1 . TYR A 161 ? 0.0762 0.1602 0.1534 0.0202  -0.0529 -0.0082 842 TYR A CE1 
1299 C CE2 . TYR A 161 ? 0.0926 0.1717 0.1707 0.0232  -0.0482 -0.0039 842 TYR A CE2 
1300 C CZ  . TYR A 161 ? 0.1199 0.2021 0.1999 0.0202  -0.0489 -0.0060 842 TYR A CZ  
1301 O OH  . TYR A 161 ? 0.1183 0.2013 0.2022 0.0170  -0.0461 -0.0062 842 TYR A OH  
1302 N N   . GLN A 162 ? 0.1456 0.2283 0.1947 0.0321  -0.0687 -0.0061 843 GLN A N   
1303 C CA  . GLN A 162 ? 0.1379 0.2274 0.1881 0.0291  -0.0736 -0.0081 843 GLN A CA  
1304 C C   . GLN A 162 ? 0.1907 0.2813 0.2447 0.0234  -0.0730 -0.0125 843 GLN A C   
1305 O O   . GLN A 162 ? 0.1704 0.2534 0.2211 0.0218  -0.0685 -0.0136 843 GLN A O   
1306 C CB  . GLN A 162 ? 0.3078 0.3952 0.3455 0.0313  -0.0795 -0.0083 843 GLN A CB  
1307 C CG  . GLN A 162 ? 0.3883 0.4745 0.4220 0.0372  -0.0802 -0.0034 843 GLN A CG  
1308 C CD  . GLN A 162 ? 0.3667 0.4503 0.3866 0.0394  -0.0860 -0.0030 843 GLN A CD  
1309 O OE1 . GLN A 162 ? 0.5092 0.5981 0.5282 0.0357  -0.0908 -0.0045 843 GLN A OE1 
1310 N NE2 . GLN A 162 ? 0.3891 0.4623 0.3973 0.0437  -0.0836 -0.0001 843 GLN A NE2 
1311 N N   . GLY A 163 ? 0.1654 0.2628 0.2251 0.0192  -0.0744 -0.0134 844 GLY A N   
1312 C CA  . GLY A 163 ? 0.1751 0.2732 0.2369 0.0136  -0.0745 -0.0179 844 GLY A CA  
1313 C C   . GLY A 163 ? 0.2127 0.3158 0.2851 0.0099  -0.0712 -0.0177 844 GLY A C   
1314 O O   . GLY A 163 ? 0.2613 0.3669 0.3355 0.0049  -0.0726 -0.0210 844 GLY A O   
1315 N N   . GLY A 164 ? 0.1869 0.2908 0.2653 0.0121  -0.0668 -0.0140 845 GLY A N   
1316 C CA  . GLY A 164 ? 0.1717 0.2785 0.2581 0.0092  -0.0632 -0.0139 845 GLY A CA  
1317 C C   . GLY A 164 ? 0.1688 0.2843 0.2604 0.0068  -0.0659 -0.0136 845 GLY A C   
1318 O O   . GLY A 164 ? 0.2777 0.3979 0.3692 0.0091  -0.0693 -0.0111 845 GLY A O   
1319 N N   . LYS A 165 ? 0.2300 0.3476 0.3267 0.0023  -0.0644 -0.0158 846 LYS A N   
1320 C CA  . LYS A 165 ? 0.2048 0.3312 0.3086 -0.0003 -0.0660 -0.0153 846 LYS A CA  
1321 C C   . LYS A 165 ? 0.1868 0.3134 0.2973 -0.0020 -0.0609 -0.0155 846 LYS A C   
1322 O O   . LYS A 165 ? 0.1785 0.2982 0.2873 -0.0017 -0.0568 -0.0163 846 LYS A O   
1323 C CB  . LYS A 165 ? 0.1893 0.3189 0.2914 -0.0057 -0.0711 -0.0190 846 LYS A CB  
1324 C CG  . LYS A 165 ? 0.2563 0.3847 0.3495 -0.0046 -0.0768 -0.0196 846 LYS A CG  
1325 C CD  . LYS A 165 ? 0.4369 0.5728 0.5320 -0.0013 -0.0808 -0.0151 846 LYS A CD  
1326 C CE  . LYS A 165 ? 0.5260 0.6719 0.6269 -0.0060 -0.0855 -0.0153 846 LYS A CE  
1327 N NZ  . LYS A 165 ? 0.6565 0.8104 0.7603 -0.0024 -0.0901 -0.0104 846 LYS A NZ  
1328 N N   . ALA A 166 ? 0.1556 0.2905 0.2740 -0.0036 -0.0613 -0.0146 847 ALA A N   
1329 C CA  . ALA A 166 ? 0.1724 0.3081 0.2973 -0.0048 -0.0565 -0.0147 847 ALA A CA  
1330 C C   . ALA A 166 ? 0.2207 0.3501 0.3439 -0.0091 -0.0542 -0.0188 847 ALA A C   
1331 O O   . ALA A 166 ? 0.1855 0.3139 0.3063 -0.0133 -0.0569 -0.0222 847 ALA A O   
1332 C CB  . ALA A 166 ? 0.1738 0.3206 0.3084 -0.0065 -0.0580 -0.0137 847 ALA A CB  
1333 N N   . GLY A 167 ? 0.1302 0.2549 0.2546 -0.0082 -0.0491 -0.0185 848 GLY A N   
1334 C CA  . GLY A 167 ? 0.0734 0.1918 0.1968 -0.0114 -0.0464 -0.0215 848 GLY A CA  
1335 C C   . GLY A 167 ? 0.0705 0.1805 0.1874 -0.0090 -0.0452 -0.0213 848 GLY A C   
1336 O O   . GLY A 167 ? 0.1257 0.2306 0.2430 -0.0102 -0.0422 -0.0225 848 GLY A O   
1337 N N   . MET A 168 ? 0.0761 0.1851 0.1880 -0.0056 -0.0475 -0.0196 849 MET A N   
1338 C CA  . MET A 168 ? 0.0688 0.1709 0.1755 -0.0034 -0.0466 -0.0192 849 MET A CA  
1339 C C   . MET A 168 ? 0.0637 0.1625 0.1696 -0.0003 -0.0431 -0.0159 849 MET A C   
1340 O O   . MET A 168 ? 0.0850 0.1785 0.1882 0.0008  -0.0417 -0.0153 849 MET A O   
1341 C CB  . MET A 168 ? 0.0725 0.1744 0.1739 -0.0012 -0.0504 -0.0190 849 MET A CB  
1342 C CG  . MET A 168 ? 0.1628 0.2584 0.2601 0.0007  -0.0497 -0.0192 849 MET A CG  
1343 S SD  . MET A 168 ? 0.3028 0.3979 0.3938 0.0021  -0.0548 -0.0211 849 MET A SD  
1344 C CE  . MET A 168 ? 0.2051 0.2931 0.2947 0.0027  -0.0528 -0.0229 849 MET A CE  
1345 N N   . SER A 169 ? 0.0662 0.1683 0.1748 0.0010  -0.0419 -0.0139 850 SER A N   
1346 C CA  . SER A 169 ? 0.0792 0.1780 0.1866 0.0035  -0.0392 -0.0116 850 SER A CA  
1347 C C   . SER A 169 ? 0.1219 0.2161 0.2295 0.0018  -0.0365 -0.0123 850 SER A C   
1348 O O   . SER A 169 ? 0.0806 0.1757 0.1922 -0.0010 -0.0354 -0.0142 850 SER A O   
1349 C CB  . SER A 169 ? 0.1820 0.2854 0.2938 0.0051  -0.0383 -0.0103 850 SER A CB  
1350 O OG  . SER A 169 ? 0.1987 0.3065 0.3106 0.0075  -0.0410 -0.0090 850 SER A OG  
1351 N N   . GLY A 170 ? 0.0807 0.1702 0.1845 0.0033  -0.0356 -0.0106 851 GLY A N   
1352 C CA  . GLY A 170 ? 0.0986 0.1842 0.2024 0.0021  -0.0338 -0.0104 851 GLY A CA  
1353 C C   . GLY A 170 ? 0.0528 0.1357 0.1552 0.0019  -0.0344 -0.0106 851 GLY A C   
1354 O O   . GLY A 170 ? 0.0860 0.1660 0.1883 0.0020  -0.0333 -0.0093 851 GLY A O   
1355 N N   . GLY A 171 ? 0.0550 0.1392 0.1569 0.0020  -0.0364 -0.0122 852 GLY A N   
1356 C CA  . GLY A 171 ? 0.0555 0.1374 0.1573 0.0025  -0.0370 -0.0128 852 GLY A CA  
1357 C C   . GLY A 171 ? 0.0726 0.1522 0.1712 0.0051  -0.0365 -0.0098 852 GLY A C   
1358 O O   . GLY A 171 ? 0.1181 0.1979 0.2137 0.0064  -0.0365 -0.0080 852 GLY A O   
1359 N N   . GLY A 172 ? 0.0757 0.1236 0.2268 -0.0064 -0.0408 -0.0353 853 GLY A N   
1360 C CA  . GLY A 172 ? 0.0691 0.1142 0.2140 0.0009  -0.0402 -0.0293 853 GLY A CA  
1361 C C   . GLY A 172 ? 0.0681 0.1206 0.2047 0.0063  -0.0409 -0.0327 853 GLY A C   
1362 O O   . GLY A 172 ? 0.0740 0.1320 0.2137 0.0064  -0.0441 -0.0425 853 GLY A O   
1363 N N   . ILE A 173 ? 0.0628 0.1159 0.1892 0.0098  -0.0383 -0.0252 854 ILE A N   
1364 C CA  . ILE A 173 ? 0.0632 0.1224 0.1851 0.0145  -0.0382 -0.0262 854 ILE A CA  
1365 C C   . ILE A 173 ? 0.0627 0.1187 0.1905 0.0173  -0.0348 -0.0244 854 ILE A C   
1366 O O   . ILE A 173 ? 0.0601 0.1104 0.1865 0.0158  -0.0329 -0.0175 854 ILE A O   
1367 C CB  . ILE A 173 ? 0.0605 0.1232 0.1716 0.0158  -0.0375 -0.0193 854 ILE A CB  
1368 C CG1 . ILE A 173 ? 0.0624 0.1300 0.1706 0.0146  -0.0403 -0.0205 854 ILE A CG1 
1369 C CG2 . ILE A 173 ? 0.0636 0.1334 0.1732 0.0209  -0.0386 -0.0200 854 ILE A CG2 
1370 C CD1 . ILE A 173 ? 0.0621 0.1320 0.1636 0.0180  -0.0403 -0.0144 854 ILE A CD1 
1371 N N   . PHE A 174 ? 0.0670 0.1289 0.2019 0.0220  -0.0338 -0.0319 855 PHE A N   
1372 C CA  . PHE A 174 ? 0.0696 0.1305 0.2138 0.0261  -0.0287 -0.0322 855 PHE A CA  
1373 C C   . PHE A 174 ? 0.0707 0.1430 0.2141 0.0298  -0.0230 -0.0328 855 PHE A C   
1374 O O   . PHE A 174 ? 0.1482 0.2223 0.2749 0.0296  -0.0219 -0.0360 855 PHE A O   
1375 C CB  . PHE A 174 ? 0.0804 0.1350 0.2347 0.0296  -0.0278 -0.0431 855 PHE A CB  
1376 C CG  . PHE A 174 ? 0.0940 0.1363 0.2555 0.0261  -0.0325 -0.0424 855 PHE A CG  
1377 C CD1 . PHE A 174 ? 0.0836 0.1243 0.2400 0.0190  -0.0368 -0.0458 855 PHE A CD1 
1378 C CD2 . PHE A 174 ? 0.0985 0.1304 0.2702 0.0293  -0.0322 -0.0377 855 PHE A CD2 
1379 C CE1 . PHE A 174 ? 0.0886 0.1174 0.2513 0.0136  -0.0388 -0.0445 855 PHE A CE1 
1380 C CE2 . PHE A 174 ? 0.0934 0.1109 0.2700 0.0261  -0.0358 -0.0352 855 PHE A CE2 
1381 C CZ  . PHE A 174 ? 0.0950 0.1099 0.2656 0.0168  -0.0379 -0.0385 855 PHE A CZ  
1382 N N   . ASN A 175 ? 0.1064 0.1813 0.2564 0.0304  -0.0177 -0.0275 856 ASN A N   
1383 C CA  . ASN A 175 ? 0.1520 0.2387 0.3047 0.0325  -0.0089 -0.0285 856 ASN A CA  
1384 C C   . ASN A 175 ? 0.1670 0.2546 0.3218 0.0380  -0.0006 -0.0392 856 ASN A C   
1385 O O   . ASN A 175 ? 0.1309 0.2095 0.2882 0.0410  -0.0034 -0.0468 856 ASN A O   
1386 C CB  . ASN A 175 ? 0.0741 0.1665 0.2357 0.0290  -0.0069 -0.0198 856 ASN A CB  
1387 C CG  . ASN A 175 ? 0.0721 0.1616 0.2406 0.0307  -0.0080 -0.0186 856 ASN A CG  
1388 O OD1 . ASN A 175 ? 0.1124 0.1966 0.2853 0.0358  -0.0078 -0.0241 856 ASN A OD1 
1389 N ND2 . ASN A 175 ? 0.0837 0.1773 0.2550 0.0269  -0.0099 -0.0123 856 ASN A ND2 
1390 N N   . SER A 176 ? 0.1606 0.2581 0.3145 0.0387  0.0109  -0.0404 857 SER A N   
1391 C CA  . SER A 176 ? 0.1616 0.2607 0.3146 0.0444  0.0214  -0.0522 857 SER A CA  
1392 C C   . SER A 176 ? 0.2192 0.3197 0.4004 0.0523  0.0220  -0.0570 857 SER A C   
1393 O O   . SER A 176 ? 0.2184 0.3129 0.3989 0.0585  0.0278  -0.0688 857 SER A O   
1394 C CB  . SER A 176 ? 0.2439 0.3548 0.3891 0.0424  0.0361  -0.0515 857 SER A CB  
1395 O OG  . SER A 176 ? 0.2079 0.3334 0.3780 0.0404  0.0399  -0.0442 857 SER A OG  
1396 N N   . LYS A 177 ? 0.1408 0.2405 0.3305 0.0495  0.0145  -0.0447 858 LYS A N   
1397 C CA  . LYS A 177 ? 0.1717 0.2650 0.3715 0.0548  0.0111  -0.0433 858 LYS A CA  
1398 C C   . LYS A 177 ? 0.1213 0.1944 0.3164 0.0550  0.0013  -0.0433 858 LYS A C   
1399 O O   . LYS A 177 ? 0.1475 0.2126 0.3502 0.0600  -0.0016 -0.0416 858 LYS A O   
1400 C CB  . LYS A 177 ? 0.1038 0.2074 0.3122 0.0522  0.0070  -0.0325 858 LYS A CB  
1401 C CG  . LYS A 177 ? 0.1957 0.3210 0.4155 0.0514  0.0172  -0.0329 858 LYS A CG  
1402 C CD  . LYS A 177 ? 0.2134 0.3499 0.4443 0.0491  0.0111  -0.0250 858 LYS A CD  
1403 C CE  . LYS A 177 ? 0.3815 0.5179 0.6033 0.0384  0.0054  -0.0179 858 LYS A CE  
1404 N NZ  . LYS A 177 ? 0.3034 0.4505 0.5263 0.0318  0.0159  -0.0187 858 LYS A NZ  
1405 N N   . GLY A 178 ? 0.1053 0.1710 0.2897 0.0499  -0.0036 -0.0450 859 GLY A N   
1406 C CA  . GLY A 178 ? 0.1078 0.1562 0.2912 0.0484  -0.0117 -0.0447 859 GLY A CA  
1407 C C   . GLY A 178 ? 0.0994 0.1439 0.2801 0.0434  -0.0197 -0.0315 859 GLY A C   
1408 O O   . GLY A 178 ? 0.1053 0.1358 0.2882 0.0431  -0.0248 -0.0294 859 GLY A O   
1409 N N   . GLU A 179 ? 0.0889 0.1442 0.2643 0.0393  -0.0200 -0.0235 860 GLU A N   
1410 C CA  . GLU A 179 ? 0.0831 0.1349 0.2513 0.0340  -0.0264 -0.0141 860 GLU A CA  
1411 C C   . GLU A 179 ? 0.0741 0.1225 0.2293 0.0271  -0.0285 -0.0130 860 GLU A C   
1412 O O   . GLU A 179 ? 0.0700 0.1239 0.2209 0.0262  -0.0258 -0.0168 860 GLU A O   
1413 C CB  . GLU A 179 ? 0.0801 0.1445 0.2499 0.0331  -0.0257 -0.0090 860 GLU A CB  
1414 C CG  . GLU A 179 ? 0.1590 0.2321 0.3445 0.0407  -0.0236 -0.0102 860 GLU A CG  
1415 C CD  . GLU A 179 ? 0.2940 0.3852 0.4865 0.0388  -0.0217 -0.0080 860 GLU A CD  
1416 O OE1 . GLU A 179 ? 0.1052 0.2025 0.2933 0.0329  -0.0179 -0.0081 860 GLU A OE1 
1417 O OE2 . GLU A 179 ? 0.1510 0.2511 0.3557 0.0435  -0.0243 -0.0062 860 GLU A OE2 
1418 N N   . VAL A 180 ? 0.0730 0.1138 0.2230 0.0232  -0.0334 -0.0078 861 VAL A N   
1419 C CA  . VAL A 180 ? 0.0668 0.1053 0.2064 0.0177  -0.0344 -0.0071 861 VAL A CA  
1420 C C   . VAL A 180 ? 0.0608 0.1052 0.1899 0.0150  -0.0327 -0.0035 861 VAL A C   
1421 O O   . VAL A 180 ? 0.0617 0.1074 0.1903 0.0141  -0.0344 0.0006  861 VAL A O   
1422 C CB  . VAL A 180 ? 0.0699 0.0997 0.2120 0.0150  -0.0391 -0.0033 861 VAL A CB  
1423 C CG1 . VAL A 180 ? 0.0640 0.0955 0.1970 0.0098  -0.0385 -0.0029 861 VAL A CG1 
1424 C CG2 . VAL A 180 ? 0.0779 0.0991 0.2353 0.0172  -0.0414 -0.0072 861 VAL A CG2 
1425 N N   . ILE A 181 ? 0.0577 0.1058 0.1805 0.0141  -0.0306 -0.0054 862 ILE A N   
1426 C CA  . ILE A 181 ? 0.0535 0.1046 0.1701 0.0121  -0.0295 -0.0024 862 ILE A CA  
1427 C C   . ILE A 181 ? 0.0964 0.1445 0.2048 0.0104  -0.0305 -0.0022 862 ILE A C   
1428 O O   . ILE A 181 ? 0.0507 0.0987 0.1564 0.0093  -0.0305 -0.0003 862 ILE A O   
1429 C CB  . ILE A 181 ? 0.0563 0.1158 0.1779 0.0141  -0.0266 -0.0032 862 ILE A CB  
1430 C CG1 . ILE A 181 ? 0.1387 0.2012 0.2591 0.0173  -0.0269 -0.0071 862 ILE A CG1 
1431 C CG2 . ILE A 181 ? 0.0743 0.1407 0.2079 0.0161  -0.0238 -0.0041 862 ILE A CG2 
1432 C CD1 . ILE A 181 ? 0.1125 0.1849 0.2392 0.0202  -0.0246 -0.0071 862 ILE A CD1 
1433 N N   . GLY A 182 ? 0.0576 0.1043 0.1654 0.0101  -0.0315 -0.0048 863 GLY A N   
1434 C CA  . GLY A 182 ? 0.0654 0.1138 0.1689 0.0095  -0.0318 -0.0054 863 GLY A CA  
1435 C C   . GLY A 182 ? 0.0547 0.1046 0.1630 0.0079  -0.0330 -0.0091 863 GLY A C   
1436 O O   . GLY A 182 ? 0.0719 0.1182 0.1874 0.0068  -0.0342 -0.0108 863 GLY A O   
1437 N N   . LEU A 183 ? 0.0868 0.1426 0.1944 0.0077  -0.0332 -0.0106 864 LEU A N   
1438 C CA  . LEU A 183 ? 0.0825 0.1432 0.1977 0.0046  -0.0341 -0.0149 864 LEU A CA  
1439 C C   . LEU A 183 ? 0.0573 0.1286 0.1723 0.0068  -0.0358 -0.0174 864 LEU A C   
1440 O O   . LEU A 183 ? 0.0690 0.1426 0.1799 0.0109  -0.0355 -0.0146 864 LEU A O   
1441 C CB  . LEU A 183 ? 0.1266 0.1867 0.2480 -0.0003 -0.0324 -0.0135 864 LEU A CB  
1442 C CG  . LEU A 183 ? 0.1013 0.1680 0.2227 -0.0002 -0.0301 -0.0125 864 LEU A CG  
1443 C CD1 . LEU A 183 ? 0.1314 0.2002 0.2623 -0.0071 -0.0280 -0.0118 864 LEU A CD1 
1444 C CD2 . LEU A 183 ? 0.1054 0.1666 0.2189 0.0036  -0.0302 -0.0091 864 LEU A CD2 
1445 N N   . HIS A 184 ? 0.0620 0.1397 0.1833 0.0043  -0.0385 -0.0230 865 HIS A N   
1446 C CA  . HIS A 184 ? 0.0877 0.1782 0.2115 0.0061  -0.0420 -0.0257 865 HIS A CA  
1447 C C   . HIS A 184 ? 0.0730 0.1723 0.2049 0.0044  -0.0392 -0.0251 865 HIS A C   
1448 O O   . HIS A 184 ? 0.0648 0.1638 0.2038 -0.0019 -0.0354 -0.0261 865 HIS A O   
1449 C CB  . HIS A 184 ? 0.0745 0.1704 0.2043 0.0021  -0.0464 -0.0340 865 HIS A CB  
1450 C CG  . HIS A 184 ? 0.1151 0.2254 0.2463 0.0047  -0.0527 -0.0371 865 HIS A CG  
1451 N ND1 . HIS A 184 ? 0.0886 0.2013 0.2105 0.0112  -0.0587 -0.0369 865 HIS A ND1 
1452 C CD2 . HIS A 184 ? 0.0882 0.2127 0.2301 0.0017  -0.0549 -0.0404 865 HIS A CD2 
1453 C CE1 . HIS A 184 ? 0.0984 0.2251 0.2237 0.0129  -0.0653 -0.0394 865 HIS A CE1 
1454 N NE2 . HIS A 184 ? 0.1092 0.2441 0.2481 0.0071  -0.0631 -0.0419 865 HIS A NE2 
1455 N N   . GLN A 185 ? 0.1173 0.2252 0.2500 0.0105  -0.0412 -0.0235 866 GLN A N   
1456 C CA  . GLN A 185 ? 0.1037 0.2213 0.2468 0.0108  -0.0379 -0.0240 866 GLN A CA  
1457 C C   . GLN A 185 ? 0.1981 0.3338 0.3532 0.0135  -0.0421 -0.0271 866 GLN A C   
1458 O O   . GLN A 185 ? 0.2422 0.3907 0.4116 0.0110  -0.0389 -0.0300 866 GLN A O   
1459 C CB  . GLN A 185 ? 0.0939 0.2047 0.2320 0.0171  -0.0352 -0.0200 866 GLN A CB  
1460 C CG  . GLN A 185 ? 0.0871 0.1850 0.2188 0.0134  -0.0312 -0.0181 866 GLN A CG  
1461 C CD  . GLN A 185 ? 0.0709 0.1618 0.1987 0.0193  -0.0302 -0.0160 866 GLN A CD  
1462 O OE1 . GLN A 185 ? 0.0643 0.1524 0.1878 0.0262  -0.0331 -0.0136 866 GLN A OE1 
1463 N NE2 . GLN A 185 ? 0.0581 0.1465 0.1891 0.0167  -0.0266 -0.0172 866 GLN A NE2 
1464 N N   . ASN A 186 ? 0.1717 0.3103 0.3224 0.0189  -0.0495 -0.0264 867 ASN A N   
1465 C CA  . ASN A 186 ? 0.2442 0.4015 0.4071 0.0224  -0.0557 -0.0290 867 ASN A CA  
1466 C C   . ASN A 186 ? 0.3154 0.4774 0.4745 0.0206  -0.0646 -0.0328 867 ASN A C   
1467 O O   . ASN A 186 ? 0.3479 0.4994 0.4920 0.0237  -0.0679 -0.0307 867 ASN A O   
1468 C CB  . ASN A 186 ? 0.2848 0.4441 0.4482 0.0345  -0.0579 -0.0237 867 ASN A CB  
1469 C CG  . ASN A 186 ? 0.4506 0.6320 0.6318 0.0393  -0.0636 -0.0262 867 ASN A CG  
1470 O OD1 . ASN A 186 ? 0.5914 0.7774 0.7714 0.0486  -0.0719 -0.0228 867 ASN A OD1 
1471 N ND2 . ASN A 186 ? 0.5486 0.7450 0.7476 0.0329  -0.0594 -0.0319 867 ASN A ND2 
1472 N N   . GLY A 187 ? 0.3908 0.5695 0.5640 0.0151  -0.0686 -0.0396 868 GLY A N   
1473 C CA  . GLY A 187 ? 0.3359 0.5221 0.5064 0.0132  -0.0787 -0.0453 868 GLY A CA  
1474 C C   . GLY A 187 ? 0.4260 0.6365 0.6129 0.0158  -0.0870 -0.0481 868 GLY A C   
1475 O O   . GLY A 187 ? 0.4677 0.6895 0.6557 0.0131  -0.0970 -0.0543 868 GLY A O   
1476 N N   . ALA A 188 ? 0.5404 0.7602 0.7409 0.0213  -0.0834 -0.0443 869 ALA A N   
1477 C CA  . ALA A 188 ? 0.6043 0.8500 0.8252 0.0253  -0.0907 -0.0467 869 ALA A CA  
1478 C C   . ALA A 188 ? 0.6237 0.8730 0.8357 0.0376  -0.1035 -0.0418 869 ALA A C   
1479 O O   . ALA A 188 ? 0.5627 0.7941 0.7522 0.0421  -0.1058 -0.0369 869 ALA A O   
1480 C CB  . ALA A 188 ? 0.5661 0.8207 0.8049 0.0289  -0.0818 -0.0449 869 ALA A CB  
1481 N N   . GLU A 189 ? 0.7542 1.0280 0.9851 0.0434  -0.1124 -0.0430 870 GLU A N   
1482 C CA  . GLU A 189 ? 0.7346 1.0141 0.9585 0.0559  -0.1266 -0.0375 870 GLU A CA  
1483 C C   . GLU A 189 ? 0.8072 1.0676 1.0178 0.0693  -0.1235 -0.0261 870 GLU A C   
1484 O O   . GLU A 189 ? 0.7727 1.0295 0.9698 0.0794  -0.1343 -0.0193 870 GLU A O   
1485 C CB  . GLU A 189 ? 0.8810 1.1932 1.1327 0.0602  -0.1364 -0.0406 870 GLU A CB  
1486 C CG  . GLU A 189 ? 0.7729 1.1058 1.0442 0.0451  -0.1367 -0.0525 870 GLU A CG  
1487 C CD  . GLU A 189 ? 0.7601 1.1286 1.0585 0.0485  -0.1498 -0.0563 870 GLU A CD  
1488 O OE1 . GLU A 189 ? 0.7790 1.1619 1.0966 0.0608  -0.1500 -0.0517 870 GLU A OE1 
1489 O OE2 . GLU A 189 ? 0.8086 1.1915 1.1102 0.0392  -0.1604 -0.0645 870 GLU A OE2 
1490 N N   . ASN A 190 ? 0.9147 1.1620 1.1275 0.0694  -0.1095 -0.0239 871 ASN A N   
1491 C CA  . ASN A 190 ? 0.9274 1.1554 1.1293 0.0809  -0.1056 -0.0144 871 ASN A CA  
1492 C C   . ASN A 190 ? 0.8992 1.0999 1.0757 0.0757  -0.0993 -0.0112 871 ASN A C   
1493 O O   . ASN A 190 ? 0.8805 1.0661 1.0536 0.0741  -0.0881 -0.0097 871 ASN A O   
1494 C CB  . ASN A 190 ? 0.7295 0.9615 0.9501 0.0856  -0.0951 -0.0151 871 ASN A CB  
1495 C CG  . ASN A 190 ? 0.8502 1.0785 1.0737 0.0727  -0.0817 -0.0215 871 ASN A CG  
1496 O OD1 . ASN A 190 ? 0.9035 1.1364 1.1268 0.0600  -0.0813 -0.0273 871 ASN A OD1 
1497 N ND2 . ASN A 190 ? 0.6730 0.8920 0.8985 0.0764  -0.0710 -0.0207 871 ASN A ND2 
1498 N N   . ARG A 191 ? 0.8243 1.0207 0.9830 0.0733  -0.1075 -0.0109 872 ARG A N   
1499 C CA  . ARG A 191 ? 0.6434 0.8172 0.7783 0.0711  -0.1041 -0.0072 872 ARG A CA  
1500 C C   . ARG A 191 ? 0.6046 0.7707 0.7383 0.0583  -0.0936 -0.0135 872 ARG A C   
1501 O O   . ARG A 191 ? 0.4641 0.6258 0.6063 0.0548  -0.0832 -0.0141 872 ARG A O   
1502 C CB  . ARG A 191 ? 0.6674 0.8224 0.7940 0.0810  -0.1000 0.0032  872 ARG A CB  
1503 C CG  . ARG A 191 ? 0.8459 0.9997 0.9650 0.0946  -0.1113 0.0124  872 ARG A CG  
1504 C CD  . ARG A 191 ? 1.0093 1.1616 1.1052 0.0943  -0.1220 0.0139  872 ARG A CD  
1505 N NE  . ARG A 191 ? 1.2660 1.4141 1.3492 0.1073  -0.1334 0.0249  872 ARG A NE  
1506 C CZ  . ARG A 191 ? 1.2956 1.4434 1.3551 0.1095  -0.1448 0.0280  872 ARG A CZ  
1507 N NH1 . ARG A 191 ? 1.1326 1.2850 1.1791 0.1000  -0.1461 0.0195  872 ARG A NH1 
1508 N NH2 . ARG A 191 ? 1.1204 1.2622 1.1671 0.1220  -0.1550 0.0401  872 ARG A NH2 
1509 N N   . SER A 192 ? 0.3426 0.5063 0.4642 0.0522  -0.0969 -0.0184 873 SER A N   
1510 C CA  . SER A 192 ? 0.2719 0.4258 0.3911 0.0421  -0.0881 -0.0234 873 SER A CA  
1511 C C   . SER A 192 ? 0.2151 0.3498 0.3227 0.0446  -0.0808 -0.0165 873 SER A C   
1512 O O   . SER A 192 ? 0.1367 0.2638 0.2304 0.0523  -0.0848 -0.0099 873 SER A O   
1513 C CB  . SER A 192 ? 0.1589 0.3165 0.2695 0.0368  -0.0946 -0.0321 873 SER A CB  
1514 O OG  . SER A 192 ? 0.1972 0.3424 0.3027 0.0305  -0.0875 -0.0360 873 SER A OG  
1515 N N   . GLY A 193 ? 0.1988 0.3255 0.3113 0.0380  -0.0708 -0.0175 874 GLY A N   
1516 C CA  . GLY A 193 ? 0.1439 0.2547 0.2476 0.0390  -0.0645 -0.0121 874 GLY A CA  
1517 C C   . GLY A 193 ? 0.1274 0.2318 0.2366 0.0315  -0.0553 -0.0138 874 GLY A C   
1518 O O   . GLY A 193 ? 0.0821 0.1924 0.2000 0.0251  -0.0535 -0.0190 874 GLY A O   
1519 N N   . GLY A 194 ? 0.0803 0.1726 0.1839 0.0323  -0.0503 -0.0094 875 GLY A N   
1520 C CA  . GLY A 194 ? 0.0697 0.1552 0.1754 0.0258  -0.0435 -0.0106 875 GLY A CA  
1521 C C   . GLY A 194 ? 0.0829 0.1576 0.1844 0.0278  -0.0403 -0.0064 875 GLY A C   
1522 O O   . GLY A 194 ? 0.1120 0.1830 0.2102 0.0344  -0.0423 -0.0024 875 GLY A O   
1523 N N   . LEU A 195 ? 0.0604 0.1291 0.1626 0.0221  -0.0363 -0.0073 876 LEU A N   
1524 C CA  . LEU A 195 ? 0.0740 0.1336 0.1752 0.0219  -0.0345 -0.0052 876 LEU A CA  
1525 C C   . LEU A 195 ? 0.0883 0.1420 0.1868 0.0179  -0.0336 -0.0035 876 LEU A C   
1526 O O   . LEU A 195 ? 0.0702 0.1241 0.1690 0.0141  -0.0326 -0.0048 876 LEU A O   
1527 C CB  . LEU A 195 ? 0.0563 0.1170 0.1631 0.0189  -0.0322 -0.0077 876 LEU A CB  
1528 C CG  . LEU A 195 ? 0.0554 0.1084 0.1634 0.0165  -0.0321 -0.0071 876 LEU A CG  
1529 C CD1 . LEU A 195 ? 0.0706 0.1174 0.1818 0.0222  -0.0336 -0.0070 876 LEU A CD1 
1530 C CD2 . LEU A 195 ? 0.0704 0.1282 0.1845 0.0128  -0.0306 -0.0100 876 LEU A CD2 
1531 N N   . ILE A 196 ? 0.0588 0.1074 0.1580 0.0194  -0.0344 -0.0004 877 ILE A N   
1532 C CA  . ILE A 196 ? 0.0554 0.1017 0.1571 0.0152  -0.0332 0.0012  877 ILE A CA  
1533 C C   . ILE A 196 ? 0.0541 0.0961 0.1589 0.0109  -0.0335 0.0010  877 ILE A C   
1534 O O   . ILE A 196 ? 0.0615 0.0994 0.1710 0.0118  -0.0354 0.0013  877 ILE A O   
1535 C CB  . ILE A 196 ? 0.0594 0.1057 0.1663 0.0175  -0.0340 0.0053  877 ILE A CB  
1536 C CG1 . ILE A 196 ? 0.0637 0.1159 0.1665 0.0232  -0.0359 0.0053  877 ILE A CG1 
1537 C CG2 . ILE A 196 ? 0.0560 0.1050 0.1714 0.0121  -0.0317 0.0064  877 ILE A CG2 
1538 C CD1 . ILE A 196 ? 0.0752 0.1340 0.1772 0.0215  -0.0347 0.0001  877 ILE A CD1 
1539 N N   . LEU A 197 ? 0.0519 0.0944 0.1551 0.0074  -0.0330 0.0006  878 LEU A N   
1540 C CA  . LEU A 197 ? 0.0541 0.0951 0.1585 0.0039  -0.0353 0.0006  878 LEU A CA  
1541 C C   . LEU A 197 ? 0.0594 0.0994 0.1699 0.0005  -0.0377 0.0015  878 LEU A C   
1542 O O   . LEU A 197 ? 0.0874 0.1301 0.2022 -0.0004 -0.0365 0.0031  878 LEU A O   
1543 C CB  . LEU A 197 ? 0.0671 0.1091 0.1697 0.0024  -0.0362 0.0019  878 LEU A CB  
1544 C CG  . LEU A 197 ? 0.0525 0.0951 0.1546 0.0032  -0.0350 0.0010  878 LEU A CG  
1545 C CD1 . LEU A 197 ? 0.0548 0.0954 0.1602 0.0028  -0.0368 0.0032  878 LEU A CD1 
1546 C CD2 . LEU A 197 ? 0.0827 0.1282 0.1869 0.0012  -0.0359 -0.0002 878 LEU A CD2 
1547 N N   . SER A 198 ? 0.0603 0.0978 0.1736 -0.0023 -0.0412 -0.0009 879 SER A N   
1548 C CA  . SER A 198 ? 0.0804 0.1157 0.2000 -0.0088 -0.0446 -0.0022 879 SER A CA  
1549 C C   . SER A 198 ? 0.0706 0.1115 0.1863 -0.0133 -0.0474 -0.0017 879 SER A C   
