data_9EBZ
# 
_entry.id   9EBZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9EBZ         pdb_00009ebz 10.2210/pdb9ebz/pdb 
WWPDB D_1000290138 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2025-01-29 
3 'Structure model' 1 2 2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 3 'Structure model' citation        
3 3 '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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 '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                        9EBZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-13 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9EAT unspecified 
PDB . 9EAW unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              janetsmith@umich.edu 
_pdbx_contact_author.name_first         Janet 
_pdbx_contact_author.name_last          Smith 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0664-9228 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rankin, M.R.' 1 0000-0002-0493-8907 
'Smith, J.L.'  2 0000-0002-0664-9228 
# 
_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                47 
_citation.page_last                 52 
_citation.title                     'Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2053230X25000068 
_citation.pdbx_database_id_PubMed   39812168 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rankin, M.R.' 1 ? 
primary 'Smith, J.L.'  2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Carbonic anhydrase' 25130.779 4 4.2.1.1 ? ? Native 
2 non-polymer syn 'ZINC ION'           65.409    4 ?       ? ? ?      
3 water       nat water                18.015    3 ?       ? ? ?      
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase' 
# 
_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       
;MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV
VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH
STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV
VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH
STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   ASP n 
1 4   ILE n 
1 5   ASP n 
1 6   THR n 
1 7   LEU n 
1 8   ILE n 
1 9   SER n 
1 10  ASN n 
1 11  ASN n 
1 12  ALA n 
1 13  LEU n 
1 14  TRP n 
1 15  SER n 
1 16  LYS n 
1 17  MET n 
1 18  LEU n 
1 19  VAL n 
1 20  GLU n 
1 21  GLU n 
1 22  ASP n 
1 23  PRO n 
1 24  GLY n 
1 25  PHE n 
1 26  PHE n 
1 27  GLU n 
1 28  LYS n 
1 29  LEU n 
1 30  ALA n 
1 31  GLN n 
1 32  ALA n 
1 33  GLN n 
1 34  LYS n 
1 35  PRO n 
1 36  ARG n 
1 37  PHE n 
1 38  LEU n 
1 39  TRP n 
1 40  ILE n 
1 41  GLY n 
1 42  CYS n 
1 43  SER n 
1 44  ASP n 
1 45  SER n 
1 46  ARG n 
1 47  VAL n 
1 48  PRO n 
1 49  ALA n 
1 50  GLU n 
1 51  ARG n 
1 52  LEU n 
1 53  THR n 
1 54  GLY n 
1 55  LEU n 
1 56  GLU n 
1 57  PRO n 
1 58  GLY n 
1 59  GLU n 
1 60  LEU n 
1 61  PHE n 
1 62  VAL n 
1 63  HIS n 
1 64  ARG n 
1 65  ASN n 
1 66  VAL n 
1 67  ALA n 
1 68  ASN n 
1 69  LEU n 
1 70  VAL n 
1 71  ILE n 
1 72  HIS n 
1 73  THR n 
1 74  ASP n 
1 75  LEU n 
1 76  ASN n 
1 77  CYS n 
1 78  LEU n 
1 79  SER n 
1 80  VAL n 
1 81  VAL n 
1 82  GLN n 
1 83  TYR n 
1 84  ALA n 
1 85  VAL n 
1 86  ASP n 
1 87  VAL n 
1 88  LEU n 
1 89  GLU n 
1 90  VAL n 
1 91  GLU n 
1 92  HIS n 
1 93  ILE n 
1 94  ILE n 
1 95  ILE n 
1 96  CYS n 
1 97  GLY n 
1 98  HIS n 
1 99  TYR n 
1 100 GLY n 
1 101 CYS n 
1 102 GLY n 
1 103 GLY n 
1 104 VAL n 
1 105 GLN n 
1 106 ALA n 
1 107 ALA n 
1 108 VAL n 
1 109 GLU n 
1 110 ASN n 
1 111 PRO n 
1 112 GLU n 
1 113 LEU n 
1 114 GLY n 
1 115 LEU n 
1 116 ILE n 
1 117 ASN n 
1 118 ASN n 
1 119 TRP n 
1 120 LEU n 
1 121 LEU n 
1 122 HIS n 
1 123 ILE n 
1 124 ARG n 
1 125 ASP n 
1 126 ILE n 
1 127 TRP n 
1 128 PHE n 
1 129 LYS n 
1 130 HIS n 
1 131 SER n 
1 132 SER n 
1 133 LEU n 
1 134 LEU n 
1 135 GLY n 
1 136 GLU n 
1 137 MET n 
1 138 PRO n 
1 139 GLN n 
1 140 GLU n 
1 141 ARG n 
1 142 ARG n 
1 143 LEU n 
1 144 ASP n 
1 145 THR n 
1 146 LEU n 
1 147 CYS n 
1 148 GLU n 
1 149 LEU n 
1 150 ASN n 
1 151 VAL n 
1 152 MET n 
1 153 GLU n 
1 154 GLN n 
1 155 VAL n 
1 156 TYR n 
1 157 ASN n 
1 158 LEU n 
1 159 GLY n 
1 160 HIS n 
1 161 SER n 
1 162 THR n 
1 163 ILE n 
1 164 MET n 
1 165 GLN n 
1 166 SER n 
1 167 ALA n 
1 168 TRP n 
1 169 LYS n 
1 170 ARG n 
1 171 GLY n 
1 172 GLN n 
1 173 LYS n 
1 174 VAL n 
1 175 THR n 
1 176 ILE n 
1 177 HIS n 
1 178 GLY n 
1 179 TRP n 
1 180 ALA n 
1 181 TYR n 
1 182 GLY n 
1 183 ILE n 
1 184 HIS n 
1 185 ASP n 
1 186 GLY n 
1 187 LEU n 
1 188 LEU n 
1 189 ARG n 
1 190 ASP n 
1 191 LEU n 
1 192 ASP n 
1 193 VAL n 
1 194 THR n 
1 195 ALA n 
1 196 THR n 
1 197 ASN n 
1 198 ARG n 
1 199 GLU n 
1 200 THR n 
1 201 LEU n 
1 202 GLU n 
1 203 GLN n 
1 204 ARG n 
1 205 TYR n 
1 206 ARG n 
1 207 HIS n 
1 208 GLY n 
1 209 ILE n 
1 210 SER n 
1 211 ASN n 
1 212 LEU n 
1 213 LYS n 
1 214 LEU n 
1 215 LYS n 
1 216 HIS n 
1 217 ALA n 
1 218 ASN n 
1 219 HIS n 
1 220 LYS n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           220 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Escherichia coli BL21(DE3)' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      469008 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  TRP 39  39  39  TRP TRP A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  CYS 42  42  42  CYS CYS A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  ARG 46  46  46  ARG ARG A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  CYS 96  96  96  CYS CYS A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 TRP 119 119 119 TRP TRP A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 TRP 127 127 127 TRP TRP A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 GLN 139 139 139 GLN GLN A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 CYS 147 147 147 CYS CYS A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 HIS 160 160 160 HIS HIS A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 MET 164 164 164 MET MET A . n 
A 1 165 GLN 165 165 165 GLN GLN A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 TRP 168 168 168 TRP TRP A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 HIS 177 177 177 HIS HIS A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 TRP 179 179 179 TRP TRP A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 THR 200 200 200 THR THR A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 TYR 205 205 205 TYR TYR A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LYS 215 215 ?   ?   ?   A . n 
A 1 216 HIS 216 216 ?   ?   ?   A . n 
A 1 217 ALA 217 217 ?   ?   ?   A . n 
A 1 218 ASN 218 218 ?   ?   ?   A . n 
A 1 219 HIS 219 219 ?   ?   ?   A . n 
A 1 220 LYS 220 220 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   THR 6   6   6   THR THR B . n 
B 1 7   LEU 7   7   7   LEU LEU B . n 
B 1 8   ILE 8   8   8   ILE ILE B . n 
B 1 9   SER 9   9   9   SER SER B . n 
B 1 10  ASN 10  10  10  ASN ASN B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  TRP 14  14  14  TRP TRP B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  PHE 25  25  25  PHE PHE B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  GLN 31  31  31  GLN GLN B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  GLN 33  33  33  GLN GLN B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PRO 35  35  35  PRO PRO B . n 
B 1 36  ARG 36  36  36  ARG ARG B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  TRP 39  39  39  TRP TRP B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  CYS 42  42  42  CYS CYS B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  ARG 46  46  46  ARG ARG B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  PRO 48  48  48  PRO PRO B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  GLU 50  50  50  GLU GLU B . n 
B 1 51  ARG 51  51  51  ARG ARG B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  THR 53  53  53  THR THR B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  GLU 56  56  56  GLU GLU B . n 
B 1 57  PRO 57  57  57  PRO PRO B . n 
B 1 58  GLY 58  58  58  GLY GLY B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  PHE 61  61  61  PHE PHE B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  ASN 68  68  68  ASN ASN B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ILE 71  71  71  ILE ILE B . n 
B 1 72  HIS 72  72  72  HIS HIS B . n 
B 1 73  THR 73  73  73  THR THR B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ASN 76  76  76  ASN ASN B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  SER 79  79  79  SER SER B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  TYR 83  83  83  TYR TYR B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  CYS 96  96  96  CYS CYS B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  TYR 99  99  99  TYR TYR B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 CYS 101 101 101 CYS CYS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 GLN 105 105 105 GLN GLN B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 VAL 108 108 108 VAL VAL B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 PRO 111 111 111 PRO PRO B . n 
B 1 112 GLU 112 112 112 GLU GLU B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 TRP 119 119 119 TRP TRP B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 ILE 126 126 126 ILE ILE B . n 
B 1 127 TRP 127 127 127 TRP TRP B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 SER 131 131 131 SER SER B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 LEU 134 134 134 LEU LEU B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 MET 137 137 137 MET MET B . n 
B 1 138 PRO 138 138 138 PRO PRO B . n 
B 1 139 GLN 139 139 139 GLN GLN B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 ARG 142 142 142 ARG ARG B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 THR 145 145 145 THR THR B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 CYS 147 147 147 CYS CYS B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 MET 152 152 152 MET MET B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 TYR 156 156 156 TYR TYR B . n 
B 1 157 ASN 157 157 157 ASN ASN B . n 
B 1 158 LEU 158 158 158 LEU LEU B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 HIS 160 160 160 HIS HIS B . n 
B 1 161 SER 161 161 161 SER SER B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 ILE 163 163 163 ILE ILE B . n 
B 1 164 MET 164 164 164 MET MET B . n 
B 1 165 GLN 165 165 165 GLN GLN B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 TRP 168 168 168 TRP TRP B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
B 1 170 ARG 170 170 170 ARG ARG B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 GLN 172 172 172 GLN GLN B . n 
B 1 173 LYS 173 173 173 LYS LYS B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ILE 176 176 176 ILE ILE B . n 
B 1 177 HIS 177 177 177 HIS HIS B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 TRP 179 179 179 TRP TRP B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 TYR 181 181 181 TYR TYR B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 HIS 184 184 184 HIS HIS B . n 
B 1 185 ASP 185 185 185 ASP ASP B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 ARG 189 189 189 ARG ARG B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 ALA 195 195 195 ALA ALA B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASN 197 197 197 ASN ASN B . n 
B 1 198 ARG 198 198 198 ARG ARG B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 THR 200 200 200 THR THR B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 GLN 203 203 203 GLN GLN B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 TYR 205 205 205 TYR TYR B . n 
B 1 206 ARG 206 206 206 ARG ARG B . n 
B 1 207 HIS 207 207 207 HIS HIS B . n 
B 1 208 GLY 208 208 208 GLY GLY B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 SER 210 210 210 SER SER B . n 
B 1 211 ASN 211 211 211 ASN ASN B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 LYS 213 213 213 LYS LYS B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 LYS 215 215 ?   ?   ?   B . n 
B 1 216 HIS 216 216 ?   ?   ?   B . n 
B 1 217 ALA 217 217 ?   ?   ?   B . n 
B 1 218 ASN 218 218 ?   ?   ?   B . n 
B 1 219 HIS 219 219 ?   ?   ?   B . n 
B 1 220 LYS 220 220 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   LYS 2   2   2   LYS LYS C . n 
C 1 3   ASP 3   3   3   ASP ASP C . n 
C 1 4   ILE 4   4   4   ILE ILE C . n 
C 1 5   ASP 5   5   5   ASP ASP C . n 
C 1 6   THR 6   6   6   THR THR C . n 
C 1 7   LEU 7   7   7   LEU LEU C . n 
C 1 8   ILE 8   8   8   ILE ILE C . n 
C 1 9   SER 9   9   9   SER SER C . n 
C 1 10  ASN 10  10  10  ASN ASN C . n 
C 1 11  ASN 11  11  11  ASN ASN C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  TRP 14  14  14  TRP TRP C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  LYS 16  16  16  LYS LYS C . n 
C 1 17  MET 17  17  17  MET MET C . n 
C 1 18  LEU 18  18  18  LEU LEU C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  GLU 20  20  20  GLU GLU C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  ASP 22  22  22  ASP ASP C . n 
C 1 23  PRO 23  23  23  PRO PRO C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  PHE 25  25  25  PHE PHE C . n 
C 1 26  PHE 26  26  26  PHE PHE C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  LYS 28  28  28  LYS LYS C . n 
C 1 29  LEU 29  29  29  LEU LEU C . n 
C 1 30  ALA 30  30  30  ALA ALA C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  ALA 32  32  32  ALA ALA C . n 
C 1 33  GLN 33  33  33  GLN GLN C . n 
C 1 34  LYS 34  34  34  LYS LYS C . n 
C 1 35  PRO 35  35  35  PRO PRO C . n 
C 1 36  ARG 36  36  36  ARG ARG C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  TRP 39  39  39  TRP TRP C . n 
C 1 40  ILE 40  40  40  ILE ILE C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  CYS 42  42  42  CYS CYS C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  ASP 44  44  44  ASP ASP C . n 
C 1 45  SER 45  45  45  SER SER C . n 
C 1 46  ARG 46  46  46  ARG ARG C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  PRO 48  48  48  PRO PRO C . n 
C 1 49  ALA 49  49  49  ALA ALA C . n 
C 1 50  GLU 50  50  50  GLU GLU C . n 
C 1 51  ARG 51  51  51  ARG ARG C . n 
C 1 52  LEU 52  52  52  LEU LEU C . n 
C 1 53  THR 53  53  53  THR THR C . n 
C 1 54  GLY 54  54  54  GLY GLY C . n 
C 1 55  LEU 55  55  55  LEU LEU C . n 
C 1 56  GLU 56  56  56  GLU GLU C . n 
C 1 57  PRO 57  57  57  PRO PRO C . n 
C 1 58  GLY 58  58  58  GLY GLY C . n 
C 1 59  GLU 59  59  59  GLU GLU C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  PHE 61  61  61  PHE PHE C . n 
C 1 62  VAL 62  62  62  VAL VAL C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  ARG 64  64  64  ARG ARG C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  VAL 66  66  66  VAL VAL C . n 
C 1 67  ALA 67  67  67  ALA ALA C . n 
C 1 68  ASN 68  68  68  ASN ASN C . n 
C 1 69  LEU 69  69  69  LEU LEU C . n 
C 1 70  VAL 70  70  70  VAL VAL C . n 
C 1 71  ILE 71  71  71  ILE ILE C . n 
C 1 72  HIS 72  72  72  HIS HIS C . n 
C 1 73  THR 73  73  73  THR THR C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  LEU 75  75  75  LEU LEU C . n 
C 1 76  ASN 76  76  76  ASN ASN C . n 
C 1 77  CYS 77  77  77  CYS CYS C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  SER 79  79  79  SER SER C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  TYR 83  83  83  TYR TYR C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  VAL 85  85  85  VAL VAL C . n 
C 1 86  ASP 86  86  86  ASP ASP C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  LEU 88  88  88  LEU LEU C . n 
C 1 89  GLU 89  89  89  GLU GLU C . n 
C 1 90  VAL 90  90  90  VAL VAL C . n 
C 1 91  GLU 91  91  91  GLU GLU C . n 
C 1 92  HIS 92  92  92  HIS HIS C . n 
C 1 93  ILE 93  93  93  ILE ILE C . n 
C 1 94  ILE 94  94  94  ILE ILE C . n 
C 1 95  ILE 95  95  95  ILE ILE C . n 
C 1 96  CYS 96  96  96  CYS CYS C . n 
C 1 97  GLY 97  97  97  GLY GLY C . n 
C 1 98  HIS 98  98  98  HIS HIS C . n 
C 1 99  TYR 99  99  99  TYR TYR C . n 
C 1 100 GLY 100 100 100 GLY GLY C . n 
C 1 101 CYS 101 101 101 CYS CYS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 VAL 104 104 104 VAL VAL C . n 
C 1 105 GLN 105 105 105 GLN GLN C . n 
C 1 106 ALA 106 106 106 ALA ALA C . n 
C 1 107 ALA 107 107 107 ALA ALA C . n 
C 1 108 VAL 108 108 108 VAL VAL C . n 
C 1 109 GLU 109 109 109 GLU GLU C . n 
C 1 110 ASN 110 110 110 ASN ASN C . n 
C 1 111 PRO 111 111 111 PRO PRO C . n 
C 1 112 GLU 112 112 112 GLU GLU C . n 
C 1 113 LEU 113 113 113 LEU LEU C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 ILE 116 116 116 ILE ILE C . n 
C 1 117 ASN 117 117 117 ASN ASN C . n 
C 1 118 ASN 118 118 118 ASN ASN C . n 
C 1 119 TRP 119 119 119 TRP TRP C . n 
C 1 120 LEU 120 120 120 LEU LEU C . n 
C 1 121 LEU 121 121 121 LEU LEU C . n 
C 1 122 HIS 122 122 122 HIS HIS C . n 
C 1 123 ILE 123 123 123 ILE ILE C . n 
C 1 124 ARG 124 124 124 ARG ARG C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 ILE 126 126 126 ILE ILE C . n 
C 1 127 TRP 127 127 127 TRP TRP C . n 
C 1 128 PHE 128 128 128 PHE PHE C . n 
C 1 129 LYS 129 129 129 LYS LYS C . n 
C 1 130 HIS 130 130 130 HIS HIS C . n 
C 1 131 SER 131 131 131 SER SER C . n 
C 1 132 SER 132 132 132 SER SER C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 LEU 134 134 134 LEU LEU C . n 
C 1 135 GLY 135 135 135 GLY GLY C . n 
C 1 136 GLU 136 136 136 GLU GLU C . n 
C 1 137 MET 137 137 137 MET MET C . n 
C 1 138 PRO 138 138 138 PRO PRO C . n 
C 1 139 GLN 139 139 139 GLN GLN C . n 
C 1 140 GLU 140 140 140 GLU GLU C . n 
C 1 141 ARG 141 141 141 ARG ARG C . n 
C 1 142 ARG 142 142 142 ARG ARG C . n 
C 1 143 LEU 143 143 143 LEU LEU C . n 
C 1 144 ASP 144 144 144 ASP ASP C . n 
C 1 145 THR 145 145 145 THR THR C . n 
C 1 146 LEU 146 146 146 LEU LEU C . n 
C 1 147 CYS 147 147 147 CYS CYS C . n 
C 1 148 GLU 148 148 148 GLU GLU C . n 
C 1 149 LEU 149 149 149 LEU LEU C . n 
C 1 150 ASN 150 150 150 ASN ASN C . n 
C 1 151 VAL 151 151 151 VAL VAL C . n 
C 1 152 MET 152 152 152 MET MET C . n 
C 1 153 GLU 153 153 153 GLU GLU C . n 
C 1 154 GLN 154 154 154 GLN GLN C . n 
C 1 155 VAL 155 155 155 VAL VAL C . n 
C 1 156 TYR 156 156 156 TYR TYR C . n 
C 1 157 ASN 157 157 157 ASN ASN C . n 
C 1 158 LEU 158 158 158 LEU LEU C . n 
C 1 159 GLY 159 159 159 GLY GLY C . n 
C 1 160 HIS 160 160 160 HIS HIS C . n 
C 1 161 SER 161 161 161 SER SER C . n 
C 1 162 THR 162 162 162 THR THR C . n 
C 1 163 ILE 163 163 163 ILE ILE C . n 
C 1 164 MET 164 164 164 MET MET C . n 
C 1 165 GLN 165 165 165 GLN GLN C . n 
C 1 166 SER 166 166 166 SER SER C . n 
C 1 167 ALA 167 167 167 ALA ALA C . n 
C 1 168 TRP 168 168 168 TRP TRP C . n 
C 1 169 LYS 169 169 169 LYS LYS C . n 
C 1 170 ARG 170 170 170 ARG ARG C . n 
C 1 171 GLY 171 171 171 GLY GLY C . n 
C 1 172 GLN 172 172 172 GLN GLN C . n 
C 1 173 LYS 173 173 173 LYS LYS C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 THR 175 175 175 THR THR C . n 
C 1 176 ILE 176 176 176 ILE ILE C . n 
C 1 177 HIS 177 177 177 HIS HIS C . n 
C 1 178 GLY 178 178 178 GLY GLY C . n 
C 1 179 TRP 179 179 179 TRP TRP C . n 
C 1 180 ALA 180 180 180 ALA ALA C . n 
C 1 181 TYR 181 181 181 TYR TYR C . n 
C 1 182 GLY 182 182 182 GLY GLY C . n 
C 1 183 ILE 183 183 183 ILE ILE C . n 
C 1 184 HIS 184 184 184 HIS HIS C . n 
C 1 185 ASP 185 185 185 ASP ASP C . n 
C 1 186 GLY 186 186 186 GLY GLY C . n 
C 1 187 LEU 187 187 187 LEU LEU C . n 
C 1 188 LEU 188 188 188 LEU LEU C . n 
C 1 189 ARG 189 189 189 ARG ARG C . n 
C 1 190 ASP 190 190 190 ASP ASP C . n 
C 1 191 LEU 191 191 191 LEU LEU C . n 
C 1 192 ASP 192 192 192 ASP ASP C . n 
C 1 193 VAL 193 193 193 VAL VAL C . n 
C 1 194 THR 194 194 194 THR THR C . n 
C 1 195 ALA 195 195 195 ALA ALA C . n 
C 1 196 THR 196 196 196 THR THR C . n 
C 1 197 ASN 197 197 197 ASN ASN C . n 
C 1 198 ARG 198 198 198 ARG ARG C . n 
C 1 199 GLU 199 199 199 GLU GLU C . n 
C 1 200 THR 200 200 200 THR THR C . n 
C 1 201 LEU 201 201 201 LEU LEU C . n 
C 1 202 GLU 202 202 202 GLU GLU C . n 
C 1 203 GLN 203 203 203 GLN GLN C . n 
C 1 204 ARG 204 204 204 ARG ARG C . n 
C 1 205 TYR 205 205 205 TYR TYR C . n 
C 1 206 ARG 206 206 206 ARG ARG C . n 
C 1 207 HIS 207 207 207 HIS HIS C . n 
C 1 208 GLY 208 208 208 GLY GLY C . n 
C 1 209 ILE 209 209 209 ILE ILE C . n 
C 1 210 SER 210 210 210 SER SER C . n 
C 1 211 ASN 211 211 211 ASN ASN C . n 
C 1 212 LEU 212 212 212 LEU LEU C . n 
C 1 213 LYS 213 213 213 LYS LYS C . n 
C 1 214 LEU 214 214 ?   ?   ?   C . n 
C 1 215 LYS 215 215 ?   ?   ?   C . n 
C 1 216 HIS 216 216 ?   ?   ?   C . n 
C 1 217 ALA 217 217 ?   ?   ?   C . n 
C 1 218 ASN 218 218 ?   ?   ?   C . n 
C 1 219 HIS 219 219 ?   ?   ?   C . n 
C 1 220 LYS 220 220 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   LYS 2   2   2   LYS LYS D . n 
D 1 3   ASP 3   3   3   ASP ASP D . n 
D 1 4   ILE 4   4   4   ILE ILE D . n 
D 1 5   ASP 5   5   5   ASP ASP D . n 
D 1 6   THR 6   6   6   THR THR D . n 
D 1 7   LEU 7   7   7   LEU LEU D . n 
D 1 8   ILE 8   8   8   ILE ILE D . n 
D 1 9   SER 9   9   9   SER SER D . n 
D 1 10  ASN 10  10  10  ASN ASN D . n 
D 1 11  ASN 11  11  11  ASN ASN D . n 
D 1 12  ALA 12  12  12  ALA ALA D . n 
D 1 13  LEU 13  13  13  LEU LEU D . n 
D 1 14  TRP 14  14  14  TRP TRP D . n 
D 1 15  SER 15  15  15  SER SER D . n 
D 1 16  LYS 16  16  16  LYS LYS D . n 
D 1 17  MET 17  17  17  MET MET D . n 
D 1 18  LEU 18  18  18  LEU LEU D . n 
D 1 19  VAL 19  19  19  VAL VAL D . n 
D 1 20  GLU 20  20  20  GLU GLU D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  ASP 22  22  22  ASP ASP D . n 
D 1 23  PRO 23  23  23  PRO PRO D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  PHE 25  25  25  PHE PHE D . n 
D 1 26  PHE 26  26  26  PHE PHE D . n 
D 1 27  GLU 27  27  27  GLU GLU D . n 
D 1 28  LYS 28  28  28  LYS LYS D . n 
D 1 29  LEU 29  29  29  LEU LEU D . n 
D 1 30  ALA 30  30  30  ALA ALA D . n 
D 1 31  GLN 31  31  31  GLN GLN D . n 
D 1 32  ALA 32  32  32  ALA ALA D . n 
D 1 33  GLN 33  33  33  GLN GLN D . n 
D 1 34  LYS 34  34  34  LYS LYS D . n 
D 1 35  PRO 35  35  35  PRO PRO D . n 
D 1 36  ARG 36  36  36  ARG ARG D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  TRP 39  39  39  TRP TRP D . n 
D 1 40  ILE 40  40  40  ILE ILE D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  CYS 42  42  42  CYS CYS D . n 
D 1 43  SER 43  43  43  SER SER D . n 
D 1 44  ASP 44  44  44  ASP ASP D . n 
D 1 45  SER 45  45  45  SER SER D . n 
D 1 46  ARG 46  46  46  ARG ARG D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  PRO 48  48  48  PRO PRO D . n 
D 1 49  ALA 49  49  49  ALA ALA D . n 
D 1 50  GLU 50  50  50  GLU GLU D . n 
D 1 51  ARG 51  51  51  ARG ARG D . n 
D 1 52  LEU 52  52  52  LEU LEU D . n 
D 1 53  THR 53  53  53  THR THR D . n 
D 1 54  GLY 54  54  54  GLY GLY D . n 
D 1 55  LEU 55  55  55  LEU LEU D . n 
D 1 56  GLU 56  56  56  GLU GLU D . n 
D 1 57  PRO 57  57  57  PRO PRO D . n 
D 1 58  GLY 58  58  58  GLY GLY D . n 
D 1 59  GLU 59  59  59  GLU GLU D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  PHE 61  61  61  PHE PHE D . n 
D 1 62  VAL 62  62  62  VAL VAL D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  ARG 64  64  64  ARG ARG D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  VAL 66  66  66  VAL VAL D . n 
D 1 67  ALA 67  67  67  ALA ALA D . n 
D 1 68  ASN 68  68  68  ASN ASN D . n 
D 1 69  LEU 69  69  69  LEU LEU D . n 
D 1 70  VAL 70  70  70  VAL VAL D . n 
D 1 71  ILE 71  71  71  ILE ILE D . n 
D 1 72  HIS 72  72  72  HIS HIS D . n 
D 1 73  THR 73  73  73  THR THR D . n 
D 1 74  ASP 74  74  74  ASP ASP D . n 
D 1 75  LEU 75  75  75  LEU LEU D . n 
D 1 76  ASN 76  76  76  ASN ASN D . n 
D 1 77  CYS 77  77  77  CYS CYS D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  SER 79  79  79  SER SER D . n 
D 1 80  VAL 80  80  80  VAL VAL D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  TYR 83  83  83  TYR TYR D . n 
D 1 84  ALA 84  84  84  ALA ALA D . n 
D 1 85  VAL 85  85  85  VAL VAL D . n 
D 1 86  ASP 86  86  86  ASP ASP D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  LEU 88  88  88  LEU LEU D . n 
D 1 89  GLU 89  89  89  GLU GLU D . n 
D 1 90  VAL 90  90  90  VAL VAL D . n 
D 1 91  GLU 91  91  91  GLU GLU D . n 
D 1 92  HIS 92  92  92  HIS HIS D . n 
D 1 93  ILE 93  93  93  ILE ILE D . n 
D 1 94  ILE 94  94  94  ILE ILE D . n 
D 1 95  ILE 95  95  95  ILE ILE D . n 
D 1 96  CYS 96  96  96  CYS CYS D . n 
D 1 97  GLY 97  97  97  GLY GLY D . n 
D 1 98  HIS 98  98  98  HIS HIS D . n 
D 1 99  TYR 99  99  99  TYR TYR D . n 
D 1 100 GLY 100 100 100 GLY GLY D . n 
D 1 101 CYS 101 101 101 CYS CYS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 GLY 103 103 103 GLY GLY D . n 
D 1 104 VAL 104 104 104 VAL VAL D . n 
D 1 105 GLN 105 105 105 GLN GLN D . n 
D 1 106 ALA 106 106 106 ALA ALA D . n 
D 1 107 ALA 107 107 107 ALA ALA D . n 
D 1 108 VAL 108 108 108 VAL VAL D . n 
D 1 109 GLU 109 109 109 GLU GLU D . n 
D 1 110 ASN 110 110 110 ASN ASN D . n 
D 1 111 PRO 111 111 111 PRO PRO D . n 
D 1 112 GLU 112 112 112 GLU GLU D . n 
D 1 113 LEU 113 113 113 LEU LEU D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 ILE 116 116 116 ILE ILE D . n 
D 1 117 ASN 117 117 117 ASN ASN D . n 
D 1 118 ASN 118 118 118 ASN ASN D . n 
D 1 119 TRP 119 119 119 TRP TRP D . n 
D 1 120 LEU 120 120 120 LEU LEU D . n 
D 1 121 LEU 121 121 121 LEU LEU D . n 
D 1 122 HIS 122 122 122 HIS HIS D . n 
D 1 123 ILE 123 123 123 ILE ILE D . n 
D 1 124 ARG 124 124 124 ARG ARG D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 ILE 126 126 126 ILE ILE D . n 
D 1 127 TRP 127 127 127 TRP TRP D . n 
D 1 128 PHE 128 128 128 PHE PHE D . n 
D 1 129 LYS 129 129 129 LYS LYS D . n 
D 1 130 HIS 130 130 130 HIS HIS D . n 
D 1 131 SER 131 131 131 SER SER D . n 
D 1 132 SER 132 132 132 SER SER D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 LEU 134 134 134 LEU LEU D . n 
D 1 135 GLY 135 135 135 GLY GLY D . n 
D 1 136 GLU 136 136 136 GLU GLU D . n 
D 1 137 MET 137 137 137 MET MET D . n 
D 1 138 PRO 138 138 138 PRO PRO D . n 
D 1 139 GLN 139 139 139 GLN GLN D . n 
D 1 140 GLU 140 140 140 GLU GLU D . n 
D 1 141 ARG 141 141 141 ARG ARG D . n 
D 1 142 ARG 142 142 142 ARG ARG D . n 
D 1 143 LEU 143 143 143 LEU LEU D . n 
D 1 144 ASP 144 144 144 ASP ASP D . n 
D 1 145 THR 145 145 145 THR THR D . n 
D 1 146 LEU 146 146 146 LEU LEU D . n 
D 1 147 CYS 147 147 147 CYS CYS D . n 
D 1 148 GLU 148 148 148 GLU GLU D . n 
D 1 149 LEU 149 149 149 LEU LEU D . n 
D 1 150 ASN 150 150 150 ASN ASN D . n 
D 1 151 VAL 151 151 151 VAL VAL D . n 
D 1 152 MET 152 152 152 MET MET D . n 
D 1 153 GLU 153 153 153 GLU GLU D . n 
D 1 154 GLN 154 154 154 GLN GLN D . n 
D 1 155 VAL 155 155 155 VAL VAL D . n 
D 1 156 TYR 156 156 156 TYR TYR D . n 
D 1 157 ASN 157 157 157 ASN ASN D . n 
D 1 158 LEU 158 158 158 LEU LEU D . n 
D 1 159 GLY 159 159 159 GLY GLY D . n 
D 1 160 HIS 160 160 160 HIS HIS D . n 
D 1 161 SER 161 161 161 SER SER D . n 
D 1 162 THR 162 162 162 THR THR D . n 
D 1 163 ILE 163 163 163 ILE ILE D . n 
D 1 164 MET 164 164 164 MET MET D . n 
D 1 165 GLN 165 165 165 GLN GLN D . n 
D 1 166 SER 166 166 166 SER SER D . n 
D 1 167 ALA 167 167 167 ALA ALA D . n 
D 1 168 TRP 168 168 168 TRP TRP D . n 
D 1 169 LYS 169 169 169 LYS LYS D . n 
D 1 170 ARG 170 170 170 ARG ARG D . n 
D 1 171 GLY 171 171 171 GLY GLY D . n 
D 1 172 GLN 172 172 172 GLN GLN D . n 
D 1 173 LYS 173 173 173 LYS LYS D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 THR 175 175 175 THR THR D . n 
D 1 176 ILE 176 176 176 ILE ILE D . n 
D 1 177 HIS 177 177 177 HIS HIS D . n 
D 1 178 GLY 178 178 178 GLY GLY D . n 
D 1 179 TRP 179 179 179 TRP TRP D . n 
D 1 180 ALA 180 180 180 ALA ALA D . n 
D 1 181 TYR 181 181 181 TYR TYR D . n 
D 1 182 GLY 182 182 182 GLY GLY D . n 
D 1 183 ILE 183 183 183 ILE ILE D . n 
D 1 184 HIS 184 184 184 HIS HIS D . n 
D 1 185 ASP 185 185 185 ASP ASP D . n 
D 1 186 GLY 186 186 186 GLY GLY D . n 
D 1 187 LEU 187 187 187 LEU LEU D . n 
D 1 188 LEU 188 188 188 LEU LEU D . n 
D 1 189 ARG 189 189 189 ARG ARG D . n 
D 1 190 ASP 190 190 190 ASP ASP D . n 
D 1 191 LEU 191 191 191 LEU LEU D . n 
D 1 192 ASP 192 192 192 ASP ASP D . n 
D 1 193 VAL 193 193 193 VAL VAL D . n 
D 1 194 THR 194 194 194 THR THR D . n 
D 1 195 ALA 195 195 195 ALA ALA D . n 
D 1 196 THR 196 196 196 THR THR D . n 
D 1 197 ASN 197 197 197 ASN ASN D . n 
D 1 198 ARG 198 198 198 ARG ARG D . n 
D 1 199 GLU 199 199 199 GLU GLU D . n 
D 1 200 THR 200 200 200 THR THR D . n 
D 1 201 LEU 201 201 201 LEU LEU D . n 
D 1 202 GLU 202 202 202 GLU GLU D . n 
D 1 203 GLN 203 203 203 GLN GLN D . n 
D 1 204 ARG 204 204 204 ARG ARG D . n 
D 1 205 TYR 205 205 205 TYR TYR D . n 
D 1 206 ARG 206 206 206 ARG ARG D . n 
D 1 207 HIS 207 207 207 HIS HIS D . n 
D 1 208 GLY 208 208 208 GLY GLY D . n 
D 1 209 ILE 209 209 209 ILE ILE D . n 
D 1 210 SER 210 210 210 SER SER D . n 
D 1 211 ASN 211 211 211 ASN ASN D . n 
D 1 212 LEU 212 212 212 LEU LEU D . n 
D 1 213 LYS 213 213 213 LYS LYS D . n 
D 1 214 LEU 214 214 214 LEU LEU D . n 
D 1 215 LYS 215 215 ?   ?   ?   D . n 
D 1 216 HIS 216 216 ?   ?   ?   D . n 
D 1 217 ALA 217 217 ?   ?   ?   D . n 
D 1 218 ASN 218 218 ?   ?   ?   D . n 
D 1 219 HIS 219 219 ?   ?   ?   D . n 
D 1 220 LYS 220 220 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN  1 301 1 ZN  ZN  A . 
F 2 ZN  1 301 2 ZN  ZN  B . 
G 2 ZN  1 301 4 ZN  ZN  C . 
H 2 ZN  1 301 3 ZN  ZN  D . 
I 3 HOH 1 401 4 HOH HOH A . 
J 3 HOH 1 401 3 HOH HOH C . 
J 3 HOH 2 402 5 HOH HOH C . 
# 
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' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EBZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.227 
_cell.length_a_esd                 ? 
_cell.length_b                     119.145 
_cell.length_b_esd                 ? 
_cell.length_c                     161.010 
_cell.length_c_esd                 ? 
_cell.volume                       2172094.282 
_cell.volume_esd                   ? 
_cell.Z_PDB                        32 
_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                         9EBZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   9EBZ 
_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             2.70 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.46 
_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, SITTING 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    '200 mM ammonium tartrate dibasic, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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 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         2022-09-28 
_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   1.0332 
_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                        'APS BEAMLINE 23-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          63.72 
_reflns.entry_id                                       9EBZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.66 
_reflns.d_resolution_low                               47.89 
_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                                     31559 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.0 
_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                                ? 
_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                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.66 
_reflns_shell.d_res_low                                     2.73 
_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                             3099 
_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                                  0.584 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               82.16 
_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                                 9EBZ 
_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                            2.66 
_refine.ls_d_res_low                             47.89 
_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                     31487 
_refine.ls_number_reflns_R_free                  2005 
_refine.ls_number_reflns_R_work                  29482 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 6.37 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2624 
_refine.ls_R_factor_R_free                       0.2873 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2606 
_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                          1.11 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 38.7874 
_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                            0.5150 
_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                       2.66 
_refine_hist.d_res_low                        47.89 
_refine_hist.number_atoms_solvent             3 
_refine_hist.number_atoms_total               6831 
_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        6824 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0039  ? 6972 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6495  ? 9459 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0447  ? 1055 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0056  ? 1216 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.3274 ? 2545 ? f_dihedral_angle_d ? ? 
# 
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' 2.66 2.73  . . 144 2077 99.82 . . . . 0.4755 . . . . . . . . . . . 0.4984 
'X-RAY DIFFRACTION' 2.73 2.80  . . 140 2042 99.23 . . . . 0.4436 . . . . . . . . . . . 0.4862 
'X-RAY DIFFRACTION' 2.80 2.88  . . 147 2098 99.69 . . . . 0.4171 . . . . . . . . . . . 0.4687 
'X-RAY DIFFRACTION' 2.88 2.98  . . 137 2088 99.64 . . . . 0.3874 . . . . . . . . . . . 0.4331 
'X-RAY DIFFRACTION' 2.98 3.08  . . 148 2055 99.64 . . . . 0.3626 . . . . . . . . . . . 0.3818 
'X-RAY DIFFRACTION' 3.08 3.21  . . 127 2106 99.64 . . . . 0.3184 . . . . . . . . . . . 0.3440 
'X-RAY DIFFRACTION' 3.21 3.35  . . 152 2093 99.47 . . . . 0.2967 . . . . . . . . . . . 0.3147 
'X-RAY DIFFRACTION' 3.35 3.53  . . 143 2090 99.64 . . . . 0.2828 . . . . . . . . . . . 0.3445 
'X-RAY DIFFRACTION' 3.53 3.75  . . 139 2100 99.29 . . . . 0.2744 . . . . . . . . . . . 0.3234 
'X-RAY DIFFRACTION' 3.75 4.04  . . 136 2102 99.60 . . . . 0.2684 . . . . . . . . . . . 0.2674 
'X-RAY DIFFRACTION' 4.04 4.44  . . 147 2099 99.87 . . . . 0.2354 . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 4.44 5.09  . . 141 2143 99.83 . . . . 0.2074 . . . . . . . . . . . 0.2707 
'X-RAY DIFFRACTION' 5.09 6.41  . . 150 2158 99.87 . . . . 0.2344 . . . . . . . . . . . 0.2723 
'X-RAY DIFFRACTION' 6.41 47.89 . . 154 2231 99.62 . . . . 0.1824 . . . . . . . . . . . 0.1889 
# 
_struct.entry_id                     9EBZ 
_struct.title                        'Escherichia coli Carbonic Anhydrase 2 in Space Group C222(1)' 
_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        9EBZ 
_struct_keywords.text            'Zinc-dependent metalloprotein, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A140NBR3_ECOBD 
_struct_ref.pdbx_db_accession          A0A140NBR3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV
VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH
STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
;
_struct_ref.pdbx_align_begin           1 
# 
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 9EBZ A 1 ? 220 ? A0A140NBR3 1 ? 220 ? 1 220 
2 1 9EBZ B 1 ? 220 ? A0A140NBR3 1 ? 220 ? 1 220 
3 1 9EBZ C 1 ? 220 ? A0A140NBR3 1 ? 220 ? 1 220 
4 1 9EBZ D 1 ? 220 ? A0A140NBR3 1 ? 220 ? 1 220 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 15670 ? 
1 MORE         -85   ? 
1 'SSA (A^2)'  32750 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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 ASP A 3   ? ASP A 22  ? ASP A 3   ASP A 22  1 ? 20 
HELX_P HELX_P2  AA2 GLY A 24  ? GLN A 31  ? GLY A 24  GLN A 31  1 ? 8  
HELX_P HELX_P3  AA3 PRO A 48  ? GLY A 54  ? PRO A 48  GLY A 54  1 ? 7  
HELX_P HELX_P4  AA4 ASP A 74  ? VAL A 87  ? ASP A 74  VAL A 87  1 ? 14 
HELX_P HELX_P5  AA5 CYS A 101 ? ASN A 110 ? CYS A 101 ASN A 110 1 ? 10 
HELX_P HELX_P6  AA6 LEU A 115 ? HIS A 130 ? LEU A 115 HIS A 130 1 ? 16 
HELX_P HELX_P7  AA7 HIS A 130 ? MET A 137 ? HIS A 130 MET A 137 1 ? 8  
HELX_P HELX_P8  AA8 PRO A 138 ? GLU A 140 ? PRO A 138 GLU A 140 5 ? 3  
HELX_P HELX_P9  AA9 ARG A 141 ? SER A 161 ? ARG A 141 SER A 161 1 ? 21 
HELX_P HELX_P10 AB1 SER A 161 ? ARG A 170 ? SER A 161 ARG A 170 1 ? 10 
HELX_P HELX_P11 AB2 ASN A 197 ? LYS A 213 ? ASN A 197 LYS A 213 1 ? 17 
HELX_P HELX_P12 AB3 ASP B 3   ? ASP B 22  ? ASP B 3   ASP B 22  1 ? 20 
HELX_P HELX_P13 AB4 GLY B 24  ? GLN B 31  ? GLY B 24  GLN B 31  1 ? 8  
HELX_P HELX_P14 AB5 PRO B 48  ? GLY B 54  ? PRO B 48  GLY B 54  1 ? 7  
HELX_P HELX_P15 AB6 ASP B 74  ? VAL B 87  ? ASP B 74  VAL B 87  1 ? 14 
HELX_P HELX_P16 AB7 CYS B 101 ? ASN B 110 ? CYS B 101 ASN B 110 1 ? 10 
HELX_P HELX_P17 AB8 LEU B 115 ? HIS B 130 ? LEU B 115 HIS B 130 1 ? 16 
HELX_P HELX_P18 AB9 HIS B 130 ? GLU B 136 ? HIS B 130 GLU B 136 1 ? 7  
HELX_P HELX_P19 AC1 MET B 137 ? GLU B 140 ? MET B 137 GLU B 140 5 ? 4  
HELX_P HELX_P20 AC2 ARG B 141 ? SER B 161 ? ARG B 141 SER B 161 1 ? 21 
HELX_P HELX_P21 AC3 SER B 161 ? ARG B 170 ? SER B 161 ARG B 170 1 ? 10 
HELX_P HELX_P22 AC4 ASN B 197 ? LYS B 213 ? ASN B 197 LYS B 213 1 ? 17 
HELX_P HELX_P23 AC5 ASP C 3   ? ASP C 22  ? ASP C 3   ASP C 22  1 ? 20 
HELX_P HELX_P24 AC6 GLY C 24  ? ALA C 32  ? GLY C 24  ALA C 32  1 ? 9  
HELX_P HELX_P25 AC7 PRO C 48  ? GLY C 54  ? PRO C 48  GLY C 54  1 ? 7  
HELX_P HELX_P26 AC8 ASP C 74  ? VAL C 87  ? ASP C 74  VAL C 87  1 ? 14 
HELX_P HELX_P27 AC9 CYS C 101 ? ASN C 110 ? CYS C 101 ASN C 110 1 ? 10 
HELX_P HELX_P28 AD1 LEU C 115 ? HIS C 130 ? LEU C 115 HIS C 130 1 ? 16 
HELX_P HELX_P29 AD2 HIS C 130 ? MET C 137 ? HIS C 130 MET C 137 1 ? 8  
HELX_P HELX_P30 AD3 PRO C 138 ? ARG C 141 ? PRO C 138 ARG C 141 5 ? 4  
HELX_P HELX_P31 AD4 ARG C 142 ? SER C 161 ? ARG C 142 SER C 161 1 ? 20 
HELX_P HELX_P32 AD5 SER C 161 ? ARG C 170 ? SER C 161 ARG C 170 1 ? 10 
HELX_P HELX_P33 AD6 ASN C 197 ? LYS C 213 ? ASN C 197 LYS C 213 1 ? 17 
HELX_P HELX_P34 AD7 ASP D 3   ? ASP D 22  ? ASP D 3   ASP D 22  1 ? 20 
HELX_P HELX_P35 AD8 GLY D 24  ? GLN D 31  ? GLY D 24  GLN D 31  1 ? 8  
HELX_P HELX_P36 AD9 PRO D 48  ? GLY D 54  ? PRO D 48  GLY D 54  1 ? 7  
HELX_P HELX_P37 AE1 ASP D 74  ? VAL D 87  ? ASP D 74  VAL D 87  1 ? 14 
HELX_P HELX_P38 AE2 CYS D 101 ? ASN D 110 ? CYS D 101 ASN D 110 1 ? 10 
HELX_P HELX_P39 AE3 LEU D 115 ? HIS D 130 ? LEU D 115 HIS D 130 1 ? 16 
HELX_P HELX_P40 AE4 HIS D 130 ? MET D 137 ? HIS D 130 MET D 137 1 ? 8  
HELX_P HELX_P41 AE5 PRO D 138 ? GLU D 140 ? PRO D 138 GLU D 140 5 ? 3  
HELX_P HELX_P42 AE6 ARG D 141 ? SER D 161 ? ARG D 141 SER D 161 1 ? 21 
HELX_P HELX_P43 AE7 SER D 161 ? ARG D 170 ? SER D 161 ARG D 170 1 ? 10 
HELX_P HELX_P44 AE8 ASN D 197 ? LYS D 213 ? ASN D 197 LYS D 213 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 42  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 42  A ZN 301 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc2  metalc ? ? A ASP 44  OD2 ? ? ? 1_555 E ZN . ZN ? ? A ASP 44  A ZN 301 1_555 ? ? ? ? ? ? ? 1.982 ? ? 
metalc3  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 E ZN . ZN ? ? A HIS 98  A ZN 301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc4  metalc ? ? A CYS 101 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 101 A ZN 301 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
metalc5  metalc ? ? B CYS 42  SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 42  B ZN 301 1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc6  metalc ? ? B ASP 44  OD2 ? ? ? 1_555 F ZN . ZN ? ? B ASP 44  B ZN 301 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc7  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 F ZN . ZN ? ? B HIS 98  B ZN 301 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc8  metalc ? ? B CYS 101 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 101 B ZN 301 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc9  metalc ? ? C CYS 42  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 42  C ZN 301 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc10 metalc ? ? C ASP 44  OD2 ? ? ? 1_555 G ZN . ZN ? ? C ASP 44  C ZN 301 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc11 metalc ? ? C HIS 98  NE2 ? ? ? 1_555 G ZN . ZN ? ? C HIS 98  C ZN 301 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc12 metalc ? ? C CYS 101 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 101 C ZN 301 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc13 metalc ? ? D CYS 42  SG  ? ? ? 1_555 H ZN . ZN ? ? D CYS 42  D ZN 301 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc14 metalc ? ? D ASP 44  OD2 ? ? ? 1_555 H ZN . ZN ? ? D ASP 44  D ZN 301 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc15 metalc ? ? D HIS 98  NE2 ? ? ? 1_555 H ZN . ZN ? ? D HIS 98  D ZN 301 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc16 metalc ? ? D CYS 101 SG  ? ? ? 1_555 H ZN . ZN ? ? D CYS 101 D ZN 301 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 42 ? A CYS 42 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 OD2 ? A ASP 44  ? A ASP 44  ? 1_555 101.1 ? 
2  SG  ? A CYS 42 ? A CYS 42 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 95.1  ? 
3  OD2 ? A ASP 44 ? A ASP 44 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 110.4 ? 
4  SG  ? A CYS 42 ? A CYS 42 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 101 ? A CYS 101 ? 1_555 106.3 ? 
5  OD2 ? A ASP 44 ? A ASP 44 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 101 ? A CYS 101 ? 1_555 126.6 ? 
6  NE2 ? A HIS 98 ? A HIS 98 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 101 ? A CYS 101 ? 1_555 111.6 ? 
7  SG  ? B CYS 42 ? B CYS 42 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 OD2 ? B ASP 44  ? B ASP 44  ? 1_555 96.8  ? 
8  SG  ? B CYS 42 ? B CYS 42 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 97.7  ? 
9  OD2 ? B ASP 44 ? B ASP 44 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 106.6 ? 
10 SG  ? B CYS 42 ? B CYS 42 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 101 ? B CYS 101 ? 1_555 112.6 ? 
11 OD2 ? B ASP 44 ? B ASP 44 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 101 ? B CYS 101 ? 1_555 118.0 ? 
12 NE2 ? B HIS 98 ? B HIS 98 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 101 ? B CYS 101 ? 1_555 120.8 ? 
13 SG  ? C CYS 42 ? C CYS 42 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 OD2 ? C ASP 44  ? C ASP 44  ? 1_555 101.9 ? 
14 SG  ? C CYS 42 ? C CYS 42 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 98  ? C HIS 98  ? 1_555 97.4  ? 
15 OD2 ? C ASP 44 ? C ASP 44 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 98  ? C HIS 98  ? 1_555 108.0 ? 
16 SG  ? C CYS 42 ? C CYS 42 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 101 ? C CYS 101 ? 1_555 115.4 ? 
17 OD2 ? C ASP 44 ? C ASP 44 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 101 ? C CYS 101 ? 1_555 114.7 ? 
18 NE2 ? C HIS 98 ? C HIS 98 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 101 ? C CYS 101 ? 1_555 117.2 ? 
19 SG  ? D CYS 42 ? D CYS 42 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 OD2 ? D ASP 44  ? D ASP 44  ? 1_555 91.9  ? 
20 SG  ? D CYS 42 ? D CYS 42 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 98  ? D HIS 98  ? 1_555 93.3  ? 
21 OD2 ? D ASP 44 ? D ASP 44 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 98  ? D HIS 98  ? 1_555 105.9 ? 
22 SG  ? D CYS 42 ? D CYS 42 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 101 ? D CYS 101 ? 1_555 124.8 ? 
23 OD2 ? D ASP 44 ? D ASP 44 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 101 ? D CYS 101 ? 1_555 119.4 ? 
24 NE2 ? D HIS 98 ? D HIS 98 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 101 ? D CYS 101 ? 1_555 116.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? 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 LEU A 60  ? ASN A 65  ? LEU A 60  ASN A 65  
AA1 2 PHE A 37  ? CYS A 42  ? PHE A 37  CYS A 42  
AA1 3 HIS A 92  ? HIS A 98  ? HIS A 92  HIS A 98  
AA1 4 THR A 175 ? TYR A 181 ? THR A 175 TYR A 181 
AA1 5 LEU A 188 ? ASP A 190 ? LEU A 188 ASP A 190 
AA2 1 LEU B 60  ? ASN B 65  ? LEU B 60  ASN B 65  
AA2 2 PHE B 37  ? CYS B 42  ? PHE B 37  CYS B 42  
AA2 3 HIS B 92  ? HIS B 98  ? HIS B 92  HIS B 98  
AA2 4 THR B 175 ? TYR B 181 ? THR B 175 TYR B 181 
AA2 5 ARG B 189 ? ASP B 190 ? ARG B 189 ASP B 190 
AA3 1 LEU C 60  ? ASN C 65  ? LEU C 60  ASN C 65  
AA3 2 PHE C 37  ? CYS C 42  ? PHE C 37  CYS C 42  
AA3 3 HIS C 92  ? HIS C 98  ? HIS C 92  HIS C 98  
AA3 4 THR C 175 ? TYR C 181 ? THR C 175 TYR C 181 
AA3 5 LEU C 188 ? ASP C 190 ? LEU C 188 ASP C 190 
AA4 1 LEU D 60  ? ASN D 65  ? LEU D 60  ASN D 65  
AA4 2 PHE D 37  ? CYS D 42  ? PHE D 37  CYS D 42  
AA4 3 HIS D 92  ? HIS D 98  ? HIS D 92  HIS D 98  
AA4 4 THR D 175 ? TYR D 181 ? THR D 175 TYR D 181 
AA4 5 LEU D 188 ? ASP D 190 ? LEU D 188 ASP D 190 
# 
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 PHE A 61  ? O PHE A 61  N TRP A 39  ? N TRP A 39  
AA1 2 3 N LEU A 38  ? N LEU A 38  O ILE A 94  ? O ILE A 94  
AA1 3 4 N ILE A 95  ? N ILE A 95  O HIS A 177 ? O HIS A 177 
AA1 4 5 N ALA A 180 ? N ALA A 180 O ARG A 189 ? O ARG A 189 
AA2 1 2 O PHE B 61  ? O PHE B 61  N TRP B 39  ? N TRP B 39  
AA2 2 3 N LEU B 38  ? N LEU B 38  O ILE B 94  ? O ILE B 94  
AA2 3 4 N ILE B 95  ? N ILE B 95  O HIS B 177 ? O HIS B 177 
AA2 4 5 N ALA B 180 ? N ALA B 180 O ARG B 189 ? O ARG B 189 
AA3 1 2 O PHE C 61  ? O PHE C 61  N TRP C 39  ? N TRP C 39  
AA3 2 3 N LEU C 38  ? N LEU C 38  O ILE C 94  ? O ILE C 94  
AA3 3 4 N ILE C 95  ? N ILE C 95  O HIS C 177 ? O HIS C 177 
AA3 4 5 N ALA C 180 ? N ALA C 180 O ARG C 189 ? O ARG C 189 
AA4 1 2 O PHE D 61  ? O PHE D 61  N TRP D 39  ? N TRP D 39  
AA4 2 3 N LEU D 38  ? N LEU D 38  O ILE D 94  ? O ILE D 94  
AA4 3 4 N ILE D 95  ? N ILE D 95  O HIS D 177 ? O HIS D 177 
AA4 4 5 N ALA D 180 ? N ALA D 180 O ARG D 189 ? O ARG D 189 
# 
_pdbx_entry_details.entry_id                   9EBZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLN B 31  ? ? -96.22  55.85   
2 1 ALA B 32  ? ? -99.68  32.73   
3 1 GLN B 33  ? ? 57.57   -140.95 
4 1 ASP B 185 ? ? -140.12 -13.16  
5 1 ASP C 185 ? ? -141.28 -11.75  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A LYS 215 ? A LYS 215 
3  1 Y 1 A HIS 216 ? A HIS 216 
4  1 Y 1 A ALA 217 ? A ALA 217 
5  1 Y 1 A ASN 218 ? A ASN 218 
6  1 Y 1 A HIS 219 ? A HIS 219 
7  1 Y 1 A LYS 220 ? A LYS 220 
8  1 Y 1 B MET 1   ? B MET 1   
9  1 Y 1 B LYS 215 ? B LYS 215 
10 1 Y 1 B HIS 216 ? B HIS 216 
11 1 Y 1 B ALA 217 ? B ALA 217 
12 1 Y 1 B ASN 218 ? B ASN 218 
13 1 Y 1 B HIS 219 ? B HIS 219 
14 1 Y 1 B LYS 220 ? B LYS 220 
15 1 Y 1 C LEU 214 ? C LEU 214 
16 1 Y 1 C LYS 215 ? C LYS 215 
17 1 Y 1 C HIS 216 ? C HIS 216 
18 1 Y 1 C ALA 217 ? C ALA 217 
19 1 Y 1 C ASN 218 ? C ASN 218 
20 1 Y 1 C HIS 219 ? C HIS 219 
21 1 Y 1 C LYS 220 ? C LYS 220 
22 1 Y 1 D MET 1   ? D MET 1   
23 1 Y 1 D LYS 215 ? D LYS 215 
24 1 Y 1 D HIS 216 ? D HIS 216 
25 1 Y 1 D ALA 217 ? D ALA 217 
26 1 Y 1 D ASN 218 ? D ASN 218 
27 1 Y 1 D HIS 219 ? D HIS 219 
28 1 Y 1 D LYS 220 ? D LYS 220 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
VAL N    N  N N 372 
VAL CA   C  N S 373 
VAL C    C  N N 374 
VAL O    O  N N 375 
VAL CB   C  N N 376 
VAL CG1  C  N N 377 
VAL CG2  C  N N 378 
VAL OXT  O  N N 379 
VAL H    H  N N 380 
VAL H2   H  N N 381 
VAL HA   H  N N 382 
VAL HB   H  N N 383 
VAL HG11 H  N N 384 
VAL HG12 H  N N 385 
VAL HG13 H  N N 386 
VAL HG21 H  N N 387 
VAL HG22 H  N N 388 
VAL HG23 H  N N 389 
VAL HXT  H  N N 390 
ZN  ZN   ZN N N 391 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)' 'United States' 
R01DK042303 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                                         'United States' 
F31CA265082 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1,2 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9EAT 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EBZ 
_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]   0.008832 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008393 
_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]   0.006211 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527  ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN  ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . LYS A 1 2   ? 11.87600  49.61300  80.76300  1.000 105.22878 ?  2   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 2   ? 13.18800  48.98200  80.78700  1.000 105.26658 ?  2   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 2   ? 13.53400  48.64000  82.23700  1.000 105.49935 ?  2   LYS A C   1 
ATOM   4    O  O   . LYS A 1 2   ? 13.58100  49.52600  83.08700  1.000 108.57867 ?  2   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 2   ? 14.22700  49.92300  80.16800  1.000 100.05809 ?  2   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 2   ? 13.99800  50.16500  78.67800  1.000 105.41799 ?  2   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 2   ? 15.02900  51.09800  78.06000  1.000 110.73871 ?  2   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 2   ? 14.70500  51.34900  76.59200  1.000 106.52370 ?  2   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 2   ? 15.68900  52.24900  75.93100  1.000 101.17049 ?  2   LYS A NZ  1 
ATOM   10   N  N   . ASP A 1 3   ? 13.80000  47.36300  82.52000  1.000 104.22744 ?  3   ASP A N   1 
ATOM   11   C  CA  . ASP A 1 3   ? 14.11400  46.92400  83.87600  1.000 101.77786 ?  3   ASP A CA  1 
ATOM   12   C  C   . ASP A 1 3   ? 15.54800  46.42800  84.00500  1.000 97.91185  ?  3   ASP A C   1 
ATOM   13   O  O   . ASP A 1 3   ? 15.86300  45.70100  84.95300  1.000 97.75010  ?  3   ASP A O   1 
ATOM   14   C  CB  . ASP A 1 3   ? 13.14500  45.83300  84.33700  1.000 101.15771 ?  3   ASP A CB  1 
ATOM   15   C  CG  . ASP A 1 3   ? 11.69200  46.23800  84.18400  1.000 106.61168 ?  3   ASP A CG  1 
ATOM   16   O  OD1 . ASP A 1 3   ? 11.39700  47.44600  84.28000  1.000 111.59517 ?  3   ASP A OD1 1 
ATOM   17   O  OD2 . ASP A 1 3   ? 10.84400  45.34500  83.96100  1.000 105.29037 -1 3   ASP A OD2 1 
ATOM   18   N  N   . ILE A 1 4   ? 16.41700  46.78800  83.05900  1.000 96.57714  ?  4   ILE A N   1 
ATOM   19   C  CA  . ILE A 1 4   ? 17.81000  46.35800  83.13300  1.000 98.41763  ?  4   ILE A CA  1 
ATOM   20   C  C   . ILE A 1 4   ? 18.44400  46.88100  84.41600  1.000 100.90925 ?  4   ILE A C   1 
ATOM   21   O  O   . ILE A 1 4   ? 19.14800  46.15400  85.12700  1.000 97.23282  ?  4   ILE A O   1 
ATOM   22   C  CB  . ILE A 1 4   ? 18.57800  46.82300  81.88300  1.000 91.61967  ?  4   ILE A CB  1 
ATOM   23   C  CG1 . ILE A 1 4   ? 18.14600  45.99500  80.67400  1.000 94.11032  ?  4   ILE A CG1 1 
ATOM   24   C  CG2 . ILE A 1 4   ? 20.07900  46.71900  82.09900  1.000 87.63161  ?  4   ILE A CG2 1 
ATOM   25   C  CD1 . ILE A 1 4   ? 18.44700  44.51700  80.80700  1.000 91.01420  ?  4   ILE A CD1 1 
ATOM   26   N  N   . ASP A 1 5   ? 18.19400  48.15600  84.73000  1.000 103.30706 ?  5   ASP A N   1 
ATOM   27   C  CA  . ASP A 1 5   ? 18.70900  48.74400  85.96200  1.000 103.29295 ?  5   ASP A CA  1 
ATOM   28   C  C   . ASP A 1 5   ? 18.20700  47.98800  87.18700  1.000 100.62503 ?  5   ASP A C   1 
ATOM   29   O  O   . ASP A 1 5   ? 18.94600  47.81300  88.16300  1.000 101.81653 ?  5   ASP A O   1 
ATOM   30   C  CB  . ASP A 1 5   ? 18.30800  50.21600  86.03300  1.000 105.33636 ?  5   ASP A CB  1 
ATOM   31   C  CG  . ASP A 1 5   ? 19.06100  51.07000  85.03100  1.000 112.68372 ?  5   ASP A CG  1 
ATOM   32   O  OD1 . ASP A 1 5   ? 20.08000  50.59500  84.48500  1.000 111.32737 ?  5   ASP A OD1 1 
ATOM   33   O  OD2 . ASP A 1 5   ? 18.63700  52.22200  84.79500  1.000 123.75603 -1 5   ASP A OD2 1 
ATOM   34   N  N   . THR A 1 6   ? 16.94600  47.54700  87.15900  1.000 95.02165  ?  6   THR A N   1 
ATOM   35   C  CA  . THR A 1 6   ? 16.42900  46.70500  88.23400  1.000 93.16682  ?  6   THR A CA  1 
ATOM   36   C  C   . THR A 1 6   ? 17.27700  45.44900  88.38900  1.000 95.90528  ?  6   THR A C   1 
ATOM   37   O  O   . THR A 1 6   ? 17.70400  45.10600  89.49700  1.000 99.39424  ?  6   THR A O   1 
ATOM   38   C  CB  . THR A 1 6   ? 14.96800  46.34000  87.96100  1.000 89.10818  ?  6   THR A CB  1 
ATOM   39   O  OG1 . THR A 1 6   ? 14.17800  47.53300  87.88600  1.000 88.88295  ?  6   THR A OG1 1 
ATOM   40   C  CG2 . THR A 1 6   ? 14.42300  45.44400  89.06400  1.000 94.09416  ?  6   THR A CG2 1 
ATOM   41   N  N   . LEU A 1 7   ? 17.52800  44.74900  87.28100  1.000 95.40902  ?  7   LEU A N   1 
ATOM   42   C  CA  . LEU A 1 7   ? 18.33500  43.53400  87.33000  1.000 94.65102  ?  7   LEU A CA  1 
ATOM   43   C  C   . LEU A 1 7   ? 19.76400  43.83900  87.76300  1.000 96.87277  ?  7   LEU A C   1 
ATOM   44   O  O   . LEU A 1 7   ? 20.38200  43.05200  88.48900  1.000 101.93391 ?  7   LEU A O   1 
ATOM   45   C  CB  . LEU A 1 7   ? 18.33700  42.83400  85.97100  1.000 95.47347  ?  7   LEU A CB  1 
ATOM   46   C  CG  . LEU A 1 7   ? 17.02700  42.68200  85.19500  1.000 93.76666  ?  7   LEU A CG  1 
ATOM   47   C  CD1 . LEU A 1 7   ? 17.22300  41.73200  84.02000  1.000 93.27149  ?  7   LEU A CD1 1 
ATOM   48   C  CD2 . LEU A 1 7   ? 15.89500  42.22000  86.09200  1.000 89.56660  ?  7   LEU A CD2 1 
ATOM   49   N  N   . ILE A 1 8   ? 20.31200  44.96900  87.30600  1.000 96.19889  ?  8   ILE A N   1 
ATOM   50   C  CA  . ILE A 1 8   ? 21.68600  45.33400  87.64800  1.000 99.11521  ?  8   ILE A CA  1 
ATOM   51   C  C   . ILE A 1 8   ? 21.84700  45.47900  89.15800  1.000 103.41162 ?  8   ILE A C   1 
ATOM   52   O  O   . ILE A 1 8   ? 22.77600  44.92300  89.75600  1.000 99.68064  ?  8   ILE A O   1 
ATOM   53   C  CB  . ILE A 1 8   ? 22.09100  46.62600  86.91500  1.000 100.58170 ?  8   ILE A CB  1 
ATOM   54   C  CG1 . ILE A 1 8   ? 22.27700  46.36200  85.42000  1.000 99.39844  ?  8   ILE A CG1 1 
ATOM   55   C  CG2 . ILE A 1 8   ? 23.36000  47.21000  87.51700  1.000 95.65797  ?  8   ILE A CG2 1 
ATOM   56   C  CD1 . ILE A 1 8   ? 23.32900  45.32400  85.10800  1.000 91.81563  ?  8   ILE A CD1 1 
ATOM   57   N  N   . SER A 1 9   ? 20.94400  46.22800  89.79500  1.000 103.24583 ?  9   SER A N   1 
ATOM   58   C  CA  . SER A 1 9   ? 21.03800  46.42200  91.24000  1.000 96.28311  ?  9   SER A CA  1 
ATOM   59   C  C   . SER A 1 9   ? 20.81700  45.11500  91.99100  1.000 100.04503 ?  9   SER A C   1 
ATOM   60   O  O   . SER A 1 9   ? 21.51800  44.83200  92.97000  1.000 102.53418 ?  9   SER A O   1 
ATOM   61   C  CB  . SER A 1 9   ? 20.04000  47.48100  91.70400  1.000 102.16108 ?  9   SER A CB  1 
ATOM   62   O  OG  . SER A 1 9   ? 18.72100  46.96800  91.72300  1.000 103.44703 ?  9   SER A OG  1 
ATOM   63   N  N   . ASN A 1 10  ? 19.83800  44.31300  91.55500  1.000 99.74382  ?  10  ASN A N   1 
ATOM   64   C  CA  . ASN A 1 10  ? 19.59200  43.02300  92.19400  1.000 98.71643  ?  10  ASN A CA  1 
ATOM   65   C  C   . ASN A 1 10  ? 20.85100  42.16900  92.23500  1.000 96.19686  ?  10  ASN A C   1 
ATOM   66   O  O   . ASN A 1 10  ? 21.09900  41.46800  93.22200  1.000 98.26330  ?  10  ASN A O   1 
ATOM   67   C  CB  . ASN A 1 10  ? 18.46600  42.27800  91.47400  1.000 90.38344  ?  10  ASN A CB  1 
ATOM   68   C  CG  . ASN A 1 10  ? 17.14200  43.01100  91.54300  1.000 92.13785  ?  10  ASN A CG  1 
ATOM   69   O  OD1 . ASN A 1 10  ? 17.00000  43.99300  92.27200  1.000 96.85001  ?  10  ASN A OD1 1 
ATOM   70   N  ND2 . ASN A 1 10  ? 16.16000  42.53300  90.78800  1.000 90.24308  ?  10  ASN A ND2 1 
ATOM   71   N  N   . ASN A 1 11  ? 21.65800  42.24400  91.20100  1.000 96.23128  ?  11  ASN A N   1 
ATOM   72   C  CA  . ASN A 1 11  ? 22.85900  41.47600  91.22700  1.000 96.18454  ?  11  ASN A CA  1 
ATOM   73   C  C   . ASN A 1 11  ? 23.73900  42.03200  92.31900  1.000 92.19415  ?  11  ASN A C   1 
ATOM   74   O  O   . ASN A 1 11  ? 24.10300  41.32700  93.24800  1.000 93.67016  ?  11  ASN A O   1 
ATOM   75   C  CB  . ASN A 1 11  ? 23.56100  41.54300  89.88500  1.000 88.27472  ?  11  ASN A CB  1 
ATOM   76   C  CG  . ASN A 1 11  ? 24.88700  40.82600  89.89800  1.000 87.28204  ?  11  ASN A CG  1 
ATOM   77   O  OD1 . ASN A 1 11  ? 25.93800  41.45400  89.90100  1.000 88.48381  ?  11  ASN A OD1 1 
ATOM   78   N  ND2 . ASN A 1 11  ? 24.84400  39.50300  89.92300  1.000 83.47911  ?  11  ASN A ND2 1 
ATOM   79   N  N   . ALA A 1 12  ? 24.07600  43.30700  92.21700  1.000 95.35076  ?  12  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 12  ? 24.98100  43.91000  93.19000  1.000 95.60248  ?  12  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 12  ? 24.48200  43.67200  94.60800  1.000 99.70344  ?  12  ALA A C   1 
ATOM   82   O  O   . ALA A 1 12  ? 25.26700  43.35100  95.50800  1.000 101.51299 ?  12  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 12  ? 25.13500  45.40500  92.91500  1.000 96.41599  ?  12  ALA A CB  1 
ATOM   84   N  N   . LEU A 1 13  ? 23.17700  43.84200  94.82400  1.000 97.17993  ?  13  LEU A N   1 
ATOM   85   C  CA  . LEU A 1 13  ? 22.57900  43.54900  96.12000  1.000 96.82668  ?  13  LEU A CA  1 
ATOM   86   C  C   . LEU A 1 13  ? 22.81600  42.09100  96.50300  1.000 99.82123  ?  13  LEU A C   1 
ATOM   87   O  O   . LEU A 1 13  ? 23.43500  41.79600  97.53000  1.000 104.36718 ?  13  LEU A O   1 
ATOM   88   C  CB  . LEU A 1 13  ? 21.08300  43.86900  96.06700  1.000 94.91875  ?  13  LEU A CB  1 
ATOM   89   C  CG  . LEU A 1 13  ? 20.28000  44.00500  97.35800  1.000 99.28170  ?  13  LEU A CG  1 
ATOM   90   C  CD1 . LEU A 1 13  ? 20.87500  45.10000  98.22400  1.000 108.06233 ?  13  LEU A CD1 1 
ATOM   91   C  CD2 . LEU A 1 13  ? 18.82500  44.30900  97.03300  1.000 96.69615  ?  13  LEU A CD2 1 
ATOM   92   N  N   . TRP A 1 14  ? 22.32800  41.16600  95.66900  1.000 96.48558  ?  14  TRP A N   1 
ATOM   93   C  CA  . TRP A 1 14  ? 22.53600  39.73400  95.88500  1.000 97.19380  ?  14  TRP A CA  1 
ATOM   94   C  C   . TRP A 1 14  ? 24.00900  39.39300  96.09700  1.000 96.45506  ?  14  TRP A C   1 
ATOM   95   O  O   . TRP A 1 14  ? 24.33900  38.50400  96.89000  1.000 97.81047  ?  14  TRP A O   1 
ATOM   96   C  CB  . TRP A 1 14  ? 21.95900  38.95400  94.70100  1.000 96.34485  ?  14  TRP A CB  1 
ATOM   97   C  CG  . TRP A 1 14  ? 22.30700  37.49700  94.63300  1.000 94.24353  ?  14  TRP A CG  1 
ATOM   98   C  CD1 . TRP A 1 14  ? 21.63500  36.46700  95.22100  1.000 99.17776  ?  14  TRP A CD1 1 
ATOM   99   C  CD2 . TRP A 1 14  ? 23.39000  36.90500  93.90400  1.000 93.05750  ?  14  TRP A CD2 1 
ATOM   100  N  NE1 . TRP A 1 14  ? 22.23900  35.27100  94.91600  1.000 97.45202  ?  14  TRP A NE1 1 
ATOM   101  C  CE2 . TRP A 1 14  ? 23.31900  35.51300  94.10800  1.000 94.05901  ?  14  TRP A CE2 1 
ATOM   102  C  CE3 . TRP A 1 14  ? 24.41700  37.41700  93.10500  1.000 98.65807  ?  14  TRP A CE3 1 
ATOM   103  C  CZ2 . TRP A 1 14  ? 24.23500  34.62800  93.54400  1.000 96.39560  ?  14  TRP A CZ2 1 
ATOM   104  C  CZ3 . TRP A 1 14  ? 25.32600  36.53600  92.54700  1.000 99.93803  ?  14  TRP A CZ3 1 
ATOM   105  C  CH2 . TRP A 1 14  ? 25.23000  35.15800  92.77000  1.000 98.69119  ?  14  TRP A CH2 1 
ATOM   106  N  N   . SER A 1 15  ? 24.91000  40.08400  95.39100  1.000 93.05462  ?  15  SER A N   1 
ATOM   107  C  CA  . SER A 1 15  ? 26.33500  39.78600  95.52000  1.000 92.53734  ?  15  SER A CA  1 
ATOM   108  C  C   . SER A 1 15  ? 26.84300  40.11400  96.91900  1.000 102.13096 ?  15  SER A C   1 
ATOM   109  O  O   . SER A 1 15  ? 27.44400  39.26200  97.58300  1.000 103.33961 ?  15  SER A O   1 
ATOM   110  C  CB  . SER A 1 15  ? 27.13600  40.54800  94.46500  1.000 92.75294  ?  15  SER A CB  1 
ATOM   111  O  OG  . SER A 1 15  ? 28.46100  40.05000  94.38100  1.000 90.87850  ?  15  SER A OG  1 
ATOM   112  N  N   . LYS A 1 16  ? 26.61300  41.34400  97.38700  1.000 102.56552 ?  16  LYS A N   1 
ATOM   113  C  CA  . LYS A 1 16  ? 27.05700  41.70800  98.73000  1.000 101.79681 ?  16  LYS A CA  1 
ATOM   114  C  C   . LYS A 1 16  ? 26.36600  40.85800  99.78700  1.000 107.39470 ?  16  LYS A C   1 
ATOM   115  O  O   . LYS A 1 16  ? 27.01000  40.38900  100.73400 1.000 104.36048 ?  16  LYS A O   1 
ATOM   116  C  CB  . LYS A 1 16  ? 26.83500  43.19700  99.00400  1.000 99.89205  ?  16  LYS A CB  1 
ATOM   117  C  CG  . LYS A 1 16  ? 27.74800  44.13500  98.22800  1.000 107.31413 ?  16  LYS A CG  1 
ATOM   118  C  CD  . LYS A 1 16  ? 27.28300  45.57700  98.34800  1.000 116.59075 ?  16  LYS A CD  1 
ATOM   119  C  CE  . LYS A 1 16  ? 28.11000  46.50500  97.47600  1.000 115.27419 ?  16  LYS A CE  1 
ATOM   120  N  NZ  . LYS A 1 16  ? 29.55900  46.43500  97.82000  1.000 113.97354 ?  16  LYS A NZ  1 
ATOM   121  N  N   . MET A 1 17  ? 25.04500  40.68700  99.66700  1.000 110.80817 ?  17  MET A N   1 
ATOM   122  C  CA  . MET A 1 17  ? 24.30000  39.85500  100.60800 1.000 104.68426 ?  17  MET A CA  1 
ATOM   123  C  C   . MET A 1 17  ? 25.00500  38.53100  100.87600 1.000 104.26851 ?  17  MET A C   1 
ATOM   124  O  O   . MET A 1 17  ? 25.24800  38.16300  102.02800 1.000 113.36712 ?  17  MET A O   1 
ATOM   125  C  CB  . MET A 1 17  ? 22.89400  39.58700  100.06100 1.000 109.53352 ?  17  MET A CB  1 
ATOM   126  C  CG  . MET A 1 17  ? 21.97400  40.79100  100.01300 1.000 109.05742 ?  17  MET A CG  1 
ATOM   127  S  SD  . MET A 1 17  ? 21.70000  41.56200  101.61400 1.000 130.99404 ?  17  MET A SD  1 
ATOM   128  C  CE  . MET A 1 17  ? 20.68700  42.95800  101.13500 1.000 117.07876 ?  17  MET A CE  1 
ATOM   129  N  N   . LEU A 1 18  ? 25.35100  37.80600  99.81100  1.000 105.09419 ?  18  LEU A N   1 
ATOM   130  C  CA  . LEU A 1 18  ? 26.05100  36.53600  99.97200  1.000 104.71332 ?  18  LEU A CA  1 
ATOM   131  C  C   . LEU A 1 18  ? 27.46300  36.72300  100.52300 1.000 104.07807 ?  18  LEU A C   1 
ATOM   132  O  O   . LEU A 1 18  ? 27.85000  36.04600  101.48000 1.000 109.96677 ?  18  LEU A O   1 
ATOM   133  C  CB  . LEU A 1 18  ? 26.07100  35.77700  98.65000  1.000 108.20382 ?  18  LEU A CB  1 
ATOM   134  C  CG  . LEU A 1 18  ? 24.79200  34.99500  98.35200  1.000 106.70951 ?  18  LEU A CG  1 
ATOM   135  C  CD1 . LEU A 1 18  ? 24.83000  34.43600  96.95400  1.000 105.51667 ?  18  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A 1 18  ? 24.62400  33.87100  99.36100  1.000 107.58340 ?  18  LEU A CD2 1 
ATOM   137  N  N   . VAL A 1 19  ? 28.24500  37.64700  99.94800  1.000 104.87098 ?  19  VAL A N   1 
ATOM   138  C  CA  . VAL A 1 19  ? 29.60900  37.87200  100.43500 1.000 107.55412 ?  19  VAL A CA  1 
ATOM   139  C  C   . VAL A 1 19  ? 29.60900  38.16100  101.93000 1.000 108.35048 ?  19  VAL A C   1 
ATOM   140  O  O   . VAL A 1 19  ? 30.43200  37.62800  102.68500 1.000 110.46121 ?  19  VAL A O   1 
ATOM   141  C  CB  . VAL A 1 19  ? 30.28400  39.01600  99.65100  1.000 106.77932 ?  19  VAL A CB  1 
ATOM   142  C  CG1 . VAL A 1 19  ? 31.64700  39.33000  100.24600 1.000 104.68229 ?  19  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A 1 19  ? 30.43700  38.65700  98.19000  1.000 99.90407  ?  19  VAL A CG2 1 
ATOM   144  N  N   . GLU A 1 20  ? 28.68700  39.00900  102.37900 1.000 110.46749 ?  20  GLU A N   1 
ATOM   145  C  CA  . GLU A 1 20  ? 28.57900  39.32300  103.79900 1.000 108.56298 ?  20  GLU A CA  1 
ATOM   146  C  C   . GLU A 1 20  ? 28.12900  38.10600  104.60600 1.000 108.00992 ?  20  GLU A C   1 
ATOM   147  O  O   . GLU A 1 20  ? 28.70700  37.79500  105.65500 1.000 107.06687 ?  20  GLU A O   1 
ATOM   148  C  CB  . GLU A 1 20  ? 27.63000  40.51100  103.97200 1.000 106.08680 ?  20  GLU A CB  1 
ATOM   149  C  CG  . GLU A 1 20  ? 27.42200  41.00100  105.38700 1.000 117.30303 ?  20  GLU A CG  1 
ATOM   150  C  CD  . GLU A 1 20  ? 26.45000  42.16600  105.43300 1.000 120.89938 ?  20  GLU A CD  1 
ATOM   151  O  OE1 . GLU A 1 20  ? 25.87300  42.49600  104.37300 1.000 113.68990 ?  20  GLU A OE1 1 
ATOM   152  O  OE2 . GLU A 1 20  ? 26.27200  42.75900  106.51700 1.000 122.32343 -1 20  GLU A OE2 1 
ATOM   153  N  N   . GLU A 1 21  ? 27.09600  37.40700  104.13300 1.000 105.71395 ?  21  GLU A N   1 
ATOM   154  C  CA  . GLU A 1 21  ? 26.48300  36.29400  104.85900 1.000 110.15371 ?  21  GLU A CA  1 
ATOM   155  C  C   . GLU A 1 21  ? 27.18400  34.95600  104.62100 1.000 109.64863 ?  21  GLU A C   1 
ATOM   156  O  O   . GLU A 1 21  ? 27.65100  34.31500  105.56800 1.000 117.46836 ?  21  GLU A O   1 
ATOM   157  C  CB  . GLU A 1 21  ? 25.00100  36.19800  104.48200 1.000 111.61035 ?  21  GLU A CB  1 
ATOM   158  C  CG  . GLU A 1 21  ? 24.18400  37.39000  104.94100 1.000 115.01591 ?  21  GLU A CG  1 
ATOM   159  C  CD  . GLU A 1 21  ? 22.86600  37.51300  104.20800 1.000 124.28901 ?  21  GLU A CD  1 
ATOM   160  O  OE1 . GLU A 1 21  ? 22.62900  36.72700  103.26600 1.000 123.08902 ?  21  GLU A OE1 1 
ATOM   161  O  OE2 . GLU A 1 21  ? 22.06000  38.39000  104.58200 1.000 131.72094 -1 21  GLU A OE2 1 
ATOM   162  N  N   . ASP A 1 22  ? 27.26000  34.52100  103.36400 1.000 109.91298 ?  22  ASP A N   1 
ATOM   163  C  CA  . ASP A 1 22  ? 27.85600  33.23400  103.00400 1.000 113.00143 ?  22  ASP A CA  1 
ATOM   164  C  C   . ASP A 1 22  ? 28.93800  33.48800  101.96500 1.000 112.25337 ?  22  ASP A C   1 
ATOM   165  O  O   . ASP A 1 22  ? 28.67600  33.45600  100.75300 1.000 111.07905 ?  22  ASP A O   1 
ATOM   166  C  CB  . ASP A 1 22  ? 26.79200  32.26900  102.47600 1.000 112.64299 ?  22  ASP A CB  1 
ATOM   167  C  CG  . ASP A 1 22  ? 27.36500  30.92400  102.05100 1.000 114.05247 ?  22  ASP A CG  1 
ATOM   168  O  OD1 . ASP A 1 22  ? 28.51500  30.60400  102.42100 1.000 113.95258 ?  22  ASP A OD1 1 
ATOM   169  O  OD2 . ASP A 1 22  ? 26.65600  30.18200  101.33500 1.000 113.38786 -1 22  ASP A OD2 1 
ATOM   170  N  N   . PRO A 1 23  ? 30.17700  33.73200  102.40300 1.000 111.84862 ?  23  PRO A N   1 
ATOM   171  C  CA  . PRO A 1 23  ? 31.27000  33.93200  101.44500 1.000 108.86229 ?  23  PRO A CA  1 
ATOM   172  C  C   . PRO A 1 23  ? 31.74000  32.65100  100.79700 1.000 110.97230 ?  23  PRO A C   1 
ATOM   173  O  O   . PRO A 1 23  ? 32.53700  32.71300  99.85400  1.000 113.78918 ?  23  PRO A O   1 
ATOM   174  C  CB  . PRO A 1 23  ? 32.38000  34.54500  102.30500 1.000 110.84632 ?  23  PRO A CB  1 
ATOM   175  C  CG  . PRO A 1 23  ? 32.14300  33.99100  103.66600 1.000 108.08886 ?  23  PRO A CG  1 
ATOM   176  C  CD  . PRO A 1 23  ? 30.65400  33.73600  103.79700 1.000 110.41456 ?  23  PRO A CD  1 
ATOM   177  N  N   . GLY A 1 24  ? 31.25900  31.49600  101.25300 1.000 108.59579 ?  24  GLY A N   1 
ATOM   178  C  CA  . GLY A 1 24  ? 31.66000  30.26600  100.61200 1.000 109.83362 ?  24  GLY A CA  1 
ATOM   179  C  C   . GLY A 1 24  ? 30.84200  29.92100  99.39400  1.000 113.66977 ?  24  GLY A C   1 
ATOM   180  O  O   . GLY A 1 24  ? 31.26900  29.07400  98.60500  1.000 116.65415 ?  24  GLY A O   1 
ATOM   181  N  N   . PHE A 1 25  ? 29.66900  30.54200  99.23100  1.000 112.41832 ?  25  PHE A N   1 
ATOM   182  C  CA  . PHE A 1 25  ? 28.87000  30.29600  98.03600  1.000 110.95891 ?  25  PHE A CA  1 
ATOM   183  C  C   . PHE A 1 25  ? 29.72500  30.52000  96.79900  1.000 108.03405 ?  25  PHE A C   1 
ATOM   184  O  O   . PHE A 1 25  ? 29.78500  29.67700  95.89900  1.000 107.39703 ?  25  PHE A O   1 
ATOM   185  C  CB  . PHE A 1 25  ? 27.64800  31.21500  98.01400  1.000 108.83104 ?  25  PHE A CB  1 
ATOM   186  C  CG  . PHE A 1 25  ? 26.92000  31.22500  96.69800  1.000 107.44059 ?  25  PHE A CG  1 
ATOM   187  C  CD1 . PHE A 1 25  ? 26.05000  30.19600  96.37400  1.000 107.55347 ?  25  PHE A CD1 1 
ATOM   188  C  CD2 . PHE A 1 25  ? 27.12700  32.23600  95.77400  1.000 109.94859 ?  25  PHE A CD2 1 
ATOM   189  C  CE1 . PHE A 1 25  ? 25.37600  30.19000  95.16700  1.000 107.18130 ?  25  PHE A CE1 1 
ATOM   190  C  CE2 . PHE A 1 25  ? 26.45900  32.23300  94.56200  1.000 107.49396 ?  25  PHE A CE2 1 
ATOM   191  C  CZ  . PHE A 1 25  ? 25.58200  31.20900  94.25900  1.000 103.38603 ?  25  PHE A CZ  1 
ATOM   192  N  N   . PHE A 1 26  ? 30.42000  31.65500  96.76200  1.000 107.23116 ?  26  PHE A N   1 
ATOM   193  C  CA  . PHE A 1 26  ? 31.34300  31.94800  95.67900  1.000 108.59059 ?  26  PHE A CA  1 
ATOM   194  C  C   . PHE A 1 26  ? 32.58600  31.07500  95.74600  1.000 110.25473 ?  26  PHE A C   1 
ATOM   195  O  O   . PHE A 1 26  ? 33.24900  30.88500  94.72200  1.000 112.33697 ?  26  PHE A O   1 
ATOM   196  C  CB  . PHE A 1 26  ? 31.70400  33.42800  95.71900  1.000 99.34074  ?  26  PHE A CB  1 
ATOM   197  C  CG  . PHE A 1 26  ? 30.50600  34.31700  95.81600  1.000 99.72012  ?  26  PHE A CG  1 
ATOM   198  C  CD1 . PHE A 1 26  ? 29.65800  34.47500  94.73500  1.000 102.14782 ?  26  PHE A CD1 1 
ATOM   199  C  CD2 . PHE A 1 26  ? 30.20600  34.96700  96.99700  1.000 103.19633 ?  26  PHE A CD2 1 
ATOM   200  C  CE1 . PHE A 1 26  ? 28.54000  35.27600  94.82800  1.000 103.10191 ?  26  PHE A CE1 1 
ATOM   201  C  CE2 . PHE A 1 26  ? 29.09400  35.77000  97.09200  1.000 102.32584 ?  26  PHE A CE2 1 
ATOM   202  C  CZ  . PHE A 1 26  ? 28.26200  35.92900  96.00600  1.000 101.03564 ?  26  PHE A CZ  1 
ATOM   203  N  N   . GLU A 1 27  ? 32.92400  30.55400  96.92800  1.000 105.69214 ?  27  GLU A N   1 
ATOM   204  C  CA  . GLU A 1 27  ? 34.04500  29.62600  97.02800  1.000 110.00191 ?  27  GLU A CA  1 
ATOM   205  C  C   . GLU A 1 27  ? 33.70400  28.27500  96.40800  1.000 108.82959 ?  27  GLU A C   1 
ATOM   206  O  O   . GLU A 1 27  ? 34.54000  27.67500  95.72500  1.000 110.61962 ?  27  GLU A O   1 
ATOM   207  C  CB  . GLU A 1 27  ? 34.46500  29.45800  98.49000  1.000 119.63656 ?  27  GLU A CB  1 
ATOM   208  C  CG  . GLU A 1 27  ? 35.02600  30.72000  99.15000  1.000 122.61701 ?  27  GLU A CG  1 
ATOM   209  C  CD  . GLU A 1 27  ? 36.23800  31.28800  98.43100  1.000 133.48428 ?  27  GLU A CD  1 
ATOM   210  O  OE1 . GLU A 1 27  ? 37.09600  30.49900  97.98100  1.000 133.32246 ?  27  GLU A OE1 1 
ATOM   211  O  OE2 . GLU A 1 27  ? 36.32700  32.52900  98.30600  1.000 140.68907 -1 27  GLU A OE2 1 
ATOM   212  N  N   . LYS A 1 28  ? 32.48500  27.77700  96.64300  1.000 107.02968 ?  28  LYS A N   1 
ATOM   213  C  CA  . LYS A 1 28  ? 32.05800  26.51900  96.03200  1.000 111.12214 ?  28  LYS A CA  1 
ATOM   214  C  C   . LYS A 1 28  ? 32.02800  26.63900  94.52100  1.000 109.75354 ?  28  LYS A C   1 
ATOM   215  O  O   . LYS A 1 28  ? 32.54600  25.78200  93.79800  1.000 107.56728 ?  28  LYS A O   1 
ATOM   216  C  CB  . LYS A 1 28  ? 30.65400  26.17600  96.50100  1.000 109.93229 ?  28  LYS A CB  1 
ATOM   217  C  CG  . LYS A 1 28  ? 30.48100  26.23800  97.95700  1.000 113.54234 ?  28  LYS A CG  1 
ATOM   218  C  CD  . LYS A 1 28  ? 29.09500  26.77600  98.19400  1.000 114.03714 ?  28  LYS A CD  1 
ATOM   219  C  CE  . LYS A 1 28  ? 28.86800  27.01700  99.64200  1.000 111.82304 ?  28  LYS A CE  1 
ATOM   220  N  NZ  . LYS A 1 28  ? 30.15000  27.34000  100.32900 1.000 114.16147 ?  28  LYS A NZ  1 
ATOM   221  N  N   . LEU A 1 29  ? 31.38500  27.69900  94.03000  1.000 108.15845 ?  29  LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? 31.31100  27.94700  92.59800  1.000 104.94320 ?  29  LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? 32.70100  28.13500  92.00800  1.000 107.49060 ?  29  LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? 32.94200  27.76500  90.85200  1.000 114.51350 ?  29  LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? 30.40800  29.15400  92.34200  1.000 102.04519 ?  29  LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? 28.89900  28.84500  92.30500  1.000 104.16873 ?  29  LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? 28.36900  28.17400  93.57600  1.000 105.98696 ?  29  LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? 28.10900  30.10000  92.04000  1.000 100.74210 ?  29  LEU A CD2 1 
ATOM   229  N  N   . ALA A 1 30  ? 33.62400  28.70800  92.78400  1.000 108.14047 ?  30  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 30  ? 35.01700  28.83500  92.36700  1.000 109.11861 ?  30  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 30  ? 35.72000  27.48700  92.29200  1.000 104.99389 ?  30  ALA A C   1 
ATOM   232  O  O   . ALA A 1 30  ? 36.72900  27.36000  91.58900  1.000 108.87824 ?  30  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 30  ? 35.77300  29.75500  93.32700  1.000 111.36827 ?  30  ALA A CB  1 
ATOM   234  N  N   . GLN A 1 31  ? 35.20500  26.48400  92.99400  1.000 103.69282 ?  31  GLN A N   1 
ATOM   235  C  CA  . GLN A 1 31  ? 35.80200  25.15800  92.98200  1.000 106.15721 ?  31  GLN A CA  1 
ATOM   236  C  C   . GLN A 1 31  ? 35.56600  24.50600  91.62700  1.000 113.69392 ?  31  GLN A C   1 
ATOM   237  O  O   . GLN A 1 31  ? 34.46700  24.57900  91.07000  1.000 114.49641 ?  31  GLN A O   1 
ATOM   238  C  CB  . GLN A 1 31  ? 35.18600  24.31500  94.09400  1.000 107.06682 ?  31  GLN A CB  1 
ATOM   239  C  CG  . GLN A 1 31  ? 35.55400  24.79600  95.48300  1.000 108.06735 ?  31  GLN A CG  1 
ATOM   240  C  CD  . GLN A 1 31  ? 34.65200  24.22400  96.55900  1.000 111.14521 ?  31  GLN A CD  1 
ATOM   241  O  OE1 . GLN A 1 31  ? 33.82000  23.35800  96.29300  1.000 108.31997 ?  31  GLN A OE1 1 
ATOM   242  N  NE2 . GLN A 1 31  ? 34.79600  24.73000  97.78000  1.000 119.78375 ?  31  GLN A NE2 1 
ATOM   243  N  N   . ALA A 1 32  ? 36.60400  23.85900  91.09900  1.000 113.87083 ?  32  ALA A N   1 
ATOM   244  C  CA  . ALA A 1 32  ? 36.52900  23.23800  89.77900  1.000 107.21443 ?  32  ALA A CA  1 
ATOM   245  C  C   . ALA A 1 32  ? 35.71700  21.95100  89.87300  1.000 108.44299 ?  32  ALA A C   1 
ATOM   246  O  O   . ALA A 1 32  ? 36.24200  20.84000  89.96900  1.000 107.89871 ?  32  ALA A O   1 
ATOM   247  C  CB  . ALA A 1 32  ? 37.92700  22.98100  89.23000  1.000 108.68931 ?  32  ALA A CB  1 
ATOM   248  N  N   . GLN A 1 33  ? 34.39500  22.12500  89.86700  1.000 108.49583 ?  33  GLN A N   1 
ATOM   249  C  CA  . GLN A 1 33  ? 33.42100  21.03800  89.90500  1.000 105.25787 ?  33  GLN A CA  1 
ATOM   250  C  C   . GLN A 1 33  ? 32.91300  20.81200  88.49000  1.000 90.17959  ?  33  GLN A C   1 
ATOM   251  O  O   . GLN A 1 33  ? 32.02800  21.53000  88.01500  1.000 83.58680  ?  33  GLN A O   1 
ATOM   252  C  CB  . GLN A 1 33  ? 32.27500  21.36500  90.85800  1.000 101.56684 ?  33  GLN A CB  1 
ATOM   253  C  CG  . GLN A 1 33  ? 32.63400  21.35500  92.33000  1.000 103.24623 ?  33  GLN A CG  1 
ATOM   254  C  CD  . GLN A 1 33  ? 32.96500  19.95200  92.81900  1.000 111.98863 ?  33  GLN A CD  1 
ATOM   255  O  OE1 . GLN A 1 33  ? 34.12700  19.60200  93.02500  1.000 116.51328 ?  33  GLN A OE1 1 
ATOM   256  N  NE2 . GLN A 1 33  ? 31.92700  19.14000  93.01500  1.000 109.38281 ?  33  GLN A NE2 1 
ATOM   257  N  N   . LYS A 1 34  ? 33.46300  19.81000  87.82100  1.000 83.71242  ?  34  LYS A N   1 
ATOM   258  C  CA  . LYS A 1 34  ? 32.96100  19.47100  86.50200  1.000 91.61697  ?  34  LYS A CA  1 
ATOM   259  C  C   . LYS A 1 34  ? 31.58400  18.84400  86.66000  1.000 85.64684  ?  34  LYS A C   1 
ATOM   260  O  O   . LYS A 1 34  ? 31.40900  17.94900  87.49500  1.000 79.57566  ?  34  LYS A O   1 
ATOM   261  C  CB  . LYS A 1 34  ? 33.90300  18.51600  85.76900  1.000 85.47797  ?  34  LYS A CB  1 
ATOM   262  C  CG  . LYS A 1 34  ? 35.17500  19.17100  85.25100  1.000 82.76721  ?  34  LYS A CG  1 
ATOM   263  C  CD  . LYS A 1 34  ? 36.05700  18.18200  84.50100  1.000 81.45197  ?  34  LYS A CD  1 
ATOM   264  C  CE  . LYS A 1 34  ? 36.40700  16.97600  85.35500  1.000 95.80285  ?  34  LYS A CE  1 
ATOM   265  N  NZ  . LYS A 1 34  ? 37.34300  16.05500  84.64900  1.000 84.76117  ?  34  LYS A NZ  1 
ATOM   266  N  N   . PRO A 1 35  ? 30.58600  19.30300  85.91000  1.000 82.79243  ?  35  PRO A N   1 
ATOM   267  C  CA  . PRO A 1 35  ? 29.23500  18.76000  86.06200  1.000 80.96283  ?  35  PRO A CA  1 
ATOM   268  C  C   . PRO A 1 35  ? 29.17800  17.27600  85.73600  1.000 76.05931  ?  35  PRO A C   1 
ATOM   269  O  O   . PRO A 1 35  ? 30.02400  16.72200  85.02900  1.000 68.90040  ?  35  PRO A O   1 
ATOM   270  C  CB  . PRO A 1 35  ? 28.40300  19.58300  85.06900  1.000 81.58517  ?  35  PRO A CB  1 
ATOM   271  C  CG  . PRO A 1 35  ? 29.39100  20.16200  84.11900  1.000 77.86766  ?  35  PRO A CG  1 
ATOM   272  C  CD  . PRO A 1 35  ? 30.64100  20.38200  84.91100  1.000 79.05784  ?  35  PRO A CD  1 
ATOM   273  N  N   . ARG A 1 36  ? 28.16600  16.62800  86.30200  1.000 75.89825  ?  36  ARG A N   1 
ATOM   274  C  CA  . ARG A 1 36  ? 27.88100  15.22900  86.04500  1.000 74.61016  ?  36  ARG A CA  1 
ATOM   275  C  C   . ARG A 1 36  ? 26.60600  15.05000  85.24300  1.000 68.58482  ?  36  ARG A C   1 
ATOM   276  O  O   . ARG A 1 36  ? 26.31700  13.92900  84.81000  1.000 66.48550  ?  36  ARG A O   1 
ATOM   277  C  CB  . ARG A 1 36  ? 27.75200  14.46100  87.36900  1.000 77.72218  ?  36  ARG A CB  1 
ATOM   278  C  CG  . ARG A 1 36  ? 29.03600  14.39000  88.17500  1.000 76.05584  ?  36  ARG A CG  1 
ATOM   279  C  CD  . ARG A 1 36  ? 28.85000  13.67100  89.51300  1.000 93.48316  ?  36  ARG A CD  1 
ATOM   280  N  NE  . ARG A 1 36  ? 27.48500  13.20300  89.73500  1.000 95.04869  ?  36  ARG A NE  1 
ATOM   281  C  CZ  . ARG A 1 36  ? 27.02700  11.99200  89.44100  1.000 89.21500  ?  36  ARG A CZ  1 
ATOM   282  N  NH1 . ARG A 1 36  ? 27.80300  11.06500  88.90300  1.000 84.69060  ?  36  ARG A NH1 1 
ATOM   283  N  NH2 . ARG A 1 36  ? 25.75000  11.70700  89.68200  1.000 83.93026  ?  36  ARG A NH2 1 
ATOM   284  N  N   . PHE A 1 37  ? 25.85100  16.12300  85.02500  1.000 66.50273  ?  37  PHE A N   1 
ATOM   285  C  CA  . PHE A 1 37  ? 24.58400  16.07500  84.31900  1.000 65.51481  ?  37  PHE A CA  1 
ATOM   286  C  C   . PHE A 1 37  ? 24.59400  17.09300  83.19100  1.000 75.41136  ?  37  PHE A C   1 
ATOM   287  O  O   . PHE A 1 37  ? 25.10500  18.20600  83.35200  1.000 77.60803  ?  37  PHE A O   1 
ATOM   288  C  CB  . PHE A 1 37  ? 23.42300  16.36500  85.27400  1.000 68.17700  ?  37  PHE A CB  1 
ATOM   289  C  CG  . PHE A 1 37  ? 23.31100  15.38700  86.40800  1.000 74.96792  ?  37  PHE A CG  1 
ATOM   290  C  CD1 . PHE A 1 37  ? 24.06600  15.55100  87.55900  1.000 76.68309  ?  37  PHE A CD1 1 
ATOM   291  C  CD2 . PHE A 1 37  ? 22.44900  14.30800  86.32800  1.000 74.27883  ?  37  PHE A CD2 1 
ATOM   292  C  CE1 . PHE A 1 37  ? 23.96800  14.65400  88.60400  1.000 74.12513  ?  37  PHE A CE1 1 
ATOM   293  C  CE2 . PHE A 1 37  ? 22.34600  13.40800  87.37100  1.000 74.76571  ?  37  PHE A CE2 1 
ATOM   294  C  CZ  . PHE A 1 37  ? 23.10600  13.58200  88.51100  1.000 73.26771  ?  37  PHE A CZ  1 
ATOM   295  N  N   . LEU A 1 38  ? 24.00900  16.71400  82.06000  1.000 71.20807  ?  38  LEU A N   1 
ATOM   296  C  CA  . LEU A 1 38  ? 23.73200  17.62700  80.96100  1.000 56.49666  ?  38  LEU A CA  1 
ATOM   297  C  C   . LEU A 1 38  ? 22.22400  17.76900  80.83500  1.000 56.30490  ?  38  LEU A C   1 
ATOM   298  O  O   . LEU A 1 38  ? 21.50900  16.76700  80.73700  1.000 58.18846  ?  38  LEU A O   1 
ATOM   299  C  CB  . LEU A 1 38  ? 24.32700  17.12200  79.64400  1.000 67.23504  ?  38  LEU A CB  1 
ATOM   300  C  CG  . LEU A 1 38  ? 23.91700  17.89100  78.38000  1.000 65.84184  ?  38  LEU A CG  1 
ATOM   301  C  CD1 . LEU A 1 38  ? 24.33000  19.35500  78.45100  1.000 61.63325  ?  38  LEU A CD1 1 
ATOM   302  C  CD2 . LEU A 1 38  ? 24.47000  17.23400  77.12100  1.000 60.83433  ?  38  LEU A CD2 1 
ATOM   303  N  N   . TRP A 1 39  ? 21.74500  19.00600  80.86300  1.000 58.81898  ?  39  TRP A N   1 
ATOM   304  C  CA  . TRP A 1 39  ? 20.32400  19.29900  80.75000  1.000 62.40891  ?  39  TRP A CA  1 
ATOM   305  C  C   . TRP A 1 39  ? 20.04900  19.89700  79.37700  1.000 63.98896  ?  39  TRP A C   1 
ATOM   306  O  O   . TRP A 1 39  ? 20.55800  20.97600  79.05400  1.000 61.44161  ?  39  TRP A O   1 
ATOM   307  C  CB  . TRP A 1 39  ? 19.87300  20.25700  81.85300  1.000 61.00180  ?  39  TRP A CB  1 
ATOM   308  C  CG  . TRP A 1 39  ? 18.38300  20.37400  81.98800  1.000 60.42982  ?  39  TRP A CG  1 
ATOM   309  C  CD1 . TRP A 1 39  ? 17.55200  21.18800  81.27100  1.000 59.29231  ?  39  TRP A CD1 1 
ATOM   310  C  CD2 . TRP A 1 39  ? 17.54900  19.67400  82.92000  1.000 61.87804  ?  39  TRP A CD2 1 
ATOM   311  N  NE1 . TRP A 1 39  ? 16.25300  21.02600  81.68800  1.000 57.92745  ?  39  TRP A NE1 1 
ATOM   312  C  CE2 . TRP A 1 39  ? 16.22400  20.10300  82.70100  1.000 66.00832  ?  39  TRP A CE2 1 
ATOM   313  C  CE3 . TRP A 1 39  ? 17.79400  18.72100  83.91400  1.000 55.37437  ?  39  TRP A CE3 1 
ATOM   314  C  CZ2 . TRP A 1 39  ? 15.14900  19.61200  83.44000  1.000 63.43846  ?  39  TRP A CZ2 1 
ATOM   315  C  CZ3 . TRP A 1 39  ? 16.72500  18.23300  84.64600  1.000 58.47885  ?  39  TRP A CZ3 1 
ATOM   316  C  CH2 . TRP A 1 39  ? 15.41900  18.68000  84.40500  1.000 58.38809  ?  39  TRP A CH2 1 
ATOM   317  N  N   . ILE A 1 40  ? 19.26800  19.18800  78.57000  1.000 56.54949  ?  40  ILE A N   1 
ATOM   318  C  CA  . ILE A 1 40  ? 18.77200  19.70000  77.29900  1.000 55.05468  ?  40  ILE A CA  1 
ATOM   319  C  C   . ILE A 1 40  ? 17.29300  19.98400  77.50500  1.000 57.20805  ?  40  ILE A C   1 
ATOM   320  O  O   . ILE A 1 40  ? 16.47600  19.05700  77.55200  1.000 61.38419  ?  40  ILE A O   1 
ATOM   321  C  CB  . ILE A 1 40  ? 18.99700  18.71300  76.14600  1.000 63.06496  ?  40  ILE A CB  1 
ATOM   322  C  CG1 . ILE A 1 40  ? 20.48600  18.40700  75.97500  1.000 61.81004  ?  40  ILE A CG1 1 
ATOM   323  C  CG2 . ILE A 1 40  ? 18.42800  19.27400  74.85200  1.000 56.30075  ?  40  ILE A CG2 1 
ATOM   324  C  CD1 . ILE A 1 40  ? 20.77200  17.34200  74.93700  1.000 52.29572  ?  40  ILE A CD1 1 
ATOM   325  N  N   . GLY A 1 41  ? 16.93800  21.26400  77.62000  1.000 57.12081  ?  41  GLY A N   1 
ATOM   326  C  CA  . GLY A 1 41  ? 15.58200  21.65500  77.93900  1.000 57.61019  ?  41  GLY A CA  1 
ATOM   327  C  C   . GLY A 1 41  ? 15.06900  22.72900  76.99700  1.000 60.64531  ?  41  GLY A C   1 
ATOM   328  O  O   . GLY A 1 41  ? 15.79000  23.21700  76.12600  1.000 60.47661  ?  41  GLY A O   1 
ATOM   329  N  N   . CYS A 1 42  ? 13.80800  23.09100  77.20700  1.000 62.25970  ?  42  CYS A N   1 
ATOM   330  C  CA  . CYS A 1 42  ? 13.14900  24.07200  76.36000  1.000 60.08231  ?  42  CYS A CA  1 
ATOM   331  C  C   . CYS A 1 42  ? 13.59400  25.48200  76.72800  1.000 61.99213  ?  42  CYS A C   1 
ATOM   332  O  O   . CYS A 1 42  ? 13.92500  25.77400  77.88100  1.000 66.27462  ?  42  CYS A O   1 
ATOM   333  C  CB  . CYS A 1 42  ? 11.62900  23.94600  76.48700  1.000 59.79847  ?  42  CYS A CB  1 
ATOM   334  S  SG  . CYS A 1 42  ? 10.67400  25.12300  75.50100  1.000 51.33670  ?  42  CYS A SG  1 
ATOM   335  N  N   . SER A 1 43  ? 13.60100  26.36200  75.72500  1.000 67.55986  ?  43  SER A N   1 
ATOM   336  C  CA  . SER A 1 43  ? 13.96000  27.75500  75.96600  1.000 69.92045  ?  43  SER A CA  1 
ATOM   337  C  C   . SER A 1 43  ? 12.91900  28.49000  76.79500  1.000 69.17300  ?  43  SER A C   1 
ATOM   338  O  O   . SER A 1 43  ? 13.22700  29.55500  77.34200  1.000 70.61260  ?  43  SER A O   1 
ATOM   339  C  CB  . SER A 1 43  ? 14.17300  28.48600  74.63900  1.000 68.59095  ?  43  SER A CB  1 
ATOM   340  O  OG  . SER A 1 43  ? 15.38800  28.09100  74.03000  1.000 69.98522  ?  43  SER A OG  1 
ATOM   341  N  N   . ASP A 1 44  ? 11.70100  27.95200  76.90100  1.000 65.98879  ?  44  ASP A N   1 
ATOM   342  C  CA  . ASP A 1 44  ? 10.71100  28.54900  77.79100  1.000 70.13340  ?  44  ASP A CA  1 
ATOM   343  C  C   . ASP A 1 44  ? 11.22800  28.62000  79.22000  1.000 74.15684  ?  44  ASP A C   1 
ATOM   344  O  O   . ASP A 1 44  ? 11.05600  29.64100  79.89600  1.000 75.13379  ?  44  ASP A O   1 
ATOM   345  C  CB  . ASP A 1 44  ? 9.40100   27.76500  77.72900  1.000 68.86035  ?  44  ASP A CB  1 
ATOM   346  C  CG  . ASP A 1 44  ? 8.59900   28.07400  76.48200  1.000 74.83335  ?  44  ASP A CG  1 
ATOM   347  O  OD1 . ASP A 1 44  ? 8.53400   29.26000  76.09900  1.000 73.85401  ?  44  ASP A OD1 1 
ATOM   348  O  OD2 . ASP A 1 44  ? 8.03500   27.13500  75.88300  1.000 72.92998  -1 44  ASP A OD2 1 
ATOM   349  N  N   . SER A 1 45  ? 11.89500  27.56000  79.68100  1.000 72.88939  ?  45  SER A N   1 
ATOM   350  C  CA  . SER A 1 45  ? 12.43300  27.49200  81.03700  1.000 69.25176  ?  45  SER A CA  1 
ATOM   351  C  C   . SER A 1 45  ? 11.38400  27.94300  82.04900  1.000 67.64970  ?  45  SER A C   1 
ATOM   352  O  O   . SER A 1 45  ? 11.61000  28.84100  82.86200  1.000 78.07592  ?  45  SER A O   1 
ATOM   353  C  CB  . SER A 1 45  ? 13.71400  28.32000  81.15800  1.000 65.65437  ?  45  SER A CB  1 
ATOM   354  O  OG  . SER A 1 45  ? 14.44500  27.96700  82.32000  1.000 69.35363  ?  45  SER A OG  1 
ATOM   355  N  N   . ARG A 1 46  ? 10.20400  27.32300  81.95800  1.000 67.54479  ?  46  ARG A N   1 
ATOM   356  C  CA  . ARG A 1 46  ? 9.08900   27.70400  82.81800  1.000 76.37210  ?  46  ARG A CA  1 
ATOM   357  C  C   . ARG A 1 46  ? 9.46600   27.59600  84.28800  1.000 79.99610  ?  46  ARG A C   1 
ATOM   358  O  O   . ARG A 1 46  ? 9.13600   28.47600  85.08900  1.000 81.61275  ?  46  ARG A O   1 
ATOM   359  C  CB  . ARG A 1 46  ? 7.88000   26.82100  82.51200  1.000 75.97351  ?  46  ARG A CB  1 
ATOM   360  C  CG  . ARG A 1 46  ? 7.32800   26.97500  81.11000  1.000 77.10279  ?  46  ARG A CG  1 
ATOM   361  C  CD  . ARG A 1 46  ? 7.01400   28.42600  80.82300  1.000 79.07831  ?  46  ARG A CD  1 
ATOM   362  N  NE  . ARG A 1 46  ? 5.82000   28.85100  81.54400  1.000 87.20234  ?  46  ARG A NE  1 
ATOM   363  C  CZ  . ARG A 1 46  ? 5.38600   30.10100  81.60900  1.000 95.24311  ?  46  ARG A CZ  1 
ATOM   364  N  NH1 . ARG A 1 46  ? 6.03100   31.08900  81.01000  1.000 93.35879  ?  46  ARG A NH1 1 
ATOM   365  N  NH2 . ARG A 1 46  ? 4.27800   30.36800  82.29400  1.000 100.96354 ?  46  ARG A NH2 1 
ATOM   366  N  N   . VAL A 1 47  ? 10.18200  26.53300  84.65300  1.000 78.21535  ?  47  VAL A N   1 
ATOM   367  C  CA  . VAL A 1 47  ? 10.79000  26.40000  85.96700  1.000 74.75116  ?  47  VAL A CA  1 
ATOM   368  C  C   . VAL A 1 47  ? 12.25700  26.06800  85.72600  1.000 74.03454  ?  47  VAL A C   1 
ATOM   369  O  O   . VAL A 1 47  ? 12.56100  25.09100  85.03600  1.000 80.68844  ?  47  VAL A O   1 
ATOM   370  C  CB  . VAL A 1 47  ? 10.12700  25.31300  86.83200  1.000 72.79660  ?  47  VAL A CB  1 
ATOM   371  C  CG1 . VAL A 1 47  ? 10.69000  25.34700  88.24200  1.000 74.73337  ?  47  VAL A CG1 1 
ATOM   372  C  CG2 . VAL A 1 47  ? 8.61800   25.50200  86.85900  1.000 70.13598  ?  47  VAL A CG2 1 
ATOM   373  N  N   . PRO A 1 48  ? 13.19900  26.86200  86.23600  1.000 73.68389  ?  48  PRO A N   1 
ATOM   374  C  CA  . PRO A 1 48  ? 14.61800  26.57000  86.00300  1.000 74.53132  ?  48  PRO A CA  1 
ATOM   375  C  C   . PRO A 1 48  ? 14.97700  25.15800  86.44500  1.000 76.57973  ?  48  PRO A C   1 
ATOM   376  O  O   . PRO A 1 48  ? 14.34900  24.58400  87.33800  1.000 77.76137  ?  48  PRO A O   1 
ATOM   377  C  CB  . PRO A 1 48  ? 15.33800  27.62200  86.85300  1.000 78.56724  ?  48  PRO A CB  1 
ATOM   378  C  CG  . PRO A 1 48  ? 14.36700  28.75700  86.93100  1.000 84.70075  ?  48  PRO A CG  1 
ATOM   379  C  CD  . PRO A 1 48  ? 13.00400  28.12000  86.97600  1.000 85.43134  ?  48  PRO A CD  1 
ATOM   380  N  N   . ALA A 1 49  ? 15.99700  24.59400  85.79500  1.000 76.72455  ?  49  ALA A N   1 