1550 O O   . SER A 198 ? 0.0725 0.1165 0.1819 -0.0112 -0.0487 -0.0002 879 SER A O   
1551 C CB  . SER A 198 ? 0.0789 0.1027 0.1913 -0.0102 -0.0441 -0.0076 879 SER A CB  
1552 O OG  . SER A 198 ? 0.0934 0.1197 0.1979 -0.0130 -0.0471 -0.0110 879 SER A OG  
1553 N N   . PRO A 199 ? 0.0774 0.1201 0.1985 -0.0199 -0.0492 -0.0030 880 PRO A N   
1554 C CA  . PRO A 199 ? 0.0842 0.1353 0.2032 -0.0237 -0.0543 -0.0037 880 PRO A CA  
1555 C C   . PRO A 199 ? 0.0975 0.1469 0.2049 -0.0251 -0.0607 -0.0058 880 PRO A C   
1556 O O   . PRO A 199 ? 0.0945 0.1507 0.1984 -0.0233 -0.0653 -0.0028 880 PRO A O   
1557 C CB  . PRO A 199 ? 0.1159 0.1675 0.2420 -0.0333 -0.0550 -0.0075 880 PRO A CB  
1558 C CG  . PRO A 199 ? 0.0900 0.1361 0.2252 -0.0331 -0.0480 -0.0051 880 PRO A CG  
1559 C CD  . PRO A 199 ? 0.1104 0.1476 0.2411 -0.0255 -0.0466 -0.0037 880 PRO A CD  
1560 N N   . THR A 200 ? 0.1195 0.1589 0.2212 -0.0283 -0.0617 -0.0113 881 THR A N   
1561 C CA  A THR A 200 ? 0.1084 0.1459 0.1968 -0.0310 -0.0677 -0.0146 881 THR A CA  
1562 C CA  B THR A 200 ? 0.1084 0.1459 0.1968 -0.0310 -0.0677 -0.0146 881 THR A CA  
1563 C C   . THR A 200 ? 0.1002 0.1414 0.1858 -0.0246 -0.0658 -0.0083 881 THR A C   
1564 O O   . THR A 200 ? 0.1098 0.1531 0.1843 -0.0259 -0.0712 -0.0050 881 THR A O   
1565 C CB  A THR A 200 ? 0.2003 0.2219 0.2747 -0.0320 -0.0604 -0.0233 881 THR A CB  
1566 C CB  B THR A 200 ? 0.1988 0.2203 0.2733 -0.0321 -0.0604 -0.0234 881 THR A CB  
1567 O OG1 A THR A 200 ? 0.2777 0.2936 0.3597 -0.0244 -0.0515 -0.0221 881 THR A OG1 
1568 O OG1 B THR A 200 ? 0.1603 0.1740 0.2358 -0.0401 -0.0625 -0.0300 881 THR A OG1 
1569 C CG2 A THR A 200 ? 0.1596 0.1731 0.2313 -0.0414 -0.0637 -0.0314 881 THR A CG2 
1570 C CG2 B THR A 200 ? 0.1400 0.1584 0.1925 -0.0335 -0.0599 -0.0272 881 THR A CG2 
1571 N N   . GLN A 201 ? 0.0963 0.1370 0.1903 -0.0183 -0.0585 -0.0065 882 GLN A N   
1572 C CA  . GLN A 201 ? 0.0915 0.1350 0.1848 -0.0144 -0.0559 -0.0022 882 GLN A CA  
1573 C C   . GLN A 201 ? 0.1022 0.1484 0.1966 -0.0121 -0.0583 0.0047  882 GLN A C   
1574 O O   . GLN A 201 ? 0.0845 0.1305 0.1759 -0.0126 -0.0621 0.0097  882 GLN A O   
1575 C CB  . GLN A 201 ? 0.0818 0.1258 0.1839 -0.0087 -0.0486 -0.0036 882 GLN A CB  
1576 C CG  . GLN A 201 ? 0.0767 0.1151 0.1723 -0.0071 -0.0419 -0.0102 882 GLN A CG  
1577 C CD  . GLN A 201 ? 0.0984 0.1393 0.2045 0.0003  -0.0379 -0.0109 882 GLN A CD  
1578 O OE1 . GLN A 201 ? 0.0600 0.1016 0.1734 0.0028  -0.0399 -0.0078 882 GLN A OE1 
1579 N NE2 . GLN A 201 ? 0.0744 0.1184 0.1811 0.0039  -0.0322 -0.0151 882 GLN A NE2 
1580 N N   . LEU A 202 ? 0.1133 0.1610 0.2123 -0.0099 -0.0561 0.0052  883 LEU A N   
1581 C CA  . LEU A 202 ? 0.0955 0.1459 0.1976 -0.0066 -0.0580 0.0096  883 LEU A CA  
1582 C C   . LEU A 202 ? 0.0942 0.1477 0.1914 -0.0087 -0.0684 0.0129  883 LEU A C   
1583 O O   . LEU A 202 ? 0.1210 0.1721 0.2169 -0.0058 -0.0729 0.0191  883 LEU A O   
1584 C CB  . LEU A 202 ? 0.0742 0.1295 0.1846 -0.0051 -0.0542 0.0080  883 LEU A CB  
1585 C CG  . LEU A 202 ? 0.0652 0.1174 0.1777 -0.0023 -0.0461 0.0066  883 LEU A CG  
1586 C CD1 . LEU A 202 ? 0.0976 0.1571 0.2196 -0.0028 -0.0436 0.0057  883 LEU A CD1 
1587 C CD2 . LEU A 202 ? 0.0632 0.1116 0.1750 0.0018  -0.0440 0.0078  883 LEU A CD2 
1588 N N   . ASP A 203 ? 0.1029 0.1606 0.1964 -0.0141 -0.0734 0.0092  884 ASP A N   
1589 C CA  . ASP A 203 ? 0.1182 0.1795 0.2021 -0.0168 -0.0849 0.0114  884 ASP A CA  
1590 C C   . ASP A 203 ? 0.1298 0.1832 0.1969 -0.0188 -0.0903 0.0166  884 ASP A C   
1591 O O   . ASP A 203 ? 0.1468 0.1989 0.2034 -0.0173 -0.0991 0.0242  884 ASP A O   
1592 C CB  . ASP A 203 ? 0.1277 0.1930 0.2075 -0.0247 -0.0890 0.0035  884 ASP A CB  
1593 C CG  . ASP A 203 ? 0.2235 0.3003 0.3192 -0.0253 -0.0878 0.0008  884 ASP A CG  
1594 O OD1 . ASP A 203 ? 0.2016 0.2848 0.3091 -0.0187 -0.0855 0.0051  884 ASP A OD1 
1595 O OD2 . ASP A 203 ? 0.2115 0.2905 0.3079 -0.0333 -0.0889 -0.0063 884 ASP A OD2 
1596 N N   . TRP A 204 ? 0.1247 0.1726 0.1873 -0.0223 -0.0849 0.0131  885 TRP A N   
1597 C CA  . TRP A 204 ? 0.1457 0.1838 0.1856 -0.0241 -0.0796 0.0164  885 TRP A CA  
1598 C C   . TRP A 204 ? 0.1402 0.1742 0.1850 -0.0198 -0.0788 0.0267  885 TRP A C   
1599 O O   . TRP A 204 ? 0.1627 0.1884 0.1886 -0.0212 -0.0817 0.0352  885 TRP A O   
1600 C CB  . TRP A 204 ? 0.1381 0.1721 0.1735 -0.0260 -0.0657 0.0078  885 TRP A CB  
1601 C CG  . TRP A 204 ? 0.1536 0.1815 0.1711 -0.0286 -0.0571 0.0110  885 TRP A CG  
1602 C CD1 . TRP A 204 ? 0.1823 0.2042 0.1708 -0.0341 -0.0567 0.0120  885 TRP A CD1 
1603 C CD2 . TRP A 204 ? 0.1445 0.1724 0.1717 -0.0275 -0.0471 0.0134  885 TRP A CD2 
1604 N NE1 . TRP A 204 ? 0.1917 0.2096 0.1715 -0.0368 -0.0450 0.0158  885 TRP A NE1 
1605 C CE2 . TRP A 204 ? 0.1679 0.1902 0.1732 -0.0333 -0.0394 0.0163  885 TRP A CE2 
1606 C CE3 . TRP A 204 ? 0.1216 0.1545 0.1727 -0.0232 -0.0440 0.0128  885 TRP A CE3 
1607 C CZ2 . TRP A 204 ? 0.1674 0.1900 0.1783 -0.0360 -0.0280 0.0184  885 TRP A CZ2 
1608 C CZ3 . TRP A 204 ? 0.1214 0.1547 0.1770 -0.0254 -0.0347 0.0139  885 TRP A CZ3 
1609 C CH2 . TRP A 204 ? 0.1433 0.1721 0.1809 -0.0323 -0.0266 0.0167  885 TRP A CH2 
1610 N N   . ILE A 205 ? 0.1188 0.1559 0.1864 -0.0149 -0.0748 0.0262  886 ILE A N   
1611 C CA  . ILE A 205 ? 0.1211 0.1510 0.1939 -0.0114 -0.0739 0.0340  886 ILE A CA  
1612 C C   . ILE A 205 ? 0.1359 0.1637 0.2079 -0.0066 -0.0867 0.0437  886 ILE A C   
1613 O O   . ILE A 205 ? 0.1716 0.1860 0.2317 -0.0059 -0.0881 0.0535  886 ILE A O   
1614 C CB  . ILE A 205 ? 0.0986 0.1328 0.1942 -0.0071 -0.0684 0.0293  886 ILE A CB  
1615 C CG1 . ILE A 205 ? 0.0883 0.1249 0.1844 -0.0102 -0.0577 0.0216  886 ILE A CG1 
1616 C CG2 . ILE A 205 ? 0.1051 0.1294 0.2066 -0.0037 -0.0684 0.0354  886 ILE A CG2 
1617 C CD1 . ILE A 205 ? 0.1019 0.1421 0.2098 -0.0056 -0.0519 0.0151  886 ILE A CD1 
1618 N N   . ARG A 206 ? 0.1681 0.2056 0.2479 -0.0033 -0.0895 0.0389  887 ARG A N   
1619 C CA  . ARG A 206 ? 0.1651 0.2030 0.2443 0.0026  -0.0974 0.0447  887 ARG A CA  
1620 C C   . ARG A 206 ? 0.2144 0.2471 0.2689 -0.0003 -0.1091 0.0534  887 ARG A C   
1621 O O   . ARG A 206 ? 0.2744 0.3000 0.3224 0.0055  -0.1157 0.0630  887 ARG A O   
1622 C CB  . ARG A 206 ? 0.1404 0.1936 0.2331 0.0049  -0.0960 0.0367  887 ARG A CB  
1623 C CG  . ARG A 206 ? 0.1470 0.2024 0.2572 0.0094  -0.0859 0.0320  887 ARG A CG  
1624 C CD  . ARG A 206 ? 0.1822 0.2536 0.3052 0.0115  -0.0861 0.0273  887 ARG A CD  
1625 N NE  . ARG A 206 ? 0.1168 0.1944 0.2401 0.0045  -0.0810 0.0202  887 ARG A NE  
1626 C CZ  . ARG A 206 ? 0.1019 0.1791 0.2309 0.0036  -0.0708 0.0157  887 ARG A CZ  
1627 N NH1 . ARG A 206 ? 0.1099 0.1827 0.2441 0.0085  -0.0646 0.0159  887 ARG A NH1 
1628 N NH2 . ARG A 206 ? 0.1791 0.2589 0.3072 -0.0027 -0.0676 0.0111  887 ARG A NH2 
1629 N N   . SER A 207 ? 0.1935 0.2277 0.2302 -0.0090 -0.1112 0.0501  888 SER A N   
1630 C CA  . SER A 207 ? 0.2760 0.3030 0.2796 -0.0133 -0.1208 0.0577  888 SER A CA  
1631 C C   . SER A 207 ? 0.3157 0.3224 0.2993 -0.0140 -0.1145 0.0699  888 SER A C   
1632 O O   . SER A 207 ? 0.3656 0.3617 0.3242 -0.0131 -0.1232 0.0823  888 SER A O   
1633 C CB  . SER A 207 ? 0.2210 0.2507 0.2057 -0.0232 -0.1172 0.0465  888 SER A CB  
1634 O OG  . SER A 207 ? 0.2586 0.2796 0.2369 -0.0274 -0.0989 0.0417  888 SER A OG  
1635 N N   . ILE A 208 ? 0.2508 0.2516 0.2445 -0.0162 -0.0984 0.0663  889 ILE A N   
1636 C CA  . ILE A 208 ? 0.3638 0.3455 0.3441 -0.0189 -0.0893 0.0762  889 ILE A CA  
1637 C C   . ILE A 208 ? 0.3688 0.3389 0.3605 -0.0098 -0.0977 0.0883  889 ILE A C   
1638 O O   . ILE A 208 ? 0.4764 0.4265 0.4470 -0.0099 -0.0997 0.1026  889 ILE A O   
1639 C CB  . ILE A 208 ? 0.2661 0.2496 0.2596 -0.0244 -0.0715 0.0668  889 ILE A CB  
1640 C CG1 . ILE A 208 ? 0.2190 0.2145 0.2062 -0.0299 -0.0638 0.0539  889 ILE A CG1 
1641 C CG2 . ILE A 208 ? 0.2950 0.2605 0.2759 -0.0307 -0.0607 0.0758  889 ILE A CG2 
1642 C CD1 . ILE A 208 ? 0.2834 0.2726 0.2344 -0.0371 -0.0611 0.0564  889 ILE A CD1 
1643 N N   . ILE A 209 ? 0.3267 0.3072 0.3508 -0.0013 -0.1016 0.0829  890 ILE A N   
1644 C CA  . ILE A 209 ? 0.3215 0.2923 0.3592 0.0092  -0.1066 0.0900  890 ILE A CA  
1645 C C   . ILE A 209 ? 0.4190 0.3891 0.4413 0.0156  -0.1172 0.0970  890 ILE A C   
1646 O O   . ILE A 209 ? 0.5758 0.5270 0.5881 0.0212  -0.1190 0.1082  890 ILE A O   
1647 C CB  . ILE A 209 ? 0.2641 0.2510 0.3343 0.0156  -0.1017 0.0760  890 ILE A CB  
1648 C CG1 . ILE A 209 ? 0.1912 0.1763 0.2756 0.0113  -0.0918 0.0698  890 ILE A CG1 
1649 C CG2 . ILE A 209 ? 0.2655 0.2468 0.3461 0.0270  -0.1035 0.0784  890 ILE A CG2 
1650 C CD1 . ILE A 209 ? 0.1731 0.1732 0.2799 0.0153  -0.0849 0.0557  890 ILE A CD1 
1651 N N   . LYS A 210 ? 0.3960 0.3861 0.4163 0.0151  -0.1243 0.0904  891 LYS A N   
1652 C CA  . LYS A 210 ? 0.4699 0.4642 0.4792 0.0220  -0.1360 0.0959  891 LYS A CA  
1653 C C   . LYS A 210 ? 0.4895 0.4667 0.4580 0.0173  -0.1410 0.1089  891 LYS A C   
1654 O O   . LYS A 210 ? 0.7192 0.6982 0.6745 0.0239  -0.1517 0.1152  891 LYS A O   
1655 C CB  . LYS A 210 ? 0.4109 0.4327 0.4330 0.0217  -0.1414 0.0835  891 LYS A CB  
1656 C CG  . LYS A 210 ? 0.4770 0.5150 0.5324 0.0312  -0.1398 0.0768  891 LYS A CG  
1657 C CD  . LYS A 210 ? 0.5353 0.5999 0.6035 0.0288  -0.1435 0.0658  891 LYS A CD  
1658 C CE  . LYS A 210 ? 0.2949 0.3647 0.3706 0.0187  -0.1329 0.0539  891 LYS A CE  
1659 N NZ  . LYS A 210 ? 0.6265 0.7194 0.7178 0.0159  -0.1341 0.0436  891 LYS A NZ  
1660 N N   . GLY A 211 ? 0.5248 0.4865 0.4714 0.0059  -0.1327 0.1132  892 GLY A N   
1661 C CA  . GLY A 211 ? 0.6709 0.6093 0.5772 0.0013  -0.1314 0.1280  892 GLY A CA  
1662 C C   . GLY A 211 ? 0.7827 0.6957 0.6901 0.0073  -0.1265 0.1410  892 GLY A C   
1663 O O   . GLY A 211 ? 0.7857 0.6795 0.6628 0.0080  -0.1273 0.1547  892 GLY A O   
1664 N N   . LYS A 212 ? 0.7412 0.6527 0.6819 0.0117  -0.1208 0.1360  893 LYS A N   
1665 C CA  . LYS A 212 ? 0.7272 0.6134 0.6725 0.0177  -0.1156 0.1448  893 LYS A CA  
1666 C C   . LYS A 212 ? 0.7904 0.6841 0.7556 0.0354  -0.1254 0.1439  893 LYS A C   
1667 O O   . LYS A 212 ? 0.8513 0.7249 0.8221 0.0435  -0.1226 0.1500  893 LYS A O   
1668 C CB  . LYS A 212 ? 0.6239 0.5031 0.5919 0.0113  -0.1027 0.1379  893 LYS A CB  
1669 C CG  . LYS A 212 ? 0.5840 0.4654 0.5420 -0.0056 -0.0928 0.1356  893 LYS A CG  
1670 C CD  . LYS A 212 ? 0.6386 0.4971 0.5578 -0.0181 -0.0835 0.1489  893 LYS A CD  
1671 C CE  . LYS A 212 ? 0.7203 0.5502 0.6424 -0.0219 -0.0711 0.1549  893 LYS A CE  
1672 N NZ  . LYS A 212 ? 0.7836 0.5926 0.6699 -0.0354 -0.0582 0.1669  893 LYS A NZ  
1673 N N   . SER B 2   ? 0.7003 0.7337 0.7350 0.0207  0.0835  -0.0453 -1  SER B N   
1674 C CA  . SER B 2   ? 0.5857 0.6204 0.6173 0.0163  0.0746  -0.0375 -1  SER B CA  
1675 C C   . SER B 2   ? 0.6989 0.7278 0.6997 0.0153  0.0765  -0.0344 -1  SER B C   
1676 O O   . SER B 2   ? 0.4564 0.4848 0.4511 0.0123  0.0694  -0.0282 -1  SER B O   
1677 C CB  . SER B 2   ? 0.7106 0.7545 0.7684 0.0141  0.0784  -0.0323 -1  SER B CB  
1678 O OG  . SER B 2   ? 0.7033 0.7543 0.7887 0.0161  0.0720  -0.0353 -1  SER B OG  
1679 N N   . ASN B 3   ? 1.0127 1.0372 0.9933 0.0191  0.0859  -0.0391 684 ASN B N   
1680 C CA  . ASN B 3   ? 0.8830 0.9023 0.8303 0.0207  0.0865  -0.0370 684 ASN B CA  
1681 C C   . ASN B 3   ? 0.8691 0.8857 0.8047 0.0186  0.0695  -0.0390 684 ASN B C   
1682 O O   . ASN B 3   ? 0.7660 0.7809 0.6821 0.0188  0.0657  -0.0339 684 ASN B O   
1683 C CB  . ASN B 3   ? 0.9496 0.9651 0.8755 0.0267  0.0968  -0.0451 684 ASN B CB  
1684 C CG  . ASN B 3   ? 1.0682 1.0797 0.9584 0.0310  0.1019  -0.0406 684 ASN B CG  
1685 O OD1 . ASN B 3   ? 1.1131 1.1223 0.9830 0.0314  0.0896  -0.0412 684 ASN B OD1 
1686 N ND2 . ASN B 3   ? 0.9535 0.9643 0.8359 0.0350  0.1206  -0.0356 684 ASN B ND2 
1687 N N   . ASN B 4   ? 0.6260 0.6421 0.5754 0.0171  0.0601  -0.0455 685 ASN B N   
1688 C CA  . ASN B 4   ? 0.3936 0.4072 0.3370 0.0148  0.0460  -0.0486 685 ASN B CA  
1689 C C   . ASN B 4   ? 0.3023 0.3187 0.2616 0.0108  0.0373  -0.0409 685 ASN B C   
1690 O O   . ASN B 4   ? 0.2783 0.2930 0.2361 0.0087  0.0271  -0.0422 685 ASN B O   
1691 C CB  . ASN B 4   ? 0.5401 0.5493 0.4897 0.0158  0.0433  -0.0602 685 ASN B CB  
1692 C CG  . ASN B 4   ? 0.6088 0.6185 0.5837 0.0169  0.0484  -0.0603 685 ASN B CG  
1693 O OD1 . ASN B 4   ? 0.6053 0.6202 0.5913 0.0178  0.0560  -0.0546 685 ASN B OD1 
1694 N ND2 . ASN B 4   ? 0.5831 0.5876 0.5695 0.0171  0.0444  -0.0666 685 ASN B ND2 
1695 N N   . VAL B 5   ? 0.1833 0.2043 0.1588 0.0099  0.0412  -0.0338 686 VAL B N   
1696 C CA  . VAL B 5   ? 0.1816 0.2056 0.1713 0.0074  0.0324  -0.0285 686 VAL B CA  
1697 C C   . VAL B 5   ? 0.2040 0.2275 0.1810 0.0050  0.0258  -0.0235 686 VAL B C   
1698 O O   . VAL B 5   ? 0.2150 0.2379 0.1941 0.0036  0.0165  -0.0230 686 VAL B O   
1699 C CB  . VAL B 5   ? 0.2302 0.2609 0.2423 0.0075  0.0367  -0.0251 686 VAL B CB  
1700 C CG1 . VAL B 5   ? 0.1828 0.2171 0.2041 0.0056  0.0273  -0.0203 686 VAL B CG1 
1701 C CG2 . VAL B 5   ? 0.3285 0.3607 0.3573 0.0109  0.0391  -0.0302 686 VAL B CG2 
1702 N N   . PRO B 6   ? 0.2584 0.2814 0.2226 0.0051  0.0307  -0.0188 687 PRO B N   
1703 C CA  . PRO B 6   ? 0.1607 0.1828 0.1136 0.0040  0.0235  -0.0140 687 PRO B CA  
1704 C C   . PRO B 6   ? 0.2014 0.2217 0.1417 0.0044  0.0143  -0.0197 687 PRO B C   
1705 O O   . PRO B 6   ? 0.1963 0.2178 0.1392 0.0025  0.0057  -0.0178 687 PRO B O   
1706 C CB  . PRO B 6   ? 0.2054 0.2251 0.1442 0.0060  0.0327  -0.0077 687 PRO B CB  
1707 C CG  . PRO B 6   ? 0.1839 0.2052 0.1370 0.0060  0.0452  -0.0070 687 PRO B CG  
1708 C CD  . PRO B 6   ? 0.2706 0.2935 0.2319 0.0068  0.0442  -0.0160 687 PRO B CD  
1709 N N   . LYS B 7   ? 0.1824 0.2006 0.1110 0.0067  0.0159  -0.0276 688 LYS B N   
1710 C CA  . LYS B 7   ? 0.2276 0.2452 0.1489 0.0065  0.0064  -0.0355 688 LYS B CA  
1711 C C   . LYS B 7   ? 0.1957 0.2128 0.1371 0.0029  0.0009  -0.0378 688 LYS B C   
1712 O O   . LYS B 7   ? 0.1877 0.2062 0.1321 0.0007  -0.0071 -0.0379 688 LYS B O   
1713 C CB  . LYS B 7   ? 0.2270 0.2423 0.1340 0.0100  0.0091  -0.0463 688 LYS B CB  
1714 C CG  . LYS B 7   ? 0.3526 0.3682 0.2587 0.0090  -0.0016 -0.0576 688 LYS B CG  
1715 C CD  . LYS B 7   ? 0.4285 0.4424 0.3184 0.0132  -0.0006 -0.0708 688 LYS B CD  
1716 C CE  . LYS B 7   ? 0.4291 0.4444 0.3228 0.0114  -0.0127 -0.0842 688 LYS B CE  
1717 N NZ  . LYS B 7   ? 0.5724 0.5870 0.4487 0.0163  -0.0138 -0.0998 688 LYS B NZ  
1718 N N   . ASN B 8   ? 0.1606 0.1758 0.1165 0.0029  0.0059  -0.0390 689 ASN B N   
1719 C CA  . ASN B 8   ? 0.1506 0.1633 0.1231 0.0012  0.0024  -0.0395 689 ASN B CA  
1720 C C   . ASN B 8   ? 0.1616 0.1770 0.1420 0.0001  -0.0012 -0.0302 689 ASN B C   
1721 O O   . ASN B 8   ? 0.1914 0.2045 0.1819 -0.0005 -0.0037 -0.0285 689 ASN B O   
1722 C CB  . ASN B 8   ? 0.2095 0.2186 0.1939 0.0034  0.0085  -0.0427 689 ASN B CB  
1723 C CG  . ASN B 8   ? 0.2495 0.2541 0.2287 0.0043  0.0111  -0.0544 689 ASN B CG  
1724 O OD1 . ASN B 8   ? 0.2794 0.2836 0.2555 0.0073  0.0184  -0.0583 689 ASN B OD1 
1725 N ND2 . ASN B 8   ? 0.3104 0.3121 0.2904 0.0018  0.0052  -0.0613 689 ASN B ND2 
1726 N N   . ALA B 9   ? 0.1477 0.1674 0.1236 0.0002  -0.0009 -0.0242 690 ALA B N   
1727 C CA  . ALA B 9   ? 0.1267 0.1490 0.1083 -0.0005 -0.0052 -0.0176 690 ALA B CA  
1728 C C   . ALA B 9   ? 0.1411 0.1647 0.1143 -0.0022 -0.0106 -0.0159 690 ALA B C   
1729 O O   . ALA B 9   ? 0.1574 0.1828 0.1348 -0.0025 -0.0141 -0.0115 690 ALA B O   
1730 C CB  . ALA B 9   ? 0.1469 0.1730 0.1344 0.0003  -0.0020 -0.0135 690 ALA B CB  
1731 N N   . SER B 10  ? 0.1607 0.1840 0.1219 -0.0022 -0.0118 -0.0199 691 SER B N   
1732 C CA  . SER B 10  ? 0.1593 0.1850 0.1128 -0.0023 -0.0179 -0.0186 691 SER B CA  
1733 C C   . SER B 10  ? 0.1946 0.2213 0.1567 -0.0046 -0.0236 -0.0232 691 SER B C   
1734 O O   . SER B 10  ? 0.2156 0.2415 0.1777 -0.0053 -0.0254 -0.0316 691 SER B O   
1735 C CB  . SER B 10  ? 0.1667 0.1924 0.1016 0.0006  -0.0177 -0.0206 691 SER B CB  
1736 O OG  . SER B 10  ? 0.1978 0.2217 0.1278 0.0023  -0.0095 -0.0147 691 SER B OG  
1737 N N   . ALA B 11  ? 0.1187 0.1470 0.0895 -0.0057 -0.0256 -0.0182 692 ALA B N   
1738 C CA  . ALA B 11  ? 0.1248 0.1539 0.1074 -0.0080 -0.0281 -0.0205 692 ALA B CA  
1739 C C   . ALA B 11  ? 0.1493 0.1843 0.1311 -0.0083 -0.0348 -0.0219 692 ALA B C   
1740 O O   . ALA B 11  ? 0.1515 0.1889 0.1254 -0.0061 -0.0368 -0.0170 692 ALA B O   
1741 C CB  . ALA B 11  ? 0.1537 0.1810 0.1448 -0.0076 -0.0247 -0.0137 692 ALA B CB  
1742 N N   . LEU B 12  ? 0.1382 0.1755 0.1311 -0.0109 -0.0380 -0.0289 693 LEU B N   
1743 C CA  . LEU B 12  ? 0.1375 0.1823 0.1374 -0.0114 -0.0445 -0.0308 693 LEU B CA  
1744 C C   . LEU B 12  ? 0.1255 0.1706 0.1389 -0.0127 -0.0401 -0.0241 693 LEU B C   
1745 O O   . LEU B 12  ? 0.1783 0.2180 0.2003 -0.0144 -0.0332 -0.0216 693 LEU B O   
1746 C CB  . LEU B 12  ? 0.1523 0.2010 0.1631 -0.0139 -0.0502 -0.0432 693 LEU B CB  
1747 C CG  . LEU B 12  ? 0.1274 0.1855 0.1562 -0.0158 -0.0566 -0.0479 693 LEU B CG  
1748 C CD1 . LEU B 12  ? 0.1320 0.1985 0.1478 -0.0107 -0.0671 -0.0494 693 LEU B CD1 
1749 C CD2 . LEU B 12  ? 0.1833 0.2426 0.2329 -0.0206 -0.0585 -0.0608 693 LEU B CD2 
1750 N N   . LEU B 13  ? 0.1469 0.1978 0.1609 -0.0110 -0.0435 -0.0207 694 LEU B N   
1751 C CA  . LEU B 13  ? 0.0966 0.1490 0.1231 -0.0116 -0.0392 -0.0158 694 LEU B CA  
1752 C C   . LEU B 13  ? 0.0981 0.1591 0.1433 -0.0138 -0.0432 -0.0216 694 LEU B C   
1753 O O   . LEU B 13  ? 0.1212 0.1893 0.1645 -0.0121 -0.0525 -0.0266 694 LEU B O   
1754 C CB  . LEU B 13  ? 0.1045 0.1572 0.1215 -0.0077 -0.0388 -0.0086 694 LEU B CB  
1755 C CG  . LEU B 13  ? 0.1139 0.1602 0.1176 -0.0057 -0.0355 -0.0039 694 LEU B CG  
1756 C CD1 . LEU B 13  ? 0.1205 0.1677 0.1206 -0.0025 -0.0358 0.0006  694 LEU B CD1 
1757 C CD2 . LEU B 13  ? 0.1483 0.1891 0.1543 -0.0062 -0.0290 -0.0020 694 LEU B CD2 
1758 N N   . ARG B 14  ? 0.0966 0.1571 0.1608 -0.0170 -0.0360 -0.0207 695 ARG B N   
1759 C CA  . ARG B 14  ? 0.0970 0.1666 0.1858 -0.0197 -0.0372 -0.0255 695 ARG B CA  
1760 C C   . ARG B 14  ? 0.1243 0.1949 0.2186 -0.0178 -0.0290 -0.0170 695 ARG B C   
1761 O O   . ARG B 14  ? 0.1509 0.2134 0.2387 -0.0166 -0.0190 -0.0090 695 ARG B O   
1762 C CB  . ARG B 14  ? 0.1401 0.2077 0.2519 -0.0258 -0.0328 -0.0321 695 ARG B CB  
1763 C CG  . ARG B 14  ? 0.1093 0.1785 0.2206 -0.0277 -0.0424 -0.0445 695 ARG B CG  
1764 C CD  . ARG B 14  ? 0.1621 0.2308 0.3036 -0.0344 -0.0390 -0.0537 695 ARG B CD  
1765 N NE  . ARG B 14  ? 0.2314 0.3038 0.3723 -0.0354 -0.0506 -0.0688 695 ARG B NE  
1766 C CZ  . ARG B 14  ? 0.2868 0.3502 0.4149 -0.0353 -0.0500 -0.0726 695 ARG B CZ  
1767 N NH1 . ARG B 14  ? 0.2183 0.2687 0.3367 -0.0346 -0.0387 -0.0623 695 ARG B NH1 
1768 N NH2 . ARG B 14  ? 0.2582 0.3236 0.3783 -0.0336 -0.0589 -0.0844 695 ARG B NH2 
1769 N N   . MET B 15  ? 0.1234 0.2046 0.2287 -0.0165 -0.0336 -0.0190 696 MET B N   
1770 C CA  . MET B 15  ? 0.1008 0.1840 0.2115 -0.0139 -0.0257 -0.0123 696 MET B CA  
1771 C C   . MET B 15  ? 0.1436 0.2379 0.2867 -0.0170 -0.0240 -0.0172 696 MET B C   
1772 O O   . MET B 15  ? 0.1089 0.2141 0.2646 -0.0175 -0.0354 -0.0258 696 MET B O   
1773 C CB  . MET B 15  ? 0.1347 0.2194 0.2283 -0.0079 -0.0316 -0.0092 696 MET B CB  
1774 C CG  . MET B 15  ? 0.1032 0.1777 0.1697 -0.0054 -0.0324 -0.0049 696 MET B CG  
1775 S SD  . MET B 15  ? 0.1426 0.2169 0.1952 -0.0052 -0.0442 -0.0096 696 MET B SD  
1776 C CE  . MET B 15  ? 0.2664 0.3477 0.3175 0.0004  -0.0529 -0.0089 696 MET B CE  
1777 N N   . ASN B 16  ? 0.1402 0.2321 0.2968 -0.0183 -0.0095 -0.0116 697 ASN B N   
1778 C CA  . ASN B 16  ? 0.1837 0.2861 0.3745 -0.0213 -0.0037 -0.0146 697 ASN B CA  
1779 C C   . ASN B 16  ? 0.1566 0.2612 0.3429 -0.0155 0.0041  -0.0074 697 ASN B C   
1780 O O   . ASN B 16  ? 0.1559 0.2524 0.3343 -0.0133 0.0189  0.0016  697 ASN B O   
1781 C CB  . ASN B 16  ? 0.1977 0.2942 0.4103 -0.0275 0.0100  -0.0131 697 ASN B CB  
1782 C CG  . ASN B 16  ? 0.3920 0.4871 0.6144 -0.0335 0.0019  -0.0231 697 ASN B CG  
1783 O OD1 . ASN B 16  ? 0.4042 0.5111 0.6415 -0.0357 -0.0121 -0.0355 697 ASN B OD1 
1784 N ND2 . ASN B 16  ? 0.4339 0.5147 0.6468 -0.0351 0.0097  -0.0184 697 ASN B ND2 
1785 N N   . PHE B 17  ? 0.1419 0.2570 0.3312 -0.0118 -0.0061 -0.0114 698 PHE B N   
1786 C CA  . PHE B 17  ? 0.1013 0.2190 0.2880 -0.0058 0.0003  -0.0065 698 PHE B CA  
1787 C C   . PHE B 17  ? 0.0905 0.2186 0.3130 -0.0080 0.0113  -0.0077 698 PHE B C   
1788 O O   . PHE B 17  ? 0.1622 0.3039 0.4149 -0.0113 0.0036  -0.0162 698 PHE B O   
1789 C CB  . PHE B 17  ? 0.1442 0.2672 0.3212 -0.0003 -0.0142 -0.0094 698 PHE B CB  
1790 C CG  . PHE B 17  ? 0.1057 0.2191 0.2521 0.0013  -0.0239 -0.0083 698 PHE B CG  
1791 C CD1 . PHE B 17  ? 0.0834 0.1843 0.2038 0.0036  -0.0181 -0.0022 698 PHE B CD1 
1792 C CD2 . PHE B 17  ? 0.1855 0.3030 0.3296 0.0011  -0.0388 -0.0137 698 PHE B CD2 
1793 C CE1 . PHE B 17  ? 0.2464 0.3395 0.3434 0.0045  -0.0258 -0.0014 698 PHE B CE1 
1794 C CE2 . PHE B 17  ? 0.1362 0.2445 0.2529 0.0027  -0.0451 -0.0117 698 PHE B CE2 
1795 C CZ  . PHE B 17  ? 0.2188 0.3151 0.3142 0.0038  -0.0381 -0.0055 698 PHE B CZ  
1796 N N   . VAL B 18  ? 0.0975 0.2201 0.3173 -0.0057 0.0294  0.0005  699 VAL B N   
1797 C CA  . VAL B 18  ? 0.1151 0.2460 0.3690 -0.0078 0.0445  0.0013  699 VAL B CA  
1798 C C   . VAL B 18  ? 0.1972 0.3360 0.4534 -0.0006 0.0475  0.0017  699 VAL B C   
1799 O O   . VAL B 18  ? 0.1567 0.2875 0.3823 0.0066  0.0497  0.0064  699 VAL B O   
1800 C CB  . VAL B 18  ? 0.2334 0.3519 0.4832 -0.0091 0.0658  0.0116  699 VAL B CB  
1801 C CG1 . VAL B 18  ? 0.3017 0.4217 0.5755 -0.0106 0.0806  0.0131  699 VAL B CG1 
1802 C CG2 . VAL B 18  ? 0.1771 0.2871 0.4277 -0.0159 0.0628  0.0107  699 VAL B CG2 
1803 N N   . LYS B 19  ? 0.2348 0.3844 0.5187 -0.0022 0.0452  -0.0043 700 LYS B N   
1804 C CA  . LYS B 19  ? 0.2082 0.3653 0.4973 0.0044  0.0472  -0.0051 700 LYS B CA  
1805 C C   . LYS B 19  ? 0.1231 0.2836 0.4394 0.0007  0.0588  -0.0061 700 LYS B C   
1806 O O   . LYS B 19  ? 0.1485 0.3169 0.4881 -0.0035 0.0487  -0.0140 700 LYS B O   
1807 C CB  . LYS B 19  ? 0.3088 0.4745 0.5977 0.0080  0.0259  -0.0121 700 LYS B CB  
1808 C CG  . LYS B 19  ? 0.2929 0.4602 0.5841 0.0024  0.0086  -0.0188 700 LYS B CG  
1809 C CD  . LYS B 19  ? 0.4960 0.6703 0.7839 0.0072  -0.0107 -0.0242 700 LYS B CD  
1810 C CE  . LYS B 19  ? 0.3734 0.5478 0.6578 0.0030  -0.0261 -0.0307 700 LYS B CE  
1811 N NZ  . LYS B 19  ? 0.5439 0.7239 0.8212 0.0090  -0.0433 -0.0342 700 LYS B NZ  
1812 N N   . GLY B 20  ? 0.2104 0.3640 0.5220 0.0030  0.0797  0.0019  701 GLY B N   
1813 C CA  . GLY B 20  ? 0.2975 0.4502 0.6334 -0.0015 0.0937  0.0032  701 GLY B CA  
1814 C C   . GLY B 20  ? 0.2610 0.4047 0.6053 -0.0098 0.0959  0.0040  701 GLY B C   
1815 O O   . GLY B 20  ? 0.3176 0.4488 0.6395 -0.0096 0.1023  0.0115  701 GLY B O   
1816 N N   . ASN B 21  ? 0.3202 0.4696 0.6968 -0.0165 0.0905  -0.0043 702 ASN B N   
1817 C CA  . ASN B 21  ? 0.2233 0.3650 0.6111 -0.0242 0.0889  -0.0071 702 ASN B CA  
1818 C C   . ASN B 21  ? 0.2292 0.3792 0.6208 -0.0272 0.0645  -0.0196 702 ASN B C   
1819 O O   . ASN B 21  ? 0.2436 0.3912 0.6520 -0.0334 0.0600  -0.0267 702 ASN B O   
1820 C CB  . ASN B 21  ? 0.2388 0.3778 0.6603 -0.0291 0.1025  -0.0079 702 ASN B CB  
1821 C CG  . ASN B 21  ? 0.2427 0.3978 0.6954 -0.0295 0.0953  -0.0180 702 ASN B CG  
1822 O OD1 . ASN B 21  ? 0.3423 0.5103 0.7921 -0.0264 0.0773  -0.0255 702 ASN B OD1 
1823 N ND2 . ASN B 21  ? 0.2071 0.3608 0.6904 -0.0327 0.1098  -0.0177 702 ASN B ND2 
1824 N N   . GLN B 22  ? 0.1393 0.2981 0.5143 -0.0218 0.0492  -0.0225 703 GLN B N   
1825 C CA  . GLN B 22  ? 0.1320 0.2980 0.5040 -0.0222 0.0259  -0.0329 703 GLN B CA  
1826 C C   . GLN B 22  ? 0.2319 0.3898 0.5738 -0.0218 0.0193  -0.0299 703 GLN B C   
1827 O O   . GLN B 22  ? 0.2255 0.3800 0.5452 -0.0169 0.0238  -0.0219 703 GLN B O   
1828 C CB  . GLN B 22  ? 0.2888 0.4676 0.6603 -0.0153 0.0134  -0.0365 703 GLN B CB  
1829 C CG  . GLN B 22  ? 0.3301 0.5159 0.6975 -0.0139 -0.0098 -0.0463 703 GLN B CG  
1830 C CD  . GLN B 22  ? 0.3692 0.5627 0.7678 -0.0182 -0.0151 -0.0573 703 GLN B CD  
1831 O OE1 . GLN B 22  ? 0.4045 0.6051 0.8302 -0.0184 -0.0079 -0.0589 703 GLN B OE1 
1832 N NE2 . GLN B 22  ? 0.4203 0.6123 0.8160 -0.0213 -0.0273 -0.0657 703 GLN B NE2 
1833 N N   . VAL B 23  ? 0.1223 0.2773 0.4640 -0.0263 0.0089  -0.0371 704 VAL B N   
1834 C CA  . VAL B 23  ? 0.1134 0.2614 0.4279 -0.0262 0.0011  -0.0358 704 VAL B CA  
1835 C C   . VAL B 23  ? 0.1190 0.2741 0.4177 -0.0216 -0.0205 -0.0428 704 VAL B C   
1836 O O   . VAL B 23  ? 0.2717 0.4345 0.5830 -0.0216 -0.0315 -0.0521 704 VAL B O   
1837 C CB  . VAL B 23  ? 0.1234 0.2612 0.4437 -0.0331 0.0051  -0.0386 704 VAL B CB  
1838 C CG1 . VAL B 23  ? 0.2023 0.3326 0.4944 -0.0326 -0.0011 -0.0364 704 VAL B CG1 
1839 C CG2 . VAL B 23  ? 0.2302 0.3586 0.5661 -0.0365 0.0278  -0.0301 704 VAL B CG2 
1840 N N   . LEU B 24  ? 0.1203 0.2720 0.3906 -0.0171 -0.0261 -0.0377 705 LEU B N   
1841 C CA  . LEU B 24  ? 0.1825 0.3355 0.4298 -0.0123 -0.0442 -0.0413 705 LEU B CA  
1842 C C   . LEU B 24  ? 0.1590 0.3017 0.3823 -0.0140 -0.0462 -0.0395 705 LEU B C   
1843 O O   . LEU B 24  ? 0.1402 0.2775 0.3521 -0.0129 -0.0392 -0.0319 705 LEU B O   
1844 C CB  . LEU B 24  ? 0.2250 0.3818 0.4603 -0.0040 -0.0486 -0.0361 705 LEU B CB  
1845 C CG  . LEU B 24  ? 0.2862 0.4407 0.4938 0.0018  -0.0640 -0.0361 705 LEU B CG  
1846 C CD1 . LEU B 24  ? 0.2348 0.3962 0.4493 0.0022  -0.0758 -0.0448 705 LEU B CD1 
1847 C CD2 . LEU B 24  ? 0.3795 0.5340 0.5764 0.0098  -0.0652 -0.0292 705 LEU B CD2 
1848 N N   . SER B 25  ? 0.1115 0.2519 0.3285 -0.0162 -0.0553 -0.0471 706 SER B N   
1849 C CA  . SER B 25  ? 0.1776 0.3080 0.3733 -0.0179 -0.0566 -0.0465 706 SER B CA  
1850 C C   . SER B 25  ? 0.1812 0.3086 0.3435 -0.0112 -0.0675 -0.0437 706 SER B C   
1851 O O   . SER B 25  ? 0.2169 0.3491 0.3728 -0.0064 -0.0771 -0.0458 706 SER B O   
1852 C CB  . SER B 25  ? 0.1883 0.3161 0.3939 -0.0233 -0.0586 -0.0564 706 SER B CB  
1853 O OG  . SER B 25  ? 0.4417 0.5670 0.6753 -0.0300 -0.0450 -0.0563 706 SER B OG  
1854 N N   . GLY B 26  ? 0.2018 0.3206 0.3436 -0.0106 -0.0649 -0.0380 707 GLY B N   
1855 C CA  . GLY B 26  ? 0.1275 0.2400 0.2372 -0.0052 -0.0719 -0.0344 707 GLY B CA  
1856 C C   . GLY B 26  ? 0.1137 0.2166 0.2071 -0.0076 -0.0693 -0.0340 707 GLY B C   
1857 O O   . GLY B 26  ? 0.1068 0.2054 0.2099 -0.0124 -0.0605 -0.0335 707 GLY B O   
1858 N N   . THR B 27  ? 0.1118 0.2082 0.1781 -0.0038 -0.0739 -0.0318 708 THR B N   
1859 C CA  . THR B 27  ? 0.1115 0.1990 0.1609 -0.0050 -0.0711 -0.0312 708 THR B CA  
1860 C C   . THR B 27  ? 0.1446 0.2245 0.1695 -0.0002 -0.0697 -0.0218 708 THR B C   
1861 O O   . THR B 27  ? 0.1186 0.1989 0.1366 0.0043  -0.0727 -0.0170 708 THR B O   
1862 C CB  . THR B 27  ? 0.1246 0.2103 0.1680 -0.0064 -0.0753 -0.0398 708 THR B CB  
1863 O OG1 . THR B 27  ? 0.1396 0.2255 0.1652 -0.0009 -0.0818 -0.0387 708 THR B OG1 
1864 C CG2 . THR B 27  ? 0.1623 0.2543 0.2334 -0.0117 -0.0762 -0.0501 708 THR B CG2 
1865 N N   . GLY B 28  ? 0.1084 0.1810 0.1228 -0.0013 -0.0642 -0.0191 709 GLY B N   
1866 C CA  . GLY B 28  ? 0.1135 0.1788 0.1086 0.0022  -0.0617 -0.0115 709 GLY B CA  
1867 C C   . GLY B 28  ? 0.1821 0.2400 0.1657 0.0004  -0.0569 -0.0121 709 GLY B C   
1868 O O   . GLY B 28  ? 0.1391 0.1976 0.1260 -0.0023 -0.0577 -0.0193 709 GLY B O   
1869 N N   . SER B 29  ? 0.1164 0.1675 0.0896 0.0016  -0.0516 -0.0055 710 SER B N   
1870 C CA  . SER B 29  ? 0.1652 0.2104 0.1301 0.0004  -0.0463 -0.0059 710 SER B CA  
1871 C C   . SER B 29  ? 0.1454 0.1863 0.1147 -0.0008 -0.0398 -0.0011 710 SER B C   
1872 O O   . SER B 29  ? 0.1185 0.1596 0.0919 0.0002  -0.0396 0.0027  710 SER B O   
1873 C CB  . SER B 29  ? 0.1561 0.1987 0.1028 0.0043  -0.0466 -0.0039 710 SER B CB  
1874 O OG  . SER B 29  ? 0.1819 0.2290 0.1219 0.0071  -0.0544 -0.0089 710 SER B OG  
1875 N N   . ALA B 30  ? 0.1288 0.1662 0.0975 -0.0023 -0.0352 -0.0025 711 ALA B N   
1876 C CA  . ALA B 30  ? 0.1144 0.1494 0.0878 -0.0025 -0.0309 0.0003  711 ALA B CA  
1877 C C   . ALA B 30  ? 0.1496 0.1818 0.1211 -0.0029 -0.0267 -0.0016 711 ALA B C   
1878 O O   . ALA B 30  ? 0.1504 0.1818 0.1178 -0.0035 -0.0263 -0.0057 711 ALA B O   
1879 C CB  . ALA B 30  ? 0.0900 0.1261 0.0720 -0.0027 -0.0307 0.0005  711 ALA B CB  
1880 N N   . THR B 31  ? 0.1034 0.1350 0.0797 -0.0024 -0.0238 0.0002  712 THR B N   
1881 C CA  . THR B 31  ? 0.1003 0.1308 0.0789 -0.0023 -0.0193 -0.0014 712 THR B CA  
1882 C C   . THR B 31  ? 0.1359 0.1676 0.1236 -0.0007 -0.0199 -0.0019 712 THR B C   
1883 O O   . THR B 31  ? 0.1392 0.1730 0.1306 0.0007  -0.0227 -0.0007 712 THR B O   
1884 C CB  . THR B 31  ? 0.1144 0.1442 0.0931 -0.0025 -0.0148 0.0010  712 THR B CB  
1885 O OG1 . THR B 31  ? 0.2013 0.2290 0.1680 -0.0019 -0.0139 0.0036  712 THR B OG1 
1886 C CG2 . THR B 31  ? 0.1276 0.1576 0.1111 -0.0023 -0.0088 -0.0012 712 THR B CG2 
1887 N N   . PHE B 32  ? 0.1151 0.1452 0.1055 0.0001  -0.0176 -0.0041 713 PHE B N   
1888 C CA  . PHE B 32  ? 0.0964 0.1276 0.0943 0.0036  -0.0185 -0.0037 713 PHE B CA  
1889 C C   . PHE B 32  ? 0.1398 0.1757 0.1464 0.0044  -0.0178 -0.0051 713 PHE B C   
1890 O O   . PHE B 32  ? 0.1486 0.1845 0.1581 0.0031  -0.0128 -0.0069 713 PHE B O   
1891 C CB  . PHE B 32  ? 0.1282 0.1552 0.1285 0.0049  -0.0157 -0.0049 713 PHE B CB  
1892 C CG  . PHE B 32  ? 0.1612 0.1838 0.1604 0.0055  -0.0161 -0.0024 713 PHE B CG  
1893 C CD1 . PHE B 32  ? 0.1974 0.2194 0.1969 0.0103  -0.0172 0.0024  713 PHE B CD1 
1894 C CD2 . PHE B 32  ? 0.1639 0.1833 0.1623 0.0016  -0.0148 -0.0051 713 PHE B CD2 
1895 C CE1 . PHE B 32  ? 0.2102 0.2270 0.2093 0.0110  -0.0147 0.0064  713 PHE B CE1 
1896 C CE2 . PHE B 32  ? 0.1448 0.1603 0.1473 0.0012  -0.0134 -0.0028 713 PHE B CE2 
1897 C CZ  . PHE B 32  ? 0.1692 0.1826 0.1721 0.0057  -0.0121 0.0039  713 PHE B CZ  
1898 N N   . ILE B 33  ? 0.1044 0.1445 0.1160 0.0068  -0.0226 -0.0053 714 ILE B N   
1899 C CA  . ILE B 33  ? 0.0987 0.1448 0.1242 0.0074  -0.0233 -0.0088 714 ILE B CA  
1900 C C   . ILE B 33  ? 0.1629 0.2140 0.1952 0.0136  -0.0291 -0.0110 714 ILE B C   
1901 O O   . ILE B 33  ? 0.1660 0.2245 0.2133 0.0149  -0.0321 -0.0158 714 ILE B O   
1902 C CB  . ILE B 33  ? 0.0835 0.1311 0.1130 0.0048  -0.0249 -0.0097 714 ILE B CB  
1903 C CG1 . ILE B 33  ? 0.0827 0.1307 0.1048 0.0078  -0.0316 -0.0097 714 ILE B CG1 
1904 C CG2 . ILE B 33  ? 0.1074 0.1498 0.1304 0.0003  -0.0185 -0.0061 714 ILE B CG2 
1905 C CD1 . ILE B 33  ? 0.1422 0.1914 0.1706 0.0061  -0.0338 -0.0124 714 ILE B CD1 
1906 N N   . ALA B 34  ? 0.1071 0.1547 0.1300 0.0181  -0.0306 -0.0077 715 ALA B N   
1907 C CA  . ALA B 34  ? 0.1634 0.2138 0.1885 0.0262  -0.0355 -0.0075 715 ALA B CA  
1908 C C   . ALA B 34  ? 0.1016 0.1430 0.1182 0.0282  -0.0310 -0.0017 715 ALA B C   
1909 O O   . ALA B 34  ? 0.1736 0.2087 0.1842 0.0230  -0.0260 0.0003  715 ALA B O   
1910 C CB  . ALA B 34  ? 0.1288 0.1837 0.1479 0.0320  -0.0438 -0.0086 715 ALA B CB  
1911 N N   . PRO B 35  ? 0.1292 0.1700 0.1472 0.0361  -0.0328 0.0008  716 PRO B N   
1912 C CA  . PRO B 35  ? 0.1464 0.1764 0.1590 0.0379  -0.0270 0.0071  716 PRO B CA  
1913 C C   . PRO B 35  ? 0.1697 0.1933 0.1701 0.0366  -0.0243 0.0127  716 PRO B C   
1914 O O   . PRO B 35  ? 0.1693 0.1839 0.1702 0.0336  -0.0176 0.0158  716 PRO B O   
1915 C CB  . PRO B 35  ? 0.1783 0.2088 0.1926 0.0492  -0.0307 0.0105  716 PRO B CB  
1916 C CG  . PRO B 35  ? 0.1871 0.2299 0.2150 0.0506  -0.0369 0.0029  716 PRO B CG  
1917 C CD  . PRO B 35  ? 0.1127 0.1622 0.1414 0.0433  -0.0393 -0.0027 716 PRO B CD  
1918 N N   . ASN B 36  ? 0.1460 0.1742 0.1378 0.0383  -0.0288 0.0129  717 ASN B N   
1919 C CA  . ASN B 36  ? 0.1849 0.2082 0.1662 0.0382  -0.0252 0.0184  717 ASN B CA  
1920 C C   . ASN B 36  ? 0.1356 0.1649 0.1134 0.0346  -0.0287 0.0143  717 ASN B C   
1921 O O   . ASN B 36  ? 0.1640 0.1929 0.1316 0.0384  -0.0284 0.0175  717 ASN B O   
1922 C CB  . ASN B 36  ? 0.1859 0.2054 0.1553 0.0494  -0.0248 0.0265  717 ASN B CB  
1923 C CG  . ASN B 36  ? 0.2467 0.2754 0.2088 0.0582  -0.0350 0.0230  717 ASN B CG  
1924 O OD1 . ASN B 36  ? 0.2602 0.2978 0.2324 0.0560  -0.0419 0.0144  717 ASN B OD1 
1925 N ND2 . ASN B 36  ? 0.2915 0.3182 0.2368 0.0681  -0.0353 0.0290  717 ASN B ND2 
1926 N N   . VAL B 37  ? 0.1481 0.1820 0.1340 0.0280  -0.0308 0.0080  718 VAL B N   
1927 C CA  . VAL B 37  ? 0.1141 0.1523 0.0990 0.0249  -0.0337 0.0044  718 VAL B CA  
1928 C C   . VAL B 37  ? 0.1352 0.1722 0.1252 0.0165  -0.0306 0.0027  718 VAL B C   
1929 O O   . VAL B 37  ? 0.0986 0.1354 0.0947 0.0136  -0.0288 0.0006  718 VAL B O   
1930 C CB  . VAL B 37  ? 0.1506 0.1965 0.1408 0.0281  -0.0411 -0.0020 718 VAL B CB  
1931 C CG1 . VAL B 37  ? 0.1801 0.2283 0.1729 0.0240  -0.0428 -0.0061 718 VAL B CG1 
1932 C CG2 . VAL B 37  ? 0.1765 0.2251 0.1577 0.0386  -0.0466 -0.0015 718 VAL B CG2 
1933 N N   . LEU B 38  ? 0.1019 0.1381 0.0884 0.0137  -0.0298 0.0037  719 LEU B N   
1934 C CA  . LEU B 38  ? 0.1033 0.1388 0.0916 0.0078  -0.0283 0.0028  719 LEU B CA  
1935 C C   . LEU B 38  ? 0.0843 0.1221 0.0740 0.0069  -0.0308 0.0011  719 LEU B C   
1936 O O   . LEU B 38  ? 0.1467 0.1862 0.1348 0.0099  -0.0332 0.0004  719 LEU B O   
1937 C CB  . LEU B 38  ? 0.1285 0.1617 0.1152 0.0056  -0.0259 0.0049  719 LEU B CB  
1938 C CG  . LEU B 38  ? 0.1410 0.1701 0.1305 0.0047  -0.0223 0.0054  719 LEU B CG  
1939 C CD1 . LEU B 38  ? 0.1353 0.1633 0.1285 0.0028  -0.0198 0.0070  719 LEU B CD1 
1940 C CD2 . LEU B 38  ? 0.1381 0.1664 0.1286 0.0013  -0.0220 0.0014  719 LEU B CD2 
1941 N N   . LEU B 39  ? 0.0826 0.1196 0.0746 0.0034  -0.0294 0.0007  720 LEU B N   
1942 C CA  . LEU B 39  ? 0.1124 0.1490 0.1069 0.0023  -0.0300 0.0009  720 LEU B CA  
1943 C C   . LEU B 39  ? 0.1306 0.1653 0.1190 0.0009  -0.0295 0.0040  720 LEU B C   
1944 O O   . LEU B 39  ? 0.1131 0.1467 0.0964 -0.0004 -0.0280 0.0047  720 LEU B O   
1945 C CB  . LEU B 39  ? 0.1230 0.1592 0.1257 0.0004  -0.0271 -0.0002 720 LEU B CB  
1946 C CG  . LEU B 39  ? 0.1744 0.2078 0.1829 -0.0010 -0.0257 0.0010  720 LEU B CG  
1947 C CD1 . LEU B 39  ? 0.1482 0.1840 0.1650 0.0008  -0.0304 -0.0042 720 LEU B CD1 
1948 C CD2 . LEU B 39  ? 0.2091 0.2404 0.2256 -0.0036 -0.0191 0.0024  720 LEU B CD2 
1949 N N   . THR B 40  ? 0.1089 0.1437 0.0979 0.0021  -0.0315 0.0049  721 THR B N   
1950 C CA  . THR B 40  ? 0.1166 0.1513 0.1018 0.0022  -0.0328 0.0075  721 THR B CA  
1951 C C   . THR B 40  ? 0.1025 0.1356 0.0915 0.0040  -0.0338 0.0089  721 THR B C   
1952 O O   . THR B 40  ? 0.0998 0.1312 0.0950 0.0043  -0.0331 0.0068  721 THR B O   
1953 C CB  . THR B 40  ? 0.1013 0.1396 0.0863 0.0021  -0.0343 0.0065  721 THR B CB  
1954 O OG1 . THR B 40  ? 0.1526 0.1929 0.1362 0.0024  -0.0373 0.0073  721 THR B OG1 
1955 C CG2 . THR B 40  ? 0.0991 0.1393 0.0880 0.0042  -0.0338 0.0059  721 THR B CG2 
1956 N N   . VAL B 41  ? 0.1226 0.1566 0.1099 0.0056  -0.0360 0.0114  722 VAL B N   
1957 C CA  . VAL B 41  ? 0.1689 0.2008 0.1610 0.0083  -0.0368 0.0130  722 VAL B CA  
1958 C C   . VAL B 41  ? 0.1057 0.1425 0.1028 0.0100  -0.0382 0.0100  722 VAL B C   
1959 O O   . VAL B 41  ? 0.0915 0.1334 0.0887 0.0094  -0.0386 0.0089  722 VAL B O   
1960 C CB  . VAL B 41  ? 0.1373 0.1673 0.1246 0.0110  -0.0386 0.0186  722 VAL B CB  
1961 C CG1 . VAL B 41  ? 0.2298 0.2527 0.2107 0.0106  -0.0343 0.0234  722 VAL B CG1 
1962 C CG2 . VAL B 41  ? 0.1547 0.1916 0.1378 0.0117  -0.0434 0.0173  722 VAL B CG2 
1963 N N   . ALA B 42  ? 0.1022 0.1369 0.1051 0.0124  -0.0378 0.0083  723 ALA B N   
1964 C CA  . ALA B 42  ? 0.1121 0.1509 0.1185 0.0152  -0.0374 0.0053  723 ALA B CA  
1965 C C   . ALA B 42  ? 0.1372 0.1813 0.1481 0.0167  -0.0389 0.0078  723 ALA B C   
1966 O O   . ALA B 42  ? 0.1594 0.2091 0.1743 0.0176  -0.0369 0.0062  723 ALA B O   
1967 C CB  . ALA B 42  ? 0.2075 0.2424 0.2193 0.0180  -0.0369 0.0014  723 ALA B CB  
1968 N N   . HIS B 43  ? 0.1666 0.2094 0.1774 0.0178  -0.0423 0.0118  724 HIS B N   
1969 C CA  . HIS B 43  ? 0.1485 0.1980 0.1660 0.0207  -0.0459 0.0128  724 HIS B CA  
1970 C C   . HIS B 43  ? 0.1634 0.2209 0.1825 0.0180  -0.0482 0.0108  724 HIS B C   
1971 O O   . HIS B 43  ? 0.1590 0.2246 0.1879 0.0198  -0.0520 0.0097  724 HIS B O   
1972 C CB  . HIS B 43  ? 0.1975 0.2427 0.2129 0.0251  -0.0497 0.0183  724 HIS B CB  
1973 C CG  . HIS B 43  ? 0.1800 0.2241 0.1833 0.0249  -0.0531 0.0219  724 HIS B CG  
1974 N ND1 . HIS B 43  ? 0.2470 0.2812 0.2405 0.0254  -0.0501 0.0274  724 HIS B ND1 
1975 C CD2 . HIS B 43  ? 0.2553 0.3069 0.2549 0.0251  -0.0588 0.0202  724 HIS B CD2 
1976 C CE1 . HIS B 43  ? 0.2598 0.2952 0.2406 0.0265  -0.0531 0.0297  724 HIS B CE1 
1977 N NE2 . HIS B 43  ? 0.2410 0.2871 0.2249 0.0265  -0.0595 0.0245  724 HIS B NE2 
1978 N N   . ASN B 44  ? 0.1784 0.2344 0.1912 0.0137  -0.0461 0.0094  725 ASN B N   
1979 C CA  . ASN B 44  ? 0.2200 0.2822 0.2387 0.0105  -0.0463 0.0063  725 ASN B CA  
1980 C C   . ASN B 44  ? 0.1976 0.2641 0.2281 0.0102  -0.0406 0.0050  725 ASN B C   
1981 O O   . ASN B 44  ? 0.1234 0.1961 0.1658 0.0077  -0.0397 0.0026  725 ASN B O   
1982 C CB  . ASN B 44  ? 0.1663 0.2241 0.1762 0.0067  -0.0445 0.0054  725 ASN B CB  
1983 C CG  . ASN B 44  ? 0.1758 0.2318 0.1753 0.0070  -0.0492 0.0057  725 ASN B CG  
1984 O OD1 . ASN B 44  ? 0.1636 0.2243 0.1634 0.0095  -0.0555 0.0049  725 ASN B OD1 
1985 N ND2 . ASN B 44  ? 0.1465 0.1962 0.1363 0.0054  -0.0461 0.0067  725 ASN B ND2 
1986 N N   . PHE B 45  ? 0.1351 0.1986 0.1636 0.0131  -0.0361 0.0059  726 PHE B N   
1987 C CA  . PHE B 45  ? 0.1194 0.1858 0.1541 0.0142  -0.0285 0.0056  726 PHE B CA  
1988 C C   . PHE B 45  ? 0.1007 0.1696 0.1418 0.0191  -0.0266 0.0048  726 PHE B C   
1989 O O   . PHE B 45  ? 0.1259 0.1999 0.1768 0.0204  -0.0200 0.0046  726 PHE B O   
1990 C CB  . PHE B 45  ? 0.1652 0.2254 0.1871 0.0146  -0.0235 0.0066  726 PHE B CB  
1991 C CG  . PHE B 45  ? 0.1122 0.1693 0.1293 0.0106  -0.0247 0.0073  726 PHE B CG  
1992 C CD1 . PHE B 45  ? 0.1379 0.1972 0.1639 0.0071  -0.0215 0.0078  726 PHE B CD1 
1993 C CD2 . PHE B 45  ? 0.1368 0.1888 0.1434 0.0101  -0.0282 0.0069  726 PHE B CD2 
1994 C CE1 . PHE B 45  ? 0.1659 0.2215 0.1885 0.0038  -0.0223 0.0075  726 PHE B CE1 
1995 C CE2 . PHE B 45  ? 0.1592 0.2086 0.1624 0.0070  -0.0286 0.0071  726 PHE B CE2 
1996 C CZ  . PHE B 45  ? 0.1788 0.2296 0.1889 0.0042  -0.0258 0.0073  726 PHE B CZ  
1997 N N   . ILE B 46  ? 0.1145 0.1793 0.1518 0.0221  -0.0308 0.0044  727 ILE B N   
1998 C CA  . ILE B 46  ? 0.1819 0.2474 0.2253 0.0272  -0.0284 0.0025  727 ILE B CA  
1999 C C   . ILE B 46  ? 0.2134 0.2793 0.2649 0.0300  -0.0347 0.0040  727 ILE B C   
2000 O O   . ILE B 46  ? 0.1777 0.2398 0.2239 0.0289  -0.0405 0.0070  727 ILE B O   
2001 C CB  . ILE B 46  ? 0.1744 0.2324 0.2066 0.0299  -0.0259 -0.0009 727 ILE B CB  
2002 C CG1 . ILE B 46  ? 0.1379 0.1881 0.1644 0.0280  -0.0313 -0.0008 727 ILE B CG1 
2003 C CG2 . ILE B 46  ? 0.1572 0.2156 0.1790 0.0300  -0.0199 -0.0015 727 ILE B CG2 
2004 C CD1 . ILE B 46  ? 0.1248 0.1691 0.1465 0.0302  -0.0307 -0.0067 727 ILE B CD1 
2005 N N   . ASN B 47  ? 0.1319 0.2021 0.1956 0.0347  -0.0326 0.0024  728 ASN B N   
2006 C CA  . ASN B 47  ? 0.2055 0.2755 0.2783 0.0396  -0.0378 0.0042  728 ASN B CA  
2007 C C   . ASN B 47  ? 0.1084 0.1725 0.1839 0.0446  -0.0334 0.0008  728 ASN B C   
2008 O O   . ASN B 47  ? 0.1301 0.1924 0.2000 0.0448  -0.0270 -0.0039 728 ASN B O   
2009 C CB  . ASN B 47  ? 0.1341 0.2174 0.2252 0.0415  -0.0408 0.0041  728 ASN B CB  
2010 C CG  . ASN B 47  ? 0.2501 0.3385 0.3398 0.0386  -0.0493 0.0059  728 ASN B CG  
2011 O OD1 . ASN B 47  ? 0.5030 0.5839 0.5774 0.0375  -0.0537 0.0092  728 ASN B OD1 
2012 N ND2 . ASN B 47  ? 0.2921 0.3939 0.3992 0.0375  -0.0512 0.0029  728 ASN B ND2 
2013 N N   . ASN B 48  ? 0.1408 0.2015 0.2245 0.0498  -0.0371 0.0030  729 ASN B N   
2014 C CA  . ASN B 48  ? 0.1290 0.1842 0.2193 0.0550  -0.0328 -0.0015 729 ASN B CA  
2015 C C   . ASN B 48  ? 0.1544 0.2205 0.2578 0.0589  -0.0270 -0.0056 729 ASN B C   
2016 O O   . ASN B 48  ? 0.1186 0.1962 0.2355 0.0600  -0.0291 -0.0033 729 ASN B O   
2017 C CB  . ASN B 48  ? 0.1459 0.1925 0.2431 0.0601  -0.0372 0.0033  729 ASN B CB  
2018 C CG  . ASN B 48  ? 0.2055 0.2402 0.2909 0.0567  -0.0401 0.0088  729 ASN B CG  
2019 O OD1 . ASN B 48  ? 0.3319 0.3631 0.4066 0.0507  -0.0382 0.0061  729 ASN B OD1 
2020 N ND2 . ASN B 48  ? 0.2625 0.2911 0.3503 0.0611  -0.0440 0.0172  729 ASN B ND2 
2021 N N   . SER B 49  ? 0.1882 0.2514 0.2882 0.0614  -0.0195 -0.0127 730 SER B N   
2022 C CA  . SER B 49  ? 0.1696 0.2417 0.2807 0.0661  -0.0112 -0.0166 730 SER B CA  
2023 C C   . SER B 49  ? 0.1651 0.2396 0.2972 0.0729  -0.0133 -0.0162 730 SER B C   
2024 O O   . SER B 49  ? 0.1389 0.2050 0.2737 0.0751  -0.0202 -0.0131 730 SER B O   
2025 C CB  . SER B 49  ? 0.1937 0.2606 0.2917 0.0692  -0.0032 -0.0249 730 SER B CB  
2026 O OG  . SER B 49  ? 0.1674 0.2230 0.2656 0.0726  -0.0062 -0.0307 730 SER B OG  
2027 N N   . ALA B 50  ? 0.1606 0.2463 0.3084 0.0770  -0.0061 -0.0188 731 ALA B N   
2028 C CA  . ALA B 50  ? 0.1413 0.2321 0.3126 0.0843  -0.0081 -0.0185 731 ALA B CA  
2029 C C   . ALA B 50  ? 0.1525 0.2291 0.3233 0.0904  -0.0089 -0.0221 731 ALA B C   
2030 O O   . ALA B 50  ? 0.1565 0.2301 0.3400 0.0954  -0.0156 -0.0179 731 ALA B O   
2031 C CB  . ALA B 50  ? 0.1428 0.2478 0.3325 0.0877  0.0028  -0.0223 731 ALA B CB  
2032 N N   . ASP B 51  ? 0.1645 0.2320 0.3213 0.0907  -0.0023 -0.0302 732 ASP B N   
2033 C CA  . ASP B 51  ? 0.1720 0.2253 0.3310 0.0957  -0.0026 -0.0362 732 ASP B CA  
2034 C C   . ASP B 51  ? 0.1722 0.2106 0.3191 0.0905  -0.0094 -0.0345 732 ASP B C   
2035 O O   . ASP B 51  ? 0.1831 0.2082 0.3334 0.0930  -0.0092 -0.0406 732 ASP B O   
2036 C CB  . ASP B 51  ? 0.1881 0.2404 0.3410 0.1004  0.0077  -0.0490 732 ASP B CB  
2037 C CG  . ASP B 51  ? 0.1916 0.2419 0.3184 0.0959  0.0098  -0.0541 732 ASP B CG  
2038 O OD1 . ASP B 51  ? 0.1746 0.2241 0.2898 0.0884  0.0040  -0.0480 732 ASP B OD1 
2039 O OD2 . ASP B 51  ? 0.3366 0.3862 0.4534 0.1010  0.0171  -0.0648 732 ASP B OD2 
2040 N N   . ASN B 52  ? 0.1616 0.2019 0.2969 0.0831  -0.0147 -0.0269 733 ASN B N   
2041 C CA  . ASN B 52  ? 0.1612 0.1892 0.2871 0.0778  -0.0201 -0.0234 733 ASN B CA  
2042 C C   . ASN B 52  ? 0.1839 0.2039 0.2989 0.0749  -0.0179 -0.0343 733 ASN B C   
2043 O O   . ASN B 52  ? 0.1681 0.1770 0.2815 0.0709  -0.0210 -0.0338 733 ASN B O   
2044 C CB  . ASN B 52  ? 0.2199 0.2364 0.3585 0.0818  -0.0238 -0.0164 733 ASN B CB  
2045 C CG  . ASN B 52  ? 0.1925 0.1987 0.3224 0.0763  -0.0279 -0.0082 733 ASN B CG  
2046 O OD1 . ASN B 52  ? 0.2435 0.2560 0.3633 0.0725  -0.0319 -0.0005 733 ASN B OD1 
2047 N ND2 . ASN B 52  ? 0.2150 0.2049 0.3504 0.0759  -0.0259 -0.0104 733 ASN B ND2 
2048 N N   . SER B 53  ? 0.1700 0.1957 0.2775 0.0776  -0.0124 -0.0444 734 SER B N   
2049 C CA  . SER B 53  ? 0.1823 0.2019 0.2786 0.0771  -0.0123 -0.0569 734 SER B CA  
2050 C C   . SER B 53  ? 0.1957 0.2181 0.2741 0.0705  -0.0157 -0.0553 734 SER B C   
2051 O O   . SER B 53  ? 0.1974 0.2145 0.2694 0.0690  -0.0189 -0.0647 734 SER B O   
2052 C CB  . SER B 53  ? 0.1974 0.2220 0.2880 0.0847  -0.0052 -0.0684 734 SER B CB  
2053 O OG  . SER B 53  ? 0.1998 0.2365 0.2775 0.0850  0.0004  -0.0638 734 SER B OG  
2054 N N   . THR B 54  ? 0.1830 0.2137 0.2554 0.0668  -0.0156 -0.0447 735 THR B N   