ATOM   381  C  CA  . ALA A 1 49  ? 16.35000  23.20200  86.04900  1.000 76.15735  ?  49  ALA A CA  1 
ATOM   382  C  C   . ALA A 1 49  ? 16.85300  23.00300  87.47000  1.000 76.70506  ?  49  ALA A C   1 
ATOM   383  O  O   . ALA A 1 49  ? 16.62800  21.94200  88.06400  1.000 72.19958  ?  49  ALA A O   1 
ATOM   384  C  CB  . ALA A 1 49  ? 17.40400  22.73700  85.04600  1.000 71.60441  ?  49  ALA A CB  1 
ATOM   385  N  N   . GLU A 1 50  ? 17.52700  24.00800  88.02600  1.000 79.88595  ?  50  GLU A N   1 
ATOM   386  C  CA  . GLU A 1 50  ? 18.05100  23.89500  89.38000  1.000 82.80801  ?  50  GLU A CA  1 
ATOM   387  C  C   . GLU A 1 50  ? 16.92300  23.85700  90.40600  1.000 81.19835  ?  50  GLU A C   1 
ATOM   388  O  O   . GLU A 1 50  ? 17.03400  23.17300  91.43000  1.000 77.36041  ?  50  GLU A O   1 
ATOM   389  C  CB  . GLU A 1 50  ? 19.01600  25.04800  89.66400  1.000 85.30181  ?  50  GLU A CB  1 
ATOM   390  C  CG  . GLU A 1 50  ? 20.29000  25.03700  88.81200  1.000 85.83479  ?  50  GLU A CG  1 
ATOM   391  C  CD  . GLU A 1 50  ? 20.08200  25.55900  87.39800  1.000 90.75986  ?  50  GLU A CD  1 
ATOM   392  O  OE1 . GLU A 1 50  ? 18.94700  25.96300  87.06600  1.000 91.35396  ?  50  GLU A OE1 1 
ATOM   393  O  OE2 . GLU A 1 50  ? 21.06000  25.56700  86.62000  1.000 87.83557  -1 50  GLU A OE2 1 
ATOM   394  N  N   . ARG A 1 51  ? 15.83500  24.59200  90.15600  1.000 81.47496  ?  51  ARG A N   1 
ATOM   395  C  CA  . ARG A 1 51  ? 14.71300  24.57000  91.08600  1.000 74.93981  ?  51  ARG A CA  1 
ATOM   396  C  C   . ARG A 1 51  ? 13.95000  23.25700  91.01500  1.000 78.62811  ?  51  ARG A C   1 
ATOM   397  O  O   . ARG A 1 51  ? 13.52700  22.72600  92.04800  1.000 81.81754  ?  51  ARG A O   1 
ATOM   398  C  CB  . ARG A 1 51  ? 13.78900  25.74800  90.82000  1.000 81.72484  ?  51  ARG A CB  1 
ATOM   399  C  CG  . ARG A 1 51  ? 14.50300  27.05000  91.02400  1.000 95.58847  ?  51  ARG A CG  1 
ATOM   400  C  CD  . ARG A 1 51  ? 13.52500  28.18900  91.07700  1.000 105.14210 ?  51  ARG A CD  1 
ATOM   401  N  NE  . ARG A 1 51  ? 14.20800  29.47700  91.18700  1.000 107.04100 ?  51  ARG A NE  1 
ATOM   402  C  CZ  . ARG A 1 51  ? 13.59300  30.65100  91.03100  1.000 106.57383 ?  51  ARG A CZ  1 
ATOM   403  N  NH1 . ARG A 1 51  ? 12.28900  30.72400  90.79700  1.000 107.29511 ?  51  ARG A NH1 1 
ATOM   404  N  NH2 . ARG A 1 51  ? 14.30100  31.78200  91.10500  1.000 101.22946 ?  51  ARG A NH2 1 
ATOM   405  N  N   . LEU A 1 52  ? 13.76500  22.71800  89.80800  1.000 81.63808  ?  52  LEU A N   1 
ATOM   406  C  CA  . LEU A 1 52  ? 13.02500  21.46900  89.65500  1.000 79.75873  ?  52  LEU A CA  1 
ATOM   407  C  C   . LEU A 1 52  ? 13.75200  20.30300  90.31100  1.000 75.45490  ?  52  LEU A C   1 
ATOM   408  O  O   . LEU A 1 52  ? 13.11900  19.42600  90.90800  1.000 69.00691  ?  52  LEU A O   1 
ATOM   409  C  CB  . LEU A 1 52  ? 12.79200  21.16800  88.17400  1.000 78.17406  ?  52  LEU A CB  1 
ATOM   410  C  CG  . LEU A 1 52  ? 11.71200  21.92300  87.40100  1.000 73.70204  ?  52  LEU A CG  1 
ATOM   411  C  CD1 . LEU A 1 52  ? 11.90500  21.68400  85.91700  1.000 77.53091  ?  52  LEU A CD1 1 
ATOM   412  C  CD2 . LEU A 1 52  ? 10.32200  21.48100  87.83600  1.000 70.90894  ?  52  LEU A CD2 1 
ATOM   413  N  N   . THR A 1 53  ? 15.07900  20.27600  90.21400  1.000 77.17179  ?  53  THR A N   1 
ATOM   414  C  CA  . THR A 1 53  ? 15.86200  19.13400  90.65400  1.000 71.77930  ?  53  THR A CA  1 
ATOM   415  C  C   . THR A 1 53  ? 16.61800  19.37800  91.95000  1.000 73.75417  ?  53  THR A C   1 
ATOM   416  O  O   . THR A 1 53  ? 17.22800  18.44000  92.47500  1.000 79.05085  ?  53  THR A O   1 
ATOM   417  C  CB  . THR A 1 53  ? 16.85800  18.72000  89.56000  1.000 75.30793  ?  53  THR A CB  1 
ATOM   418  O  OG1 . THR A 1 53  ? 17.69700  19.83400  89.23000  1.000 72.27229  ?  53  THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 53  ? 16.11900  18.25800  88.31300  1.000 69.95238  ?  53  THR A CG2 1 
ATOM   420  N  N   . GLY A 1 54  ? 16.60900  20.60300  92.47000  1.000 74.96687  ?  54  GLY A N   1 
ATOM   421  C  CA  . GLY A 1 54  ? 17.38900  20.89600  93.65500  1.000 82.23362  ?  54  GLY A CA  1 
ATOM   422  C  C   . GLY A 1 54  ? 18.88000  20.81500  93.44700  1.000 80.38361  ?  54  GLY A C   1 
ATOM   423  O  O   . GLY A 1 54  ? 19.62100  20.59500  94.40800  1.000 84.45616  ?  54  GLY A O   1 
ATOM   424  N  N   . LEU A 1 55  ? 19.34400  20.97000  92.21200  1.000 79.45683  ?  55  LEU A N   1 
ATOM   425  C  CA  . LEU A 1 55  ? 20.76200  20.90000  91.90800  1.000 85.75657  ?  55  LEU A CA  1 
ATOM   426  C  C   . LEU A 1 55  ? 21.38500  22.27600  92.11300  1.000 86.66058  ?  55  LEU A C   1 
ATOM   427  O  O   . LEU A 1 55  ? 20.81100  23.29500  91.71800  1.000 84.66132  ?  55  LEU A O   1 
ATOM   428  C  CB  . LEU A 1 55  ? 20.95600  20.41800  90.46800  1.000 85.48262  ?  55  LEU A CB  1 
ATOM   429  C  CG  . LEU A 1 55  ? 20.65100  18.94100  90.18000  1.000 83.99574  ?  55  LEU A CG  1 
ATOM   430  C  CD1 . LEU A 1 55  ? 20.60500  18.66500  88.67300  1.000 84.50124  ?  55  LEU A CD1 1 
ATOM   431  C  CD2 . LEU A 1 55  ? 21.62000  18.03400  90.87400  1.000 86.53558  ?  55  LEU A CD2 1 
ATOM   432  N  N   . GLU A 1 56  ? 22.54800  22.30200  92.75000  1.000 94.42935  ?  56  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 56  ? 23.22700  23.54100  93.10400  1.000 98.56306  ?  56  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 56  ? 24.16900  23.98400  91.98700  1.000 99.58652  ?  56  GLU A C   1 
ATOM   435  O  O   . GLU A 1 56  ? 24.56300  23.18000  91.13700  1.000 92.39556  ?  56  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 56  ? 23.95100  23.37100  94.44200  1.000 97.00091  ?  56  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 56  ? 25.04200  22.33300  94.51400  1.000 97.16217  ?  56  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 56  ? 25.46600  22.09400  95.95100  1.000 104.06989 ?  56  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 56  ? 24.95600  22.81100  96.84100  1.000 101.22902 ?  56  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 56  ? 26.29600  21.19500  96.19500  1.000 105.86164 -1 56  GLU A OE2 1 
ATOM   441  N  N   . PRO A 1 57  ? 24.52900  25.29100  91.94500  1.000 100.27931 ?  57  PRO A N   1 
ATOM   442  C  CA  . PRO A 1 57  ? 25.36700  25.80800  90.84800  1.000 95.71075  ?  57  PRO A CA  1 
ATOM   443  C  C   . PRO A 1 57  ? 26.66300  25.05100  90.60600  1.000 97.03479  ?  57  PRO A C   1 
ATOM   444  O  O   . PRO A 1 57  ? 27.49400  24.93500  91.51000  1.000 92.46186  ?  57  PRO A O   1 
ATOM   445  C  CB  . PRO A 1 57  ? 25.68900  27.24000  91.30100  1.000 96.18011  ?  57  PRO A CB  1 
ATOM   446  C  CG  . PRO A 1 57  ? 24.67400  27.59100  92.28500  1.000 96.16718  ?  57  PRO A CG  1 
ATOM   447  C  CD  . PRO A 1 57  ? 24.28400  26.32200  92.97100  1.000 96.85504  ?  57  PRO A CD  1 
ATOM   448  N  N   . GLY A 1 58  ? 26.85600  24.54500  89.39100  1.000 105.60448 ?  58  GLY A N   1 
ATOM   449  C  CA  . GLY A 1 58  ? 28.11100  23.94200  88.98100  1.000 103.88410 ?  58  GLY A CA  1 
ATOM   450  C  C   . GLY A 1 58  ? 28.04300  22.48700  88.55600  1.000 96.37381  ?  58  GLY A C   1 
ATOM   451  O  O   . GLY A 1 58  ? 28.97000  22.01300  87.88900  1.000 91.92955  ?  58  GLY A O   1 
ATOM   452  N  N   . GLU A 1 59  ? 26.97400  21.75500  88.89300  1.000 96.68885  ?  59  GLU A N   1 
ATOM   453  C  CA  . GLU A 1 59  ? 26.83800  20.36900  88.46000  1.000 95.42920  ?  59  GLU A CA  1 
ATOM   454  C  C   . GLU A 1 59  ? 25.83800  20.20400  87.32700  1.000 91.38152  ?  59  GLU A C   1 
ATOM   455  O  O   . GLU A 1 59  ? 25.36300  19.09000  87.09100  1.000 87.79694  ?  59  GLU A O   1 
ATOM   456  C  CB  . GLU A 1 59  ? 26.45200  19.44800  89.61800  1.000 92.79046  ?  59  GLU A CB  1 
ATOM   457  C  CG  . GLU A 1 59  ? 25.18400  19.81300  90.36600  1.000 100.31484 ?  59  GLU A CG  1 
ATOM   458  C  CD  . GLU A 1 59  ? 24.90300  18.82600  91.46700  1.000 107.84132 ?  59  GLU A CD  1 
ATOM   459  O  OE1 . GLU A 1 59  ? 25.57000  17.77300  91.48200  1.000 113.24997 ?  59  GLU A OE1 1 
ATOM   460  O  OE2 . GLU A 1 59  ? 24.09800  19.13700  92.36600  1.000 106.69489 -1 59  GLU A OE2 1 
ATOM   461  N  N   . LEU A 1 60  ? 25.50300  21.27800  86.62400  1.000 89.40033  ?  60  LEU A N   1 
ATOM   462  C  CA  . LEU A 1 60  ? 24.54100  21.19600  85.53800  1.000 80.77935  ?  60  LEU A CA  1 
ATOM   463  C  C   . LEU A 1 60  ? 25.12500  21.88600  84.31800  1.000 78.03611  ?  60  LEU A C   1 
ATOM   464  O  O   . LEU A 1 60  ? 25.39500  23.09100  84.35500  1.000 78.07454  ?  60  LEU A O   1 
ATOM   465  C  CB  . LEU A 1 60  ? 23.21000  21.83000  85.93600  1.000 83.61421  ?  60  LEU A CB  1 
ATOM   466  C  CG  . LEU A 1 60  ? 22.11500  20.84900  86.36500  1.000 86.33111  ?  60  LEU A CG  1 
ATOM   467  C  CD1 . LEU A 1 60  ? 20.76100  21.53800  86.45000  1.000 82.68716  ?  60  LEU A CD1 1 
ATOM   468  C  CD2 . LEU A 1 60  ? 22.05100  19.64900  85.43400  1.000 78.37412  ?  60  LEU A CD2 1 
ATOM   469  N  N   . PHE A 1 61  ? 25.31400  21.12400  83.24600  1.000 82.49358  ?  61  PHE A N   1 
ATOM   470  C  CA  . PHE A 1 61  ? 25.55800  21.67800  81.92300  1.000 72.05152  ?  61  PHE A CA  1 
ATOM   471  C  C   . PHE A 1 61  ? 24.21600  21.78900  81.21400  1.000 70.88556  ?  61  PHE A C   1 
ATOM   472  O  O   . PHE A 1 61  ? 23.47200  20.80700  81.12700  1.000 70.67099  ?  61  PHE A O   1 
ATOM   473  C  CB  . PHE A 1 61  ? 26.52100  20.78800  81.13800  1.000 63.69969  ?  61  PHE A CB  1 
ATOM   474  C  CG  . PHE A 1 61  ? 27.46800  21.54700  80.24800  1.000 65.86446  ?  61  PHE A CG  1 
ATOM   475  C  CD1 . PHE A 1 61  ? 28.32700  22.49300  80.78100  1.000 63.29783  ?  61  PHE A CD1 1 
ATOM   476  C  CD2 . PHE A 1 61  ? 27.51000  21.30300  78.88400  1.000 76.67613  ?  61  PHE A CD2 1 
ATOM   477  C  CE1 . PHE A 1 61  ? 29.20600  23.18900  79.96900  1.000 65.82644  ?  61  PHE A CE1 1 
ATOM   478  C  CE2 . PHE A 1 61  ? 28.38800  21.99800  78.06500  1.000 75.62732  ?  61  PHE A CE2 1 
ATOM   479  C  CZ  . PHE A 1 61  ? 29.23600  22.94200  78.61000  1.000 77.52362  ?  61  PHE A CZ  1 
ATOM   480  N  N   . VAL A 1 62  ? 23.89300  22.98500  80.73300  1.000 73.21356  ?  62  VAL A N   1 
ATOM   481  C  CA  . VAL A 1 62  ? 22.54500  23.29600  80.27300  1.000 70.18630  ?  62  VAL A CA  1 
ATOM   482  C  C   . VAL A 1 62  ? 22.59800  23.77200  78.82900  1.000 72.06244  ?  62  VAL A C   1 
ATOM   483  O  O   . VAL A 1 62  ? 23.38800  24.65900  78.48700  1.000 71.89757  ?  62  VAL A O   1 
ATOM   484  C  CB  . VAL A 1 62  ? 21.87100  24.35300  81.16900  1.000 67.91727  ?  62  VAL A CB  1 
ATOM   485  C  CG1 . VAL A 1 62  ? 20.46500  24.65600  80.66700  1.000 64.15637  ?  62  VAL A CG1 1 
ATOM   486  C  CG2 . VAL A 1 62  ? 21.83700  23.88200  82.61400  1.000 75.24576  ?  62  VAL A CG2 1 
ATOM   487  N  N   . HIS A 1 63  ? 21.74800  23.18400  77.99000  1.000 69.45640  ?  63  HIS A N   1 
ATOM   488  C  CA  . HIS A 1 63  ? 21.47900  23.67700  76.64800  1.000 65.02236  ?  63  HIS A CA  1 
ATOM   489  C  C   . HIS A 1 63  ? 19.97500  23.81700  76.47900  1.000 63.49379  ?  63  HIS A C   1 
ATOM   490  O  O   . HIS A 1 63  ? 19.20900  22.96600  76.94000  1.000 58.15870  ?  63  HIS A O   1 
ATOM   491  C  CB  . HIS A 1 63  ? 22.04900  22.74200  75.57000  1.000 64.88449  ?  63  HIS A CB  1 
ATOM   492  C  CG  . HIS A 1 63  ? 21.56200  23.04800  74.18600  1.000 68.20141  ?  63  HIS A CG  1 
ATOM   493  N  ND1 . HIS A 1 63  ? 21.94300  24.17800  73.49400  1.000 65.65869  ?  63  HIS A ND1 1 
ATOM   494  C  CD2 . HIS A 1 63  ? 20.72600  22.36900  73.36500  1.000 66.92547  ?  63  HIS A CD2 1 
ATOM   495  C  CE1 . HIS A 1 63  ? 21.36000  24.18300  72.30900  1.000 70.59794  ?  63  HIS A CE1 1 
ATOM   496  N  NE2 . HIS A 1 63  ? 20.61800  23.09600  72.20500  1.000 65.32886  ?  63  HIS A NE2 1 
ATOM   497  N  N   . ARG A 1 64  ? 19.55400  24.89300  75.82000  1.000 67.66960  ?  64  ARG A N   1 
ATOM   498  C  CA  . ARG A 1 64  ? 18.13600  25.14900  75.61500  1.000 65.63793  ?  64  ARG A CA  1 
ATOM   499  C  C   . ARG A 1 64  ? 17.89100  25.70100  74.22100  1.000 64.40108  ?  64  ARG A C   1 
ATOM   500  O  O   . ARG A 1 64  ? 18.55400  26.65100  73.79400  1.000 69.75281  ?  64  ARG A O   1 
ATOM   501  C  CB  . ARG A 1 64  ? 17.59300  26.11600  76.67900  1.000 67.89700  ?  64  ARG A CB  1 
ATOM   502  C  CG  . ARG A 1 64  ? 17.49600  25.49900  78.07300  1.000 67.77048  ?  64  ARG A CG  1 
ATOM   503  C  CD  . ARG A 1 64  ? 16.96900  26.47500  79.11900  1.000 66.01219  ?  64  ARG A CD  1 
ATOM   504  N  NE  . ARG A 1 64  ? 16.83700  25.83400  80.42300  1.000 59.14113  ?  64  ARG A NE  1 
ATOM   505  C  CZ  . ARG A 1 64  ? 15.76700  25.16000  80.82500  1.000 59.43657  ?  64  ARG A CZ  1 
ATOM   506  N  NH1 . ARG A 1 64  ? 14.68700  25.06000  80.06700  1.000 64.21419  ?  64  ARG A NH1 1 
ATOM   507  N  NH2 . ARG A 1 64  ? 15.78000  24.57300  82.01700  1.000 69.71407  ?  64  ARG A NH2 1 
ATOM   508  N  N   . ASN A 1 65  ? 16.93400  25.09400  73.52000  1.000 64.37017  ?  65  ASN A N   1 
ATOM   509  C  CA  . ASN A 1 65  ? 16.43800  25.58000  72.24100  1.000 61.76235  ?  65  ASN A CA  1 
ATOM   510  C  C   . ASN A 1 65  ? 14.92000  25.47900  72.28000  1.000 59.23192  ?  65  ASN A C   1 
ATOM   511  O  O   . ASN A 1 65  ? 14.34000  24.96400  73.24200  1.000 58.18605  ?  65  ASN A O   1 
ATOM   512  C  CB  . ASN A 1 65  ? 17.02600  24.79300  71.06200  1.000 55.96728  ?  65  ASN A CB  1 
ATOM   513  C  CG  . ASN A 1 65  ? 16.73000  23.30200  71.13900  1.000 57.17531  ?  65  ASN A CG  1 
ATOM   514  O  OD1 . ASN A 1 65  ? 15.57300  22.88000  71.07300  1.000 54.37553  ?  65  ASN A OD1 1 
ATOM   515  N  ND2 . ASN A 1 65  ? 17.78100  22.49500  71.24800  1.000 56.91208  ?  65  ASN A ND2 1 
ATOM   516  N  N   . VAL A 1 66  ? 14.26500  25.96900  71.23000  1.000 52.09112  ?  66  VAL A N   1 
ATOM   517  C  CA  . VAL A 1 66  ? 12.80600  25.96500  71.21200  1.000 53.41262  ?  66  VAL A CA  1 
ATOM   518  C  C   . VAL A 1 66  ? 12.30900  24.52600  71.14100  1.000 57.40795  ?  66  VAL A C   1 
ATOM   519  O  O   . VAL A 1 66  ? 12.63400  23.78800  70.20300  1.000 52.73118  ?  66  VAL A O   1 
ATOM   520  C  CB  . VAL A 1 66  ? 12.26300  26.80400  70.04900  1.000 51.53252  ?  66  VAL A CB  1 
ATOM   521  C  CG1 . VAL A 1 66  ? 10.74400  26.84800  70.10400  1.000 51.56650  ?  66  VAL A CG1 1 
ATOM   522  C  CG2 . VAL A 1 66  ? 12.83300  28.21200  70.10800  1.000 56.39990  ?  66  VAL A CG2 1 
ATOM   523  N  N   . ALA A 1 67  ? 11.54200  24.12000  72.15700  1.000 64.07002  ?  67  ALA A N   1 
ATOM   524  C  CA  . ALA A 1 67  ? 10.90500  22.80500  72.24000  1.000 56.64599  ?  67  ALA A CA  1 
ATOM   525  C  C   . ALA A 1 67  ? 11.91300  21.67100  72.41300  1.000 53.80337  ?  67  ALA A C   1 
ATOM   526  O  O   . ALA A 1 67  ? 11.63800  20.53200  72.02800  1.000 52.46247  ?  67  ALA A O   1 
ATOM   527  C  CB  . ALA A 1 67  ? 10.00600  22.53900  71.03000  1.000 56.90085  ?  67  ALA A CB  1 
ATOM   528  N  N   . ASN A 1 68  ? 13.06900  21.98300  73.00000  1.000 56.39229  ?  68  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 68  ? 14.09400  21.02000  73.42400  1.000 58.88390  ?  68  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 68  ? 14.33100  19.92700  72.38000  1.000 58.90507  ?  68  ASN A C   1 
ATOM   531  O  O   . ASN A 1 68  ? 14.12800  18.73600  72.61900  1.000 55.71579  ?  68  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 68  ? 13.75500  20.41200  74.79000  1.000 51.53167  ?  68  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 68  ? 12.36600  19.80000  74.84100  1.000 48.45667  ?  68  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 68  ? 11.39300  20.46600  75.19700  1.000 45.13763  ?  68  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 68  ? 12.27100  18.52200  74.49500  1.000 47.62586  ?  68  ASN A ND2 1 
ATOM   536  N  N   . LEU A 1 69  ? 14.78300  20.36200  71.20800  1.000 58.28728  ?  69  LEU A N   1 
ATOM   537  C  CA  . LEU A 1 69  ? 15.02500  19.46700  70.08700  1.000 53.35579  ?  69  LEU A CA  1 
ATOM   538  C  C   . LEU A 1 69  ? 16.48300  19.02700  70.06000  1.000 55.41614  ?  69  LEU A C   1 
ATOM   539  O  O   . LEU A 1 69  ? 17.38200  19.76100  70.48100  1.000 49.74022  ?  69  LEU A O   1 
ATOM   540  C  CB  . LEU A 1 69  ? 14.66100  20.14900  68.76600  1.000 59.61776  ?  69  LEU A CB  1 
ATOM   541  C  CG  . LEU A 1 69  ? 13.18100  20.46500  68.54300  1.000 59.41201  ?  69  LEU A CG  1 
ATOM   542  C  CD1 . LEU A 1 69  ? 12.94000  20.93600  67.12100  1.000 46.26911  ?  69  LEU A CD1 1 
ATOM   543  C  CD2 . LEU A 1 69  ? 12.32200  19.24900  68.85500  1.000 54.75414  ?  69  LEU A CD2 1 
ATOM   544  N  N   . VAL A 1 70  ? 16.70900  17.81100  69.56500  1.000 55.62750  ?  70  VAL A N   1 
ATOM   545  C  CA  . VAL A 1 70  ? 18.05400  17.29000  69.31300  1.000 58.39222  ?  70  VAL A CA  1 
ATOM   546  C  C   . VAL A 1 70  ? 18.07500  16.85400  67.84900  1.000 57.93144  ?  70  VAL A C   1 
ATOM   547  O  O   . VAL A 1 70  ? 17.83700  15.68500  67.52400  1.000 51.91673  ?  70  VAL A O   1 
ATOM   548  C  CB  . VAL A 1 70  ? 18.42500  16.13300  70.24800  1.000 52.45938  ?  70  VAL A CB  1 
ATOM   549  C  CG1 . VAL A 1 70  ? 19.85300  15.66600  69.98500  1.000 51.82723  ?  70  VAL A CG1 1 
ATOM   550  C  CG2 . VAL A 1 70  ? 18.24600  16.54700  71.70500  1.000 64.22211  ?  70  VAL A CG2 1 
ATOM   551  N  N   . ILE A 1 71  ? 18.37100  17.79200  66.95400  1.000 58.82518  ?  71  ILE A N   1 
ATOM   552  C  CA  . ILE A 1 71  ? 18.36700  17.51400  65.52300  1.000 58.54002  ?  71  ILE A CA  1 
ATOM   553  C  C   . ILE A 1 71  ? 19.68800  16.87700  65.11900  1.000 62.70844  ?  71  ILE A C   1 
ATOM   554  O  O   . ILE A 1 71  ? 20.76000  17.27100  65.59700  1.000 65.91034  ?  71  ILE A O   1 
ATOM   555  C  CB  . ILE A 1 71  ? 18.09400  18.80200  64.72500  1.000 52.33164  ?  71  ILE A CB  1 
ATOM   556  C  CG1 . ILE A 1 71  ? 16.73800  19.38900  65.11800  1.000 52.93863  ?  71  ILE A CG1 1 
ATOM   557  C  CG2 . ILE A 1 71  ? 18.15300  18.54100  63.22300  1.000 69.71541  ?  71  ILE A CG2 1 
ATOM   558  C  CD1 . ILE A 1 71  ? 16.55000  20.82600  64.69300  1.000 57.24632  ?  71  ILE A CD1 1 
ATOM   559  N  N   . HIS A 1 72  ? 19.60500  15.88700  64.22300  1.000 55.58472  ?  72  HIS A N   1 
ATOM   560  C  CA  . HIS A 1 72  ? 20.77900  15.12900  63.80400  1.000 54.06042  ?  72  HIS A CA  1 
ATOM   561  C  C   . HIS A 1 72  ? 21.87800  16.04000  63.27800  1.000 63.42613  ?  72  HIS A C   1 
ATOM   562  O  O   . HIS A 1 72  ? 23.06500  15.70700  63.37800  1.000 63.66918  ?  72  HIS A O   1 
ATOM   563  C  CB  . HIS A 1 72  ? 20.39800  14.13200  62.70700  1.000 65.66626  ?  72  HIS A CB  1 
ATOM   564  C  CG  . HIS A 1 72  ? 19.17600  13.32200  63.01200  1.000 66.60167  ?  72  HIS A CG  1 
ATOM   565  N  ND1 . HIS A 1 72  ? 17.90100  13.80400  62.80800  1.000 66.69552  ?  72  HIS A ND1 1 
ATOM   566  C  CD2 . HIS A 1 72  ? 19.02900  12.06100  63.48300  1.000 65.34142  ?  72  HIS A CD2 1 
ATOM   567  C  CE1 . HIS A 1 72  ? 17.02200  12.88000  63.14800  1.000 67.63824  ?  72  HIS A CE1 1 
ATOM   568  N  NE2 . HIS A 1 72  ? 17.68000  11.81200  63.56200  1.000 68.82535  ?  72  HIS A NE2 1 
ATOM   569  N  N   . THR A 1 73  ? 21.50200  17.18600  62.70200  1.000 67.40399  ?  73  THR A N   1 
ATOM   570  C  CA  . THR A 1 73  ? 22.43700  18.05900  62.00300  1.000 64.14239  ?  73  THR A CA  1 
ATOM   571  C  C   . THR A 1 73  ? 22.54500  19.44300  62.63400  1.000 68.70538  ?  73  THR A C   1 
ATOM   572  O  O   . THR A 1 73  ? 22.97700  20.38600  61.96400  1.000 75.54880  ?  73  THR A O   1 
ATOM   573  C  CB  . THR A 1 73  ? 22.03600  18.19400  60.53200  1.000 67.44156  ?  73  THR A CB  1 
ATOM   574  O  OG1 . THR A 1 73  ? 20.62800  18.45100  60.44000  1.000 67.13628  ?  73  THR A OG1 1 
ATOM   575  C  CG2 . THR A 1 73  ? 22.37100  16.92400  59.76700  1.000 57.25154  ?  73  THR A CG2 1 
ATOM   576  N  N   . ASP A 1 74  ? 22.16300  19.59800  63.90000  1.000 69.42459  ?  74  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 74  ? 22.29900  20.88700  64.57700  1.000 69.43098  ?  74  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 74  ? 23.62900  20.89400  65.32000  1.000 69.91638  ?  74  ASP A C   1 
ATOM   579  O  O   . ASP A 1 74  ? 23.74800  20.32800  66.40900  1.000 70.15759  ?  74  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 74  ? 21.12900  21.14000  65.52100  1.000 67.39662  ?  74  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 74  ? 21.31000  22.40300  66.34600  1.000 75.63163  ?  74  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 74  ? 21.99000  23.33500  65.86400  1.000 74.76866  ?  74  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 74  ? 20.77600  22.46300  67.47400  1.000 76.29992  -1 74  ASP A OD2 1 
ATOM   584  N  N   . LEU A 1 75  ? 24.63000  21.56000  64.73800  1.000 68.29842  ?  75  LEU A N   1 
ATOM   585  C  CA  . LEU A 1 75  ? 25.95900  21.57600  65.34300  1.000 69.52904  ?  75  LEU A CA  1 
ATOM   586  C  C   . LEU A 1 75  ? 25.96600  22.29700  66.68400  1.000 67.81276  ?  75  LEU A C   1 
ATOM   587  O  O   . LEU A 1 75  ? 26.83700  22.03400  67.52200  1.000 62.79811  ?  75  LEU A O   1 
ATOM   588  C  CB  . LEU A 1 75  ? 26.96800  22.21200  64.38800  1.000 64.01031  ?  75  LEU A CB  1 
ATOM   589  C  CG  . LEU A 1 75  ? 28.42000  21.82600  64.67200  1.000 65.16075  ?  75  LEU A CG  1 
ATOM   590  C  CD1 . LEU A 1 75  ? 28.52900  20.34400  65.00100  1.000 64.59248  ?  75  LEU A CD1 1 
ATOM   591  C  CD2 . LEU A 1 75  ? 29.30000  22.16700  63.48500  1.000 69.78937  ?  75  LEU A CD2 1 
ATOM   592  N  N   . ASN A 1 76  ? 25.02800  23.21900  66.89700  1.000 66.58010  ?  76  ASN A N   1 
ATOM   593  C  CA  . ASN A 1 76  ? 24.88200  23.88400  68.18500  1.000 68.08617  ?  76  ASN A CA  1 
ATOM   594  C  C   . ASN A 1 76  ? 24.72100  22.84100  69.28500  1.000 69.31606  ?  76  ASN A C   1 
ATOM   595  O  O   . ASN A 1 76  ? 25.60300  22.68500  70.13500  1.000 67.27303  ?  76  ASN A O   1 
ATOM   596  C  CB  . ASN A 1 76  ? 23.69000  24.84500  68.15400  1.000 72.99205  ?  76  ASN A CB  1 
ATOM   597  C  CG  . ASN A 1 76  ? 23.60900  25.73400  69.38500  1.000 72.38174  ?  76  ASN A CG  1 
ATOM   598  O  OD1 . ASN A 1 76  ? 23.90000  25.30900  70.50300  1.000 67.42730  ?  76  ASN A OD1 1 
ATOM   599  N  ND2 . ASN A 1 76  ? 23.21200  26.98400  69.17800  1.000 72.99468  ?  76  ASN A ND2 1 
ATOM   600  N  N   . CYS A 1 77  ? 23.59400  22.12600  69.27000  1.000 68.88469  ?  77  CYS A N   1 
ATOM   601  C  CA  . CYS A 1 77  ? 23.34100  21.10400  70.28200  1.000 62.21802  ?  77  CYS A CA  1 
ATOM   602  C  C   . CYS A 1 77  ? 24.41700  20.02200  70.27400  1.000 58.54574  ?  77  CYS A C   1 
ATOM   603  O  O   . CYS A 1 77  ? 24.83900  19.55000  71.33400  1.000 69.27475  ?  77  CYS A O   1 
ATOM   604  C  CB  . CYS A 1 77  ? 21.96200  20.48500  70.06100  1.000 65.13726  ?  77  CYS A CB  1 
ATOM   605  S  SG  . CYS A 1 77  ? 21.51200  19.21000  71.25800  1.000 62.72096  ?  77  CYS A SG  1 
ATOM   606  N  N   . LEU A 1 78  ? 24.86900  19.61100  69.08700  1.000 66.62158  ?  78  LEU A N   1 
ATOM   607  C  CA  . LEU A 1 78  ? 25.84900  18.53100  68.99900  1.000 65.21373  ?  78  LEU A CA  1 
ATOM   608  C  C   . LEU A 1 78  ? 27.19900  18.93000  69.58200  1.000 62.13449  ?  78  LEU A C   1 
ATOM   609  O  O   . LEU A 1 78  ? 27.89900  18.08100  70.14600  1.000 63.27372  ?  78  LEU A O   1 
ATOM   610  C  CB  . LEU A 1 78  ? 25.99300  18.06900  67.55200  1.000 64.51966  ?  78  LEU A CB  1 
ATOM   611  C  CG  . LEU A 1 78  ? 24.73200  17.36800  67.05200  1.000 66.76511  ?  78  LEU A CG  1 
ATOM   612  C  CD1 . LEU A 1 78  ? 24.83300  17.08100  65.56900  1.000 71.00501  ?  78  LEU A CD1 1 
ATOM   613  C  CD2 . LEU A 1 78  ? 24.50200  16.08600  67.84000  1.000 56.39948  ?  78  LEU A CD2 1 
ATOM   614  N  N   . SER A 1 79  ? 27.59700  20.19500  69.43900  1.000 60.77660  ?  79  SER A N   1 
ATOM   615  C  CA  . SER A 1 79  ? 28.83600  20.63300  70.07200  1.000 64.19969  ?  79  SER A CA  1 
ATOM   616  C  C   . SER A 1 79  ? 28.71000  20.59600  71.58900  1.000 70.14471  ?  79  SER A C   1 
ATOM   617  O  O   . SER A 1 79  ? 29.66200  20.23300  72.29000  1.000 69.60947  ?  79  SER A O   1 
ATOM   618  C  CB  . SER A 1 79  ? 29.21300  22.03500  69.59500  1.000 70.51026  ?  79  SER A CB  1 
ATOM   619  O  OG  . SER A 1 79  ? 29.47100  22.04700  68.20100  1.000 70.16358  ?  79  SER A OG  1 
ATOM   620  N  N   . VAL A 1 80  ? 27.53900  20.97000  72.11100  1.000 68.11808  ?  80  VAL A N   1 
ATOM   621  C  CA  . VAL A 1 80  ? 27.29000  20.87500  73.54700  1.000 63.45677  ?  80  VAL A CA  1 
ATOM   622  C  C   . VAL A 1 80  ? 27.41200  19.42800  74.01000  1.000 62.61764  ?  80  VAL A C   1 
ATOM   623  O  O   . VAL A 1 80  ? 28.11900  19.12400  74.97900  1.000 69.59603  ?  80  VAL A O   1 
ATOM   624  C  CB  . VAL A 1 80  ? 25.90900  21.46100  73.89400  1.000 62.77064  ?  80  VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 80  ? 25.60900  21.28000  75.37500  1.000 61.81749  ?  80  VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 80  ? 25.84100  22.93000  73.50300  1.000 62.58045  ?  80  VAL A CG2 1 
ATOM   627  N  N   . VAL A 1 81  ? 26.72600  18.51500  73.31900  1.000 57.89205  ?  81  VAL A N   1 
ATOM   628  C  CA  . VAL A 1 81  ? 26.74100  17.10700  73.71000  1.000 60.38154  ?  81  VAL A CA  1 
ATOM   629  C  C   . VAL A 1 81  ? 28.15300  16.53600  73.63700  1.000 64.58733  ?  81  VAL A C   1 
ATOM   630  O  O   . VAL A 1 81  ? 28.59200  15.81700  74.54100  1.000 69.46118  ?  81  VAL A O   1 
ATOM   631  C  CB  . VAL A 1 81  ? 25.75600  16.30200  72.84200  1.000 64.30479  ?  81  VAL A CB  1 
ATOM   632  C  CG1 . VAL A 1 81  ? 25.84100  14.82400  73.17100  1.000 57.94372  ?  81  VAL A CG1 1 
ATOM   633  C  CG2 . VAL A 1 81  ? 24.33500  16.79800  73.06500  1.000 62.80011  ?  81  VAL A CG2 1 
ATOM   634  N  N   . GLN A 1 82  ? 28.88500  16.84400  72.56400  1.000 64.82982  ?  82  GLN A N   1 
ATOM   635  C  CA  . GLN A 1 82  ? 30.23500  16.30400  72.42200  1.000 68.58712  ?  82  GLN A CA  1 
ATOM   636  C  C   . GLN A 1 82  ? 31.16400  16.83900  73.50400  1.000 68.70940  ?  82  GLN A C   1 
ATOM   637  O  O   . GLN A 1 82  ? 31.96600  16.08500  74.06700  1.000 69.51668  ?  82  GLN A O   1 
ATOM   638  C  CB  . GLN A 1 82  ? 30.79500  16.62100  71.03600  1.000 70.54761  ?  82  GLN A CB  1 
ATOM   639  C  CG  . GLN A 1 82  ? 32.04500  15.82500  70.67800  1.000 71.52981  ?  82  GLN A CG  1 
ATOM   640  C  CD  . GLN A 1 82  ? 33.32600  16.52200  71.09400  1.000 65.58088  ?  82  GLN A CD  1 
ATOM   641  O  OE1 . GLN A 1 82  ? 33.39100  17.74800  71.13900  1.000 64.76702  ?  82  GLN A OE1 1 
ATOM   642  N  NE2 . GLN A 1 82  ? 34.35400  15.73900  71.39900  1.000 65.83319  ?  82  GLN A NE2 1 
ATOM   643  N  N   . TYR A 1 83  ? 31.07800  18.13700  73.80200  1.000 66.62511  ?  83  TYR A N   1 
ATOM   644  C  CA  . TYR A 1 83  ? 31.91400  18.70400  74.85500  1.000 69.37347  ?  83  TYR A CA  1 
ATOM   645  C  C   . TYR A 1 83  ? 31.58500  18.09600  76.21300  1.000 71.46366  ?  83  TYR A C   1 
ATOM   646  O  O   . TYR A 1 83  ? 32.48900  17.80800  77.00600  1.000 70.70258  ?  83  TYR A O   1 
ATOM   647  C  CB  . TYR A 1 83  ? 31.75700  20.22400  74.89300  1.000 69.28562  ?  83  TYR A CB  1 
ATOM   648  C  CG  . TYR A 1 83  ? 32.67500  20.89900  75.88700  1.000 73.68909  ?  83  TYR A CG  1 
ATOM   649  C  CD1 . TYR A 1 83  ? 34.05000  20.91500  75.69100  1.000 70.31149  ?  83  TYR A CD1 1 
ATOM   650  C  CD2 . TYR A 1 83  ? 32.16400  21.52800  77.01700  1.000 74.66642  ?  83  TYR A CD2 1 
ATOM   651  C  CE1 . TYR A 1 83  ? 34.89300  21.52800  76.59600  1.000 70.34615  ?  83  TYR A CE1 1 
ATOM   652  C  CE2 . TYR A 1 83  ? 32.99900  22.14800  77.92700  1.000 70.38633  ?  83  TYR A CE2 1 
ATOM   653  C  CZ  . TYR A 1 83  ? 34.36200  22.14500  77.71200  1.000 73.12969  ?  83  TYR A CZ  1 
ATOM   654  O  OH  . TYR A 1 83  ? 35.19800  22.76000  78.61500  1.000 82.32875  ?  83  TYR A OH  1 
ATOM   655  N  N   . ALA A 1 84  ? 30.29900  17.89100  76.49900  1.000 69.75153  ?  84  ALA A N   1 
ATOM   656  C  CA  . ALA A 1 84  ? 29.91200  17.28500  77.76800  1.000 67.11815  ?  84  ALA A CA  1 
ATOM   657  C  C   . ALA A 1 84  ? 30.40500  15.84500  77.86600  1.000 70.88675  ?  84  ALA A C   1 
ATOM   658  O  O   . ALA A 1 84  ? 31.01500  15.45500  78.86800  1.000 68.24470  ?  84  ALA A O   1 
ATOM   659  C  CB  . ALA A 1 84  ? 28.39500  17.35200  77.94100  1.000 59.95620  ?  84  ALA A CB  1 
ATOM   660  N  N   . VAL A 1 85  ? 30.15800  15.04200  76.83100  1.000 64.66968  ?  85  VAL A N   1 
ATOM   661  C  CA  . VAL A 1 85  ? 30.45200  13.61500  76.91400  1.000 63.12240  ?  85  VAL A CA  1 
ATOM   662  C  C   . VAL A 1 85  ? 31.94900  13.34900  76.79000  1.000 69.06698  ?  85  VAL A C   1 
ATOM   663  O  O   . VAL A 1 85  ? 32.50800  12.53800  77.53600  1.000 73.89983  ?  85  VAL A O   1 
ATOM   664  C  CB  . VAL A 1 85  ? 29.65000  12.84500  75.85100  1.000 61.58261  ?  85  VAL A CB  1 
ATOM   665  C  CG1 . VAL A 1 85  ? 30.04500  11.37900  75.85000  1.000 65.18662  ?  85  VAL A CG1 1 
ATOM   666  C  CG2 . VAL A 1 85  ? 28.15700  12.99300  76.10300  1.000 59.66303  ?  85  VAL A CG2 1 
ATOM   667  N  N   . ASP A 1 86  ? 32.62700  14.02300  75.86100  1.000 71.55264  ?  86  ASP A N   1 
ATOM   668  C  CA  . ASP A 1 86  ? 34.02500  13.70700  75.58600  1.000 75.64084  ?  86  ASP A CA  1 
ATOM   669  C  C   . ASP A 1 86  ? 35.00800  14.49800  76.43600  1.000 72.96432  ?  86  ASP A C   1 
ATOM   670  O  O   . ASP A 1 86  ? 36.08700  13.98400  76.75100  1.000 77.19359  ?  86  ASP A O   1 
ATOM   671  C  CB  . ASP A 1 86  ? 34.34400  13.94000  74.10600  1.000 73.51100  ?  86  ASP A CB  1 
ATOM   672  C  CG  . ASP A 1 86  ? 33.58200  13.00300  73.18900  1.000 76.51843  ?  86  ASP A CG  1 
ATOM   673  O  OD1 . ASP A 1 86  ? 32.88800  12.09900  73.69900  1.000 82.24651  ?  86  ASP A OD1 1 
ATOM   674  O  OD2 . ASP A 1 86  ? 33.67800  13.17000  71.95500  1.000 83.69049  -1 86  ASP A OD2 1 
ATOM   675  N  N   . VAL A 1 87  ? 34.67900  15.73100  76.81300  1.000 67.57637  ?  87  VAL A N   1 
ATOM   676  C  CA  . VAL A 1 87  ? 35.62400  16.56000  77.55500  1.000 72.12614  ?  87  VAL A CA  1 
ATOM   677  C  C   . VAL A 1 87  ? 35.24900  16.58800  79.03100  1.000 74.60800  ?  87  VAL A C   1 
ATOM   678  O  O   . VAL A 1 87  ? 36.06200  16.23800  79.89400  1.000 74.66101  ?  87  VAL A O   1 
ATOM   679  C  CB  . VAL A 1 87  ? 35.69100  17.98400  76.97400  1.000 72.82126  ?  87  VAL A CB  1 
ATOM   680  C  CG1 . VAL A 1 87  ? 36.80700  18.77500  77.63900  1.000 74.03146  ?  87  VAL A CG1 1 
ATOM   681  C  CG2 . VAL A 1 87  ? 35.88600  17.93000  75.46600  1.000 76.58216  ?  87  VAL A CG2 1 
ATOM   682  N  N   . LEU A 1 88  ? 34.02000  17.01200  79.33500  1.000 71.87032  ?  88  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 88  ? 33.57000  17.06500  80.72100  1.000 68.23066  ?  88  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 88  ? 33.21500  15.69100  81.27300  1.000 72.31698  ?  88  LEU A C   1 
ATOM   685  O  O   . LEU A 1 88  ? 33.21400  15.51300  82.49600  1.000 71.05502  ?  88  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 88  ? 32.35700  17.99000  80.85100  1.000 68.53205  ?  88  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 88  ? 32.52400  19.45600  80.44500  1.000 69.60307  ?  88  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 88  ? 31.24200  20.22900  80.73000  1.000 67.70094  ?  88  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 88  ? 33.71400  20.09700  81.14100  1.000 63.10453  ?  88  LEU A CD2 1 
ATOM   690  N  N   . GLU A 1 89  ? 32.91000  14.72700  80.40200  1.000 75.06829  ?  89  GLU A N   1 
ATOM   691  C  CA  . GLU A 1 89  ? 32.58700  13.35600  80.80100  1.000 73.32613  ?  89  GLU A CA  1 
ATOM   692  C  C   . GLU A 1 89  ? 31.40400  13.31900  81.77000  1.000 64.23522  ?  89  GLU A C   1 
ATOM   693  O  O   . GLU A 1 89  ? 31.47200  12.73300  82.85100  1.000 65.76249  ?  89  GLU A O   1 
ATOM   694  C  CB  . GLU A 1 89  ? 33.81000  12.63800  81.37600  1.000 64.67071  ?  89  GLU A CB  1 
ATOM   695  C  CG  . GLU A 1 89  ? 34.87700  12.36700  80.32000  1.000 78.07941  ?  89  GLU A CG  1 
ATOM   696  C  CD  . GLU A 1 89  ? 36.08800  11.62900  80.85600  1.000 84.68689  ?  89  GLU A CD  1 
ATOM   697  O  OE1 . GLU A 1 89  ? 36.28300  11.61300  82.08800  1.000 82.61960  ?  89  GLU A OE1 1 
ATOM   698  O  OE2 . GLU A 1 89  ? 36.83900  11.05400  80.03800  1.000 89.40075  -1 89  GLU A OE2 1 
ATOM   699  N  N   . VAL A 1 90  ? 30.30700  13.96800  81.36700  1.000 66.42367  ?  90  VAL A N   1 
ATOM   700  C  CA  . VAL A 1 90  ? 29.07000  13.87500  82.12700  1.000 65.15063  ?  90  VAL A CA  1 
ATOM   701  C  C   . VAL A 1 90  ? 28.57500  12.43300  82.09200  1.000 71.93134  ?  90  VAL A C   1 
ATOM   702  O  O   . VAL A 1 90  ? 28.80300  11.69100  81.12700  1.000 66.17854  ?  90  VAL A O   1 
ATOM   703  C  CB  . VAL A 1 90  ? 27.99800  14.83700  81.58700  1.000 62.40413  ?  90  VAL A CB  1 
ATOM   704  C  CG1 . VAL A 1 90  ? 28.48100  16.27700  81.67300  1.000 61.92504  ?  90  VAL A CG1 1 
ATOM   705  C  CG2 . VAL A 1 90  ? 27.61700  14.47400  80.15700  1.000 68.81135  ?  90  VAL A CG2 1 
ATOM   706  N  N   . GLU A 1 91  ? 27.90000  12.02800  83.16300  1.000 77.28109  ?  91  GLU A N   1 
ATOM   707  C  CA  . GLU A 1 91  ? 27.40900  10.66600  83.28100  1.000 74.22113  ?  91  GLU A CA  1 
ATOM   708  C  C   . GLU A 1 91  ? 25.92000  10.55700  83.00500  1.000 67.65118  ?  91  GLU A C   1 
ATOM   709  O  O   . GLU A 1 91  ? 25.40300  9.43900   82.90300  1.000 69.38998  ?  91  GLU A O   1 
ATOM   710  C  CB  . GLU A 1 91  ? 27.68800  10.13300  84.69100  1.000 73.97981  ?  91  GLU A CB  1 
ATOM   711  C  CG  . GLU A 1 91  ? 29.04100  10.54300  85.25000  1.000 80.92403  ?  91  GLU A CG  1 
ATOM   712  C  CD  . GLU A 1 91  ? 29.34500  9.88800   86.58600  1.000 94.15938  ?  91  GLU A CD  1 
ATOM   713  O  OE1 . GLU A 1 91  ? 28.44800  9.21400   87.13700  1.000 91.92551  ?  91  GLU A OE1 1 
ATOM   714  O  OE2 . GLU A 1 91  ? 30.46800  10.08400  87.10300  1.000 94.38159  -1 91  GLU A OE2 1 
ATOM   715  N  N   . HIS A 1 92  ? 25.22200  11.68400  82.89000  1.000 62.58362  ?  92  HIS A N   1 
ATOM   716  C  CA  . HIS A 1 92  ? 23.79200  11.69400  82.63500  1.000 63.41592  ?  92  HIS A CA  1 
ATOM   717  C  C   . HIS A 1 92  ? 23.43500  12.84400  81.70800  1.000 65.58873  ?  92  HIS A C   1 
ATOM   718  O  O   . HIS A 1 92  ? 23.92200  13.96400  81.88100  1.000 68.85932  ?  92  HIS A O   1 
ATOM   719  C  CB  . HIS A 1 92  ? 23.00100  11.82400  83.94000  1.000 63.75814  ?  92  HIS A CB  1 
ATOM   720  C  CG  . HIS A 1 92  ? 23.18500  10.66700  84.87100  1.000 65.40052  ?  92  HIS A CG  1 
ATOM   721  N  ND1 . HIS A 1 92  ? 22.61800  9.43200   84.64700  1.000 65.53023  ?  92  HIS A ND1 1 
ATOM   722  C  CD2 . HIS A 1 92  ? 23.88700  10.55700  86.02300  1.000 65.02271  ?  92  HIS A CD2 1 
ATOM   723  C  CE1 . HIS A 1 92  ? 22.95800  8.61100   85.62500  1.000 60.72338  ?  92  HIS A CE1 1 
ATOM   724  N  NE2 . HIS A 1 92  ? 23.72900  9.26900   86.47200  1.000 64.24358  ?  92  HIS A NE2 1 
ATOM   725  N  N   . ILE A 1 93  ? 22.60100  12.55800  80.71400  1.000 55.91206  ?  93  ILE A N   1 
ATOM   726  C  CA  . ILE A 1 93  ? 22.02000  13.58400  79.85900  1.000 62.06422  ?  93  ILE A CA  1 
ATOM   727  C  C   . ILE A 1 93  ? 20.51100  13.49600  80.01800  1.000 61.92287  ?  93  ILE A C   1 
ATOM   728  O  O   . ILE A 1 93  ? 19.92100  12.43000  79.80500  1.000 60.88154  ?  93  ILE A O   1 
ATOM   729  C  CB  . ILE A 1 93  ? 22.43300  13.41900  78.38900  1.000 62.99360  ?  93  ILE A CB  1 
ATOM   730  C  CG1 . ILE A 1 93  ? 23.95700  13.36400  78.26900  1.000 60.57285  ?  93  ILE A CG1 1 
ATOM   731  C  CG2 . ILE A 1 93  ? 21.89200  14.57400  77.56200  1.000 52.81823  ?  93  ILE A CG2 1 
ATOM   732  C  CD1 . ILE A 1 93  ? 24.45400  13.15900  76.86200  1.000 50.13429  ?  93  ILE A CD1 1 
ATOM   733  N  N   . ILE A 1 94  ? 19.88800  14.60900  80.39200  1.000 62.16955  ?  94  ILE A N   1 
ATOM   734  C  CA  . ILE A 1 94  ? 18.45800  14.65200  80.66500  1.000 60.64132  ?  94  ILE A CA  1 
ATOM   735  C  C   . ILE A 1 94  ? 17.81100  15.54400  79.61900  1.000 59.38135  ?  94  ILE A C   1 
ATOM   736  O  O   . ILE A 1 94  ? 18.09900  16.74600  79.55200  1.000 60.30593  ?  94  ILE A O   1 
ATOM   737  C  CB  . ILE A 1 94  ? 18.15900  15.17200  82.08100  1.000 60.07325  ?  94  ILE A CB  1 
ATOM   738  C  CG1 . ILE A 1 94  ? 18.71400  14.21900  83.13900  1.000 61.74732  ?  94  ILE A CG1 1 
ATOM   739  C  CG2 . ILE A 1 94  ? 16.66100  15.35700  82.27200  1.000 59.15034  ?  94  ILE A CG2 1 
ATOM   740  C  CD1 . ILE A 1 94  ? 19.21700  14.92600  84.38500  1.000 63.00597  ?  94  ILE A CD1 1 
ATOM   741  N  N   . ILE A 1 95  ? 16.93400  14.96100  78.80900  1.000 54.62382  ?  95  ILE A N   1 
ATOM   742  C  CA  . ILE A 1 95  ? 16.10400  15.71600  77.88300  1.000 56.54367  ?  95  ILE A CA  1 
ATOM   743  C  C   . ILE A 1 95  ? 14.73800  15.85400  78.53400  1.000 56.03154  ?  95  ILE A C   1 
ATOM   744  O  O   . ILE A 1 95  ? 14.06100  14.85100  78.79100  1.000 55.21928  ?  95  ILE A O   1 
ATOM   745  C  CB  . ILE A 1 95  ? 15.99900  15.02700  76.51400  1.000 53.80525  ?  95  ILE A CB  1 
ATOM   746  C  CG1 . ILE A 1 95  ? 17.38100  14.85700  75.88900  1.000 51.45354  ?  95  ILE A CG1 1 
ATOM   747  C  CG2 . ILE A 1 95  ? 15.12300  15.84500  75.58000  1.000 52.99301  ?  95  ILE A CG2 1 
ATOM   748  C  CD1 . ILE A 1 95  ? 17.34300  14.20500  74.52800  1.000 52.62358  ?  95  ILE A CD1 1 
ATOM   749  N  N   . CYS A 1 96  ? 14.33700  17.08800  78.81400  1.000 48.94090  ?  96  CYS A N   1 
ATOM   750  C  CA  . CYS A 1 96  ? 13.13000  17.35100  79.58300  1.000 48.37796  ?  96  CYS A CA  1 
ATOM   751  C  C   . CYS A 1 96  ? 12.27000  18.34900  78.83000  1.000 50.71736  ?  96  CYS A C   1 
ATOM   752  O  O   . CYS A 1 96  ? 12.71200  19.46800  78.55000  1.000 53.17808  ?  96  CYS A O   1 
ATOM   753  C  CB  . CYS A 1 96  ? 13.47500  17.87700  80.97800  1.000 63.05348  ?  96  CYS A CB  1 
ATOM   754  S  SG  . CYS A 1 96  ? 12.06200  18.04800  82.09400  1.000 69.95967  ?  96  CYS A SG  1 
ATOM   755  N  N   . GLY A 1 97  ? 11.04800  17.93800  78.49200  1.000 55.17257  ?  97  GLY A N   1 
ATOM   756  C  CA  . GLY A 1 97  ? 10.04900  18.83600  77.96500  1.000 53.85910  ?  97  GLY A CA  1 
ATOM   757  C  C   . GLY A 1 97  ? 9.07000   19.25200  79.05200  1.000 61.90713  ?  97  GLY A C   1 
ATOM   758  O  O   . GLY A 1 97  ? 9.18400   18.87200  80.21300  1.000 66.79432  ?  97  GLY A O   1 
ATOM   759  N  N   . HIS A 1 98  ? 8.09400   20.05900  78.65200  1.000 58.00089  ?  98  HIS A N   1 
ATOM   760  C  CA  . HIS A 1 98  ? 7.11600   20.54500  79.61300  1.000 57.48402  ?  98  HIS A CA  1 
ATOM   761  C  C   . HIS A 1 98  ? 5.76700   20.66300  78.92300  1.000 58.49522  ?  98  HIS A C   1 
ATOM   762  O  O   . HIS A 1 98  ? 5.67000   21.25300  77.84400  1.000 74.22430  ?  98  HIS A O   1 
ATOM   763  C  CB  . HIS A 1 98  ? 7.54800   21.88900  80.21100  1.000 62.06988  ?  98  HIS A CB  1 
ATOM   764  C  CG  . HIS A 1 98  ? 7.72400   22.97800  79.20100  1.000 59.49905  ?  98  HIS A CG  1 
ATOM   765  N  ND1 . HIS A 1 98  ? 6.88400   24.06800  79.13300  1.000 60.72613  ?  98  HIS A ND1 1 
ATOM   766  C  CD2 . HIS A 1 98  ? 8.63000   23.13800  78.20700  1.000 62.85986  ?  98  HIS A CD2 1 
ATOM   767  C  CE1 . HIS A 1 98  ? 7.27400   24.86200  78.15100  1.000 67.63989  ?  98  HIS A CE1 1 
ATOM   768  N  NE2 . HIS A 1 98  ? 8.32900   24.31800  77.57100  1.000 68.70591  ?  98  HIS A NE2 1 
ATOM   769  N  N   . TYR A 1 99  ? 4.74100   20.08800  79.54600  1.000 59.41156  ?  99  TYR A N   1 
ATOM   770  C  CA  . TYR A 1 99  ? 3.39800   20.13900  78.98500  1.000 60.70704  ?  99  TYR A CA  1 
ATOM   771  C  C   . TYR A 1 99  ? 2.93700   21.58200  78.84800  1.000 64.15822  ?  99  TYR A C   1 
ATOM   772  O  O   . TYR A 1 99  ? 3.17200   22.41500  79.72700  1.000 65.54177  ?  99  TYR A O   1 
ATOM   773  C  CB  . TYR A 1 99  ? 2.43100   19.34400  79.86400  1.000 63.17506  ?  99  TYR A CB  1 
ATOM   774  C  CG  . TYR A 1 99  ? 2.88900   17.92700  80.12400  1.000 66.49270  ?  99  TYR A CG  1 
ATOM   775  C  CD1 . TYR A 1 99  ? 2.60900   16.91200  79.22100  1.000 59.96543  ?  99  TYR A CD1 1 
ATOM   776  C  CD2 . TYR A 1 99  ? 3.62200   17.61000  81.25900  1.000 72.04373  ?  99  TYR A CD2 1 
ATOM   777  C  CE1 . TYR A 1 99  ? 3.03000   15.61800  79.45000  1.000 60.92543  ?  99  TYR A CE1 1 
ATOM   778  C  CE2 . TYR A 1 99  ? 4.05100   16.31700  81.49500  1.000 72.24563  ?  99  TYR A CE2 1 
ATOM   779  C  CZ  . TYR A 1 99  ? 3.75200   15.32500  80.58600  1.000 69.54672  ?  99  TYR A CZ  1 
ATOM   780  O  OH  . TYR A 1 99  ? 4.17500   14.03600  80.81700  1.000 71.04456  ?  99  TYR A OH  1 
ATOM   781  N  N   . GLY A 1 100 ? 2.29500   21.88000  77.72400  1.000 71.79808  ?  100 GLY A N   1 
ATOM   782  C  CA  . GLY A 1 100 ? 1.88900   23.23400  77.42500  1.000 67.21452  ?  100 GLY A CA  1 
ATOM   783  C  C   . GLY A 1 100 ? 2.92000   24.04700  76.68000  1.000 72.60621  ?  100 GLY A C   1 
ATOM   784  O  O   . GLY A 1 100 ? 2.72000   25.25500  76.50300  1.000 80.42060  ?  100 GLY A O   1 
ATOM   785  N  N   . CYS A 1 101 ? 4.01800   23.42400  76.24700  1.000 67.34535  ?  101 CYS A N   1 
ATOM   786  C  CA  . CYS A 1 101 ? 5.09600   24.12700  75.56300  1.000 61.70277  ?  101 CYS A CA  1 
ATOM   787  C  C   . CYS A 1 101 ? 4.55900   24.91600  74.37600  1.000 63.15319  ?  101 CYS A C   1 
ATOM   788  O  O   . CYS A 1 101 ? 3.78700   24.39500  73.56600  1.000 70.12486  ?  101 CYS A O   1 
ATOM   789  C  CB  . CYS A 1 101 ? 6.15300   23.11900  75.10500  1.000 58.80254  ?  101 CYS A CB  1 
ATOM   790  S  SG  . CYS A 1 101 ? 7.52500   23.81000  74.15700  1.000 76.44443  ?  101 CYS A SG  1 
ATOM   791  N  N   . GLY A 1 102 ? 4.95700   26.18700  74.29200  1.000 66.02918  ?  102 GLY A N   1 
ATOM   792  C  CA  . GLY A 1 102 ? 4.48000   27.03400  73.20800  1.000 69.12464  ?  102 GLY A CA  1 
ATOM   793  C  C   . GLY A 1 102 ? 4.94000   26.56600  71.84100  1.000 63.56205  ?  102 GLY A C   1 
ATOM   794  O  O   . GLY A 1 102 ? 4.19900   26.66400  70.86000  1.000 66.31218  ?  102 GLY A O   1 
ATOM   795  N  N   . GLY A 1 103 ? 6.16500   26.04600  71.75700  1.000 58.03901  ?  103 GLY A N   1 
ATOM   796  C  CA  . GLY A 1 103 ? 6.66400   25.55300  70.48400  1.000 64.66799  ?  103 GLY A CA  1 
ATOM   797  C  C   . GLY A 1 103 ? 5.91200   24.32500  70.01000  1.000 63.27808  ?  103 GLY A C   1 
ATOM   798  O  O   . GLY A 1 103 ? 5.58300   24.20400  68.82700  1.000 66.32836  ?  103 GLY A O   1 
ATOM   799  N  N   . VAL A 1 104 ? 5.64100   23.39400  70.92700  1.000 57.89863  ?  104 VAL A N   1 
ATOM   800  C  CA  . VAL A 1 104 ? 4.91500   22.17600  70.57900  1.000 60.72584  ?  104 VAL A CA  1 
ATOM   801  C  C   . VAL A 1 104 ? 3.51100   22.51200  70.09000  1.000 62.06314  ?  104 VAL A C   1 
ATOM   802  O  O   . VAL A 1 104 ? 2.99100   21.87800  69.16400  1.000 63.47585  ?  104 VAL A O   1 
ATOM   803  C  CB  . VAL A 1 104 ? 4.88700   21.22000  71.78600  1.000 56.33851  ?  104 VAL A CB  1 
ATOM   804  C  CG1 . VAL A 1 104 ? 4.09300   19.96600  71.46500  1.000 56.56428  ?  104 VAL A CG1 1 
ATOM   805  C  CG2 . VAL A 1 104 ? 6.30500   20.86200  72.20900  1.000 52.79808  ?  104 VAL A CG2 1 
ATOM   806  N  N   . GLN A 1 105 ? 2.87900   23.51800  70.69900  1.000 59.13459  ?  105 GLN A N   1 
ATOM   807  C  CA  . GLN A 1 105 ? 1.54400   23.92200  70.26600  1.000 65.94746  ?  105 GLN A CA  1 
ATOM   808  C  C   . GLN A 1 105 ? 1.57700   24.60100  68.90200  1.000 70.93748  ?  105 GLN A C   1 
ATOM   809  O  O   . GLN A 1 105 ? 0.68500   24.38300  68.07400  1.000 69.93970  ?  105 GLN A O   1 
ATOM   810  C  CB  . GLN A 1 105 ? 0.91200   24.84600  71.30500  1.000 65.41019  ?  105 GLN A CB  1 