2055 C CA  . THR B 54  ? 0.1526 0.1861 0.2086 0.0617  -0.0177 -0.0432 735 THR B CA  
2056 C C   . THR B 54  ? 0.1938 0.2333 0.2508 0.0567  -0.0189 -0.0307 735 THR B C   
2057 O O   . THR B 54  ? 0.1361 0.1811 0.2046 0.0582  -0.0177 -0.0251 735 THR B O   
2058 C CB  . THR B 54  ? 0.1662 0.2055 0.2050 0.0662  -0.0125 -0.0498 735 THR B CB  
2059 O OG1 . THR B 54  ? 0.1600 0.2013 0.1833 0.0622  -0.0149 -0.0467 735 THR B OG1 
2060 C CG2 . THR B 54  ? 0.1666 0.2148 0.2086 0.0702  -0.0035 -0.0454 735 THR B CG2 
2061 N N   . GLY B 55  ? 0.1965 0.2354 0.2429 0.0511  -0.0222 -0.0278 736 GLY B N   
2062 C CA  . GLY B 55  ? 0.1991 0.2446 0.2431 0.0468  -0.0223 -0.0190 736 GLY B CA  
2063 C C   . GLY B 55  ? 0.1418 0.1957 0.1808 0.0490  -0.0151 -0.0188 736 GLY B C   
2064 O O   . GLY B 55  ? 0.1845 0.2382 0.2130 0.0534  -0.0104 -0.0246 736 GLY B O   
2065 N N   . GLU B 56  ? 0.1581 0.2193 0.2054 0.0462  -0.0137 -0.0123 737 GLU B N   
2066 C CA  . GLU B 56  ? 0.1214 0.1903 0.1706 0.0474  -0.0047 -0.0106 737 GLU B CA  
2067 C C   . GLU B 56  ? 0.1100 0.1835 0.1640 0.0409  -0.0061 -0.0046 737 GLU B C   
2068 O O   . GLU B 56  ? 0.1335 0.2082 0.1952 0.0376  -0.0141 -0.0025 737 GLU B O   
2069 C CB  . GLU B 56  ? 0.1319 0.2074 0.1987 0.0522  0.0004  -0.0122 737 GLU B CB  
2070 C CG  . GLU B 56  ? 0.3106 0.3950 0.3852 0.0529  0.0122  -0.0097 737 GLU B CG  
2071 C CD  . GLU B 56  ? 0.2808 0.3736 0.3775 0.0575  0.0174  -0.0116 737 GLU B CD  
2072 O OE1 . GLU B 56  ? 0.2187 0.3083 0.3180 0.0628  0.0149  -0.0163 737 GLU B OE1 
2073 O OE2 . GLU B 56  ? 0.5604 0.6630 0.6745 0.0557  0.0247  -0.0087 737 GLU B OE2 
2074 N N   . PHE B 57  ? 0.1236 0.1990 0.1725 0.0398  0.0021  -0.0019 738 PHE B N   
2075 C CA  . PHE B 57  ? 0.1732 0.2514 0.2283 0.0333  0.0015  0.0025  738 PHE B CA  
2076 C C   . PHE B 57  ? 0.1066 0.1951 0.1873 0.0308  0.0002  0.0026  738 PHE B C   
2077 O O   . PHE B 57  ? 0.1487 0.2440 0.2443 0.0341  0.0067  0.0016  738 PHE B O   
2078 C CB  . PHE B 57  ? 0.1723 0.2485 0.2184 0.0336  0.0125  0.0064  738 PHE B CB  
2079 C CG  . PHE B 57  ? 0.1903 0.2582 0.2146 0.0334  0.0092  0.0075  738 PHE B CG  
2080 C CD1 . PHE B 57  ? 0.2421 0.3052 0.2466 0.0398  0.0093  0.0045  738 PHE B CD1 
2081 C CD2 . PHE B 57  ? 0.1576 0.2236 0.1829 0.0275  0.0055  0.0102  738 PHE B CD2 
2082 C CE1 . PHE B 57  ? 0.1899 0.2474 0.1774 0.0404  0.0049  0.0046  738 PHE B CE1 
2083 C CE2 . PHE B 57  ? 0.2681 0.3274 0.2761 0.0279  0.0025  0.0110  738 PHE B CE2 
2084 C CZ  . PHE B 57  ? 0.1712 0.2270 0.1612 0.0344  0.0019  0.0084  738 PHE B CZ  
2085 N N   . ILE B 58  ? 0.0931 0.1835 0.1791 0.0258  -0.0090 0.0028  739 ILE B N   
2086 C CA  . ILE B 58  ? 0.1514 0.2532 0.2619 0.0231  -0.0122 0.0012  739 ILE B CA  
2087 C C   . ILE B 58  ? 0.1177 0.2234 0.2419 0.0193  -0.0005 0.0024  739 ILE B C   
2088 O O   . ILE B 58  ? 0.1169 0.2155 0.2298 0.0162  0.0045  0.0053  739 ILE B O   
2089 C CB  . ILE B 58  ? 0.1449 0.2470 0.2527 0.0198  -0.0252 0.0000  739 ILE B CB  
2090 C CG1 . ILE B 58  ? 0.0966 0.1912 0.1877 0.0237  -0.0332 0.0014  739 ILE B CG1 
2091 C CG2 . ILE B 58  ? 0.1322 0.2479 0.2653 0.0185  -0.0318 -0.0041 739 ILE B CG2 
2092 C CD1 . ILE B 58  ? 0.1828 0.2756 0.2649 0.0217  -0.0436 0.0018  739 ILE B CD1 
2093 N N   . GLY B 59  ? 0.1691 0.2857 0.3194 0.0199  0.0050  0.0008  740 GLY B N   
2094 C CA  . GLY B 59  ? 0.1561 0.2755 0.3226 0.0164  0.0196  0.0031  740 GLY B CA  
2095 C C   . GLY B 59  ? 0.1506 0.2622 0.2998 0.0215  0.0356  0.0087  740 GLY B C   
2096 O O   . GLY B 59  ? 0.3298 0.4375 0.4613 0.0283  0.0354  0.0081  740 GLY B O   
2097 N N   . ASP B 60  ? 0.1874 0.2962 0.3417 0.0188  0.0498  0.0139  741 ASP B N   
2098 C CA  . ASP B 60  ? 0.1947 0.2958 0.3305 0.0249  0.0667  0.0209  741 ASP B CA  
2099 C C   . ASP B 60  ? 0.2414 0.3294 0.3486 0.0250  0.0657  0.0259  741 ASP B C   
2100 O O   . ASP B 60  ? 0.2462 0.3309 0.3622 0.0191  0.0684  0.0292  741 ASP B O   
2101 C CB  . ASP B 60  ? 0.2167 0.3231 0.3796 0.0231  0.0861  0.0255  741 ASP B CB  
2102 C CG  . ASP B 60  ? 0.3036 0.4027 0.4454 0.0316  0.1059  0.0337  741 ASP B CG  
2103 O OD1 . ASP B 60  ? 0.3144 0.4027 0.4190 0.0380  0.1041  0.0366  741 ASP B OD1 
2104 O OD2 . ASP B 60  ? 0.3890 0.4936 0.5521 0.0324  0.1235  0.0372  741 ASP B OD2 
2105 N N   . LYS B 61  ? 0.2352 0.3162 0.3105 0.0320  0.0614  0.0255  742 LYS B N   
2106 C CA  . LYS B 61  ? 0.2867 0.3574 0.3370 0.0327  0.0566  0.0284  742 LYS B CA  
2107 C C   . LYS B 61  ? 0.3332 0.3962 0.3756 0.0348  0.0720  0.0386  742 LYS B C   
2108 O O   . LYS B 61  ? 0.3696 0.4248 0.3990 0.0341  0.0686  0.0419  742 LYS B O   
2109 C CB  . LYS B 61  ? 0.3324 0.3990 0.3545 0.0401  0.0486  0.0242  742 LYS B CB  
2110 C CG  . LYS B 61  ? 0.4151 0.4801 0.4196 0.0503  0.0603  0.0258  742 LYS B CG  
2111 C CD  . LYS B 61  ? 0.4160 0.4772 0.3938 0.0575  0.0507  0.0192  742 LYS B CD  
2112 C CE  . LYS B 61  ? 0.6099 0.6703 0.5685 0.0689  0.0618  0.0189  742 LYS B CE  
2113 N NZ  . LYS B 61  ? 0.6983 0.7657 0.6769 0.0693  0.0707  0.0167  742 LYS B NZ  
2114 N N   . SER B 62  ? 0.3549 0.4193 0.4051 0.0382  0.0898  0.0443  743 SER B N   
2115 C CA  . SER B 62  ? 0.3642 0.4195 0.4088 0.0404  0.1068  0.0562  743 SER B CA  
2116 C C   . SER B 62  ? 0.3421 0.3983 0.4219 0.0295  0.1124  0.0587  743 SER B C   
2117 O O   . SER B 62  ? 0.5282 0.5744 0.6063 0.0296  0.1244  0.0686  743 SER B O   
2118 C CB  . SER B 62  ? 0.4883 0.5431 0.5234 0.0498  0.1266  0.0630  743 SER B CB  
2119 O OG  . SER B 62  ? 0.3489 0.4134 0.4193 0.0447  0.1363  0.0612  743 SER B OG  
2120 N N   . LYS B 63  ? 0.2443 0.3120 0.3562 0.0208  0.1033  0.0494  744 LYS B N   
2121 C CA  . LYS B 63  ? 0.2403 0.3111 0.3889 0.0102  0.1055  0.0477  744 LYS B CA  
2122 C C   . LYS B 63  ? 0.1873 0.2593 0.3394 0.0033  0.0854  0.0388  744 LYS B C   
2123 O O   . LYS B 63  ? 0.1714 0.2415 0.3451 -0.0044 0.0866  0.0376  744 LYS B O   
2124 C CB  . LYS B 63  ? 0.2128 0.2982 0.4007 0.0061  0.1110  0.0426  744 LYS B CB  
2125 C CG  . LYS B 63  ? 0.2842 0.3654 0.4692 0.0116  0.1297  0.0497  744 LYS B CG  
2126 C CD  . LYS B 63  ? 0.4047 0.4981 0.6249 0.0070  0.1291  0.0420  744 LYS B CD  
2127 C CE  . LYS B 63  ? 0.4686 0.5609 0.6805 0.0144  0.1436  0.0465  744 LYS B CE  
2128 N NZ  . LYS B 63  ? 0.3149 0.4214 0.5601 0.0112  0.1408  0.0380  744 LYS B NZ  
2129 N N   . ASN B 64  ? 0.1329 0.2075 0.2654 0.0059  0.0682  0.0325  745 ASN B N   
2130 C CA  . ASN B 64  ? 0.1200 0.1950 0.2510 0.0008  0.0507  0.0253  745 ASN B CA  
2131 C C   . ASN B 64  ? 0.1642 0.2266 0.2823 -0.0005 0.0529  0.0300  745 ASN B C   
2132 O O   . ASN B 64  ? 0.1971 0.2498 0.2927 0.0058  0.0616  0.0387  745 ASN B O   
2133 C CB  . ASN B 64  ? 0.1679 0.2444 0.2763 0.0053  0.0360  0.0209  745 ASN B CB  
2134 C CG  . ASN B 64  ? 0.2043 0.2918 0.3247 0.0075  0.0321  0.0162  745 ASN B CG  
2135 O OD1 . ASN B 64  ? 0.1224 0.2197 0.2719 0.0047  0.0360  0.0136  745 ASN B OD1 
2136 N ND2 . ASN B 64  ? 0.1557 0.2416 0.2562 0.0128  0.0242  0.0144  745 ASN B ND2 
2137 N N   . THR B 65  ? 0.1738 0.2369 0.3052 -0.0076 0.0442  0.0235  746 THR B N   
2138 C CA  . THR B 65  ? 0.1536 0.2054 0.2739 -0.0088 0.0438  0.0259  746 THR B CA  
2139 C C   . THR B 65  ? 0.1791 0.2334 0.2912 -0.0112 0.0263  0.0169  746 THR B C   
2140 O O   . THR B 65  ? 0.1027 0.1672 0.2274 -0.0145 0.0159  0.0081  746 THR B O   
2141 C CB  . THR B 65  ? 0.1849 0.2318 0.3326 -0.0151 0.0551  0.0274  746 THR B CB  
2142 O OG1 . THR B 65  ? 0.2643 0.3228 0.4446 -0.0230 0.0485  0.0159  746 THR B OG1 
2143 C CG2 . THR B 65  ? 0.2175 0.2585 0.3697 -0.0116 0.0759  0.0396  746 THR B CG2 
2144 N N   . TYR B 66  ? 0.1654 0.2108 0.2558 -0.0086 0.0235  0.0196  747 TYR B N   
2145 C CA  . TYR B 66  ? 0.1627 0.2093 0.2426 -0.0100 0.0098  0.0126  747 TYR B CA  
2146 C C   . TYR B 66  ? 0.1433 0.1804 0.2212 -0.0118 0.0115  0.0128  747 TYR B C   
2147 O O   . TYR B 66  ? 0.1553 0.1832 0.2319 -0.0096 0.0220  0.0207  747 TYR B O   
2148 C CB  . TYR B 66  ? 0.1714 0.2182 0.2267 -0.0041 0.0035  0.0142  747 TYR B CB  
2149 C CG  . TYR B 66  ? 0.1711 0.2238 0.2252 -0.0002 0.0049  0.0157  747 TYR B CG  
2150 C CD1 . TYR B 66  ? 0.2073 0.2692 0.2717 -0.0016 -0.0022 0.0104  747 TYR B CD1 
2151 C CD2 . TYR B 66  ? 0.2005 0.2494 0.2417 0.0062  0.0130  0.0222  747 TYR B CD2 
2152 C CE1 . TYR B 66  ? 0.1830 0.2496 0.2477 0.0025  -0.0005 0.0114  747 TYR B CE1 
2153 C CE2 . TYR B 66  ? 0.2283 0.2821 0.2679 0.0103  0.0149  0.0221  747 TYR B CE2 
2154 C CZ  . TYR B 66  ? 0.1961 0.2585 0.2488 0.0081  0.0085  0.0167  747 TYR B CZ  
2155 O OH  . TYR B 66  ? 0.1868 0.2536 0.2396 0.0127  0.0107  0.0163  747 TYR B OH  
2156 N N   . GLU B 67  ? 0.1198 0.1586 0.1963 -0.0149 0.0013  0.0045  748 GLU B N   
2157 C CA  . GLU B 67  ? 0.1401 0.1709 0.2166 -0.0168 0.0019  0.0023  748 GLU B CA  
2158 C C   . GLU B 67  ? 0.2024 0.2351 0.2625 -0.0158 -0.0087 -0.0033 748 GLU B C   
2159 O O   . GLU B 67  ? 0.1823 0.2229 0.2387 -0.0160 -0.0172 -0.0080 748 GLU B O   
2160 C CB  . GLU B 67  ? 0.1537 0.1845 0.2574 -0.0236 0.0042  -0.0051 748 GLU B CB  
2161 C CG  . GLU B 67  ? 0.2810 0.3040 0.3870 -0.0260 0.0033  -0.0108 748 GLU B CG  
2162 C CD  . GLU B 67  ? 0.4020 0.4258 0.5380 -0.0333 0.0042  -0.0211 748 GLU B CD  
2163 O OE1 . GLU B 67  ? 0.3609 0.3775 0.5169 -0.0357 0.0165  -0.0160 748 GLU B OE1 
2164 O OE2 . GLU B 67  ? 0.4258 0.4573 0.5656 -0.0361 -0.0072 -0.0345 748 GLU B OE2 
2165 N N   . TRP B 68  ? 0.1319 0.1570 0.1823 -0.0140 -0.0073 -0.0018 749 TRP B N   
2166 C CA  . TRP B 68  ? 0.1243 0.1500 0.1629 -0.0137 -0.0142 -0.0074 749 TRP B CA  
2167 C C   . TRP B 68  ? 0.1541 0.1746 0.2021 -0.0170 -0.0133 -0.0148 749 TRP B C   
2168 O O   . TRP B 68  ? 0.1172 0.1307 0.1789 -0.0184 -0.0059 -0.0129 749 TRP B O   
2169 C CB  . TRP B 68  ? 0.1395 0.1621 0.1621 -0.0085 -0.0136 -0.0014 749 TRP B CB  
2170 C CG  . TRP B 68  ? 0.1387 0.1530 0.1626 -0.0052 -0.0064 0.0048  749 TRP B CG  
2171 C CD1 . TRP B 68  ? 0.1637 0.1753 0.1848 -0.0007 -0.0009 0.0135  749 TRP B CD1 
2172 C CD2 . TRP B 68  ? 0.1337 0.1409 0.1604 -0.0047 -0.0038 0.0032  749 TRP B CD2 
2173 N NE1 . TRP B 68  ? 0.1208 0.1239 0.1417 0.0032  0.0044  0.0187  749 TRP B NE1 
2174 C CE2 . TRP B 68  ? 0.1545 0.1547 0.1805 0.0006  0.0027  0.0124  749 TRP B CE2 
2175 C CE3 . TRP B 68  ? 0.1181 0.1240 0.1468 -0.0072 -0.0061 -0.0050 749 TRP B CE3 
2176 C CZ2 . TRP B 68  ? 0.1292 0.1207 0.1586 0.0033  0.0067  0.0141  749 TRP B CZ2 
2177 C CZ3 . TRP B 68  ? 0.1694 0.1670 0.2025 -0.0051 -0.0015 -0.0046 749 TRP B CZ3 
2178 C CH2 . TRP B 68  ? 0.1289 0.1193 0.1633 0.0001  0.0045  0.0052  749 TRP B CH2 
2179 N N   . GLN B 69  ? 0.1692 0.1925 0.2092 -0.0175 -0.0199 -0.0229 750 GLN B N   
2180 C CA  . GLN B 69  ? 0.1714 0.1905 0.2178 -0.0199 -0.0202 -0.0328 750 GLN B CA  
2181 C C   . GLN B 69  ? 0.1481 0.1676 0.1760 -0.0170 -0.0234 -0.0362 750 GLN B C   
2182 O O   . GLN B 69  ? 0.1234 0.1491 0.1375 -0.0153 -0.0290 -0.0365 750 GLN B O   
2183 C CB  . GLN B 69  ? 0.2134 0.2385 0.2751 -0.0245 -0.0259 -0.0442 750 GLN B CB  
2184 C CG  . GLN B 69  ? 0.1480 0.1701 0.2160 -0.0268 -0.0284 -0.0581 750 GLN B CG  
2185 C CD  . GLN B 69  ? 0.1858 0.2167 0.2693 -0.0306 -0.0372 -0.0716 750 GLN B CD  
2186 O OE1 . GLN B 69  ? 0.2309 0.2648 0.3373 -0.0346 -0.0353 -0.0711 750 GLN B OE1 
2187 N NE2 . GLN B 69  ? 0.2060 0.2422 0.2771 -0.0287 -0.0468 -0.0841 750 GLN B NE2 
2188 N N   . THR B 70  ? 0.1353 0.1475 0.1635 -0.0160 -0.0187 -0.0381 751 THR B N   
2189 C CA  . THR B 70  ? 0.1336 0.1456 0.1466 -0.0130 -0.0189 -0.0410 751 THR B CA  
2190 C C   . THR B 70  ? 0.1514 0.1615 0.1650 -0.0141 -0.0207 -0.0548 751 THR B C   
2191 O O   . THR B 70  ? 0.1528 0.1600 0.1829 -0.0177 -0.0211 -0.0625 751 THR B O   
2192 C CB  . THR B 70  ? 0.1636 0.1704 0.1766 -0.0095 -0.0125 -0.0334 751 THR B CB  
2193 O OG1 . THR B 70  ? 0.1878 0.1865 0.2160 -0.0098 -0.0074 -0.0316 751 THR B OG1 
2194 C CG2 . THR B 70  ? 0.1669 0.1782 0.1734 -0.0071 -0.0133 -0.0231 751 THR B CG2 
2195 N N   . PRO B 71  ? 0.1548 0.1664 0.1512 -0.0110 -0.0210 -0.0589 752 PRO B N   
2196 C CA  . PRO B 71  ? 0.1772 0.1878 0.1697 -0.0106 -0.0233 -0.0737 752 PRO B CA  
2197 C C   . PRO B 71  ? 0.2491 0.2505 0.2586 -0.0121 -0.0178 -0.0805 752 PRO B C   
2198 O O   . PRO B 71  ? 0.2103 0.2103 0.2254 -0.0137 -0.0211 -0.0952 752 PRO B O   
2199 C CB  . PRO B 71  ? 0.1984 0.2110 0.1671 -0.0056 -0.0209 -0.0725 752 PRO B CB  
2200 C CG  . PRO B 71  ? 0.1833 0.2007 0.1442 -0.0047 -0.0217 -0.0593 752 PRO B CG  
2201 C CD  . PRO B 71  ? 0.1836 0.1990 0.1626 -0.0075 -0.0198 -0.0509 752 PRO B CD  
2202 N N   . ASP B 72  ? 0.1888 0.1838 0.2072 -0.0109 -0.0101 -0.0710 753 ASP B N   
2203 C CA  . ASP B 72  ? 0.2025 0.1870 0.2387 -0.0114 -0.0044 -0.0757 753 ASP B CA  
2204 C C   . ASP B 72  ? 0.1787 0.1584 0.2374 -0.0166 -0.0045 -0.0773 753 ASP B C   
2205 O O   . ASP B 72  ? 0.1911 0.1601 0.2678 -0.0174 0.0013  -0.0803 753 ASP B O   
2206 C CB  . ASP B 72  ? 0.1945 0.1742 0.2337 -0.0070 0.0029  -0.0641 753 ASP B CB  
2207 C CG  . ASP B 72  ? 0.2217 0.2032 0.2627 -0.0063 0.0028  -0.0490 753 ASP B CG  
2208 O OD1 . ASP B 72  ? 0.2122 0.1975 0.2542 -0.0097 -0.0009 -0.0469 753 ASP B OD1 
2209 O OD2 . ASP B 72  ? 0.2809 0.2609 0.3221 -0.0015 0.0062  -0.0400 753 ASP B OD2 
2210 N N   . GLY B 73  ? 0.2187 0.2055 0.2794 -0.0199 -0.0098 -0.0749 754 GLY B N   
2211 C CA  . GLY B 73  ? 0.2183 0.2020 0.3035 -0.0253 -0.0085 -0.0765 754 GLY B CA  
2212 C C   . GLY B 73  ? 0.2612 0.2404 0.3545 -0.0247 -0.0010 -0.0595 754 GLY B C   
2213 O O   . GLY B 73  ? 0.2939 0.2713 0.4074 -0.0291 0.0019  -0.0585 754 GLY B O   
2214 N N   . GLN B 74  ? 0.1730 0.1508 0.2517 -0.0189 0.0022  -0.0468 755 GLN B N   
2215 C CA  . GLN B 74  ? 0.2112 0.1850 0.2926 -0.0163 0.0084  -0.0312 755 GLN B CA  
2216 C C   . GLN B 74  ? 0.2069 0.1907 0.2837 -0.0180 0.0045  -0.0268 755 GLN B C   
2217 O O   . GLN B 74  ? 0.1507 0.1446 0.2151 -0.0186 -0.0035 -0.0314 755 GLN B O   
2218 C CB  . GLN B 74  ? 0.1994 0.1715 0.2668 -0.0086 0.0102  -0.0215 755 GLN B CB  
2219 C CG  . GLN B 74  ? 0.4508 0.4177 0.5175 -0.0033 0.0160  -0.0060 755 GLN B CG  
2220 C CD  . GLN B 74  ? 0.3143 0.2795 0.3712 0.0053  0.0162  0.0010  755 GLN B CD  
2221 O OE1 . GLN B 74  ? 0.4763 0.4419 0.5326 0.0066  0.0146  -0.0054 755 GLN B OE1 
2222 N NE2 . GLN B 74  ? 0.3854 0.3494 0.4350 0.0120  0.0181  0.0137  755 GLN B NE2 
2223 N N   . LYS B 75  ? 0.1839 0.1638 0.2707 -0.0181 0.0113  -0.0171 756 LYS B N   
2224 C CA  . LYS B 75  ? 0.2458 0.2345 0.3295 -0.0189 0.0094  -0.0124 756 LYS B CA  
2225 C C   . LYS B 75  ? 0.2864 0.2694 0.3663 -0.0135 0.0183  0.0031  756 LYS B C   
2226 O O   . LYS B 75  ? 0.2081 0.1794 0.2920 -0.0101 0.0266  0.0104  756 LYS B O   
2227 C CB  . LYS B 75  ? 0.2122 0.2060 0.3176 -0.0263 0.0079  -0.0215 756 LYS B CB  
2228 C CG  . LYS B 75  ? 0.3518 0.3352 0.4847 -0.0305 0.0181  -0.0219 756 LYS B CG  
2229 C CD  . LYS B 75  ? 0.4024 0.3938 0.5614 -0.0384 0.0149  -0.0338 756 LYS B CD  
2230 C CE  . LYS B 75  ? 0.4161 0.4180 0.5688 -0.0403 -0.0001 -0.0508 756 LYS B CE  
2231 N NZ  . LYS B 75  ? 0.3143 0.3241 0.4955 -0.0474 -0.0055 -0.0660 756 LYS B NZ  
2232 N N   . GLY B 76  ? 0.1407 0.1315 0.2111 -0.0117 0.0165  0.0082  757 GLY B N   
2233 C CA  . GLY B 76  ? 0.1996 0.1863 0.2629 -0.0056 0.0245  0.0217  757 GLY B CA  
2234 C C   . GLY B 76  ? 0.2309 0.2272 0.2919 -0.0063 0.0231  0.0227  757 GLY B C   
2235 O O   . GLY B 76  ? 0.1673 0.1736 0.2288 -0.0101 0.0142  0.0142  757 GLY B O   
2236 N N   . SER B 77  ? 0.2657 0.2585 0.3234 -0.0016 0.0327  0.0337  758 SER B N   
2237 C CA  . SER B 77  ? 0.1773 0.1783 0.2342 -0.0012 0.0340  0.0353  758 SER B CA  
2238 C C   . SER B 77  ? 0.2193 0.2227 0.2500 0.0078  0.0309  0.0406  758 SER B C   
2239 O O   . SER B 77  ? 0.1843 0.1824 0.1991 0.0147  0.0299  0.0454  758 SER B O   
2240 C CB  . SER B 77  ? 0.2598 0.2559 0.3342 -0.0025 0.0492  0.0428  758 SER B CB  
2241 O OG  . SER B 77  ? 0.3187 0.3140 0.4228 -0.0118 0.0514  0.0354  758 SER B OG  
2242 N N   . PHE B 78  ? 0.1707 0.1828 0.1990 0.0079  0.0286  0.0386  759 PHE B N   
2243 C CA  . PHE B 78  ? 0.1669 0.1815 0.1738 0.0163  0.0271  0.0421  759 PHE B CA  
2244 C C   . PHE B 78  ? 0.2176 0.2389 0.2307 0.0157  0.0312  0.0417  759 PHE B C   
2245 O O   . PHE B 78  ? 0.1386 0.1647 0.1733 0.0085  0.0324  0.0376  759 PHE B O   
2246 C CB  . PHE B 78  ? 0.1685 0.1876 0.1624 0.0177  0.0137  0.0354  759 PHE B CB  
2247 C CG  . PHE B 78  ? 0.1378 0.1642 0.1411 0.0107  0.0050  0.0264  759 PHE B CG  
2248 C CD1 . PHE B 78  ? 0.1371 0.1631 0.1509 0.0043  0.0013  0.0212  759 PHE B CD1 
2249 C CD2 . PHE B 78  ? 0.1482 0.1813 0.1481 0.0116  0.0004  0.0231  759 PHE B CD2 
2250 C CE1 . PHE B 78  ? 0.1593 0.1917 0.1770 0.0000  -0.0068 0.0141  759 PHE B CE1 
2251 C CE2 . PHE B 78  ? 0.1039 0.1424 0.1103 0.0069  -0.0072 0.0169  759 PHE B CE2 
2252 C CZ  . PHE B 78  ? 0.1382 0.1764 0.1519 0.0015  -0.0109 0.0129  759 PHE B CZ  
2253 N N   . THR B 79  ? 0.2209 0.2433 0.2160 0.0239  0.0331  0.0450  760 THR B N   
2254 C CA  . THR B 79  ? 0.2219 0.2504 0.2212 0.0249  0.0380  0.0444  760 THR B CA  
2255 C C   . THR B 79  ? 0.2039 0.2382 0.1894 0.0286  0.0272  0.0374  760 THR B C   
2256 O O   . THR B 79  ? 0.1882 0.2222 0.1637 0.0294  0.0167  0.0332  760 THR B O   
2257 C CB  . THR B 79  ? 0.2579 0.2809 0.2491 0.0323  0.0542  0.0551  760 THR B CB  
2258 O OG1 . THR B 79  ? 0.3358 0.3551 0.2969 0.0436  0.0520  0.0584  760 THR B OG1 
2259 C CG2 . THR B 79  ? 0.3386 0.3530 0.3447 0.0288  0.0662  0.0633  760 THR B CG2 
2260 N N   . SER B 80  ? 0.2413 0.2809 0.2292 0.0308  0.0309  0.0359  761 SER B N   
2261 C CA  . SER B 80  ? 0.2420 0.2860 0.2205 0.0341  0.0218  0.0286  761 SER B CA  
2262 C C   . SER B 80  ? 0.1971 0.2376 0.1501 0.0431  0.0182  0.0280  761 SER B C   
2263 O O   . SER B 80  ? 0.1447 0.1873 0.0923 0.0440  0.0074  0.0203  761 SER B O   
2264 C CB  . SER B 80  ? 0.2234 0.2731 0.2106 0.0357  0.0279  0.0271  761 SER B CB  
2265 O OG  . SER B 80  ? 0.3762 0.4234 0.3540 0.0427  0.0420  0.0338  761 SER B OG  
2266 N N   . GLU B 81  ? 0.1901 0.2252 0.1283 0.0503  0.0270  0.0360  762 GLU B N   
2267 C CA  . GLU B 81  ? 0.2266 0.2596 0.1389 0.0610  0.0222  0.0352  762 GLU B CA  
2268 C C   . GLU B 81  ? 0.2234 0.2563 0.1348 0.0589  0.0093  0.0308  762 GLU B C   
2269 O O   . GLU B 81  ? 0.2777 0.3122 0.1732 0.0666  0.0009  0.0259  762 GLU B O   
2270 C CB  . GLU B 81  ? 0.2078 0.2339 0.1034 0.0701  0.0352  0.0473  762 GLU B CB  
2271 C CG  . GLU B 81  ? 0.3007 0.3267 0.1984 0.0723  0.0512  0.0529  762 GLU B CG  
2272 C CD  . GLU B 81  ? 0.4365 0.4539 0.3177 0.0818  0.0655  0.0659  762 GLU B CD  
2273 O OE1 . GLU B 81  ? 0.3960 0.4058 0.2778 0.0817  0.0662  0.0728  762 GLU B OE1 
2274 O OE2 . GLU B 81  ? 0.3197 0.3367 0.1932 0.0879  0.0738  0.0667  762 GLU B OE2 
2275 N N   . ASP B 82  ? 0.2315 0.2632 0.1604 0.0495  0.0076  0.0316  763 ASP B N   
2276 C CA  . ASP B 82  ? 0.1800 0.2115 0.1104 0.0473  -0.0023 0.0281  763 ASP B CA  
2277 C C   . ASP B 82  ? 0.2233 0.2600 0.1640 0.0409  -0.0123 0.0184  763 ASP B C   
2278 O O   . ASP B 82  ? 0.1485 0.1857 0.0929 0.0384  -0.0191 0.0151  763 ASP B O   
2279 C CB  . ASP B 82  ? 0.1800 0.2063 0.1223 0.0414  0.0024  0.0337  763 ASP B CB  
2280 C CG  . ASP B 82  ? 0.2733 0.2918 0.2085 0.0473  0.0140  0.0450  763 ASP B CG  
2281 O OD1 . ASP B 82  ? 0.2646 0.2810 0.1798 0.0583  0.0137  0.0489  763 ASP B OD1 
2282 O OD2 . ASP B 82  ? 0.2277 0.2421 0.1781 0.0414  0.0233  0.0497  763 ASP B OD2 
2283 N N   . ILE B 83  ? 0.1454 0.1854 0.0918 0.0387  -0.0121 0.0146  764 ILE B N   
2284 C CA  . ILE B 83  ? 0.2069 0.2496 0.1640 0.0329  -0.0193 0.0079  764 ILE B CA  
2285 C C   . ILE B 83  ? 0.1937 0.2386 0.1446 0.0379  -0.0253 0.0000  764 ILE B C   
2286 O O   . ILE B 83  ? 0.1659 0.2117 0.1078 0.0443  -0.0224 -0.0015 764 ILE B O   
2287 C CB  . ILE B 83  ? 0.1623 0.2069 0.1326 0.0275  -0.0161 0.0090  764 ILE B CB  
2288 C CG1 . ILE B 83  ? 0.1670 0.2104 0.1455 0.0231  -0.0102 0.0147  764 ILE B CG1 
2289 C CG2 . ILE B 83  ? 0.1598 0.2052 0.1386 0.0225  -0.0230 0.0049  764 ILE B CG2 
2290 C CD1 . ILE B 83  ? 0.1422 0.1899 0.1361 0.0186  -0.0084 0.0143  764 ILE B CD1 
2291 N N   . HIS B 84  ? 0.1816 0.2272 0.1386 0.0351  -0.0329 -0.0058 765 HIS B N   
2292 C CA  . HIS B 84  ? 0.2066 0.2542 0.1635 0.0385  -0.0396 -0.0155 765 HIS B CA  
2293 C C   . HIS B 84  ? 0.1721 0.2181 0.1447 0.0318  -0.0413 -0.0184 765 HIS B C   
2294 O O   . HIS B 84  ? 0.1926 0.2373 0.1741 0.0259  -0.0422 -0.0164 765 HIS B O   
2295 C CB  . HIS B 84  ? 0.1651 0.2137 0.1207 0.0406  -0.0451 -0.0197 765 HIS B CB  
2296 C CG  . HIS B 84  ? 0.2116 0.2589 0.1532 0.0468  -0.0418 -0.0142 765 HIS B CG  
2297 N ND1 . HIS B 84  ? 0.2610 0.3087 0.1886 0.0557  -0.0416 -0.0166 765 HIS B ND1 
2298 C CD2 . HIS B 84  ? 0.2274 0.2725 0.1665 0.0464  -0.0384 -0.0061 765 HIS B CD2 
2299 C CE1 . HIS B 84  ? 0.3233 0.3685 0.2401 0.0605  -0.0377 -0.0090 765 HIS B CE1 
2300 N NE2 . HIS B 84  ? 0.2628 0.3061 0.1870 0.0549  -0.0358 -0.0026 765 HIS B NE2 
2301 N N   . PHE B 85  ? 0.1733 0.2186 0.1485 0.0336  -0.0408 -0.0226 766 PHE B N   
2302 C CA  . PHE B 85  ? 0.1803 0.2224 0.1699 0.0288  -0.0413 -0.0235 766 PHE B CA  
2303 C C   . PHE B 85  ? 0.1628 0.2036 0.1620 0.0286  -0.0468 -0.0334 766 PHE B C   
2304 O O   . PHE B 85  ? 0.1628 0.2063 0.1572 0.0341  -0.0510 -0.0429 766 PHE B O   
2305 C CB  . PHE B 85  ? 0.1361 0.1777 0.1273 0.0311  -0.0374 -0.0224 766 PHE B CB  
2306 C CG  . PHE B 85  ? 0.1232 0.1675 0.1109 0.0307  -0.0319 -0.0141 766 PHE B CG  
2307 C CD1 . PHE B 85  ? 0.1442 0.1883 0.1392 0.0254  -0.0315 -0.0077 766 PHE B CD1 
2308 C CD2 . PHE B 85  ? 0.1311 0.1781 0.1087 0.0358  -0.0267 -0.0130 766 PHE B CD2 
2309 C CE1 . PHE B 85  ? 0.1947 0.2424 0.1909 0.0243  -0.0275 -0.0025 766 PHE B CE1 
2310 C CE2 . PHE B 85  ? 0.2204 0.2697 0.2002 0.0343  -0.0203 -0.0057 766 PHE B CE2 
2311 C CZ  . PHE B 85  ? 0.1817 0.2318 0.1727 0.0280  -0.0214 -0.0015 766 PHE B CZ  
2312 N N   . TYR B 86  ? 0.1552 0.1919 0.1683 0.0226  -0.0464 -0.0316 767 TYR B N   
2313 C CA  . TYR B 86  ? 0.2130 0.2476 0.2417 0.0208  -0.0498 -0.0407 767 TYR B CA  
2314 C C   . TYR B 86  ? 0.1557 0.1882 0.1886 0.0249  -0.0514 -0.0499 767 TYR B C   
2315 O O   . TYR B 86  ? 0.1291 0.1640 0.1669 0.0275  -0.0572 -0.0629 767 TYR B O   
2316 C CB  . TYR B 86  ? 0.1530 0.1812 0.1956 0.0142  -0.0454 -0.0340 767 TYR B CB  
2317 C CG  . TYR B 86  ? 0.1284 0.1528 0.1931 0.0109  -0.0460 -0.0419 767 TYR B CG  
2318 C CD1 . TYR B 86  ? 0.1585 0.1889 0.2330 0.0101  -0.0511 -0.0520 767 TYR B CD1 
2319 C CD2 . TYR B 86  ? 0.1742 0.1890 0.2524 0.0087  -0.0413 -0.0391 767 TYR B CD2 
2320 C CE1 . TYR B 86  ? 0.1264 0.1543 0.2266 0.0061  -0.0514 -0.0605 767 TYR B CE1 
2321 C CE2 . TYR B 86  ? 0.2618 0.2716 0.3642 0.0049  -0.0400 -0.0460 767 TYR B CE2 
2322 C CZ  . TYR B 86  ? 0.1791 0.1959 0.2940 0.0030  -0.0450 -0.0574 767 TYR B CZ  
2323 O OH  . TYR B 86  ? 0.2596 0.2724 0.4040 -0.0018 -0.0435 -0.0656 767 TYR B OH  
2324 N N   . ASN B 87  ? 0.2005 0.2293 0.2316 0.0263  -0.0471 -0.0446 768 ASN B N   
2325 C CA  . ASN B 87  ? 0.1310 0.1572 0.1664 0.0308  -0.0475 -0.0534 768 ASN B CA  
2326 C C   . ASN B 87  ? 0.1549 0.1812 0.1840 0.0336  -0.0422 -0.0451 768 ASN B C   
2327 O O   . ASN B 87  ? 0.1721 0.1930 0.2113 0.0319  -0.0395 -0.0389 768 ASN B O   
2328 C CB  . ASN B 87  ? 0.1974 0.2152 0.2551 0.0272  -0.0475 -0.0584 768 ASN B CB  
2329 C CG  . ASN B 87  ? 0.2610 0.2761 0.3251 0.0321  -0.0492 -0.0716 768 ASN B CG  
2330 O OD1 . ASN B 87  ? 0.2542 0.2724 0.3056 0.0385  -0.0481 -0.0736 768 ASN B OD1 
2331 N ND2 . ASN B 87  ? 0.2545 0.2634 0.3403 0.0291  -0.0510 -0.0813 768 ASN B ND2 
2332 N N   . LYS B 88  ? 0.1899 0.2225 0.2033 0.0384  -0.0405 -0.0447 769 LYS B N   
2333 C CA  . LYS B 88  ? 0.1847 0.2195 0.1962 0.0406  -0.0348 -0.0376 769 LYS B CA  
2334 C C   . LYS B 88  ? 0.1612 0.1926 0.1825 0.0447  -0.0330 -0.0430 769 LYS B C   
2335 O O   . LYS B 88  ? 0.1845 0.2157 0.2144 0.0448  -0.0300 -0.0365 769 LYS B O   
2336 C CB  . LYS B 88  ? 0.2212 0.2623 0.2161 0.0450  -0.0308 -0.0359 769 LYS B CB  
2337 C CG  . LYS B 88  ? 0.2372 0.2821 0.2349 0.0468  -0.0235 -0.0294 769 LYS B CG  
2338 C CD  . LYS B 88  ? 0.3168 0.3662 0.2999 0.0505  -0.0169 -0.0258 769 LYS B CD  
2339 C CE  . LYS B 88  ? 0.3902 0.4443 0.3811 0.0516  -0.0080 -0.0203 769 LYS B CE  
2340 N NZ  . LYS B 88  ? 0.5510 0.6077 0.5289 0.0556  0.0014  -0.0157 769 LYS B NZ  
2341 N N   . LYS B 89  ? 0.2178 0.2471 0.2386 0.0488  -0.0354 -0.0560 770 LYS B N   
2342 C CA  . LYS B 89  ? 0.1971 0.2223 0.2278 0.0534  -0.0332 -0.0631 770 LYS B CA  
2343 C C   . LYS B 89  ? 0.2507 0.2668 0.3021 0.0492  -0.0337 -0.0588 770 LYS B C   
2344 O O   . LYS B 89  ? 0.2414 0.2549 0.3023 0.0523  -0.0302 -0.0558 770 LYS B O   
2345 C CB  . LYS B 89  ? 0.2189 0.2436 0.2446 0.0586  -0.0371 -0.0804 770 LYS B CB  
2346 C CG  . LYS B 89  ? 0.2784 0.2972 0.3163 0.0633  -0.0353 -0.0907 770 LYS B CG  
2347 C CD  . LYS B 89  ? 0.3509 0.3738 0.3830 0.0698  -0.0271 -0.0868 770 LYS B CD  
2348 C CE  . LYS B 89  ? 0.3215 0.3384 0.3666 0.0753  -0.0248 -0.0978 770 LYS B CE  
2349 N NZ  . LYS B 89  ? 0.3400 0.3468 0.4103 0.0709  -0.0255 -0.0926 770 LYS B NZ  
2350 N N   . ASP B 90  ? 0.2005 0.2115 0.2598 0.0431  -0.0370 -0.0578 771 ASP B N   
2351 C CA  . ASP B 90  ? 0.1820 0.1824 0.2594 0.0398  -0.0354 -0.0519 771 ASP B CA  
2352 C C   . ASP B 90  ? 0.2191 0.2198 0.2929 0.0366  -0.0338 -0.0353 771 ASP B C   
2353 O O   . ASP B 90  ? 0.1801 0.1716 0.2643 0.0345  -0.0319 -0.0277 771 ASP B O   
2354 C CB  . ASP B 90  ? 0.2511 0.2448 0.3427 0.0349  -0.0378 -0.0602 771 ASP B CB  
2355 C CG  . ASP B 90  ? 0.2520 0.2427 0.3539 0.0384  -0.0403 -0.0784 771 ASP B CG  
2356 O OD1 . ASP B 90  ? 0.2814 0.2694 0.3854 0.0442  -0.0379 -0.0819 771 ASP B OD1 
2357 O OD2 . ASP B 90  ? 0.4183 0.4098 0.5277 0.0356  -0.0450 -0.0905 771 ASP B OD2 
2358 N N   . TYR B 91  ? 0.2004 0.2110 0.2598 0.0367  -0.0341 -0.0298 772 TYR B N   
2359 C CA  . TYR B 91  ? 0.1916 0.2039 0.2473 0.0345  -0.0340 -0.0167 772 TYR B CA  
2360 C C   . TYR B 91  ? 0.2178 0.2248 0.2827 0.0380  -0.0332 -0.0090 772 TYR B C   
2361 O O   . TYR B 91  ? 0.1777 0.1805 0.2412 0.0365  -0.0335 0.0010  772 TYR B O   
2362 C CB  . TYR B 91  ? 0.2209 0.2445 0.2648 0.0347  -0.0339 -0.0144 772 TYR B CB  
2363 C CG  . TYR B 91  ? 0.1905 0.2173 0.2333 0.0335  -0.0352 -0.0040 772 TYR B CG  
2364 C CD1 . TYR B 91  ? 0.2046 0.2297 0.2410 0.0289  -0.0367 0.0015  772 TYR B CD1 
2365 C CD2 . TYR B 91  ? 0.1877 0.2200 0.2366 0.0374  -0.0354 -0.0010 772 TYR B CD2 
2366 C CE1 . TYR B 91  ? 0.1797 0.2080 0.2129 0.0289  -0.0391 0.0091  772 TYR B CE1 
2367 C CE2 . TYR B 91  ? 0.2127 0.2495 0.2613 0.0371  -0.0389 0.0063  772 TYR B CE2 
2368 C CZ  . TYR B 91  ? 0.2219 0.2564 0.2611 0.0331  -0.0411 0.0109  772 TYR B CZ  
2369 O OH  . TYR B 91  ? 0.2380 0.2774 0.2746 0.0338  -0.0457 0.0164  772 TYR B OH  
2370 N N   . PRO B 92  ? 0.1772 0.1842 0.2505 0.0438  -0.0319 -0.0125 773 PRO B N   
2371 C CA  . PRO B 92  ? 0.2490 0.2508 0.3319 0.0485  -0.0320 -0.0041 773 PRO B CA  
2372 C C   . PRO B 92  ? 0.2989 0.2851 0.3908 0.0479  -0.0300 0.0004  773 PRO B C   
2373 O O   . PRO B 92  ? 0.2114 0.1918 0.3064 0.0521  -0.0301 0.0113  773 PRO B O   
2374 C CB  . PRO B 92  ? 0.1505 0.1555 0.2427 0.0549  -0.0300 -0.0114 773 PRO B CB  
2375 C CG  . PRO B 92  ? 0.1639 0.1796 0.2462 0.0538  -0.0286 -0.0194 773 PRO B CG  
2376 C CD  . PRO B 92  ? 0.2071 0.2201 0.2795 0.0477  -0.0300 -0.0229 773 PRO B CD  
2377 N N   . LYS B 93  ? 0.2696 0.2487 0.3669 0.0433  -0.0281 -0.0076 774 LYS B N   
2378 C CA  . LYS B 93  ? 0.2077 0.1708 0.3195 0.0421  -0.0240 -0.0042 774 LYS B CA  
2379 C C   . LYS B 93  ? 0.3790 0.3371 0.4837 0.0392  -0.0216 0.0103  774 LYS B C   
2380 O O   . LYS B 93  ? 0.4741 0.4177 0.5886 0.0402  -0.0162 0.0188  774 LYS B O   
2381 C CB  . LYS B 93  ? 0.3017 0.2606 0.4258 0.0376  -0.0232 -0.0194 774 LYS B CB  
2382 C CG  . LYS B 93  ? 0.1910 0.1516 0.3217 0.0422  -0.0248 -0.0346 774 LYS B CG  
2383 C CD  . LYS B 93  ? 0.3478 0.3036 0.4929 0.0386  -0.0257 -0.0515 774 LYS B CD  
2384 C CE  . LYS B 93  ? 0.3132 0.2706 0.4618 0.0446  -0.0274 -0.0680 774 LYS B CE  
2385 N NZ  . LYS B 93  ? 0.3626 0.3348 0.4889 0.0495  -0.0294 -0.0696 774 LYS B NZ  
2386 N N   . GLY B 94  ? 0.3398 0.3084 0.4279 0.0361  -0.0244 0.0135  775 GLY B N   
2387 C CA  . GLY B 94  ? 0.3549 0.3207 0.4314 0.0366  -0.0231 0.0280  775 GLY B CA  
2388 C C   . GLY B 94  ? 0.3070 0.2770 0.3740 0.0299  -0.0221 0.0278  775 GLY B C   
2389 O O   . GLY B 94  ? 0.2408 0.2193 0.3069 0.0255  -0.0245 0.0175  775 GLY B O   
2390 N N   . PHE B 95  ? 0.2296 0.1931 0.2883 0.0304  -0.0180 0.0403  776 PHE B N   
2391 C CA  . PHE B 95  ? 0.3117 0.2769 0.3602 0.0257  -0.0150 0.0437  776 PHE B CA  
2392 C C   . PHE B 95  ? 0.3233 0.2933 0.3809 0.0180  -0.0143 0.0320  776 PHE B C   
2393 O O   . PHE B 95  ? 0.3170 0.2967 0.3638 0.0153  -0.0172 0.0290  776 PHE B O   
2394 C CB  . PHE B 95  ? 0.4260 0.3763 0.4742 0.0276  -0.0055 0.0577  776 PHE B CB  
2395 C CG  . PHE B 95  ? 0.5108 0.4615 0.5462 0.0247  -0.0003 0.0634  776 PHE B CG  
2396 C CD1 . PHE B 95  ? 0.5100 0.4655 0.5208 0.0296  -0.0036 0.0711  776 PHE B CD1 
2397 C CD2 . PHE B 95  ? 0.4943 0.4413 0.5440 0.0174  0.0078  0.0601  776 PHE B CD2 
2398 C CE1 . PHE B 95  ? 0.4240 0.3793 0.4218 0.0277  0.0020  0.0756  776 PHE B CE1 
2399 C CE2 . PHE B 95  ? 0.4170 0.3647 0.4563 0.0151  0.0139  0.0653  776 PHE B CE2 
2400 C CZ  . PHE B 95  ? 0.3659 0.3173 0.3779 0.0205  0.0115  0.0731  776 PHE B CZ  
2401 N N   . ILE B 96  ? 0.2162 0.1798 0.2948 0.0150  -0.0111 0.0246  777 ILE B N   
2402 C CA  . ILE B 96  ? 0.3037 0.2718 0.3933 0.0085  -0.0110 0.0139  777 ILE B CA  
2403 C C   . ILE B 96  ? 0.3265 0.3085 0.4082 0.0086  -0.0198 0.0020  777 ILE B C   
2404 O O   . ILE B 96  ? 0.2792 0.2677 0.3638 0.0048  -0.0215 -0.0051 777 ILE B O   
2405 C CB  . ILE B 96  ? 0.3174 0.2760 0.4350 0.0053  -0.0067 0.0066  777 ILE B CB  
2406 C CG1 . ILE B 96  ? 0.2915 0.2496 0.4166 0.0090  -0.0121 -0.0039 777 ILE B CG1 
2407 C CG2 . ILE B 96  ? 0.2983 0.2409 0.4249 0.0052  0.0048  0.0206  777 ILE B CG2 
2408 C CD1 . ILE B 96  ? 0.4105 0.3621 0.5644 0.0054  -0.0107 -0.0169 777 ILE B CD1 
2409 N N   . TYR B 97  ? 0.2107 0.1975 0.2830 0.0134  -0.0247 0.0002  778 TYR B N   
2410 C CA  . TYR B 97  ? 0.2315 0.2298 0.2953 0.0145  -0.0307 -0.0092 778 TYR B CA  
2411 C C   . TYR B 97  ? 0.2121 0.2185 0.2579 0.0154  -0.0325 -0.0029 778 TYR B C   
2412 O O   . TYR B 97  ? 0.2185 0.2331 0.2566 0.0170  -0.0355 -0.0079 778 TYR B O   
2413 C CB  . TYR B 97  ? 0.1547 0.1530 0.2230 0.0193  -0.0329 -0.0172 778 TYR B CB  
2414 C CG  . TYR B 97  ? 0.2473 0.2376 0.3353 0.0184  -0.0321 -0.0268 778 TYR B CG  
2415 C CD1 . TYR B 97  ? 0.2453 0.2386 0.3421 0.0153  -0.0352 -0.0389 778 TYR B CD1 
2416 C CD2 . TYR B 97  ? 0.2590 0.2388 0.3593 0.0211  -0.0288 -0.0246 778 TYR B CD2 
2417 C CE1 . TYR B 97  ? 0.3085 0.2953 0.4273 0.0139  -0.0353 -0.0501 778 TYR B CE1 
2418 C CE2 . TYR B 97  ? 0.3481 0.3194 0.4701 0.0197  -0.0276 -0.0346 778 TYR B CE2 
2419 C CZ  . TYR B 97  ? 0.2388 0.2139 0.3707 0.0157  -0.0310 -0.0482 778 TYR B CZ  
2420 O OH  . TYR B 97  ? 0.3815 0.3489 0.5385 0.0138  -0.0306 -0.0605 778 TYR B OH  
2421 N N   . ASP B 98  ? 0.1448 0.1489 0.1837 0.0147  -0.0303 0.0077  779 ASP B N   
2422 C CA  . ASP B 98  ? 0.2186 0.2303 0.2436 0.0156  -0.0329 0.0117  779 ASP B CA  
2423 C C   . ASP B 98  ? 0.1406 0.1564 0.1595 0.0115  -0.0325 0.0100  779 ASP B C   
2424 O O   . ASP B 98  ? 0.1658 0.1799 0.1785 0.0098  -0.0304 0.0155  779 ASP B O   
2425 C CB  . ASP B 98  ? 0.2033 0.2118 0.2222 0.0186  -0.0328 0.0218  779 ASP B CB  
2426 C CG  . ASP B 98  ? 0.2459 0.2637 0.2546 0.0197  -0.0374 0.0229  779 ASP B CG  
2427 O OD1 . ASP B 98  ? 0.1802 0.2055 0.1888 0.0178  -0.0388 0.0171  779 ASP B OD1 
2428 O OD2 . ASP B 98  ? 0.2939 0.3113 0.2952 0.0229  -0.0396 0.0295  779 ASP B OD2 
2429 N N   . LEU B 99  ? 0.1263 0.1476 0.1457 0.0111  -0.0346 0.0024  780 LEU B N   
2430 C CA  . LEU B 99  ? 0.1263 0.1504 0.1439 0.0082  -0.0344 -0.0002 780 LEU B CA  
2431 C C   . LEU B 99  ? 0.1032 0.1338 0.1152 0.0105  -0.0373 -0.0056 780 LEU B C   
2432 O O   . LEU B 99  ? 0.1574 0.1891 0.1710 0.0138  -0.0392 -0.0115 780 LEU B O   
2433 C CB  . LEU B 99  ? 0.1361 0.1562 0.1674 0.0057  -0.0327 -0.0041 780 LEU B CB  
2434 C CG  . LEU B 99  ? 0.1795 0.2045 0.2140 0.0038  -0.0340 -0.0094 780 LEU B CG  
2435 C CD1 . LEU B 99  ? 0.1747 0.2008 0.2004 0.0019  -0.0309 -0.0030 780 LEU B CD1 
2436 C CD2 . LEU B 99  ? 0.1017 0.1243 0.1560 0.0008  -0.0324 -0.0148 780 LEU B CD2 
2437 N N   . ALA B 100 ? 0.0887 0.1226 0.0932 0.0096  -0.0371 -0.0036 781 ALA B N   
2438 C CA  . ALA B 100 ? 0.1412 0.1794 0.1388 0.0127  -0.0380 -0.0059 781 ALA B CA  
2439 C C   . ALA B 100 ? 0.0998 0.1395 0.0943 0.0117  -0.0380 -0.0052 781 ALA B C   
2440 O O   . ALA B 100 ? 0.1279 0.1661 0.1241 0.0081  -0.0363 -0.0026 781 ALA B O   
2441 C CB  . ALA B 100 ? 0.1139 0.1540 0.1072 0.0140  -0.0358 -0.0021 781 ALA B CB  
2442 N N   . VAL B 101 ? 0.0898 0.1322 0.0784 0.0161  -0.0394 -0.0075 782 VAL B N   
2443 C CA  . VAL B 101 ? 0.1601 0.2036 0.1458 0.0171  -0.0396 -0.0063 782 VAL B CA  
2444 C C   . VAL B 101 ? 0.1869 0.2298 0.1623 0.0212  -0.0365 -0.0019 782 VAL B C   
2445 O O   . VAL B 101 ? 0.2045 0.2483 0.1731 0.0260  -0.0359 -0.0025 782 VAL B O   
2446 C CB  . VAL B 101 ? 0.1567 0.2037 0.1468 0.0201  -0.0451 -0.0132 782 VAL B CB  
2447 C CG1 . VAL B 101 ? 0.1902 0.2390 0.1762 0.0236  -0.0460 -0.0115 782 VAL B CG1 
2448 C CG2 . VAL B 101 ? 0.2347 0.2814 0.2398 0.0146  -0.0451 -0.0163 782 VAL B CG2 
2449 N N   . ILE B 102 ? 0.1298 0.1705 0.1049 0.0194  -0.0331 0.0026  783 ILE B N   
2450 C CA  . ILE B 102 ? 0.1605 0.1986 0.1297 0.0223  -0.0279 0.0083  783 ILE B CA  
2451 C C   . ILE B 102 ? 0.1560 0.1927 0.1204 0.0273  -0.0287 0.0100  783 ILE B C   
2452 O O   . ILE B 102 ? 0.1381 0.1741 0.1085 0.0246  -0.0297 0.0091  783 ILE B O   
2453 C CB  . ILE B 102 ? 0.1757 0.2116 0.1522 0.0162  -0.0233 0.0112  783 ILE B CB  
2454 C CG1 . ILE B 102 ? 0.1975 0.2362 0.1793 0.0126  -0.0244 0.0093  783 ILE B CG1 
2455 C CG2 . ILE B 102 ? 0.1811 0.2131 0.1566 0.0183  -0.0159 0.0172  783 ILE B CG2 
2456 C CD1 . ILE B 102 ? 0.1754 0.2142 0.1645 0.0068  -0.0244 0.0088  783 ILE B CD1 
2457 N N   . THR B 103 ? 0.1546 0.1907 0.1072 0.0357  -0.0278 0.0130  784 THR B N   
2458 C CA  . THR B 103 ? 0.1995 0.2341 0.1453 0.0430  -0.0292 0.0160  784 THR B CA  
2459 C C   . THR B 103 ? 0.2350 0.2616 0.1780 0.0446  -0.0194 0.0261  784 THR B C   
2460 O O   . THR B 103 ? 0.2183 0.2420 0.1542 0.0473  -0.0123 0.0315  784 THR B O   
2461 C CB  . THR B 103 ? 0.1671 0.2045 0.1024 0.0510  -0.0340 0.0119  784 THR B CB  
2462 O OG1 . THR B 103 ? 0.2221 0.2581 0.1462 0.0548  -0.0289 0.0146  784 THR B OG1 
2463 C CG2 . THR B 103 ? 0.2538 0.2968 0.2002 0.0466  -0.0416 0.0008  784 THR B CG2 
2464 N N   . LEU B 104 ? 0.1890 0.2113 0.1393 0.0428  -0.0178 0.0284  785 LEU B N   
2465 C CA  . LEU B 104 ? 0.2243 0.2372 0.1775 0.0428  -0.0080 0.0370  785 LEU B CA  
2466 C C   . LEU B 104 ? 0.2233 0.2310 0.1645 0.0546  -0.0067 0.0450  785 LEU B C   
2467 O O   . LEU B 104 ? 0.2383 0.2516 0.1708 0.0624  -0.0157 0.0420  785 LEU B O   
2468 C CB  . LEU B 104 ? 0.1630 0.1734 0.1323 0.0338  -0.0070 0.0331  785 LEU B CB  
2469 C CG  . LEU B 104 ? 0.2012 0.2164 0.1793 0.0240  -0.0087 0.0262  785 LEU B CG  
2470 C CD1 . LEU B 104 ? 0.1689 0.1828 0.1576 0.0175  -0.0095 0.0209  785 LEU B CD1 
2471 C CD2 . LEU B 104 ? 0.2257 0.2393 0.2080 0.0210  -0.0019 0.0295  785 LEU B CD2 
2472 N N   . PRO B 105 ? 0.2843 0.2812 0.2260 0.0568  0.0044  0.0554  786 PRO B N   
2473 C CA  . PRO B 105 ? 0.2760 0.2662 0.2041 0.0699  0.0065  0.0655  786 PRO B CA  
2474 C C   . PRO B 105 ? 0.2296 0.2222 0.1620 0.0735  -0.0025 0.0615  786 PRO B C   
2475 O O   . PRO B 105 ? 0.2442 0.2389 0.1935 0.0645  -0.0050 0.0538  786 PRO B O   
2476 C CB  . PRO B 105 ? 0.2830 0.2591 0.2195 0.0680  0.0221  0.0766  786 PRO B CB  
2477 C CG  . PRO B 105 ? 0.2628 0.2414 0.2101 0.0573  0.0278  0.0732  786 PRO B CG  
2478 C CD  . PRO B 105 ? 0.2737 0.2641 0.2288 0.0486  0.0160  0.0590  786 PRO B CD  
2479 N N   . GLN B 106 ? 0.2649 0.2583 0.1845 0.0845  -0.0067 0.0640  787 GLN B N   
2480 C CA  . GLN B 106 ? 0.3261 0.3233 0.2518 0.0887  -0.0153 0.0600  787 GLN B CA  
2481 C C   . GLN B 106 ? 0.3319 0.3183 0.2712 0.0889  -0.0088 0.0668  787 GLN B C   
2482 O O   . GLN B 106 ? 0.3554 0.3461 0.3054 0.0904  -0.0153 0.0617  787 GLN B O   
2483 C CB  . GLN B 106 ? 0.4216 0.4203 0.3329 0.0990  -0.0192 0.0613  787 GLN B CB  
2484 C CG  . GLN B 106 ? 0.4816 0.4904 0.3997 0.1025  -0.0321 0.0526  787 GLN B CG  
2485 C CD  . GLN B 106 ? 0.5590 0.5815 0.4818 0.0972  -0.0423 0.0385  787 GLN B CD  
2486 O OE1 . GLN B 106 ? 0.5285 0.5530 0.4417 0.0956  -0.0417 0.0354  787 GLN B OE1 
2487 N NE2 . GLN B 106 ? 0.6329 0.6642 0.5725 0.0945  -0.0504 0.0299  787 GLN B NE2 
2488 N N   . SER B 107 ? 0.2841 0.2569 0.2275 0.0852  0.0050  0.0758  788 SER B N   
2489 C CA  . SER B 107 ? 0.2676 0.2288 0.2291 0.0812  0.0129  0.0783  788 SER B CA  
2490 C C   . SER B 107 ? 0.3295 0.2946 0.3110 0.0660  0.0119  0.0649  788 SER B C   
2491 O O   . SER B 107 ? 0.2871 0.2434 0.2842 0.0621  0.0176  0.0638  788 SER B O   
2492 C CB  . SER B 107 ? 0.3298 0.2744 0.2921 0.0821  0.0289  0.0918  788 SER B CB  
2493 O OG  . SER B 107 ? 0.3676 0.3141 0.3331 0.0722  0.0347  0.0896  788 SER B OG  
2494 N N   . THR B 108 ? 0.2610 0.2383 0.2416 0.0584  0.0051  0.0549  789 THR B N   
2495 C CA  . THR B 108 ? 0.2710 0.2515 0.2662 0.0457  0.0046  0.0437  789 THR B CA  
2496 C C   . THR B 108 ? 0.2452 0.2273 0.2503 0.0460  0.0012  0.0373  789 THR B C   
2497 O O   . THR B 108 ? 0.3657 0.3403 0.3832 0.0412  0.0066  0.0339  789 THR B O   
2498 C CB  . THR B 108 ? 0.2096 0.2018 0.1998 0.0398  -0.0018 0.0366  789 THR B CB  
2499 O OG1 . THR B 108 ? 0.3113 0.3025 0.2922 0.0415  0.0017  0.0428  789 THR B OG1 
2500 C CG2 . THR B 108 ? 0.1764 0.1704 0.1776 0.0283  -0.0013 0.0274  789 THR B CG2 
2501 N N   . ARG B 109 ? 0.2053 0.1974 0.2068 0.0516  -0.0075 0.0342  790 ARG B N   
2502 C CA  . ARG B 109 ? 0.2459 0.2406 0.2582 0.0547  -0.0100 0.0296  790 ARG B CA  
2503 C C   . ARG B 109 ? 0.2686 0.2641 0.2924 0.0445  -0.0069 0.0196  790 ARG B C   
2504 O O   . ARG B 109 ? 0.1792 0.1699 0.2135 0.0454  -0.0032 0.0170  790 ARG B O   
2505 C CB  . ARG B 109 ? 0.2440 0.2273 0.2590 0.0643  -0.0055 0.0384  790 ARG B CB  
2506 C CG  . ARG B 109 ? 0.3229 0.3021 0.3223 0.0766  -0.0063 0.0510  790 ARG B CG  
2507 C CD  . ARG B 109 ? 0.3610 0.3538 0.3521 0.0872  -0.0190 0.0494  790 ARG B CD  
2508 N NE  . ARG B 109 ? 0.4155 0.4027 0.3900 0.1019  -0.0197 0.0618  790 ARG B NE  
2509 C CZ  . ARG B 109 ? 0.3744 0.3570 0.3516 0.1098  -0.0202 0.0662  790 ARG B CZ  
2510 N NH1 . ARG B 109 ? 0.2598 0.2425 0.2556 0.1113  -0.0207 0.0625  790 ARG B NH1 
2511 N NH2 . ARG B 109 ? 0.4016 0.3796 0.3624 0.1172  -0.0194 0.0744  790 ARG B NH2 
2512 N N   . ARG B 110 ? 0.2137 0.2152 0.2345 0.0359  -0.0084 0.0138  791 ARG B N   
2513 C CA  . ARG B 110 ? 0.1908 0.1922 0.2175 0.0278  -0.0051 0.0052  791 ARG B CA  
2514 C C   . ARG B 110 ? 0.1287 0.1398 0.1603 0.0276  -0.0074 -0.0009 791 ARG B C   
2515 O O   . ARG B 110 ? 0.1486 0.1685 0.1809 0.0311  -0.0129 -0.0002 791 ARG B O   
2516 C CB  . ARG B 110 ? 0.2091 0.2111 0.2298 0.0196  -0.0050 0.0028  791 ARG B CB  
2517 C CG  . ARG B 110 ? 0.2351 0.2278 0.2585 0.0171  -0.0004 0.0054  791 ARG B CG  
2518 C CD  . ARG B 110 ? 0.2083 0.2042 0.2291 0.0094  -0.0019 0.0007  791 ARG B CD  
2519 N NE  . ARG B 110 ? 0.2142 0.2139 0.2336 0.0053  -0.0033 -0.0085 791 ARG B NE  
2520 C CZ  . ARG B 110 ? 0.2191 0.2138 0.2438 0.0029  -0.0006 -0.0161 791 ARG B CZ  
2521 N NH1 . ARG B 110 ? 0.2797 0.2650 0.3156 0.0032  0.0039  -0.0161 791 ARG B NH1 
2522 N NH2 . ARG B 110 ? 0.1991 0.1978 0.2175 0.0006  -0.0018 -0.0240 791 ARG B NH2 
2523 N N   . GLN B 111 ? 0.1244 0.1338 0.1603 0.0237  -0.0026 -0.0076 792 GLN B N   
2524 C CA  . GLN B 111 ? 0.1380 0.1558 0.1766 0.0215  -0.0016 -0.0128 792 GLN B CA  
2525 C C   . GLN B 111 ? 0.1536 0.1761 0.1830 0.0161  -0.0042 -0.0125 792 GLN B C   
2526 O O   . GLN B 111 ? 0.1585 0.1774 0.1790 0.0129  -0.0057 -0.0109 792 GLN B O   
2527 C CB  . GLN B 111 ? 0.1749 0.1889 0.2155 0.0193  0.0055  -0.0199 792 GLN B CB  
2528 C CG  . GLN B 111 ? 0.2304 0.2384 0.2600 0.0135  0.0069  -0.0240 792 GLN B CG  
2529 C CD  . GLN B 111 ? 0.3063 0.3134 0.3324 0.0121  0.0129  -0.0326 792 GLN B CD  
2530 O OE1 . GLN B 111 ? 0.3312 0.3441 0.3538 0.0118  0.0163  -0.0335 792 GLN B OE1 
2531 N NE2 . GLN B 111 ? 0.2601 0.2590 0.2872 0.0115  0.0151  -0.0393 792 GLN B NE2 
2532 N N   . HIS B 112 ? 0.1257 0.1561 0.1596 0.0152  -0.0042 -0.0139 793 HIS B N   
2533 C CA  . HIS B 112 ? 0.1025 0.1359 0.1294 0.0111  -0.0063 -0.0125 793 HIS B CA  
2534 C C   . HIS B 112 ? 0.1276 0.1659 0.1607 0.0086  -0.0010 -0.0146 793 HIS B C   
2535 O O   . HIS B 112 ? 0.1710 0.2122 0.2152 0.0103  0.0040  -0.0174 793 HIS B O   
2536 C CB  . HIS B 112 ? 0.0980 0.1352 0.1258 0.0138  -0.0139 -0.0093 793 HIS B CB  
2537 C CG  . HIS B 112 ? 0.1939 0.2391 0.2357 0.0187  -0.0178 -0.0112 793 HIS B CG  
2538 N ND1 . HIS B 112 ? 0.1627 0.2158 0.2161 0.0168  -0.0188 -0.0145 793 HIS B ND1 
2539 C CD2 . HIS B 112 ? 0.1216 0.1683 0.1694 0.0260  -0.0212 -0.0106 793 HIS B CD2 
2540 C CE1 . HIS B 112 ? 0.1477 0.2087 0.2154 0.0223  -0.0239 -0.0175 793 HIS B CE1 
2541 N NE2 . HIS B 112 ? 0.2003 0.2578 0.2633 0.0286  -0.0260 -0.0148 793 HIS B NE2 
2542 N N   . ALA B 113 ? 0.1194 0.1582 0.1463 0.0050  -0.0009 -0.0125 794 ALA B N   
2543 C CA  . ALA B 113 ? 0.1198 0.1618 0.1541 0.0027  0.0053  -0.0123 794 ALA B CA  
2544 C C   . ALA B 113 ? 0.1362 0.1854 0.1878 0.0029  0.0003  -0.0132 794 ALA B C   
2545 O O   . ALA B 113 ? 0.1129 0.1639 0.1637 0.0052  -0.0087 -0.0135 794 ALA B O   
2546 C CB  . ALA B 113 ? 0.1471 0.1842 0.1655 -0.0002 0.0086  -0.0087 794 ALA B CB  
2547 N N   . ASN B 114 ? 0.1463 0.2187 0.3121 0.0495  -0.0686 -0.0145 795 ASN B N   
2548 C CA  . ASN B 114 ? 0.1301 0.2162 0.3004 0.0497  -0.0800 -0.0140 795 ASN B CA  
2549 C C   . ASN B 114 ? 0.1130 0.2088 0.2706 0.0389  -0.0732 -0.0172 795 ASN B C   
2550 O O   . ASN B 114 ? 0.1152 0.2183 0.2808 0.0334  -0.0600 -0.0245 795 ASN B O   
2551 C CB  . ASN B 114 ? 0.1344 0.2334 0.3342 0.0538  -0.0784 -0.0213 795 ASN B CB  
2552 C CG  . ASN B 114 ? 0.2040 0.2937 0.4178 0.0655  -0.0871 -0.0178 795 ASN B CG  
2553 O OD1 . ASN B 114 ? 0.2216 0.2952 0.4171 0.0703  -0.1005 -0.0071 795 ASN B OD1 
2554 N ND2 . ASN B 114 ? 0.3147 0.4124 0.5597 0.0695  -0.0789 -0.0271 795 ASN B ND2 
2555 N N   . LEU B 115 ? 0.1189 0.2128 0.2557 0.0354  -0.0816 -0.0120 796 LEU B N   
2556 C CA  . LEU B 115 ? 0.1073 0.2094 0.2358 0.0266  -0.0756 -0.0156 796 LEU B CA  
2557 C C   . LEU B 115 ? 0.1257 0.2417 0.2743 0.0250  -0.0720 -0.0226 796 LEU B C   
2558 O O   . LEU B 115 ? 0.1158 0.2371 0.2780 0.0298  -0.0797 -0.0227 796 LEU B O   