ATOM   811  C  CG  . GLN A 1 105 ? -0.53600  25.19700  71.01100  1.000 68.95321  ?  105 GLN A CG  1 
ATOM   812  C  CD  . GLN A 1 105 ? -1.07400  26.28000  71.92400  1.000 89.11841  ?  105 GLN A CD  1 
ATOM   813  O  OE1 . GLN A 1 105 ? -0.86700  26.24500  73.13800  1.000 95.26180  ?  105 GLN A OE1 1 
ATOM   814  N  NE2 . GLN A 1 105 ? -1.76900  27.25300  71.34300  1.000 89.31300  ?  105 GLN A NE2 1 
ATOM   815  N  N   . ALA A 1 106 ? 2.59300   25.43100  68.65100  1.000 65.74600  ?  106 ALA A N   1 
ATOM   816  C  CA  . ALA A 1 106 ? 2.70100   26.09700  67.35700  1.000 66.45480  ?  106 ALA A CA  1 
ATOM   817  C  C   . ALA A 1 106 ? 2.92100   25.09300  66.23100  1.000 67.31725  ?  106 ALA A C   1 
ATOM   818  O  O   . ALA A 1 106 ? 2.42300   25.28300  65.11600  1.000 70.99602  ?  106 ALA A O   1 
ATOM   819  C  CB  . ALA A 1 106 ? 3.83100   27.12400  67.38900  1.000 65.58308  ?  106 ALA A CB  1 
ATOM   820  N  N   . ALA A 1 107 ? 3.67400   24.02500  66.50100  1.000 64.66991  ?  107 ALA A N   1 
ATOM   821  C  CA  . ALA A 1 107 ? 3.86000   22.97600  65.50300  1.000 65.70341  ?  107 ALA A CA  1 
ATOM   822  C  C   . ALA A 1 107 ? 2.52600   22.39600  65.04700  1.000 67.87029  ?  107 ALA A C   1 
ATOM   823  O  O   . ALA A 1 107 ? 2.32900   22.13800  63.85500  1.000 73.83114  ?  107 ALA A O   1 
ATOM   824  C  CB  . ALA A 1 107 ? 4.76400   21.87700  66.06100  1.000 60.96133  ?  107 ALA A CB  1 
ATOM   825  N  N   . VAL A 1 108 ? 1.59500   22.19000  65.97800  1.000 68.72692  ?  108 VAL A N   1 
ATOM   826  C  CA  . VAL A 1 108 ? 0.33500   21.54100  65.63100  1.000 71.38548  ?  108 VAL A CA  1 
ATOM   827  C  C   . VAL A 1 108 ? -0.59300  22.51100  64.91300  1.000 69.52492  ?  108 VAL A C   1 
ATOM   828  O  O   . VAL A 1 108 ? -1.16900  22.18600  63.86900  1.000 76.06455  ?  108 VAL A O   1 
ATOM   829  C  CB  . VAL A 1 108 ? -0.33300  20.97000  66.89600  1.000 71.94929  ?  108 VAL A CB  1 
ATOM   830  C  CG1 . VAL A 1 108 ? -1.69600  20.38500  66.56000  1.000 75.90405  ?  108 VAL A CG1 1 
ATOM   831  C  CG2 . VAL A 1 108 ? 0.55600   19.93300  67.54000  1.000 63.01754  ?  108 VAL A CG2 1 
ATOM   832  N  N   . GLU A 1 109 ? -0.74900  23.71700  65.45800  1.000 68.14475  ?  109 GLU A N   1 
ATOM   833  C  CA  . GLU A 1 109 ? -1.64500  24.70100  64.86600  1.000 73.46186  ?  109 GLU A CA  1 
ATOM   834  C  C   . GLU A 1 109 ? -1.04400  25.37200  63.64100  1.000 81.22235  ?  109 GLU A C   1 
ATOM   835  O  O   . GLU A 1 109 ? -1.78600  25.95400  62.84300  1.000 77.53781  ?  109 GLU A O   1 
ATOM   836  C  CB  . GLU A 1 109 ? -2.01400  25.74900  65.91400  1.000 72.85785  ?  109 GLU A CB  1 
ATOM   837  C  CG  . GLU A 1 109 ? -2.60900  25.13900  67.17100  1.000 83.68008  ?  109 GLU A CG  1 
ATOM   838  C  CD  . GLU A 1 109 ? -2.53700  26.06700  68.36400  1.000 89.56461  ?  109 GLU A CD  1 
ATOM   839  O  OE1 . GLU A 1 109 ? -1.63100  26.92800  68.39300  1.000 88.42398  ?  109 GLU A OE1 1 
ATOM   840  O  OE2 . GLU A 1 109 ? -3.37700  25.92500  69.27900  1.000 93.31027  -1 109 GLU A OE2 1 
ATOM   841  N  N   . ASN A 1 110 ? 0.27500   25.28500  63.47900  1.000 77.91384  ?  110 ASN A N   1 
ATOM   842  C  CA  . ASN A 1 110 ? 1.01900   25.80500  62.33400  1.000 77.25433  ?  110 ASN A CA  1 
ATOM   843  C  C   . ASN A 1 110 ? 0.59300   27.22600  61.94500  1.000 79.39686  ?  110 ASN A C   1 
ATOM   844  O  O   . ASN A 1 110 ? 0.12300   27.44800  60.82200  1.000 79.56908  ?  110 ASN A O   1 
ATOM   845  C  CB  . ASN A 1 110 ? 0.91100   24.85800  61.14300  1.000 77.36261  ?  110 ASN A CB  1 
ATOM   846  C  CG  . ASN A 1 110 ? 1.99900   25.09100  60.10800  1.000 71.50929  ?  110 ASN A CG  1 
ATOM   847  O  OD1 . ASN A 1 110 ? 2.82900   25.99100  60.24800  1.000 69.51583  ?  110 ASN A OD1 1 
ATOM   848  N  ND2 . ASN A 1 110 ? 2.01400   24.26000  59.07200  1.000 78.51366  ?  110 ASN A ND2 1 
ATOM   849  N  N   . PRO A 1 111 ? 0.73800   28.20200  62.83800  1.000 78.42889  ?  111 PRO A N   1 
ATOM   850  C  CA  . PRO A 1 111 ? 0.56600   29.59500  62.42500  1.000 76.40825  ?  111 PRO A CA  1 
ATOM   851  C  C   . PRO A 1 111 ? 1.83800   30.10300  61.76300  1.000 73.36185  ?  111 PRO A C   1 
ATOM   852  O  O   . PRO A 1 111 ? 2.94100   29.61100  62.00500  1.000 72.85970  ?  111 PRO A O   1 
ATOM   853  C  CB  . PRO A 1 111 ? 0.29100   30.32700  63.74100  1.000 77.80148  ?  111 PRO A CB  1 
ATOM   854  C  CG  . PRO A 1 111 ? 1.02700   29.53200  64.75700  1.000 76.04926  ?  111 PRO A CG  1 
ATOM   855  C  CD  . PRO A 1 111 ? 1.08400   28.10100  64.27000  1.000 73.29862  ?  111 PRO A CD  1 
ATOM   856  N  N   . GLU A 1 112 ? 1.66700   31.11800  60.92400  1.000 74.00464  ?  112 GLU A N   1 
ATOM   857  C  CA  . GLU A 1 112 ? 2.79500   31.69900  60.20100  1.000 80.02952  ?  112 GLU A CA  1 
ATOM   858  C  C   . GLU A 1 112 ? 3.57500   32.59700  61.15000  1.000 72.33044  ?  112 GLU A C   1 
ATOM   859  O  O   . GLU A 1 112 ? 3.23900   33.76800  61.34200  1.000 77.03830  ?  112 GLU A O   1 
ATOM   860  C  CB  . GLU A 1 112 ? 2.31100   32.44800  58.96600  1.000 87.10601  ?  112 GLU A CB  1 
ATOM   861  C  CG  . GLU A 1 112 ? 1.84200   31.51200  57.86200  1.000 81.85308  ?  112 GLU A CG  1 
ATOM   862  C  CD  . GLU A 1 112 ? 1.22100   32.24300  56.69500  1.000 92.77548  ?  112 GLU A CD  1 
ATOM   863  O  OE1 . GLU A 1 112 ? 1.68000   33.36200  56.38200  1.000 95.97361  ?  112 GLU A OE1 1 
ATOM   864  O  OE2 . GLU A 1 112 ? 0.27600   31.69600  56.08700  1.000 101.72801 -1 112 GLU A OE2 1 
ATOM   865  N  N   . LEU A 1 113 ? 4.62500   32.03800  61.74800  1.000 67.23145  ?  113 LEU A N   1 
ATOM   866  C  CA  . LEU A 1 113 ? 5.44300   32.73600  62.72800  1.000 73.90475  ?  113 LEU A CA  1 
ATOM   867  C  C   . LEU A 1 113 ? 6.77700   33.20400  62.16400  1.000 72.50477  ?  113 LEU A C   1 
ATOM   868  O  O   . LEU A 1 113 ? 7.48200   33.96700  62.83300  1.000 76.65114  ?  113 LEU A O   1 
ATOM   869  C  CB  . LEU A 1 113 ? 5.68600   31.83200  63.94100  1.000 71.25675  ?  113 LEU A CB  1 
ATOM   870  C  CG  . LEU A 1 113 ? 4.42600   31.21000  64.54500  1.000 76.55013  ?  113 LEU A CG  1 
ATOM   871  C  CD1 . LEU A 1 113 ? 4.77500   30.27600  65.69200  1.000 74.66673  ?  113 LEU A CD1 1 
ATOM   872  C  CD2 . LEU A 1 113 ? 3.46200   32.29400  65.00000  1.000 74.97078  ?  113 LEU A CD2 1 
ATOM   873  N  N   . GLY A 1 114 ? 7.14000   32.76400  60.96200  1.000 55.93327  ?  114 GLY A N   1 
ATOM   874  C  CA  . GLY A 1 114 ? 8.38600   33.16900  60.34400  1.000 55.31572  ?  114 GLY A CA  1 
ATOM   875  C  C   . GLY A 1 114 ? 9.45500   32.09500  60.35000  1.000 58.24374  ?  114 GLY A C   1 
ATOM   876  O  O   . GLY A 1 114 ? 9.15300   30.90800  60.18800  1.000 64.17883  ?  114 GLY A O   1 
ATOM   877  N  N   . LEU A 1 115 ? 10.71200  32.51000  60.53900  1.000 50.29488  ?  115 LEU A N   1 
ATOM   878  C  CA  . LEU A 1 115 ? 11.83900  31.58400  60.45600  1.000 51.86456  ?  115 LEU A CA  1 
ATOM   879  C  C   . LEU A 1 115 ? 11.70900  30.42100  61.43600  1.000 65.58503  ?  115 LEU A C   1 
ATOM   880  O  O   . LEU A 1 115 ? 12.18800  29.31700  61.15000  1.000 64.55608  ?  115 LEU A O   1 
ATOM   881  C  CB  . LEU A 1 115 ? 13.14900  32.34400  60.67700  1.000 47.40937  ?  115 LEU A CB  1 
ATOM   882  C  CG  . LEU A 1 115 ? 14.45500  31.54800  60.72500  1.000 52.18185  ?  115 LEU A CG  1 
ATOM   883  C  CD1 . LEU A 1 115 ? 14.68200  30.80000  59.42500  1.000 63.09811  ?  115 LEU A CD1 1 
ATOM   884  C  CD2 . LEU A 1 115 ? 15.61800  32.48700  60.99700  1.000 51.06354  ?  115 LEU A CD2 1 
ATOM   885  N  N   . ILE A 1 116 ? 11.06000  30.64200  62.58500  1.000 61.35336  ?  116 ILE A N   1 
ATOM   886  C  CA  . ILE A 1 116 ? 10.97700  29.60500  63.61300  1.000 60.29050  ?  116 ILE A CA  1 
ATOM   887  C  C   . ILE A 1 116 ? 10.20000  28.39300  63.11200  1.000 64.22215  ?  116 ILE A C   1 
ATOM   888  O  O   . ILE A 1 116 ? 10.43200  27.26600  63.56900  1.000 63.49275  ?  116 ILE A O   1 
ATOM   889  C  CB  . ILE A 1 116 ? 10.34800  30.19400  64.89400  1.000 67.86039  ?  116 ILE A CB  1 
ATOM   890  C  CG1 . ILE A 1 116 ? 10.28500  29.15400  66.01800  1.000 66.34046  ?  116 ILE A CG1 1 
ATOM   891  C  CG2 . ILE A 1 116 ? 8.96400   30.74100  64.60200  1.000 62.18199  ?  116 ILE A CG2 1 
ATOM   892  C  CD1 . ILE A 1 116 ? 11.63400  28.70100  66.51200  1.000 60.44090  ?  116 ILE A CD1 1 
ATOM   893  N  N   . ASN A 1 117 ? 9.27700   28.59600  62.16500  1.000 65.75493  ?  117 ASN A N   1 
ATOM   894  C  CA  . ASN A 1 117 ? 8.45700   27.49600  61.66300  1.000 61.28021  ?  117 ASN A CA  1 
ATOM   895  C  C   . ASN A 1 117 ? 9.30200   26.38100  61.06000  1.000 55.62147  ?  117 ASN A C   1 
ATOM   896  O  O   . ASN A 1 117 ? 8.91000   25.20900  61.11300  1.000 53.22883  ?  117 ASN A O   1 
ATOM   897  C  CB  . ASN A 1 117 ? 7.44000   28.01800  60.65100  1.000 52.97581  ?  117 ASN A CB  1 
ATOM   898  C  CG  . ASN A 1 117 ? 6.21400   28.60800  61.31800  1.000 67.27036  ?  117 ASN A CG  1 
ATOM   899  O  OD1 . ASN A 1 117 ? 6.25100   28.98100  62.49100  1.000 75.93190  ?  117 ASN A OD1 1 
ATOM   900  N  ND2 . ASN A 1 117 ? 5.11900   28.69700  60.57300  1.000 70.29659  ?  117 ASN A ND2 1 
ATOM   901  N  N   . ASN A 1 118 ? 10.44700  26.72000  60.46500  1.000 55.36828  ?  118 ASN A N   1 
ATOM   902  C  CA  . ASN A 1 118 ? 11.31300  25.68500  59.91000  1.000 61.10280  ?  118 ASN A CA  1 
ATOM   903  C  C   . ASN A 1 118 ? 11.85600  24.79200  61.01500  1.000 58.81650  ?  118 ASN A C   1 
ATOM   904  O  O   . ASN A 1 118 ? 11.95600  23.57100  60.84700  1.000 62.26236  ?  118 ASN A O   1 
ATOM   905  C  CB  . ASN A 1 118 ? 12.45800  26.32000  59.12100  1.000 62.14328  ?  118 ASN A CB  1 
ATOM   906  C  CG  . ASN A 1 118 ? 11.96700  27.24900  58.02900  1.000 56.74123  ?  118 ASN A CG  1 
ATOM   907  O  OD1 . ASN A 1 118 ? 11.39900  26.80700  57.03200  1.000 60.42486  ?  118 ASN A OD1 1 
ATOM   908  N  ND2 . ASN A 1 118 ? 12.18800  28.54500  58.21200  1.000 61.43378  ?  118 ASN A ND2 1 
ATOM   909  N  N   . TRP A 1 119 ? 12.22100  25.39000  62.14900  1.000 67.43342  ?  119 TRP A N   1 
ATOM   910  C  CA  . TRP A 1 119 ? 12.64600  24.60900  63.30500  1.000 64.00514  ?  119 TRP A CA  1 
ATOM   911  C  C   . TRP A 1 119 ? 11.53700  23.67500  63.77400  1.000 60.14153  ?  119 TRP A C   1 
ATOM   912  O  O   . TRP A 1 119 ? 11.79000  22.50400  64.08200  1.000 63.18538  ?  119 TRP A O   1 
ATOM   913  C  CB  . TRP A 1 119 ? 13.07500  25.56100  64.42400  1.000 58.98626  ?  119 TRP A CB  1 
ATOM   914  C  CG  . TRP A 1 119 ? 13.66600  24.91400  65.64100  1.000 63.35577  ?  119 TRP A CG  1 
ATOM   915  C  CD1 . TRP A 1 119 ? 13.00700  24.55100  66.78200  1.000 57.91693  ?  119 TRP A CD1 1 
ATOM   916  C  CD2 . TRP A 1 119 ? 15.03900  24.56300  65.84400  1.000 60.46024  ?  119 TRP A CD2 1 
ATOM   917  N  NE1 . TRP A 1 119 ? 13.88700  23.99700  67.68100  1.000 51.77632  ?  119 TRP A NE1 1 
ATOM   918  C  CE2 . TRP A 1 119 ? 15.14000  23.99100  67.12800  1.000 53.80618  ?  119 TRP A CE2 1 
ATOM   919  C  CE3 . TRP A 1 119 ? 16.19300  24.67500  65.06300  1.000 61.64094  ?  119 TRP A CE3 1 
ATOM   920  C  CZ2 . TRP A 1 119 ? 16.34800  23.53000  67.64700  1.000 59.10406  ?  119 TRP A CZ2 1 
ATOM   921  C  CZ3 . TRP A 1 119 ? 17.39200  24.21800  65.58100  1.000 65.05430  ?  119 TRP A CZ3 1 
ATOM   922  C  CH2 . TRP A 1 119 ? 17.46000  23.65300  66.86000  1.000 61.22457  ?  119 TRP A CH2 1 
ATOM   923  N  N   . LEU A 1 120 ? 10.29500  24.16300  63.80000  1.000 56.31693  ?  120 LEU A N   1 
ATOM   924  C  CA  . LEU A 1 120 ? 9.18200   23.37600  64.31800  1.000 57.10579  ?  120 LEU A CA  1 
ATOM   925  C  C   . LEU A 1 120 ? 8.73700   22.26100  63.38100  1.000 59.71711  ?  120 LEU A C   1 
ATOM   926  O  O   . LEU A 1 120 ? 7.94500   21.41100  63.80400  1.000 58.27944  ?  120 LEU A O   1 
ATOM   927  C  CB  . LEU A 1 120 ? 7.99800   24.28700  64.63600  1.000 59.73419  ?  120 LEU A CB  1 
ATOM   928  C  CG  . LEU A 1 120 ? 8.34200   25.40700  65.62200  1.000 65.76218  ?  120 LEU A CG  1 
ATOM   929  C  CD1 . LEU A 1 120 ? 7.12000   26.26000  65.93600  1.000 65.18409  ?  120 LEU A CD1 1 
ATOM   930  C  CD2 . LEU A 1 120 ? 8.96900   24.84400  66.88800  1.000 57.64481  ?  120 LEU A CD2 1 
ATOM   931  N  N   . LEU A 1 121 ? 9.21100   22.23700  62.13100  1.000 65.19498  ?  121 LEU A N   1 
ATOM   932  C  CA  . LEU A 1 121 ? 8.83700   21.14500  61.23600  1.000 62.05331  ?  121 LEU A CA  1 
ATOM   933  C  C   . LEU A 1 121 ? 9.36000   19.80900  61.74600  1.000 64.39304  ?  121 LEU A C   1 
ATOM   934  O  O   . LEU A 1 121 ? 8.78600   18.75800  61.43700  1.000 61.42266  ?  121 LEU A O   1 
ATOM   935  C  CB  . LEU A 1 121 ? 9.35100   21.41200  59.82000  1.000 63.30566  ?  121 LEU A CB  1 
ATOM   936  C  CG  . LEU A 1 121 ? 8.54600   22.39500  58.96900  1.000 60.15334  ?  121 LEU A CG  1 
ATOM   937  C  CD1 . LEU A 1 121 ? 9.29400   22.72800  57.69000  1.000 61.60789  ?  121 LEU A CD1 1 
ATOM   938  C  CD2 . LEU A 1 121 ? 7.17000   21.82300  58.65500  1.000 58.20134  ?  121 LEU A CD2 1 
ATOM   939  N  N   . HIS A 1 122 ? 10.44500  19.83000  62.52700  1.000 62.15275  ?  122 HIS A N   1 
ATOM   940  C  CA  . HIS A 1 122 ? 10.92500  18.60300  63.15100  1.000 63.28121  ?  122 HIS A CA  1 
ATOM   941  C  C   . HIS A 1 122 ? 9.91100   18.05100  64.14500  1.000 60.02246  ?  122 HIS A C   1 
ATOM   942  O  O   . HIS A 1 122 ? 9.85100   16.83500  64.35800  1.000 59.81206  ?  122 HIS A O   1 
ATOM   943  C  CB  . HIS A 1 122 ? 12.26600  18.85400  63.83900  1.000 61.57074  ?  122 HIS A CB  1 
ATOM   944  C  CG  . HIS A 1 122 ? 13.38400  19.14900  62.88900  1.000 55.74636  ?  122 HIS A CG  1 
ATOM   945  N  ND1 . HIS A 1 122 ? 14.05900  18.16100  62.20400  1.000 57.24105  ?  122 HIS A ND1 1 
ATOM   946  C  CD2 . HIS A 1 122 ? 13.95100  20.32000  62.51400  1.000 57.85873  ?  122 HIS A CD2 1 
ATOM   947  C  CE1 . HIS A 1 122 ? 14.99100  18.71100  61.44600  1.000 58.43737  ?  122 HIS A CE1 1 
ATOM   948  N  NE2 . HIS A 1 122 ? 14.94700  20.02000  61.61600  1.000 63.16910  ?  122 HIS A NE2 1 
ATOM   949  N  N   . ILE A 1 123 ? 9.12300   18.92300  64.77500  1.000 55.72925  ?  123 ILE A N   1 
ATOM   950  C  CA  . ILE A 1 123 ? 8.05400   18.45000  65.64700  1.000 57.06245  ?  123 ILE A CA  1 
ATOM   951  C  C   . ILE A 1 123 ? 6.86400   17.97600  64.82500  1.000 59.24785  ?  123 ILE A C   1 
ATOM   952  O  O   . ILE A 1 123 ? 6.25600   16.94600  65.13400  1.000 60.55093  ?  123 ILE A O   1 
ATOM   953  C  CB  . ILE A 1 123 ? 7.64800   19.54100  66.65100  1.000 58.92258  ?  123 ILE A CB  1 
ATOM   954  C  CG1 . ILE A 1 123 ? 8.86100   19.99500  67.45700  1.000 52.22448  ?  123 ILE A CG1 1 
ATOM   955  C  CG2 . ILE A 1 123 ? 6.57200   19.02200  67.59100  1.000 52.50107  ?  123 ILE A CG2 1 
ATOM   956  C  CD1 . ILE A 1 123 ? 8.67900   21.35000  68.06500  1.000 52.54460  ?  123 ILE A CD1 1 
ATOM   957  N  N   . ARG A 1 124 ? 6.50400   18.72100  63.77400  1.000 62.15284  ?  124 ARG A N   1 
ATOM   958  C  CA  . ARG A 1 124 ? 5.42900   18.27200  62.89400  1.000 64.01413  ?  124 ARG A CA  1 
ATOM   959  C  C   . ARG A 1 124 ? 5.74600   16.91400  62.28700  1.000 62.15001  ?  124 ARG A C   1 
ATOM   960  O  O   . ARG A 1 124 ? 4.83300   16.12200  62.02900  1.000 58.44108  ?  124 ARG A O   1 
ATOM   961  C  CB  . ARG A 1 124 ? 5.15600   19.29900  61.79400  1.000 59.92992  ?  124 ARG A CB  1 
ATOM   962  C  CG  . ARG A 1 124 ? 4.53400   20.58000  62.30700  1.000 59.75537  ?  124 ARG A CG  1 
ATOM   963  C  CD  . ARG A 1 124 ? 4.10000   21.50200  61.18100  1.000 69.66522  ?  124 ARG A CD  1 
ATOM   964  N  NE  . ARG A 1 124 ? 3.07600   20.88800  60.34400  1.000 72.42707  ?  124 ARG A NE  1 
ATOM   965  C  CZ  . ARG A 1 124 ? 1.77100   21.00600  60.55200  1.000 74.53064  ?  124 ARG A CZ  1 
ATOM   966  N  NH1 . ARG A 1 124 ? 1.29200   21.69200  61.57600  1.000 75.77799  ?  124 ARG A NH1 1 
ATOM   967  N  NH2 . ARG A 1 124 ? 0.92300   20.42100  59.71100  1.000 69.57952  ?  124 ARG A NH2 1 
ATOM   968  N  N   . ASP A 1 125 ? 7.03000   16.62700  62.05700  1.000 61.80102  ?  125 ASP A N   1 
ATOM   969  C  CA  . ASP A 1 125 ? 7.42400   15.28300  61.64900  1.000 58.91989  ?  125 ASP A CA  1 
ATOM   970  C  C   . ASP A 1 125 ? 6.96300   14.25800  62.67600  1.000 60.96733  ?  125 ASP A C   1 
ATOM   971  O  O   . ASP A 1 125 ? 6.40200   13.21400  62.32400  1.000 56.65151  ?  125 ASP A O   1 
ATOM   972  C  CB  . ASP A 1 125 ? 8.94200   15.21300  61.47100  1.000 59.23942  ?  125 ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 125 ? 9.42300   15.95300  60.23900  1.000 77.12176  ?  125 ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 125 ? 8.57800   16.35100  59.40800  1.000 75.51757  ?  125 ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 125 ? 10.65200  16.14400  60.10900  1.000 80.66091  -1 125 ASP A OD2 1 
ATOM   976  N  N   . ILE A 1 126 ? 7.17400   14.55800  63.96100  1.000 67.98214  ?  126 ILE A N   1 
ATOM   977  C  CA  . ILE A 1 126 ? 6.74300   13.66300  65.03200  1.000 55.09630  ?  126 ILE A CA  1 
ATOM   978  C  C   . ILE A 1 126 ? 5.22600   13.53100  65.03900  1.000 56.32215  ?  126 ILE A C   1 
ATOM   979  O  O   . ILE A 1 126 ? 4.68200   12.44100  65.25400  1.000 55.82649  ?  126 ILE A O   1 
ATOM   980  C  CB  . ILE A 1 126 ? 7.26700   14.16700  66.39000  1.000 59.09946  ?  126 ILE A CB  1 
ATOM   981  C  CG1 . ILE A 1 126 ? 8.75000   14.53200  66.29700  1.000 55.50930  ?  126 ILE A CG1 1 
ATOM   982  C  CG2 . ILE A 1 126 ? 7.02300   13.13200  67.47800  1.000 59.54152  ?  126 ILE A CG2 1 
ATOM   983  C  CD1 . ILE A 1 126 ? 9.63800   13.39900  65.85500  1.000 53.10538  ?  126 ILE A CD1 1 
ATOM   984  N  N   . TRP A 1 127 ? 4.52100   14.63900  64.79500  1.000 59.49092  ?  127 TRP A N   1 
ATOM   985  C  CA  . TRP A 1 127 ? 3.06400   14.63400  64.89000  1.000 61.19366  ?  127 TRP A CA  1 
ATOM   986  C  C   . TRP A 1 127 ? 2.45600   13.70100  63.84700  1.000 66.46469  ?  127 TRP A C   1 
ATOM   987  O  O   . TRP A 1 127 ? 1.51800   12.95200  64.14500  1.000 70.51493  ?  127 TRP A O   1 
ATOM   988  C  CB  . TRP A 1 127 ? 2.53000   16.06100  64.74600  1.000 61.68838  ?  127 TRP A CB  1 
ATOM   989  C  CG  . TRP A 1 127 ? 1.06000   16.22000  65.03600  1.000 69.00435  ?  127 TRP A CG  1 
ATOM   990  C  CD1 . TRP A 1 127 ? 0.39800   15.80600  66.15900  1.000 73.24144  ?  127 TRP A CD1 1 
ATOM   991  C  CD2 . TRP A 1 127 ? 0.08300   16.88000  64.22000  1.000 69.46539  ?  127 TRP A CD2 1 
ATOM   992  N  NE1 . TRP A 1 127 ? -0.93000  16.14600  66.08100  1.000 75.61526  ?  127 TRP A NE1 1 
ATOM   993  C  CE2 . TRP A 1 127 ? -1.15000  16.80700  64.90100  1.000 77.55277  ?  127 TRP A CE2 1 
ATOM   994  C  CE3 . TRP A 1 127 ? 0.12900   17.51700  62.97600  1.000 72.84853  ?  127 TRP A CE3 1 
ATOM   995  C  CZ2 . TRP A 1 127 ? -2.32500  17.34400  64.37900  1.000 82.95070  ?  127 TRP A CZ2 1 
ATOM   996  C  CZ3 . TRP A 1 127 ? -1.04100  18.05000  62.45900  1.000 79.15983  ?  127 TRP A CZ3 1 
ATOM   997  C  CH2 . TRP A 1 127 ? -2.25000  17.96000  63.16000  1.000 82.12725  ?  127 TRP A CH2 1 
ATOM   998  N  N   . PHE A 1 128 ? 2.97300   13.73700  62.61500  1.000 66.84066  ?  128 PHE A N   1 
ATOM   999  C  CA  . PHE A 1 128 ? 2.45500   12.86700  61.56400  1.000 63.31537  ?  128 PHE A CA  1 
ATOM   1000 C  C   . PHE A 1 128 ? 2.99300   11.44400  61.66700  1.000 62.07064  ?  128 PHE A C   1 
ATOM   1001 O  O   . PHE A 1 128 ? 2.29200   10.49900  61.28800  1.000 66.73759  ?  128 PHE A O   1 
ATOM   1002 C  CB  . PHE A 1 128 ? 2.78800   13.44200  60.18600  1.000 65.88853  ?  128 PHE A CB  1 
ATOM   1003 C  CG  . PHE A 1 128 ? 2.17500   14.78700  59.92500  1.000 65.36089  ?  128 PHE A CG  1 
ATOM   1004 C  CD1 . PHE A 1 128 ? 0.79900   14.93900  59.90100  1.000 61.49221  ?  128 PHE A CD1 1 
ATOM   1005 C  CD2 . PHE A 1 128 ? 2.97100   15.89400  59.68700  1.000 68.23472  ?  128 PHE A CD2 1 
ATOM   1006 C  CE1 . PHE A 1 128 ? 0.22800   16.17200  59.65800  1.000 60.80230  ?  128 PHE A CE1 1 
ATOM   1007 C  CE2 . PHE A 1 128 ? 2.40600   17.13000  59.44300  1.000 69.01253  ?  128 PHE A CE2 1 
ATOM   1008 C  CZ  . PHE A 1 128 ? 1.03200   17.26800  59.42800  1.000 65.85639  ?  128 PHE A CZ  1 
ATOM   1009 N  N   . LYS A 1 129 ? 4.22700   11.27100  62.15300  1.000 61.19568  ?  129 LYS A N   1 
ATOM   1010 C  CA  . LYS A 1 129 ? 4.77800   9.92900   62.33000  1.000 57.66793  ?  129 LYS A CA  1 
ATOM   1011 C  C   . LYS A 1 129 ? 3.88000   9.07400   63.21500  1.000 63.23916  ?  129 LYS A C   1 
ATOM   1012 O  O   . LYS A 1 129 ? 3.64900   7.89300   62.92700  1.000 54.79157  ?  129 LYS A O   1 
ATOM   1013 C  CB  . LYS A 1 129 ? 6.18500   10.01300  62.92000  1.000 58.40335  ?  129 LYS A CB  1 
ATOM   1014 C  CG  . LYS A 1 129 ? 6.78800   8.67100   63.31500  1.000 53.45877  ?  129 LYS A CG  1 
ATOM   1015 C  CD  . LYS A 1 129 ? 8.19000   8.86100   63.86900  1.000 54.92148  ?  129 LYS A CD  1 
ATOM   1016 C  CE  . LYS A 1 129 ? 8.86000   7.53700   64.18600  1.000 55.99026  ?  129 LYS A CE  1 
ATOM   1017 N  NZ  . LYS A 1 129 ? 10.27600  7.74000   64.59900  1.000 53.21744  ?  129 LYS A NZ  1 
ATOM   1018 N  N   . HIS A 1 130 ? 3.34800   9.66000   64.28800  1.000 69.45047  ?  130 HIS A N   1 
ATOM   1019 C  CA  . HIS A 1 130 ? 2.44000   8.97400   65.19700  1.000 66.10536  ?  130 HIS A CA  1 
ATOM   1020 C  C   . HIS A 1 130 ? 0.99300   9.39700   64.97700  1.000 70.44998  ?  130 HIS A C   1 
ATOM   1021 O  O   . HIS A 1 130 ? 0.21500   9.48500   65.93300  1.000 73.08522  ?  130 HIS A O   1 
ATOM   1022 C  CB  . HIS A 1 130 ? 2.86100   9.20500   66.64800  1.000 59.00612  ?  130 HIS A CB  1 
ATOM   1023 C  CG  . HIS A 1 130 ? 4.28400   8.83100   66.92800  1.000 56.88038  ?  130 HIS A CG  1 
ATOM   1024 N  ND1 . HIS A 1 130 ? 4.68900   7.52500   67.10400  1.000 51.37679  ?  130 HIS A ND1 1 
ATOM   1025 C  CD2 . HIS A 1 130 ? 5.39400   9.59200   67.07800  1.000 56.36199  ?  130 HIS A CD2 1 
ATOM   1026 C  CE1 . HIS A 1 130 ? 5.98900   7.49700   67.33700  1.000 51.02639  ?  130 HIS A CE1 1 
ATOM   1027 N  NE2 . HIS A 1 130 ? 6.44100   8.73800   67.32900  1.000 52.51814  ?  130 HIS A NE2 1 
ATOM   1028 N  N   . SER A 1 131 ? 0.63000   9.68700   63.72300  1.000 73.17496  ?  131 SER A N   1 
ATOM   1029 C  CA  . SER A 1 131 ? -0.74300  10.05300  63.39300  1.000 73.01146  ?  131 SER A CA  1 
ATOM   1030 C  C   . SER A 1 131 ? -1.73800  8.99500   63.84800  1.000 73.49582  ?  131 SER A C   1 
ATOM   1031 O  O   . SER A 1 131 ? -2.87700  9.32200   64.19800  1.000 67.96010  ?  131 SER A O   1 
ATOM   1032 C  CB  . SER A 1 131 ? -0.87000  10.27900  61.88400  1.000 72.43901  ?  131 SER A CB  1 
ATOM   1033 O  OG  . SER A 1 131 ? -2.22600  10.36400  61.48600  1.000 78.51949  ?  131 SER A OG  1 
ATOM   1034 N  N   . SER A 1 132 ? -1.33300  7.72400   63.83700  1.000 78.29466  ?  132 SER A N   1 
ATOM   1035 C  CA  . SER A 1 132 ? -2.21500  6.66000   64.30400  1.000 78.31938  ?  132 SER A CA  1 
ATOM   1036 C  C   . SER A 1 132 ? -2.46800  6.77200   65.80200  1.000 79.38132  ?  132 SER A C   1 
ATOM   1037 O  O   . SER A 1 132 ? -3.62300  6.80900   66.24500  1.000 84.56223  ?  132 SER A O   1 
ATOM   1038 C  CB  . SER A 1 132 ? -1.61600  5.29600   63.96200  1.000 85.98083  ?  132 SER A CB  1 
ATOM   1039 O  OG  . SER A 1 132 ? -2.35000  4.25200   64.57800  1.000 89.31740  ?  132 SER A OG  1 
ATOM   1040 N  N   . LEU A 1 133 ? -1.39500  6.81500   66.59700  1.000 81.05941  ?  133 LEU A N   1 
ATOM   1041 C  CA  . LEU A 1 133 ? -1.51700  6.89400   68.05000  1.000 76.15369  ?  133 LEU A CA  1 
ATOM   1042 C  C   . LEU A 1 133 ? -2.37500  8.08200   68.47200  1.000 74.97769  ?  133 LEU A C   1 
ATOM   1043 O  O   . LEU A 1 133 ? -3.37600  7.92500   69.17900  1.000 77.62921  ?  133 LEU A O   1 
ATOM   1044 C  CB  . LEU A 1 133 ? -0.11800  6.97400   68.67100  1.000 71.63857  ?  133 LEU A CB  1 
ATOM   1045 C  CG  . LEU A 1 133 ? 0.05900   7.16500   70.17800  1.000 77.02056  ?  133 LEU A CG  1 
ATOM   1046 C  CD1 . LEU A 1 133 ? 1.26300   6.36700   70.64800  1.000 73.43178  ?  133 LEU A CD1 1 
ATOM   1047 C  CD2 . LEU A 1 133 ? 0.23300   8.63400   70.53300  1.000 77.75648  ?  133 LEU A CD2 1 
ATOM   1048 N  N   . LEU A 1 134 ? -1.98700  9.28500   68.04300  1.000 72.90639  ?  134 LEU A N   1 
ATOM   1049 C  CA  . LEU A 1 134 ? -2.72600  10.48700  68.41600  1.000 75.10198  ?  134 LEU A CA  1 
ATOM   1050 C  C   . LEU A 1 134 ? -4.15800  10.45600  67.89500  1.000 79.25293  ?  134 LEU A C   1 
ATOM   1051 O  O   . LEU A 1 134 ? -5.05300  11.05500  68.50300  1.000 83.23920  ?  134 LEU A O   1 
ATOM   1052 C  CB  . LEU A 1 134 ? -1.99200  11.72300  67.90100  1.000 72.47101  ?  134 LEU A CB  1 
ATOM   1053 C  CG  . LEU A 1 134 ? -0.53700  11.83200  68.35900  1.000 72.33160  ?  134 LEU A CG  1 
ATOM   1054 C  CD1 . LEU A 1 134 ? 0.27100   12.66000  67.37900  1.000 63.13721  ?  134 LEU A CD1 1 
ATOM   1055 C  CD2 . LEU A 1 134 ? -0.45300  12.42100  69.75800  1.000 68.49103  ?  134 LEU A CD2 1 
ATOM   1056 N  N   . GLY A 1 135 ? -4.39100  9.77600   66.77000  1.000 78.03390  ?  135 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 135 ? -5.74200  9.67800   66.24000  1.000 79.26084  ?  135 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 135 ? -6.67500  8.89300   67.14300  1.000 83.88031  ?  135 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 135 ? -7.85300  9.23600   67.28000  1.000 88.56254  ?  135 GLY A O   1 
ATOM   1060 N  N   . GLU A 1 136 ? -6.16400  7.83200   67.76800  1.000 84.21523  ?  136 GLU A N   1 
ATOM   1061 C  CA  . GLU A 1 136 ? -6.97600  6.99000   68.63800  1.000 89.52479  ?  136 GLU A CA  1 
ATOM   1062 C  C   . GLU A 1 136 ? -7.32600  7.68000   69.95300  1.000 94.52264  ?  136 GLU A C   1 
ATOM   1063 O  O   . GLU A 1 136 ? -8.22500  7.21600   70.66300  1.000 99.43202  ?  136 GLU A O   1 
ATOM   1064 C  CB  . GLU A 1 136 ? -6.24100  5.66700   68.89500  1.000 91.54253  ?  136 GLU A CB  1 
ATOM   1065 C  CG  . GLU A 1 136 ? -6.98400  4.65900   69.76400  1.000 102.37841 ?  136 GLU A CG  1 
ATOM   1066 C  CD  . GLU A 1 136 ? -6.13300  3.45900   70.13400  1.000 114.79859 ?  136 GLU A CD  1 
ATOM   1067 O  OE1 . GLU A 1 136 ? -5.00400  3.34200   69.61200  1.000 114.61989 ?  136 GLU A OE1 1 
ATOM   1068 O  OE2 . GLU A 1 136 ? -6.59500  2.63100   70.94800  1.000 117.98497 -1 136 GLU A OE2 1 
ATOM   1069 N  N   . MET A 1 137 ? -6.67400  8.81800   70.27200  1.000 93.16443  ?  137 MET A N   1 
ATOM   1070 C  CA  . MET A 1 137 ? -6.90100  9.49000   71.53900  1.000 84.04195  ?  137 MET A CA  1 
ATOM   1071 C  C   . MET A 1 137 ? -7.86100  10.66000  71.35800  1.000 85.18626  ?  137 MET A C   1 
ATOM   1072 O  O   . MET A 1 137 ? -7.98200  11.20600  70.25700  1.000 88.21229  ?  137 MET A O   1 
ATOM   1073 C  CB  . MET A 1 137 ? -5.58300  10.01800  72.11300  1.000 74.03211  ?  137 MET A CB  1 
ATOM   1074 C  CG  . MET A 1 137 ? -4.53900  8.95500   72.38800  1.000 70.62773  ?  137 MET A CG  1 
ATOM   1075 S  SD  . MET A 1 137 ? -3.00900  9.69300   72.99000  1.000 75.00490  ?  137 MET A SD  1 
ATOM   1076 C  CE  . MET A 1 137 ? -3.10900  11.31600  72.23500  1.000 75.66069  ?  137 MET A CE  1 
ATOM   1077 N  N   . PRO A 1 138 ? -8.56100  11.06300  72.41500  1.000 89.10294  ?  138 PRO A N   1 
ATOM   1078 C  CA  . PRO A 1 138 ? -9.41300  12.25400  72.31200  1.000 92.96292  ?  138 PRO A CA  1 
ATOM   1079 C  C   . PRO A 1 138 ? -8.56800  13.50000  72.09300  1.000 93.38201  ?  138 PRO A C   1 
ATOM   1080 O  O   . PRO A 1 138 ? -7.48000  13.63400  72.65900  1.000 89.66123  ?  138 PRO A O   1 
ATOM   1081 C  CB  . PRO A 1 138 ? -10.14200 12.28400  73.66000  1.000 92.90245  ?  138 PRO A CB  1 
ATOM   1082 C  CG  . PRO A 1 138 ? -9.27400  11.49800  74.58500  1.000 90.97499  ?  138 PRO A CG  1 
ATOM   1083 C  CD  . PRO A 1 138 ? -8.66600  10.42200  73.73800  1.000 94.31872  ?  138 PRO A CD  1 
ATOM   1084 N  N   . GLN A 1 139 ? -9.09500  14.41800  71.27000  1.000 93.18416  ?  139 GLN A N   1 
ATOM   1085 C  CA  . GLN A 1 139 ? -8.33300  15.58200  70.81300  1.000 91.60505  ?  139 GLN A CA  1 
ATOM   1086 C  C   . GLN A 1 139 ? -7.63000  16.26900  71.97700  1.000 91.66948  ?  139 GLN A C   1 
ATOM   1087 O  O   . GLN A 1 139 ? -6.49300  16.73400  71.85100  1.000 90.57190  ?  139 GLN A O   1 
ATOM   1088 C  CB  . GLN A 1 139 ? -9.24100  16.56800  70.07500  1.000 89.16925  ?  139 GLN A CB  1 
ATOM   1089 C  CG  . GLN A 1 139 ? -8.48500  17.58300  69.20200  1.000 87.49193  ?  139 GLN A CG  1 
ATOM   1090 C  CD  . GLN A 1 139 ? -7.85100  18.72700  69.96800  1.000 93.65622  ?  139 GLN A CD  1 
ATOM   1091 O  OE1 . GLN A 1 139 ? -6.64800  18.97000  69.85200  1.000 93.08859  ?  139 GLN A OE1 1 
ATOM   1092 N  NE2 . GLN A 1 139 ? -8.65500  19.44600  70.73900  1.000 95.76939  ?  139 GLN A NE2 1 
ATOM   1093 N  N   . GLU A 1 140 ? -8.31500  16.35000  73.11500  1.000 93.70312  ?  140 GLU A N   1 
ATOM   1094 C  CA  . GLU A 1 140 ? -7.80500  17.04700  74.28800  1.000 100.17635 ?  140 GLU A CA  1 
ATOM   1095 C  C   . GLU A 1 140 ? -6.45700  16.49400  74.74800  1.000 96.98684  ?  140 GLU A C   1 
ATOM   1096 O  O   . GLU A 1 140 ? -5.61300  17.24700  75.24900  1.000 90.02833  ?  140 GLU A O   1 
ATOM   1097 C  CB  . GLU A 1 140 ? -8.84500  16.93700  75.40100  1.000 101.66312 ?  140 GLU A CB  1 
ATOM   1098 C  CG  . GLU A 1 140 ? -9.52900  15.56600  75.43700  1.000 102.49962 ?  140 GLU A CG  1 
ATOM   1099 C  CD  . GLU A 1 140 ? -10.72900 15.46700  74.49400  1.000 107.63350 ?  140 GLU A CD  1 
ATOM   1100 O  OE1 . GLU A 1 140 ? -10.73000 16.15200  73.44800  1.000 103.26957 ?  140 GLU A OE1 1 
ATOM   1101 O  OE2 . GLU A 1 140 ? -11.66200 14.68800  74.78900  1.000 113.58883 -1 140 GLU A OE2 1 
ATOM   1102 N  N   . ARG A 1 141 ? -6.23900  15.18400  74.61900  1.000 94.15974  ?  141 ARG A N   1 
ATOM   1103 C  CA  . ARG A 1 141 ? -5.02300  14.56800  75.13900  1.000 87.19494  ?  141 ARG A CA  1 
ATOM   1104 C  C   . ARG A 1 141 ? -3.89900  14.45500  74.10300  1.000 84.88530  ?  141 ARG A C   1 
ATOM   1105 O  O   . ARG A 1 141 ? -2.95300  13.69300  74.32700  1.000 77.88151  ?  141 ARG A O   1 
ATOM   1106 C  CB  . ARG A 1 141 ? -5.33600  13.18500  75.71900  1.000 86.84891  ?  141 ARG A CB  1 
ATOM   1107 C  CG  . ARG A 1 141 ? -6.39400  13.20800  76.80900  1.000 96.99591  ?  141 ARG A CG  1 
ATOM   1108 C  CD  . ARG A 1 141 ? -6.73000  11.82700  77.36000  1.000 100.75486 ?  141 ARG A CD  1 
ATOM   1109 N  NE  . ARG A 1 141 ? -5.59400  11.20500  78.02900  1.000 101.63785 ?  141 ARG A NE  1 
ATOM   1110 C  CZ  . ARG A 1 141 ? -5.47400  11.10300  79.34700  1.000 96.35205  ?  141 ARG A CZ  1 
ATOM   1111 N  NH1 . ARG A 1 141 ? -6.41600  11.55000  80.16300  1.000 97.10557  ?  141 ARG A NH1 1 
ATOM   1112 N  NH2 . ARG A 1 141 ? -4.38300  10.54200  79.86000  1.000 91.49558  ?  141 ARG A NH2 1 
ATOM   1113 N  N   . ARG A 1 142 ? -3.94700  15.21400  73.00200  1.000 88.01947  ?  142 ARG A N   1 
ATOM   1114 C  CA  . ARG A 1 142 ? -2.92000  15.05800  71.97100  1.000 78.03515  ?  142 ARG A CA  1 
ATOM   1115 C  C   . ARG A 1 142 ? -1.70300  15.95600  72.17200  1.000 73.27482  ?  142 ARG A C   1 
ATOM   1116 O  O   . ARG A 1 142 ? -0.56900  15.49600  72.00900  1.000 68.73482  ?  142 ARG A O   1 
ATOM   1117 C  CB  . ARG A 1 142 ? -3.49100  15.31800  70.56800  1.000 78.14413  ?  142 ARG A CB  1 
ATOM   1118 C  CG  . ARG A 1 142 ? -4.10300  14.11600  69.85200  1.000 81.24884  ?  142 ARG A CG  1 
ATOM   1119 C  CD  . ARG A 1 142 ? -5.52500  13.86100  70.26200  1.000 86.70022  ?  142 ARG A CD  1 
ATOM   1120 N  NE  . ARG A 1 142 ? -6.25500  13.01700  69.32000  1.000 85.55342  ?  142 ARG A NE  1 
ATOM   1121 C  CZ  . ARG A 1 142 ? -6.93300  13.46500  68.27000  1.000 78.35276  ?  142 ARG A CZ  1 
ATOM   1122 N  NH1 . ARG A 1 142 ? -6.98500  14.75400  67.97700  1.000 77.89410  ?  142 ARG A NH1 1 
ATOM   1123 N  NH2 . ARG A 1 142 ? -7.57800  12.59600  67.49600  1.000 77.33040  ?  142 ARG A NH2 1 
ATOM   1124 N  N   . LEU A 1 143 ? -1.91000  17.23300  72.49700  1.000 76.53179  ?  143 LEU A N   1 
ATOM   1125 C  CA  . LEU A 1 143 ? -0.76900  18.13800  72.61900  1.000 75.83042  ?  143 LEU A CA  1 
ATOM   1126 C  C   . LEU A 1 143 ? 0.15900   17.72300  73.75500  1.000 73.02457  ?  143 LEU A C   1 
ATOM   1127 O  O   . LEU A 1 143 ? 1.38200   17.87400  73.65200  1.000 71.10334  ?  143 LEU A O   1 
ATOM   1128 C  CB  . LEU A 1 143 ? -1.24900  19.57300  72.81000  1.000 73.09651  ?  143 LEU A CB  1 
ATOM   1129 C  CG  . LEU A 1 143 ? -0.15000  20.61200  72.58800  1.000 80.33126  ?  143 LEU A CG  1 
ATOM   1130 C  CD1 . LEU A 1 143 ? 0.48400   20.42500  71.21700  1.000 64.91573  ?  143 LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A 1 143 ? -0.71600  22.00800  72.73100  1.000 92.02385  ?  143 LEU A CD2 1 
ATOM   1132 N  N   . ASP A 1 144 ? -0.39900  17.18800  74.84400  1.000 69.22668  ?  144 ASP A N   1 
ATOM   1133 C  CA  . ASP A 1 144 ? 0.44600   16.67800  75.91800  1.000 65.14302  ?  144 ASP A CA  1 
ATOM   1134 C  C   . ASP A 1 144 ? 1.16800   15.40800  75.49000  1.000 64.35443  ?  144 ASP A C   1 
ATOM   1135 O  O   . ASP A 1 144 ? 2.31900   15.18000  75.88000  1.000 64.58833  ?  144 ASP A O   1 
ATOM   1136 C  CB  . ASP A 1 144 ? -0.38400  16.42500  77.17600  1.000 76.39786  ?  144 ASP A CB  1 
ATOM   1137 C  CG  . ASP A 1 144 ? -0.71300  17.70100  77.92600  1.000 71.49801  ?  144 ASP A CG  1 
ATOM   1138 O  OD1 . ASP A 1 144 ? -0.47700  18.79700  77.37700  1.000 76.69454  ?  144 ASP A OD1 1 
ATOM   1139 O  OD2 . ASP A 1 144 ? -1.20400  17.60600  79.07000  1.000 66.21071  -1 144 ASP A OD2 1 
ATOM   1140 N  N   . THR A 1 145 ? 0.50600   14.56700  74.69200  1.000 66.28592  ?  145 THR A N   1 
ATOM   1141 C  CA  . THR A 1 145 ? 1.12700   13.32200  74.25100  1.000 62.84255  ?  145 THR A CA  1 
ATOM   1142 C  C   . THR A 1 145 ? 2.26900   13.59500  73.28200  1.000 58.32391  ?  145 THR A C   1 
ATOM   1143 O  O   . THR A 1 145 ? 3.35700   13.02200  73.41200  1.000 54.47252  ?  145 THR A O   1 
ATOM   1144 C  CB  . THR A 1 145 ? 0.08200   12.41800  73.60200  1.000 61.49653  ?  145 THR A CB  1 
ATOM   1145 O  OG1 . THR A 1 145 ? -1.03700  12.27900  74.48400  1.000 72.04071  ?  145 THR A OG1 1 
ATOM   1146 C  CG2 . THR A 1 145 ? 0.66900   11.04500  73.31900  1.000 58.32148  ?  145 THR A CG2 1 
ATOM   1147 N  N   . LEU A 1 146 ? 2.03500   14.47400  72.30100  1.000 62.73173  ?  146 LEU A N   1 
ATOM   1148 C  CA  . LEU A 1 146 ? 3.10100   14.89400  71.39600  1.000 63.68318  ?  146 LEU A CA  1 
ATOM   1149 C  C   . LEU A 1 146 ? 4.28800   15.44400  72.17700  1.000 60.33882  ?  146 LEU A C   1 
ATOM   1150 O  O   . LEU A 1 146 ? 5.44700   15.21800  71.80700  1.000 55.57286  ?  146 LEU A O   1 
ATOM   1151 C  CB  . LEU A 1 146 ? 2.57300   15.94000  70.41200  1.000 57.10910  ?  146 LEU A CB  1 
ATOM   1152 C  CG  . LEU A 1 146 ? 3.59700   16.56300  69.46200  1.000 50.05838  ?  146 LEU A CG  1 
ATOM   1153 C  CD1 . LEU A 1 146 ? 4.19700   15.50300  68.54600  1.000 55.34189  ?  146 LEU A CD1 1 
ATOM   1154 C  CD2 . LEU A 1 146 ? 2.99000   17.69200  68.66100  1.000 52.16265  ?  146 LEU A CD2 1 
ATOM   1155 N  N   . CYS A 1 147 ? 4.01200   16.18800  73.25400  1.000 60.94547  ?  147 CYS A N   1 
ATOM   1156 C  CA  . CYS A 1 147 ? 5.07800   16.69300  74.11400  1.000 66.72282  ?  147 CYS A CA  1 
ATOM   1157 C  C   . CYS A 1 147 ? 5.91500   15.55700  74.69100  1.000 65.61115  ?  147 CYS A C   1 
ATOM   1158 O  O   . CYS A 1 147 ? 7.14500   15.65800  74.76400  1.000 65.96864  ?  147 CYS A O   1 
ATOM   1159 C  CB  . CYS A 1 147 ? 4.48300   17.54000  75.23800  1.000 61.55080  ?  147 CYS A CB  1 
ATOM   1160 S  SG  . CYS A 1 147 ? 5.68600   18.11200  76.45300  1.000 74.11545  ?  147 CYS A SG  1 
ATOM   1161 N  N   . GLU A 1 148 ? 5.26700   14.46600  75.10800  1.000 60.42326  ?  148 GLU A N   1 
ATOM   1162 C  CA  . GLU A 1 148 ? 6.01800   13.30200  75.56500  1.000 56.75918  ?  148 GLU A CA  1 
ATOM   1163 C  C   . GLU A 1 148 ? 6.64200   12.56600  74.38900  1.000 61.80726  ?  148 GLU A C   1 
ATOM   1164 O  O   . GLU A 1 148 ? 7.75500   12.03800  74.49800  1.000 65.00461  ?  148 GLU A O   1 
ATOM   1165 C  CB  . GLU A 1 148 ? 5.11100   12.36800  76.36400  1.000 60.83441  ?  148 GLU A CB  1 
ATOM   1166 C  CG  . GLU A 1 148 ? 4.49700   13.00800  77.59600  1.000 66.99028  ?  148 GLU A CG  1 
ATOM   1167 C  CD  . GLU A 1 148 ? 3.55900   12.07600  78.33500  1.000 68.31937  ?  148 GLU A CD  1 
ATOM   1168 O  OE1 . GLU A 1 148 ? 3.28500   10.97300  77.81400  1.000 62.94506  ?  148 GLU A OE1 1 
ATOM   1169 O  OE2 . GLU A 1 148 ? 3.09700   12.44600  79.43600  1.000 71.75262  -1 148 GLU A OE2 1 
ATOM   1170 N  N   . LEU A 1 149 ? 5.93500   12.52500  73.25600  1.000 62.51942  ?  149 LEU A N   1 
ATOM   1171 C  CA  . LEU A 1 149 ? 6.47500   11.90200  72.05300  1.000 55.56741  ?  149 LEU A CA  1 
ATOM   1172 C  C   . LEU A 1 149 ? 7.74200   12.60400  71.58900  1.000 54.87264  ?  149 LEU A C   1 
ATOM   1173 O  O   . LEU A 1 149 ? 8.72600   11.94800  71.22600  1.000 56.20791  ?  149 LEU A O   1 
ATOM   1174 C  CB  . LEU A 1 149 ? 5.41900   11.91000  70.94900  1.000 49.30323  ?  149 LEU A CB  1 
ATOM   1175 C  CG  . LEU A 1 149 ? 4.27900   10.91200  71.14900  1.000 53.02785  ?  149 LEU A CG  1 
ATOM   1176 C  CD1 . LEU A 1 149 ? 3.12000   11.23100  70.22200  1.000 54.63384  ?  149 LEU A CD1 1 
ATOM   1177 C  CD2 . LEU A 1 149 ? 4.78300   9.50000   70.91700  1.000 51.01455  ?  149 LEU A CD2 1 
ATOM   1178 N  N   . ASN A 1 150 ? 7.73500   13.94000  71.58700  1.000 51.13049  ?  150 ASN A N   1 
ATOM   1179 C  CA  . ASN A 1 150 ? 8.91900   14.68100  71.16800  1.000 49.89297  ?  150 ASN A CA  1 
ATOM   1180 C  C   . ASN A 1 150 ? 10.11900  14.32900  72.03600  1.000 57.22157  ?  150 ASN A C   1 
ATOM   1181 O  O   . ASN A 1 150 ? 11.22600  14.12600  71.52500  1.000 54.15149  ?  150 ASN A O   1 
ATOM   1182 C  CB  . ASN A 1 150 ? 8.64200   16.18400  71.20600  1.000 46.81186  ?  150 ASN A CB  1 
ATOM   1183 C  CG  . ASN A 1 150 ? 9.82800   17.00900  70.73600  1.000 53.70477  ?  150 ASN A CG  1 
ATOM   1184 O  OD1 . ASN A 1 150 ? 10.63800  16.55200  69.92900  1.000 57.85398  ?  150 ASN A OD1 1 
ATOM   1185 N  ND2 . ASN A 1 150 ? 9.92700   18.23800  71.23100  1.000 52.61594  ?  150 ASN A ND2 1 
ATOM   1186 N  N   . VAL A 1 151 ? 9.90600   14.21200  73.34900  1.000 59.72127  ?  151 VAL A N   1 
ATOM   1187 C  CA  . VAL A 1 151 ? 11.00800  13.92200  74.26000  1.000 53.79864  ?  151 VAL A CA  1 
ATOM   1188 C  C   . VAL A 1 151 ? 11.57400  12.53200  73.99400  1.000 52.62537  ?  151 VAL A C   1 
ATOM   1189 O  O   . VAL A 1 151 ? 12.79300  12.32600  74.04500  1.000 48.87973  ?  151 VAL A O   1 
ATOM   1190 C  CB  . VAL A 1 151 ? 10.54400  14.08200  75.71900  1.000 58.05942  ?  151 VAL A CB  1 
ATOM   1191 C  CG1 . VAL A 1 151 ? 11.63900  13.64200  76.67800  1.000 50.22994  ?  151 VAL A CG1 1 
ATOM   1192 C  CG2 . VAL A 1 151 ? 10.14700  15.52600  75.98600  1.000 54.05136  ?  151 VAL A CG2 1 
ATOM   1193 N  N   . MET A 1 152 ? 10.70600  11.55900  73.70400  1.000 54.89047  ?  152 MET A N   1 
ATOM   1194 C  CA  . MET A 1 152 ? 11.19100  10.21900  73.39000  1.000 55.83734  ?  152 MET A CA  1 
ATOM   1195 C  C   . MET A 1 152 ? 11.99300  10.21600  72.09500  1.000 54.28876  ?  152 MET A C   1 
ATOM   1196 O  O   . MET A 1 152 ? 13.04900  9.57600   72.01100  1.000 51.87615  ?  152 MET A O   1 
ATOM   1197 C  CB  . MET A 1 152 ? 10.01400  9.24800   73.29300  1.000 51.85374  ?  152 MET A CB  1 
ATOM   1198 C  CG  . MET A 1 152 ? 9.16500   9.17700   74.55400  1.000 54.04766  ?  152 MET A CG  1 
ATOM   1199 S  SD  . MET A 1 152 ? 7.77100   8.04100   74.42200  1.000 48.46121  ?  152 MET A SD  1 
ATOM   1200 C  CE  . MET A 1 152 ? 6.95100   8.34300   75.98600  1.000 73.50832  ?  152 MET A CE  1 
ATOM   1201 N  N   . GLU A 1 153 ? 11.51300  10.94300  71.08200  1.000 56.70262  ?  153 GLU A N   1 
ATOM   1202 C  CA  . GLU A 1 153 ? 12.20800  11.00000  69.80000  1.000 54.12355  ?  153 GLU A CA  1 
ATOM   1203 C  C   . GLU A 1 153 ? 13.56200  11.68900  69.92700  1.000 57.62502  ?  153 GLU A C   1 
ATOM   1204 O  O   . GLU A 1 153 ? 14.54300  11.25400  69.31100  1.000 52.82936  ?  153 GLU A O   1 
ATOM   1205 C  CB  . GLU A 1 153 ? 11.33500  11.71400  68.76800  1.000 52.24947  ?  153 GLU A CB  1 
ATOM   1206 C  CG  . GLU A 1 153 ? 10.01500  11.01200  68.45300  1.000 52.52406  ?  153 GLU A CG  1 
ATOM   1207 C  CD  . GLU A 1 153 ? 10.18000  9.76800   67.60100  1.000 61.12613  ?  153 GLU A CD  1 
ATOM   1208 O  OE1 . GLU A 1 153 ? 11.27600  9.56700   67.03300  1.000 61.11441  ?  153 GLU A OE1 1 
ATOM   1209 O  OE2 . GLU A 1 153 ? 9.20300   8.99400   67.48900  1.000 57.91175  -1 153 GLU A OE2 1 
ATOM   1210 N  N   . GLN A 1 154 ? 13.63700  12.77200  70.71000  1.000 56.53664  ?  154 GLN A N   1 
ATOM   1211 C  CA  . GLN A 1 154 ? 14.91300  13.46500  70.87000  1.000 53.02244  ?  154 GLN A CA  1 
ATOM   1212 C  C   . GLN A 1 154 ? 15.91400  12.59100  71.61300  1.000 56.13064  ?  154 GLN A C   1 
ATOM   1213 O  O   . GLN A 1 154 ? 17.10600  12.58700  71.28500  1.000 56.39581  ?  154 GLN A O   1 
ATOM   1214 C  CB  . GLN A 1 154 ? 14.71900  14.79200  71.60600  1.000 54.92628  ?  154 GLN A CB  1 
ATOM   1215 C  CG  . GLN A 1 154 ? 13.70800  15.74900  70.98100  1.000 56.30110  ?  154 GLN A CG  1 
ATOM   1216 C  CD  . GLN A 1 154 ? 13.81900  15.84300  69.47200  1.000 59.21630  ?  154 GLN A CD  1 
ATOM   1217 O  OE1 . GLN A 1 154 ? 14.87300  16.17900  68.93400  1.000 61.00365  ?  154 GLN A OE1 1 
ATOM   1218 N  NE2 . GLN A 1 154 ? 12.72600  15.54200  68.78000  1.000 55.80141  ?  154 GLN A NE2 1 
ATOM   1219 N  N   . VAL A 1 155 ? 15.44200  11.84200  72.61300  1.000 59.40921  ?  155 VAL A N   1 
ATOM   1220 C  CA  . VAL A 1 155 ? 16.28400  10.83600  73.25100  1.000 57.62665  ?  155 VAL A CA  1 
ATOM   1221 C  C   . VAL A 1 155 ? 16.70500  9.79400   72.22700  1.000 54.88235  ?  155 VAL A C   1 
ATOM   1222 O  O   . VAL A 1 155 ? 17.85700  9.34200   72.21000  1.000 57.02601  ?  155 VAL A O   1 
ATOM   1223 C  CB  . VAL A 1 155 ? 15.54700  10.20100  74.44600  1.000 56.54555  ?  155 VAL A CB  1 
ATOM   1224 C  CG1 . VAL A 1 155 ? 16.31500  9.00000   74.97500  1.000 53.16325  ?  155 VAL A CG1 1 
ATOM   1225 C  CG2 . VAL A 1 155 ? 15.34200  11.22900  75.54700  1.000 52.20570  ?  155 VAL A CG2 1 
ATOM   1226 N  N   . TYR A 1 156 ? 15.77300  9.39600   71.35800  1.000 58.78119  ?  156 TYR A N   1 
ATOM   1227 C  CA  . TYR A 1 156 ? 16.09700  8.48200   70.26900  1.000 57.39822  ?  156 TYR A CA  1 
ATOM   1228 C  C   . TYR A 1 156 ? 17.15400  9.08500   69.34900  1.000 49.70846  ?  156 TYR A C   1 
ATOM   1229 O  O   . TYR A 1 156 ? 18.14200  8.42600   69.00400  1.000 50.14721  ?  156 TYR A O   1 
ATOM   1230 C  CB  . TYR A 1 156 ? 14.82500  8.13200   69.49500  1.000 51.95393  ?  156 TYR A CB  1 
ATOM   1231 C  CG  . TYR A 1 156 ? 14.89700  6.82100   68.74800  1.000 63.04395  ?  156 TYR A CG  1 
ATOM   1232 C  CD1 . TYR A 1 156 ? 15.35500  5.66900   69.37200  1.000 64.88471  ?  156 TYR A CD1 1 
ATOM   1233 C  CD2 . TYR A 1 156 ? 14.49200  6.73200   67.42600  1.000 65.07266  ?  156 TYR A CD2 1 
ATOM   1234 C  CE1 . TYR A 1 156 ? 15.41700  4.46700   68.69400  1.000 67.16007  ?  156 TYR A CE1 1 
ATOM   1235 C  CE2 . TYR A 1 156 ? 14.55100  5.53600   66.74000  1.000 66.40752  ?  156 TYR A CE2 1 
ATOM   1236 C  CZ  . TYR A 1 156 ? 15.01400  4.40700   67.37900  1.000 68.77187  ?  156 TYR A CZ  1 
ATOM   1237 O  OH  . TYR A 1 156 ? 15.07400  3.21400   66.70000  1.000 72.85484  ?  156 TYR A OH  1 
ATOM   1238 N  N   . ASN A 1 157 ? 16.95200  10.33800  68.92400  1.000 48.47878  ?  157 ASN A N   1 
ATOM   1239 C  CA  . ASN A 1 157 ? 17.94200  11.01100  68.08500  1.000 52.99767  ?  157 ASN A CA  1 
ATOM   1240 C  C   . ASN A 1 157 ? 19.29300  11.10500  68.78500  1.000 53.53926  ?  157 ASN A C   1 
ATOM   1241 O  O   . ASN A 1 157 ? 20.33300  10.79500  68.19300  1.000 44.90541  ?  157 ASN A O   1 
ATOM   1242 C  CB  . ASN A 1 157 ? 17.45000  12.40800  67.69900  1.000 56.53808  ?  157 ASN A CB  1 