2559 C CB  . LEU B 115 ? 0.1217 0.2177 0.2252 0.0228  -0.0847 -0.0102 796 LEU B CB  
2560 C CG  . LEU B 115 ? 0.1092 0.2106 0.2039 0.0144  -0.0790 -0.0142 796 LEU B CG  
2561 C CD1 . LEU B 115 ? 0.1170 0.2155 0.2051 0.0111  -0.0684 -0.0158 796 LEU B CD1 
2562 C CD2 . LEU B 115 ? 0.1413 0.2373 0.2141 0.0104  -0.0889 -0.0111 796 LEU B CD2 
2563 N N   . VAL B 116 ? 0.0918 0.2129 0.2421 0.0179  -0.0607 -0.0285 797 VAL B N   
2564 C CA  . VAL B 116 ? 0.1169 0.2492 0.2850 0.0145  -0.0557 -0.0364 797 VAL B CA  
2565 C C   . VAL B 116 ? 0.1008 0.2394 0.2679 0.0136  -0.0662 -0.0352 797 VAL B C   
2566 O O   . VAL B 116 ? 0.1150 0.2488 0.2624 0.0111  -0.0727 -0.0303 797 VAL B O   
2567 C CB  . VAL B 116 ? 0.0811 0.2129 0.2447 0.0056  -0.0431 -0.0417 797 VAL B CB  
2568 C CG1 . VAL B 116 ? 0.1734 0.3001 0.3164 0.0010  -0.0454 -0.0383 797 VAL B CG1 
2569 C CG2 . VAL B 116 ? 0.2318 0.3731 0.4138 0.0007  -0.0356 -0.0515 797 VAL B CG2 
2570 N N   . GLU B 117 ? 0.1071 0.2577 0.2968 0.0151  -0.0678 -0.0408 798 GLU B N   
2571 C CA  . GLU B 117 ? 0.2138 0.3730 0.4054 0.0145  -0.0801 -0.0396 798 GLU B CA  
2572 C C   . GLU B 117 ? 0.2495 0.4112 0.4311 0.0041  -0.0765 -0.0435 798 GLU B C   
2573 O O   . GLU B 117 ? 0.2495 0.4088 0.4140 0.0005  -0.0853 -0.0396 798 GLU B O   
2574 C CB  . GLU B 117 ? 0.2245 0.3979 0.4471 0.0194  -0.0834 -0.0454 798 GLU B CB  
2575 C CG  . GLU B 117 ? 0.3683 0.5524 0.5953 0.0202  -0.0995 -0.0430 798 GLU B CG  
2576 C CD  . GLU B 117 ? 0.5817 0.7820 0.8442 0.0263  -0.1035 -0.0494 798 GLU B CD  
2577 O OE1 . GLU B 117 ? 0.5718 0.7751 0.8555 0.0279  -0.0909 -0.0578 798 GLU B OE1 
2578 O OE2 . GLU B 117 ? 0.3741 0.5844 0.6434 0.0289  -0.1193 -0.0466 798 GLU B OE2 
2579 N N   . ASN B 118 ? 0.2230 0.3875 0.4134 -0.0020 -0.0633 -0.0520 799 ASN B N   
2580 C CA  A ASN B 118 ? 0.2401 0.4041 0.4217 -0.0118 -0.0585 -0.0567 799 ASN B CA  
2581 C CA  B ASN B 118 ? 0.2397 0.4035 0.4208 -0.0118 -0.0587 -0.0565 799 ASN B CA  
2582 C C   . ASN B 118 ? 0.2162 0.3692 0.3871 -0.0162 -0.0452 -0.0585 799 ASN B C   
2583 O O   . ASN B 118 ? 0.2031 0.3535 0.3794 -0.0143 -0.0374 -0.0594 799 ASN B O   
2584 C CB  A ASN B 118 ? 0.2371 0.4150 0.4392 -0.0173 -0.0559 -0.0665 799 ASN B CB  
2585 C CB  B ASN B 118 ? 0.2370 0.4148 0.4377 -0.0174 -0.0569 -0.0660 799 ASN B CB  
2586 C CG  A ASN B 118 ? 0.2248 0.4160 0.4385 -0.0140 -0.0713 -0.0647 799 ASN B CG  
2587 C CG  B ASN B 118 ? 0.2003 0.3848 0.4241 -0.0169 -0.0457 -0.0745 799 ASN B CG  
2588 O OD1 A ASN B 118 ? 0.2352 0.4260 0.4350 -0.0178 -0.0815 -0.0612 799 ASN B OD1 
2589 O OD1 B ASN B 118 ? 0.1997 0.3755 0.4191 -0.0190 -0.0333 -0.0765 799 ASN B OD1 
2590 N ND2 A ASN B 118 ? 0.2596 0.4626 0.4994 -0.0076 -0.0734 -0.0679 799 ASN B ND2 
2591 N ND2 B ASN B 118 ? 0.2732 0.4735 0.5219 -0.0151 -0.0501 -0.0802 799 ASN B ND2 
2592 N N   . TYR B 119 ? 0.2423 0.3889 0.3984 -0.0229 -0.0430 -0.0597 800 TYR B N   
2593 C CA  . TYR B 119 ? 0.1592 0.2956 0.3057 -0.0277 -0.0323 -0.0611 800 TYR B CA  
2594 C C   . TYR B 119 ? 0.1399 0.2774 0.2967 -0.0356 -0.0196 -0.0693 800 TYR B C   
2595 O O   . TYR B 119 ? 0.2553 0.3999 0.4222 -0.0411 -0.0169 -0.0765 800 TYR B O   
2596 C CB  . TYR B 119 ? 0.1889 0.3181 0.3205 -0.0331 -0.0330 -0.0623 800 TYR B CB  
2597 C CG  . TYR B 119 ? 0.1580 0.2749 0.2819 -0.0403 -0.0223 -0.0650 800 TYR B CG  
2598 C CD1 . TYR B 119 ? 0.0967 0.1978 0.2040 -0.0349 -0.0205 -0.0561 800 TYR B CD1 
2599 C CD2 . TYR B 119 ? 0.1080 0.2210 0.2335 -0.0512 -0.0133 -0.0727 800 TYR B CD2 
2600 C CE1 . TYR B 119 ? 0.1568 0.2385 0.2502 -0.0384 -0.0126 -0.0535 800 TYR B CE1 
2601 C CE2 . TYR B 119 ? 0.1311 0.2210 0.2388 -0.0559 -0.0036 -0.0699 800 TYR B CE2 
2602 C CZ  . TYR B 119 ? 0.1469 0.2208 0.2386 -0.0486 -0.0046 -0.0596 800 TYR B CZ  
2603 O OH  . TYR B 119 ? 0.2026 0.2521 0.2766 -0.0519 0.0017  -0.0553 800 TYR B OH  
2604 N N   . SER B 120 ? 0.0919 0.2218 0.2445 -0.0378 -0.0111 -0.0686 801 SER B N   
2605 C CA  A SER B 120 ? 0.1491 0.2737 0.3025 -0.0490 0.0035  -0.0757 801 SER B CA  
2606 C CA  B SER B 120 ? 0.1497 0.2743 0.3032 -0.0489 0.0035  -0.0757 801 SER B CA  
2607 C C   . SER B 120 ? 0.2112 0.3142 0.3395 -0.0549 0.0087  -0.0701 801 SER B C   
2608 O O   . SER B 120 ? 0.2137 0.3080 0.3289 -0.0477 0.0044  -0.0607 801 SER B O   
2609 C CB  A SER B 120 ? 0.1718 0.3015 0.3383 -0.0474 0.0104  -0.0796 801 SER B CB  
2610 C CB  B SER B 120 ? 0.1715 0.3015 0.3382 -0.0470 0.0101  -0.0794 801 SER B CB  
2611 O OG  A SER B 120 ? 0.1529 0.2971 0.3411 -0.0438 0.0083  -0.0861 801 SER B OG  
2612 O OG  B SER B 120 ? 0.1377 0.2600 0.3007 -0.0598 0.0261  -0.0873 801 SER B OG  
2613 N N   . LYS B 121 ? 0.1426 0.2314 0.2587 -0.0660 0.0172  -0.0733 802 LYS B N   
2614 C CA  . LYS B 121 ? 0.2177 0.2775 0.3034 -0.0686 0.0200  -0.0642 802 LYS B CA  
2615 C C   . LYS B 121 ? 0.1748 0.2240 0.2473 -0.0707 0.0246  -0.0595 802 LYS B C   
2616 O O   . LYS B 121 ? 0.1747 0.2288 0.2543 -0.0794 0.0351  -0.0675 802 LYS B O   
2617 C CB  . LYS B 121 ? 0.1999 0.2426 0.2735 -0.0819 0.0296  -0.0690 802 LYS B CB  
2618 C CG  . LYS B 121 ? 0.2711 0.2791 0.3116 -0.0856 0.0320  -0.0590 802 LYS B CG  
2619 C CD  . LYS B 121 ? 0.3335 0.3310 0.3661 -0.0738 0.0214  -0.0497 802 LYS B CD  
2620 C CE  . LYS B 121 ? 0.2191 0.1806 0.2240 -0.0780 0.0232  -0.0419 802 LYS B CE  
2621 N NZ  . LYS B 121 ? 0.3109 0.2531 0.2925 -0.0854 0.0261  -0.0354 802 LYS B NZ  
2622 N N   . VAL B 122 ? 0.1670 0.2027 0.2216 -0.0636 0.0171  -0.0478 803 VAL B N   
2623 C CA  . VAL B 122 ? 0.2048 0.2267 0.2404 -0.0671 0.0191  -0.0419 803 VAL B CA  
2624 C C   . VAL B 122 ? 0.2157 0.2067 0.2210 -0.0761 0.0216  -0.0357 803 VAL B C   
2625 O O   . VAL B 122 ? 0.2408 0.2198 0.2393 -0.0710 0.0150  -0.0298 803 VAL B O   
2626 C CB  . VAL B 122 ? 0.1501 0.1774 0.1857 -0.0549 0.0078  -0.0332 803 VAL B CB  
2627 C CG1 . VAL B 122 ? 0.1825 0.1949 0.1960 -0.0602 0.0085  -0.0272 803 VAL B CG1 
2628 C CG2 . VAL B 122 ? 0.1949 0.2469 0.2556 -0.0471 0.0056  -0.0383 803 VAL B CG2 
2629 N N   . ASN B 123 ? 0.2149 0.1903 0.2004 -0.0900 0.0313  -0.0372 804 ASN B N   
2630 C CA  . ASN B 123 ? 0.3089 0.2497 0.2595 -0.1015 0.0341  -0.0309 804 ASN B CA  
2631 C C   . ASN B 123 ? 0.3893 0.3110 0.3111 -0.1021 0.0256  -0.0186 804 ASN B C   
2632 O O   . ASN B 123 ? 0.3123 0.2472 0.2391 -0.0995 0.0238  -0.0189 804 ASN B O   
2633 C CB  . ASN B 123 ? 0.2754 0.2074 0.2177 -0.1216 0.0532  -0.0424 804 ASN B CB  
2634 C CG  . ASN B 123 ? 0.4115 0.3566 0.3768 -0.1242 0.0603  -0.0536 804 ASN B CG  
2635 O OD1 . ASN B 123 ? 0.3654 0.3195 0.3454 -0.1123 0.0507  -0.0514 804 ASN B OD1 
2636 N ND2 . ASN B 123 ? 0.4377 0.3846 0.4056 -0.1393 0.0774  -0.0664 804 ASN B ND2 
2637 N N   . VAL B 124 ? 0.3135 0.2025 0.2044 -0.1058 0.0193  -0.0076 805 VAL B N   
2638 C CA  . VAL B 124 ? 0.3841 0.2498 0.2410 -0.1107 0.0105  0.0042  805 VAL B CA  
2639 C C   . VAL B 124 ? 0.3542 0.2147 0.1923 -0.1299 0.0258  -0.0036 805 VAL B C   
2640 O O   . VAL B 124 ? 0.4585 0.3165 0.2963 -0.1442 0.0443  -0.0155 805 VAL B O   
2641 C CB  . VAL B 124 ? 0.4490 0.2752 0.2733 -0.1134 0.0018  0.0171  805 VAL B CB  
2642 C CG1 . VAL B 124 ? 0.4798 0.2793 0.2643 -0.1206 -0.0098 0.0303  805 VAL B CG1 
2643 C CG2 . VAL B 124 ? 0.3782 0.2100 0.2252 -0.0934 -0.0117 0.0231  805 VAL B CG2 
2644 N N   . ASN B 125 ? 0.3638 0.2239 0.1881 -0.1313 0.0192  0.0013  806 ASN B N   
2645 C CA  . ASN B 125 ? 0.4737 0.3289 0.2791 -0.1489 0.0329  -0.0061 806 ASN B CA  
2646 C C   . ASN B 125 ? 0.3375 0.2273 0.1825 -0.1454 0.0467  -0.0222 806 ASN B C   
2647 O O   . ASN B 125 ? 0.4229 0.3113 0.2593 -0.1589 0.0610  -0.0315 806 ASN B O   
2648 C CB  . ASN B 125 ? 0.4483 0.2701 0.2147 -0.1732 0.0488  -0.0098 806 ASN B CB  
2649 C CG  . ASN B 125 ? 0.5189 0.3015 0.2382 -0.1776 0.0333  0.0071  806 ASN B CG  
2650 O OD1 . ASN B 125 ? 0.5791 0.3537 0.2817 -0.1734 0.0147  0.0208  806 ASN B OD1 
2651 N ND2 . ASN B 125 ? 0.6109 0.3707 0.3107 -0.1840 0.0390  0.0058  806 ASN B ND2 
2652 N N   . ASP B 126 ? 0.3298 0.2482 0.2164 -0.1282 0.0429  -0.0260 807 ASP B N   
2653 C CA  . ASP B 126 ? 0.3016 0.2507 0.2244 -0.1214 0.0498  -0.0374 807 ASP B CA  
2654 C C   . ASP B 126 ? 0.2626 0.2155 0.1795 -0.1169 0.0419  -0.0322 807 ASP B C   
2655 O O   . ASP B 126 ? 0.3421 0.2861 0.2422 -0.1116 0.0258  -0.0193 807 ASP B O   
2656 C CB  . ASP B 126 ? 0.2596 0.2346 0.2207 -0.1039 0.0426  -0.0392 807 ASP B CB  
2657 C CG  . ASP B 126 ? 0.3108 0.2909 0.2874 -0.1093 0.0531  -0.0493 807 ASP B CG  
2658 O OD1 . ASP B 126 ? 0.3209 0.2830 0.2782 -0.1268 0.0667  -0.0547 807 ASP B OD1 
2659 O OD2 . ASP B 126 ? 0.2204 0.2220 0.2267 -0.0975 0.0476  -0.0523 807 ASP B OD2 
2660 N N   . LYS B 127 ? 0.3472 0.3140 0.2809 -0.1188 0.0533  -0.0431 808 LYS B N   
2661 C CA  . LYS B 127 ? 0.3169 0.2882 0.2481 -0.1150 0.0481  -0.0404 808 LYS B CA  
2662 C C   . LYS B 127 ? 0.2456 0.2437 0.2156 -0.0964 0.0422  -0.0423 808 LYS B C   
2663 O O   . LYS B 127 ? 0.2856 0.2995 0.2859 -0.0918 0.0504  -0.0522 808 LYS B O   
2664 C CB  . LYS B 127 ? 0.3334 0.2947 0.2496 -0.1322 0.0660  -0.0511 808 LYS B CB  
2665 C CG  . LYS B 127 ? 0.3680 0.2973 0.2346 -0.1530 0.0689  -0.0465 808 LYS B CG  
2666 C CD  . LYS B 127 ? 0.5049 0.4237 0.3529 -0.1662 0.0870  -0.0593 808 LYS B CD  
2667 C CE  . LYS B 127 ? 0.4963 0.3820 0.2906 -0.1832 0.0855  -0.0545 808 LYS B CE  
2668 N NZ  . LYS B 127 ? 0.6860 0.5587 0.4571 -0.1968 0.0998  -0.0683 808 LYS B NZ  
2669 N N   . LEU B 128 ? 0.2326 0.2351 0.2011 -0.0863 0.0274  -0.0326 809 LEU B N   
2670 C CA  . LEU B 128 ? 0.1620 0.1845 0.1588 -0.0705 0.0206  -0.0322 809 LEU B CA  
2671 C C   . LEU B 128 ? 0.1693 0.1932 0.1634 -0.0706 0.0210  -0.0326 809 LEU B C   
2672 O O   . LEU B 128 ? 0.1890 0.2002 0.1580 -0.0817 0.0221  -0.0310 809 LEU B O   
2673 C CB  . LEU B 128 ? 0.1792 0.2062 0.1789 -0.0594 0.0054  -0.0224 809 LEU B CB  
2674 C CG  . LEU B 128 ? 0.1685 0.1928 0.1713 -0.0582 0.0045  -0.0219 809 LEU B CG  
2675 C CD1 . LEU B 128 ? 0.1754 0.2019 0.1809 -0.0477 -0.0088 -0.0135 809 LEU B CD1 
2676 C CD2 . LEU B 128 ? 0.2101 0.2488 0.2391 -0.0552 0.0121  -0.0317 809 LEU B CD2 
2677 N N   . ASN B 129 ? 0.1427 0.1801 0.1602 -0.0592 0.0195  -0.0346 810 ASN B N   
2678 C CA  . ASN B 129 ? 0.1408 0.1781 0.1571 -0.0586 0.0204  -0.0352 810 ASN B CA  
2679 C C   . ASN B 129 ? 0.1332 0.1797 0.1571 -0.0472 0.0079  -0.0278 810 ASN B C   
2680 O O   . ASN B 129 ? 0.1568 0.2122 0.1992 -0.0368 0.0047  -0.0278 810 ASN B O   
2681 C CB  . ASN B 129 ? 0.1982 0.2374 0.2336 -0.0573 0.0331  -0.0457 810 ASN B CB  
2682 C CG  . ASN B 129 ? 0.2537 0.2820 0.2784 -0.0722 0.0493  -0.0555 810 ASN B CG  
2683 O OD1 . ASN B 129 ? 0.2072 0.2238 0.2110 -0.0830 0.0549  -0.0573 810 ASN B OD1 
2684 N ND2 . ASN B 129 ? 0.1839 0.2155 0.2207 -0.0750 0.0578  -0.0629 810 ASN B ND2 
2685 N N   . VAL B 130 ? 0.1982 0.2427 0.2072 -0.0504 0.0009  -0.0222 811 VAL B N   
2686 C CA  . VAL B 130 ? 0.1381 0.1918 0.1536 -0.0423 -0.0092 -0.0166 811 VAL B CA  
2687 C C   . VAL B 130 ? 0.1473 0.2003 0.1588 -0.0454 -0.0072 -0.0179 811 VAL B C   
2688 O O   . VAL B 130 ? 0.1342 0.1801 0.1308 -0.0559 -0.0036 -0.0200 811 VAL B O   
2689 C CB  . VAL B 130 ? 0.1239 0.1792 0.1320 -0.0424 -0.0200 -0.0098 811 VAL B CB  
2690 C CG1 . VAL B 130 ? 0.1478 0.2149 0.1690 -0.0335 -0.0272 -0.0070 811 VAL B CG1 
2691 C CG2 . VAL B 130 ? 0.1834 0.2323 0.1888 -0.0428 -0.0199 -0.0088 811 VAL B CG2 
2692 N N   . TYR B 131 ? 0.1082 0.1663 0.1300 -0.0380 -0.0088 -0.0170 812 TYR B N   
2693 C CA  . TYR B 131 ? 0.1618 0.2165 0.1792 -0.0411 -0.0056 -0.0184 812 TYR B CA  
2694 C C   . TYR B 131 ? 0.1189 0.1830 0.1387 -0.0390 -0.0123 -0.0151 812 TYR B C   
2695 O O   . TYR B 131 ? 0.1084 0.1793 0.1366 -0.0319 -0.0170 -0.0127 812 TYR B O   
2696 C CB  . TYR B 131 ? 0.1444 0.1910 0.1698 -0.0354 0.0008  -0.0212 812 TYR B CB  
2697 C CG  . TYR B 131 ? 0.1342 0.1734 0.1638 -0.0374 0.0101  -0.0275 812 TYR B CG  
2698 C CD1 . TYR B 131 ? 0.1318 0.1758 0.1720 -0.0343 0.0108  -0.0296 812 TYR B CD1 
2699 C CD2 . TYR B 131 ? 0.1962 0.2236 0.2209 -0.0432 0.0200  -0.0330 812 TYR B CD2 
2700 C CE1 . TYR B 131 ? 0.1563 0.1957 0.2041 -0.0372 0.0217  -0.0377 812 TYR B CE1 
2701 C CE2 . TYR B 131 ? 0.1878 0.2090 0.2198 -0.0453 0.0312  -0.0412 812 TYR B CE2 
2702 C CZ  . TYR B 131 ? 0.1822 0.2104 0.2267 -0.0424 0.0323  -0.0438 812 TYR B CZ  
2703 O OH  . TYR B 131 ? 0.2154 0.2394 0.2705 -0.0458 0.0458  -0.0542 812 TYR B OH  
2704 N N   . GLY B 132 ? 0.1403 0.2050 0.1531 -0.0467 -0.0113 -0.0165 813 GLY B N   
2705 C CA  . GLY B 132 ? 0.1502 0.2264 0.1687 -0.0466 -0.0155 -0.0157 813 GLY B CA  
2706 C C   . GLY B 132 ? 0.1364 0.2146 0.1482 -0.0576 -0.0136 -0.0190 813 GLY B C   
2707 O O   . GLY B 132 ? 0.1311 0.1989 0.1311 -0.0655 -0.0083 -0.0217 813 GLY B O   
2708 N N   . TYR B 133 ? 0.1146 0.2071 0.1355 -0.0591 -0.0168 -0.0202 814 TYR B N   
2709 C CA  . TYR B 133 ? 0.1670 0.2662 0.1859 -0.0706 -0.0154 -0.0247 814 TYR B CA  
2710 C C   . TYR B 133 ? 0.1970 0.3190 0.2315 -0.0711 -0.0270 -0.0250 814 TYR B C   
2711 O O   . TYR B 133 ? 0.1180 0.2544 0.1680 -0.0708 -0.0265 -0.0286 814 TYR B O   
2712 C CB  . TYR B 133 ? 0.1285 0.2221 0.1451 -0.0740 -0.0056 -0.0282 814 TYR B CB  
2713 C CG  . TYR B 133 ? 0.1399 0.2081 0.1406 -0.0734 0.0033  -0.0271 814 TYR B CG  
2714 C CD1 . TYR B 133 ? 0.1358 0.1933 0.1365 -0.0623 0.0032  -0.0226 814 TYR B CD1 
2715 C CD2 . TYR B 133 ? 0.1815 0.2362 0.1689 -0.0839 0.0110  -0.0308 814 TYR B CD2 
2716 C CE1 . TYR B 133 ? 0.2027 0.2380 0.1938 -0.0596 0.0088  -0.0213 814 TYR B CE1 
2717 C CE2 . TYR B 133 ? 0.2169 0.2465 0.1932 -0.0814 0.0188  -0.0300 814 TYR B CE2 
2718 C CZ  . TYR B 133 ? 0.2237 0.2445 0.2036 -0.0683 0.0168  -0.0249 814 TYR B CZ  
2719 O OH  . TYR B 133 ? 0.2117 0.2090 0.1856 -0.0638 0.0221  -0.0237 814 TYR B OH  
2720 N N   . PRO B 134 ? 0.1890 0.3115 0.2193 -0.0708 -0.0371 -0.0209 815 PRO B N   
2721 C CA  . PRO B 134 ? 0.1982 0.3324 0.2413 -0.0669 -0.0490 -0.0190 815 PRO B CA  
2722 C C   . PRO B 134 ? 0.2344 0.3763 0.2795 -0.0762 -0.0476 -0.0243 815 PRO B C   
2723 O O   . PRO B 134 ? 0.2548 0.3874 0.2811 -0.0877 -0.0416 -0.0268 815 PRO B O   
2724 C CB  . PRO B 134 ? 0.1895 0.3132 0.2165 -0.0679 -0.0582 -0.0129 815 PRO B CB  
2725 C CG  . PRO B 134 ? 0.1810 0.2889 0.1848 -0.0781 -0.0478 -0.0149 815 PRO B CG  
2726 C CD  . PRO B 134 ? 0.1340 0.2396 0.1451 -0.0734 -0.0361 -0.0180 815 PRO B CD  
2727 N N   . ARG B 135 ? 0.1460 0.3047 0.2153 -0.0717 -0.0520 -0.0271 816 ARG B N   
2728 C CA  . ARG B 135 ? 0.2041 0.3741 0.2813 -0.0802 -0.0503 -0.0334 816 ARG B CA  
2729 C C   . ARG B 135 ? 0.1984 0.3608 0.2619 -0.0909 -0.0331 -0.0395 816 ARG B C   
2730 O O   . ARG B 135 ? 0.2827 0.4472 0.3413 -0.1017 -0.0291 -0.0446 816 ARG B O   
2731 C CB  . ARG B 135 ? 0.2040 0.3742 0.2721 -0.0868 -0.0617 -0.0319 816 ARG B CB  
2732 C CG  . ARG B 135 ? 0.5015 0.6727 0.5751 -0.0775 -0.0800 -0.0254 816 ARG B CG  
2733 C CD  . ARG B 135 ? 0.5188 0.7080 0.6291 -0.0661 -0.0904 -0.0266 816 ARG B CD  
2734 N NE  . ARG B 135 ? 0.5655 0.7532 0.6792 -0.0551 -0.1074 -0.0219 816 ARG B NE  
2735 C CZ  . ARG B 135 ? 0.5541 0.7577 0.6987 -0.0439 -0.1206 -0.0250 816 ARG B CZ  
2736 N NH1 . ARG B 135 ? 0.6950 0.9111 0.8706 -0.0464 -0.1193 -0.0239 816 ARG B NH1 
2737 N NH2 . ARG B 135 ? 0.5655 0.7744 0.7009 -0.0340 -0.1302 -0.0212 816 ARG B NH2 
2738 N N   . GLY B 136 ? 0.1580 0.3100 0.2143 -0.0884 -0.0235 -0.0391 817 GLY B N   
2739 C CA  . GLY B 136 ? 0.1996 0.3387 0.2411 -0.0982 -0.0086 -0.0438 817 GLY B CA  
2740 C C   . GLY B 136 ? 0.2438 0.3619 0.2605 -0.1067 -0.0034 -0.0432 817 GLY B C   
2741 O O   . GLY B 136 ? 0.2825 0.3849 0.2858 -0.1153 0.0088  -0.0469 817 GLY B O   
2742 N N   . GLU B 137 ? 0.1586 0.2724 0.1673 -0.1052 -0.0110 -0.0391 818 GLU B N   
2743 C CA  . GLU B 137 ? 0.2050 0.2980 0.1912 -0.1140 -0.0039 -0.0406 818 GLU B CA  
2744 C C   . GLU B 137 ? 0.1832 0.2644 0.1644 -0.1061 -0.0048 -0.0361 818 GLU B C   
2745 O O   . GLU B 137 ? 0.1661 0.2570 0.1552 -0.0982 -0.0152 -0.0311 818 GLU B O   
2746 C CB  . GLU B 137 ? 0.2417 0.3370 0.2177 -0.1228 -0.0082 -0.0419 818 GLU B CB  
2747 C CG  . GLU B 137 ? 0.2014 0.3088 0.1840 -0.1298 -0.0067 -0.0470 818 GLU B CG  
2748 C CD  . GLU B 137 ? 0.2244 0.3349 0.1970 -0.1396 -0.0122 -0.0483 818 GLU B CD  
2749 O OE1 . GLU B 137 ? 0.3680 0.4672 0.3233 -0.1428 -0.0146 -0.0454 818 GLU B OE1 
2750 O OE2 . GLU B 137 ? 0.3498 0.4741 0.3313 -0.1452 -0.0137 -0.0527 818 GLU B OE2 
2751 N N   . TYR B 138 ? 0.2069 0.2647 0.1762 -0.1058 0.0072  -0.0375 819 TYR B N   
2752 C CA  . TYR B 138 ? 0.1719 0.2181 0.1412 -0.0954 0.0091  -0.0343 819 TYR B CA  
2753 C C   . TYR B 138 ? 0.1956 0.2441 0.1574 -0.0994 0.0034  -0.0334 819 TYR B C   
2754 O O   . TYR B 138 ? 0.2151 0.2618 0.1621 -0.1133 0.0031  -0.0369 819 TYR B O   
2755 C CB  . TYR B 138 ? 0.1858 0.2076 0.1475 -0.0954 0.0228  -0.0379 819 TYR B CB  
2756 C CG  . TYR B 138 ? 0.1826 0.1952 0.1498 -0.0855 0.0260  -0.0371 819 TYR B CG  
2757 C CD1 . TYR B 138 ? 0.1938 0.2055 0.1742 -0.0708 0.0236  -0.0326 819 TYR B CD1 
2758 C CD2 . TYR B 138 ? 0.1942 0.1992 0.1533 -0.0926 0.0323  -0.0422 819 TYR B CD2 
2759 C CE1 . TYR B 138 ? 0.1852 0.1923 0.1755 -0.0622 0.0261  -0.0333 819 TYR B CE1 
2760 C CE2 . TYR B 138 ? 0.2021 0.2009 0.1701 -0.0848 0.0375  -0.0439 819 TYR B CE2 
2761 C CZ  . TYR B 138 ? 0.2154 0.2170 0.2014 -0.0691 0.0338  -0.0395 819 TYR B CZ  
2762 O OH  . TYR B 138 ? 0.2280 0.2275 0.2275 -0.0619 0.0383  -0.0425 819 TYR B OH  
2763 N N   . ALA B 139 ? 0.1996 0.2498 0.1686 -0.0890 -0.0006 -0.0289 820 ALA B N   
2764 C CA  . ALA B 139 ? 0.2046 0.2506 0.1622 -0.0935 -0.0034 -0.0280 820 ALA B CA  
2765 C C   . ALA B 139 ? 0.1651 0.2047 0.1309 -0.0833 0.0017  -0.0272 820 ALA B C   
2766 O O   . ALA B 139 ? 0.1485 0.1934 0.1305 -0.0708 0.0001  -0.0246 820 ALA B O   
2767 C CB  . ALA B 139 ? 0.2059 0.2660 0.1632 -0.0944 -0.0200 -0.0219 820 ALA B CB  
2768 N N   . HIS B 140 ? 0.1794 0.2076 0.1328 -0.0905 0.0084  -0.0307 821 HIS B N   
2769 C CA  . HIS B 140 ? 0.1742 0.1987 0.1360 -0.0840 0.0135  -0.0317 821 HIS B CA  
2770 C C   . HIS B 140 ? 0.2077 0.2286 0.1519 -0.0921 0.0081  -0.0285 821 HIS B C   
2771 O O   . HIS B 140 ? 0.2389 0.2484 0.1593 -0.1073 0.0120  -0.0316 821 HIS B O   
2772 C CB  . HIS B 140 ? 0.1838 0.1960 0.1495 -0.0861 0.0306  -0.0414 821 HIS B CB  
2773 C CG  . HIS B 140 ? 0.1992 0.2103 0.1760 -0.0823 0.0374  -0.0451 821 HIS B CG  
2774 N ND1 . HIS B 140 ? 0.2427 0.2436 0.2207 -0.0890 0.0541  -0.0560 821 HIS B ND1 
2775 C CD2 . HIS B 140 ? 0.2194 0.2393 0.2083 -0.0736 0.0311  -0.0410 821 HIS B CD2 
2776 C CE1 . HIS B 140 ? 0.2007 0.2061 0.1929 -0.0847 0.0575  -0.0587 821 HIS B CE1 
2777 N NE2 . HIS B 140 ? 0.1822 0.1985 0.1799 -0.0756 0.0433  -0.0494 821 HIS B NE2 
2778 N N   . LEU B 141 ? 0.1755 0.2030 0.1281 -0.0832 -0.0010 -0.0221 822 LEU B N   
2779 C CA  . LEU B 141 ? 0.2414 0.2600 0.1760 -0.0900 -0.0052 -0.0183 822 LEU B CA  
2780 C C   . LEU B 141 ? 0.2156 0.2248 0.1513 -0.0935 0.0105  -0.0260 822 LEU B C   
2781 O O   . LEU B 141 ? 0.1799 0.1963 0.1376 -0.0827 0.0133  -0.0276 822 LEU B O   
2782 C CB  . LEU B 141 ? 0.2087 0.2356 0.1529 -0.0791 -0.0197 -0.0094 822 LEU B CB  
2783 C CG  . LEU B 141 ? 0.2106 0.2523 0.1655 -0.0727 -0.0335 -0.0041 822 LEU B CG  
2784 C CD1 . LEU B 141 ? 0.2986 0.3455 0.2643 -0.0621 -0.0454 0.0029  822 LEU B CD1 
2785 C CD2 . LEU B 141 ? 0.2299 0.2699 0.1660 -0.0848 -0.0411 -0.0026 822 LEU B CD2 
2786 N N   . LYS B 142 ? 0.2241 0.2183 0.1371 -0.1096 0.0214  -0.0322 823 LYS B N   
2787 C CA  . LYS B 142 ? 0.2317 0.2187 0.1499 -0.1149 0.0406  -0.0435 823 LYS B CA  
2788 C C   . LYS B 142 ? 0.2478 0.2244 0.1499 -0.1226 0.0416  -0.0416 823 LYS B C   
2789 O O   . LYS B 142 ? 0.2779 0.2378 0.1444 -0.1375 0.0380  -0.0374 823 LYS B O   
2790 C CB  . LYS B 142 ? 0.3082 0.2824 0.2099 -0.1303 0.0559  -0.0539 823 LYS B CB  
2791 C CG  . LYS B 142 ? 0.2658 0.2338 0.1779 -0.1362 0.0788  -0.0687 823 LYS B CG  
2792 C CD  . LYS B 142 ? 0.2957 0.2485 0.1864 -0.1509 0.0945  -0.0794 823 LYS B CD  
2793 C CE  . LYS B 142 ? 0.3099 0.2571 0.2109 -0.1525 0.1165  -0.0958 823 LYS B CE  
2794 N NZ  . LYS B 142 ? 0.4170 0.3783 0.3673 -0.1373 0.1245  -0.1037 823 LYS B NZ  
2795 N N   . ASP B 143 ? 0.2315 0.2163 0.1576 -0.1136 0.0460  -0.0446 824 ASP B N   
2796 C CA  . ASP B 143 ? 0.2593 0.2337 0.1731 -0.1214 0.0499  -0.0445 824 ASP B CA  
2797 C C   . ASP B 143 ? 0.2833 0.2440 0.1656 -0.1256 0.0328  -0.0304 824 ASP B C   
2798 O O   . ASP B 143 ? 0.3416 0.2800 0.1879 -0.1424 0.0355  -0.0287 824 ASP B O   
2799 C CB  . ASP B 143 ? 0.3073 0.2677 0.2074 -0.1402 0.0724  -0.0581 824 ASP B CB  
2800 C CG  . ASP B 143 ? 0.2797 0.2552 0.2190 -0.1338 0.0891  -0.0732 824 ASP B CG  
2801 O OD1 . ASP B 143 ? 0.2639 0.2588 0.2389 -0.1159 0.0826  -0.0723 824 ASP B OD1 
2802 O OD2 . ASP B 143 ? 0.3217 0.2889 0.2545 -0.1412 0.1052  -0.0854 824 ASP B OD2 
2803 N N   . THR B 144 ? 0.2819 0.2548 0.1781 -0.1101 0.0150  -0.0203 825 THR B N   
2804 C CA  . THR B 144 ? 0.2591 0.2217 0.1353 -0.1096 -0.0029 -0.0070 825 THR B CA  
2805 C C   . THR B 144 ? 0.2678 0.2224 0.1453 -0.1070 -0.0023 -0.0046 825 THR B C   
2806 O O   . THR B 144 ? 0.3266 0.2946 0.2321 -0.0981 0.0046  -0.0106 825 THR B O   
2807 C CB  . THR B 144 ? 0.2670 0.2470 0.1613 -0.0949 -0.0199 0.0004  825 THR B CB  
2808 O OG1 . THR B 144 ? 0.2751 0.2460 0.1550 -0.0931 -0.0381 0.0125  825 THR B OG1 
2809 C CG2 . THR B 144 ? 0.2005 0.2005 0.1315 -0.0782 -0.0183 -0.0027 825 THR B CG2 
2810 N N   . THR B 145 ? 0.2958 0.2267 0.1411 -0.1153 -0.0108 0.0048  826 THR B N   
2811 C CA  . THR B 145 ? 0.3105 0.2252 0.1474 -0.1179 -0.0073 0.0065  826 THR B CA  
2812 C C   . THR B 145 ? 0.2988 0.2197 0.1547 -0.1002 -0.0226 0.0154  826 THR B C   
2813 O O   . THR B 145 ? 0.3275 0.2484 0.1811 -0.0922 -0.0411 0.0259  826 THR B O   
2814 C CB  . THR B 145 ? 0.3631 0.2423 0.1500 -0.1373 -0.0083 0.0130  826 THR B CB  
2815 O OG1 . THR B 145 ? 0.4727 0.3440 0.2417 -0.1567 0.0118  0.0012  826 THR B OG1 
2816 C CG2 . THR B 145 ? 0.4660 0.3238 0.2408 -0.1394 -0.0074 0.0174  826 THR B CG2 
2817 N N   . VAL B 146 ? 0.2991 0.2257 0.1749 -0.0948 -0.0144 0.0099  827 VAL B N   
2818 C CA  . VAL B 146 ? 0.3319 0.2586 0.2213 -0.0811 -0.0252 0.0163  827 VAL B CA  
2819 C C   . VAL B 146 ? 0.3297 0.2222 0.1846 -0.0877 -0.0341 0.0279  827 VAL B C   
2820 O O   . VAL B 146 ? 0.3427 0.2121 0.1732 -0.1022 -0.0233 0.0259  827 VAL B O   
2821 C CB  . VAL B 146 ? 0.3212 0.2601 0.2356 -0.0773 -0.0136 0.0066  827 VAL B CB  
2822 C CG1 . VAL B 146 ? 0.2584 0.1952 0.1847 -0.0646 -0.0229 0.0118  827 VAL B CG1 
2823 C CG2 . VAL B 146 ? 0.2139 0.1825 0.1586 -0.0709 -0.0074 -0.0031 827 VAL B CG2 
2824 N N   . GLU B 147 ? 0.3368 0.2251 0.1900 -0.0774 -0.0540 0.0399  828 GLU B N   
2825 C CA  . GLU B 147 ? 0.3987 0.2520 0.2193 -0.0814 -0.0666 0.0531  828 GLU B CA  
2826 C C   . GLU B 147 ? 0.3894 0.2320 0.2225 -0.0700 -0.0697 0.0565  828 GLU B C   
2827 O O   . GLU B 147 ? 0.5056 0.3133 0.3093 -0.0777 -0.0702 0.0632  828 GLU B O   
2828 C CB  . GLU B 147 ? 0.4766 0.3294 0.2893 -0.0764 -0.0894 0.0650  828 GLU B CB  
2829 C CG  . GLU B 147 ? 0.5313 0.3932 0.3295 -0.0888 -0.0869 0.0614  828 GLU B CG  
2830 C CD  . GLU B 147 ? 0.6131 0.4850 0.4146 -0.0821 -0.1097 0.0703  828 GLU B CD  
2831 O OE1 . GLU B 147 ? 0.7106 0.5798 0.5238 -0.0680 -0.1290 0.0804  828 GLU B OE1 
2832 O OE2 . GLU B 147 ? 0.6118 0.4949 0.4062 -0.0912 -0.1080 0.0662  828 GLU B OE2 
2833 N N   . ILE B 148 ? 0.4097 0.2791 0.2833 -0.0530 -0.0709 0.0516  829 ILE B N   
2834 C CA  . ILE B 148 ? 0.3342 0.1958 0.2236 -0.0411 -0.0732 0.0530  829 ILE B CA  
2835 C C   . ILE B 148 ? 0.3048 0.1960 0.2284 -0.0350 -0.0602 0.0394  829 ILE B C   
2836 O O   . ILE B 148 ? 0.3378 0.2580 0.2803 -0.0321 -0.0578 0.0333  829 ILE B O   
2837 C CB  . ILE B 148 ? 0.4143 0.2749 0.3175 -0.0243 -0.0946 0.0636  829 ILE B CB  
2838 C CG1 . ILE B 148 ? 0.4611 0.2885 0.3276 -0.0299 -0.1118 0.0793  829 ILE B CG1 
2839 C CG2 . ILE B 148 ? 0.4769 0.3337 0.4040 -0.0105 -0.0938 0.0617  829 ILE B CG2 
2840 C CD1 . ILE B 148 ? 0.4951 0.3373 0.3584 -0.0308 -0.1266 0.0844  829 ILE B CD1 
2841 N N   . GLU B 149 ? 0.2947 0.1763 0.2233 -0.0343 -0.0520 0.0349  830 GLU B N   
2842 C CA  . GLU B 149 ? 0.3140 0.2205 0.2724 -0.0281 -0.0430 0.0234  830 GLU B CA  
2843 C C   . GLU B 149 ? 0.3144 0.2128 0.2876 -0.0157 -0.0472 0.0245  830 GLU B C   
2844 O O   . GLU B 149 ? 0.3779 0.2456 0.3360 -0.0149 -0.0519 0.0320  830 GLU B O   
2845 C CB  . GLU B 149 ? 0.3448 0.2529 0.2994 -0.0412 -0.0267 0.0128  830 GLU B CB  
2846 C CG  . GLU B 149 ? 0.3832 0.2584 0.3157 -0.0508 -0.0205 0.0140  830 GLU B CG  
2847 C CD  . GLU B 149 ? 0.3919 0.2734 0.3259 -0.0647 -0.0039 0.0013  830 GLU B CD  
2848 O OE1 . GLU B 149 ? 0.4349 0.3479 0.3923 -0.0634 0.0006  -0.0083 830 GLU B OE1 
2849 O OE2 . GLU B 149 ? 0.5075 0.3620 0.4199 -0.0772 0.0041  0.0009  830 GLU B OE2 
2850 N N   . GLN B 150 ? 0.2367 0.1604 0.2382 -0.0065 -0.0449 0.0167  831 GLN B N   
2851 C CA  . GLN B 150 ? 0.3799 0.2993 0.3992 0.0048  -0.0457 0.0144  831 GLN B CA  
2852 C C   . GLN B 150 ? 0.2822 0.2166 0.3137 0.0016  -0.0330 0.0014  831 GLN B C   
2853 O O   . GLN B 150 ? 0.1981 0.1590 0.2410 0.0014  -0.0306 -0.0045 831 GLN B O   
2854 C CB  . GLN B 150 ? 0.3036 0.2386 0.3457 0.0189  -0.0565 0.0174  831 GLN B CB  
2855 C CG  . GLN B 150 ? 0.4522 0.3766 0.4842 0.0221  -0.0727 0.0306  831 GLN B CG  
2856 C CD  . GLN B 150 ? 0.5298 0.4205 0.5536 0.0286  -0.0823 0.0402  831 GLN B CD  
2857 O OE1 . GLN B 150 ? 0.5571 0.4178 0.5548 0.0199  -0.0777 0.0434  831 GLN B OE1 
2858 N NE2 . GLN B 150 ? 0.5228 0.4177 0.5699 0.0438  -0.0958 0.0448  831 GLN B NE2 
2859 N N   . LYS B 151 ? 0.2626 0.1781 0.2893 -0.0017 -0.0257 -0.0029 832 LYS B N   
2860 C CA  . LYS B 151 ? 0.2812 0.2084 0.3162 -0.0067 -0.0149 -0.0155 832 LYS B CA  
2861 C C   . LYS B 151 ? 0.2827 0.2157 0.3376 0.0040  -0.0138 -0.0209 832 LYS B C   
2862 O O   . LYS B 151 ? 0.2689 0.1804 0.3273 0.0105  -0.0133 -0.0199 832 LYS B O   
2863 C CB  . LYS B 151 ? 0.2784 0.1828 0.2978 -0.0183 -0.0060 -0.0193 832 LYS B CB  
2864 C CG  . LYS B 151 ? 0.3054 0.2220 0.3319 -0.0254 0.0035  -0.0329 832 LYS B CG  
2865 C CD  . LYS B 151 ? 0.3505 0.2474 0.3618 -0.0396 0.0126  -0.0375 832 LYS B CD  
2866 C CE  . LYS B 151 ? 0.3613 0.2714 0.3796 -0.0482 0.0204  -0.0515 832 LYS B CE  
2867 N NZ  . LYS B 151 ? 0.3884 0.2859 0.3949 -0.0646 0.0297  -0.0578 832 LYS B NZ  
2868 N N   . TYR B 152 ? 0.2291 0.1887 0.2963 0.0052  -0.0123 -0.0272 833 TYR B N   
2869 C CA  . TYR B 152 ? 0.2987 0.2651 0.3832 0.0124  -0.0082 -0.0346 833 TYR B CA  
2870 C C   . TYR B 152 ? 0.3286 0.2942 0.4097 0.0041  0.0027  -0.0470 833 TYR B C   
2871 O O   . TYR B 152 ? 0.2707 0.2305 0.3616 0.0077  0.0098  -0.0547 833 TYR B O   
2872 C CB  . TYR B 152 ? 0.2572 0.2493 0.3528 0.0164  -0.0117 -0.0347 833 TYR B CB  
2873 C CG  . TYR B 152 ? 0.3646 0.3597 0.4677 0.0249  -0.0224 -0.0247 833 TYR B CG  
2874 C CD1 . TYR B 152 ? 0.3245 0.3218 0.4144 0.0207  -0.0295 -0.0162 833 TYR B CD1 
2875 C CD2 . TYR B 152 ? 0.3672 0.3638 0.4921 0.0365  -0.0254 -0.0249 833 TYR B CD2 
2876 C CE1 . TYR B 152 ? 0.4321 0.4315 0.5255 0.0265  -0.0403 -0.0074 833 TYR B CE1 
2877 C CE2 . TYR B 152 ? 0.3814 0.3832 0.5146 0.0438  -0.0377 -0.0159 833 TYR B CE2 
2878 C CZ  . TYR B 152 ? 0.4357 0.4381 0.5507 0.0380  -0.0456 -0.0068 833 TYR B CZ  
2879 O OH  . TYR B 152 ? 0.4479 0.4548 0.5677 0.0432  -0.0587 0.0018  833 TYR B OH  
2880 N N   . ALA B 153 ? 0.2165 0.1887 0.2853 -0.0075 0.0042  -0.0499 834 ALA B N   
2881 C CA  . ALA B 153 ? 0.2643 0.2377 0.3275 -0.0177 0.0117  -0.0613 834 ALA B CA  
2882 C C   . ALA B 153 ? 0.1937 0.1720 0.2478 -0.0287 0.0101  -0.0615 834 ALA B C   
2883 O O   . ALA B 153 ? 0.2101 0.1917 0.2627 -0.0280 0.0052  -0.0538 834 ALA B O   
2884 C CB  . ALA B 153 ? 0.2365 0.2285 0.3026 -0.0186 0.0128  -0.0678 834 ALA B CB  
2885 N N   . ASN B 154 ? 0.2776 0.2569 0.3266 -0.0398 0.0150  -0.0714 835 ASN B N   
2886 C CA  . ASN B 154 ? 0.2074 0.1952 0.2540 -0.0506 0.0140  -0.0739 835 ASN B CA  
2887 C C   . ASN B 154 ? 0.2216 0.2344 0.2753 -0.0479 0.0051  -0.0694 835 ASN B C   
2888 O O   . ASN B 154 ? 0.1935 0.2218 0.2496 -0.0449 -0.0003 -0.0700 835 ASN B O   
2889 C CB  . ASN B 154 ? 0.3417 0.3326 0.3847 -0.0635 0.0182  -0.0864 835 ASN B CB  
2890 C CG  . ASN B 154 ? 0.3794 0.3807 0.4202 -0.0636 0.0162  -0.0920 835 ASN B CG  
2891 O OD1 . ASN B 154 ? 0.5037 0.5131 0.5468 -0.0549 0.0119  -0.0870 835 ASN B OD1 
2892 N ND2 . ASN B 154 ? 0.5244 0.5240 0.5579 -0.0758 0.0201  -0.1032 835 ASN B ND2 
2893 N N   . ASN B 155 ? 0.1891 0.2021 0.2440 -0.0496 0.0047  -0.0649 836 ASN B N   
2894 C CA  . ASN B 155 ? 0.1531 0.1864 0.2164 -0.0474 -0.0013 -0.0616 836 ASN B CA  
2895 C C   . ASN B 155 ? 0.1394 0.1784 0.2040 -0.0360 -0.0075 -0.0538 836 ASN B C   
2896 O O   . ASN B 155 ? 0.1247 0.1807 0.1957 -0.0335 -0.0131 -0.0522 836 ASN B O   
2897 C CB  . ASN B 155 ? 0.1454 0.2017 0.2193 -0.0534 -0.0057 -0.0696 836 ASN B CB  
2898 C CG  . ASN B 155 ? 0.1597 0.2138 0.2347 -0.0663 0.0004  -0.0797 836 ASN B CG  
2899 O OD1 . ASN B 155 ? 0.1661 0.2255 0.2403 -0.0718 -0.0015 -0.0871 836 ASN B OD1 
2900 N ND2 . ASN B 155 ? 0.1684 0.2130 0.2425 -0.0731 0.0084  -0.0807 836 ASN B ND2 
2901 N N   . THR B 156 ? 0.1498 0.1748 0.2103 -0.0291 -0.0064 -0.0494 837 THR B N   
2902 C CA  . THR B 156 ? 0.1450 0.1767 0.2090 -0.0196 -0.0111 -0.0436 837 THR B CA  
2903 C C   . THR B 156 ? 0.1786 0.1964 0.2403 -0.0141 -0.0127 -0.0350 837 THR B C   
2904 O O   . THR B 156 ? 0.1871 0.1886 0.2487 -0.0100 -0.0111 -0.0339 837 THR B O   
2905 C CB  . THR B 156 ? 0.1732 0.2056 0.2390 -0.0168 -0.0087 -0.0486 837 THR B CB  
2906 O OG1 . THR B 156 ? 0.1880 0.2283 0.2495 -0.0246 -0.0083 -0.0563 837 THR B OG1 
2907 C CG2 . THR B 156 ? 0.1862 0.2289 0.2566 -0.0098 -0.0120 -0.0447 837 THR B CG2 
2908 N N   . TYR B 157 ? 0.1443 0.1673 0.2039 -0.0140 -0.0164 -0.0292 838 TYR B N   
2909 C CA  . TYR B 157 ? 0.1448 0.1533 0.1964 -0.0122 -0.0196 -0.0206 838 TYR B CA  
2910 C C   . TYR B 157 ? 0.2166 0.2354 0.2725 -0.0056 -0.0263 -0.0149 838 TYR B C   
2911 O O   . TYR B 157 ? 0.1409 0.1764 0.2013 -0.0059 -0.0267 -0.0166 838 TYR B O   
2912 C CB  . TYR B 157 ? 0.1535 0.1547 0.1933 -0.0224 -0.0159 -0.0200 838 TYR B CB  
2913 C CG  . TYR B 157 ? 0.1904 0.1741 0.2219 -0.0307 -0.0090 -0.0240 838 TYR B CG  
2914 C CD1 . TYR B 157 ? 0.1771 0.1716 0.2161 -0.0377 -0.0030 -0.0342 838 TYR B CD1 
2915 C CD2 . TYR B 157 ? 0.2342 0.1894 0.2495 -0.0322 -0.0093 -0.0174 838 TYR B CD2 
2916 C CE1 . TYR B 157 ? 0.2417 0.2205 0.2731 -0.0473 0.0045  -0.0392 838 TYR B CE1 
2917 C CE2 . TYR B 157 ? 0.3597 0.2951 0.3645 -0.0412 -0.0016 -0.0211 838 TYR B CE2 
2918 C CZ  . TYR B 157 ? 0.2671 0.2151 0.2805 -0.0494 0.0063  -0.0327 838 TYR B CZ  
2919 O OH  . TYR B 157 ? 0.3229 0.2513 0.3258 -0.0602 0.0150  -0.0376 838 TYR B OH  
2920 N N   . GLY B 158 ? 0.1647 0.1726 0.2194 0.0001  -0.0324 -0.0078 839 GLY B N   
2921 C CA  . GLY B 158 ? 0.1410 0.1561 0.1962 0.0032  -0.0399 -0.0016 839 GLY B CA  
2922 C C   . GLY B 158 ? 0.1590 0.1580 0.1938 -0.0039 -0.0430 0.0055  839 GLY B C   
2923 O O   . GLY B 158 ? 0.1949 0.1723 0.2159 -0.0082 -0.0417 0.0081  839 GLY B O   
2924 N N   . VAL B 159 ? 0.1533 0.1606 0.1830 -0.0071 -0.0459 0.0081  840 VAL B N   
2925 C CA  . VAL B 159 ? 0.1894 0.1809 0.1957 -0.0165 -0.0476 0.0137  840 VAL B CA  
2926 C C   . VAL B 159 ? 0.2672 0.2620 0.2709 -0.0137 -0.0595 0.0209  840 VAL B C   
2927 O O   . VAL B 159 ? 0.1882 0.2030 0.2099 -0.0073 -0.0624 0.0187  840 VAL B O   
2928 C CB  . VAL B 159 ? 0.1974 0.1944 0.1977 -0.0270 -0.0365 0.0071  840 VAL B CB  
2929 C CG1 . VAL B 159 ? 0.1661 0.1604 0.1699 -0.0313 -0.0265 -0.0002 840 VAL B CG1 
2930 C CG2 . VAL B 159 ? 0.1446 0.1645 0.1600 -0.0235 -0.0352 0.0027  840 VAL B CG2 
2931 N N   . GLN B 160 ? 0.3105 0.2846 0.2900 -0.0201 -0.0667 0.0292  841 GLN B N   
2932 C CA  . GLN B 160 ? 0.2781 0.2540 0.2516 -0.0196 -0.0805 0.0366  841 GLN B CA  
2933 C C   . GLN B 160 ? 0.2577 0.2238 0.2021 -0.0354 -0.0765 0.0371  841 GLN B C   
2934 O O   . GLN B 160 ? 0.3236 0.2686 0.2439 -0.0467 -0.0686 0.0371  841 GLN B O   
2935 C CB  . GLN B 160 ? 0.2915 0.2493 0.2607 -0.0124 -0.0971 0.0476  841 GLN B CB  
2936 C CG  . GLN B 160 ? 0.3776 0.3465 0.3803 0.0039  -0.0998 0.0451  841 GLN B CG  
2937 C CD  . GLN B 160 ? 0.5481 0.5044 0.5561 0.0146  -0.1187 0.0554  841 GLN B CD  
2938 O OE1 . GLN B 160 ? 0.5938 0.5335 0.5783 0.0099  -0.1332 0.0663  841 GLN B OE1 
2939 N NE2 . GLN B 160 ? 0.5463 0.5097 0.5855 0.0289  -0.1192 0.0519  841 GLN B NE2 
2940 N N   . TYR B 161 ? 0.2252 0.2065 0.1720 -0.0377 -0.0798 0.0360  842 TYR B N   
2941 C CA  . TYR B 161 ? 0.2570 0.2305 0.1776 -0.0533 -0.0746 0.0346  842 TYR B CA  
2942 C C   . TYR B 161 ? 0.2745 0.2603 0.1962 -0.0536 -0.0872 0.0377  842 TYR B C   
2943 O O   . TYR B 161 ? 0.2481 0.2544 0.1975 -0.0418 -0.0949 0.0376  842 TYR B O   
2944 C CB  . TYR B 161 ? 0.2193 0.2027 0.1479 -0.0581 -0.0551 0.0227  842 TYR B CB  
2945 C CG  . TYR B 161 ? 0.2120 0.2212 0.1736 -0.0462 -0.0524 0.0168  842 TYR B CG  
2946 C CD1 . TYR B 161 ? 0.1719 0.1961 0.1413 -0.0453 -0.0551 0.0152  842 TYR B CD1 
2947 C CD2 . TYR B 161 ? 0.1952 0.2114 0.1764 -0.0375 -0.0471 0.0128  842 TYR B CD2 
2948 C CE1 . TYR B 161 ? 0.1453 0.1882 0.1390 -0.0365 -0.0519 0.0104  842 TYR B CE1 
2949 C CE2 . TYR B 161 ? 0.1397 0.1753 0.1443 -0.0288 -0.0452 0.0082  842 TYR B CE2 
2950 C CZ  . TYR B 161 ? 0.1299 0.1777 0.1397 -0.0284 -0.0474 0.0074  842 TYR B CZ  
2951 O OH  . TYR B 161 ? 0.1325 0.1953 0.1603 -0.0217 -0.0446 0.0033  842 TYR B OH  
2952 N N   . GLN B 162 ? 0.2933 0.2664 0.1843 -0.0688 -0.0880 0.0393  843 GLN B N   
2953 C CA  . GLN B 162 ? 0.3609 0.3446 0.2495 -0.0720 -0.1010 0.0420  843 GLN B CA  
2954 C C   . GLN B 162 ? 0.2964 0.3007 0.2007 -0.0740 -0.0884 0.0312  843 GLN B C   
2955 O O   . GLN B 162 ? 0.3732 0.3756 0.2773 -0.0782 -0.0699 0.0226  843 GLN B O   
2956 C CB  . GLN B 162 ? 0.3866 0.3456 0.2328 -0.0888 -0.1068 0.0478  843 GLN B CB  
2957 C CG  . GLN B 162 ? 0.6060 0.5406 0.4355 -0.0864 -0.1201 0.0597  843 GLN B CG  
2958 C CD  . GLN B 162 ? 0.6941 0.6425 0.5528 -0.0686 -0.1387 0.0661  843 GLN B CD  
2959 O OE1 . GLN B 162 ? 0.8617 0.8380 0.7502 -0.0604 -0.1410 0.0612  843 GLN B OE1 
2960 N NE2 . GLN B 162 ? 0.5999 0.5275 0.4497 -0.0633 -0.1504 0.0760  843 GLN B NE2 
2961 N N   . GLY B 163 ? 0.3190 0.3422 0.2386 -0.0706 -0.0984 0.0312  844 GLY B N   
2962 C CA  . GLY B 163 ? 0.3465 0.3836 0.2733 -0.0758 -0.0876 0.0221  844 GLY B CA  
2963 C C   . GLY B 163 ? 0.2719 0.3339 0.2338 -0.0638 -0.0877 0.0179  844 GLY B C   
2964 O O   . GLY B 163 ? 0.2913 0.3623 0.2563 -0.0684 -0.0841 0.0128  844 GLY B O   
2965 N N   . GLY B 164 ? 0.2896 0.3608 0.2759 -0.0499 -0.0902 0.0191  845 GLY B N   
2966 C CA  . GLY B 164 ? 0.2514 0.3430 0.2671 -0.0410 -0.0860 0.0130  845 GLY B CA  
2967 C C   . GLY B 164 ? 0.2819 0.3870 0.3127 -0.0367 -0.0950 0.0116  845 GLY B C   
2968 O O   . GLY B 164 ? 0.2572 0.3590 0.2852 -0.0337 -0.1077 0.0172  845 GLY B O   
2969 N N   . LYS B 165 ? 0.2307 0.3507 0.2773 -0.0375 -0.0884 0.0039  846 LYS B N   
2970 C CA  . LYS B 165 ? 0.1463 0.2842 0.2151 -0.0336 -0.0950 -0.0009 846 LYS B CA  
2971 C C   . LYS B 165 ? 0.1841 0.3344 0.2778 -0.0296 -0.0852 -0.0083 846 LYS B C   
2972 O O   . LYS B 165 ? 0.1674 0.3120 0.2561 -0.0303 -0.0739 -0.0085 846 LYS B O   
2973 C CB  . LYS B 165 ? 0.3094 0.4486 0.3663 -0.0454 -0.0979 -0.0026 846 LYS B CB  
2974 C CG  . LYS B 165 ? 0.3662 0.4913 0.3966 -0.0514 -0.1085 0.0050  846 LYS B CG  
2975 C CD  . LYS B 165 ? 0.5186 0.6489 0.5418 -0.0619 -0.1135 0.0022  846 LYS B CD  
2976 C CE  . LYS B 165 ? 0.6965 0.8085 0.6871 -0.0710 -0.1223 0.0101  846 LYS B CE  
2977 N NZ  . LYS B 165 ? 0.7023 0.7917 0.6621 -0.0819 -0.1097 0.0120  846 LYS B NZ  
2978 N N   . ALA B 166 ? 0.2048 0.3710 0.3256 -0.0266 -0.0899 -0.0134 847 ALA B N   
2979 C CA  . ALA B 166 ? 0.2495 0.4259 0.3895 -0.0285 -0.0782 -0.0143 847 ALA B CA  
2980 C C   . ALA B 166 ? 0.1501 0.3220 0.2715 -0.0377 -0.0627 -0.0205 847 ALA B C   
2981 O O   . ALA B 166 ? 0.2056 0.3732 0.3100 -0.0471 -0.0622 -0.0215 847 ALA B O   
2982 C CB  . ALA B 166 ? 0.2955 0.4937 0.4610 -0.0301 -0.0823 -0.0151 847 ALA B CB  
2983 N N   . GLY B 167 ? 0.0968 0.2685 0.2197 -0.0359 -0.0502 -0.0241 848 GLY B N   
2984 C CA  . GLY B 167 ? 0.0944 0.2598 0.2001 -0.0443 -0.0373 -0.0283 848 GLY B CA  
2985 C C   . GLY B 167 ? 0.1061 0.2569 0.1929 -0.0429 -0.0354 -0.0239 848 GLY B C   
2986 O O   . GLY B 167 ? 0.0894 0.2310 0.1647 -0.0461 -0.0256 -0.0257 848 GLY B O   
2987 N N   . MET B 168 ? 0.0906 0.2345 0.1720 -0.0379 -0.0442 -0.0176 849 MET B N   
2988 C CA  . MET B 168 ? 0.0886 0.2174 0.1541 -0.0363 -0.0409 -0.0140 849 MET B CA  
2989 C C   . MET B 168 ? 0.1039 0.2296 0.1757 -0.0271 -0.0381 -0.0136 849 MET B C   
2990 O O   . MET B 168 ? 0.1131 0.2259 0.1741 -0.0251 -0.0340 -0.0119 849 MET B O   
2991 C CB  . MET B 168 ? 0.1366 0.2573 0.1903 -0.0379 -0.0490 -0.0087 849 MET B CB  
2992 C CG  . MET B 168 ? 0.1858 0.2885 0.2221 -0.0397 -0.0417 -0.0077 849 MET B CG  
2993 S SD  . MET B 168 ? 0.3056 0.3968 0.3206 -0.0493 -0.0464 -0.0046 849 MET B SD  
2994 C CE  . MET B 168 ? 0.2624 0.3371 0.2669 -0.0515 -0.0318 -0.0084 849 MET B CE  
2995 N N   . SER B 169 ? 0.0768 0.2147 0.1673 -0.0217 -0.0399 -0.0162 850 SER B N   
2996 C CA  A SER B 169 ? 0.1250 0.2584 0.2190 -0.0147 -0.0364 -0.0169 850 SER B CA  
2997 C CA  B SER B 169 ? 0.1254 0.2590 0.2196 -0.0147 -0.0364 -0.0170 850 SER B CA  
2998 C C   . SER B 169 ? 0.1236 0.2479 0.2046 -0.0179 -0.0269 -0.0191 850 SER B C   
2999 O O   . SER B 169 ? 0.1037 0.2296 0.1811 -0.0245 -0.0207 -0.0226 850 SER B O   
3000 C CB  A SER B 169 ? 0.1815 0.3281 0.2990 -0.0094 -0.0372 -0.0214 850 SER B CB  
3001 C CB  B SER B 169 ? 0.1805 0.3275 0.2982 -0.0096 -0.0369 -0.0217 850 SER B CB  
3002 O OG  A SER B 169 ? 0.2483 0.4059 0.3748 -0.0148 -0.0299 -0.0284 850 SER B OG  
3003 O OG  B SER B 169 ? 0.1637 0.3113 0.2903 -0.0044 -0.0474 -0.0162 850 SER B OG  
3004 N N   . GLY B 170 ? 0.0886 0.2023 0.1614 -0.0141 -0.0265 -0.0167 851 GLY B N   
3005 C CA  . GLY B 170 ? 0.0760 0.1788 0.1348 -0.0159 -0.0220 -0.0165 851 GLY B CA  
3006 C C   . GLY B 170 ? 0.0785 0.1710 0.1272 -0.0166 -0.0229 -0.0129 851 GLY B C   
3007 O O   . GLY B 170 ? 0.0842 0.1669 0.1243 -0.0155 -0.0222 -0.0115 851 GLY B O   
3008 N N   . GLY B 171 ? 0.0776 0.1712 0.1271 -0.0187 -0.0248 -0.0117 852 GLY B N   
3009 C CA  . GLY B 171 ? 0.0948 0.1785 0.1371 -0.0199 -0.0231 -0.0106 852 GLY B CA  
3010 C C   . GLY B 171 ? 0.0983 0.1790 0.1442 -0.0149 -0.0246 -0.0099 852 GLY B C   
3011 O O   . GLY B 171 ? 0.1180 0.2030 0.1692 -0.0120 -0.0276 -0.0096 852 GLY B O   
3012 N N   . GLY B 172 ? 0.1017 0.1750 0.1469 -0.0139 -0.0218 -0.0107 853 GLY B N   
3013 C CA  . GLY B 172 ? 0.0791 0.1528 0.1325 -0.0095 -0.0228 -0.0119 853 GLY B CA  
3014 C C   . GLY B 172 ? 0.1135 0.1872 0.1681 -0.0134 -0.0198 -0.0140 853 GLY B C   
3015 O O   . GLY B 172 ? 0.0863 0.1553 0.1339 -0.0195 -0.0155 -0.0152 853 GLY B O   
3016 N N   . ILE B 173 ? 0.0813 0.1583 0.1416 -0.0117 -0.0214 -0.0149 854 ILE B N   
3017 C CA  . ILE B 173 ? 0.1487 0.2227 0.2088 -0.0166 -0.0167 -0.0179 854 ILE B CA  
3018 C C   . ILE B 173 ? 0.0842 0.1619 0.1597 -0.0143 -0.0128 -0.0237 854 ILE B C   
3019 O O   . ILE B 173 ? 0.0791 0.1633 0.1650 -0.0083 -0.0180 -0.0240 854 ILE B O   
3020 C CB  . ILE B 173 ? 0.0815 0.1546 0.1384 -0.0174 -0.0198 -0.0160 854 ILE B CB  
3021 C CG1 . ILE B 173 ? 0.1016 0.1736 0.1506 -0.0167 -0.0258 -0.0105 854 ILE B CG1 
3022 C CG2 . ILE B 173 ? 0.0927 0.1581 0.1435 -0.0253 -0.0135 -0.0188 854 ILE B CG2 
3023 C CD1 . ILE B 173 ? 0.1164 0.1843 0.1641 -0.0155 -0.0294 -0.0082 854 ILE B CD1 
3024 N N   . PHE B 174 ? 0.1000 0.1741 0.1778 -0.0196 -0.0039 -0.0292 855 PHE B N   
3025 C CA  . PHE B 174 ? 0.1147 0.1945 0.2139 -0.0165 0.0009  -0.0366 855 PHE B CA  
3026 C C   . PHE B 174 ? 0.1106 0.1913 0.2147 -0.0250 0.0110  -0.0446 855 PHE B C   
3027 O O   . PHE B 174 ? 0.1573 0.2275 0.2420 -0.0355 0.0175  -0.0447 855 PHE B O   
3028 C CB  . PHE B 174 ? 0.1322 0.2061 0.2350 -0.0153 0.0066  -0.0393 855 PHE B CB  
3029 C CG  . PHE B 174 ? 0.0923 0.1622 0.1898 -0.0084 -0.0013 -0.0325 855 PHE B CG  
3030 C CD1 . PHE B 174 ? 0.0927 0.1574 0.1697 -0.0124 -0.0040 -0.0266 855 PHE B CD1 
3031 C CD2 . PHE B 174 ? 0.0943 0.1646 0.2072 0.0013  -0.0061 -0.0323 855 PHE B CD2 
3032 C CE1 . PHE B 174 ? 0.1622 0.2220 0.2330 -0.0087 -0.0085 -0.0218 855 PHE B CE1 
3033 C CE2 . PHE B 174 ? 0.1260 0.1873 0.2283 0.0056  -0.0123 -0.0256 855 PHE B CE2 
3034 C CZ  . PHE B 174 ? 0.1066 0.1627 0.1871 -0.0005 -0.0120 -0.0210 855 PHE B CZ  
3035 N N   . ASN B 175 ? 0.1615 0.2542 0.2907 -0.0214 0.0120  -0.0516 856 ASN B N   
3036 C CA  . ASN B 175 ? 0.1437 0.2391 0.2824 -0.0309 0.0248  -0.0622 856 ASN B CA  
3037 C C   . ASN B 175 ? 0.1775 0.2717 0.3292 -0.0337 0.0382  -0.0721 856 ASN B C   
3038 O O   . ASN B 175 ? 0.1541 0.2432 0.3053 -0.0282 0.0371  -0.0697 856 ASN B O   
3039 C CB  . ASN B 175 ? 0.1456 0.2576 0.3092 -0.0274 0.0207  -0.0676 856 ASN B CB  
3040 C CG  . ASN B 175 ? 0.2172 0.3437 0.4111 -0.0141 0.0116  -0.0695 856 ASN B CG  
3041 O OD1 . ASN B 175 ? 0.1098 0.2335 0.3116 -0.0080 0.0124  -0.0696 856 ASN B OD1 
3042 N ND2 . ASN B 175 ? 0.0982 0.2315 0.2986 -0.0094 0.0020  -0.0682 856 ASN B ND2 
3043 N N   . SER B 176 ? 0.1681 0.2660 0.3321 -0.0434 0.0530  -0.0846 857 SER B N   
3044 C CA  A SER B 176 ? 0.2292 0.3256 0.4071 -0.0484 0.0700  -0.0972 857 SER B CA  
3045 C CA  B SER B 176 ? 0.2287 0.3247 0.4060 -0.0484 0.0698  -0.0970 857 SER B CA  
3046 C C   . SER B 176 ? 0.2204 0.3266 0.4326 -0.0321 0.0643  -0.1004 857 SER B C   
3047 O O   . SER B 176 ? 0.1734 0.2727 0.3937 -0.0326 0.0754  -0.1080 857 SER B O   
3048 C CB  A SER B 176 ? 0.2635 0.3553 0.4398 -0.0600 0.0841  -0.1089 857 SER B CB  
3049 C CB  B SER B 176 ? 0.2635 0.3542 0.4376 -0.0607 0.0846  -0.1086 857 SER B CB  
3050 O OG  A SER B 176 ? 0.3702 0.4495 0.5127 -0.0741 0.0870  -0.1042 857 SER B OG  
3051 O OG  B SER B 176 ? 0.1404 0.2451 0.3377 -0.0540 0.0780  -0.1120 857 SER B OG  
3052 N N   . LYS B 177 ? 0.2071 0.3250 0.4353 -0.0184 0.0466  -0.0940 858 LYS B N   
3053 C CA  . LYS B 177 ? 0.2440 0.3667 0.4987 -0.0032 0.0371  -0.0937 858 LYS B CA  
3054 C C   . LYS B 177 ? 0.1750 0.2922 0.4244 0.0073  0.0263  -0.0832 858 LYS B C   
3055 O O   . LYS B 177 ? 0.1383 0.2546 0.4043 0.0203  0.0164  -0.0803 858 LYS B O   
3056 C CB  . LYS B 177 ? 0.1425 0.2777 0.4117 0.0037  0.0232  -0.0920 858 LYS B CB  
3057 C CG  . LYS B 177 ? 0.3699 0.5119 0.6538 -0.0046 0.0345  -0.1052 858 LYS B CG  
3058 C CD  . LYS B 177 ? 0.2543 0.4103 0.5529 0.0011  0.0210  -0.1042 858 LYS B CD  
3059 C CE  . LYS B 177 ? 0.3875 0.5442 0.6636 -0.0057 0.0169  -0.0986 858 LYS B CE  
3060 N NZ  . LYS B 177 ? 0.3785 0.5296 0.6420 -0.0215 0.0346  -0.1074 858 LYS B NZ  
3061 N N   . GLY B 178 ? 0.1657 0.2704 0.3803 0.0006  0.0262  -0.0747 859 GLY B N   
3062 C CA  . GLY B 178 ? 0.2140 0.3061 0.4108 0.0077  0.0157  -0.0631 859 GLY B CA  
3063 C C   . GLY B 178 ? 0.1260 0.2228 0.3180 0.0159  -0.0032 -0.0524 859 GLY B C   