ATOM   1243 C  CG  . ASN A 1 157 ? 16.16800  12.38000  66.89200  1.000 56.89677  ?  157 ASN A CG  1 
ATOM   1244 O  OD1 . ASN A 1 157 ? 15.72100  11.32300  66.44400  1.000 50.54467  ?  157 ASN A OD1 1 
ATOM   1245 N  ND2 . ASN A 1 157 ? 15.56600  13.55000  66.70500  1.000 55.26508  ?  157 ASN A ND2 1 
ATOM   1246 N  N   . LEU A 1 158 ? 19.29200  11.52800  70.05400  1.000 59.18266  ?  158 LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 158 ? 20.54200  11.68600  70.79300  1.000 54.08084  ?  158 LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 158 ? 21.32100  10.38000  70.85400  1.000 53.75873  ?  158 LEU A C   1 
ATOM   1249 O  O   . LEU A 1 158 ? 22.53000  10.35900  70.60000  1.000 53.86079  ?  158 LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 158 ? 20.25000  12.21400  72.20100  1.000 60.59573  ?  158 LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 158 ? 21.34600  12.38800  73.26200  1.000 51.10838  ?  158 LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 158 ? 22.56000  13.15200  72.76000  1.000 55.18918  ?  158 LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 158 ? 20.75700  13.08600  74.47600  1.000 56.42786  ?  158 LEU A CD2 1 
ATOM   1254 N  N   . GLY A 1 159 ? 20.63600  9.27000   71.14100  1.000 49.73663  ?  159 GLY A N   1 
ATOM   1255 C  CA  . GLY A 1 159 ? 21.31600  7.99200   71.23100  1.000 51.98183  ?  159 GLY A CA  1 
ATOM   1256 C  C   . GLY A 1 159 ? 21.87600  7.49200   69.91600  1.000 61.52748  ?  159 GLY A C   1 
ATOM   1257 O  O   . GLY A 1 159 ? 22.77500  6.64400   69.92100  1.000 60.67211  ?  159 GLY A O   1 
ATOM   1258 N  N   . HIS A 1 160 ? 21.35600  7.98400   68.79100  1.000 60.90025  ?  160 HIS A N   1 
ATOM   1259 C  CA  . HIS A 1 160 ? 21.82900  7.55700   67.48000  1.000 61.78843  ?  160 HIS A CA  1 
ATOM   1260 C  C   . HIS A 1 160 ? 23.00000  8.37400   66.95100  1.000 58.36269  ?  160 HIS A C   1 
ATOM   1261 O  O   . HIS A 1 160 ? 23.70200  7.89800   66.05200  1.000 58.93017  ?  160 HIS A O   1 
ATOM   1262 C  CB  . HIS A 1 160 ? 20.68200  7.59900   66.46700  1.000 54.62452  ?  160 HIS A CB  1 
ATOM   1263 C  CG  . HIS A 1 160 ? 19.74900  6.43400   66.57000  1.000 56.45704  ?  160 HIS A CG  1 
ATOM   1264 N  ND1 . HIS A 1 160 ? 20.15100  5.19800   67.02900  1.000 59.76989  ?  160 HIS A ND1 1 
ATOM   1265 C  CD2 . HIS A 1 160 ? 18.43200  6.31500   66.27800  1.000 59.90863  ?  160 HIS A CD2 1 
ATOM   1266 C  CE1 . HIS A 1 160 ? 19.12400  4.36800   67.01200  1.000 64.41001  ?  160 HIS A CE1 1 
ATOM   1267 N  NE2 . HIS A 1 160 ? 18.06800  5.02100   66.56200  1.000 66.43756  ?  160 HIS A NE2 1 
ATOM   1268 N  N   . SER A 1 161 ? 23.23100  9.57700   67.47600  1.000 57.16324  ?  161 SER A N   1 
ATOM   1269 C  CA  . SER A 1 161 ? 24.32600  10.40800  66.99300  1.000 53.74269  ?  161 SER A CA  1 
ATOM   1270 C  C   . SER A 1 161 ? 25.66700  9.70300   67.18300  1.000 56.58929  ?  161 SER A C   1 
ATOM   1271 O  O   . SER A 1 161 ? 25.82000  8.80400   68.01300  1.000 61.50020  ?  161 SER A O   1 
ATOM   1272 C  CB  . SER A 1 161 ? 24.34400  11.75400  67.71600  1.000 58.88988  ?  161 SER A CB  1 
ATOM   1273 O  OG  . SER A 1 161 ? 24.96600  11.64300  68.98500  1.000 66.61290  ?  161 SER A OG  1 
ATOM   1274 N  N   . THR A 1 162 ? 26.65600  10.13700  66.40000  1.000 63.29660  ?  162 THR A N   1 
ATOM   1275 C  CA  . THR A 1 162 ? 27.97700  9.52000   66.47100  1.000 67.72729  ?  162 THR A CA  1 
ATOM   1276 C  C   . THR A 1 162 ? 28.64700  9.77200   67.81400  1.000 66.60256  ?  162 THR A C   1 
ATOM   1277 O  O   . THR A 1 162 ? 29.44400  8.94400   68.26900  1.000 66.99197  ?  162 THR A O   1 
ATOM   1278 C  CB  . THR A 1 162 ? 28.86200  10.02600  65.33300  1.000 64.13610  ?  162 THR A CB  1 
ATOM   1279 O  OG1 . THR A 1 162 ? 29.01700  11.44700  65.43700  1.000 61.55209  ?  162 THR A OG1 1 
ATOM   1280 C  CG2 . THR A 1 162 ? 28.23400  9.69300   64.00100  1.000 63.88671  ?  162 THR A CG2 1 
ATOM   1281 N  N   . ILE A 1 163 ? 28.35100  10.90600  68.45300  1.000 65.94334  ?  163 ILE A N   1 
ATOM   1282 C  CA  . ILE A 1 163 ? 28.93400  11.20500  69.75900  1.000 71.81630  ?  163 ILE A CA  1 
ATOM   1283 C  C   . ILE A 1 163 ? 28.54500  10.13700  70.77300  1.000 67.18475  ?  163 ILE A C   1 
ATOM   1284 O  O   . ILE A 1 163 ? 29.39600  9.59200   71.48600  1.000 65.58567  ?  163 ILE A O   1 
ATOM   1285 C  CB  . ILE A 1 163 ? 28.51200  12.61000  70.22600  1.000 63.46233  ?  163 ILE A CB  1 
ATOM   1286 C  CG1 . ILE A 1 163 ? 28.93400  13.65200  69.18800  1.000 59.35034  ?  163 ILE A CG1 1 
ATOM   1287 C  CG2 . ILE A 1 163 ? 29.09200  12.91200  71.60000  1.000 70.40585  ?  163 ILE A CG2 1 
ATOM   1288 C  CD1 . ILE A 1 163 ? 28.20100  14.96200  69.30400  1.000 65.96803  ?  163 ILE A CD1 1 
ATOM   1289 N  N   . MET A 1 164 ? 27.25000  9.82900   70.86200  1.000 59.98320  ?  164 MET A N   1 
ATOM   1290 C  CA  . MET A 1 164 ? 26.80300  8.80500   71.79900  1.000 65.69599  ?  164 MET A CA  1 
ATOM   1291 C  C   . MET A 1 164 ? 27.27200  7.42100   71.36400  1.000 69.62449  ?  164 MET A C   1 
ATOM   1292 O  O   . MET A 1 164 ? 27.75700  6.63200   72.18400  1.000 74.01549  ?  164 MET A O   1 
ATOM   1293 C  CB  . MET A 1 164 ? 25.28100  8.84200   71.92800  1.000 63.24665  ?  164 MET A CB  1 
ATOM   1294 C  CG  . MET A 1 164 ? 24.75700  10.06600  72.65900  1.000 61.27574  ?  164 MET A CG  1 
ATOM   1295 S  SD  . MET A 1 164 ? 25.53100  10.32300  74.26100  1.000 60.38061  ?  164 MET A SD  1 
ATOM   1296 C  CE  . MET A 1 164 ? 25.16500  8.76800   75.06800  1.000 63.31594  ?  164 MET A CE  1 
ATOM   1297 N  N   . GLN A 1 165 ? 27.12700  7.10600   70.07400  1.000 67.34438  ?  165 GLN A N   1 
ATOM   1298 C  CA  . GLN A 1 165 ? 27.51900  5.79000   69.57700  1.000 67.03515  ?  165 GLN A CA  1 
ATOM   1299 C  C   . GLN A 1 165 ? 29.00900  5.53500   69.78100  1.000 69.53229  ?  165 GLN A C   1 
ATOM   1300 O  O   . GLN A 1 165 ? 29.41000  4.42200   70.13800  1.000 73.11583  ?  165 GLN A O   1 
ATOM   1301 C  CB  . GLN A 1 165 ? 27.13300  5.65900   68.10400  1.000 65.37531  ?  165 GLN A CB  1 
ATOM   1302 C  CG  . GLN A 1 165 ? 25.62800  5.72500   67.86900  1.000 62.82221  ?  165 GLN A CG  1 
ATOM   1303 C  CD  . GLN A 1 165 ? 24.93100  4.40300   68.12500  1.000 72.91190  ?  165 GLN A CD  1 
ATOM   1304 O  OE1 . GLN A 1 165 ? 25.33900  3.36400   67.60800  1.000 77.38021  ?  165 GLN A OE1 1 
ATOM   1305 N  NE2 . GLN A 1 165 ? 23.88300  4.43400   68.94300  1.000 69.61498  ?  165 GLN A NE2 1 
ATOM   1306 N  N   . SER A 1 166 ? 29.84700  6.54800   69.54400  1.000 68.22791  ?  166 SER A N   1 
ATOM   1307 C  CA  . SER A 1 166 ? 31.27900  6.38500   69.78700  1.000 73.62211  ?  166 SER A CA  1 
ATOM   1308 C  C   . SER A 1 166 ? 31.57200  6.23700   71.27500  1.000 82.28397  ?  166 SER A C   1 
ATOM   1309 O  O   . SER A 1 166 ? 32.38900  5.39800   71.67100  1.000 85.37593  ?  166 SER A O   1 
ATOM   1310 C  CB  . SER A 1 166 ? 32.05900  7.56200   69.20200  1.000 74.51156  ?  166 SER A CB  1 
ATOM   1311 O  OG  . SER A 1 166 ? 31.84100  7.67900   67.80700  1.000 89.47286  ?  166 SER A OG  1 
ATOM   1312 N  N   . ALA A 1 167 ? 30.92300  7.05300   72.11000  1.000 77.50635  ?  167 ALA A N   1 
ATOM   1313 C  CA  . ALA A 1 167 ? 31.17000  7.00600   73.54800  1.000 80.23858  ?  167 ALA A CA  1 
ATOM   1314 C  C   . ALA A 1 167 ? 30.75600  5.66300   74.13700  1.000 78.39729  ?  167 ALA A C   1 
ATOM   1315 O  O   . ALA A 1 167 ? 31.49100  5.06800   74.93400  1.000 82.51811  ?  167 ALA A O   1 
ATOM   1316 C  CB  . ALA A 1 167 ? 30.43200  8.14900   74.24400  1.000 75.41267  ?  167 ALA A CB  1 
ATOM   1317 N  N   . TRP A 1 168 ? 29.57000  5.17500   73.76800  1.000 70.37691  ?  168 TRP A N   1 
ATOM   1318 C  CA  . TRP A 1 168 ? 29.12300  3.88000   74.26900  1.000 71.44094  ?  168 TRP A CA  1 
ATOM   1319 C  C   . TRP A 1 168 ? 30.03500  2.75200   73.80100  1.000 75.10867  ?  168 TRP A C   1 
ATOM   1320 O  O   . TRP A 1 168 ? 30.27000  1.78900   74.54000  1.000 79.20141  ?  168 TRP A O   1 
ATOM   1321 C  CB  . TRP A 1 168 ? 27.68100  3.61400   73.83900  1.000 64.93227  ?  168 TRP A CB  1 
ATOM   1322 C  CG  . TRP A 1 168 ? 26.65800  4.34600   74.65400  1.000 67.25033  ?  168 TRP A CG  1 
ATOM   1323 C  CD1 . TRP A 1 168 ? 26.83000  4.88200   75.89700  1.000 66.76594  ?  168 TRP A CD1 1 
ATOM   1324 C  CD2 . TRP A 1 168 ? 25.29700  4.60800   74.28900  1.000 67.66146  ?  168 TRP A CD2 1 
ATOM   1325 N  NE1 . TRP A 1 168 ? 25.66300  5.46700   76.32700  1.000 64.27580  ?  168 TRP A NE1 1 
ATOM   1326 C  CE2 . TRP A 1 168 ? 24.70600  5.31200   75.35900  1.000 64.56590  ?  168 TRP A CE2 1 
ATOM   1327 C  CE3 . TRP A 1 168 ? 24.52200  4.31900   73.16200  1.000 62.53862  ?  168 TRP A CE3 1 
ATOM   1328 C  CZ2 . TRP A 1 168 ? 23.37700  5.73200   75.33300  1.000 62.64619  ?  168 TRP A CZ2 1 
ATOM   1329 C  CZ3 . TRP A 1 168 ? 23.20200  4.73600   73.13900  1.000 62.22974  ?  168 TRP A CZ3 1 
ATOM   1330 C  CH2 . TRP A 1 168 ? 22.64400  5.43400   74.21800  1.000 64.07099  ?  168 TRP A CH2 1 
ATOM   1331 N  N   . LYS A 1 169 ? 30.56500  2.85100   72.57900  1.000 79.13495  ?  169 LYS A N   1 
ATOM   1332 C  CA  . LYS A 1 169 ? 31.40100  1.77000   72.06900  1.000 81.62993  ?  169 LYS A CA  1 
ATOM   1333 C  C   . LYS A 1 169 ? 32.76200  1.73200   72.75700  1.000 83.95393  ?  169 LYS A C   1 
ATOM   1334 O  O   . LYS A 1 169 ? 33.37200  0.66100   72.85200  1.000 80.40163  ?  169 LYS A O   1 
ATOM   1335 C  CB  . LYS A 1 169 ? 31.57800  1.88200   70.55500  1.000 78.15564  ?  169 LYS A CB  1 
ATOM   1336 C  CG  . LYS A 1 169 ? 32.24900  0.65000   69.95500  1.000 85.77529  ?  169 LYS A CG  1 
ATOM   1337 C  CD  . LYS A 1 169 ? 32.68100  0.84400   68.51900  1.000 84.01546  ?  169 LYS A CD  1 
ATOM   1338 C  CE  . LYS A 1 169 ? 33.74100  1.92200   68.41800  1.000 91.95958  ?  169 LYS A CE  1 
ATOM   1339 N  NZ  . LYS A 1 169 ? 34.56600  1.76200   67.18900  1.000 103.47249 ?  169 LYS A NZ  1 
ATOM   1340 N  N   . ARG A 1 170 ? 33.25600  2.87100   73.24700  1.000 83.13582  ?  170 ARG A N   1 
ATOM   1341 C  CA  . ARG A 1 170 ? 34.51800  2.87200   73.97900  1.000 81.73702  ?  170 ARG A CA  1 
ATOM   1342 C  C   . ARG A 1 170 ? 34.33800  2.52300   75.44900  1.000 86.34634  ?  170 ARG A C   1 
ATOM   1343 O  O   . ARG A 1 170 ? 35.30500  2.60400   76.21500  1.000 93.93645  ?  170 ARG A O   1 
ATOM   1344 C  CB  . ARG A 1 170 ? 35.21800  4.23200   73.86700  1.000 83.54636  ?  170 ARG A CB  1 
ATOM   1345 C  CG  . ARG A 1 170 ? 34.54700  5.36600   74.63600  1.000 85.73735  ?  170 ARG A CG  1 
ATOM   1346 C  CD  . ARG A 1 170 ? 35.26200  6.69300   74.41200  1.000 85.52826  ?  170 ARG A CD  1 
ATOM   1347 N  NE  . ARG A 1 170 ? 35.11200  7.17800   73.04500  1.000 86.30258  ?  170 ARG A NE  1 
ATOM   1348 C  CZ  . ARG A 1 170 ? 34.41900  8.25600   72.70500  1.000 88.92553  ?  170 ARG A CZ  1 
ATOM   1349 N  NH1 . ARG A 1 170 ? 33.81000  9.00300   73.61200  1.000 90.22929  ?  170 ARG A NH1 1 
ATOM   1350 N  NH2 . ARG A 1 170 ? 34.33500  8.59500   71.42100  1.000 96.45656  ?  170 ARG A NH2 1 
ATOM   1351 N  N   . GLY A 1 171 ? 33.13000  2.14400   75.85900  1.000 85.74195  ?  171 GLY A N   1 
ATOM   1352 C  CA  . GLY A 1 171 ? 32.88100  1.69100   77.20800  1.000 80.40421  ?  171 GLY A CA  1 
ATOM   1353 C  C   . GLY A 1 171 ? 32.55300  2.79000   78.19000  1.000 77.29688  ?  171 GLY A C   1 
ATOM   1354 O  O   . GLY A 1 171 ? 32.30400  2.49400   79.36500  1.000 84.49096  ?  171 GLY A O   1 
ATOM   1355 N  N   . GLN A 1 172 ? 32.54800  4.04500   77.74600  1.000 76.44605  ?  172 GLN A N   1 
ATOM   1356 C  CA  . GLN A 1 172 ? 32.22900  5.15900   78.62800  1.000 75.38616  ?  172 GLN A CA  1 
ATOM   1357 C  C   . GLN A 1 172 ? 30.81400  5.01800   79.17100  1.000 77.69514  ?  172 GLN A C   1 
ATOM   1358 O  O   . GLN A 1 172 ? 29.90400  4.55900   78.47500  1.000 78.66064  ?  172 GLN A O   1 
ATOM   1359 C  CB  . GLN A 1 172 ? 32.39600  6.48000   77.87800  1.000 77.71716  ?  172 GLN A CB  1 
ATOM   1360 C  CG  . GLN A 1 172 ? 32.21200  7.71900   78.73100  1.000 72.66822  ?  172 GLN A CG  1 
ATOM   1361 C  CD  . GLN A 1 172 ? 32.82100  8.94800   78.08800  1.000 81.98626  ?  172 GLN A CD  1 
ATOM   1362 O  OE1 . GLN A 1 172 ? 33.80100  8.85300   77.34800  1.000 85.16609  ?  172 GLN A OE1 1 
ATOM   1363 N  NE2 . GLN A 1 172 ? 32.23600  10.11000  78.35600  1.000 79.74024  ?  172 GLN A NE2 1 
ATOM   1364 N  N   . LYS A 1 173 ? 30.63800  5.40500   80.43100  1.000 80.50789  ?  173 LYS A N   1 
ATOM   1365 C  CA  . LYS A 1 173 ? 29.35700  5.27500   81.11800  1.000 70.94118  ?  173 LYS A CA  1 
ATOM   1366 C  C   . LYS A 1 173 ? 28.57200  6.56800   80.91800  1.000 66.39595  ?  173 LYS A C   1 
ATOM   1367 O  O   . LYS A 1 173 ? 28.83900  7.57700   81.57500  1.000 67.82849  ?  173 LYS A O   1 
ATOM   1368 C  CB  . LYS A 1 173 ? 29.59800  4.97900   82.59200  1.000 74.37462  ?  173 LYS A CB  1 
ATOM   1369 C  CG  . LYS A 1 173 ? 30.43900  3.72500   82.79500  1.000 77.88859  ?  173 LYS A CG  1 
ATOM   1370 C  CD  . LYS A 1 173 ? 29.85400  2.50300   82.11800  1.000 87.36952  ?  173 LYS A CD  1 
ATOM   1371 C  CE  . LYS A 1 173 ? 30.74000  1.29000   82.36200  1.000 87.98635  ?  173 LYS A CE  1 
ATOM   1372 N  NZ  . LYS A 1 173 ? 32.15100  1.56800   81.95100  1.000 88.59929  ?  173 LYS A NZ  1 
ATOM   1373 N  N   . VAL A 1 174 ? 27.59600  6.54400   80.01100  1.000 62.77247  ?  174 VAL A N   1 
ATOM   1374 C  CA  . VAL A 1 174 ? 26.69600  7.67100   79.78500  1.000 60.72540  ?  174 VAL A CA  1 
ATOM   1375 C  C   . VAL A 1 174 ? 25.27200  7.14100   79.71400  1.000 54.05014  ?  174 VAL A C   1 
ATOM   1376 O  O   . VAL A 1 174 ? 25.02600  6.07200   79.14600  1.000 54.82458  ?  174 VAL A O   1 
ATOM   1377 C  CB  . VAL A 1 174 ? 27.04200  8.45500   78.49800  1.000 65.44003  ?  174 VAL A CB  1 
ATOM   1378 C  CG1 . VAL A 1 174 ? 26.26300  9.76500   78.44800  1.000 63.59707  ?  174 VAL A CG1 1 
ATOM   1379 C  CG2 . VAL A 1 174 ? 28.53700  8.72000   78.40300  1.000 68.69501  ?  174 VAL A CG2 1 
ATOM   1380 N  N   . THR A 1 175 ? 24.33500  7.88300   80.30200  1.000 54.56016  ?  175 THR A N   1 
ATOM   1381 C  CA  . THR A 1 175 ? 22.93600  7.48200   80.35500  1.000 57.17367  ?  175 THR A CA  1 
ATOM   1382 C  C   . THR A 1 175 ? 22.05100  8.63800   79.91200  1.000 59.14753  ?  175 THR A C   1 
ATOM   1383 O  O   . THR A 1 175 ? 22.21800  9.76700   80.38300  1.000 63.55503  ?  175 THR A O   1 
ATOM   1384 C  CB  . THR A 1 175 ? 22.54900  7.02600   81.76400  1.000 57.19503  ?  175 THR A CB  1 
ATOM   1385 O  OG1 . THR A 1 175 ? 23.45300  6.00200   82.19500  1.000 65.00712  ?  175 THR A OG1 1 
ATOM   1386 C  CG2 . THR A 1 175 ? 21.14300  6.46800   81.77100  1.000 54.38002  ?  175 THR A CG2 1 
ATOM   1387 N  N   . ILE A 1 176 ? 21.11400  8.35200   79.00900  1.000 52.09767  ?  176 ILE A N   1 
ATOM   1388 C  CA  . ILE A 1 176 ? 20.20000  9.34800   78.46200  1.000 56.09378  ?  176 ILE A CA  1 
ATOM   1389 C  C   . ILE A 1 176 ? 18.83100  9.14200   79.09500  1.000 57.64486  ?  176 ILE A C   1 
ATOM   1390 O  O   . ILE A 1 176 ? 18.34700  8.00700   79.18100  1.000 60.61582  ?  176 ILE A O   1 
ATOM   1391 C  CB  . ILE A 1 176 ? 20.11700  9.24800   76.92900  1.000 60.22056  ?  176 ILE A CB  1 
ATOM   1392 C  CG1 . ILE A 1 176 ? 21.52000  9.21100   76.31900  1.000 58.90884  ?  176 ILE A CG1 1 
ATOM   1393 C  CG2 . ILE A 1 176 ? 19.31500  10.40400  76.36100  1.000 61.99437  ?  176 ILE A CG2 1 
ATOM   1394 C  CD1 . ILE A 1 176 ? 21.53000  8.96600   74.82500  1.000 59.87514  ?  176 ILE A CD1 1 
ATOM   1395 N  N   . HIS A 1 177 ? 18.19800  10.23800  79.51400  1.000 52.04519  ?  177 HIS A N   1 
ATOM   1396 C  CA  . HIS A 1 177 ? 16.91600  10.19300  80.20300  1.000 52.19571  ?  177 HIS A CA  1 
ATOM   1397 C  C   . HIS A 1 177 ? 15.93000  11.13400  79.53200  1.000 55.04516  ?  177 HIS A C   1 
ATOM   1398 O  O   . HIS A 1 177 ? 16.30200  12.22300  79.08500  1.000 55.97840  ?  177 HIS A O   1 
ATOM   1399 C  CB  . HIS A 1 177 ? 17.04500  10.59000  81.68300  1.000 61.79600  ?  177 HIS A CB  1 
ATOM   1400 C  CG  . HIS A 1 177 ? 18.12900  9.87000   82.42300  1.000 61.65382  ?  177 HIS A CG  1 
ATOM   1401 N  ND1 . HIS A 1 177 ? 17.89100  8.74000   83.17500  1.000 56.50227  ?  177 HIS A ND1 1 
ATOM   1402 C  CD2 . HIS A 1 177 ? 19.45300  10.12900  82.54100  1.000 60.54364  ?  177 HIS A CD2 1 
ATOM   1403 C  CE1 . HIS A 1 177 ? 19.02300  8.32900   83.71900  1.000 56.27191  ?  177 HIS A CE1 1 
ATOM   1404 N  NE2 . HIS A 1 177 ? 19.98500  9.15400   83.34800  1.000 57.08520  ?  177 HIS A NE2 1 
ATOM   1405 N  N   . GLY A 1 178 ? 14.66800  10.71500  79.47900  1.000 52.99160  ?  178 GLY A N   1 
ATOM   1406 C  CA  . GLY A 1 178 ? 13.61300  11.55900  78.95500  1.000 49.90091  ?  178 GLY A CA  1 
ATOM   1407 C  C   . GLY A 1 178 ? 12.56300  11.87800  79.99900  1.000 53.40688  ?  178 GLY A C   1 
ATOM   1408 O  O   . GLY A 1 178 ? 11.87500  10.97800  80.49000  1.000 54.04461  ?  178 GLY A O   1 
ATOM   1409 N  N   . TRP A 1 179 ? 12.43100  13.15300  80.35000  1.000 55.04280  ?  179 TRP A N   1 
ATOM   1410 C  CA  . TRP A 1 179 ? 11.52700  13.59100  81.40300  1.000 60.07399  ?  179 TRP A CA  1 
ATOM   1411 C  C   . TRP A 1 179 ? 10.55400  14.63600  80.87500  1.000 58.31503  ?  179 TRP A C   1 
ATOM   1412 O  O   . TRP A 1 179 ? 10.69000  15.15100  79.76300  1.000 56.07002  ?  179 TRP A O   1 
ATOM   1413 C  CB  . TRP A 1 179 ? 12.28800  14.17600  82.60000  1.000 57.74643  ?  179 TRP A CB  1 
ATOM   1414 C  CG  . TRP A 1 179 ? 13.15500  13.20800  83.33100  1.000 55.55511  ?  179 TRP A CG  1 
ATOM   1415 C  CD1 . TRP A 1 179 ? 13.22700  11.85800  83.14500  1.000 57.78952  ?  179 TRP A CD1 1 
ATOM   1416 C  CD2 . TRP A 1 179 ? 14.04900  13.51400  84.40300  1.000 61.23137  ?  179 TRP A CD2 1 
ATOM   1417 N  NE1 . TRP A 1 179 ? 14.13300  11.30800  84.02000  1.000 59.59509  ?  179 TRP A NE1 1 
ATOM   1418 C  CE2 . TRP A 1 179 ? 14.64900  12.30500  84.80600  1.000 62.96657  ?  179 TRP A CE2 1 
ATOM   1419 C  CE3 . TRP A 1 179 ? 14.40700  14.69700  85.05800  1.000 62.69078  ?  179 TRP A CE3 1 
ATOM   1420 C  CZ2 . TRP A 1 179 ? 15.58800  12.24500  85.83400  1.000 63.81206  ?  179 TRP A CZ2 1 
ATOM   1421 C  CZ3 . TRP A 1 179 ? 15.33800  14.63600  86.07700  1.000 63.23801  ?  179 TRP A CZ3 1 
ATOM   1422 C  CH2 . TRP A 1 179 ? 15.91800  13.41900  86.45500  1.000 64.97808  ?  179 TRP A CH2 1 
ATOM   1423 N  N   . ALA A 1 180 ? 9.56100   14.93900  81.70600  1.000 64.42832  ?  180 ALA A N   1 
ATOM   1424 C  CA  . ALA A 1 180 ? 8.63200   16.02800  81.45600  1.000 64.65446  ?  180 ALA A CA  1 
ATOM   1425 C  C   . ALA A 1 180 ? 8.08400   16.51900  82.78700  1.000 69.61384  ?  180 ALA A C   1 
ATOM   1426 O  O   . ALA A 1 180 ? 8.03700   15.77200  83.76800  1.000 65.61089  ?  180 ALA A O   1 
ATOM   1427 C  CB  . ALA A 1 180 ? 7.48600   15.59700  80.53300  1.000 55.36798  ?  180 ALA A CB  1 
ATOM   1428 N  N   . TYR A 1 181 ? 7.68700   17.78900  82.81700  1.000 67.85654  ?  181 TYR A N   1 
ATOM   1429 C  CA  . TYR A 1 181 ? 7.05400   18.36400  83.99300  1.000 65.80195  ?  181 TYR A CA  1 
ATOM   1430 C  C   . TYR A 1 181 ? 5.90900   19.25500  83.53900  1.000 69.09823  ?  181 TYR A C   1 
ATOM   1431 O  O   . TYR A 1 181 ? 5.89200   19.75400  82.41200  1.000 68.55666  ?  181 TYR A O   1 
ATOM   1432 C  CB  . TYR A 1 181 ? 8.03500   19.16200  84.86700  1.000 66.20050  ?  181 TYR A CB  1 
ATOM   1433 C  CG  . TYR A 1 181 ? 8.46500   20.50200  84.30500  1.000 70.78108  ?  181 TYR A CG  1 
ATOM   1434 C  CD1 . TYR A 1 181 ? 9.56000   20.60500  83.45900  1.000 73.44229  ?  181 TYR A CD1 1 
ATOM   1435 C  CD2 . TYR A 1 181 ? 7.78300   21.66700  84.63600  1.000 71.58428  ?  181 TYR A CD2 1 
ATOM   1436 C  CE1 . TYR A 1 181 ? 9.96000   21.83100  82.95400  1.000 71.20967  ?  181 TYR A CE1 1 
ATOM   1437 C  CE2 . TYR A 1 181 ? 8.17300   22.89400  84.13200  1.000 71.82622  ?  181 TYR A CE2 1 
ATOM   1438 C  CZ  . TYR A 1 181 ? 9.26300   22.96900  83.29400  1.000 69.56119  ?  181 TYR A CZ  1 
ATOM   1439 O  OH  . TYR A 1 181 ? 9.65800   24.18700  82.79200  1.000 77.09852  ?  181 TYR A OH  1 
ATOM   1440 N  N   . GLY A 1 182 ? 4.94500   19.44400  84.43100  1.000 72.32354  ?  182 GLY A N   1 
ATOM   1441 C  CA  . GLY A 1 182 ? 3.77200   20.24700  84.15100  1.000 74.12602  ?  182 GLY A CA  1 
ATOM   1442 C  C   . GLY A 1 182 ? 3.82300   21.53700  84.94200  1.000 77.23498  ?  182 GLY A C   1 
ATOM   1443 O  O   . GLY A 1 182 ? 4.47000   21.61300  85.98900  1.000 82.15361  ?  182 GLY A O   1 
ATOM   1444 N  N   . ILE A 1 183 ? 3.15200   22.56900  84.42200  1.000 80.15014  ?  183 ILE A N   1 
ATOM   1445 C  CA  . ILE A 1 183 ? 3.08100   23.84300  85.13400  1.000 78.55081  ?  183 ILE A CA  1 
ATOM   1446 C  C   . ILE A 1 183 ? 2.04200   23.82100  86.24000  1.000 84.30116  ?  183 ILE A C   1 
ATOM   1447 O  O   . ILE A 1 183 ? 1.95900   24.77500  87.02600  1.000 86.42918  ?  183 ILE A O   1 
ATOM   1448 C  CB  . ILE A 1 183 ? 2.82900   24.96800  84.10800  1.000 80.94110  ?  183 ILE A CB  1 
ATOM   1449 C  CG1 . ILE A 1 183 ? 3.92700   24.96600  83.04700  1.000 93.10549  ?  183 ILE A CG1 1 
ATOM   1450 C  CG2 . ILE A 1 183 ? 2.70200   26.33400  84.78300  1.000 83.63069  ?  183 ILE A CG2 1 
ATOM   1451 C  CD1 . ILE A 1 183 ? 5.31600   25.15900  83.61700  1.000 89.45854  ?  183 ILE A CD1 1 
ATOM   1452 N  N   . HIS A 1 184 ? 1.28500   22.72900  86.36400  1.000 86.78344  ?  184 HIS A N   1 
ATOM   1453 C  CA  . HIS A 1 184 ? 0.31100   22.59300  87.44000  1.000 85.08068  ?  184 HIS A CA  1 
ATOM   1454 C  C   . HIS A 1 184 ? 0.95400   22.19100  88.76100  1.000 87.00905  ?  184 HIS A C   1 
ATOM   1455 O  O   . HIS A 1 184 ? 0.47100   22.59700  89.82400  1.000 89.17808  ?  184 HIS A O   1 
ATOM   1456 C  CB  . HIS A 1 184 ? -0.76200  21.57400  87.05000  1.000 83.32563  ?  184 HIS A CB  1 
ATOM   1457 C  CG  . HIS A 1 184 ? -0.21000  20.26700  86.57300  1.000 87.54850  ?  184 HIS A CG  1 
ATOM   1458 N  ND1 . HIS A 1 184 ? 0.40500   20.12200  85.34800  1.000 93.57226  ?  184 HIS A ND1 1 
ATOM   1459 C  CD2 . HIS A 1 184 ? -0.16800  19.04900  87.16200  1.000 83.85126  ?  184 HIS A CD2 1 
ATOM   1460 C  CE1 . HIS A 1 184 ? 0.79500   18.86800  85.19900  1.000 92.61997  ?  184 HIS A CE1 1 
ATOM   1461 N  NE2 . HIS A 1 184 ? 0.46000   18.19600  86.28600  1.000 90.76129  ?  184 HIS A NE2 1 
ATOM   1462 N  N   . ASP A 1 185 ? 2.03000   21.40100  88.72800  1.000 82.76358  ?  185 ASP A N   1 
ATOM   1463 C  CA  . ASP A 1 185 ? 2.67500   20.98700  89.97000  1.000 83.47637  ?  185 ASP A CA  1 
ATOM   1464 C  C   . ASP A 1 185 ? 4.19600   20.99000  89.94100  1.000 82.14191  ?  185 ASP A C   1 
ATOM   1465 O  O   . ASP A 1 185 ? 4.79900   20.87800  91.01300  1.000 80.02989  ?  185 ASP A O   1 
ATOM   1466 C  CB  . ASP A 1 185 ? 2.19900   19.58300  90.38000  1.000 77.90634  ?  185 ASP A CB  1 
ATOM   1467 C  CG  . ASP A 1 185 ? 2.49400   18.52400  89.32500  1.000 81.97512  ?  185 ASP A CG  1 
ATOM   1468 O  OD1 . ASP A 1 185 ? 3.12200   18.85000  88.29300  1.000 84.17157  ?  185 ASP A OD1 1 
ATOM   1469 O  OD2 . ASP A 1 185 ? 2.10600   17.35500  89.53900  1.000 73.62325  -1 185 ASP A OD2 1 
ATOM   1470 N  N   . GLY A 1 186 ? 4.84100   21.10200  88.78300  1.000 72.53890  ?  186 GLY A N   1 
ATOM   1471 C  CA  . GLY A 1 186 ? 6.29000   21.06500  88.76400  1.000 64.60421  ?  186 GLY A CA  1 
ATOM   1472 C  C   . GLY A 1 186 ? 6.87500   19.70500  89.06200  1.000 64.63386  ?  186 GLY A C   1 
ATOM   1473 O  O   . GLY A 1 186 ? 8.04700   19.61000  89.43600  1.000 63.12449  ?  186 GLY A O   1 
ATOM   1474 N  N   . LEU A 1 187 ? 6.08100   18.64900  88.93100  1.000 65.57243  ?  187 LEU A N   1 
ATOM   1475 C  CA  . LEU A 1 187 ? 6.51500   17.29300  89.23800  1.000 66.43941  ?  187 LEU A CA  1 
ATOM   1476 C  C   . LEU A 1 187 ? 7.08700   16.63500  87.98600  1.000 66.42938  ?  187 LEU A C   1 
ATOM   1477 O  O   . LEU A 1 187 ? 6.40100   16.54200  86.96100  1.000 60.66234  ?  187 LEU A O   1 
ATOM   1478 C  CB  . LEU A 1 187 ? 5.34100   16.48300  89.78900  1.000 68.19418  ?  187 LEU A CB  1 
ATOM   1479 C  CG  . LEU A 1 187 ? 5.64300   15.13900  90.44800  1.000 62.35686  ?  187 LEU A CG  1 
ATOM   1480 C  CD1 . LEU A 1 187 ? 6.53900   15.33200  91.65600  1.000 64.95091  ?  187 LEU A CD1 1 
ATOM   1481 C  CD2 . LEU A 1 187 ? 4.34800   14.45100  90.84800  1.000 60.15976  ?  187 LEU A CD2 1 
ATOM   1482 N  N   . LEU A 1 188 ? 8.33800   16.17700  88.06400  1.000 61.23062  ?  188 LEU A N   1 
ATOM   1483 C  CA  . LEU A 1 188 ? 8.92200   15.45600  86.94000  1.000 59.59939  ?  188 LEU A CA  1 
ATOM   1484 C  C   . LEU A 1 188 ? 8.27200   14.08900  86.77300  1.000 61.39857  ?  188 LEU A C   1 
ATOM   1485 O  O   . LEU A 1 188 ? 8.19300   13.30100  87.72000  1.000 65.45303  ?  188 LEU A O   1 
ATOM   1486 C  CB  . LEU A 1 188 ? 10.43700  15.28400  87.09300  1.000 56.84329  ?  188 LEU A CB  1 
ATOM   1487 C  CG  . LEU A 1 188 ? 11.45200  16.39900  86.80200  1.000 63.15088  ?  188 LEU A CG  1 
ATOM   1488 C  CD1 . LEU A 1 188 ? 11.05300  17.16600  85.54600  1.000 67.36130  ?  188 LEU A CD1 1 
ATOM   1489 C  CD2 . LEU A 1 188 ? 11.70700  17.34400  87.94700  1.000 62.33810  ?  188 LEU A CD2 1 
ATOM   1490 N  N   . ARG A 1 189 ? 7.80800   13.81800  85.55900  1.000 67.39882  ?  189 ARG A N   1 
ATOM   1491 C  CA  . ARG A 1 189 ? 7.32600   12.50500  85.16000  1.000 64.61697  ?  189 ARG A CA  1 
ATOM   1492 C  C   . ARG A 1 189 ? 8.40200   11.85600  84.30100  1.000 64.31974  ?  189 ARG A C   1 
ATOM   1493 O  O   . ARG A 1 189 ? 8.84500   12.44400  83.30900  1.000 62.24349  ?  189 ARG A O   1 
ATOM   1494 C  CB  . ARG A 1 189 ? 6.01700   12.61000  84.37400  1.000 68.02461  ?  189 ARG A CB  1 
ATOM   1495 C  CG  . ARG A 1 189 ? 5.57500   11.29400  83.74700  1.000 78.95779  ?  189 ARG A CG  1 
ATOM   1496 C  CD  . ARG A 1 189 ? 4.28200   11.41200  82.93700  1.000 85.83357  ?  189 ARG A CD  1 
ATOM   1497 N  NE  . ARG A 1 189 ? 3.07400   11.44500  83.75400  1.000 81.66137  ?  189 ARG A NE  1 
ATOM   1498 C  CZ  . ARG A 1 189 ? 2.36300   12.53600  84.00700  1.000 83.65284  ?  189 ARG A CZ  1 
ATOM   1499 N  NH1 . ARG A 1 189 ? 2.71500   13.71800  83.52800  1.000 79.33065  ?  189 ARG A NH1 1 
ATOM   1500 N  NH2 . ARG A 1 189 ? 1.26200   12.43500  84.74600  1.000 89.88931  ?  189 ARG A NH2 1 
ATOM   1501 N  N   . ASP A 1 190 ? 8.83100   10.65800  84.68600  1.000 66.72849  ?  190 ASP A N   1 
ATOM   1502 C  CA  . ASP A 1 190 ? 9.83300   9.92700   83.92200  1.000 63.21777  ?  190 ASP A CA  1 
ATOM   1503 C  C   . ASP A 1 190 ? 9.13900   9.15500   82.80600  1.000 62.43933  ?  190 ASP A C   1 
ATOM   1504 O  O   . ASP A 1 190 ? 8.30200   8.28400   83.07200  1.000 56.48193  ?  190 ASP A O   1 
ATOM   1505 C  CB  . ASP A 1 190 ? 10.64000  8.98600   84.81600  1.000 66.98083  ?  190 ASP A CB  1 
ATOM   1506 C  CG  . ASP A 1 190 ? 11.90400  8.47500   84.13600  1.000 66.32063  ?  190 ASP A CG  1 
ATOM   1507 O  OD1 . ASP A 1 190 ? 11.91400  8.34400   82.89300  1.000 71.56269  ?  190 ASP A OD1 1 
ATOM   1508 O  OD2 . ASP A 1 190 ? 12.89900  8.21700   84.84800  1.000 67.78308  -1 190 ASP A OD2 1 
ATOM   1509 N  N   . LEU A 1 191 ? 9.48800   9.47900   81.56300  1.000 70.52623  ?  191 LEU A N   1 
ATOM   1510 C  CA  . LEU A 1 191 ? 8.88400   8.87000   80.38400  1.000 59.90955  ?  191 LEU A CA  1 
ATOM   1511 C  C   . LEU A 1 191 ? 9.41000   7.47100   80.09200  1.000 61.89857  ?  191 LEU A C   1 
ATOM   1512 O  O   . LEU A 1 191 ? 8.95800   6.85200   79.12200  1.000 59.80537  ?  191 LEU A O   1 
ATOM   1513 C  CB  . LEU A 1 191 ? 9.10200   9.77200   79.17000  1.000 57.57916  ?  191 LEU A CB  1 
ATOM   1514 C  CG  . LEU A 1 191 ? 8.43300   11.14000  79.28900  1.000 58.22866  ?  191 LEU A CG  1 
ATOM   1515 C  CD1 . LEU A 1 191 ? 8.72500   11.98900  78.06800  1.000 66.71669  ?  191 LEU A CD1 1 
ATOM   1516 C  CD2 . LEU A 1 191 ? 6.93500   10.97400  79.47800  1.000 63.34253  ?  191 LEU A CD2 1 
ATOM   1517 N  N   . ASP A 1 192 ? 10.35900  6.97300   80.89000  1.000 60.22775  ?  192 ASP A N   1 
ATOM   1518 C  CA  . ASP A 1 192 ? 10.77800  5.57000   80.85000  1.000 60.55528  ?  192 ASP A CA  1 
ATOM   1519 C  C   . ASP A 1 192 ? 11.45900  5.21000   79.52800  1.000 60.66496  ?  192 ASP A C   1 
ATOM   1520 O  O   . ASP A 1 192 ? 11.18100  4.17000   78.93000  1.000 60.74451  ?  192 ASP A O   1 
ATOM   1521 C  CB  . ASP A 1 192 ? 9.59400   4.63900   81.11800  1.000 66.00940  ?  192 ASP A CB  1 
ATOM   1522 C  CG  . ASP A 1 192 ? 10.01600  3.34600   81.75700  1.000 69.49265  ?  192 ASP A CG  1 
ATOM   1523 O  OD1 . ASP A 1 192 ? 11.20400  3.24000   82.13400  1.000 67.46200  ?  192 ASP A OD1 1 
ATOM   1524 O  OD2 . ASP A 1 192 ? 9.18000   2.42200   81.86000  1.000 66.44204  -1 192 ASP A OD2 1 
ATOM   1525 N  N   . VAL A 1 193 ? 12.37300  6.07100   79.08500  1.000 58.82658  ?  193 VAL A N   1 
ATOM   1526 C  CA  . VAL A 1 193 ? 13.16000  5.79900   77.88700  1.000 61.53753  ?  193 VAL A CA  1 
ATOM   1527 C  C   . VAL A 1 193 ? 14.63800  5.85200   78.25000  1.000 58.90498  ?  193 VAL A C   1 
ATOM   1528 O  O   . VAL A 1 193 ? 15.48600  6.17300   77.41000  1.000 62.19216  ?  193 VAL A O   1 
ATOM   1529 C  CB  . VAL A 1 193 ? 12.82500  6.78200   76.74900  1.000 62.01144  ?  193 VAL A CB  1 
ATOM   1530 C  CG1 . VAL A 1 193 ? 11.40600  6.55100   76.25100  1.000 59.85842  ?  193 VAL A CG1 1 
ATOM   1531 C  CG2 . VAL A 1 193 ? 13.00300  8.22000   77.21100  1.000 55.80384  ?  193 VAL A CG2 1 
ATOM   1532 N  N   . THR A 1 194 ? 14.94900  5.53700   79.50600  1.000 59.70884  ?  194 THR A N   1 
ATOM   1533 C  CA  . THR A 1 194 ? 16.31600  5.62800   80.00400  1.000 57.23116  ?  194 THR A CA  1 
ATOM   1534 C  C   . THR A 1 194 ? 17.19500  4.61200   79.28800  1.000 60.71205  ?  194 THR A C   1 
ATOM   1535 O  O   . THR A 1 194 ? 16.92500  3.40800   79.33600  1.000 66.22802  ?  194 THR A O   1 
ATOM   1536 C  CB  . THR A 1 194 ? 16.34400  5.38300   81.51000  1.000 59.72057  ?  194 THR A CB  1 
ATOM   1537 O  OG1 . THR A 1 194 ? 15.68700  6.46300   82.18400  1.000 73.70273  ?  194 THR A OG1 1 
ATOM   1538 C  CG2 . THR A 1 194 ? 17.77200  5.27900   82.00700  1.000 55.16680  ?  194 THR A CG2 1 
ATOM   1539 N  N   . ALA A 1 195 ? 18.26000  5.08700   78.64900  1.000 58.43447  ?  195 ALA A N   1 
ATOM   1540 C  CA  . ALA A 1 195 ? 19.11500  4.24600   77.82500  1.000 59.61094  ?  195 ALA A CA  1 
ATOM   1541 C  C   . ALA A 1 195 ? 20.55100  4.30600   78.32100  1.000 59.49050  ?  195 ALA A C   1 
ATOM   1542 O  O   . ALA A 1 195 ? 21.04600  5.37400   78.69500  1.000 58.57218  ?  195 ALA A O   1 
ATOM   1543 C  CB  . ALA A 1 195 ? 19.05700  4.67200   76.35600  1.000 66.14899  ?  195 ALA A CB  1 
ATOM   1544 N  N   . THR A 1 196 ? 21.21400  3.14800   78.31800  1.000 63.46680  ?  196 THR A N   1 
ATOM   1545 C  CA  . THR A 1 196 ? 22.61800  3.04400   78.68500  1.000 66.97795  ?  196 THR A CA  1 
ATOM   1546 C  C   . THR A 1 196 ? 23.48500  2.48900   77.56500  1.000 66.41652  ?  196 THR A C   1 
ATOM   1547 O  O   . THR A 1 196 ? 24.71400  2.48700   77.70000  1.000 69.40191  ?  196 THR A O   1 
ATOM   1548 C  CB  . THR A 1 196 ? 22.79300  2.16900   79.93800  1.000 66.25374  ?  196 THR A CB  1 
ATOM   1549 O  OG1 . THR A 1 196 ? 22.33900  0.83700   79.66600  1.000 69.00020  ?  196 THR A OG1 1 
ATOM   1550 C  CG2 . THR A 1 196 ? 22.00400  2.74500   81.10600  1.000 58.36224  ?  196 THR A CG2 1 
ATOM   1551 N  N   . ASN A 1 197 ? 22.88500  2.01900   76.47500  1.000 66.08914  ?  197 ASN A N   1 
ATOM   1552 C  CA  . ASN A 1 197 ? 23.61300  1.54500   75.30500  1.000 66.45471  ?  197 ASN A CA  1 
ATOM   1553 C  C   . ASN A 1 197 ? 22.66600  1.62300   74.11400  1.000 69.92074  ?  197 ASN A C   1 
ATOM   1554 O  O   . ASN A 1 197 ? 21.53100  2.09500   74.23200  1.000 65.76651  ?  197 ASN A O   1 
ATOM   1555 C  CB  . ASN A 1 197 ? 24.14900  0.12200   75.50700  1.000 64.25265  ?  197 ASN A CB  1 
ATOM   1556 C  CG  . ASN A 1 197 ? 23.06400  -0.87000  75.89000  1.000 67.32287  ?  197 ASN A CG  1 
ATOM   1557 O  OD1 . ASN A 1 197 ? 21.99000  -0.90400  75.28700  1.000 71.22740  ?  197 ASN A OD1 1 
ATOM   1558 N  ND2 . ASN A 1 197 ? 23.34900  -1.69700  76.88600  1.000 68.75549  ?  197 ASN A ND2 1 
ATOM   1559 N  N   . ARG A 1 198 ? 23.14600  1.16500   72.95400  1.000 68.47804  ?  198 ARG A N   1 
ATOM   1560 C  CA  . ARG A 1 198 ? 22.32600  1.24400   71.74900  1.000 67.58827  ?  198 ARG A CA  1 
ATOM   1561 C  C   . ARG A 1 198 ? 21.13800  0.29000   71.82100  1.000 66.57051  ?  198 ARG A C   1 
ATOM   1562 O  O   . ARG A 1 198 ? 20.03800  0.63200   71.37200  1.000 64.69007  ?  198 ARG A O   1 
ATOM   1563 C  CB  . ARG A 1 198 ? 23.17300  0.98500   70.50000  1.000 75.64770  ?  198 ARG A CB  1 
ATOM   1564 C  CG  . ARG A 1 198 ? 23.98900  -0.28600  70.52200  1.000 84.53889  ?  198 ARG A CG  1 
ATOM   1565 C  CD  . ARG A 1 198 ? 24.83000  -0.41200  69.26500  1.000 83.84483  ?  198 ARG A CD  1 
ATOM   1566 N  NE  . ARG A 1 198 ? 24.01300  -0.38700  68.05800  1.000 94.32135  ?  198 ARG A NE  1 
ATOM   1567 C  CZ  . ARG A 1 198 ? 23.35800  -1.43500  67.57700  1.000 99.99132  ?  198 ARG A CZ  1 
ATOM   1568 N  NH1 . ARG A 1 198 ? 23.38900  -2.60800  68.18700  1.000 89.42587  ?  198 ARG A NH1 1 
ATOM   1569 N  NH2 . ARG A 1 198 ? 22.65500  -1.30200  66.45600  1.000 101.94789 ?  198 ARG A NH2 1 
ATOM   1570 N  N   . GLU A 1 199 ? 21.33200  -0.90600  72.39000  1.000 68.22137  ?  199 GLU A N   1 
ATOM   1571 C  CA  . GLU A 1 199 ? 20.24800  -1.88600  72.41100  1.000 66.89129  ?  199 GLU A CA  1 
ATOM   1572 C  C   . GLU A 1 199 ? 19.12100  -1.44000  73.33100  1.000 64.79942  ?  199 GLU A C   1 
ATOM   1573 O  O   . GLU A 1 199 ? 17.94100  -1.57700  72.98600  1.000 65.73986  ?  199 GLU A O   1 
ATOM   1574 C  CB  . GLU A 1 199 ? 20.75800  -3.25900  72.86000  1.000 63.72371  ?  199 GLU A CB  1 
ATOM   1575 C  CG  . GLU A 1 199 ? 21.90300  -3.84500  72.04900  1.000 68.01588  ?  199 GLU A CG  1 
ATOM   1576 C  CD  . GLU A 1 199 ? 23.26100  -3.36700  72.53200  1.000 75.48997  ?  199 GLU A CD  1 
ATOM   1577 O  OE1 . GLU A 1 199 ? 23.37400  -2.19000  72.93700  1.000 70.56375  ?  199 GLU A OE1 1 
ATOM   1578 O  OE2 . GLU A 1 199 ? 24.21500  -4.17600  72.51800  1.000 83.37327  -1 199 GLU A OE2 1 
ATOM   1579 N  N   . THR A 1 200 ? 19.46300  -0.91600  74.51000  1.000 66.94961  ?  200 THR A N   1 
ATOM   1580 C  CA  . THR A 1 200 ? 18.43700  -0.42600  75.42400  1.000 63.99192  ?  200 THR A CA  1 
ATOM   1581 C  C   . THR A 1 200 ? 17.69900  0.76500   74.83000  1.000 67.37901  ?  200 THR A C   1 
ATOM   1582 O  O   . THR A 1 200 ? 16.48300  0.89700   75.00700  1.000 66.22945  ?  200 THR A O   1 
ATOM   1583 C  CB  . THR A 1 200 ? 19.06200  -0.05700  76.76800  1.000 56.78298  ?  200 THR A CB  1 
ATOM   1584 O  OG1 . THR A 1 200 ? 20.11200  0.89500   76.55900  1.000 66.58882  ?  200 THR A OG1 1 
ATOM   1585 C  CG2 . THR A 1 200 ? 19.64000  -1.29500  77.43400  1.000 58.00708  ?  200 THR A CG2 1 
ATOM   1586 N  N   . LEU A 1 201 ? 18.42200  1.64200   74.12300  1.000 65.87283  ?  201 LEU A N   1 
ATOM   1587 C  CA  . LEU A 1 201 ? 17.78300  2.77400   73.45700  1.000 63.66967  ?  201 LEU A CA  1 
ATOM   1588 C  C   . LEU A 1 201 ? 16.68600  2.30600   72.51200  1.000 64.14170  ?  201 LEU A C   1 
ATOM   1589 O  O   . LEU A 1 201 ? 15.60900  2.91200   72.44400  1.000 65.68613  ?  201 LEU A O   1 
ATOM   1590 C  CB  . LEU A 1 201 ? 18.81700  3.59700   72.69200  1.000 63.08153  ?  201 LEU A CB  1 
ATOM   1591 C  CG  . LEU A 1 201 ? 18.20800  4.78000   71.94000  1.000 67.88869  ?  201 LEU A CG  1 
ATOM   1592 C  CD1 . LEU A 1 201 ? 17.85800  5.90300   72.90800  1.000 62.55915  ?  201 LEU A CD1 1 
ATOM   1593 C  CD2 . LEU A 1 201 ? 19.11800  5.26400   70.82500  1.000 62.25661  ?  201 LEU A CD2 1 
ATOM   1594 N  N   . GLU A 1 202 ? 16.94300  1.22200   71.77800  1.000 62.81112  ?  202 GLU A N   1 
ATOM   1595 C  CA  . GLU A 1 202 ? 15.95100  0.69600   70.84900  1.000 61.24907  ?  202 GLU A CA  1 
ATOM   1596 C  C   . GLU A 1 202 ? 14.74200  0.16500   71.60700  1.000 62.35647  ?  202 GLU A C   1 
ATOM   1597 O  O   . GLU A 1 202 ? 13.59800  0.54000   71.31800  1.000 57.12436  ?  202 GLU A O   1 
ATOM   1598 C  CB  . GLU A 1 202 ? 16.57100  -0.41000  69.99500  1.000 64.25964  ?  202 GLU A CB  1 
ATOM   1599 C  CG  . GLU A 1 202 ? 15.74500  -0.78600  68.77700  1.000 66.87620  ?  202 GLU A CG  1 
ATOM   1600 C  CD  . GLU A 1 202 ? 15.52600  0.38800   67.84300  1.000 76.55424  ?  202 GLU A CD  1 
ATOM   1601 O  OE1 . GLU A 1 202 ? 16.37800  1.30600   67.83200  1.000 73.75870  ?  202 GLU A OE1 1 
ATOM   1602 O  OE2 . GLU A 1 202 ? 14.49500  0.40200   67.13400  1.000 79.34844  -1 202 GLU A OE2 1 
ATOM   1603 N  N   . GLN A 1 203 ? 14.98300  -0.73100  72.56600  1.000 69.22816  ?  203 GLN A N   1 
ATOM   1604 C  CA  . GLN A 1 203 ? 13.90300  -1.33600  73.33900  1.000 64.99099  ?  203 GLN A CA  1 
ATOM   1605 C  C   . GLN A 1 203 ? 13.11200  -0.28300  74.11100  1.000 63.14719  ?  203 GLN A C   1 
ATOM   1606 O  O   . GLN A 1 203 ? 11.87600  -0.31200  74.13200  1.000 63.36841  ?  203 GLN A O   1 
ATOM   1607 C  CB  . GLN A 1 203 ? 14.47700  -2.39800  74.27400  1.000 62.68043  ?  203 GLN A CB  1 
ATOM   1608 C  CG  . GLN A 1 203 ? 13.43900  -3.13100  75.08900  1.000 77.66289  ?  203 GLN A CG  1 
ATOM   1609 C  CD  . GLN A 1 203 ? 14.01800  -4.31500  75.83500  1.000 88.88823  ?  203 GLN A CD  1 
ATOM   1610 O  OE1 . GLN A 1 203 ? 15.19200  -4.64900  75.67700  1.000 96.19723  ?  203 GLN A OE1 1 
ATOM   1611 N  NE2 . GLN A 1 203 ? 13.19400  -4.95900  76.65400  1.000 85.91611  ?  203 GLN A NE2 1 
ATOM   1612 N  N   . ARG A 1 204 ? 13.81500  0.64400   74.77200  1.000 59.47110  ?  204 ARG A N   1 
ATOM   1613 C  CA  . ARG A 1 204 ? 13.14800  1.71500   75.51400  1.000 58.92201  ?  204 ARG A CA  1 
ATOM   1614 C  C   . ARG A 1 204 ? 12.20800  2.52000   74.62700  1.000 63.60076  ?  204 ARG A C   1 
ATOM   1615 O  O   . ARG A 1 204 ? 11.05800  2.78000   75.00200  1.000 65.01801  ?  204 ARG A O   1 
ATOM   1616 C  CB  . ARG A 1 204 ? 14.18800  2.64600   76.14500  1.000 61.43845  ?  204 ARG A CB  1 
ATOM   1617 C  CG  . ARG A 1 204 ? 14.84300  2.17900   77.43300  1.000 63.65772  ?  204 ARG A CG  1 
ATOM   1618 C  CD  . ARG A 1 204 ? 13.79600  1.88200   78.49100  1.000 54.73069  ?  204 ARG A CD  1 
ATOM   1619 N  NE  . ARG A 1 204 ? 13.28700  0.52200   78.44800  1.000 51.68239  ?  204 ARG A NE  1 
ATOM   1620 C  CZ  . ARG A 1 204 ? 12.05400  0.18700   78.79900  1.000 57.22035  ?  204 ARG A CZ  1 
ATOM   1621 N  NH1 . ARG A 1 204 ? 11.17700  1.09400   79.20000  1.000 59.15314  ?  204 ARG A NH1 1 
ATOM   1622 N  NH2 . ARG A 1 204 ? 11.69400  -1.08700  78.75100  1.000 55.15798  ?  204 ARG A NH2 1 
ATOM   1623 N  N   . TYR A 1 205 ? 12.68200  2.93200   73.44900  1.000 58.16106  ?  205 TYR A N   1 
ATOM   1624 C  CA  . TYR A 1 205 ? 11.85300  3.73400   72.55600  1.000 55.65872  ?  205 TYR A CA  1 
ATOM   1625 C  C   . TYR A 1 205 ? 10.59300  2.98900   72.12800  1.000 60.58489  ?  205 TYR A C   1 
ATOM   1626 O  O   . TYR A 1 205 ? 9.48300   3.52100   72.24300  1.000 61.79685  ?  205 TYR A O   1 
ATOM   1627 C  CB  . TYR A 1 205 ? 12.66400  4.16700   71.33700  1.000 68.15175  ?  205 TYR A CB  1 
ATOM   1628 C  CG  . TYR A 1 205 ? 11.81600  4.79500   70.25900  1.000 66.12111  ?  205 TYR A CG  1 
ATOM   1629 C  CD1 . TYR A 1 205 ? 11.24300  6.04700   70.43700  1.000 63.83191  ?  205 TYR A CD1 1 
ATOM   1630 C  CD2 . TYR A 1 205 ? 11.58500  4.13200   69.06300  1.000 61.97894  ?  205 TYR A CD2 1 
ATOM   1631 C  CE1 . TYR A 1 205 ? 10.46200  6.61900   69.45100  1.000 63.72010  ?  205 TYR A CE1 1 
ATOM   1632 C  CE2 . TYR A 1 205 ? 10.80800  4.69500   68.07300  1.000 67.01322  ?  205 TYR A CE2 1 
ATOM   1633 C  CZ  . TYR A 1 205 ? 10.24800  5.93900   68.26900  1.000 65.81038  ?  205 TYR A CZ  1 
ATOM   1634 O  OH  . TYR A 1 205 ? 9.47300   6.50200   67.27800  1.000 60.08874  ?  205 TYR A OH  1 
ATOM   1635 N  N   . ARG A 1 206 ? 10.74000  1.75400   71.63900  1.000 62.65589  ?  206 ARG A N   1 
ATOM   1636 C  CA  . ARG A 1 206 ? 9.57200   0.98200   71.21800  1.000 65.63907  ?  206 ARG A CA  1 
ATOM   1637 C  C   . ARG A 1 206 ? 8.58200   0.78800   72.36100  1.000 63.14876  ?  206 ARG A C   1 
ATOM   1638 O  O   . ARG A 1 206 ? 7.37400   0.98400   72.18600  1.000 62.06488  ?  206 ARG A O   1 
ATOM   1639 C  CB  . ARG A 1 206 ? 10.00600  -0.36500  70.63600  1.000 61.44069  ?  206 ARG A CB  1 
ATOM   1640 C  CG  . ARG A 1 206 ? 11.02400  -0.25600  69.51100  1.000 66.51310  ?  206 ARG A CG  1 
ATOM   1641 C  CD  . ARG A 1 206 ? 10.41200  0.41700   68.28700  1.000 75.41436  ?  206 ARG A CD  1 
ATOM   1642 N  NE  . ARG A 1 206 ? 11.35100  0.51600   67.17600  1.000 72.00760  ?  206 ARG A NE  1 
ATOM   1643 C  CZ  . ARG A 1 206 ? 11.09600  1.15800   66.04400  1.000 85.87181  ?  206 ARG A CZ  1 
ATOM   1644 N  NH1 . ARG A 1 206 ? 9.94100   1.77100   65.84300  1.000 87.48061  ?  206 ARG A NH1 1 
ATOM   1645 N  NH2 . ARG A 1 206 ? 12.02000  1.18000   65.08700  1.000 84.64230  ?  206 ARG A NH2 1 
ATOM   1646 N  N   . HIS A 1 207 ? 9.07500   0.39500   73.53900  1.000 65.24845  ?  207 HIS A N   1 
ATOM   1647 C  CA  . HIS A 1 207 ? 8.18600   0.21800   74.68300  1.000 65.33528  ?  207 HIS A CA  1 
ATOM   1648 C  C   . HIS A 1 207 ? 7.49400   1.52300   75.05800  1.000 61.74144  ?  207 HIS A C   1 
ATOM   1649 O  O   . HIS A 1 207 ? 6.31400   1.52300   75.42800  1.000 63.24903  ?  207 HIS A O   1 
ATOM   1650 C  CB  . HIS A 1 207 ? 8.95800   -0.34300  75.87500  1.000 68.44852  ?  207 HIS A CB  1 
ATOM   1651 C  CG  . HIS A 1 207 ? 9.17100   -1.82300  75.80900  1.000 74.20269  ?  207 HIS A CG  1 
ATOM   1652 N  ND1 . HIS A 1 207 ? 10.25100  -2.39300  75.17100  1.000 77.73287  ?  207 HIS A ND1 1 
ATOM   1653 C  CD2 . HIS A 1 207 ? 8.44700   -2.85100  76.31200  1.000 79.61262  ?  207 HIS A CD2 1 
ATOM   1654 C  CE1 . HIS A 1 207 ? 10.18000  -3.70800  75.27700  1.000 79.37997  ?  207 HIS A CE1 1 
ATOM   1655 N  NE2 . HIS A 1 207 ? 9.09600   -4.01200  75.96800  1.000 78.45210  ?  207 HIS A NE2 1 
ATOM   1656 N  N   . GLY A 1 208 ? 8.21900   2.64100   74.99100  1.000 60.31839  ?  208 GLY A N   1 
ATOM   1657 C  CA  . GLY A 1 208 ? 7.60100   3.93300   75.24600  1.000 63.90396  ?  208 GLY A CA  1 
ATOM   1658 C  C   . GLY A 1 208 ? 6.41500   4.20500   74.34000  1.000 69.36006  ?  208 GLY A C   1 
ATOM   1659 O  O   . GLY A 1 208 ? 5.35500   4.64300   74.79800  1.000 75.00861  ?  208 GLY A O   1 
ATOM   1660 N  N   . ILE A 1 209 ? 6.57700   3.95200   73.03900  1.000 59.27180  ?  209 ILE A N   1 
ATOM   1661 C  CA  . ILE A 1 209 ? 5.47400   4.15500   72.10400  1.000 63.95020  ?  209 ILE A CA  1 
ATOM   1662 C  C   . ILE A 1 209 ? 4.38400   3.11500   72.33400  1.000 67.29604  ?  209 ILE A C   1 
ATOM   1663 O  O   . ILE A 1 209 ? 3.18800   3.42900   72.29600  1.000 73.20298  ?  209 ILE A O   1 
ATOM   1664 C  CB  . ILE A 1 209 ? 5.98500   4.12100   70.65200  1.000 63.14778  ?  209 ILE A CB  1 
ATOM   1665 C  CG1 . ILE A 1 209 ? 7.27900   4.92400   70.51100  1.000 58.54392  ?  209 ILE A CG1 1 
ATOM   1666 C  CG2 . ILE A 1 209 ? 4.92500   4.66500   69.70900  1.000 53.99588  ?  209 ILE A CG2 1 
ATOM   1667 C  CD1 . ILE A 1 209 ? 7.09600   6.41600   70.65100  1.000 53.29771  ?  209 ILE A CD1 1 
ATOM   1668 N  N   . SER A 1 210 ? 4.78000   1.86100   72.57000  1.000 64.72463  ?  210 SER A N   1 
ATOM   1669 C  CA  . SER A 1 210 ? 3.80500   0.79600   72.78300  1.000 71.37538  ?  210 SER A CA  1 
ATOM   1670 C  C   . SER A 1 210 ? 2.95000   1.05800   74.01800  1.000 76.88893  ?  210 SER A C   1 
ATOM   1671 O  O   . SER A 1 210 ? 1.74400   0.78700   74.01300  1.000 77.01446  ?  210 SER A O   1 
ATOM   1672 C  CB  . SER A 1 210 ? 4.52000   -0.55100  72.89200  1.000 69.37898  ?  210 SER A CB  1 
ATOM   1673 O  OG  . SER A 1 210 ? 3.59500   -1.62400  72.89000  1.000 82.87342  ?  210 SER A OG  1 
ATOM   1674 N  N   . ASN A 1 211 ? 3.55900   1.56000   75.09600  1.000 72.27117  ?  211 ASN A N   1 
ATOM   1675 C  CA  . ASN A 1 211 ? 2.79400   1.84700   76.30600  1.000 75.07151  ?  211 ASN A CA  1 
ATOM   1676 C  C   . ASN A 1 211 ? 1.77900   2.96300   76.07900  1.000 78.07142  ?  211 ASN A C   1 
ATOM   1677 O  O   . ASN A 1 211 ? 0.67800   2.92800   76.64200  1.000 86.15653  ?  211 ASN A O   1 
ATOM   1678 C  CB  . ASN A 1 211 ? 3.73200   2.20700   77.45900  1.000 74.81786  ?  211 ASN A CB  1 
ATOM   1679 C  CG  . ASN A 1 211 ? 4.42900   0.99500   78.04600  1.000 76.54291  ?  211 ASN A CG  1 
ATOM   1680 O  OD1 . ASN A 1 211 ? 3.85800   -0.09200  78.11400  1.000 72.35480  ?  211 ASN A OD1 1 
ATOM   1681 N  ND2 . ASN A 1 211 ? 5.66900   1.18100   78.49000  1.000 69.17349  ?  211 ASN A ND2 1 
ATOM   1682 N  N   . LEU A 1 212 ? 2.13000   3.96100   75.26300  1.000 70.93525  ?  212 LEU A N   1 
ATOM   1683 C  CA  . LEU A 1 212 ? 1.19800   5.04600   74.96400  1.000 71.96649  ?  212 LEU A CA  1 
ATOM   1684 C  C   . LEU A 1 212 ? -0.01400  4.55800   74.18200  1.000 85.57784  ?  212 LEU A C   1 
ATOM   1685 O  O   . LEU A 1 212 ? -1.07800  5.18500   74.24300  1.000 87.30408  ?  212 LEU A O   1 
ATOM   1686 C  CB  . LEU A 1 212 ? 1.90900   6.16800   74.20800  1.000 71.70873  ?  212 LEU A CB  1 
ATOM   1687 C  CG  . LEU A 1 212 ? 3.00900   6.89800   74.97500  1.000 59.04888  ?  212 LEU A CG  1 
ATOM   1688 C  CD1 . LEU A 1 212 ? 3.93800   7.62700   74.02500  1.000 62.70663  ?  212 LEU A CD1 1 
ATOM   1689 C  CD2 . LEU A 1 212 ? 2.37700   7.88000   75.95100  1.000 66.75581  ?  212 LEU A CD2 1 
ATOM   1690 N  N   . LYS A 1 213 ? 0.13000   3.45700   73.43700  1.000 89.84421  ?  213 LYS A N   1 
ATOM   1691 C  CA  . LYS A 1 213 ? -0.99300  2.90500   72.68300  1.000 90.72311  ?  213 LYS A CA  1 
ATOM   1692 C  C   . LYS A 1 213 ? -2.19100  2.61200   73.57700  1.000 96.91098  ?  213 LYS A C   1 
ATOM   1693 O  O   . LYS A 1 213 ? -3.33600  2.66700   73.11300  1.000 105.77661 ?  213 LYS A O   1 
ATOM   1694 C  CB  . LYS A 1 213 ? -0.55800  1.62300   71.97100  1.000 86.94169  ?  213 LYS A CB  1 
ATOM   1695 C  CG  . LYS A 1 213 ? 0.63500   1.77700   71.04600  1.000 80.53909  ?  213 LYS A CG  1 
ATOM   1696 C  CD  . LYS A 1 213 ? 0.20800   2.33800   69.70400  1.000 91.18199  ?  213 LYS A CD  1 
ATOM   1697 C  CE  . LYS A 1 213 ? -0.72700  1.36300   69.00300  1.000 102.26084 ?  213 LYS A CE  1 
ATOM   1698 N  NZ  . LYS A 1 213 ? -1.03700  1.76700   67.60400  1.000 108.35790 ?  213 LYS A NZ  1 
ATOM   1699 N  N   . LEU A 1 214 ? -1.95600  2.30100   74.84800  1.000 90.13819  ?  214 LEU A N   1 
ATOM   1700 C  CA  . LEU A 1 214 ? -3.03800  2.02200   75.78800  1.000 97.07485  ?  214 LEU A CA  1 
ATOM   1701 C  C   . LEU A 1 214 ? -2.70000  2.55000   77.17900  1.000 90.95192  ?  214 LEU A C   1 
ATOM   1702 O  O   . LEU A 1 214 ? -2.93600  3.71900   77.48600  1.000 88.98976  ?  214 LEU A O   1 
ATOM   1703 C  CB  . LEU A 1 214 ? -3.32400  0.51900   75.85000  1.000 101.40419 ?  214 LEU A CB  1 
ATOM   1704 C  CG  . LEU A 1 214 ? -3.91300  -0.14100  74.60000  1.000 103.50885 ?  214 LEU A CG  1 
ATOM   1705 C  CD1 . LEU A 1 214 ? -3.90500  -1.65500  74.73600  1.000 101.93583 ?  214 LEU A CD1 1 
ATOM   1706 C  CD2 . LEU A 1 214 ? -5.32300  0.36700   74.33200  1.000 99.72817  ?  214 LEU A CD2 1 
ATOM   1707 N  N   . LYS B 1 2   ? 46.42500  12.27400  36.93300  1.000 97.35624  ?  2   LYS B N   1 
ATOM   1708 C  CA  . LYS B 1 2   ? 46.11300  13.69600  36.82900  1.000 103.06805 ?  2   LYS B CA  1 
ATOM   1709 C  C   . LYS B 1 2   ? 46.65400  14.45300  38.02600  1.000 101.47060 ?  2   LYS B C   1 
ATOM   1710 O  O   . LYS B 1 2   ? 46.51500  13.97500  39.14000  1.000 110.55140 ?  2   LYS B O   1 
ATOM   1711 C  CB  . LYS B 1 2   ? 44.60200  13.93400  36.71700  1.000 97.62327  ?  2   LYS B CB  1 
ATOM   1712 C  CG  . LYS B 1 2   ? 43.99300  13.49100  35.40600  1.000 98.68737  ?  2   LYS B CG  1 
ATOM   1713 C  CD  . LYS B 1 2   ? 42.51300  13.82800  35.34800  1.000 93.97059  ?  2   LYS B CD  1 
ATOM   1714 C  CE  . LYS B 1 2   ? 41.89000  13.38000  34.03400  1.000 98.63967  ?  2   LYS B CE  1 
ATOM   1715 N  NZ  . LYS B 1 2   ? 40.44400  13.73800  33.96700  1.000 98.49454  ?  2   LYS B NZ  1 
ATOM   1716 N  N   . ASP B 1 3   ? 47.38400  15.54300  37.82000  1.000 97.62727  ?  3   ASP B N   1 
ATOM   1717 C  CA  . ASP B 1 3   ? 47.79000  16.38900  38.93600  1.000 97.12590  ?  3   ASP B CA  1 
ATOM   1718 C  C   . ASP B 1 3   ? 47.15100  17.76500  38.76000  1.000 96.95173  ?  3   ASP B C   1 
ATOM   1719 O  O   . ASP B 1 3   ? 46.45500  18.02000  37.77500  1.000 96.74509  ?  3   ASP B O   1 
ATOM   1720 C  CB  . ASP B 1 3   ? 49.31600  16.48700  39.05700  1.000 100.11202 ?  3   ASP B CB  1 
ATOM   1721 C  CG  . ASP B 1 3   ? 49.75500  17.33900  40.22200  1.000 113.29166 ?  3   ASP B CG  1 
ATOM   1722 O  OD1 . ASP B 1 3   ? 49.49200  16.95500  41.38000  1.000 115.00711 ?  3   ASP B OD1 1 
ATOM   1723 O  OD2 . ASP B 1 3   ? 50.38700  18.38500  39.97100  1.000 109.80693 -1 3   ASP B OD2 1 
ATOM   1724 N  N   . ILE B 1 4   ? 47.38000  18.66000  39.72500  1.000 102.15749 ?  4   ILE B N   1 
ATOM   1725 C  CA  . ILE B 1 4   ? 46.77400  19.99200  39.65300  1.000 101.11034 ?  4   ILE B CA  1 
ATOM   1726 C  C   . ILE B 1 4   ? 47.21900  20.71900  38.38600  1.000 100.67172 ?  4   ILE B C   1 
ATOM   1727 O  O   . ILE B 1 4   ? 46.40600  21.33600  37.68500  1.000 95.89669  ?  4   ILE B O   1 
ATOM   1728 C  CB  . ILE B 1 4   ? 47.10100  20.80300  40.92100  1.000 94.01347  ?  4   ILE B CB  1 
ATOM   1729 C  CG1 . ILE B 1 4   ? 46.29200  20.26300  42.10100  1.000 96.17125  ?  4   ILE B CG1 1 
ATOM   1730 C  CG2 . ILE B 1 4   ? 46.81100  22.28000  40.71000  1.000 89.86104  ?  4   ILE B CG2 1 
ATOM   1731 C  CD1 . ILE B 1 4   ? 44.79000  20.38100  41.92100  1.000 92.13398  ?  4   ILE B CD1 1 
ATOM   1732 N  N   . ASP B 1 5   ? 48.51700  20.65900  38.07500  1.000 104.14219 ?  5   ASP B N   1 
ATOM   1733 C  CA  . ASP B 1 5   ? 49.02800  21.30500  36.86700  1.000 100.78353 ?  5   ASP B CA  1 
ATOM   1734 C  C   . ASP B 1 5   ? 48.36600  20.75400  35.60900  1.000 95.94930  ?  5   ASP B C   1 
ATOM   1735 O  O   . ASP B 1 5   ? 48.11000  21.50000  34.65600  1.000 91.58763  ?  5   ASP B O   1 
ATOM   1736 C  CB  . ASP B 1 5   ? 50.54700  21.14700  36.78600  1.000 99.54391  ?  5   ASP B CB  1 
ATOM   1737 C  CG  . ASP B 1 5   ? 51.25700  21.73700  37.98600  1.000 112.81433 ?  5   ASP B CG  1 
ATOM   1738 O  OD1 . ASP B 1 5   ? 50.66900  22.61300  38.65400  1.000 110.54513 ?  5   ASP B OD1 1 
ATOM   1739 O  OD2 . ASP B 1 5   ? 52.40500  21.32900  38.25800  1.000 115.95393 -1 5   ASP B OD2 1 
ATOM   1740 N  N   . THR B 1 6   ? 48.09600  19.44500  35.58000  1.000 92.41321  ?  6   THR B N   1 
ATOM   1741 C  CA  . THR B 1 6   ? 47.38600  18.85300  34.44800  1.000 91.77051  ?  6   THR B CA  1 
ATOM   1742 C  C   . THR B 1 6   ? 46.04400  19.53700  34.22200  1.000 90.52842  ?  6   THR B C   1 
ATOM   1743 O  O   . THR B 1 6   ? 45.71800  19.94000  33.09900  1.000 94.95205  ?  6   THR B O   1 
ATOM   1744 C  CB  . THR B 1 6   ? 47.19000  17.35300  34.67700  1.000 94.45036  ?  6   THR B CB  1 
ATOM   1745 O  OG1 . THR B 1 6   ? 48.46500  16.71400  34.81000  1.000 93.26046  ?  6   THR B OG1 1 
ATOM   1746 C  CG2 . THR B 1 6   ? 46.42800  16.72800  33.51600  1.000 86.11640  ?  6   THR B CG2 1 
ATOM   1747 N  N   . LEU B 1 7   ? 45.24700  19.67200  35.28300  1.000 93.16233  ?  7   LEU B N   1 
ATOM   1748 C  CA  . LEU B 1 7   ? 43.94200  20.31000  35.15400  1.000 91.11996  ?  7   LEU B CA  1 
ATOM   1749 C  C   . LEU B 1 7   ? 44.08300  21.77000  34.74300  1.000 90.15732  ?  7   LEU B C   1 
ATOM   1750 O  O   . LEU B 1 7   ? 43.26200  22.29100  33.97800  1.000 91.81060  ?  7   LEU B O   1 
ATOM   1751 C  CB  . LEU B 1 7   ? 43.16700  20.19800  36.46200  1.000 89.05646  ?  7   LEU B CB  1 
ATOM   1752 C  CG  . LEU B 1 7   ? 43.17000  18.85400  37.18500  1.000 90.25555  ?  7   LEU B CG  1 
ATOM   1753 C  CD1 . LEU B 1 7   ? 42.12700  18.94200  38.26000  1.000 88.30222  ?  7   LEU B CD1 1 
ATOM   1754 C  CD2 . LEU B 1 7   ? 42.89700  17.68200  36.25300  1.000 93.70657  ?  7   LEU B CD2 1 
ATOM   1755 N  N   . ILE B 1 8   ? 45.10100  22.45300  35.27100  1.000 93.01942  ?  8   ILE B N   1 
ATOM   1756 C  CA  . ILE B 1 8   ? 45.34100  23.85200  34.92100  1.000 93.42931  ?  8   ILE B CA  1 
ATOM   1757 C  C   . ILE B 1 8   ? 45.60000  23.99600  33.42600  1.000 96.90522  ?  8   ILE B C   1 
ATOM   1758 O  O   . ILE B 1 8   ? 45.05300  24.89000  32.76800  1.000 94.18276  ?  8   ILE B O   1 
ATOM   1759 C  CB  . ILE B 1 8   ? 46.50000  24.42200  35.75800  1.000 90.92143  ?  8   ILE B CB  1 
ATOM   1760 C  CG1 . ILE B 1 8   ? 46.04700  24.63000  37.20200  1.000 90.57566  ?  8   ILE B CG1 1 
ATOM   1761 C  CG2 . ILE B 1 8   ? 47.01100  25.72200  35.15600  1.000 89.74478  ?  8   ILE B CG2 1 
ATOM   1762 C  CD1 . ILE B 1 8   ? 44.86800  25.57400  37.32900  1.000 88.00115  ?  8   ILE B CD1 1 
ATOM   1763 N  N   . SER B 1 9   ? 46.44000  23.12100  32.86600  1.000 94.72163  ?  9   SER B N   1 
ATOM   1764 C  CA  . SER B 1 9   ? 46.75500  23.22200  31.44500  1.000 92.49814  ?  9   SER B CA  1 
ATOM   1765 C  C   . SER B 1 9   ? 45.50700  23.03400  30.59300  1.000 92.27906  ?  9   SER B C   1 
ATOM   1766 O  O   . SER B 1 9   ? 45.29400  23.76900  29.62300  1.000 94.80740  ?  9   SER B O   1 
ATOM   1767 C  CB  . SER B 1 9   ? 47.82000  22.19300  31.06500  1.000 85.82563  ?  9   SER B CB  1 
ATOM   1768 O  OG  . SER B 1 9   ? 47.26800  20.89000  30.99700  1.000 81.44089  ?  9   SER B OG  1 
ATOM   1769 N  N   . ASN B 1 10  ? 44.67000  22.05500  30.94600  1.000 88.46392  ?  10  ASN B N   1 
ATOM   1770 C  CA  . ASN B 1 10  ? 43.40800  21.85300  30.23900  1.000 87.24021  ?  10  ASN B CA  1 
ATOM   1771 C  C   . ASN B 1 10  ? 42.55500  23.11700  30.24600  1.000 87.36711  ?  10  ASN B C   1 
ATOM   1772 O  O   . ASN B 1 10  ? 41.86000  23.41000  29.26600  1.000 92.47573  ?  10  ASN B O   1 
ATOM   1773 C  CB  . ASN B 1 10  ? 42.64200  20.68600  30.86100  1.000 84.41253  ?  10  ASN B CB  1 
ATOM   1774 C  CG  . ASN B 1 10  ? 43.39600  19.37400  30.75700  1.000 85.31195  ?  10  ASN B CG  1 
ATOM   1775 O  OD1 . ASN B 1 10  ? 44.41300  19.28200  30.06900  1.000 82.39100  ?  10  ASN B OD1 1 
ATOM   1776 N  ND2 . ASN B 1 10  ? 42.89700  18.34900  31.43900  1.000 86.00989  ?  10  ASN B ND2 1 
ATOM   1777 N  N   . ASN B 1 11  ? 42.58800  23.87300  31.34600  1.000 85.55738  ?  11  ASN B N   1 
ATOM   1778 C  CA  . ASN B 1 11  ? 41.77900  25.08400  31.43400  1.000 89.35827  ?  11  ASN B CA  1 
ATOM   1779 C  C   . ASN B 1 11  ? 42.24200  26.12900  30.42500  1.000 88.10571  ?  11  ASN B C   1 
ATOM   1780 O  O   . ASN B 1 11  ? 41.41500  26.76300  29.75700  1.000 86.21082  ?  11  ASN B O   1 
ATOM   1781 C  CB  . ASN B 1 11  ? 41.82600  25.64700  32.85400  1.000 81.86139  ?  11  ASN B CB  1 
ATOM   1782 C  CG  . ASN B 1 11  ? 41.06600  26.95400  32.99000  1.000 80.95137  ?  11  ASN B CG  1 
ATOM   1783 O  OD1 . ASN B 1 11  ? 41.65900  28.02600  33.10300  1.000 85.18517  ?  11  ASN B OD1 1 
ATOM   1784 N  ND2 . ASN B 1 11  ? 39.73900  26.86700  32.98900  1.000 79.93696  ?  11  ASN B ND2 1 
ATOM   1785 N  N   . ALA B 1 12  ? 43.55600  26.33300  30.31400  1.000 89.29306  ?  12  ALA B N   1 
ATOM   1786 C  CA  . ALA B 1 12  ? 44.08000  27.31400  29.36600  1.000 93.56958  ?  12  ALA B CA  1 
ATOM   1787 C  C   . ALA B 1 12  ? 43.74300  26.93800  27.92700  1.000 93.62445  ?  12  ALA B C   1 
ATOM   1788 O  O   . ALA B 1 12  ? 43.33100  27.79500  27.13700  1.000 93.10295  ?  12  ALA B O   1 
ATOM   1789 C  CB  . ALA B 1 12  ? 45.59000  27.46000  29.54600  1.000 92.66505  ?  12  ALA B CB  1 
ATOM   1790 N  N   . LEU B 1 13  ? 43.91200  25.66200  27.56800  1.000 90.03018  ?  13  LEU B N   1 
ATOM   1791 C  CA  . LEU B 1 13  ? 43.55100  25.20400  26.22800  1.000 89.78891  ?  13  LEU B CA  1 
ATOM   1792 C  C   . LEU B 1 13  ? 42.08100  25.47600  25.93300  1.000 91.20781  ?  13  LEU B C   1 
ATOM   1793 O  O   . LEU B 1 13  ? 41.74300  26.14400  24.94900  1.000 103.00278 ?  13  LEU B O   1 
ATOM   1794 C  CB  . LEU B 1 13  ? 43.86200  23.71400  26.07300  1.000 94.12840  ?  13  LEU B CB  1 
ATOM   1795 C  CG  . LEU B 1 13  ? 45.22900  23.20200  26.52700  1.000 99.17890  ?  13  LEU B CG  1 
ATOM   1796 C  CD1 . LEU B 1 13  ? 45.30300  21.68800  26.38700  1.000 99.36185  ?  13  LEU B CD1 1 
ATOM   1797 C  CD2 . LEU B 1 13  ? 46.34700  23.87000  25.74500  1.000 93.71248  ?  13  LEU B CD2 1 
ATOM   1798 N  N   . TRP B 1 14  ? 41.19000  24.93800  26.77300  1.000 85.32405  ?  14  TRP B N   1 
ATOM   1799 C  CA  . TRP B 1 14  ? 39.75600  25.17900  26.63100  1.000 88.08555  ?  14  TRP B CA  1 
ATOM   1800 C  C   . TRP B 1 14  ? 39.43800  26.66300  26.47900  1.000 88.68109  ?  14  TRP B C   1 
ATOM   1801 O  O   . TRP B 1 14  ? 38.52800  27.03900  25.73000  1.000 89.33039  ?  14  TRP B O   1 
ATOM   1802 C  CB  . TRP B 1 14  ? 39.02000  24.59300  27.83500  1.000 91.56706  ?  14  TRP B CB  1 
ATOM   1803 C  CG  . TRP B 1 14  ? 37.61600  25.07300  27.97200  1.000 89.50021  ?  14  TRP B CG  1 
ATOM   1804 C  CD1 . TRP B 1 14  ? 36.50200  24.54600  27.39100  1.000 80.52212  ?  14  TRP B CD1 1 
ATOM   1805 C  CD2 . TRP B 1 14  ? 37.17400  26.18500  28.75700  1.000 89.66452  ?  14  TRP B CD2 1 
ATOM   1806 N  NE1 . TRP B 1 14  ? 35.39100  25.26700  27.76100  1.000 84.59194  ?  14  TRP B NE1 1 
ATOM   1807 C  CE2 . TRP B 1 14  ? 35.77800  26.27900  28.60100  1.000 88.60402  ?  14  TRP B CE2 1 
ATOM   1808 C  CE3 . TRP B 1 14  ? 37.82600  27.11400  29.57300  1.000 87.74941  ?  14  TRP B CE3 1 
ATOM   1809 C  CZ2 . TRP B 1 14  ? 35.02100  27.26300  29.23300  1.000 85.24628  ?  14  TRP B CZ2 1 
ATOM   1810 C  CZ3 . TRP B 1 14  ? 37.07400  28.09000  30.19800  1.000 91.31403  ?  14  TRP B CZ3 1 
ATOM   1811 C  CH2 . TRP B 1 14  ? 35.68700  28.15800  30.02400  1.000 88.76344  ?  14  TRP B CH2 1 
ATOM   1812 N  N   . SER B 1 15  ? 40.17200  27.51900  27.18900  1.000 93.01656  ?  15  SER B N   1 
ATOM   1813 C  CA  . SER B 1 15  ? 39.95600  28.95700  27.08200  1.000 95.50868  ?  15  SER B CA  1 
ATOM   1814 C  C   . SER B 1 15  ? 40.30000  29.44500  25.68100  1.000 95.35695  ?  15  SER B C   1 
ATOM   1815 O  O   . SER B 1 15  ? 39.53200  30.18900  25.06000  1.000 98.38524  ?  15  SER B O   1 
ATOM   1816 C  CB  . SER B 1 15  ? 40.78400  29.69200  28.13700  1.000 94.91322  ?  15  SER B CB  1 
ATOM   1817 O  OG  . SER B 1 15  ? 40.38400  31.04600  28.25400  1.000 96.05176  ?  15  SER B OG  1 
ATOM   1818 N  N   . LYS B 1 16  ? 41.46800  29.04000  25.17900  1.000 97.42106  ?  16  LYS B N   1 
ATOM   1819 C  CA  . LYS B 1 16  ? 41.93400  29.46200  23.86200  1.000 96.84963  ?  16  LYS B CA  1 
ATOM   1820 C  C   . LYS B 1 16  ? 40.98800  29.00000  22.76000  1.000 94.01607  ?  16  LYS B C   1 
ATOM   1821 O  O   . LYS B 1 16  ? 40.53800  29.80100  21.93100  1.000 93.95285  ?  16  LYS B O   1 
ATOM   1822 C  CB  . LYS B 1 16  ? 43.31200  28.85000  23.62100  1.000 93.13487  ?  16  LYS B CB  1 
ATOM   1823 C  CG  . LYS B 1 16  ? 44.39700  29.29000  24.56900  1.000 89.88580  ?  16  LYS B CG  1 
ATOM   1824 C  CD  . LYS B 1 16  ? 45.56200  28.31600  24.46400  1.000 88.13941  ?  16  LYS B CD  1 
ATOM   1825 C  CE  . LYS B 1 16  ? 46.61300  28.57700  25.52600  1.000 97.46924  ?  16  LYS B CE  1 
ATOM   1826 N  NZ  . LYS B 1 16  ? 46.01100  29.18000  26.74800  1.000 102.45734 ?  16  LYS B NZ  1 
ATOM   1827 N  N   . MET B 1 17  ? 40.68400  27.69900  22.74300  1.000 89.32952  ?  17  MET B N   1 
ATOM   1828 C  CA  . MET B 1 17  ? 39.80000  27.10400  21.74200  1.000 92.54956  ?  17  MET B CA  1 
ATOM   1829 C  C   . MET B 1 17  ? 38.51500  27.89900  21.54600  1.000 96.66121  ?  17  MET B C   1 
ATOM   1830 O  O   . MET B 1 17  ? 38.10800  28.17400  20.41100  1.000 104.85487 ?  17  MET B O   1 
ATOM   1831 C  CB  . MET B 1 17  ? 39.47400  25.66500  22.14000  1.000 96.56014  ?  17  MET B CB  1 
ATOM   1832 C  CG  . MET B 1 17  ? 40.63600  24.69300  22.03600  1.000 103.95305 ?  17  MET B CG  1 
ATOM   1833 S  SD  . MET B 1 17  ? 40.10000  23.02000  22.44100  1.000 132.01456 ?  17  MET B SD  1 
ATOM   1834 C  CE  . MET B 1 17  ? 38.80500  22.79500  21.22400  1.000 111.00347 ?  17  MET B CE  1 
ATOM   1835 N  N   . LEU B 1 18  ? 37.84500  28.24800  22.64400  1.000 94.21891  ?  18  LEU B N   1 
ATOM   1836 C  CA  . LEU B 1 18  ? 36.58900  28.98500  22.54500  1.000 97.77730  ?  18  LEU B CA  1 
ATOM   1837 C  C   . LEU B 1 18  ? 36.79200  30.35300  21.90100  1.000 102.74802 ?  18  LEU B C   1 
ATOM   1838 O  O   . LEU B 1 18  ? 36.03400  30.74400  21.00700  1.000 111.15798 ?  18  LEU B O   1 
ATOM   1839 C  CB  . LEU B 1 18  ? 35.95700  29.12900  23.92700  1.000 94.46071  ?  18  LEU B CB  1 
ATOM   1840 C  CG  . LEU B 1 18  ? 35.20400  27.90000  24.43800  1.000 91.50630  ?  18  LEU B CG  1 
ATOM   1841 C  CD1 . LEU B 1 18  ? 34.75400  28.12100  25.86900  1.000 99.07807  ?  18  LEU B CD1 1 
ATOM   1842 C  CD2 . LEU B 1 18  ? 34.02500  27.55500  23.54200  1.000 94.77489  ?  18  LEU B CD2 1 
ATOM   1843 N  N   . VAL B 1 19  ? 37.80900  31.09800  22.35000  1.000 98.56169  ?  19  VAL B N   1 
ATOM   1844 C  CA  . VAL B 1 19  ? 38.10100  32.40900  21.77000  1.000 106.37071 ?  19  VAL B CA  1 
ATOM   1845 C  C   . VAL B 1 19  ? 38.30500  32.30500  20.26300  1.000 110.34624 ?  19  VAL B C   1 
ATOM   1846 O  O   . VAL B 1 19  ? 37.81300  33.14100  19.49500  1.000 108.72036 ?  19  VAL B O   1 
ATOM   1847 C  CB  . VAL B 1 19  ? 39.33000  33.03600  22.45600  1.000 106.69566 ?  19  VAL B CB  1 
ATOM   1848 C  CG1 . VAL B 1 19  ? 39.69500  34.35200  21.78600  1.000 112.85954 ?  19  VAL B CG1 1 
ATOM   1849 C  CG2 . VAL B 1 19  ? 39.07000  33.24100  23.93300  1.000 101.55070 ?  19  VAL B CG2 1 
ATOM   1850 N  N   . GLU B 1 20  ? 39.02400  31.27300  19.81700  1.000 110.44180 ?  20  GLU B N   1 
ATOM   1851 C  CA  . GLU B 1 20  ? 39.25800  31.08800  18.38900  1.000 102.65532 ?  20  GLU B CA  1 
ATOM   1852 C  C   . GLU B 1 20  ? 37.94300  30.87000  17.64800  1.000 105.17861 ?  20  GLU B C   1 
ATOM   1853 O  O   . GLU B 1 20  ? 37.73100  31.43100  16.56600  1.000 117.11928 ?  20  GLU B O   1 
ATOM   1854 C  CB  . GLU B 1 20  ? 40.23400  29.93100  18.17200  1.000 99.42424  ?  20  GLU B CB  1 
ATOM   1855 C  CG  . GLU B 1 20  ? 40.59700  29.65500  16.72700  1.000 108.88264 ?  20  GLU B CG  1 
ATOM   1856 C  CD  . GLU B 1 20  ? 41.55300  28.48700  16.60000  1.000 115.61033 ?  20  GLU B CD  1 
ATOM   1857 O  OE1 . GLU B 1 20  ? 41.83400  27.83900  17.63100  1.000 111.63504 ?  20  GLU B OE1 1 
ATOM   1858 O  OE2 . GLU B 1 20  ? 42.03200  28.22300  15.47700  1.000 122.75668 -1 20  GLU B OE2 1 
ATOM   1859 N  N   . GLU B 1 21  ? 37.04500  30.05800  18.21200  1.000 100.07443 ?  21  GLU B N   1 
ATOM   1860 C  CA  . GLU B 1 21  ? 35.78000  29.76600  17.54300  1.000 105.67458 ?  21  GLU B CA  1 
ATOM   1861 C  C   . GLU B 1 21  ? 34.77900  30.89200  17.77300  1.000 109.56267 ?  21  GLU B C   1 
ATOM   1862 O  O   . GLU B 1 21  ? 34.31200  31.53100  16.82400  1.000 115.83552 ?  21  GLU B O   1 
ATOM   1863 C  CB  . GLU B 1 21  ? 35.21300  28.43300  18.04700  1.000 104.70207 ?  21  GLU B CB  1 
ATOM   1864 C  CG  . GLU B 1 21  ? 36.03300  27.21400  17.67700  1.000 107.28189 ?  21  GLU B CG  1 
ATOM   1865 C  CD  . GLU B 1 21  ? 36.15300  27.04400  16.17800  1.000 112.81754 ?  21  GLU B CD  1 
ATOM   1866 O  OE1 . GLU B 1 21  ? 35.15300  27.30500  15.47400  1.000 112.25159 ?  21  GLU B OE1 1 
ATOM   1867 O  OE2 . GLU B 1 21  ? 37.24100  26.65700  15.70300  1.000 116.39613 -1 21  GLU B OE2 1 
ATOM   1868 N  N   . ASP B 1 22  ? 34.43000  31.14200  19.03300  1.000 106.53229 ?  22  ASP B N   1 
ATOM   1869 C  CA  . ASP B 1 22  ? 33.50500  32.21100  19.40900  1.000 106.68681 ?  22  ASP B CA  1 
ATOM   1870 C  C   . ASP B 1 22  ? 34.13200  33.02000  20.53500  1.000 111.73688 ?  22  ASP B C   1 
ATOM   1871 O  O   . ASP B 1 22  ? 33.99800  32.66400  21.71400  1.000 114.61820 ?  22  ASP B O   1 
ATOM   1872 C  CB  . ASP B 1 22  ? 32.14400  31.66400  19.83500  1.000 108.73549 ?  22  ASP B CB  1 
ATOM   1873 C  CG  . ASP B 1 22  ? 31.17500  32.76700  20.23900  1.000 114.79071 ?  22  ASP B CG  1 
ATOM   1874 O  OD1 . ASP B 1 22  ? 31.42300  33.94400  19.89400  1.000 112.00888 ?  22  ASP B OD1 1 
ATOM   1875 O  OD2 . ASP B 1 22  ? 30.18100  32.46200  20.93000  1.000 118.02415 -1 22  ASP B OD2 1 
ATOM   1876 N  N   . PRO B 1 23  ? 34.82800  34.11600  20.21800  1.000 113.43607 ?  23  PRO B N   1 
ATOM   1877 C  CA  . PRO B 1 23  ? 35.37100  34.96300  21.29100  1.000 113.87483 ?  23  PRO B CA  1 
ATOM   1878 C  C   . PRO B 1 23  ? 34.29900  35.76500  22.00700  1.000 116.59564 ?  23  PRO B C   1 
ATOM   1879 O  O   . PRO B 1 23  ? 34.59800  36.39400  23.03200  1.000 118.98723 ?  23  PRO B O   1 
ATOM   1880 C  CB  . PRO B 1 23  ? 36.35400  35.87700  20.55200  1.000 112.38016 ?  23  PRO B CB  1 
ATOM   1881 C  CG  . PRO B 1 23  ? 35.79200  35.98500  19.17400  1.000 110.16370 ?  23  PRO B CG  1 
ATOM   1882 C  CD  . PRO B 1 23  ? 35.04200  34.70300  18.88300  1.000 111.65659 ?  23  PRO B CD  1 
ATOM   1883 N  N   . GLY B 1 24  ? 33.06600  35.75000  21.50100  1.000 113.72145 ?  24  GLY B N   1 
ATOM   1884 C  CA  . GLY B 1 24  ? 31.91400  36.38700  22.10600  1.000 111.81478 ?  24  GLY B CA  1 
ATOM   1885 C  C   . GLY B 1 24  ? 31.17500  35.54300  23.11700  1.000 113.71107 ?  24  GLY B C   1 
ATOM   1886 O  O   . GLY B 1 24  ? 30.32500  36.06800  23.84200  1.000 114.88804 ?  24  GLY B O   1 
ATOM   1887 N  N   . PHE B 1 25  ? 31.48400  34.25400  23.16300  1.000 113.10388 ?  25  PHE B N   1 
ATOM   1888 C  CA  . PHE B 1 25  ? 30.82900  33.34900  24.09600  1.000 114.01016 ?  25  PHE B CA  1 
ATOM   1889 C  C   . PHE B 1 25  ? 30.91900  33.84500  25.51600  1.000 110.12747 ?  25  PHE B C   1 
ATOM   1890 O  O   . PHE B 1 25  ? 29.91800  33.93700  26.21900  1.000 106.59695 ?  25  PHE B O   1 
ATOM   1891 C  CB  . PHE B 1 25  ? 31.48300  31.98100  24.00300  1.000 111.09785 ?  25  PHE B CB  1 
ATOM   1892 C  CG  . PHE B 1 25  ? 30.93900  30.97900  24.97100  1.000 113.58764 ?  25  PHE B CG  1 
ATOM   1893 C  CD1 . PHE B 1 25  ? 29.75100  30.32100  24.70900  1.000 113.53989 ?  25  PHE B CD1 1 
ATOM   1894 C  CD2 . PHE B 1 25  ? 31.62100  30.68500  26.13500  1.000 111.99885 ?  25  PHE B CD2 1 
ATOM   1895 C  CE1 . PHE B 1 25  ? 29.24900  29.39200  25.59300  1.000 115.31447 ?  25  PHE B CE1 1 
ATOM   1896 C  CE2 . PHE B 1 25  ? 31.12200  29.75800  27.02600  1.000 108.79815 ?  25  PHE B CE2 1 
ATOM   1897 C  CZ  . PHE B 1 25  ? 29.93600  29.10700  26.75400  1.000 111.24890 ?  25  PHE B CZ  1 
ATOM   1898 N  N   . PHE B 1 26  ? 32.13000  34.15000  25.94400  1.000 107.12987 ?  26  PHE B N   1 
ATOM   1899 C  CA  . PHE B 1 26  ? 32.32300  34.62300  27.29300  1.000 109.29433 ?  26  PHE B CA  1 
ATOM   1900 C  C   . PHE B 1 26  ? 31.47600  35.85600  27.51600  1.000 110.99034 ?  26  PHE B C   1 
ATOM   1901 O  O   . PHE B 1 26  ? 30.88000  36.02600  28.58000  1.000 115.02585 ?  26  PHE B O   1 
ATOM   1902 C  CB  . PHE B 1 26  ? 33.79600  34.88900  27.52500  1.000 106.23555 ?  26  PHE B CB  1 
ATOM   1903 C  CG  . PHE B 1 26  ? 34.64000  33.66600  27.37600  1.000 107.19547 ?  26  PHE B CG  1 
ATOM   1904 C  CD1 . PHE B 1 26  ? 34.55000  32.64000  28.29600  1.000 107.12839 ?  26  PHE B CD1 1 
ATOM   1905 C  CD2 . PHE B 1 26  ? 35.49300  33.52300  26.30100  1.000 109.18941 ?  26  PHE B CD2 1 
ATOM   1906 C  CE1 . PHE B 1 26  ? 35.31100  31.50000  28.15700  1.000 106.76363 ?  26  PHE B CE1 1 
ATOM   1907 C  CE2 . PHE B 1 26  ? 36.26100  32.38600  26.15600  1.000 106.25870 ?  26  PHE B CE2 1 
ATOM   1908 C  CZ  . PHE B 1 26  ? 36.16800  31.37100  27.08400  1.000 99.56221  ?  26  PHE B CZ  1 
ATOM   1909 N  N   . GLU B 1 27  ? 31.38600  36.70600  26.50700  1.000 111.45934 ?  27  GLU B N   1 
ATOM   1910 C  CA  . GLU B 1 27  ? 30.53300  37.87100  26.62600  1.000 112.04290 ?  27  GLU B CA  1 
ATOM   1911 C  C   . GLU B 1 27  ? 29.13400  37.42000  26.93000  1.000 111.48344 ?  27  GLU B C   1 
ATOM   1912 O  O   . GLU B 1 27  ? 28.51200  37.89000  27.86600  1.000 112.38427 ?  27  GLU B O   1 
ATOM   1913 C  CB  . GLU B 1 27  ? 30.53100  38.66400  25.33200  1.000 114.53169 ?  27  GLU B CB  1 
ATOM   1914 C  CG  . GLU B 1 27  ? 31.90300  38.84500  24.71300  1.000 117.72245 ?  27  GLU B CG  1 
ATOM   1915 C  CD  . GLU B 1 27  ? 31.85000  39.65000  23.43200  1.000 116.41705 ?  27  GLU B CD  1 
ATOM   1916 O  OE1 . GLU B 1 27  ? 30.94600  39.39700  22.61100  1.000 113.76486 ?  27  GLU B OE1 1 
ATOM   1917 O  OE2 . GLU B 1 27  ? 32.70700  40.53800  23.24600  1.000 114.40966 -1 27  GLU B OE2 1 
ATOM   1918 N  N   . LYS B 1 28  ? 28.63700  36.49000  26.13900  1.000 111.24629 ?  28  LYS B N   1 
ATOM   1919 C  CA  . LYS B 1 28  ? 27.28300  36.01100  26.33000  1.000 110.98571 ?  28  LYS B CA  1 
ATOM   1920 C  C   . LYS B 1 28  ? 26.97500  35.69800  27.78100  1.000 112.46818 ?  28  LYS B C   1 
ATOM   1921 O  O   . LYS B 1 28  ? 26.07800  36.29400  28.36700  1.000 112.09347 ?  28  LYS B O   1 
ATOM   1922 C  CB  . LYS B 1 28  ? 27.07100  34.76900  25.48100  1.000 112.10800 ?  28  LYS B CB  1 
ATOM   1923 C  CG  . LYS B 1 28  ? 27.37200  34.99200  24.01200  1.000 117.62420 ?  28  LYS B CG  1 
ATOM   1924 C  CD  . LYS B 1 28  ? 27.47900  33.67900  23.26000  1.000 115.01076 ?  28  LYS B CD  1 
ATOM   1925 C  CE  . LYS B 1 28  ? 27.62200  33.92600  21.77000  1.000 112.82420 ?  28  LYS B CE  1 
ATOM   1926 N  NZ  . LYS B 1 28  ? 28.71400  34.89100  21.47100  1.000 113.97376 ?  28  LYS B NZ  1 
ATOM   1927 N  N   . LEU B 1 29  ? 27.71400  34.76100  28.36100  1.000 114.83336 ?  29  LEU B N   1 
ATOM   1928 C  CA  . LEU B 1 29  ? 27.45300  34.36100  29.74200  1.000 111.29201 ?  29  LEU B CA  1 
ATOM   1929 C  C   . LEU B 1 29  ? 27.31100  35.57000  30.63700  1.000 111.54065 ?  29  LEU B C   1 
ATOM   1930 O  O   . LEU B 1 29  ? 26.41300  35.63800  31.46200  1.000 109.38600 ?  29  LEU B O   1 
ATOM   1931 C  CB  . LEU B 1 29  ? 28.56800  33.47000  30.27500  1.000 104.07522 ?  29  LEU B CB  1 
ATOM   1932 C  CG  . LEU B 1 29  ? 28.76700  32.10700  29.63300  1.000 108.55796 ?  29  LEU B CG  1 
ATOM   1933 C  CD1 . LEU B 1 29  ? 30.01500  31.47200  30.22200  1.000 107.18507 ?  29  LEU B CD1 1 
ATOM   1934 C  CD2 . LEU B 1 29  ? 27.54400  31.25200  29.91700  1.000 104.64113 ?  29  LEU B CD2 1 
ATOM   1935 N  N   . ALA B 1 30  ? 28.21100  36.52700  30.48600  1.000 110.53276 ?  30  ALA B N   1 
ATOM   1936 C  CA  . ALA B 1 30  ? 28.10400  37.73900  31.26600  1.000 108.85987 ?  30  ALA B CA  1 
ATOM   1937 C  C   . ALA B 1 30  ? 26.66500  38.20000  31.30700  1.000 113.15872 ?  30  ALA B C   1 
ATOM   1938 O  O   . ALA B 1 30  ? 26.07900  38.33700  32.37600  1.000 115.56693 ?  30  ALA B O   1 
ATOM   1939 C  CB  . ALA B 1 30  ? 28.98100  38.81500  30.67900  1.000 108.05222 ?  30  ALA B CB  1 
ATOM   1940 N  N   . GLN B 1 31  ? 26.08500  38.43100  30.14300  1.000 113.34057 ?  31  GLN B N   1 
ATOM   1941 C  CA  . GLN B 1 31  ? 24.70600  38.86800  30.08700  1.000 115.88243 ?  31  GLN B CA  1 
ATOM   1942 C  C   . GLN B 1 31  ? 23.80200  37.68200  29.85800  1.000 118.81643 ?  31  GLN B C   1 
ATOM   1943 O  O   . GLN B 1 31  ? 23.03300  37.66400  28.90200  1.000 120.67335 ?  31  GLN B O   1 
ATOM   1944 C  CB  . GLN B 1 31  ? 24.51700  39.87900  28.96700  1.000 119.49395 ?  31  GLN B CB  1 
ATOM   1945 C  CG  . GLN B 1 31  ? 25.23500  41.19900  29.20200  1.000 123.73918 ?  31  GLN B CG  1 
ATOM   1946 C  CD  . GLN B 1 31  ? 25.09200  42.16400  28.04000  1.000 129.29322 ?  31  GLN B CD  1 
ATOM   1947 O  OE1 . GLN B 1 31  ? 24.87300  41.75400  26.90000  1.000 130.51106 ?  31  GLN B OE1 1 
ATOM   1948 N  NE2 . GLN B 1 31  ? 25.20800  43.45600  28.32600  1.000 127.79238 ?  31  GLN B NE2 1 
ATOM   1949 N  N   . ALA B 1 32  ? 23.89500  36.68400  30.72800  1.000 119.02441 ?  32  ALA B N   1 
ATOM   1950 C  CA  . ALA B 1 32  ? 23.08800  35.48200  30.56600  1.000 116.68487 ?  32  ALA B CA  1 
ATOM   1951 C  C   . ALA B 1 32  ? 21.86900  35.49100  31.45700  1.000 118.56900 ?  32  ALA B C   1 
ATOM   1952 O  O   . ALA B 1 32  ? 21.42900  34.44200  31.92000  1.000 116.85005 ?  32  ALA B O   1 
ATOM   1953 C  CB  . ALA B 1 32  ? 23.92100  34.25700  30.85700  1.000 112.32286 ?  32  ALA B CB  1 
ATOM   1954 N  N   . GLN B 1 33  ? 21.32200  36.66900  31.70400  1.000 119.67058 ?  33  GLN B N   1 
ATOM   1955 C  CA  . GLN B 1 33  ? 20.13800  36.77400  32.53700  1.000 113.55708 ?  33  GLN B CA  1 
ATOM   1956 C  C   . GLN B 1 33  ? 20.29100  36.20400  33.92700  1.000 111.07442 ?  33  GLN B C   1 
ATOM   1957 O  O   . GLN B 1 33  ? 21.33200  36.35500  34.56900  1.000 108.60842 ?  33  GLN B O   1 
ATOM   1958 C  CB  . GLN B 1 33  ? 18.92100  36.20700  31.81300  1.000 112.09572 ?  33  GLN B CB  1 
ATOM   1959 C  CG  . GLN B 1 33  ? 18.76600  36.71300  30.39300  1.000 123.35319 ?  33  GLN B CG  1 
ATOM   1960 C  CD  . GLN B 1 33  ? 19.08200  38.19000  30.27100  1.000 128.42263 ?  33  GLN B CD  1 
ATOM   1961 O  OE1 . GLN B 1 33  ? 20.17200  38.56900  29.83900  1.000 127.70197 ?  33  GLN B OE1 1 
ATOM   1962 N  NE2 . GLN B 1 33  ? 18.13200  39.03300  30.65800  1.000 128.52979 ?  33  GLN B NE2 1 
ATOM   1963 N  N   . LYS B 1 34  ? 19.24300  35.55200  34.40400  1.000 102.87526 ?  34  LYS B N   1 
ATOM   1964 C  CA  . LYS B 1 34  ? 19.27700  35.01800  35.74700  1.000 92.97347  ?  34  LYS B CA  1 
ATOM   1965 C  C   . LYS B 1 34  ? 18.79500  33.60600  35.60300  1.000 88.91674  ?  34  LYS B C   1 
ATOM   1966 O  O   . LYS B 1 34  ? 17.82700  33.34900  34.90000  1.000 90.05738  ?  34  LYS B O   1 
ATOM   1967 C  CB  . LYS B 1 34  ? 18.42900  35.77100  36.76500  1.000 91.35866  ?  34  LYS B CB  1 
ATOM   1968 C  CG  . LYS B 1 34  ? 18.92300  37.17200  37.06500  1.000 92.38288  ?  34  LYS B CG  1 
ATOM   1969 C  CD  . LYS B 1 34  ? 18.01200  37.85900  38.06500  1.000 87.22312  ?  34  LYS B CD  1 
ATOM   1970 C  CE  . LYS B 1 34  ? 18.51000  39.25700  38.39300  1.000 92.80936  ?  34  LYS B CE  1 
ATOM   1971 N  NZ  . LYS B 1 34  ? 17.60700  39.94600  39.35700  1.000 82.96524  ?  34  LYS B NZ  1 
ATOM   1972 N  N   . PRO B 1 35  ? 19.47900  32.67600  36.26400  1.000 81.83239  ?  35  PRO B N   1 
ATOM   1973 C  CA  . PRO B 1 35  ? 19.10600  31.27900  36.10500  1.000 73.73105  ?  35  PRO B CA  1 
ATOM   1974 C  C   . PRO B 1 35  ? 17.62800  31.10500  36.38200  1.000 71.01370  ?  35  PRO B C   1 
ATOM   1975 O  O   . PRO B 1 35  ? 17.05800  31.85600  37.16200  1.000 81.98244  ?  35  PRO B O   1 
ATOM   1976 C  CB  . PRO B 1 35  ? 19.96100  30.56500  37.14800  1.000 71.45271  ?  35  PRO B CB  1 
ATOM   1977 C  CG  . PRO B 1 35  ? 20.62600  31.62400  37.95600  1.000 77.10972  ?  35  PRO B CG  1 
ATOM   1978 C  CD  . PRO B 1 35  ? 20.66900  32.84400  37.10300  1.000 78.49787  ?  35  PRO B CD  1 
ATOM   1979 N  N   . ARG B 1 36  ? 17.00500  30.13500  35.73600  1.000 65.63764  ?  36  ARG B N   1 
ATOM   1980 C  CA  . ARG B 1 36  ? 15.58300  29.92700  35.91600  1.000 71.73233  ?  36  ARG B CA  1 
ATOM   1981 C  C   . ARG B 1 36  ? 15.32500  28.56500  36.50200  1.000 77.33799  ?  36  ARG B C   1 
ATOM   1982 O  O   . ARG B 1 36  ? 14.18500  28.18600  36.73500  1.000 74.84747  ?  36  ARG B O   1 
ATOM   1983 C  CB  . ARG B 1 36  ? 14.85500  30.07300  34.59200  1.000 80.92394  ?  36  ARG B CB  1 
ATOM   1984 C  CG  . ARG B 1 36  ? 13.51900  30.78800  34.70800  1.000 86.92266  ?  36  ARG B CG  1 
ATOM   1985 C  CD  . ARG B 1 36  ? 12.60000  30.44000  33.55100  1.000 83.78130  ?  36  ARG B CD  1 
ATOM   1986 N  NE  . ARG B 1 36  ? 13.34800  29.93700  32.40500  1.000 89.35714  ?  36  ARG B NE  1 
ATOM   1987 C  CZ  . ARG B 1 36  ? 13.01000  28.86100  31.70800  1.000 90.97456  ?  36  ARG B CZ  1 
ATOM   1988 N  NH1 . ARG B 1 36  ? 11.92800  28.17000  32.03500  1.000 85.43664  ?  36  ARG B NH1 1 
ATOM   1989 N  NH2 . ARG B 1 36  ? 13.75400  28.47600  30.68200  1.000 83.88237  ?  36  ARG B NH2 1 
ATOM   1990 N  N   . PHE B 1 37  ? 16.39000  27.82900  36.75600  1.000 78.93203  ?  37  PHE B N   1 
ATOM   1991 C  CA  . PHE B 1 37  ? 16.25000  26.52300  37.35700  1.000 74.56139  ?  37  PHE B CA  1 
ATOM   1992 C  C   . PHE B 1 37  ? 17.22300  26.32000  38.50500  1.000 72.72666  ?  37  PHE B C   1 
ATOM   1993 O  O   . PHE B 1 37  ? 18.36600  26.75500  38.43200  1.000 72.48022  ?  37  PHE B O   1 
ATOM   1994 C  CB  . PHE B 1 37  ? 16.50100  25.42900  36.31900  1.000 76.55984  ?  37  PHE B CB  1 
ATOM   1995 C  CG  . PHE B 1 37  ? 15.51500  25.39800  35.19400  1.000 79.76717  ?  37  PHE B CG  1 
ATOM   1996 C  CD1 . PHE B 1 37  ? 15.65700  26.24000  34.10800  1.000 86.38266  ?  37  PHE B CD1 1 
ATOM   1997 C  CD2 . PHE B 1 37  ? 14.47100  24.49700  35.20500  1.000 77.46234  ?  37  PHE B CD2 1 
ATOM   1998 C  CE1 . PHE B 1 37  ? 14.75500  26.20200  33.06500  1.000 85.89025  ?  37  PHE B CE1 1 
ATOM   1999 C  CE2 . PHE B 1 37  ? 13.56600  24.45200  34.16600  1.000 82.96953  ?  37  PHE B CE2 1 
ATOM   2000 C  CZ  . PHE B 1 37  ? 13.70800  25.30600  33.09400  1.000 84.60609  ?  37  PHE B CZ  1 
ATOM   2001 N  N   . LEU B 1 38  ? 16.78200  25.66300  39.56500  1.000 67.26030  ?  38  LEU B N   1 
ATOM   2002 C  CA  . LEU B 1 38  ? 17.65300  25.33000  40.68400  1.000 62.06339  ?  38  LEU B CA  1 
ATOM   2003 C  C   . LEU B 1 38  ? 17.84300  23.82000  40.70100  1.000 61.71664  ?  38  LEU B C   1 
ATOM   2004 O  O   . LEU B 1 38  ? 16.86300  23.06900  40.72200  1.000 61.34387  ?  38  LEU B O   1 
ATOM   2005 C  CB  . LEU B 1 38  ? 17.06300  25.82100  42.00800  1.000 69.99465  ?  38  LEU B CB  1 
ATOM   2006 C  CG  . LEU B 1 38  ? 17.72700  25.38500  43.31800  1.000 64.99598  ?  38  LEU B CG  1 
ATOM   2007 C  CD1 . LEU B 1 38  ? 19.17800  25.83100  43.37100  1.000 64.58569  ?  38  LEU B CD1 1 
ATOM   2008 C  CD2 . LEU B 1 38  ? 16.95400  25.93400  44.50800  1.000 49.82279  ?  38  LEU B CD2 1 
ATOM   2009 N  N   . TRP B 1 39  ? 19.09700  23.37900  40.67500  1.000 61.33018  ?  39  TRP B N   1 
ATOM   2010 C  CA  . TRP B 1 39  ? 19.42400  21.95900  40.69000  1.000 64.43852  ?  39  TRP B CA  1 
ATOM   2011 C  C   . TRP B 1 39  ? 19.97300  21.59900  42.06200  1.000 68.16479  ?  39  TRP B C   1 
ATOM   2012 O  O   . TRP B 1 39  ? 21.03400  22.09100  42.46000  1.000 64.70780  ?  39  TRP B O   1 
ATOM   2013 C  CB  . TRP B 1 39  ? 20.43200  21.60500  39.59500  1.000 60.92185  ?  39  TRP B CB  1 
ATOM   2014 C  CG  . TRP B 1 39  ? 20.59600  20.11900  39.37600  1.000 61.23776  ?  39  TRP B CG  1 
ATOM   2015 C  CD1 . TRP B 1 39  ? 21.42100  19.27400  40.06300  1.000 61.93563  ?  39  TRP B CD1 1 
ATOM   2016 C  CD2 . TRP B 1 39  ? 19.91800  19.31100  38.40300  1.000 72.44364  ?  39  TRP B CD2 1 
ATOM   2017 N  NE1 . TRP B 1 39  ? 21.29700  17.99200  39.58000  1.000 62.78587  ?  39  TRP B NE1 1 
ATOM   2018 C  CE2 . TRP B 1 39  ? 20.38100  17.98800  38.56100  1.000 71.69498  ?  39  TRP B CE2 1 
ATOM   2019 C  CE3 . TRP B 1 39  ? 18.96600  19.57800  37.41200  1.000 72.17333  ?  39  TRP B CE3 1 
ATOM   2020 C  CZ2 . TRP B 1 39  ? 19.92500  16.93600  37.76500  1.000 74.33264  ?  39  TRP B CZ2 1 
ATOM   2021 C  CZ3 . TRP B 1 39  ? 18.51300  18.53100  36.62400  1.000 71.32586  ?  39  TRP B CZ3 1 
ATOM   2022 C  CH2 . TRP B 1 39  ? 18.99300  17.22800  36.80600  1.000 71.55940  ?  39  TRP B CH2 1 
ATOM   2023 N  N   . ILE B 1 40  ? 19.24200  20.75200  42.77800  1.000 62.48316  ?  40  ILE B N   1 
ATOM   2024 C  CA  . ILE B 1 40  ? 19.68100  20.18900  44.04700  1.000 56.91940  ?  40  ILE B CA  1 
ATOM   2025 C  C   . ILE B 1 40  ? 20.03100  18.73500  43.77700  1.000 57.99802  ?  40  ILE B C   1 
ATOM   2026 O  O   . ILE B 1 40  ? 19.14300  17.90100  43.56000  1.000 58.90568  ?  40  ILE B O   1 
ATOM   2027 C  CB  . ILE B 1 40  ? 18.61000  20.31400  45.13800  1.000 58.57517  ?  40  ILE B CB  1 
ATOM   2028 C  CG1 . ILE B 1 40  ? 18.26400  21.78400  45.38400  1.000 54.85039  ?  40  ILE B CG1 1 
ATOM   2029 C  CG2 . ILE B 1 40  ? 19.08000  19.64700  46.42000  1.000 52.18026  ?  40  ILE B CG2 1 
ATOM   2030 C  CD1 . ILE B 1 40  ? 17.12200  21.98400  46.36100  1.000 50.80259  ?  40  ILE B CD1 1 
ATOM   2031 N  N   . GLY B 1 41  ? 21.32700  18.42700  43.77100  1.000 58.48333  ?  41  GLY B N   1 
ATOM   2032 C  CA  . GLY B 1 41  ? 21.79700  17.10500  43.42300  1.000 57.76271  ?  41  GLY B CA  1 
ATOM   2033 C  C   . GLY B 1 41  ? 22.79500  16.58200  44.43900  1.000 58.98533  ?  41  GLY B C   1 
ATOM   2034 O  O   . GLY B 1 41  ? 23.14100  17.25800  45.40900  1.000 66.07430  ?  41  GLY B O   1 
ATOM   2035 N  N   . CYS B 1 42  ? 23.22900  15.35100  44.19800  1.000 56.68308  ?  42  CYS B N   1 
ATOM   2036 C  CA  . CYS B 1 42  ? 24.17600  14.68600  45.07700  1.000 60.09676  ?  42  CYS B CA  1 
ATOM   2037 C  C   . CYS B 1 42  ? 25.59100  15.18100  44.80700  1.000 63.56745  ?  42  CYS B C   1 
ATOM   2038 O  O   . CYS B 1 42  ? 25.93200  15.57800  43.69000  1.000 72.82226  ?  42  CYS B O   1 
ATOM   2039 C  CB  . CYS B 1 42  ? 24.10100  13.17200  44.88600  1.000 56.08348  ?  42  CYS B CB  1 
ATOM   2040 S  SG  . CYS B 1 42  ? 25.24800  12.23600  45.90200  1.000 64.15511  ?  42  CYS B SG  1 
ATOM   2041 N  N   . SER B 1 43  ? 26.42200  15.16200  45.85200  1.000 67.38967  ?  43  SER B N   1 
ATOM   2042 C  CA  . SER B 1 43  ? 27.81900  15.54200  45.67800  1.000 67.78879  ?  43  SER B CA  1 
ATOM   2043 C  C   . SER B 1 43  ? 28.58700  14.53400  44.83800  1.000 65.53960  ?  43  SER B C   1 
ATOM   2044 O  O   . SER B 1 43  ? 29.67200  14.85800  44.34200  1.000 64.51987  ?  43  SER B O   1 
ATOM   2045 C  CB  . SER B 1 43  ? 28.50300  15.71100  47.03800  1.000 72.17504  ?  43  SER B CB  1 
ATOM   2046 O  OG  . SER B 1 43  ? 28.08200  16.90200  47.67800  1.000 68.52643  ?  43  SER B OG  1 
ATOM   2047 N  N   . ASP B 1 44  ? 28.04900  13.32300  44.67200  1.000 66.52174  ?  44  ASP B N   1 
ATOM   2048 C  CA  . ASP B 1 44  ? 28.65700  12.35800  43.76500  1.000 72.59386  ?  44  ASP B CA  1 
ATOM   2049 C  C   . ASP B 1 44  ? 28.75700  12.92200  42.35600  1.000 76.88531  ?  44  ASP B C   1 
ATOM   2050 O  O   . ASP B 1 44  ? 29.79900  12.78900  41.70100  1.000 80.99098  ?  44  ASP B O   1 
ATOM   2051 C  CB  . ASP B 1 44  ? 27.84300  11.06500  43.75500  1.000 72.62528  ?  44  ASP B CB  1 
ATOM   2052 C  CG  . ASP B 1 44  ? 28.06900  10.22300  44.99000  1.000 75.30433  ?  44  ASP B CG  1 
ATOM   2053 O  OD1 . ASP B 1 44  ? 29.23100  10.10700  45.42900  1.000 72.49368  ?  44  ASP B OD1 1 
ATOM   2054 O  OD2 . ASP B 1 44  ? 27.07900  9.68800   45.53300  1.000 77.70478  -1 44  ASP B OD2 1 
ATOM   2055 N  N   . SER B 1 45  ? 27.69700  13.58700  41.89300  1.000 74.49891  ?  45  SER B N   1 
ATOM   2056 C  CA  . SER B 1 45  ? 27.63700  14.16000  40.55200  1.000 71.36836  ?  45  SER B CA  1 
ATOM   2057 C  C   . SER B 1 45  ? 28.11900  13.14600  39.51700  1.000 74.20367  ?  45  SER B C   1 
ATOM   2058 O  O   . SER B 1 45  ? 29.02700  13.40900  38.72600  1.000 78.68506  ?  45  SER B O   1 
ATOM   2059 C  CB  . SER B 1 45  ? 28.44200  15.45800  40.47500  1.000 70.62085  ?  45  SER B CB  1 
ATOM   2060 O  OG  . SER B 1 45  ? 28.08600  16.21500  39.33100  1.000 77.71109  ?  45  SER B OG  1 
ATOM   2061 N  N   . ARG B 1 46  ? 27.51800  11.95100  39.56200  1.000 75.69613  ?  46  ARG B N   1 
ATOM   2062 C  CA  . ARG B 1 46  ? 27.94400  10.87000  38.67700  1.000 80.31609  ?  46  ARG B CA  1 
ATOM   2063 C  C   . ARG B 1 46  ? 27.85500  11.28400  37.21700  1.000 81.16376  ?  46  ARG B C   1 
ATOM   2064 O  O   . ARG B 1 46  ? 28.71500  10.91900  36.41000  1.000 80.69735  ?  46  ARG B O   1 
ATOM   2065 C  CB  . ARG B 1 46  ? 27.11400  9.61200   38.92600  1.000 76.71740  ?  46  ARG B CB  1 
ATOM   2066 C  CG  . ARG B 1 46  ? 27.28300  9.03200   40.31300  1.000 81.27035  ?  46  ARG B CG  1 
ATOM   2067 C  CD  . ARG B 1 46  ? 28.75800  8.86500   40.63300  1.000 87.67248  ?  46  ARG B CD  1 
ATOM   2068 N  NE  . ARG B 1 46  ? 29.38100  7.77800   39.88800  1.000 90.38263  ?  46  ARG B NE  1 
ATOM   2069 C  CZ  . ARG B 1 46  ? 30.68500  7.53500   39.88100  1.000 98.94525  ?  46  ARG B CZ  1 
ATOM   2070 N  NH1 . ARG B 1 46  ? 31.53100  8.28700   40.56600  1.000 96.63032  ?  46  ARG B NH1 1 
ATOM   2071 N  NH2 . ARG B 1 46  ? 31.15200  6.51900   39.16200  1.000 106.99607 ?  46  ARG B NH2 1 
ATOM   2072 N  N   . VAL B 1 47  ? 26.80200  12.01300  36.84900  1.000 77.53744  ?  47  VAL B N   1 
ATOM   2073 C  CA  . VAL B 1 47  ? 26.71900  12.68500  35.56400  1.000 76.84188  ?  47  VAL B CA  1 
ATOM   2074 C  C   . VAL B 1 47  ? 26.32900  14.12700  35.86100  1.000 73.00109  ?  47  VAL B C   1 
ATOM   2075 O  O   . VAL B 1 47  ? 25.27700  14.36900  36.46100  1.000 76.23055  ?  47  VAL B O   1 
ATOM   2076 C  CB  . VAL B 1 47  ? 25.70200  12.03700  34.60800  1.000 82.22790  ?  47  VAL B CB  1 
ATOM   2077 C  CG1 . VAL B 1 47  ? 25.79900  12.66900  33.22800  1.000 86.02221  ?  47  VAL B CG1 1 
ATOM   2078 C  CG2 . VAL B 1 47  ? 25.93300  10.53500  34.52100  1.000 79.94418  ?  47  VAL B CG2 1 
ATOM   2079 N  N   . PRO B 1 48  ? 27.14400  15.11700  35.49100  1.000 73.17369  ?  48  PRO B N   1 
ATOM   2080 C  CA  . PRO B 1 48  ? 26.78300  16.51000  35.77300  1.000 75.48912  ?  48  PRO B CA  1 
ATOM   2081 C  C   . PRO B 1 48  ? 25.43300  16.86500  35.17200  1.000 74.95477  ?  48  PRO B C   1 
ATOM   2082 O  O   . PRO B 1 48  ? 25.00300  16.29600  34.16700  1.000 80.76803  ?  48  PRO B O   1 
ATOM   2083 C  CB  . PRO B 1 48  ? 27.91500  17.30900  35.12200  1.000 76.07813  ?  48  PRO B CB  1 
ATOM   2084 C  CG  . PRO B 1 48  ? 29.07600  16.37300  35.13500  1.000 82.34487  ?  48  PRO B CG  1 
ATOM   2085 C  CD  . PRO B 1 48  ? 28.49200  15.00500  34.91200  1.000 81.83710  ?  48  PRO B CD  1 
ATOM   2086 N  N   . ALA B 1 49  ? 24.76700  17.83000  35.80600  1.000 76.47700  ?  49  ALA B N   1 
ATOM   2087 C  CA  . ALA B 1 49  ? 23.40700  18.17500  35.41100  1.000 78.55011  ?  49  ALA B CA  1 
ATOM   2088 C  C   . ALA B 1 49  ? 23.35900  18.73800  34.00100  1.000 79.27677  ?  49  ALA B C   1 
ATOM   2089 O  O   . ALA B 1 49  ? 22.35500  18.57000  33.30000  1.000 79.88084  ?  49  ALA B O   1 
ATOM   2090 C  CB  . ALA B 1 49  ? 22.81000  19.17600  36.40000  1.000 77.51811  ?  49  ALA B CB  1 
ATOM   2091 N  N   . GLU B 1 50  ? 24.42900  19.40700  33.56800  1.000 84.57157  ?  50  GLU B N   1 
ATOM   2092 C  CA  . GLU B 1 50  ? 24.43200  20.02200  32.24600  1.000 87.07903  ?  50  GLU B CA  1 
ATOM   2093 C  C   . GLU B 1 50  ? 24.41000  18.97800  31.13500  1.000 82.49819  ?  50  GLU B C   1 
ATOM   2094 O  O   . GLU B 1 50  ? 23.73900  19.16900  30.11400  1.000 85.13454  ?  50  GLU B O   1 
ATOM   2095 C  CB  . GLU B 1 50  ? 25.65300  20.93000  32.10100  1.000 86.06975  ?  50  GLU B CB  1 
ATOM   2096 C  CG  . GLU B 1 50  ? 25.66400  22.12100  33.05200  1.000 90.33887  ?  50  GLU B CG  1 
ATOM   2097 C  CD  . GLU B 1 50  ? 26.09900  21.75400  34.46300  1.000 88.62728  ?  50  GLU B CD  1 
ATOM   2098 O  OE1 . GLU B 1 50  ? 26.42900  20.57200  34.70100  1.000 88.62878  ?  50  GLU B OE1 1 
ATOM   2099 O  OE2 . GLU B 1 50  ? 26.10700  22.64800  35.33500  1.000 86.14677  -1 50  GLU B OE2 1 
ATOM   2100 N  N   . ARG B 1 51  ? 25.12200  17.86100  31.31000  1.000 81.92985  ?  51  ARG B N   1 
ATOM   2101 C  CA  . ARG B 1 51  ? 25.08000  16.82100  30.28700  1.000 77.80185  ?  51  ARG B CA  1 
ATOM   2102 C  C   . ARG B 1 51  ? 23.74000  16.09300  30.30100  1.000 82.47841  ?  51  ARG B C   1 
ATOM   2103 O  O   . ARG B 1 51  ? 23.21300  15.73000  29.24300  1.000 78.82995  ?  51  ARG B O   1 
ATOM   2104 C  CB  . ARG B 1 51  ? 26.22700  15.82800  30.46600  1.000 81.65446  ?  51  ARG B CB  1 
ATOM   2105 C  CG  . ARG B 1 51  ? 27.60700  16.44600  30.36000  1.000 93.57482  ?  51  ARG B CG  1 
ATOM   2106 C  CD  . ARG B 1 51  ? 28.67900  15.37900  30.24200  1.000 103.74644 ?  51  ARG B CD  1 
ATOM   2107 N  NE  . ARG B 1 51  ? 30.02400  15.93700  30.29200  1.000 112.43274 ?  51  ARG B NE  1 