3064 O O   . GLY B 178 ? 0.1415 0.2278 0.3224 0.0224  -0.0122 -0.0438 859 GLY B O   
3065 N N   . GLU B 179 ? 0.0872 0.1973 0.2848 0.0142  -0.0083 -0.0535 860 GLU B N   
3066 C CA  . GLU B 179 ? 0.0881 0.2016 0.2774 0.0190  -0.0245 -0.0450 860 GLU B CA  
3067 C C   . GLU B 179 ? 0.1138 0.2195 0.2713 0.0113  -0.0239 -0.0384 860 GLU B C   
3068 O O   . GLU B 179 ? 0.1101 0.2135 0.2580 0.0022  -0.0139 -0.0413 860 GLU B O   
3069 C CB  . GLU B 179 ? 0.0844 0.2103 0.2879 0.0192  -0.0287 -0.0490 860 GLU B CB  
3070 C CG  . GLU B 179 ? 0.0957 0.2267 0.3260 0.0264  -0.0299 -0.0542 860 GLU B CG  
3071 C CD  . GLU B 179 ? 0.1494 0.2925 0.3917 0.0233  -0.0308 -0.0599 860 GLU B CD  
3072 O OE1 . GLU B 179 ? 0.1672 0.3132 0.4031 0.0132  -0.0215 -0.0649 860 GLU B OE1 
3073 O OE2 . GLU B 179 ? 0.3249 0.4745 0.5831 0.0307  -0.0412 -0.0592 860 GLU B OE2 
3074 N N   . VAL B 180 ? 0.0844 0.1850 0.2258 0.0147  -0.0345 -0.0299 861 VAL B N   
3075 C CA  . VAL B 180 ? 0.0761 0.1716 0.1937 0.0091  -0.0340 -0.0251 861 VAL B CA  
3076 C C   . VAL B 180 ? 0.0710 0.1749 0.1909 0.0058  -0.0356 -0.0278 861 VAL B C   
3077 O O   . VAL B 180 ? 0.0733 0.1844 0.2011 0.0087  -0.0442 -0.0286 861 VAL B O   
3078 C CB  . VAL B 180 ? 0.0847 0.1716 0.1851 0.0118  -0.0414 -0.0175 861 VAL B CB  
3079 C CG1 . VAL B 180 ? 0.0782 0.1641 0.1619 0.0067  -0.0400 -0.0153 861 VAL B CG1 
3080 C CG2 . VAL B 180 ? 0.0903 0.1654 0.1843 0.0129  -0.0379 -0.0149 861 VAL B CG2 
3081 N N   . ILE B 181 ? 0.0685 0.1693 0.1794 -0.0008 -0.0285 -0.0287 862 ILE B N   
3082 C CA  . ILE B 181 ? 0.0676 0.1712 0.1774 -0.0047 -0.0285 -0.0310 862 ILE B CA  
3083 C C   . ILE B 181 ? 0.1059 0.2022 0.1987 -0.0057 -0.0297 -0.0260 862 ILE B C   
3084 O O   . ILE B 181 ? 0.1041 0.1998 0.1949 -0.0079 -0.0300 -0.0276 862 ILE B O   
3085 C CB  . ILE B 181 ? 0.0708 0.1741 0.1859 -0.0122 -0.0187 -0.0371 862 ILE B CB  
3086 C CG1 . ILE B 181 ? 0.0766 0.1677 0.1756 -0.0173 -0.0120 -0.0342 862 ILE B CG1 
3087 C CG2 . ILE B 181 ? 0.0705 0.1854 0.2104 -0.0113 -0.0158 -0.0454 862 ILE B CG2 
3088 C CD1 . ILE B 181 ? 0.1527 0.2370 0.2466 -0.0277 -0.0019 -0.0389 862 ILE B CD1 
3089 N N   . GLY B 182 ? 0.0675 0.1587 0.1503 -0.0043 -0.0300 -0.0212 863 GLY B N   
3090 C CA  . GLY B 182 ? 0.1052 0.1926 0.1787 -0.0046 -0.0307 -0.0181 863 GLY B CA  
3091 C C   . GLY B 182 ? 0.1680 0.2540 0.2353 -0.0039 -0.0309 -0.0146 863 GLY B C   
3092 O O   . GLY B 182 ? 0.0895 0.1747 0.1563 -0.0034 -0.0304 -0.0141 863 GLY B O   
3093 N N   . LEU B 183 ? 0.1216 0.2073 0.1862 -0.0038 -0.0315 -0.0129 864 LEU B N   
3094 C CA  . LEU B 183 ? 0.1072 0.1954 0.1695 -0.0042 -0.0316 -0.0113 864 LEU B CA  
3095 C C   . LEU B 183 ? 0.1420 0.2305 0.2054 -0.0050 -0.0341 -0.0090 864 LEU B C   
3096 O O   . LEU B 183 ? 0.1289 0.2150 0.1955 -0.0027 -0.0363 -0.0083 864 LEU B O   
3097 C CB  . LEU B 183 ? 0.1829 0.2744 0.2460 -0.0030 -0.0308 -0.0134 864 LEU B CB  
3098 C CG  . LEU B 183 ? 0.2591 0.3477 0.3152 -0.0034 -0.0307 -0.0146 864 LEU B CG  
3099 C CD1 . LEU B 183 ? 0.3516 0.4413 0.4073 -0.0041 -0.0284 -0.0185 864 LEU B CD1 
3100 C CD2 . LEU B 183 ? 0.2462 0.3315 0.2942 -0.0060 -0.0292 -0.0130 864 LEU B CD2 
3101 N N   . HIS B 184 ? 0.1683 0.2586 0.2284 -0.0083 -0.0348 -0.0075 865 HIS B N   
3102 C CA  . HIS B 184 ? 0.1630 0.2559 0.2249 -0.0089 -0.0406 -0.0048 865 HIS B CA  
3103 C C   . HIS B 184 ? 0.1243 0.2270 0.2011 -0.0038 -0.0425 -0.0068 865 HIS B C   
3104 O O   . HIS B 184 ? 0.1191 0.2279 0.2002 -0.0041 -0.0374 -0.0110 865 HIS B O   
3105 C CB  . HIS B 184 ? 0.1079 0.2025 0.1629 -0.0154 -0.0412 -0.0042 865 HIS B CB  
3106 C CG  . HIS B 184 ? 0.1335 0.2303 0.1878 -0.0173 -0.0504 -0.0005 865 HIS B CG  
3107 N ND1 . HIS B 184 ? 0.1421 0.2271 0.1820 -0.0213 -0.0549 0.0040  865 HIS B ND1 
3108 C CD2 . HIS B 184 ? 0.1014 0.2109 0.1680 -0.0161 -0.0571 -0.0006 865 HIS B CD2 
3109 C CE1 . HIS B 184 ? 0.1853 0.2736 0.2257 -0.0220 -0.0662 0.0081  865 HIS B CE1 
3110 N NE2 . HIS B 184 ? 0.1078 0.2131 0.1676 -0.0181 -0.0682 0.0050  865 HIS B NE2 
3111 N N   . GLN B 185 ? 0.1640 0.2664 0.2483 0.0004  -0.0494 -0.0042 866 GLN B N   
3112 C CA  . GLN B 185 ? 0.2155 0.3286 0.3205 0.0065  -0.0511 -0.0074 866 GLN B CA  
3113 C C   . GLN B 185 ? 0.2699 0.3860 0.3833 0.0096  -0.0635 -0.0025 866 GLN B C   
3114 O O   . GLN B 185 ? 0.4733 0.5766 0.5814 0.0129  -0.0706 0.0034  866 GLN B O   
3115 C CB  . GLN B 185 ? 0.3156 0.4226 0.4262 0.0118  -0.0468 -0.0104 866 GLN B CB  
3116 C CG  . GLN B 185 ? 0.3270 0.4348 0.4325 0.0088  -0.0368 -0.0164 866 GLN B CG  
3117 C CD  . GLN B 185 ? 0.3984 0.4989 0.5054 0.0115  -0.0327 -0.0199 866 GLN B CD  
3118 O OE1 . GLN B 185 ? 0.4662 0.5567 0.5720 0.0143  -0.0360 -0.0169 866 GLN B OE1 
3119 N NE2 . GLN B 185 ? 0.3668 0.4698 0.4729 0.0090  -0.0248 -0.0267 866 GLN B NE2 
3120 N N   . ASN B 186 ? 0.3951 0.5247 0.5166 0.0074  -0.0648 -0.0040 867 ASN B N   
3121 C CA  . ASN B 186 ? 0.5689 0.7026 0.6975 0.0110  -0.0755 0.0003  867 ASN B CA  
3122 C C   . ASN B 186 ? 0.6913 0.8266 0.8422 0.0219  -0.0762 -0.0015 867 ASN B C   
3123 O O   . ASN B 186 ? 0.7778 0.9237 0.9466 0.0237  -0.0666 -0.0095 867 ASN B O   
3124 C CB  . ASN B 186 ? 0.5350 0.6855 0.6693 0.0049  -0.0756 -0.0023 867 ASN B CB  
3125 C CG  . ASN B 186 ? 0.5708 0.7174 0.6832 -0.0050 -0.0778 -0.0019 867 ASN B CG  
3126 O OD1 . ASN B 186 ? 0.5067 0.6365 0.5998 -0.0072 -0.0848 0.0039  867 ASN B OD1 
3127 N ND2 . ASN B 186 ? 0.4464 0.5941 0.5632 -0.0132 -0.0730 -0.0055 867 ASN B ND2 
3128 N N   . GLY B 187 ? 0.5448 0.6668 0.6936 0.0283  -0.0871 0.0055  868 GLY B N   
3129 C CA  . GLY B 187 ? 0.6525 0.7734 0.8237 0.0396  -0.0890 0.0041  868 GLY B CA  
3130 C C   . GLY B 187 ? 0.6914 0.8276 0.8829 0.0442  -0.0960 0.0036  868 GLY B C   
3131 O O   . GLY B 187 ? 0.5956 0.7454 0.7845 0.0379  -0.0989 0.0038  868 GLY B O   
3132 N N   . ALA B 188 ? 0.8412 0.9754 1.0551 0.0554  -0.0986 0.0023  869 ALA B N   
3133 C CA  . ALA B 188 ? 0.6742 0.8229 0.9120 0.0618  -0.1071 0.0019  869 ALA B CA  
3134 C C   . ALA B 188 ? 0.6518 0.7929 0.8729 0.0613  -0.1262 0.0140  869 ALA B C   
3135 O O   . ALA B 188 ? 0.6739 0.7911 0.8679 0.0594  -0.1335 0.0233  869 ALA B O   
3136 C CB  . ALA B 188 ? 0.5718 0.7167 0.8376 0.0746  -0.1056 -0.0024 869 ALA B CB  
3137 N N   . GLU B 189 ? 0.6565 0.8176 0.8930 0.0617  -0.1342 0.0133  870 GLU B N   
3138 C CA  . GLU B 189 ? 0.7017 0.8592 0.9220 0.0593  -0.1528 0.0232  870 GLU B CA  
3139 C C   . GLU B 189 ? 0.7702 0.9177 0.9525 0.0452  -0.1518 0.0269  870 GLU B C   
3140 O O   . GLU B 189 ? 0.8387 0.9676 0.9941 0.0415  -0.1647 0.0367  870 GLU B O   
3141 C CB  . GLU B 189 ? 0.6344 0.7684 0.8509 0.0696  -0.1686 0.0341  870 GLU B CB  
3142 C CG  . GLU B 189 ? 0.5854 0.7309 0.8417 0.0843  -0.1744 0.0312  870 GLU B CG  
3143 C CD  . GLU B 189 ? 0.7893 0.9635 1.0670 0.0844  -0.1848 0.0292  870 GLU B CD  
3144 O OE1 . GLU B 189 ? 0.7429 0.9209 0.9983 0.0743  -0.1933 0.0338  870 GLU B OE1 
3145 O OE2 . GLU B 189 ? 0.8091 1.0023 1.1269 0.0941  -0.1840 0.0220  870 GLU B OE2 
3146 N N   . ASN B 190 ? 0.8520 1.0095 1.0309 0.0367  -0.1361 0.0189  871 ASN B N   
3147 C CA  . ASN B 190 ? 0.8945 1.0441 1.0418 0.0236  -0.1328 0.0197  871 ASN B CA  
3148 C C   . ASN B 190 ? 0.9311 1.0497 1.0486 0.0215  -0.1361 0.0284  871 ASN B C   
3149 O O   . ASN B 190 ? 0.8900 0.9943 0.9780 0.0119  -0.1422 0.0340  871 ASN B O   
3150 C CB  . ASN B 190 ? 0.9157 1.0762 1.0548 0.0156  -0.1425 0.0201  871 ASN B CB  
3151 C CG  . ASN B 190 ? 1.0027 1.1947 1.1668 0.0125  -0.1358 0.0103  871 ASN B CG  
3152 O OD1 . ASN B 190 ? 1.0637 1.2624 1.2232 0.0034  -0.1229 0.0034  871 ASN B OD1 
3153 N ND2 . ASN B 190 ? 0.7527 0.9632 0.9441 0.0191  -0.1449 0.0102  871 ASN B ND2 
3154 N N   . ARG B 191 ? 0.6249 0.7320 0.7491 0.0289  -0.1312 0.0289  872 ARG B N   
3155 C CA  . ARG B 191 ? 0.6399 0.7186 0.7379 0.0259  -0.1331 0.0364  872 ARG B CA  
3156 C C   . ARG B 191 ? 0.4828 0.5615 0.5669 0.0160  -0.1202 0.0316  872 ARG B C   
3157 O O   . ARG B 191 ? 0.4839 0.5728 0.5838 0.0188  -0.1081 0.0238  872 ARG B O   
3158 C CB  . ARG B 191 ? 0.6739 0.7408 0.7867 0.0377  -0.1333 0.0377  872 ARG B CB  
3159 C CG  . ARG B 191 ? 0.7164 0.7500 0.8015 0.0352  -0.1392 0.0476  872 ARG B CG  
3160 C CD  . ARG B 191 ? 0.8227 0.8435 0.9249 0.0480  -0.1399 0.0483  872 ARG B CD  
3161 N NE  . ARG B 191 ? 0.9140 0.9394 1.0370 0.0591  -0.1499 0.0504  872 ARG B NE  
3162 C CZ  . ARG B 191 ? 0.8686 0.9172 1.0286 0.0687  -0.1444 0.0410  872 ARG B CZ  
3163 N NH1 . ARG B 191 ? 0.8088 0.8761 0.9860 0.0675  -0.1282 0.0289  872 ARG B NH1 
3164 N NH2 . ARG B 191 ? 0.7392 0.7914 0.9183 0.0786  -0.1553 0.0437  872 ARG B NH2 
3165 N N   . SER B 192 ? 0.3190 0.3855 0.3728 0.0035  -0.1223 0.0359  873 SER B N   
3166 C CA  . SER B 192 ? 0.3078 0.3748 0.3493 -0.0065 -0.1106 0.0314  873 SER B CA  
3167 C C   . SER B 192 ? 0.2037 0.2549 0.2376 -0.0057 -0.1010 0.0310  873 SER B C   
3168 O O   . SER B 192 ? 0.2527 0.2814 0.2686 -0.0070 -0.1056 0.0378  873 SER B O   
3169 C CB  . SER B 192 ? 0.2021 0.2590 0.2125 -0.0214 -0.1125 0.0343  873 SER B CB  
3170 O OG  . SER B 192 ? 0.2703 0.3260 0.2698 -0.0304 -0.0972 0.0281  873 SER B OG  
3171 N N   . GLY B 193 ? 0.1684 0.2298 0.2137 -0.0044 -0.0865 0.0224  874 GLY B N   
3172 C CA  . GLY B 193 ? 0.2371 0.2866 0.2751 -0.0053 -0.0754 0.0198  874 GLY B CA  
3173 C C   . GLY B 193 ? 0.1903 0.2539 0.2420 -0.0035 -0.0636 0.0111  874 GLY B C   
3174 O O   . GLY B 193 ? 0.2111 0.2895 0.2717 -0.0036 -0.0619 0.0076  874 GLY B O   
3175 N N   . GLY B 194 ? 0.1761 0.2333 0.2274 -0.0027 -0.0560 0.0079  875 GLY B N   
3176 C CA  . GLY B 194 ? 0.1734 0.2409 0.2333 -0.0016 -0.0474 0.0010  875 GLY B CA  
3177 C C   . GLY B 194 ? 0.1392 0.2017 0.2028 0.0007  -0.0429 -0.0024 875 GLY B C   
3178 O O   . GLY B 194 ? 0.1422 0.1916 0.2021 0.0016  -0.0447 0.0000  875 GLY B O   
3179 N N   . LEU B 195 ? 0.0861 0.1571 0.1551 0.0011  -0.0377 -0.0079 876 LEU B N   
3180 C CA  . LEU B 195 ? 0.1029 0.1713 0.1737 0.0011  -0.0337 -0.0126 876 LEU B CA  
3181 C C   . LEU B 195 ? 0.1238 0.1937 0.1908 -0.0038 -0.0308 -0.0151 876 LEU B C   
3182 O O   . LEU B 195 ? 0.1466 0.2232 0.2138 -0.0045 -0.0308 -0.0152 876 LEU B O   
3183 C CB  . LEU B 195 ? 0.0816 0.1578 0.1595 0.0039  -0.0313 -0.0174 876 LEU B CB  
3184 C CG  . LEU B 195 ? 0.2452 0.3213 0.3203 0.0011  -0.0280 -0.0230 876 LEU B CG  
3185 C CD1 . LEU B 195 ? 0.3470 0.4130 0.4230 0.0007  -0.0256 -0.0257 876 LEU B CD1 
3186 C CD2 . LEU B 195 ? 0.2994 0.3810 0.3736 0.0006  -0.0254 -0.0270 876 LEU B CD2 
3187 N N   . ILE B 196 ? 0.1167 0.1804 0.1823 -0.0073 -0.0281 -0.0179 877 ILE B N   
3188 C CA  . ILE B 196 ? 0.0874 0.1571 0.1567 -0.0115 -0.0255 -0.0226 877 ILE B CA  
3189 C C   . ILE B 196 ? 0.1130 0.1893 0.1870 -0.0106 -0.0269 -0.0274 877 ILE B C   
3190 O O   . ILE B 196 ? 0.1564 0.2268 0.2287 -0.0117 -0.0252 -0.0300 877 ILE B O   
3191 C CB  . ILE B 196 ? 0.1143 0.1745 0.1793 -0.0188 -0.0203 -0.0246 877 ILE B CB  
3192 C CG1 . ILE B 196 ? 0.1259 0.1757 0.1791 -0.0220 -0.0194 -0.0193 877 ILE B CG1 
3193 C CG2 . ILE B 196 ? 0.0930 0.1641 0.1691 -0.0231 -0.0170 -0.0319 877 ILE B CG2 
3194 C CD1 . ILE B 196 ? 0.1644 0.2229 0.2201 -0.0216 -0.0193 -0.0189 877 ILE B CD1 
3195 N N   . LEU B 197 ? 0.0776 0.1640 0.1555 -0.0091 -0.0306 -0.0284 878 LEU B N   
3196 C CA  . LEU B 197 ? 0.0806 0.1712 0.1569 -0.0095 -0.0343 -0.0314 878 LEU B CA  
3197 C C   . LEU B 197 ? 0.1266 0.2194 0.2073 -0.0147 -0.0339 -0.0378 878 LEU B C   
3198 O O   . LEU B 197 ? 0.1479 0.2469 0.2390 -0.0173 -0.0335 -0.0408 878 LEU B O   
3199 C CB  . LEU B 197 ? 0.1139 0.2108 0.1906 -0.0068 -0.0407 -0.0291 878 LEU B CB  
3200 C CG  . LEU B 197 ? 0.1117 0.2045 0.1808 -0.0039 -0.0398 -0.0241 878 LEU B CG  
3201 C CD1 . LEU B 197 ? 0.0803 0.1746 0.1501 -0.0011 -0.0449 -0.0209 878 LEU B CD1 
3202 C CD2 . LEU B 197 ? 0.1084 0.1972 0.1669 -0.0054 -0.0381 -0.0251 878 LEU B CD2 
3203 N N   . SER B 198 ? 0.0945 0.1826 0.1685 -0.0175 -0.0326 -0.0414 879 SER B N   
3204 C CA  . SER B 198 ? 0.1445 0.2336 0.2203 -0.0244 -0.0317 -0.0485 879 SER B CA  
3205 C C   . SER B 198 ? 0.1357 0.2383 0.2153 -0.0267 -0.0414 -0.0513 879 SER B C   
3206 O O   . SER B 198 ? 0.1266 0.2330 0.2026 -0.0225 -0.0488 -0.0467 879 SER B O   
3207 C CB  . SER B 198 ? 0.1275 0.2050 0.1935 -0.0269 -0.0262 -0.0523 879 SER B CB  
3208 O OG  . SER B 198 ? 0.1647 0.2440 0.2208 -0.0274 -0.0294 -0.0531 879 SER B OG  
3209 N N   . PRO B 199 ? 0.1103 0.2198 0.1970 -0.0337 -0.0426 -0.0586 880 PRO B N   
3210 C CA  . PRO B 199 ? 0.1269 0.2473 0.2152 -0.0355 -0.0543 -0.0597 880 PRO B CA  
3211 C C   . PRO B 199 ? 0.2003 0.3159 0.2684 -0.0371 -0.0611 -0.0584 880 PRO B C   
3212 O O   . PRO B 199 ? 0.2056 0.3227 0.2685 -0.0340 -0.0722 -0.0520 880 PRO B O   
3213 C CB  . PRO B 199 ? 0.1709 0.2942 0.2649 -0.0445 -0.0509 -0.0679 880 PRO B CB  
3214 C CG  . PRO B 199 ? 0.1195 0.2392 0.2228 -0.0466 -0.0389 -0.0713 880 PRO B CG  
3215 C CD  . PRO B 199 ? 0.1149 0.2194 0.2060 -0.0407 -0.0335 -0.0647 880 PRO B CD  
3216 N N   . THR B 200 ? 0.1382 0.2406 0.1909 -0.0416 -0.0519 -0.0618 881 THR B N   
3217 C CA  . THR B 200 ? 0.2029 0.2967 0.2327 -0.0454 -0.0536 -0.0616 881 THR B CA  
3218 C C   . THR B 200 ? 0.1734 0.2635 0.1967 -0.0383 -0.0551 -0.0531 881 THR B C   
3219 O O   . THR B 200 ? 0.1657 0.2523 0.1712 -0.0410 -0.0632 -0.0499 881 THR B O   
3220 C CB  . THR B 200 ? 0.2148 0.2949 0.2350 -0.0508 -0.0396 -0.0689 881 THR B CB  
3221 O OG1 . THR B 200 ? 0.2394 0.3201 0.2607 -0.0599 -0.0384 -0.0776 881 THR B OG1 
3222 C CG2 . THR B 200 ? 0.2589 0.3290 0.2555 -0.0561 -0.0369 -0.0707 881 THR B CG2 
3223 N N   . GLN B 201 ? 0.1505 0.2394 0.1851 -0.0307 -0.0478 -0.0493 882 GLN B N   
3224 C CA  . GLN B 201 ? 0.1429 0.2286 0.1722 -0.0255 -0.0478 -0.0425 882 GLN B CA  
3225 C C   . GLN B 201 ? 0.2002 0.2918 0.2324 -0.0214 -0.0601 -0.0360 882 GLN B C   
3226 O O   . GLN B 201 ? 0.1530 0.2380 0.1702 -0.0213 -0.0645 -0.0310 882 GLN B O   
3227 C CB  . GLN B 201 ? 0.1574 0.2418 0.1989 -0.0195 -0.0390 -0.0405 882 GLN B CB  
3228 C CG  . GLN B 201 ? 0.1188 0.1956 0.1585 -0.0206 -0.0283 -0.0454 882 GLN B CG  
3229 C CD  . GLN B 201 ? 0.1378 0.2133 0.1914 -0.0142 -0.0238 -0.0427 882 GLN B CD  
3230 O OE1 . GLN B 201 ? 0.1316 0.2091 0.1925 -0.0120 -0.0266 -0.0391 882 GLN B OE1 
3231 N NE2 . GLN B 201 ? 0.1707 0.2425 0.2282 -0.0117 -0.0169 -0.0450 882 GLN B NE2 
3232 N N   . LEU B 202 ? 0.1815 0.2841 0.2334 -0.0184 -0.0649 -0.0368 883 LEU B N   
3233 C CA  . LEU B 202 ? 0.1341 0.2425 0.1941 -0.0132 -0.0766 -0.0319 883 LEU B CA  
3234 C C   . LEU B 202 ? 0.1432 0.2482 0.1864 -0.0170 -0.0899 -0.0292 883 LEU B C   
3235 O O   . LEU B 202 ? 0.1544 0.2536 0.1888 -0.0131 -0.0983 -0.0217 883 LEU B O   
3236 C CB  . LEU B 202 ? 0.1133 0.2307 0.1965 -0.0115 -0.0736 -0.0335 883 LEU B CB  
3237 C CG  . LEU B 202 ? 0.1121 0.2297 0.2072 -0.0091 -0.0620 -0.0350 883 LEU B CG  
3238 C CD1 . LEU B 202 ? 0.1677 0.2935 0.2815 -0.0111 -0.0576 -0.0402 883 LEU B CD1 
3239 C CD2 . LEU B 202 ? 0.1206 0.2342 0.2158 -0.0025 -0.0618 -0.0290 883 LEU B CD2 
3240 N N   . ASP B 203 ? 0.1544 0.2607 0.1901 -0.0254 -0.0917 -0.0350 884 ASP B N   
3241 C CA  . ASP B 203 ? 0.2093 0.3119 0.2250 -0.0315 -0.1051 -0.0321 884 ASP B CA  
3242 C C   . ASP B 203 ? 0.1999 0.2849 0.1829 -0.0343 -0.1061 -0.0294 884 ASP B C   
3243 O O   . ASP B 203 ? 0.2222 0.2990 0.1892 -0.0325 -0.1160 -0.0224 884 ASP B O   
3244 C CB  . ASP B 203 ? 0.2213 0.3232 0.2335 -0.0408 -0.1055 -0.0409 884 ASP B CB  
3245 C CG  . ASP B 203 ? 0.2788 0.3967 0.3171 -0.0407 -0.1088 -0.0411 884 ASP B CG  
3246 O OD1 . ASP B 203 ? 0.2640 0.3938 0.3223 -0.0322 -0.1112 -0.0356 884 ASP B OD1 
3247 O OD2 . ASP B 203 ? 0.3711 0.4901 0.4106 -0.0481 -0.1068 -0.0494 884 ASP B OD2 
3248 N N   . TRP B 204 ? 0.1946 0.2712 0.1679 -0.0386 -0.0894 -0.0329 885 TRP B N   
3249 C CA  . TRP B 204 ? 0.2139 0.2729 0.1572 -0.0443 -0.0838 -0.0303 885 TRP B CA  
3250 C C   . TRP B 204 ? 0.2140 0.2664 0.1550 -0.0371 -0.0888 -0.0202 885 TRP B C   
3251 O O   . TRP B 204 ? 0.2460 0.2820 0.1576 -0.0422 -0.0952 -0.0143 885 TRP B O   
3252 C CB  . TRP B 204 ? 0.2044 0.2603 0.1497 -0.0472 -0.0631 -0.0380 885 TRP B CB  
3253 C CG  . TRP B 204 ? 0.2217 0.2631 0.1428 -0.0536 -0.0540 -0.0376 885 TRP B CG  
3254 C CD1 . TRP B 204 ? 0.2618 0.2885 0.1496 -0.0673 -0.0505 -0.0418 885 TRP B CD1 
3255 C CD2 . TRP B 204 ? 0.2528 0.2927 0.1798 -0.0488 -0.0458 -0.0343 885 TRP B CD2 
3256 N NE1 . TRP B 204 ? 0.2692 0.2854 0.1428 -0.0716 -0.0392 -0.0417 885 TRP B NE1 
3257 C CE2 . TRP B 204 ? 0.2487 0.2739 0.1474 -0.0601 -0.0368 -0.0371 885 TRP B CE2 
3258 C CE3 . TRP B 204 ? 0.2029 0.2521 0.1547 -0.0379 -0.0446 -0.0300 885 TRP B CE3 
3259 C CZ2 . TRP B 204 ? 0.2612 0.2828 0.1591 -0.0604 -0.0267 -0.0363 885 TRP B CZ2 
3260 C CZ3 . TRP B 204 ? 0.2310 0.2763 0.1806 -0.0380 -0.0362 -0.0286 885 TRP B CZ3 
3261 C CH2 . TRP B 204 ? 0.2402 0.2729 0.1646 -0.0490 -0.0273 -0.0319 885 TRP B CH2 
3262 N N   . ILE B 205 ? 0.1871 0.2491 0.1553 -0.0266 -0.0849 -0.0182 886 ILE B N   
3263 C CA  . ILE B 205 ? 0.1882 0.2429 0.1554 -0.0202 -0.0882 -0.0098 886 ILE B CA  
3264 C C   . ILE B 205 ? 0.2552 0.3038 0.2145 -0.0170 -0.1083 -0.0019 886 ILE B C   
3265 O O   . ILE B 205 ? 0.2348 0.2647 0.1697 -0.0184 -0.1136 0.0059  886 ILE B O   
3266 C CB  . ILE B 205 ? 0.1587 0.2251 0.1562 -0.0110 -0.0815 -0.0105 886 ILE B CB  
3267 C CG1 . ILE B 205 ? 0.1423 0.2116 0.1448 -0.0134 -0.0651 -0.0159 886 ILE B CG1 
3268 C CG2 . ILE B 205 ? 0.1707 0.2286 0.1678 -0.0048 -0.0853 -0.0029 886 ILE B CG2 
3269 C CD1 . ILE B 205 ? 0.1184 0.1981 0.1460 -0.0071 -0.0601 -0.0170 886 ILE B CD1 
3270 N N   . ARG B 206 ? 0.2091 0.2733 0.1904 -0.0122 -0.1164 -0.0041 887 ARG B N   
3271 C CA  . ARG B 206 ? 0.2270 0.2890 0.2083 -0.0066 -0.1301 0.0026  887 ARG B CA  
3272 C C   . ARG B 206 ? 0.3020 0.3461 0.2450 -0.0156 -0.1382 0.0065  887 ARG B C   
3273 O O   . ARG B 206 ? 0.3963 0.4268 0.3265 -0.0122 -0.1497 0.0157  887 ARG B O   
3274 C CB  . ARG B 206 ? 0.2710 0.3563 0.2847 -0.0024 -0.1329 -0.0022 887 ARG B CB  
3275 C CG  . ARG B 206 ? 0.2580 0.3543 0.3061 0.0070  -0.1262 -0.0033 887 ARG B CG  
3276 C CD  . ARG B 206 ? 0.2213 0.3377 0.2988 0.0091  -0.1285 -0.0080 887 ARG B CD  
3277 N NE  . ARG B 206 ? 0.3420 0.4690 0.4248 0.0002  -0.1195 -0.0162 887 ARG B NE  
3278 C CZ  . ARG B 206 ? 0.2121 0.3443 0.3127 0.0000  -0.1062 -0.0218 887 ARG B CZ  
3279 N NH1 . ARG B 206 ? 0.1855 0.3169 0.3013 0.0072  -0.0995 -0.0213 887 ARG B NH1 
3280 N NH2 . ARG B 206 ? 0.2724 0.4087 0.3739 -0.0083 -0.0995 -0.0286 887 ARG B NH2 
3281 N N   . SER B 207 ? 0.3628 0.4039 0.2859 -0.0278 -0.1314 -0.0006 888 SER B N   
3282 C CA  . SER B 207 ? 0.4371 0.4583 0.3202 -0.0390 -0.1351 0.0018  888 SER B CA  
3283 C C   . SER B 207 ? 0.3989 0.3938 0.2497 -0.0440 -0.1308 0.0093  888 SER B C   
3284 O O   . SER B 207 ? 0.4846 0.4592 0.3048 -0.0496 -0.1382 0.0162  888 SER B O   
3285 C CB  . SER B 207 ? 0.3387 0.3612 0.2095 -0.0520 -0.1245 -0.0095 888 SER B CB  
3286 O OG  . SER B 207 ? 0.4023 0.4206 0.2679 -0.0579 -0.1070 -0.0149 888 SER B OG  
3287 N N   . ILE B 208 ? 0.4272 0.4215 0.2829 -0.0436 -0.1186 0.0076  889 ILE B N   
3288 C CA  . ILE B 208 ? 0.4229 0.3933 0.2493 -0.0492 -0.1129 0.0136  889 ILE B CA  
3289 C C   . ILE B 208 ? 0.4742 0.4339 0.3044 -0.0379 -0.1266 0.0259  889 ILE B C   
3290 O O   . ILE B 208 ? 0.5269 0.4603 0.3252 -0.0431 -0.1297 0.0339  889 ILE B O   
3291 C CB  . ILE B 208 ? 0.3734 0.3510 0.2118 -0.0508 -0.0926 0.0065  889 ILE B CB  
3292 C CG1 . ILE B 208 ? 0.3799 0.3699 0.2250 -0.0583 -0.0770 -0.0067 889 ILE B CG1 
3293 C CG2 . ILE B 208 ? 0.4096 0.3642 0.2185 -0.0592 -0.0826 0.0099  889 ILE B CG2 
3294 C CD1 . ILE B 208 ? 0.4419 0.4139 0.2460 -0.0762 -0.0706 -0.0117 889 ILE B CD1 
3295 N N   . ILE B 209 ? 0.4020 0.3805 0.2719 -0.0229 -0.1334 0.0267  890 ILE B N   
3296 C CA  . ILE B 209 ? 0.4099 0.3794 0.2897 -0.0109 -0.1447 0.0364  890 ILE B CA  
3297 C C   . ILE B 209 ? 0.5807 0.5379 0.4442 -0.0108 -0.1606 0.0438  890 ILE B C   
3298 O O   . ILE B 209 ? 0.6195 0.5519 0.4637 -0.0089 -0.1681 0.0538  890 ILE B O   
3299 C CB  . ILE B 209 ? 0.3632 0.3583 0.2924 0.0034  -0.1452 0.0323  890 ILE B CB  
3300 C CG1 . ILE B 209 ? 0.3969 0.4003 0.3393 0.0030  -0.1311 0.0266  890 ILE B CG1 
3301 C CG2 . ILE B 209 ? 0.3957 0.3827 0.3391 0.0161  -0.1561 0.0402  890 ILE B CG2 
3302 C CD1 . ILE B 209 ? 0.2959 0.3224 0.2834 0.0139  -0.1276 0.0210  890 ILE B CD1 
3303 N N   . LYS B 210 ? 0.4567 0.4298 0.3267 -0.0131 -0.1665 0.0390  891 LYS B N   
3304 C CA  . LYS B 210 ? 0.5152 0.4793 0.3711 -0.0132 -0.1838 0.0458  891 LYS B CA  
3305 C C   . LYS B 210 ? 0.7426 0.6722 0.5456 -0.0272 -0.1841 0.0524  891 LYS B C   
3306 O O   . LYS B 210 ? 0.7143 0.6246 0.4994 -0.0259 -0.1991 0.0624  891 LYS B O   
3307 C CB  . LYS B 210 ? 0.5138 0.5027 0.3849 -0.0155 -0.1886 0.0378  891 LYS B CB  
3308 C CG  . LYS B 210 ? 0.6547 0.6437 0.5250 -0.0119 -0.2097 0.0441  891 LYS B CG  
3309 C CD  . LYS B 210 ? 0.7578 0.7729 0.6427 -0.0157 -0.2135 0.0347  891 LYS B CD  
3310 C CE  . LYS B 210 ? 0.7640 0.7823 0.6507 -0.0118 -0.2363 0.0409  891 LYS B CE  
3311 N NZ  . LYS B 210 ? 0.5482 0.5915 0.4456 -0.0178 -0.2404 0.0311  891 LYS B NZ  
3312 N N   . GLY B 211 ? 0.6930 0.6137 0.4707 -0.0414 -0.1667 0.0464  892 GLY B N   
3313 C CA  . GLY B 211 ? 0.7253 0.6130 0.4533 -0.0575 -0.1617 0.0503  892 GLY B CA  
3314 C C   . GLY B 211 ? 0.8513 0.7134 0.5626 -0.0572 -0.1571 0.0581  892 GLY B C   
3315 O O   . GLY B 211 ? 0.8494 0.6809 0.5266 -0.0637 -0.1633 0.0668  892 GLY B O   
# 