ATOM   2108 C  CZ  . ARG B 1 51  ? 31.12800  15.21000  30.39000  1.000 110.91505 ?  51  ARG B CZ  1 
ATOM   2109 N  NH1 . ARG B 1 51  ? 31.08600  13.88800  30.36800  1.000 99.32241  ?  51  ARG B NH1 1 
ATOM   2110 N  NH2 . ARG B 1 51  ? 32.30200  15.82400  30.51600  1.000 111.91274 ?  51  ARG B NH2 1 
ATOM   2111 N  N   . LEU B 1 52  ? 23.18400  15.85900  31.49300  1.000 85.28071  ?  52  LEU B N   1 
ATOM   2112 C  CA  . LEU B 1 52  ? 21.92500  15.12700  31.60400  1.000 83.80659  ?  52  LEU B CA  1 
ATOM   2113 C  C   . LEU B 1 52  ? 20.76900  15.87900  30.95500  1.000 79.23219  ?  52  LEU B C   1 
ATOM   2114 O  O   . LEU B 1 52  ? 19.90700  15.26900  30.31400  1.000 72.76230  ?  52  LEU B O   1 
ATOM   2115 C  CB  . LEU B 1 52  ? 21.60500  14.86700  33.07600  1.000 77.14096  ?  52  LEU B CB  1 
ATOM   2116 C  CG  . LEU B 1 52  ? 22.35600  13.75800  33.80200  1.000 78.79241  ?  52  LEU B CG  1 
ATOM   2117 C  CD1 . LEU B 1 52  ? 22.15000  13.89800  35.29600  1.000 80.68937  ?  52  LEU B CD1 1 
ATOM   2118 C  CD2 . LEU B 1 52  ? 21.85700  12.40900  33.32000  1.000 77.40764  ?  52  LEU B CD2 1 
ATOM   2119 N  N   . THR B 1 53  ? 20.72900  17.20000  31.11400  1.000 79.50389  ?  53  THR B N   1 
ATOM   2120 C  CA  . THR B 1 53  ? 19.58200  17.98700  30.68800  1.000 79.76195  ?  53  THR B CA  1 
ATOM   2121 C  C   . THR B 1 53  ? 19.83500  18.84400  29.45700  1.000 84.92407  ?  53  THR B C   1 
ATOM   2122 O  O   . THR B 1 53  ? 18.88200  19.42800  28.92900  1.000 81.59309  ?  53  THR B O   1 
ATOM   2123 C  CB  . THR B 1 53  ? 19.11300  18.89400  31.83400  1.000 83.04599  ?  53  THR B CB  1 
ATOM   2124 O  OG1 . THR B 1 53  ? 20.19400  19.74000  32.24700  1.000 86.85869  ?  53  THR B OG1 1 
ATOM   2125 C  CG2 . THR B 1 53  ? 18.64900  18.06000  33.01600  1.000 81.17618  ?  53  THR B CG2 1 
ATOM   2126 N  N   . GLY B 1 54  ? 21.07300  18.93400  28.98100  1.000 86.63110  ?  54  GLY B N   1 
ATOM   2127 C  CA  . GLY B 1 54  ? 21.34600  19.84500  27.88900  1.000 79.65747  ?  54  GLY B CA  1 
ATOM   2128 C  C   . GLY B 1 54  ? 21.21300  21.30200  28.26100  1.000 88.30371  ?  54  GLY B C   1 
ATOM   2129 O  O   . GLY B 1 54  ? 20.97300  22.14000  27.38600  1.000 94.57947  ?  54  GLY B O   1 
ATOM   2130 N  N   . LEU B 1 55  ? 21.34700  21.62700  29.54500  1.000 86.73945  ?  55  LEU B N   1 
ATOM   2131 C  CA  . LEU B 1 55  ? 21.27800  23.00100  30.01700  1.000 84.27249  ?  55  LEU B CA  1 
ATOM   2132 C  C   . LEU B 1 55  ? 22.64800  23.65500  29.90800  1.000 84.12112  ?  55  LEU B C   1 
ATOM   2133 O  O   . LEU B 1 55  ? 23.66900  23.03700  30.22400  1.000 85.81288  ?  55  LEU B O   1 
ATOM   2134 C  CB  . LEU B 1 55  ? 20.77800  23.05800  31.46300  1.000 86.03890  ?  55  LEU B CB  1 
ATOM   2135 C  CG  . LEU B 1 55  ? 19.27800  22.82300  31.64200  1.000 86.66283  ?  55  LEU B CG  1 
ATOM   2136 C  CD1 . LEU B 1 55  ? 18.90900  22.62000  33.10100  1.000 81.36857  ?  55  LEU B CD1 1 
ATOM   2137 C  CD2 . LEU B 1 55  ? 18.50600  23.99500  31.06400  1.000 88.36864  ?  55  LEU B CD2 1 
ATOM   2138 N  N   . GLU B 1 56  ? 22.66000  24.90500  29.45700  1.000 85.49001  ?  56  GLU B N   1 
ATOM   2139 C  CA  . GLU B 1 56  ? 23.90600  25.60700  29.20400  1.000 93.65336  ?  56  GLU B CA  1 
ATOM   2140 C  C   . GLU B 1 56  ? 24.38200  26.31200  30.46300  1.000 94.07937  ?  56  GLU B C   1 
ATOM   2141 O  O   . GLU B 1 56  ? 23.59300  26.59500  31.36700  1.000 97.36532  ?  56  GLU B O   1 
ATOM   2142 C  CB  . GLU B 1 56  ? 23.71500  26.64700  28.10000  1.000 99.99505  ?  56  GLU B CB  1 
ATOM   2143 C  CG  . GLU B 1 56  ? 22.78400  27.77500  28.50300  1.000 102.40731 ?  56  GLU B CG  1 
ATOM   2144 C  CD  . GLU B 1 56  ? 22.42400  28.68900  27.35400  1.000 107.75061 ?  56  GLU B CD  1 
ATOM   2145 O  OE1 . GLU B 1 56  ? 22.98100  28.51200  26.25100  1.000 103.98451 ?  56  GLU B OE1 1 
ATOM   2146 O  OE2 . GLU B 1 56  ? 21.58300  29.59000  27.55500  1.000 111.35256 -1 56  GLU B OE2 1 
ATOM   2147 N  N   . PRO B 1 57  ? 25.68300  26.57200  30.56900  1.000 90.15696  ?  57  PRO B N   1 
ATOM   2148 C  CA  . PRO B 1 57  ? 26.19000  27.35100  31.70700  1.000 89.63755  ?  57  PRO B CA  1 
ATOM   2149 C  C   . PRO B 1 57  ? 25.49300  28.70000  31.79200  1.000 89.70683  ?  57  PRO B C   1 
ATOM   2150 O  O   . PRO B 1 57  ? 25.51600  29.49200  30.84600  1.000 94.44335  ?  57  PRO B O   1 
ATOM   2151 C  CB  . PRO B 1 57  ? 27.68200  27.49400  31.39800  1.000 92.36838  ?  57  PRO B CB  1 
ATOM   2152 C  CG  . PRO B 1 57  ? 27.99000  26.37400  30.47200  1.000 90.56209  ?  57  PRO B CG  1 
ATOM   2153 C  CD  . PRO B 1 57  ? 26.76000  26.12800  29.67100  1.000 88.42001  ?  57  PRO B CD  1 
ATOM   2154 N  N   . GLY B 1 58  ? 24.85400  28.95200  32.93200  1.000 84.18548  ?  58  GLY B N   1 
ATOM   2155 C  CA  . GLY B 1 58  ? 24.20900  30.21900  33.21500  1.000 83.82999  ?  58  GLY B CA  1 
ATOM   2156 C  C   . GLY B 1 58  ? 22.71600  30.12500  33.45200  1.000 76.99060  ?  58  GLY B C   1 
ATOM   2157 O  O   . GLY B 1 58  ? 22.12700  31.06600  34.00500  1.000 73.85615  ?  58  GLY B O   1 
ATOM   2158 N  N   . GLU B 1 59  ? 22.07600  29.03100  33.04800  1.000 77.49887  ?  59  GLU B N   1 
ATOM   2159 C  CA  . GLU B 1 59  ? 20.65500  28.82400  33.28400  1.000 76.07320  ?  59  GLU B CA  1 
ATOM   2160 C  C   . GLU B 1 59  ? 20.40100  27.81200  34.39400  1.000 77.41815  ?  59  GLU B C   1 
ATOM   2161 O  O   . GLU B 1 59  ? 19.27700  27.31900  34.53400  1.000 75.80901  ?  59  GLU B O   1 
ATOM   2162 C  CB  . GLU B 1 59  ? 19.96900  28.41000  31.98000  1.000 88.28442  ?  59  GLU B CB  1 
ATOM   2163 C  CG  . GLU B 1 59  ? 20.53400  27.15400  31.33900  1.000 94.43775  ?  59  GLU B CG  1 
ATOM   2164 C  CD  . GLU B 1 59  ? 19.92500  26.86300  29.97900  1.000 92.65267  ?  59  GLU B CD  1 
ATOM   2165 O  OE1 . GLU B 1 59  ? 19.00100  27.59400  29.56400  1.000 91.03130  ?  59  GLU B OE1 1 
ATOM   2166 O  OE2 . GLU B 1 59  ? 20.37700  25.90000  29.32500  1.000 88.96525  -1 59  GLU B OE2 1 
ATOM   2167 N  N   . LEU B 1 60  ? 21.42400  27.50700  35.19300  1.000 75.36515  ?  60  LEU B N   1 
ATOM   2168 C  CA  . LEU B 1 60  ? 21.33400  26.54600  36.28600  1.000 77.69148  ?  60  LEU B CA  1 
ATOM   2169 C  C   . LEU B 1 60  ? 21.95200  27.13800  37.54200  1.000 75.78692  ?  60  LEU B C   1 
ATOM   2170 O  O   . LEU B 1 60  ? 23.13000  27.51200  37.54200  1.000 81.78800  ?  60  LEU B O   1 
ATOM   2171 C  CB  . LEU B 1 60  ? 22.03900  25.23000  35.94000  1.000 71.37224  ?  60  LEU B CB  1 
ATOM   2172 C  CG  . LEU B 1 60  ? 21.15100  24.06000  35.52700  1.000 72.06246  ?  60  LEU B CG  1 
ATOM   2173 C  CD1 . LEU B 1 60  ? 21.94200  22.76000  35.53800  1.000 74.38617  ?  60  LEU B CD1 1 
ATOM   2174 C  CD2 . LEU B 1 60  ? 19.93600  23.96700  36.43300  1.000 69.59031  ?  60  LEU B CD2 1 
ATOM   2175 N  N   . PHE B 1 61  ? 21.15300  27.24100  38.60100  1.000 69.84651  ?  61  PHE B N   1 
ATOM   2176 C  CA  . PHE B 1 61  ? 21.66400  27.44200  39.94900  1.000 71.71107  ?  61  PHE B CA  1 
ATOM   2177 C  C   . PHE B 1 61  ? 21.79300  26.07300  40.60800  1.000 66.69018  ?  61  PHE B C   1 
ATOM   2178 O  O   . PHE B 1 61  ? 20.82400  25.30900  40.65000  1.000 67.27999  ?  61  PHE B O   1 
ATOM   2179 C  CB  . PHE B 1 61  ? 20.72900  28.35600  40.74100  1.000 66.86704  ?  61  PHE B CB  1 
ATOM   2180 C  CG  . PHE B 1 61  ? 21.43900  29.27400  41.68900  1.000 70.51871  ?  61  PHE B CG  1 
ATOM   2181 C  CD1 . PHE B 1 61  ? 22.40700  30.15000  41.22700  1.000 67.73903  ?  61  PHE B CD1 1 
ATOM   2182 C  CD2 . PHE B 1 61  ? 21.11500  29.28800  43.03500  1.000 75.67068  ?  61  PHE B CD2 1 
ATOM   2183 C  CE1 . PHE B 1 61  ? 23.05800  31.00400  42.09600  1.000 77.12290  ?  61  PHE B CE1 1 
ATOM   2184 C  CE2 . PHE B 1 61  ? 21.75900  30.14100  43.91100  1.000 69.93979  ?  61  PHE B CE2 1 
ATOM   2185 C  CZ  . PHE B 1 61  ? 22.73200  31.00200  43.44200  1.000 72.02853  ?  61  PHE B CZ  1 
ATOM   2186 N  N   . VAL B 1 62  ? 22.98500  25.75700  41.11200  1.000 64.56043  ?  62  VAL B N   1 
ATOM   2187 C  CA  . VAL B 1 62  ? 23.32500  24.39300  41.50600  1.000 68.71146  ?  62  VAL B CA  1 
ATOM   2188 C  C   . VAL B 1 62  ? 23.73500  24.35600  42.97200  1.000 69.69872  ?  62  VAL B C   1 
ATOM   2189 O  O   . VAL B 1 62  ? 24.59000  25.13600  43.40700  1.000 69.06112  ?  62  VAL B O   1 
ATOM   2190 C  CB  . VAL B 1 62  ? 24.45200  23.82000  40.62400  1.000 70.75162  ?  62  VAL B CB  1 
ATOM   2191 C  CG1 . VAL B 1 62  ? 24.80100  22.40400  41.05700  1.000 67.66581  ?  62  VAL B CG1 1 
ATOM   2192 C  CG2 . VAL B 1 62  ? 24.04600  23.84600  39.15800  1.000 75.75770  ?  62  VAL B CG2 1 
ATOM   2193 N  N   . HIS B 1 63  ? 23.13000  23.44100  43.72500  1.000 66.59998  ?  63  HIS B N   1 
ATOM   2194 C  CA  . HIS B 1 63  ? 23.58600  23.07500  45.05600  1.000 66.63955  ?  63  HIS B CA  1 
ATOM   2195 C  C   . HIS B 1 63  ? 23.71300  21.56200  45.13400  1.000 66.13151  ?  63  HIS B C   1 
ATOM   2196 O  O   . HIS B 1 63  ? 22.85400  20.83200  44.63100  1.000 66.65383  ?  63  HIS B O   1 
ATOM   2197 C  CB  . HIS B 1 63  ? 22.63600  23.57100  46.15400  1.000 69.54637  ?  63  HIS B CB  1 
ATOM   2198 C  CG  . HIS B 1 63  ? 22.89700  22.95800  47.49700  1.000 69.96665  ?  63  HIS B CG  1 
ATOM   2199 N  ND1 . HIS B 1 63  ? 24.02200  23.24100  48.24100  1.000 69.13605  ?  63  HIS B ND1 1 
ATOM   2200 C  CD2 . HIS B 1 63  ? 22.17300  22.07800  48.22900  1.000 63.72794  ?  63  HIS B CD2 1 
ATOM   2201 C  CE1 . HIS B 1 63  ? 23.98400  22.55600  49.37000  1.000 67.98221  ?  63  HIS B CE1 1 
ATOM   2202 N  NE2 . HIS B 1 63  ? 22.87200  21.84500  49.38900  1.000 67.88947  ?  63  HIS B NE2 1 
ATOM   2203 N  N   . ARG B 1 64  ? 24.77700  21.09500  45.78200  1.000 65.13321  ?  64  ARG B N   1 
ATOM   2204 C  CA  . ARG B 1 64  ? 25.01700  19.66700  45.91900  1.000 68.27209  ?  64  ARG B CA  1 
ATOM   2205 C  C   . ARG B 1 64  ? 25.53800  19.35900  47.31300  1.000 71.96346  ?  64  ARG B C   1 
ATOM   2206 O  O   . ARG B 1 64  ? 26.49400  19.98600  47.77900  1.000 73.83667  ?  64  ARG B O   1 
ATOM   2207 C  CB  . ARG B 1 64  ? 25.99900  19.16200  44.85200  1.000 67.91481  ?  64  ARG B CB  1 
ATOM   2208 C  CG  . ARG B 1 64  ? 25.41000  19.13100  43.44500  1.000 65.03524  ?  64  ARG B CG  1 
ATOM   2209 C  CD  . ARG B 1 64  ? 26.39800  18.62300  42.40100  1.000 66.53517  ?  64  ARG B CD  1 
ATOM   2210 N  NE  . ARG B 1 64  ? 25.78000  18.55100  41.08200  1.000 66.56591  ?  64  ARG B NE  1 
ATOM   2211 C  CZ  . ARG B 1 64  ? 25.08500  17.51400  40.63400  1.000 63.67352  ?  64  ARG B CZ  1 
ATOM   2212 N  NH1 . ARG B 1 64  ? 24.93400  16.41700  41.35900  1.000 58.67732  ?  64  ARG B NH1 1 
ATOM   2213 N  NH2 . ARG B 1 64  ? 24.52500  17.57800  39.43000  1.000 77.44874  ?  64  ARG B NH2 1 
ATOM   2214 N  N   . ASN B 1 65  ? 24.90600  18.38200  47.96300  1.000 69.43580  ?  65  ASN B N   1 
ATOM   2215 C  CA  . ASN B 1 65  ? 25.34800  17.84100  49.23900  1.000 58.69163  ?  65  ASN B CA  1 
ATOM   2216 C  C   . ASN B 1 65  ? 25.25800  16.32500  49.14300  1.000 60.96532  ?  65  ASN B C   1 
ATOM   2217 O  O   . ASN B 1 65  ? 24.79000  15.77800  48.13900  1.000 65.49044  ?  65  ASN B O   1 
ATOM   2218 C  CB  . ASN B 1 65  ? 24.51200  18.38000  50.40900  1.000 53.93382  ?  65  ASN B CB  1 
ATOM   2219 C  CG  . ASN B 1 65  ? 23.02900  18.06600  50.27100  1.000 50.61809  ?  65  ASN B CG  1 
ATOM   2220 O  OD1 . ASN B 1 65  ? 22.62100  16.90300  50.28600  1.000 47.92721  ?  65  ASN B OD1 1 
ATOM   2221 N  ND2 . ASN B 1 65  ? 22.21200  19.10700  50.16600  1.000 50.78717  ?  65  ASN B ND2 1 
ATOM   2222 N  N   . VAL B 1 66  ? 25.70900  15.63700  50.18900  1.000 50.34484  ?  66  VAL B N   1 
ATOM   2223 C  CA  . VAL B 1 66  ? 25.71800  14.17900  50.15900  1.000 49.06731  ?  66  VAL B CA  1 
ATOM   2224 C  C   . VAL B 1 66  ? 24.28300  13.66700  50.16500  1.000 53.74573  ?  66  VAL B C   1 
ATOM   2225 O  O   . VAL B 1 66  ? 23.51300  13.94700  51.09200  1.000 57.72029  ?  66  VAL B O   1 
ATOM   2226 C  CB  . VAL B 1 66  ? 26.52500  13.60500  51.32800  1.000 39.05648  ?  66  VAL B CB  1 
ATOM   2227 C  CG1 . VAL B 1 66  ? 26.58500  12.09200  51.22100  1.000 39.03977  ?  66  VAL B CG1 1 
ATOM   2228 C  CG2 . VAL B 1 66  ? 27.92900  14.19100  51.32900  1.000 49.55269  ?  66  VAL B CG2 1 
ATOM   2229 N  N   . ALA B 1 67  ? 23.92000  12.93300  49.10900  1.000 57.21687  ?  67  ALA B N   1 
ATOM   2230 C  CA  . ALA B 1 67  ? 22.61400  12.29200  48.95100  1.000 54.58303  ?  67  ALA B CA  1 
ATOM   2231 C  C   . ALA B 1 67  ? 21.48300  13.30000  48.76700  1.000 50.90234  ?  67  ALA B C   1 
ATOM   2232 O  O   . ALA B 1 67  ? 20.32700  13.00100  49.07800  1.000 46.59189  ?  67  ALA B O   1 
ATOM   2233 C  CB  . ALA B 1 67  ? 22.30400  11.35000  50.11700  1.000 54.19612  ?  67  ALA B CB  1 
ATOM   2234 N  N   . ASN B 1 68  ? 21.81600  14.48000  48.24300  1.000 52.29081  ?  68  ASN B N   1 
ATOM   2235 C  CA  . ASN B 1 68  ? 20.86400  15.51300  47.81600  1.000 56.67918  ?  68  ASN B CA  1 
ATOM   2236 C  C   . ASN B 1 68  ? 19.72100  15.70400  48.81800  1.000 57.00965  ?  68  ASN B C   1 
ATOM   2237 O  O   . ASN B 1 68  ? 18.54500  15.48900  48.52000  1.000 53.15543  ?  68  ASN B O   1 
ATOM   2238 C  CB  . ASN B 1 68  ? 20.32800  15.21600  46.41000  1.000 54.30986  ?  68  ASN B CB  1 
ATOM   2239 C  CG  . ASN B 1 68  ? 19.75800  13.81400  46.27100  1.000 53.55819  ?  68  ASN B CG  1 
ATOM   2240 O  OD1 . ASN B 1 68  ? 20.46800  12.87400  45.90800  1.000 53.04284  ?  68  ASN B OD1 1 
ATOM   2241 N  ND2 . ASN B 1 68  ? 18.46700  13.67100  46.54500  1.000 55.64336  ?  68  ASN B ND2 1 
ATOM   2242 N  N   . LEU B 1 69  ? 20.09500  16.12000  50.02700  1.000 57.94761  ?  69  LEU B N   1 
ATOM   2243 C  CA  . LEU B 1 69  ? 19.15500  16.31000  51.12300  1.000 59.59830  ?  69  LEU B CA  1 
ATOM   2244 C  C   . LEU B 1 69  ? 18.69900  17.76100  51.22200  1.000 58.74235  ?  69  LEU B C   1 
ATOM   2245 O  O   . LEU B 1 69  ? 19.44100  18.69100  50.89400  1.000 53.07673  ?  69  LEU B O   1 
ATOM   2246 C  CB  . LEU B 1 69  ? 19.77200  15.88300  52.45700  1.000 57.22125  ?  69  LEU B CB  1 
ATOM   2247 C  CG  . LEU B 1 69  ? 20.07900  14.39900  52.66600  1.000 57.72871  ?  69  LEU B CG  1 
ATOM   2248 C  CD1 . LEU B 1 69  ? 20.45600  14.14300  54.11700  1.000 53.90035  ?  69  LEU B CD1 1 
ATOM   2249 C  CD2 . LEU B 1 69  ? 18.89600  13.53900  52.26100  1.000 48.54242  ?  69  LEU B CD2 1 
ATOM   2250 N  N   . VAL B 1 70  ? 17.45900  17.94100  51.68000  1.000 60.21875  ?  70  VAL B N   1 
ATOM   2251 C  CA  . VAL B 1 70  ? 16.91200  19.25600  52.02300  1.000 62.36139  ?  70  VAL B CA  1 
ATOM   2252 C  C   . VAL B 1 70  ? 16.39300  19.14700  53.45600  1.000 63.71525  ?  70  VAL B C   1 
ATOM   2253 O  O   . VAL B 1 70  ? 15.21900  18.84000  53.69100  1.000 54.91114  ?  70  VAL B O   1 
ATOM   2254 C  CB  . VAL B 1 70  ? 15.81200  19.71500  51.06100  1.000 56.88717  ?  70  VAL B CB  1 
ATOM   2255 C  CG1 . VAL B 1 70  ? 15.29600  21.09100  51.46300  1.000 62.18897  ?  70  VAL B CG1 1 
ATOM   2256 C  CG2 . VAL B 1 70  ? 16.34200  19.75000  49.63600  1.000 58.70856  ?  70  VAL B CG2 1 
ATOM   2257 N  N   . ILE B 1 71  ? 17.27300  19.38700  54.42500  1.000 61.13648  ?  71  ILE B N   1 
ATOM   2258 C  CA  . ILE B 1 71  ? 16.93100  19.28200  55.83900  1.000 60.75598  ?  71  ILE B CA  1 
ATOM   2259 C  C   . ILE B 1 71  ? 16.27000  20.57600  56.29400  1.000 65.34147  ?  71  ILE B C   1 
ATOM   2260 O  O   . ILE B 1 71  ? 16.65300  21.66900  55.86100  1.000 69.27838  ?  71  ILE B O   1 
ATOM   2261 C  CB  . ILE B 1 71  ? 18.18800  18.96700  56.66800  1.000 61.28903  ?  71  ILE B CB  1 
ATOM   2262 C  CG1 . ILE B 1 71  ? 18.84000  17.67800  56.17200  1.000 57.50961  ?  71  ILE B CG1 1 
ATOM   2263 C  CG2 . ILE B 1 71  ? 17.83800  18.81700  58.14100  1.000 67.17273  ?  71  ILE B CG2 1 
ATOM   2264 C  CD1 . ILE B 1 71  ? 20.26300  17.50600  56.64000  1.000 56.25926  ?  71  ILE B CD1 1 
ATOM   2265 N  N   . HIS B 1 72  ? 15.25900  20.45300  57.16300  1.000 67.65417  ?  72  HIS B N   1 
ATOM   2266 C  CA  . HIS B 1 72  ? 14.49200  21.61900  57.60000  1.000 68.46610  ?  72  HIS B CA  1 
ATOM   2267 C  C   . HIS B 1 72  ? 15.37000  22.71600  58.19600  1.000 69.35659  ?  72  HIS B C   1 
ATOM   2268 O  O   . HIS B 1 72  ? 15.02500  23.89800  58.09700  1.000 73.24922  ?  72  HIS B O   1 
ATOM   2269 C  CB  . HIS B 1 72  ? 13.43000  21.20900  58.62300  1.000 61.55328  ?  72  HIS B CB  1 
ATOM   2270 C  CG  . HIS B 1 72  ? 12.54300  20.09100  58.17000  1.000 65.12554  ?  72  HIS B CG  1 
ATOM   2271 N  ND1 . HIS B 1 72  ? 11.70300  20.20300  57.08300  1.000 71.34334  ?  72  HIS B ND1 1 
ATOM   2272 C  CD2 . HIS B 1 72  ? 12.35400  18.84500  58.66500  1.000 63.16013  ?  72  HIS B CD2 1 
ATOM   2273 C  CE1 . HIS B 1 72  ? 11.03900  19.07200  56.92400  1.000 71.54138  ?  72  HIS B CE1 1 
ATOM   2274 N  NE2 . HIS B 1 72  ? 11.41600  18.23100  57.87100  1.000 62.88547  ?  72  HIS B NE2 1 
ATOM   2275 N  N   . THR B 1 73  ? 16.49600  22.36100  58.81900  1.000 69.16570  ?  73  THR B N   1 
ATOM   2276 C  CA  . THR B 1 73  ? 17.28800  23.33800  59.56100  1.000 66.95669  ?  73  THR B CA  1 
ATOM   2277 C  C   . THR B 1 73  ? 18.69400  23.51300  58.99500  1.000 67.65131  ?  73  THR B C   1 
ATOM   2278 O  O   . THR B 1 73  ? 19.59000  23.97400  59.71200  1.000 60.45345  ?  73  THR B O   1 
ATOM   2279 C  CB  . THR B 1 73  ? 17.36200  22.96600  61.04500  1.000 69.03082  ?  73  THR B CB  1 
ATOM   2280 O  OG1 . THR B 1 73  ? 17.67900  21.57500  61.18400  1.000 67.41336  ?  73  THR B OG1 1 
ATOM   2281 C  CG2 . THR B 1 73  ? 16.03400  23.25400  61.73300  1.000 65.14522  ?  73  THR B CG2 1 
ATOM   2282 N  N   . ASP B 1 74  ? 18.91100  23.16800  57.72700  1.000 70.25531  ?  74  ASP B N   1 
ATOM   2283 C  CA  . ASP B 1 74  ? 20.21600  23.34900  57.08900  1.000 65.98754  ?  74  ASP B CA  1 
ATOM   2284 C  C   . ASP B 1 74  ? 20.22700  24.70700  56.39800  1.000 66.81255  ?  74  ASP B C   1 
ATOM   2285 O  O   . ASP B 1 74  ? 19.68300  24.86500  55.30400  1.000 70.80005  ?  74  ASP B O   1 
ATOM   2286 C  CB  . ASP B 1 74  ? 20.50000  22.22100  56.10400  1.000 63.70878  ?  74  ASP B CB  1 
ATOM   2287 C  CG  . ASP B 1 74  ? 21.77000  22.45200  55.30300  1.000 74.03141  ?  74  ASP B CG  1 
ATOM   2288 O  OD1 . ASP B 1 74  ? 22.68900  23.12700  55.81700  1.000 73.73936  ?  74  ASP B OD1 1 
ATOM   2289 O  OD2 . ASP B 1 74  ? 21.84700  21.95900  54.15600  1.000 73.84362  -1 74  ASP B OD2 1 
ATOM   2290 N  N   . LEU B 1 75  ? 20.87600  25.68700  57.03200  1.000 66.60605  ?  75  LEU B N   1 
ATOM   2291 C  CA  . LEU B 1 75  ? 20.88600  27.04300  56.49300  1.000 65.81201  ?  75  LEU B CA  1 
ATOM   2292 C  C   . LEU B 1 75  ? 21.62800  27.12000  55.16400  1.000 66.12318  ?  75  LEU B C   1 
ATOM   2293 O  O   . LEU B 1 75  ? 21.35600  28.01700  54.36000  1.000 70.99989  ?  75  LEU B O   1 
ATOM   2294 C  CB  . LEU B 1 75  ? 21.50300  28.00700  57.50600  1.000 68.19036  ?  75  LEU B CB  1 
ATOM   2295 C  CG  . LEU B 1 75  ? 21.08300  29.47000  57.35900  1.000 67.60460  ?  75  LEU B CG  1 
ATOM   2296 C  CD1 . LEU B 1 75  ? 19.58600  29.56700  57.10500  1.000 67.84428  ?  75  LEU B CD1 1 
ATOM   2297 C  CD2 . LEU B 1 75  ? 21.45900  30.26200  58.59300  1.000 73.31373  ?  75  LEU B CD2 1 
ATOM   2298 N  N   . ASN B 1 76  ? 22.57400  26.20900  54.92700  1.000 64.14065  ?  76  ASN B N   1 
ATOM   2299 C  CA  . ASN B 1 76  ? 23.27200  26.12600  53.64900  1.000 67.70357  ?  76  ASN B CA  1 
ATOM   2300 C  C   . ASN B 1 76  ? 22.26100  25.97900  52.51700  1.000 69.67266  ?  76  ASN B C   1 
ATOM   2301 O  O   . ASN B 1 76  ? 22.10500  26.88700  51.69300  1.000 66.11303  ?  76  ASN B O   1 
ATOM   2302 C  CB  . ASN B 1 76  ? 24.26100  24.95400  53.66000  1.000 72.39411  ?  76  ASN B CB  1 
ATOM   2303 C  CG  . ASN B 1 76  ? 25.19000  24.94400  52.45100  1.000 71.19141  ?  76  ASN B CG  1 
ATOM   2304 O  OD1 . ASN B 1 76  ? 24.79100  25.27800  51.33500  1.000 66.87547  ?  76  ASN B OD1 1 
ATOM   2305 N  ND2 . ASN B 1 76  ? 26.44100  24.55300  52.67400  1.000 71.86095  ?  76  ASN B ND2 1 
ATOM   2306 N  N   . CYS B 1 77  ? 21.58000  24.83200  52.46800  1.000 67.19761  ?  77  CYS B N   1 
ATOM   2307 C  CA  . CYS B 1 77  ? 20.58100  24.60500  51.42800  1.000 65.80424  ?  77  CYS B CA  1 
ATOM   2308 C  C   . CYS B 1 77  ? 19.47600  25.65300  51.47800  1.000 68.73192  ?  77  CYS B C   1 
ATOM   2309 O  O   . CYS B 1 77  ? 18.99300  26.10500  50.43400  1.000 74.81448  ?  77  CYS B O   1 
ATOM   2310 C  CB  . CYS B 1 77  ? 19.99100  23.20200  51.55800  1.000 65.41613  ?  77  CYS B CB  1 
ATOM   2311 S  SG  . CYS B 1 77  ? 18.74900  22.81600  50.29800  1.000 62.36859  ?  77  CYS B SG  1 
ATOM   2312 N  N   . LEU B 1 78  ? 19.05400  26.04500  52.68400  1.000 66.49489  ?  78  LEU B N   1 
ATOM   2313 C  CA  . LEU B 1 78  ? 17.96400  27.01000  52.80000  1.000 68.41397  ?  78  LEU B CA  1 
ATOM   2314 C  C   . LEU B 1 78  ? 18.36200  28.37900  52.26500  1.000 67.87274  ?  78  LEU B C   1 
ATOM   2315 O  O   . LEU B 1 78  ? 17.51700  29.08800  51.70700  1.000 69.01618  ?  78  LEU B O   1 
ATOM   2316 C  CB  . LEU B 1 78  ? 17.49200  27.11000  54.24900  1.000 72.89377  ?  78  LEU B CB  1 
ATOM   2317 C  CG  . LEU B 1 78  ? 16.79700  25.85500  54.77700  1.000 74.13527  ?  78  LEU B CG  1 
ATOM   2318 C  CD1 . LEU B 1 78  ? 16.52500  25.98500  56.26400  1.000 69.67804  ?  78  LEU B CD1 1 
ATOM   2319 C  CD2 . LEU B 1 78  ? 15.51400  25.58300  54.00500  1.000 61.16020  ?  78  LEU B CD2 1 
ATOM   2320 N  N   . SER B 1 79  ? 19.62400  28.77800  52.43200  1.000 64.56799  ?  79  SER B N   1 
ATOM   2321 C  CA  . SER B 1 79  ? 20.06000  30.04000  51.84400  1.000 68.61898  ?  79  SER B CA  1 
ATOM   2322 C  C   . SER B 1 79  ? 20.04400  29.96200  50.32200  1.000 72.50086  ?  79  SER B C   1 
ATOM   2323 O  O   . SER B 1 79  ? 19.66200  30.92700  49.64900  1.000 68.28985  ?  79  SER B O   1 
ATOM   2324 C  CB  . SER B 1 79  ? 21.45100  30.41300  52.35100  1.000 66.94480  ?  79  SER B CB  1 
ATOM   2325 O  OG  . SER B 1 79  ? 21.44400  30.62800  53.75000  1.000 66.40259  ?  79  SER B OG  1 
ATOM   2326 N  N   . VAL B 1 80  ? 20.44700  28.81700  49.76400  1.000 71.07011  ?  80  VAL B N   1 
ATOM   2327 C  CA  . VAL B 1 80  ? 20.37000  28.61700  48.31800  1.000 68.80757  ?  80  VAL B CA  1 
ATOM   2328 C  C   . VAL B 1 80  ? 18.92900  28.75000  47.84600  1.000 64.65271  ?  80  VAL B C   1 
ATOM   2329 O  O   . VAL B 1 80  ? 18.63400  29.46800  46.88400  1.000 67.78964  ?  80  VAL B O   1 
ATOM   2330 C  CB  . VAL B 1 80  ? 20.96300  27.25100  47.92700  1.000 64.43968  ?  80  VAL B CB  1 
ATOM   2331 C  CG1 . VAL B 1 80  ? 20.77900  27.00400  46.44000  1.000 67.75478  ?  80  VAL B CG1 1 
ATOM   2332 C  CG2 . VAL B 1 80  ? 22.43400  27.18400  48.29900  1.000 72.38715  ?  80  VAL B CG2 1 
ATOM   2333 N  N   . VAL B 1 81  ? 18.01100  28.05200  48.51800  1.000 61.13721  ?  81  VAL B N   1 
ATOM   2334 C  CA  . VAL B 1 81  ? 16.60700  28.08300  48.11700  1.000 59.62772  ?  81  VAL B CA  1 
ATOM   2335 C  C   . VAL B 1 81  ? 16.04600  29.49600  48.22600  1.000 63.45656  ?  81  VAL B C   1 
ATOM   2336 O  O   . VAL B 1 81  ? 15.36400  29.98100  47.31800  1.000 68.99036  ?  81  VAL B O   1 
ATOM   2337 C  CB  . VAL B 1 81  ? 15.78900  27.08400  48.95500  1.000 62.05559  ?  81  VAL B CB  1 
ATOM   2338 C  CG1 . VAL B 1 81  ? 14.31800  27.16900  48.59300  1.000 60.79464  ?  81  VAL B CG1 1 
ATOM   2339 C  CG2 . VAL B 1 81  ? 16.30600  25.67100  48.73800  1.000 60.06582  ?  81  VAL B CG2 1 
ATOM   2340 N  N   . GLN B 1 82  ? 16.33500  30.18700  49.33200  1.000 69.54250  ?  82  GLN B N   1 
ATOM   2341 C  CA  . GLN B 1 82  ? 15.79300  31.53200  49.50400  1.000 73.82708  ?  82  GLN B CA  1 
ATOM   2342 C  C   . GLN B 1 82  ? 16.37200  32.50000  48.48000  1.000 74.40348  ?  82  GLN B C   1 
ATOM   2343 O  O   . GLN B 1 82  ? 15.63800  33.30900  47.90000  1.000 69.95483  ?  82  GLN B O   1 
ATOM   2344 C  CB  . GLN B 1 82  ? 16.05900  32.04200  50.91800  1.000 65.98595  ?  82  GLN B CB  1 
ATOM   2345 C  CG  . GLN B 1 82  ? 15.22700  33.26200  51.29600  1.000 68.15299  ?  82  GLN B CG  1 
ATOM   2346 C  CD  . GLN B 1 82  ? 15.89200  34.57300  50.92400  1.000 68.08379  ?  82  GLN B CD  1 
ATOM   2347 O  OE1 . GLN B 1 82  ? 17.11700  34.67000  50.87500  1.000 63.17292  ?  82  GLN B OE1 1 
ATOM   2348 N  NE2 . GLN B 1 82  ? 15.08300  35.59800  50.68100  1.000 68.88614  ?  82  GLN B NE2 1 
ATOM   2349 N  N   . TYR B 1 83  ? 17.68500  32.43800  48.24900  1.000 73.14887  ?  83  TYR B N   1 
ATOM   2350 C  CA  . TYR B 1 83  ? 18.29900  33.32400  47.26500  1.000 69.12455  ?  83  TYR B CA  1 
ATOM   2351 C  C   . TYR B 1 83  ? 17.79200  33.03800  45.85700  1.000 76.19901  ?  83  TYR B C   1 
ATOM   2352 O  O   . TYR B 1 83  ? 17.51100  33.96800  45.09300  1.000 77.70314  ?  83  TYR B O   1 
ATOM   2353 C  CB  . TYR B 1 83  ? 19.81900  33.20000  47.32100  1.000 71.90757  ?  83  TYR B CB  1 
ATOM   2354 C  CG  . TYR B 1 83  ? 20.52600  34.17100  46.40700  1.000 81.08126  ?  83  TYR B CG  1 
ATOM   2355 C  CD1 . TYR B 1 83  ? 20.50200  35.53600  46.66000  1.000 80.41023  ?  83  TYR B CD1 1 
ATOM   2356 C  CD2 . TYR B 1 83  ? 21.20900  33.72200  45.28300  1.000 75.93930  ?  83  TYR B CD2 1 
ATOM   2357 C  CE1 . TYR B 1 83  ? 21.14100  36.42700  45.82200  1.000 79.29817  ?  83  TYR B CE1 1 
ATOM   2358 C  CE2 . TYR B 1 83  ? 21.85400  34.60500  44.44200  1.000 69.14938  ?  83  TYR B CE2 1 
ATOM   2359 C  CZ  . TYR B 1 83  ? 21.81700  35.95600  44.71500  1.000 70.72548  ?  83  TYR B CZ  1 
ATOM   2360 O  OH  . TYR B 1 83  ? 22.45700  36.84000  43.87900  1.000 77.33389  ?  83  TYR B OH  1 
ATOM   2361 N  N   . ALA B 1 84  ? 17.66600  31.76000  45.49500  1.000 75.83974  ?  84  ALA B N   1 
ATOM   2362 C  CA  . ALA B 1 84  ? 17.15700  31.41700  44.17200  1.000 69.52415  ?  84  ALA B CA  1 
ATOM   2363 C  C   . ALA B 1 84  ? 15.70200  31.84200  44.01900  1.000 70.74421  ?  84  ALA B C   1 
ATOM   2364 O  O   . ALA B 1 84  ? 15.32800  32.46400  43.01800  1.000 76.28147  ?  84  ALA B O   1 
ATOM   2365 C  CB  . ALA B 1 84  ? 17.31700  29.91800  43.91500  1.000 64.73297  ?  84  ALA B CB  1 
ATOM   2366 N  N   . VAL B 1 85  ? 14.86500  31.51100  45.00300  1.000 66.63295  ?  85  VAL B N   1 
ATOM   2367 C  CA  . VAL B 1 85  ? 13.43100  31.74600  44.87400  1.000 69.58601  ?  85  VAL B CA  1 
ATOM   2368 C  C   . VAL B 1 85  ? 13.09100  33.22200  45.05700  1.000 73.74868  ?  85  VAL B C   1 
ATOM   2369 O  O   . VAL B 1 85  ? 12.29100  33.78100  44.29900  1.000 75.82600  ?  85  VAL B O   1 
ATOM   2370 C  CB  . VAL B 1 85  ? 12.66000  30.86000  45.86900  1.000 62.77822  ?  85  VAL B CB  1 
ATOM   2371 C  CG1 . VAL B 1 85  ? 11.18000  31.19700  45.84700  1.000 61.49621  ?  85  VAL B CG1 1 
ATOM   2372 C  CG2 . VAL B 1 85  ? 12.86700  29.39100  45.53600  1.000 61.28697  ?  85  VAL B CG2 1 
ATOM   2373 N  N   . ASP B 1 86  ? 13.69200  33.88100  46.04600  1.000 76.24591  ?  86  ASP B N   1 
ATOM   2374 C  CA  . ASP B 1 86  ? 13.30000  35.24700  46.37600  1.000 74.80111  ?  86  ASP B CA  1 
ATOM   2375 C  C   . ASP B 1 86  ? 14.08400  36.30600  45.61200  1.000 72.26017  ?  86  ASP B C   1 
ATOM   2376 O  O   . ASP B 1 86  ? 13.54600  37.38800  45.35200  1.000 72.95269  ?  86  ASP B O   1 
ATOM   2377 C  CB  . ASP B 1 86  ? 13.43600  35.49100  47.88200  1.000 74.99603  ?  86  ASP B CB  1 
ATOM   2378 C  CG  . ASP B 1 86  ? 12.49000  34.62900  48.70000  1.000 77.89974  ?  86  ASP B CG  1 
ATOM   2379 O  OD1 . ASP B 1 86  ? 11.65700  33.92300  48.09400  1.000 78.27340  ?  86  ASP B OD1 1 
ATOM   2380 O  OD2 . ASP B 1 86  ? 12.58000  34.65600  49.94700  1.000 86.97828  -1 86  ASP B OD2 1 
ATOM   2381 N  N   . VAL B 1 87  ? 15.34000  36.03800  45.25400  1.000 72.90075  ?  87  VAL B N   1 
ATOM   2382 C  CA  . VAL B 1 87  ? 16.15800  37.04400  44.58200  1.000 75.29657  ?  87  VAL B CA  1 
ATOM   2383 C  C   . VAL B 1 87  ? 16.23500  36.75400  43.08800  1.000 73.97814  ?  87  VAL B C   1 
ATOM   2384 O  O   . VAL B 1 87  ? 15.86400  37.59700  42.26500  1.000 74.94851  ?  87  VAL B O   1 
ATOM   2385 C  CB  . VAL B 1 87  ? 17.56500  37.12000  45.20100  1.000 72.47554  ?  87  VAL B CB  1 
ATOM   2386 C  CG1 . VAL B 1 87  ? 18.34600  38.27500  44.59800  1.000 74.15729  ?  87  VAL B CG1 1 
ATOM   2387 C  CG2 . VAL B 1 87  ? 17.46700  37.27100  46.71000  1.000 74.60458  ?  87  VAL B CG2 1 
ATOM   2388 N  N   . LEU B 1 88  ? 16.71200  35.56100  42.72200  1.000 73.75341  ?  88  LEU B N   1 
ATOM   2389 C  CA  . LEU B 1 88  ? 16.80700  35.20000  41.31200  1.000 73.87420  ?  88  LEU B CA  1 
ATOM   2390 C  C   . LEU B 1 88  ? 15.45900  34.83400  40.70600  1.000 74.54082  ?  88  LEU B C   1 
ATOM   2391 O  O   . LEU B 1 88  ? 15.30800  34.90100  39.48100  1.000 79.82991  ?  88  LEU B O   1 
ATOM   2392 C  CB  . LEU B 1 88  ? 17.77400  34.02700  41.12100  1.000 71.99990  ?  88  LEU B CB  1 
ATOM   2393 C  CG  . LEU B 1 88  ? 19.23600  34.19500  41.53600  1.000 70.00102  ?  88  LEU B CG  1 
ATOM   2394 C  CD1 . LEU B 1 88  ? 20.02000  32.94000  41.18600  1.000 70.02804  ?  88  LEU B CD1 1 
ATOM   2395 C  CD2 . LEU B 1 88  ? 19.85800  35.41800  40.88000  1.000 77.07269  ?  88  LEU B CD2 1 
ATOM   2396 N  N   . GLU B 1 89  ? 14.48900  34.44700  41.53500  1.000 73.63366  ?  89  GLU B N   1 
ATOM   2397 C  CA  . GLU B 1 89  ? 13.13700  34.10700  41.09000  1.000 73.52258  ?  89  GLU B CA  1 
ATOM   2398 C  C   . GLU B 1 89  ? 13.14900  32.98600  40.05200  1.000 71.93976  ?  89  GLU B C   1 
ATOM   2399 O  O   . GLU B 1 89  ? 12.53400  33.08700  38.98800  1.000 73.24799  ?  89  GLU B O   1 
ATOM   2400 C  CB  . GLU B 1 89  ? 12.40500  35.33800  40.55400  1.000 71.89689  ?  89  GLU B CB  1 
ATOM   2401 C  CG  . GLU B 1 89  ? 12.07700  36.37500  41.60700  1.000 78.21073  ?  89  GLU B CG  1 
ATOM   2402 C  CD  . GLU B 1 89  ? 11.33000  37.56000  41.03300  1.000 81.39526  ?  89  GLU B CD  1 
ATOM   2403 O  OE1 . GLU B 1 89  ? 11.79900  38.12800  40.02500  1.000 86.64197  ?  89  GLU B OE1 1 
ATOM   2404 O  OE2 . GLU B 1 89  ? 10.26300  37.91300  41.58000  1.000 88.05912  -1 89  GLU B OE2 1 
ATOM   2405 N  N   . VAL B 1 90  ? 13.85600  31.90000  40.37200  1.000 70.43202  ?  90  VAL B N   1 
ATOM   2406 C  CA  . VAL B 1 90  ? 13.79100  30.71900  39.52600  1.000 68.80084  ?  90  VAL B CA  1 
ATOM   2407 C  C   . VAL B 1 90  ? 12.37300  30.15800  39.58400  1.000 71.78735  ?  90  VAL B C   1 
ATOM   2408 O  O   . VAL B 1 90  ? 11.67000  30.27800  40.59500  1.000 75.40674  ?  90  VAL B O   1 
ATOM   2409 C  CB  . VAL B 1 90  ? 14.83200  29.66500  39.93900  1.000 66.17335  ?  90  VAL B CB  1 
ATOM   2410 C  CG1 . VAL B 1 90  ? 16.23700  30.23000  39.80200  1.000 63.58693  ?  90  VAL B CG1 1 
ATOM   2411 C  CG2 . VAL B 1 90  ? 14.58500  29.19900  41.36200  1.000 62.74886  ?  90  VAL B CG2 1 
ATOM   2412 N  N   . GLU B 1 91  ? 11.94100  29.55600  38.47900  1.000 73.46457  ?  91  GLU B N   1 
ATOM   2413 C  CA  . GLU B 1 91  ? 10.59000  29.02600  38.36600  1.000 69.20697  ?  91  GLU B CA  1 
ATOM   2414 C  C   . GLU B 1 91  ? 10.51600  27.51200  38.49800  1.000 63.64397  ?  91  GLU B C   1 
ATOM   2415 O  O   . GLU B 1 91  ? 9.41000   26.96600  38.56000  1.000 62.98660  ?  91  GLU B O   1 
ATOM   2416 C  CB  . GLU B 1 91  ? 9.96900   29.47100  37.03600  1.000 75.65134  ?  91  GLU B CB  1 
ATOM   2417 C  CG  . GLU B 1 91  ? 10.21100  30.94100  36.73500  1.000 83.85180  ?  91  GLU B CG  1 
ATOM   2418 C  CD  . GLU B 1 91  ? 9.49800   31.41100  35.48700  1.000 98.45536  ?  91  GLU B CD  1 
ATOM   2419 O  OE1 . GLU B 1 91  ? 9.37100   30.61100  34.53700  1.000 114.60398 ?  91  GLU B OE1 1 
ATOM   2420 O  OE2 . GLU B 1 91  ? 9.03500   32.57100  35.47200  1.000 102.94093 -1 91  GLU B OE2 1 
ATOM   2421 N  N   . HIS B 1 92  ? 11.65200  26.82400  38.54500  1.000 61.58546  ?  92  HIS B N   1 
ATOM   2422 C  CA  . HIS B 1 92  ? 11.66600  25.38000  38.72200  1.000 63.93857  ?  92  HIS B CA  1 
ATOM   2423 C  C   . HIS B 1 92  ? 12.79800  24.99900  39.65800  1.000 68.44341  ?  92  HIS B C   1 
ATOM   2424 O  O   . HIS B 1 92  ? 13.92800  25.47000  39.49800  1.000 70.10391  ?  92  HIS B O   1 
ATOM   2425 C  CB  . HIS B 1 92  ? 11.82700  24.63300  37.39100  1.000 70.79796  ?  92  HIS B CB  1 
ATOM   2426 C  CG  . HIS B 1 92  ? 10.65500  24.77000  36.47100  1.000 69.05132  ?  92  HIS B CG  1 
ATOM   2427 N  ND1 . HIS B 1 92  ? 9.45800   24.12400  36.69500  1.000 70.81924  ?  92  HIS B ND1 1 
ATOM   2428 C  CD2 . HIS B 1 92  ? 10.49900  25.46000  35.31700  1.000 66.06579  ?  92  HIS B CD2 1 
ATOM   2429 C  CE1 . HIS B 1 92  ? 8.61200   24.42100  35.72500  1.000 65.39681  ?  92  HIS B CE1 1 
ATOM   2430 N  NE2 . HIS B 1 92  ? 9.21900   25.22900  34.87600  1.000 70.35897  ?  92  HIS B NE2 1 
ATOM   2431 N  N   . ILE B 1 93  ? 12.48800  24.14600  40.62900  1.000 63.87089  ?  93  ILE B N   1 
ATOM   2432 C  CA  . ILE B 1 93  ? 13.48300  23.55600  41.51200  1.000 63.80540  ?  93  ILE B CA  1 
ATOM   2433 C  C   . ILE B 1 93  ? 13.42900  22.05200  41.30900  1.000 62.15408  ?  93  ILE B C   1 
ATOM   2434 O  O   . ILE B 1 93  ? 12.36500  21.43600  41.45000  1.000 60.51723  ?  93  ILE B O   1 
ATOM   2435 C  CB  . ILE B 1 93  ? 13.24800  23.92700  42.98300  1.000 63.91129  ?  93  ILE B CB  1 
ATOM   2436 C  CG1 . ILE B 1 93  ? 13.18600  25.44600  43.14400  1.000 65.52859  ?  93  ILE B CG1 1 
ATOM   2437 C  CG2 . ILE B 1 93  ? 14.35200  23.34700  43.84900  1.000 57.61496  ?  93  ILE B CG2 1 
ATOM   2438 C  CD1 . ILE B 1 93  ? 12.92300  25.89400  44.56100  1.000 56.45071  ?  93  ILE B CD1 1 
ATOM   2439 N  N   . ILE B 1 94  ? 14.57100  21.46600  40.97100  1.000 57.27848  ?  94  ILE B N   1 
ATOM   2440 C  CA  . ILE B 1 94  ? 14.67600  20.05100  40.64900  1.000 58.64137  ?  94  ILE B CA  1 
ATOM   2441 C  C   . ILE B 1 94  ? 15.54500  19.38900  41.70200  1.000 62.21483  ?  94  ILE B C   1 
ATOM   2442 O  O   . ILE B 1 94  ? 16.71800  19.75000  41.86400  1.000 66.29552  ?  94  ILE B O   1 
ATOM   2443 C  CB  . ILE B 1 94  ? 15.25200  19.82100  39.24200  1.000 62.37882  ?  94  ILE B CB  1 
ATOM   2444 C  CG1 . ILE B 1 94  ? 14.27900  20.32800  38.17500  1.000 57.44897  ?  94  ILE B CG1 1 
ATOM   2445 C  CG2 . ILE B 1 94  ? 15.60200  18.35200  39.03900  1.000 59.51743  ?  94  ILE B CG2 1 
ATOM   2446 C  CD1 . ILE B 1 94  ? 14.95700  20.91200  36.95800  1.000 62.91765  ?  94  ILE B CD1 1 
ATOM   2447 N  N   . ILE B 1 95  ? 14.96700  18.43900  42.42600  1.000 58.99787  ?  95  ILE B N   1 
ATOM   2448 C  CA  . ILE B 1 95  ? 15.71000  17.57800  43.33300  1.000 60.03328  ?  95  ILE B CA  1 
ATOM   2449 C  C   . ILE B 1 95  ? 15.93100  16.26000  42.60800  1.000 56.69703  ?  95  ILE B C   1 
ATOM   2450 O  O   . ILE B 1 95  ? 14.96700  15.56700  42.25900  1.000 55.37557  ?  95  ILE B O   1 
ATOM   2451 C  CB  . ILE B 1 95  ? 14.95800  17.36300  44.65700  1.000 54.85573  ?  95  ILE B CB  1 
ATOM   2452 C  CG1 . ILE B 1 95  ? 14.72600  18.69600  45.37000  1.000 51.42361  ?  95  ILE B CG1 1 
ATOM   2453 C  CG2 . ILE B 1 95  ? 15.72600  16.40100  45.55200  1.000 47.73031  ?  95  ILE B CG2 1 
ATOM   2454 C  CD1 . ILE B 1 95  ? 14.01000  18.56300  46.69000  1.000 52.34843  ?  95  ILE B CD1 1 
ATOM   2455 N  N   . CYS B 1 96  ? 17.19100  15.91800  42.35600  1.000 48.09130  ?  96  CYS B N   1 
ATOM   2456 C  CA  . CYS B 1 96  ? 17.51900  14.74400  41.56000  1.000 51.37461  ?  96  CYS B CA  1 
ATOM   2457 C  C   . CYS B 1 96  ? 18.53700  13.89800  42.30500  1.000 60.49238  ?  96  CYS B C   1 
ATOM   2458 O  O   . CYS B 1 96  ? 19.64200  14.36500  42.59900  1.000 60.70496  ?  96  CYS B O   1 
ATOM   2459 C  CB  . CYS B 1 96  ? 18.05500  15.13200  40.18100  1.000 64.93492  ?  96  CYS B CB  1 
ATOM   2460 S  SG  . CYS B 1 96  ? 18.29200  13.72200  39.07400  1.000 78.11612  ?  96  CYS B SG  1 
ATOM   2461 N  N   . GLY B 1 97  ? 18.15700  12.65700  42.61000  1.000 64.06995  ?  97  GLY B N   1 
ATOM   2462 C  CA  . GLY B 1 97  ? 19.07600  11.66400  43.11500  1.000 60.11378  ?  97  GLY B CA  1 
ATOM   2463 C  C   . GLY B 1 97  ? 19.51200  10.71700  42.00700  1.000 61.70444  ?  97  GLY B C   1 
ATOM   2464 O  O   . GLY B 1 97  ? 19.11800  10.84100  40.85100  1.000 58.63820  ?  97  GLY B O   1 
ATOM   2465 N  N   . HIS B 1 98  ? 20.33800  9.74700   42.38800  1.000 57.97560  ?  98  HIS B N   1 
ATOM   2466 C  CA  . HIS B 1 98  ? 20.88000  8.79700   41.42700  1.000 62.93149  ?  98  HIS B CA  1 
ATOM   2467 C  C   . HIS B 1 98  ? 21.02000  7.42900   42.07400  1.000 63.15971  ?  98  HIS B C   1 
ATOM   2468 O  O   . HIS B 1 98  ? 21.56000  7.31300   43.17800  1.000 75.39849  ?  98  HIS B O   1 
ATOM   2469 C  CB  . HIS B 1 98  ? 22.23500  9.26300   40.88600  1.000 67.63075  ?  98  HIS B CB  1 
ATOM   2470 C  CG  . HIS B 1 98  ? 23.27100  9.45800   41.94500  1.000 61.88673  ?  98  HIS B CG  1 
ATOM   2471 N  ND1 . HIS B 1 98  ? 24.35200  8.61600   42.09100  1.000 63.70872  ?  98  HIS B ND1 1 
ATOM   2472 C  CD2 . HIS B 1 98  ? 23.39700  10.40300  42.90600  1.000 65.58612  ?  98  HIS B CD2 1 
ATOM   2473 C  CE1 . HIS B 1 98  ? 25.09700  9.03100   43.09900  1.000 68.50944  ?  98  HIS B CE1 1 
ATOM   2474 N  NE2 . HIS B 1 98  ? 24.54000  10.11400  43.61000  1.000 70.78502  ?  98  HIS B NE2 1 
ATOM   2475 N  N   . TYR B 1 99  ? 20.52200  6.40500   41.38500  1.000 58.54559  ?  99  TYR B N   1 
ATOM   2476 C  CA  . TYR B 1 99  ? 20.60200  5.03900   41.88300  1.000 61.45809  ?  99  TYR B CA  1 
ATOM   2477 C  C   . TYR B 1 99  ? 22.05200  4.61500   42.06900  1.000 65.76413  ?  99  TYR B C   1 
ATOM   2478 O  O   . TYR B 1 99  ? 22.92300  4.93800   41.25600  1.000 68.00064  ?  99  TYR B O   1 
ATOM   2479 C  CB  . TYR B 1 99  ? 19.89300  4.08900   40.92200  1.000 64.47473  ?  99  TYR B CB  1 
ATOM   2480 C  CG  . TYR B 1 99  ? 18.49100  4.53100   40.59300  1.000 66.11682  ?  99  TYR B CG  1 
ATOM   2481 C  CD1 . TYR B 1 99  ? 17.43100  4.22300   41.43500  1.000 60.90898  ?  99  TYR B CD1 1 
ATOM   2482 C  CD2 . TYR B 1 99  ? 18.22700  5.26400   39.44500  1.000 70.67789  ?  99  TYR B CD2 1 
ATOM   2483 C  CE1 . TYR B 1 99  ? 16.14700  4.63100   41.14100  1.000 64.26205  ?  99  TYR B CE1 1 
ATOM   2484 C  CE2 . TYR B 1 99  ? 16.94700  5.67700   39.14100  1.000 68.47445  ?  99  TYR B CE2 1 
ATOM   2485 C  CZ  . TYR B 1 99  ? 15.91000  5.35700   39.99400  1.000 69.39064  ?  99  TYR B CZ  1 
ATOM   2486 O  OH  . TYR B 1 99  ? 14.62900  5.76300   39.69900  1.000 67.68137  ?  99  TYR B OH  1 
ATOM   2487 N  N   . GLY B 1 100 ? 22.31100  3.90800   43.16300  1.000 62.76977  ?  100 GLY B N   1 
ATOM   2488 C  CA  . GLY B 1 100 ? 23.66000  3.51900   43.50000  1.000 63.45264  ?  100 GLY B CA  1 
ATOM   2489 C  C   . GLY B 1 100 ? 24.40000  4.53300   44.33600  1.000 72.01719  ?  100 GLY B C   1 
ATOM   2490 O  O   . GLY B 1 100 ? 25.60500  4.36500   44.55900  1.000 72.72185  ?  100 GLY B O   1 
ATOM   2491 N  N   . CYS B 1 101 ? 23.71500  5.58100   44.79600  1.000 73.18866  ?  101 CYS B N   1 
ATOM   2492 C  CA  . CYS B 1 101 ? 24.34400  6.65500   45.55200  1.000 67.39320  ?  101 CYS B CA  1 
ATOM   2493 C  C   . CYS B 1 101 ? 25.12600  6.10000   46.73200  1.000 64.30389  ?  101 CYS B C   1 
ATOM   2494 O  O   . CYS B 1 101 ? 24.61800  5.28100   47.50200  1.000 69.13798  ?  101 CYS B O   1 
ATOM   2495 C  CB  . CYS B 1 101 ? 23.27200  7.63600   46.03500  1.000 65.22735  ?  101 CYS B CB  1 
ATOM   2496 S  SG  . CYS B 1 101 ? 23.87100  8.98400   47.07400  1.000 79.42786  ?  101 CYS B SG  1 
ATOM   2497 N  N   . GLY B 1 102 ? 26.37500  6.54900   46.86200  1.000 67.34491  ?  102 GLY B N   1 
ATOM   2498 C  CA  . GLY B 1 102 ? 27.21300  6.06600   47.94700  1.000 70.16668  ?  102 GLY B CA  1 
ATOM   2499 C  C   . GLY B 1 102 ? 26.67200  6.44100   49.31200  1.000 69.24782  ?  102 GLY B C   1 
ATOM   2500 O  O   . GLY B 1 102 ? 26.78400  5.66900   50.26700  1.000 72.31082  ?  102 GLY B O   1 
ATOM   2501 N  N   . GLY B 1 103 ? 26.07500  7.62800   49.42200  1.000 63.30037  ?  103 GLY B N   1 
ATOM   2502 C  CA  . GLY B 1 103 ? 25.51900  8.04600   50.69700  1.000 64.73103  ?  103 GLY B CA  1 
ATOM   2503 C  C   . GLY B 1 103 ? 24.30700  7.23200   51.11200  1.000 66.57683  ?  103 GLY B C   1 
ATOM   2504 O  O   . GLY B 1 103 ? 24.19700  6.81500   52.26900  1.000 75.85246  ?  103 GLY B O   1 
ATOM   2505 N  N   . VAL B 1 104 ? 23.38600  6.98900   50.17500  1.000 60.48562  ?  104 VAL B N   1 
ATOM   2506 C  CA  . VAL B 1 104 ? 22.17000  6.24600   50.50000  1.000 64.12105  ?  104 VAL B CA  1 
ATOM   2507 C  C   . VAL B 1 104 ? 22.50000  4.82000   50.92300  1.000 65.53966  ?  104 VAL B C   1 
ATOM   2508 O  O   . VAL B 1 104 ? 21.89200  4.27900   51.85500  1.000 66.47693  ?  104 VAL B O   1 
ATOM   2509 C  CB  . VAL B 1 104 ? 21.19400  6.27400   49.31000  1.000 66.23337  ?  104 VAL B CB  1 
ATOM   2510 C  CG1 . VAL B 1 104 ? 19.94900  5.45700   49.62300  1.000 63.36556  ?  104 VAL B CG1 1 
ATOM   2511 C  CG2 . VAL B 1 104 ? 20.82000  7.70700   48.96700  1.000 54.25988  ?  104 VAL B CG2 1 
ATOM   2512 N  N   . GLN B 1 105 ? 23.46900  4.18700   50.25600  1.000 63.79347  ?  105 GLN B N   1 
ATOM   2513 C  CA  . GLN B 1 105 ? 23.84900  2.83500   50.65200  1.000 71.95579  ?  105 GLN B CA  1 
ATOM   2514 C  C   . GLN B 1 105 ? 24.58100  2.83900   51.98700  1.000 70.19970  ?  105 GLN B C   1 
ATOM   2515 O  O   . GLN B 1 105 ? 24.37700  1.94500   52.81700  1.000 65.68970  ?  105 GLN B O   1 
ATOM   2516 C  CB  . GLN B 1 105 ? 24.71000  2.17400   49.57900  1.000 66.65567  ?  105 GLN B CB  1 
ATOM   2517 C  CG  . GLN B 1 105 ? 24.99100  0.71100   49.88500  1.000 73.84922  ?  105 GLN B CG  1 
ATOM   2518 C  CD  . GLN B 1 105 ? 26.03500  0.10100   48.97700  1.000 86.34133  ?  105 GLN B CD  1 
ATOM   2519 O  OE1 . GLN B 1 105 ? 27.22000  0.41800   49.07700  1.000 97.24360  ?  105 GLN B OE1 1 
ATOM   2520 N  NE2 . GLN B 1 105 ? 25.60200  -0.78500  48.08900  1.000 83.81255  ?  105 GLN B NE2 1 
ATOM   2521 N  N   . ALA B 1 106 ? 25.44100  3.83600   52.21000  1.000 66.25474  ?  106 ALA B N   1 
ATOM   2522 C  CA  . ALA B 1 106 ? 26.14200  3.93400   53.48500  1.000 69.74242  ?  106 ALA B CA  1 
ATOM   2523 C  C   . ALA B 1 106 ? 25.16100  4.16300   54.62600  1.000 73.53884  ?  106 ALA B C   1 
ATOM   2524 O  O   . ALA B 1 106 ? 25.37500  3.68500   55.74600  1.000 69.50243  ?  106 ALA B O   1 
ATOM   2525 C  CB  . ALA B 1 106 ? 27.18100  5.05300   53.43000  1.000 70.23716  ?  106 ALA B CB  1 
ATOM   2526 N  N   . ALA B 1 107 ? 24.08700  4.91100   54.36300  1.000 68.26273  ?  107 ALA B N   1 
ATOM   2527 C  CA  . ALA B 1 107 ? 23.04400  5.09100   55.36500  1.000 68.26569  ?  107 ALA B CA  1 
ATOM   2528 C  C   . ALA B 1 107 ? 22.47600  3.75200   55.82100  1.000 68.44470  ?  107 ALA B C   1 
ATOM   2529 O  O   . ALA B 1 107 ? 22.25000  3.53900   57.01700  1.000 70.24080  ?  107 ALA B O   1 
ATOM   2530 C  CB  . ALA B 1 107 ? 21.93500  5.98500   54.81100  1.000 61.02540  ?  107 ALA B CB  1 
ATOM   2531 N  N   . VAL B 1 108 ? 22.26300  2.82700   54.88400  1.000 64.76276  ?  108 VAL B N   1 
ATOM   2532 C  CA  . VAL B 1 108 ? 21.61300  1.56000   55.20900  1.000 68.27120  ?  108 VAL B CA  1 
ATOM   2533 C  C   . VAL B 1 108 ? 22.58000  0.61200   55.90700  1.000 69.64652  ?  108 VAL B C   1 
ATOM   2534 O  O   . VAL B 1 108 ? 22.24000  -0.01100  56.91900  1.000 81.97218  ?  108 VAL B O   1 
ATOM   2535 C  CB  . VAL B 1 108 ? 21.02600  0.92500   53.93500  1.000 71.59981  ?  108 VAL B CB  1 
ATOM   2536 C  CG1 . VAL B 1 108 ? 20.45100  -0.44700  54.24300  1.000 67.33993  ?  108 VAL B CG1 1 
ATOM   2537 C  CG2 . VAL B 1 108 ? 19.96700  1.82700   53.34100  1.000 68.43848  ?  108 VAL B CG2 1 
ATOM   2538 N  N   . GLU B 1 109 ? 23.80400  0.49500   55.38700  1.000 68.91551  ?  109 GLU B N   1 
ATOM   2539 C  CA  . GLU B 1 109 ? 24.76900  -0.44000  55.95400  1.000 72.27399  ?  109 GLU B CA  1 
ATOM   2540 C  C   . GLU B 1 109 ? 25.34800  0.05300   57.27500  1.000 72.52867  ?  109 GLU B C   1 
ATOM   2541 O  O   . GLU B 1 109 ? 25.93600  -0.74700  58.00900  1.000 75.85227  ?  109 GLU B O   1 
ATOM   2542 C  CB  . GLU B 1 109 ? 25.89500  -0.69100  54.94900  1.000 81.49830  ?  109 GLU B CB  1 
ATOM   2543 C  CG  . GLU B 1 109 ? 25.40700  -1.18900  53.59500  1.000 84.36425  ?  109 GLU B CG  1 
ATOM   2544 C  CD  . GLU B 1 109 ? 26.42800  -0.98200  52.49200  1.000 88.25547  ?  109 GLU B CD  1 
ATOM   2545 O  OE1 . GLU B 1 109 ? 27.24800  -0.04500  52.60900  1.000 93.57198  ?  109 GLU B OE1 1 
ATOM   2546 O  OE2 . GLU B 1 109 ? 26.41000  -1.75300  51.50800  1.000 85.47387  -1 109 GLU B OE2 1 
ATOM   2547 N  N   . ASN B 1 110 ? 25.19300  1.33900   57.57600  1.000 73.81508  ?  110 ASN B N   1 
ATOM   2548 C  CA  . ASN B 1 110 ? 25.63600  1.94100   58.82900  1.000 76.41284  ?  110 ASN B CA  1 
ATOM   2549 C  C   . ASN B 1 110 ? 27.05100  1.52800   59.25200  1.000 77.34007  ?  110 ASN B C   1 
ATOM   2550 O  O   . ASN B 1 110 ? 27.24500  0.97500   60.33700  1.000 79.71276  ?  110 ASN B O   1 
ATOM   2551 C  CB  . ASN B 1 110 ? 24.64100  1.63800   59.94200  1.000 77.19302  ?  110 ASN B CB  1 
ATOM   2552 C  CG  . ASN B 1 110 ? 24.78400  2.57300   61.12300  1.000 78.32969  ?  110 ASN B CG  1 
ATOM   2553 O  OD1 . ASN B 1 110 ? 25.65100  3.44600   61.13500  1.000 80.17888  ?  110 ASN B OD1 1 
ATOM   2554 N  ND2 . ASN B 1 110 ? 23.93200  2.39600   62.12600  1.000 83.08630  ?  110 ASN B ND2 1 
ATOM   2555 N  N   . PRO B 1 111 ? 28.05700  1.78600   58.42100  1.000 75.61726  ?  111 PRO B N   1 
ATOM   2556 C  CA  . PRO B 1 111 ? 29.44000  1.61300   58.86900  1.000 75.05557  ?  111 PRO B CA  1 
ATOM   2557 C  C   . PRO B 1 111 ? 29.90900  2.83500   59.64100  1.000 74.05258  ?  111 PRO B C   1 
ATOM   2558 O  O   . PRO B 1 111 ? 29.34100  3.92400   59.54800  1.000 74.64545  ?  111 PRO B O   1 
ATOM   2559 C  CB  . PRO B 1 111 ? 30.21900  1.44800   57.56100  1.000 73.67339  ?  111 PRO B CB  1 
ATOM   2560 C  CG  . PRO B 1 111 ? 29.43800  2.24200   56.57700  1.000 75.16234  ?  111 PRO B CG  1 
ATOM   2561 C  CD  . PRO B 1 111 ? 27.99800  2.23900   57.01800  1.000 75.31361  ?  111 PRO B CD  1 
ATOM   2562 N  N   . GLU B 1 112 ? 30.95100  2.62900   60.44100  1.000 73.29710  ?  112 GLU B N   1 
ATOM   2563 C  CA  . GLU B 1 112 ? 31.53400  3.72800   61.20700  1.000 80.44072  ?  112 GLU B CA  1 
ATOM   2564 C  C   . GLU B 1 112 ? 32.39300  4.55200   60.25700  1.000 79.38214  ?  112 GLU B C   1 
ATOM   2565 O  O   . GLU B 1 112 ? 33.56100  4.25200   60.00900  1.000 84.94390  ?  112 GLU B O   1 
ATOM   2566 C  CB  . GLU B 1 112 ? 32.33100  3.19800   62.39300  1.000 87.08573  ?  112 GLU B CB  1 
ATOM   2567 C  CG  . GLU B 1 112 ? 31.44800  2.65000   63.50500  1.000 89.65814  ?  112 GLU B CG  1 
ATOM   2568 C  CD  . GLU B 1 112 ? 32.23800  1.99000   64.61700  1.000 104.45528 ?  112 GLU B CD  1 
ATOM   2569 O  OE1 . GLU B 1 112 ? 33.35200  2.46500   64.91700  1.000 100.01301 ?  112 GLU B OE1 1 
ATOM   2570 O  OE2 . GLU B 1 112 ? 31.74300  0.99500   65.18900  1.000 107.74699 -1 112 GLU B OE2 1 
ATOM   2571 N  N   . LEU B 1 113 ? 31.78600  5.60600   59.70400  1.000 75.61859  ?  113 LEU B N   1 
ATOM   2572 C  CA  . LEU B 1 113 ? 32.43800  6.47100   58.73300  1.000 71.70935  ?  113 LEU B CA  1 
ATOM   2573 C  C   . LEU B 1 113 ? 32.87100  7.81000   59.30800  1.000 68.88382  ?  113 LEU B C   1 
ATOM   2574 O  O   . LEU B 1 113 ? 33.63100  8.52900   58.65000  1.000 66.21356  ?  113 LEU B O   1 
ATOM   2575 C  CB  . LEU B 1 113 ? 31.50500  6.72300   57.54000  1.000 74.55713  ?  113 LEU B CB  1 
ATOM   2576 C  CG  . LEU B 1 113 ? 30.90100  5.50000   56.86000  1.000 68.04022  ?  113 LEU B CG  1 
ATOM   2577 C  CD1 . LEU B 1 113 ? 29.93800  5.92200   55.76300  1.000 71.82138  ?  113 LEU B CD1 1 
ATOM   2578 C  CD2 . LEU B 1 113 ? 32.01200  4.63200   56.29700  1.000 72.00089  ?  113 LEU B CD2 1 
ATOM   2579 N  N   . GLY B 1 114 ? 32.42100  8.15700   60.51100  1.000 69.95151  ?  114 GLY B N   1 
ATOM   2580 C  CA  . GLY B 1 114 ? 32.78800  9.41500   61.12800  1.000 63.91377  ?  114 GLY B CA  1 
ATOM   2581 C  C   . GLY B 1 114 ? 31.68000  10.44900  61.12900  1.000 60.58448  ?  114 GLY B C   1 
ATOM   2582 O  O   . GLY B 1 114 ? 30.50500  10.10900  61.29800  1.000 63.09626  ?  114 GLY B O   1 
ATOM   2583 N  N   . LEU B 1 115 ? 32.05300  11.71800  60.93400  1.000 54.15218  ?  115 LEU B N   1 
ATOM   2584 C  CA  . LEU B 1 115 ? 31.10000  12.82100  61.03900  1.000 55.19942  ?  115 LEU B CA  1 
ATOM   2585 C  C   . LEU B 1 115 ? 29.91500  12.66000  60.09100  1.000 64.64815  ?  115 LEU B C   1 
ATOM   2586 O  O   . LEU B 1 115 ? 28.80700  13.11300  60.40500  1.000 61.55532  ?  115 LEU B O   1 
ATOM   2587 C  CB  . LEU B 1 115 ? 31.81500  14.14800  60.77900  1.000 53.52892  ?  115 LEU B CB  1 
ATOM   2588 C  CG  . LEU B 1 115 ? 30.97700  15.42900  60.77200  1.000 54.90001  ?  115 LEU B CG  1 
ATOM   2589 C  CD1 . LEU B 1 115 ? 30.31900  15.64700  62.12700  1.000 61.80903  ?  115 LEU B CD1 1 
ATOM   2590 C  CD2 . LEU B 1 115 ? 31.82900  16.63000  60.38500  1.000 57.79767  ?  115 LEU B CD2 1 
ATOM   2591 N  N   . ILE B 1 116 ? 30.12300  12.02100  58.93500  1.000 66.87081  ?  116 ILE B N   1 
ATOM   2592 C  CA  . ILE B 1 116 ? 29.07000  11.92600  57.92500  1.000 61.38790  ?  116 ILE B CA  1 
ATOM   2593 C  C   . ILE B 1 116 ? 27.88100  11.11200  58.42500  1.000 64.44534  ?  116 ILE B C   1 
ATOM   2594 O  O   . ILE B 1 116 ? 26.74900  11.31700  57.96700  1.000 64.23400  ?  116 ILE B O   1 
ATOM   2595 C  CB  . ILE B 1 116 ? 29.64600  11.34300  56.61700  1.000 63.34347  ?  116 ILE B CB  1 
ATOM   2596 C  CG1 . ILE B 1 116 ? 28.57500  11.28100  55.52400  1.000 60.26660  ?  116 ILE B CG1 1 
ATOM   2597 C  CG2 . ILE B 1 116 ? 30.22400  9.96400   56.86200  1.000 62.03965  ?  116 ILE B CG2 1 
ATOM   2598 C  CD1 . ILE B 1 116 ? 28.06200  12.63500  55.08700  1.000 54.62371  ?  116 ILE B CD1 1 
ATOM   2599 N  N   . ASN B 1 117 ? 28.10400  10.18800  59.36800  1.000 63.77142  ?  117 ASN B N   1 
ATOM   2600 C  CA  . ASN B 1 117 ? 27.01500  9.32800   59.82600  1.000 61.62972  ?  117 ASN B CA  1 
ATOM   2601 C  C   . ASN B 1 117 ? 25.84500  10.13500  60.37300  1.000 56.29210  ?  117 ASN B C   1 
ATOM   2602 O  O   . ASN B 1 117 ? 24.68700  9.73000   60.22100  1.000 55.12712  ?  117 ASN B O   1 
ATOM   2603 C  CB  . ASN B 1 117 ? 27.51600  8.34800   60.88700  1.000 55.12895  ?  117 ASN B CB  1 
ATOM   2604 C  CG  . ASN B 1 117 ? 28.22200  7.14900   60.29000  1.000 66.69868  ?  117 ASN B CG  1 
ATOM   2605 O  OD1 . ASN B 1 117 ? 28.71200  7.19700   59.16300  1.000 75.83307  ?  117 ASN B OD1 1 
ATOM   2606 N  ND2 . ASN B 1 117 ? 28.26600  6.05700   61.04200  1.000 69.74928  ?  117 ASN B ND2 1 
ATOM   2607 N  N   . ASN B 1 118 ? 26.12300  11.27800  61.00300  1.000 55.41953  ?  118 ASN B N   1 
ATOM   2608 C  CA  . ASN B 1 118 ? 25.04500  12.10700  61.53100  1.000 59.25785  ?  118 ASN B CA  1 
ATOM   2609 C  C   . ASN B 1 118 ? 24.18600  12.67100  60.40700  1.000 56.83634  ?  118 ASN B C   1 
ATOM   2610 O  O   . ASN B 1 118 ? 22.95700  12.73200  60.52800  1.000 57.30454  ?  118 ASN B O   1 
ATOM   2611 C  CB  . ASN B 1 118 ? 25.61900  13.23400  62.39200  1.000 63.73465  ?  118 ASN B CB  1 
ATOM   2612 C  CG  . ASN B 1 118 ? 26.47800  12.71900  63.53300  1.000 63.56951  ?  118 ASN B CG  1 
ATOM   2613 O  OD1 . ASN B 1 118 ? 25.97300  12.12700  64.48700  1.000 54.41703  ?  118 ASN B OD1 1 
ATOM   2614 N  ND2 . ASN B 1 118 ? 27.78500  12.94400  63.44000  1.000 65.56651  ?  118 ASN B ND2 1 
ATOM   2615 N  N   . TRP B 1 119 ? 24.81900  13.10400  59.31400  1.000 62.59056  ?  119 TRP B N   1 
ATOM   2616 C  CA  . TRP B 1 119 ? 24.07000  13.57300  58.15100  1.000 59.21620  ?  119 TRP B CA  1 
ATOM   2617 C  C   . TRP B 1 119 ? 23.19300  12.47000  57.56800  1.000 52.59086  ?  119 TRP B C   1 
ATOM   2618 O  O   . TRP B 1 119 ? 22.02100  12.70200  57.25000  1.000 48.42659  ?  119 TRP B O   1 
ATOM   2619 C  CB  . TRP B 1 119 ? 25.04200  14.09800  57.09400  1.000 54.96758  ?  119 TRP B CB  1 
ATOM   2620 C  CG  . TRP B 1 119 ? 24.39600  14.74600  55.90500  1.000 57.98530  ?  119 TRP B CG  1 
ATOM   2621 C  CD1 . TRP B 1 119 ? 24.05600  14.14700  54.72300  1.000 58.15481  ?  119 TRP B CD1 1 
ATOM   2622 C  CD2 . TRP B 1 119 ? 24.03600  16.12500  55.77000  1.000 54.46822  ?  119 TRP B CD2 1 
ATOM   2623 N  NE1 . TRP B 1 119 ? 23.50100  15.06800  53.86800  1.000 51.02687  ?  119 TRP B NE1 1 
ATOM   2624 C  CE2 . TRP B 1 119 ? 23.47500  16.28900  54.48800  1.000 57.39291  ?  119 TRP B CE2 1 
ATOM   2625 C  CE3 . TRP B 1 119 ? 24.13300  17.23800  56.61100  1.000 52.26922  ?  119 TRP B CE3 1 
ATOM   2626 C  CZ2 . TRP B 1 119 ? 23.01100  17.52000  54.02800  1.000 59.65323  ?  119 TRP B CZ2 1 
ATOM   2627 C  CZ3 . TRP B 1 119 ? 23.67000  18.45800  56.15400  1.000 58.19950  ?  119 TRP B CZ3 1 
ATOM   2628 C  CH2 . TRP B 1 119 ? 23.11600  18.59000  54.87500  1.000 62.37876  ?  119 TRP B CH2 1 
ATOM   2629 N  N   . LEU B 1 120 ? 23.72900  11.25200  57.46800  1.000 50.80137  ?  120 LEU B N   1 
ATOM   2630 C  CA  . LEU B 1 120 ? 23.00800  10.15000  56.84200  1.000 51.92077  ?  120 LEU B CA  1 
ATOM   2631 C  C   . LEU B 1 120 ? 21.84900  9.64300   57.68800  1.000 56.30814  ?  120 LEU B C   1 
ATOM   2632 O  O   . LEU B 1 120 ? 21.04400  8.84800   57.19000  1.000 56.72886  ?  120 LEU B O   1 
ATOM   2633 C  CB  . LEU B 1 120 ? 23.97600  9.00300   56.54400  1.000 56.38286  ?  120 LEU B CB  1 
ATOM   2634 C  CG  . LEU B 1 120 ? 25.16400  9.35000   55.64200  1.000 57.46221  ?  120 LEU B CG  1 
ATOM   2635 C  CD1 . LEU B 1 120 ? 26.06000  8.13900   55.42900  1.000 62.29461  ?  120 LEU B CD1 1 
ATOM   2636 C  CD2 . LEU B 1 120 ? 24.67000  9.88500   54.30800  1.000 47.94667  ?  120 LEU B CD2 1 
ATOM   2637 N  N   . LEU B 1 121 ? 21.75000  10.07800  58.94700  1.000 61.39147  ?  121 LEU B N   1 
ATOM   2638 C  CA  . LEU B 1 121 ? 20.63600  9.66500   59.79400  1.000 56.39175  ?  121 LEU B CA  1 
ATOM   2639 C  C   . LEU B 1 121 ? 19.30100  10.18200  59.26900  1.000 60.42540  ?  121 LEU B C   1 
ATOM   2640 O  O   . LEU B 1 121 ? 18.25900  9.56500   59.52200  1.000 57.06708  ?  121 LEU B O   1 
ATOM   2641 C  CB  . LEU B 1 121 ? 20.87200  10.14800  61.22500  1.000 56.90346  ?  121 LEU B CB  1 
ATOM   2642 C  CG  . LEU B 1 121 ? 21.85800  9.33900   62.07000  1.000 57.22297  ?  121 LEU B CG  1 
ATOM   2643 C  CD1 . LEU B 1 121 ? 22.17200  10.06600  63.36300  1.000 60.33060  ?  121 LEU B CD1 1 
ATOM   2644 C  CD2 . LEU B 1 121 ? 21.29300  7.95700   62.36000  1.000 51.71639  ?  121 LEU B CD2 1 
ATOM   2645 N  N   . HIS B 1 122 ? 19.30700  11.30400  58.53900  1.000 59.37853  ?  122 HIS B N   1 
ATOM   2646 C  CA  . HIS B 1 122 ? 18.07300  11.78400  57.92300  1.000 52.04216  ?  122 HIS B CA  1 
ATOM   2647 C  C   . HIS B 1 122 ? 17.55900  10.81700  56.86500  1.000 58.60665  ?  122 HIS B C   1 
ATOM   2648 O  O   . HIS B 1 122 ? 16.34500  10.71000  56.66100  1.000 59.40592  ?  122 HIS B O   1 
ATOM   2649 C  CB  . HIS B 1 122 ? 18.28400  13.16500  57.30400  1.000 49.81305  ?  122 HIS B CB  1 
ATOM   2650 C  CG  . HIS B 1 122 ? 18.51300  14.25200  58.30600  1.000 53.48505  ?  122 HIS B CG  1 
ATOM   2651 N  ND1 . HIS B 1 122 ? 17.48400  14.86000  58.99200  1.000 56.77333  ?  122 HIS B ND1 1 
ATOM   2652 C  CD2 . HIS B 1 122 ? 19.65200  14.84900  58.72900  1.000 55.50806  ?  122 HIS B CD2 1 
ATOM   2653 C  CE1 . HIS B 1 122 ? 17.97900  15.78200  59.79800  1.000 58.82745  ?  122 HIS B CE1 1 
ATOM   2654 N  NE2 . HIS B 1 122 ? 19.29200  15.79700  59.65700  1.000 58.44043  ?  122 HIS B NE2 1 
ATOM   2655 N  N   . ILE B 1 123 ? 18.46400  10.10900  56.18900  1.000 55.54918  ?  123 ILE B N   1 
ATOM   2656 C  CA  . ILE B 1 123 ? 18.06000  9.09700   55.22000  1.000 53.97447  ?  123 ILE B CA  1 
ATOM   2657 C  C   . ILE B 1 123 ? 17.59800  7.83200   55.92600  1.000 56.46338  ?  123 ILE B C   1 
ATOM   2658 O  O   . ILE B 1 123 ? 16.60400  7.21300   55.52700  1.000 55.24882  ?  123 ILE B O   1 
ATOM   2659 C  CB  . ILE B 1 123 ? 19.21800  8.81800   54.24800  1.000 54.48051  ?  123 ILE B CB  1 
ATOM   2660 C  CG1 . ILE B 1 123 ? 19.65100  10.11600  53.56900  1.000 50.90330  ?  123 ILE B CG1 1 
ATOM   2661 C  CG2 . ILE B 1 123 ? 18.81600  7.77200   53.21900  1.000 52.06700  ?  123 ILE B CG2 1 
ATOM   2662 C  CD1 . ILE B 1 123 ? 21.04600  10.05900  53.03800  1.000 52.97576  ?  123 ILE B CD1 1 
ATOM   2663 N  N   . ARG B 1 124 ? 18.32100  7.41800   56.97300  1.000 55.09148  ?  124 ARG B N   1 
ATOM   2664 C  CA  . ARG B 1 124 ? 17.89400  6.27000   57.76800  1.000 51.94371  ?  124 ARG B CA  1 
ATOM   2665 C  C   . ARG B 1 124 ? 16.51500  6.48200   58.37400  1.000 53.62231  ?  124 ARG B C   1 
ATOM   2666 O  O   . ARG B 1 124 ? 15.74700  5.52300   58.51300  1.000 51.73711  ?  124 ARG B O   1 
ATOM   2667 C  CB  . ARG B 1 124 ? 18.90400  5.99100   58.87700  1.000 55.83675  ?  124 ARG B CB  1 
ATOM   2668 C  CG  . ARG B 1 124 ? 20.22600  5.43100   58.41300  1.000 58.75712  ?  124 ARG B CG  1 
ATOM   2669 C  CD  . ARG B 1 124 ? 21.09700  5.09200   59.61600  1.000 71.48242  ?  124 ARG B CD  1 
ATOM   2670 N  NE  . ARG B 1 124 ? 20.47900  4.10300   60.49200  1.000 64.95286  ?  124 ARG B NE  1 
ATOM   2671 C  CZ  . ARG B 1 124 ? 20.66700  2.79300   60.40600  1.000 66.26132  ?  124 ARG B CZ  1 
ATOM   2672 N  NH1 . ARG B 1 124 ? 21.45000  2.26600   59.47900  1.000 71.78463  ?  124 ARG B NH1 1 
ATOM   2673 N  NH2 . ARG B 1 124 ? 20.05600  1.99200   61.27400  1.000 56.12424  ?  124 ARG B NH2 1 
ATOM   2674 N  N   . ASP B 1 125 ? 16.18200  7.72300   58.74000  1.000 54.04846  ?  125 ASP B N   1 
ATOM   2675 C  CA  . ASP B 1 125 ? 14.82400  8.01600   59.18800  1.000 54.64619  ?  125 ASP B CA  1 
ATOM   2676 C  C   . ASP B 1 125 ? 13.81000  7.65200   58.11400  1.000 57.77848  ?  125 ASP B C   1 
ATOM   2677 O  O   . ASP B 1 125 ? 12.71500  7.16700   58.41800  1.000 53.76395  ?  125 ASP B O   1 
ATOM   2678 C  CB  . ASP B 1 125 ? 14.69900  9.49300   59.56500  1.000 59.10037  ?  125 ASP B CB  1 
ATOM   2679 C  CG  . ASP B 1 125 ? 15.41300  9.83000   60.86000  1.000 73.17616  ?  125 ASP B CG  1 
ATOM   2680 O  OD1 . ASP B 1 125 ? 15.84000  8.89400   61.57100  1.000 75.28151  ?  125 ASP B OD1 1 
ATOM   2681 O  OD2 . ASP B 1 125 ? 15.54300  11.03600  61.16800  1.000 68.46011  -1 125 ASP B OD2 1 
ATOM   2682 N  N   . ILE B 1 126 ? 14.16800  7.87000   56.84800  1.000 61.49163  ?  126 ILE B N   1 
ATOM   2683 C  CA  . ILE B 1 126 ? 13.27300  7.51800   55.75200  1.000 52.53345  ?  126 ILE B CA  1 
ATOM   2684 C  C   . ILE B 1 126 ? 13.22000  6.00500   55.57400  1.000 54.01355  ?  126 ILE B C   1 
ATOM   2685 O  O   . ILE B 1 126 ? 12.16600  5.44000   55.26000  1.000 57.80541  ?  126 ILE B O   1 
ATOM   2686 C  CB  . ILE B 1 126 ? 13.71400  8.23200   54.46200  1.000 52.72242  ?  126 ILE B CB  1 
ATOM   2687 C  CG1 . ILE B 1 126 ? 13.90300  9.72800   54.72600  1.000 55.24221  ?  126 ILE B CG1 1 
ATOM   2688 C  CG2 . ILE B 1 126 ? 12.70500  8.00300   53.34900  1.000 62.49354  ?  126 ILE B CG2 1 
ATOM   2689 C  CD1 . ILE B 1 126 ? 12.69700  10.40300  55.35100  1.000 60.87498  ?  126 ILE B CD1 1 
ATOM   2690 N  N   . TRP B 1 127 ? 14.35400  5.32800   55.77600  1.000 54.61447  ?  127 TRP B N   1 
ATOM   2691 C  CA  . TRP B 1 127 ? 14.39700  3.86900   55.71200  1.000 54.29922  ?  127 TRP B CA  1 
ATOM   2692 C  C   . TRP B 1 127 ? 13.39000  3.22300   56.65400  1.000 60.71321  ?  127 TRP B C   1 
ATOM   2693 O  O   . TRP B 1 127 ? 12.63300  2.32900   56.25600  1.000 57.38988  ?  127 TRP B O   1 
ATOM   2694 C  CB  . TRP B 1 127 ? 15.81300  3.39300   56.03900  1.000 60.26228  ?  127 TRP B CB  1 
ATOM   2695 C  CG  . TRP B 1 127 ? 15.97000  1.90700   56.06100  1.000 66.31000  ?  127 TRP B CG  1 
ATOM   2696 C  CD1 . TRP B 1 127 ? 16.10900  1.12600   57.17100  1.000 64.09834  ?  127 TRP B CD1 1 
ATOM   2697 C  CD2 . TRP B 1 127 ? 15.98400  1.01600   54.93900  1.000 72.39451  ?  127 TRP B CD2 1 
ATOM   2698 N  NE1 . TRP B 1 127 ? 16.22000  -0.19400  56.81200  1.000 71.13297  ?  127 TRP B NE1 1 
ATOM   2699 C  CE2 . TRP B 1 127 ? 16.14600  -0.28900  55.44700  1.000 72.80317  ?  127 TRP B CE2 1 
ATOM   2700 C  CE3 . TRP B 1 127 ? 15.88100  1.19400   53.55700  1.000 68.93806  ?  127 TRP B CE3 1 
ATOM   2701 C  CZ2 . TRP B 1 127 ? 16.20600  -1.41000  54.62200  1.000 72.24802  ?  127 TRP B CZ2 1 
ATOM   2702 C  CZ3 . TRP B 1 127 ? 15.93900  0.07900   52.73900  1.000 69.92712  ?  127 TRP B CZ3 1 
ATOM   2703 C  CH2 . TRP B 1 127 ? 16.10100  -1.20600  53.27500  1.000 65.84924  ?  127 TRP B CH2 1 
ATOM   2704 N  N   . PHE B 1 128 ? 13.35300  3.67600   57.90600  1.000 60.42661  ?  128 PHE B N   1 
ATOM   2705 C  CA  . PHE B 1 128 ? 12.43700  3.08600   58.87400  1.000 55.18740  ?  128 PHE B CA  1 
ATOM   2706 C  C   . PHE B 1 128 ? 11.02200  3.62500   58.72400  1.000 53.76358  ?  128 PHE B C   1 
ATOM   2707 O  O   . PHE B 1 128 ? 10.05800  2.90800   59.02100  1.000 56.02167  ?  128 PHE B O   1 
ATOM   2708 C  CB  . PHE B 1 128 ? 12.95800  3.31300   60.29200  1.000 59.96547  ?  128 PHE B CB  1 
ATOM   2709 C  CG  . PHE B 1 128 ? 14.29500  2.67500   60.55100  1.000 56.86672  ?  128 PHE B CG  1 
ATOM   2710 C  CD1 . PHE B 1 128 ? 14.44400  1.29900   60.48200  1.000 57.16548  ?  128 PHE B CD1 1 
ATOM   2711 C  CD2 . PHE B 1 128 ? 15.40100  3.44800   60.85900  1.000 58.58011  ?  128 PHE B CD2 1 
ATOM   2712 C  CE1 . PHE B 1 128 ? 15.67200  0.70600   60.72000  1.000 59.11012  ?  128 PHE B CE1 1 
ATOM   2713 C  CE2 . PHE B 1 128 ? 16.63000  2.86300   61.09500  1.000 57.80257  ?  128 PHE B CE2 1 
ATOM   2714 C  CZ  . PHE B 1 128 ? 16.76600  1.49100   61.02500  1.000 57.32197  ?  128 PHE B CZ  1 
ATOM   2715 N  N   . LYS B 1 129 ? 10.88100  4.87800   58.28300  1.000 50.89244  ?  129 LYS B N   1 
ATOM   2716 C  CA  . LYS B 1 129 ? 9.55600   5.44700   58.05700  1.000 45.65749  ?  129 LYS B CA  1 
ATOM   2717 C  C   . LYS B 1 129 ? 8.74800   4.58200   57.09900  1.000 50.69455  ?  129 LYS B C   1 
ATOM   2718 O  O   . LYS B 1 129 ? 7.54800   4.36600   57.30500  1.000 52.49921  ?  129 LYS B O   1 
ATOM   2719 C  CB  . LYS B 1 129 ? 9.69000   6.87600   57.53000  1.000 46.78569  ?  129 LYS B CB  1 
ATOM   2720 C  CG  . LYS B 1 129 ? 8.39500   7.55000   57.10500  1.000 46.72290  ?  129 LYS B CG  1 
ATOM   2721 C  CD  . LYS B 1 129 ? 8.68000   8.97200   56.64100  1.000 48.12399  ?  129 LYS B CD  1 
ATOM   2722 C  CE  . LYS B 1 129 ? 7.40900   9.72900   56.30100  1.000 50.89515  ?  129 LYS B CE  1 
ATOM   2723 N  NZ  . LYS B 1 129 ? 7.70300   11.15500  55.97700  1.000 57.03403  ?  129 LYS B NZ  1 
ATOM   2724 N  N   . HIS B 1 130 ? 9.39200   4.07100   56.05100  1.000 60.03980  ?  130 HIS B N   1 
ATOM   2725 C  CA  . HIS B 1 130 ? 8.75900   3.19300   55.07700  1.000 60.36075  ?  130 HIS B CA  1 
ATOM   2726 C  C   . HIS B 1 130 ? 9.19600   1.74300   55.26600  1.000 66.80594  ?  130 HIS B C   1 
ATOM   2727 O  O   . HIS B 1 130 ? 9.32900   0.99800   54.29300  1.000 71.26731  ?  130 HIS B O   1 
ATOM   2728 C  CB  . HIS B 1 130 ? 9.06400   3.66200   53.65500  1.000 50.34912  ?  130 HIS B CB  1 
ATOM   2729 C  CG  . HIS B 1 130 ? 8.72700   5.10000   53.41500  1.000 47.62488  ?  130 HIS B CG  1 
ATOM   2730 N  ND1 . HIS B 1 130 ? 7.44000   5.53900   53.19000  1.000 48.27050  ?  130 HIS B ND1 1 
ATOM   2731 C  CD2 . HIS B 1 130 ? 9.51300   6.20200   53.37300  1.000 47.02744  ?  130 HIS B CD2 1 
ATOM   2732 C  CE1 . HIS B 1 130 ? 7.44800   6.84900   53.02200  1.000 51.35181  ?  130 HIS B CE1 1 
ATOM   2733 N  NE2 . HIS B 1 130 ? 8.69300   7.27600   53.12700  1.000 49.29015  ?  130 HIS B NE2 1 
ATOM   2734 N  N   . SER B 1 131 ? 9.44800   1.34400   56.51700  1.000 67.00002  ?  131 SER B N   1 
ATOM   2735 C  CA  . SER B 1 131 ? 9.84300   -0.03300  56.79600  1.000 66.92403  ?  131 SER B CA  1 
ATOM   2736 C  C   . SER B 1 131 ? 8.81800   -1.02700  56.26500  1.000 71.90663  ?  131 SER B C   1 
ATOM   2737 O  O   . SER B 1 131 ? 9.17800   -2.11800  55.80900  1.000 73.87366  ?  131 SER B O   1 
ATOM   2738 C  CB  . SER B 1 131 ? 10.03200  -0.21600  58.30300  1.000 69.33289  ?  131 SER B CB  1 
ATOM   2739 O  OG  . SER B 1 131 ? 10.13800  -1.58500  58.65300  1.000 77.19810  ?  131 SER B OG  1 
ATOM   2740 N  N   . SER B 1 132 ? 7.53500   -0.66300  56.30800  1.000 77.20551  ?  132 SER B N   1 
ATOM   2741 C  CA  . SER B 1 132 ? 6.49000   -1.54100  55.79300  1.000 78.68450  ?  132 SER B CA  1 
ATOM   2742 C  C   . SER B 1 132 ? 6.55300   -1.65500  54.27200  1.000 83.29518  ?  132 SER B C   1 
ATOM   2743 O  O   . SER B 1 132 ? 6.59400   -2.76400  53.72500  1.000 83.73349  ?  132 SER B O   1 
ATOM   2744 C  CB  . SER B 1 132 ? 5.11900   -1.03900  56.24600  1.000 90.54689  ?  132 SER B CB  1 
ATOM   2745 O  OG  . SER B 1 132 ? 4.07700   -1.76600  55.62000  1.000 98.65762  ?  132 SER B OG  1 
ATOM   2746 N  N   . LEU B 1 133 ? 6.54500   -0.51300  53.57500  1.000 83.64117  ?  133 LEU B N   1 
ATOM   2747 C  CA  . LEU B 1 133 ? 6.55100   -0.49800  52.11200  1.000 75.57580  ?  133 LEU B CA  1 
ATOM   2748 C  C   . LEU B 1 133 ? 7.70900   -1.31700  51.54900  1.000 73.57098  ?  133 LEU B C   1 
ATOM   2749 O  O   . LEU B 1 133 ? 7.50900   -2.21800  50.72700  1.000 84.96088  ?  133 LEU B O   1 
ATOM   2750 C  CB  . LEU B 1 133 ? 6.60200   0.94900   51.60600  1.000 71.79828  ?  133 LEU B CB  1 
ATOM   2751 C  CG  . LEU B 1 133 ? 6.70700   1.20900   50.10000  1.000 70.90280  ?  133 LEU B CG  1 
ATOM   2752 C  CD1 . LEU B 1 133 ? 5.87800   2.42800   49.72500  1.000 71.35591  ?  133 LEU B CD1 1 
ATOM   2753 C  CD2 . LEU B 1 133 ? 8.15100   1.40700   49.65700  1.000 71.12215  ?  133 LEU B CD2 1 
ATOM   2754 N  N   . LEU B 1 134 ? 8.93600   -1.00100  51.97400  1.000 68.93449  ?  134 LEU B N   1 
ATOM   2755 C  CA  . LEU B 1 134 ? 10.10400  -1.73500  51.49500  1.000 72.32395  ?  134 LEU B CA  1 
ATOM   2756 C  C   . LEU B 1 134 ? 10.01500  -3.21400  51.84900  1.000 80.37455  ?  134 LEU B C   1 
ATOM   2757 O  O   . LEU B 1 134 ? 10.62000  -4.05300  51.17000  1.000 78.39963  ?  134 LEU B O   1 
ATOM   2758 C  CB  . LEU B 1 134 ? 11.38200  -1.11700  52.06000  1.000 71.86325  ?  134 LEU B CB  1 
ATOM   2759 C  CG  . LEU B 1 134 ? 11.57200  0.36900   51.75400  1.000 69.34645  ?  134 LEU B CG  1 
ATOM   2760 C  CD1 . LEU B 1 134 ? 12.45600  1.02800   52.79600  1.000 64.26114  ?  134 LEU B CD1 1 
ATOM   2761 C  CD2 . LEU B 1 134 ? 12.15600  0.55500   50.36200  1.000 65.54924  ?  134 LEU B CD2 1 
ATOM   2762 N  N   . GLY B 1 135 ? 9.27600   -3.54800  52.91000  1.000 79.44158  ?  135 GLY B N   1 
ATOM   2763 C  CA  . GLY B 1 135 ? 9.10300   -4.94500  53.27400  1.000 75.30068  ?  135 GLY B CA  1 
ATOM   2764 C  C   . GLY B 1 135 ? 8.38600   -5.74100  52.19800  1.000 87.22946  ?  135 GLY B C   1 
ATOM   2765 O  O   . GLY B 1 135 ? 8.68000   -6.92000  51.98800  1.000 92.56758  ?  135 GLY B O   1 
ATOM   2766 N  N   . GLU B 1 136 ? 7.42900   -5.11300  51.50800  1.000 89.40859  ?  136 GLU B N   1 
ATOM   2767 C  CA  . GLU B 1 136 ? 6.68600   -5.80900  50.46200  1.000 88.42134  ?  136 GLU B CA  1 
ATOM   2768 C  C   . GLU B 1 136 ? 7.54100   -6.07900  49.23200  1.000 93.67390  ?  136 GLU B C   1 
ATOM   2769 O  O   . GLU B 1 136 ? 7.15200   -6.89600  48.38900  1.000 103.72690 ?  136 GLU B O   1 
ATOM   2770 C  CB  . GLU B 1 136 ? 5.44400   -4.99000  50.06300  1.000 95.15948  ?  136 GLU B CB  1 
ATOM   2771 C  CG  . GLU B 1 136 ? 4.55700   -5.62100  48.98300  1.000 109.88900 ?  136 GLU B CG  1 
ATOM   2772 C  CD  . GLU B 1 136 ? 3.45800   -4.69300  48.48600  1.000 116.10000 ?  136 GLU B CD  1 
ATOM   2773 O  OE1 . GLU B 1 136 ? 3.28700   -3.59900  49.06200  1.000 101.60437 ?  136 GLU B OE1 1 
ATOM   2774 O  OE2 . GLU B 1 136 ? 2.77100   -5.05400  47.50600  1.000 120.53573 -1 136 GLU B OE2 1 
ATOM   2775 N  N   . MET B 1 137 ? 8.70600   -5.45100  49.12300  1.000 86.86694  ?  137 MET B N   1 
ATOM   2776 C  CA  . MET B 1 137 ? 9.52300   -5.59400  47.93300  1.000 89.67687  ?  137 MET B CA  1 
ATOM   2777 C  C   . MET B 1 137 ? 10.69000  -6.54000  48.16400  1.000 87.20199  ?  137 MET B C   1 
ATOM   2778 O  O   . MET B 1 137 ? 11.14700  -6.73100  49.29500  1.000 84.19812  ?  137 MET B O   1 
ATOM   2779 C  CB  . MET B 1 137 ? 10.05600  -4.22800  47.49800  1.000 80.08351  ?  137 MET B CB  1 
ATOM   2780 C  CG  . MET B 1 137 ? 8.98600   -3.20700  47.16400  1.000 81.58836  ?  137 MET B CG  1 
ATOM   2781 S  SD  . MET B 1 137 ? 9.75400   -1.63800  46.73000  1.000 94.03262  ?  137 MET B SD  1 
ATOM   2782 C  CE  . MET B 1 137 ? 11.27500  -1.76800  47.66900  1.000 75.49767  ?  137 MET B CE  1 
ATOM   2783 N  N   . PRO B 1 138 ? 11.19600  -7.15700  47.09500  1.000 82.40057  ?  138 PRO B N   1 
ATOM   2784 C  CA  . PRO B 1 138 ? 12.39900  -7.98800  47.21800  1.000 82.61551  ?  138 PRO B CA  1 
ATOM   2785 C  C   . PRO B 1 138 ? 13.63300  -7.16100  47.55600  1.000 82.91662  ?  138 PRO B C   1 
ATOM   2786 O  O   . PRO B 1 138 ? 13.78600  -6.02200  47.10700  1.000 82.98953  ?  138 PRO B O   1 
ATOM   2787 C  CB  . PRO B 1 138 ? 12.51900  -8.64200  45.83600  1.000 89.72278  ?  138 PRO B CB  1 
ATOM   2788 C  CG  . PRO B 1 138 ? 11.12500  -8.62000  45.28800  1.000 88.68932  ?  138 PRO B CG  1 
ATOM   2789 C  CD  . PRO B 1 138 ? 10.51800  -7.35000  45.80100  1.000 85.45581  ?  138 PRO B CD  1 
ATOM   2790 N  N   . GLN B 1 139 ? 14.51100  -7.76300  48.36600  1.000 87.28970  ?  139 GLN B N   1 
ATOM   2791 C  CA  . GLN B 1 139 ? 15.68900  -7.08600  48.91000  1.000 90.65221  ?  139 GLN B CA  1 
ATOM   2792 C  C   . GLN B 1 139 ? 16.48100  -6.32000  47.85700  1.000 92.09995  ?  139 GLN B C   1 
ATOM   2793 O  O   . GLN B 1 139 ? 16.89200  -5.17700  48.08400  1.000 94.97346  ?  139 GLN B O   1 
ATOM   2794 C  CB  . GLN B 1 139 ? 16.58300  -8.12000  49.60000  1.000 94.10880  ?  139 GLN B CB  1 
ATOM   2795 C  CG  . GLN B 1 139 ? 17.81400  -7.56600  50.30500  1.000 94.57244  ?  139 GLN B CG  1 
ATOM   2796 C  CD  . GLN B 1 139 ? 18.96600  -7.32900  49.33500  1.000 106.56181 ?  139 GLN B CD  1 
ATOM   2797 O  OE1 . GLN B 1 139 ? 19.22300  -8.15200  48.45500  1.000 104.24427 ?  139 GLN B OE1 1 
ATOM   2798 N  NE2 . GLN B 1 139 ? 19.65000  -6.20000  49.48200  1.000 106.61528 ?  139 GLN B NE2 1 
ATOM   2799 N  N   . GLU B 1 140 ? 16.72000  -6.94300  46.70500  1.000 94.96723  ?  140 GLU B N   1 
ATOM   2800 C  CA  . GLU B 1 140 ? 17.57500  -6.33000  45.69400  1.000 97.58852  ?  140 GLU B CA  1 
ATOM   2801 C  C   . GLU B 1 140 ? 17.04400  -4.97100  45.25200  1.000 92.48701  ?  140 GLU B C   1 
ATOM   2802 O  O   . GLU B 1 140 ? 17.82600  -4.05400  44.97300  1.000 90.69628  ?  140 GLU B O   1 
ATOM   2803 C  CB  . GLU B 1 140 ? 17.70100  -7.27100  44.50200  1.000 96.31917  ?  140 GLU B CB  1 
ATOM   2804 C  CG  . GLU B 1 140 ? 16.41300  -8.01500  44.17300  1.000 104.13366 ?  140 GLU B CG  1 
ATOM   2805 C  CD  . GLU B 1 140 ? 16.26000  -9.32500  44.92900  1.000 104.87979 ?  140 GLU B CD  1 
ATOM   2806 O  OE1 . GLU B 1 140 ? 16.76600  -9.42700  46.06900  1.000 102.38531 ?  140 GLU B OE1 1 
ATOM   2807 O  OE2 . GLU B 1 140 ? 15.63900  -10.25600 44.37000  1.000 112.13916 -1 140 GLU B OE2 1 
ATOM   2808 N  N   . ARG B 1 141 ? 15.72200  -4.82100  45.18200  1.000 90.24930  ?  141 ARG B N   1 
ATOM   2809 C  CA  . ARG B 1 141 ? 15.09900  -3.59900  44.69500  1.000 90.44315  ?  141 ARG B CA  1 
ATOM   2810 C  C   . ARG B 1 141 ? 14.79000  -2.60400  45.80500  1.000 85.62280  ?  141 ARG B C   1 
ATOM   2811 O  O   . ARG B 1 141 ? 13.99500  -1.68300  45.59300  1.000 81.81332  ?  141 ARG B O   1 
ATOM   2812 C  CB  . ARG B 1 141 ? 13.82100  -3.93200  43.92900  1.000 94.11026  ?  141 ARG B CB  1 
ATOM   2813 C  CG  . ARG B 1 141 ? 14.04600  -4.80600  42.71700  1.000 100.90663 ?  141 ARG B CG  1 
ATOM   2814 C  CD  . ARG B 1 141 ? 14.04500  -3.97900  41.44300  1.000 103.79418 ?  141 ARG B CD  1 
ATOM   2815 N  NE  . ARG B 1 141 ? 13.06700  -2.90000  41.51300  1.000 110.30714 ?  141 ARG B NE  1 
ATOM   2816 C  CZ  . ARG B 1 141 ? 11.76900  -3.05100  41.29000  1.000 115.09530 ?  141 ARG B CZ  1 
ATOM   2817 N  NH1 . ARG B 1 141 ? 11.25100  -4.23400  41.00600  1.000 113.69367 ?  141 ARG B NH1 1 
ATOM   2818 N  NH2 . ARG B 1 141 ? 10.97100  -1.98900  41.36200  1.000 117.60434 ?  141 ARG B NH2 1 
ATOM   2819 N  N   . ARG B 1 142 ? 15.41700  -2.75000  46.97100  1.000 80.46577  ?  142 ARG B N   1 
ATOM   2820 C  CA  . ARG B 1 142 ? 15.13400  -1.87500  48.10100  1.000 76.73288  ?  142 ARG B CA  1 
ATOM   2821 C  C   . ARG B 1 142 ? 16.04100  -0.65500  48.11100  1.000 74.02242  ?  142 ARG B C   1 
ATOM   2822 O  O   . ARG B 1 142 ? 15.58100  0.45800   48.38700  1.000 68.75704  ?  142 ARG B O   1 
ATOM   2823 C  CB  . ARG B 1 142 ? 15.27900  -2.64500  49.41500  1.000 75.35665  ?  142 ARG B CB  1 
ATOM   2824 C  CG  . ARG B 1 142 ? 14.05000  -3.44600  49.80700  1.000 77.55290  ?  142 ARG B CG  1 
ATOM   2825 C  CD  . ARG B 1 142 ? 14.37400  -4.42400  50.92100  1.000 72.42502  ?  142 ARG B CD  1 
ATOM   2826 N  NE  . ARG B 1 142 ? 13.27300  -5.34700  51.17100  1.000 79.26030  ?  142 ARG B NE  1 
ATOM   2827 C  CZ  . ARG B 1 142 ? 13.38700  -6.48500  51.84300  1.000 82.32473  ?  142 ARG B CZ  1 
ATOM   2828 N  NH1 . ARG B 1 142 ? 14.54300  -6.87300  52.35500  1.000 77.37118  ?  142 ARG B NH1 1 
ATOM   2829 N  NH2 . ARG B 1 142 ? 12.31100  -7.24900  52.01000  1.000 78.69460  ?  142 ARG B NH2 1 
ATOM   2830 N  N   . LEU B 1 143 ? 17.33200  -0.85400  47.83900  1.000 72.48762  ?  143 LEU B N   1 
ATOM   2831 C  CA  . LEU B 1 143 ? 18.27000  0.26100   47.83400  1.000 66.82716  ?  143 LEU B CA  1 
ATOM   2832 C  C   . LEU B 1 143 ? 17.93300  1.27300   46.74600  1.000 68.61762  ?  143 LEU B C   1 
ATOM   2833 O  O   . LEU B 1 143 ? 18.14400  2.47700   46.93300  1.000 66.92273  ?  143 LEU B O   1 
ATOM   2834 C  CB  . LEU B 1 143 ? 19.69100  -0.26400  47.65400  1.000 63.57807  ?  143 LEU B CB  1 
ATOM   2835 C  CG  . LEU B 1 143 ? 20.81700  0.71700   47.96700  1.000 76.43965  ?  143 LEU B CG  1 
ATOM   2836 C  CD1 . LEU B 1 143 ? 20.66300  1.26700   49.37900  1.000 72.99073  ?  143 LEU B CD1 1 
ATOM   2837 C  CD2 . LEU B 1 143 ? 22.16000  0.03500   47.79500  1.000 77.74683  ?  143 LEU B CD2 1 
ATOM   2838 N  N   . ASP B 1 144 ? 17.42400  0.80900   45.60200  1.000 75.15845  ?  144 ASP B N   1 
ATOM   2839 C  CA  . ASP B 1 144 ? 16.98500  1.73500   44.56200  1.000 69.74664  ?  144 ASP B CA  1 
ATOM   2840 C  C   . ASP B 1 144 ? 15.70300  2.45500   44.96500  1.000 63.53952  ?  144 ASP B C   1 
ATOM   2841 O  O   . ASP B 1 144 ? 15.52900  3.64000   44.66000  1.000 63.16139  ?  144 ASP B O   1 
ATOM   2842 C  CB  . ASP B 1 144 ? 16.78100  0.99000   43.24200  1.000 73.81741  ?  144 ASP B CB  1 
ATOM   2843 C  CG  . ASP B 1 144 ? 18.08700  0.66900   42.54400  1.000 84.69865  ?  144 ASP B CG  1 
ATOM   2844 O  OD1 . ASP B 1 144 ? 19.15500  0.83900   43.16900  1.000 83.29515  ?  144 ASP B OD1 1 
ATOM   2845 O  OD2 . ASP B 1 144 ? 18.04100  0.24900   41.36700  1.000 82.03418  -1 144 ASP B OD2 1 
ATOM   2846 N  N   . THR B 1 145 ? 14.79500  1.75500   45.64900  1.000 61.47488  ?  145 THR B N   1 
ATOM   2847 C  CA  . THR B 1 145 ? 13.52800  2.36500   46.04400  1.000 63.91917  ?  145 THR B CA  1 
ATOM   2848 C  C   . THR B 1 145 ? 13.73000  3.42900   47.11400  1.000 60.57213  ?  145 THR B C   1 
ATOM   2849 O  O   . THR B 1 145 ? 13.12400  4.50500   47.04700  1.000 55.18720  ?  145 THR B O   1 
ATOM   2850 C  CB  . THR B 1 145 ? 12.55800  1.29300   46.53100  1.000 67.56517  ?  145 THR B CB  1 
ATOM   2851 O  OG1 . THR B 1 145 ? 12.44900  0.26300   45.54000  1.000 77.04717  ?  145 THR B OG1 1 
ATOM   2852 C  CG2 . THR B 1 145 ? 11.18300  1.89200   46.79600  1.000 60.36903  ?  145 THR B CG2 1 
ATOM   2853 N  N   . LEU B 1 146 ? 14.55600  3.13800   48.12200  1.000 59.95706  ?  146 LEU B N   1 
ATOM   2854 C  CA  . LEU B 1 146 ? 14.89400  4.15300   49.11500  1.000 60.23057  ?  146 LEU B CA  1 
ATOM   2855 C  C   . LEU B 1 146 ? 15.43800  5.41000   48.45100  1.000 59.03353  ?  146 LEU B C   1 
ATOM   2856 O  O   . LEU B 1 146 ? 15.11800  6.53000   48.86500  1.000 61.27777  ?  146 LEU B O   1 
ATOM   2857 C  CB  . LEU B 1 146 ? 15.91000  3.59800   50.11400  1.000 61.92701  ?  146 LEU B CB  1 
ATOM   2858 C  CG  . LEU B 1 146 ? 16.46100  4.62500   51.10600  1.000 55.02057  ?  146 LEU B CG  1 
ATOM   2859 C  CD1 . LEU B 1 146 ? 15.34700  5.21400   51.95700  1.000 53.64012  ?  146 LEU B CD1 1 
ATOM   2860 C  CD2 . LEU B 1 146 ? 17.53000  4.00600   51.98000  1.000 60.60400  ?  146 LEU B CD2 1 
ATOM   2861 N  N   . CYS B 1 147 ? 16.25800  5.24000   47.41000  1.000 60.67321  ?  147 CYS B N   1 
ATOM   2862 C  CA  . CYS B 1 147 ? 16.77100  6.38900   46.67200  1.000 57.24330  ?  147 CYS B CA  1 
ATOM   2863 C  C   . CYS B 1 147 ? 15.63600  7.23300   46.10300  1.000 59.15981  ?  147 CYS B C   1 
ATOM   2864 O  O   . CYS B 1 147 ? 15.69000  8.46700   46.14500  1.000 60.07762  ?  147 CYS B O   1 
ATOM   2865 C  CB  . CYS B 1 147 ? 17.70500  5.91700   45.55700  1.000 56.87262  ?  147 CYS B CB  1 
ATOM   2866 S  SG  . CYS B 1 147 ? 18.31900  7.23200   44.48000  1.000 70.69214  ?  147 CYS B SG  1 
ATOM   2867 N  N   . GLU B 1 148 ? 14.59200  6.58500   45.57900  1.000 62.57230  ?  148 GLU B N   1 
ATOM   2868 C  CA  . GLU B 1 148 ? 13.42800  7.33200   45.11100  1.000 61.57546  ?  148 GLU B CA  1 
ATOM   2869 C  C   . GLU B 1 148 ? 12.60100  7.84900   46.28000  1.000 56.98047  ?  148 GLU B C   1 
ATOM   2870 O  O   . GLU B 1 148 ? 12.03100  8.94500   46.20900  1.000 54.30864  ?  148 GLU B O   1 
ATOM   2871 C  CB  . GLU B 1 148 ? 12.57700  6.46500   44.18200  1.000 56.63955  ?  148 GLU B CB  1 
ATOM   2872 C  CG  . GLU B 1 148 ? 13.31700  5.99100   42.94100  1.000 66.54657  ?  148 GLU B CG  1 
ATOM   2873 C  CD  . GLU B 1 148 ? 12.46700  5.10400   42.05000  1.000 73.52872  ?  148 GLU B CD  1 
ATOM   2874 O  OE1 . GLU B 1 148 ? 11.34300  4.74700   42.46000  1.000 71.90345  ?  148 GLU B OE1 1 
ATOM   2875 O  OE2 . GLU B 1 148 ? 12.92400  4.77100   40.93600  1.000 74.02169  -1 148 GLU B OE2 1 
ATOM   2876 N  N   . LEU B 1 149 ? 12.51900  7.07100   47.36300  1.000 54.79379  ?  149 LEU B N   1 
ATOM   2877 C  CA  . LEU B 1 149 ? 11.81300  7.53000   48.55500  1.000 53.95447  ?  149 LEU B CA  1 
ATOM   2878 C  C   . LEU B 1 149 ? 12.45300  8.78900   49.12200  1.000 55.86594  ?  149 LEU B C   1 
ATOM   2879 O  O   . LEU B 1 149 ? 11.75200  9.73500   49.50100  1.000 51.89320  ?  149 LEU B O   1 
ATOM   2880 C  CB  . LEU B 1 149 ? 11.78700  6.41600   49.59900  1.000 49.72953  ?  149 LEU B CB  1 
ATOM   2881 C  CG  . LEU B 1 149 ? 10.82300  5.27300   49.28500  1.000 54.36696  ?  149 LEU B CG  1 
ATOM   2882 C  CD1 . LEU B 1 149 ? 11.11800  4.06400   50.14900  1.000 49.12374  ?  149 LEU B CD1 1 
ATOM   2883 C  CD2 . LEU B 1 149 ? 9.39700   5.74500   49.50400  1.000 48.97332  ?  149 LEU B CD2 1 
ATOM   2884 N  N   . ASN B 1 150 ? 13.78600  8.81500   49.19400  1.000 53.74554  ?  150 ASN B N   1 
ATOM   2885 C  CA  . ASN B 1 150 ? 14.48600  9.98400   49.71400  1.000 48.87917  ?  150 ASN B CA  1 
ATOM   2886 C  C   . ASN B 1 150 ? 14.17200  11.23100  48.89100  1.000 56.82062  ?  150 ASN B C   1 
ATOM   2887 O  O   . ASN B 1 150 ? 13.93100  12.30600  49.45200  1.000 57.91237  ?  150 ASN B O   1 
ATOM   2888 C  CB  . ASN B 1 150 ? 15.99200  9.71600   49.74100  1.000 48.67376  ?  150 ASN B CB  1 
ATOM   2889 C  CG  . ASN B 1 150 ? 16.78400  10.86800  50.33200  1.000 46.92277  ?  150 ASN B CG  1 
ATOM   2890 O  OD1 . ASN B 1 150 ? 16.28700  11.61300  51.17600  1.000 56.75263  ?  150 ASN B OD1 1 
ATOM   2891 N  ND2 . ASN B 1 150 ? 18.03000  11.01300  49.89500  1.000 43.00441  ?  150 ASN B ND2 1 
ATOM   2892 N  N   . VAL B 1 151 ? 14.14100  11.09800  47.56100  1.000 51.76914  ?  151 VAL B N   1 
ATOM   2893 C  CA  . VAL B 1 151 ? 13.90400  12.25300  46.69800  1.000 48.68655  ?  151 VAL B CA  1 
ATOM   2894 C  C   . VAL B 1 151 ? 12.49700  12.80300  46.90200  1.000 45.48586  ?  151 VAL B C   1 
ATOM   2895 O  O   . VAL B 1 151 ? 12.28600  14.02200  46.89400  1.000 49.38506  ?  151 VAL B O   1 
ATOM   2896 C  CB  . VAL B 1 151 ? 14.16500  11.88200  45.22600  1.000 58.26350  ?  151 VAL B CB  1 
ATOM   2897 C  CG1 . VAL B 1 151 ? 13.75900  13.02200  44.30900  1.000 41.36479  ?  151 VAL B CG1 1 
ATOM   2898 C  CG2 . VAL B 1 151 ? 15.63300  11.55000  45.02500  1.000 60.32461  ?  151 VAL B CG2 1 
ATOM   2899 N  N   . MET B 1 152 ? 11.51000  11.92200  47.07900  1.000 42.05768  ?  152 MET B N   1 
ATOM   2900 C  CA  . MET B 1 152 ? 10.15300  12.39200  47.34100  1.000 50.54592  ?  152 MET B CA  1 
ATOM   2901 C  C   . MET B 1 152 ? 10.07800  13.13000  48.67200  1.000 63.02205  ?  152 MET B C   1 
ATOM   2902 O  O   . MET B 1 152 ? 9.41000   14.16600  48.78100  1.000 64.39940  ?  152 MET B O   1 
ATOM   2903 C  CB  . MET B 1 152 ? 9.17800   11.21600  47.32900  1.000 50.16681  ?  152 MET B CB  1 
ATOM   2904 C  CG  . MET B 1 152 ? 9.16500   10.42600  46.03600  1.000 47.74506  ?  152 MET B CG  1 
ATOM   2905 S  SD  . MET B 1 152 ? 7.99800   9.05400   46.09500  1.000 59.85746  ?  152 MET B SD  1 
ATOM   2906 C  CE  . MET B 1 152 ? 8.33000   8.26500   44.52200  1.000 66.72770  ?  152 MET B CE  1 
ATOM   2907 N  N   . GLU B 1 153 ? 10.76800  12.61300  49.69400  1.000 55.30806  ?  153 GLU B N   1 
ATOM   2908 C  CA  . GLU B 1 153 ? 10.76700  13.25500  51.00500  1.000 52.69965  ?  153 GLU B CA  1 
ATOM   2909 C  C   . GLU B 1 153 ? 11.41300  14.63600  50.95200  1.000 57.71200  ?  153 GLU B C   1 
ATOM   2910 O  O   . GLU B 1 153 ? 10.93700  15.57600  51.60100  1.000 56.50735  ?  153 GLU B O   1 
ATOM   2911 C  CB  . GLU B 1 153 ? 11.49200  12.36800  52.01900  1.000 56.42250  ?  153 GLU B CB  1 
ATOM   2912 C  CG  . GLU B 1 153 ? 10.84100  11.01400  52.30600  1.000 58.65667  ?  153 GLU B CG  1 
ATOM   2913 C  CD  . GLU B 1 153 ? 9.60100   11.11200  53.18400  1.000 62.76911  ?  153 GLU B CD  1 
ATOM   2914 O  OE1 . GLU B 1 153 ? 9.37100   12.18500  53.78300  1.000 65.25528  ?  153 GLU B OE1 1 
ATOM   2915 O  OE2 . GLU B 1 153 ? 8.87000   10.10300  53.29600  1.000 55.17522  -1 153 GLU B OE2 1 
ATOM   2916 N  N   . GLN B 1 154 ? 12.49600  14.77900  50.22100  1.000 55.12588  ?  154 GLN B N   1 
ATOM   2917 C  CA  . GLN B 1 154 ? 13.17600  16.05300  50.20800  1.000 53.56790  ?  154 GLN B CA  1 
ATOM   2918 C  C   . GLN B 1 154 ? 12.31800  17.10700  49.54600  1.000 53.69583  ?  154 GLN B C   1 
ATOM   2919 O  O   . GLN B 1 154 ? 12.41000  18.27800  49.86800  1.000 52.85217  ?  154 GLN B O   1 
ATOM   2920 C  CB  . GLN B 1 154 ? 14.50600  15.92400  49.49800  1.000 50.84463  ?  154 GLN B CB  1 
ATOM   2921 C  CG  . GLN B 1 154 ? 15.46300  14.93200  50.12400  1.000 52.69540  ?  154 GLN B CG  1 
ATOM   2922 C  CD  . GLN B 1 154 ? 15.43500  14.97400  51.63200  1.000 62.54317  ?  154 GLN B CD  1 
ATOM   2923 O  OE1 . GLN B 1 154 ? 15.79800  15.97600  52.24100  1.000 66.03735  ?  154 GLN B OE1 1 
ATOM   2924 N  NE2 . GLN B 1 154 ? 15.00300  13.88300  52.24400  1.000 53.99395  ?  154 GLN B NE2 1 
ATOM   2925 N  N   . VAL B 1 155 ? 11.46900  16.69400  48.62700  1.000 52.90278  ?  155 VAL B N   1 
ATOM   2926 C  CA  . VAL B 1 155 ? 10.58400  17.62300  47.96600  1.000 54.59425  ?  155 VAL B CA  1 
ATOM   2927 C  C   . VAL B 1 155 ? 9.53800   18.03800  48.95300  1.000 54.11941  ?  155 VAL B C   1 
ATOM   2928 O  O   . VAL B 1 155 ? 9.23700   19.21400  49.09100  1.000 55.90251  ?  155 VAL B O   1 
ATOM   2929 C  CB  . VAL B 1 155 ? 9.92100   16.97500  46.74700  1.000 52.22049  ?  155 VAL B CB  1 
ATOM   2930 C  CG1 . VAL B 1 155 ? 8.81000   17.85700  46.20700  1.000 50.41238  ?  155 VAL B CG1 1 
ATOM   2931 C  CG2 . VAL B 1 155 ? 10.95200  16.69300  45.67100  1.000 48.37379  ?  155 VAL B CG2 1 
ATOM   2932 N  N   . TYR B 1 156 ? 8.99000   17.06900  49.65600  1.000 56.00001  ?  156 TYR B N   1 
ATOM   2933 C  CA  . TYR B 1 156 ? 7.99500   17.35200  50.64900  1.000 58.97794  ?  156 TYR B CA  1 
ATOM   2934 C  C   . TYR B 1 156 ? 8.54700   18.36900  51.59200  1.000 61.54184  ?  156 TYR B C   1 
ATOM   2935 O  O   . TYR B 1 156 ? 7.89400   19.34900  51.91500  1.000 63.05577  ?  156 TYR B O   1 
ATOM   2936 C  CB  . TYR B 1 156 ? 7.69300   16.08000  51.39800  1.000 59.15966  ?  156 TYR B CB  1 
ATOM   2937 C  CG  . TYR B 1 156 ? 6.35300   16.02200  52.06800  1.000 64.25439  ?  156 TYR B CG  1 
ATOM   2938 C  CD1 . TYR B 1 156 ? 5.26200   16.69600  51.55300  1.000 65.61509  ?  156 TYR B CD1 1 
ATOM   2939 C  CD2 . TYR B 1 156 ? 6.17900   15.27600  53.21500  1.000 64.85071  ?  156 TYR B CD2 1 
ATOM   2940 C  CE1 . TYR B 1 156 ? 4.03200   16.63200  52.17300  1.000 69.02117  ?  156 TYR B CE1 1 
ATOM   2941 C  CE2 . TYR B 1 156 ? 4.95900   15.20600  53.84100  1.000 64.13614  ?  156 TYR B CE2 1 
ATOM   2942 C  CZ  . TYR B 1 156 ? 3.89100   15.88400  53.31700  1.000 69.07198  ?  156 TYR B CZ  1 
ATOM   2943 O  OH  . TYR B 1 156 ? 2.68400   15.80300  53.95600  1.000 74.44586  ?  156 TYR B OH  1 
ATOM   2944 N  N   . ASN B 1 157 ? 9.76300   18.13900  52.04300  1.000 54.97633  ?  157 ASN B N   1 
ATOM   2945 C  CA  . ASN B 1 157 ? 10.37100  19.06000  52.96100  1.000 55.99165  ?  157 ASN B CA  1 
ATOM   2946 C  C   . ASN B 1 157 ? 10.48400  20.42000  52.31400  1.000 61.11422  ?  157 ASN B C   1 
ATOM   2947 O  O   . ASN B 1 157 ? 10.00700  21.40900  52.85000  1.000 59.84419  ?  157 ASN B O   1 
ATOM   2948 C  CB  . ASN B 1 157 ? 11.73700  18.55300  53.37900  1.000 54.89344  ?  157 ASN B CB  1 
ATOM   2949 C  CG  . ASN B 1 157 ? 11.67300  17.22500  54.09100  1.000 58.90213  ?  157 ASN B CG  1 
ATOM   2950 O  OD1 . ASN B 1 157 ? 10.60200  16.76800  54.47600  1.000 57.51670  ?  157 ASN B OD1 1 
ATOM   2951 N  ND2 . ASN B 1 157 ? 12.82500  16.59600  54.27100  1.000 56.27088  ?  157 ASN B ND2 1 
ATOM   2952 N  N   . LEU B 1 158 ? 11.10900  20.47400  51.15000  1.000 62.20200  ?  158 LEU B N   1 
ATOM   2953 C  CA  . LEU B 1 158 ? 11.29600  21.75100  50.47200  1.000 56.73728  ?  158 LEU B CA  1 
ATOM   2954 C  C   . LEU B 1 158 ? 9.97900   22.50700  50.35300  1.000 56.80960  ?  158 LEU B C   1 
ATOM   2955 O  O   . LEU B 1 158 ? 9.92500   23.71600  50.60500  1.000 60.33235  ?  158 LEU B O   1 
ATOM   2956 C  CB  . LEU B 1 158 ? 11.93900  21.53100  49.10300  1.000 60.99289  ?  158 LEU B CB  1 
ATOM   2957 C  CG  . LEU B 1 158 ? 12.18000  22.78000  48.25800  1.000 57.84724  ?  158 LEU B CG  1 
ATOM   2958 C  CD1 . LEU B 1 158 ? 12.88900  23.83400  49.08800  1.000 63.02561  ?  158 LEU B CD1 1 
ATOM   2959 C  CD2 . LEU B 1 158 ? 13.02300  22.42100  47.05500  1.000 54.49074  ?  158 LEU B CD2 1 
ATOM   2960 N  N   . GLY B 1 159 ? 8.89900   21.80900  49.99500  1.000 55.57888  ?  159 GLY B N   1 
ATOM   2961 C  CA  . GLY B 1 159 ? 7.60800   22.46400  49.88600  1.000 57.49509  ?  159 GLY B CA  1 
ATOM   2962 C  C   . GLY B 1 159 ? 7.04900   22.94200  51.21000  1.000 63.94367  ?  159 GLY B C   1 
ATOM   2963 O  O   . GLY B 1 159 ? 6.18800   23.82900  51.22200  1.000 65.97119  ?  159 GLY B O   1 
ATOM   2964 N  N   . HIS B 1 160 ? 7.50600   22.36500  52.32200  1.000 65.89474  ?  160 HIS B N   1 
ATOM   2965 C  CA  . HIS B 1 160 ? 7.05200   22.77000  53.64700  1.000 65.99494  ?  160 HIS B CA  1 
ATOM   2966 C  C   . HIS B 1 160 ? 7.86200   23.91000  54.24400  1.000 63.80990  ?  160 HIS B C   1 
ATOM   2967 O  O   . HIS B 1 160 ? 7.37500   24.56900  55.17100  1.000 70.22562  ?  160 HIS B O   1 
ATOM   2968 C  CB  . HIS B 1 160 ? 7.07700   21.58200  54.61400  1.000 54.52140  ?  160 HIS B CB  1 
ATOM   2969 C  CG  . HIS B 1 160 ? 5.89800   20.67000  54.48300  1.000 57.01782  ?  160 HIS B CG  1 
ATOM   2970 N  ND1 . HIS B 1 160 ? 4.66200   21.10900  54.05700  1.000 61.01058  ?  160 HIS B ND1 1 
ATOM   2971 C  CD2 . HIS B 1 160 ? 5.76400   19.34400  54.72200  1.000 59.76712  ?  160 HIS B CD2 1 
ATOM   2972 C  CE1 . HIS B 1 160 ? 3.81700   20.09400  54.04300  1.000 60.74092  ?  160 HIS B CE1 1 
ATOM   2973 N  NE2 . HIS B 1 160 ? 4.46100   19.01000  54.43900  1.000 60.86837  ?  160 HIS B NE2 1 
ATOM   2974 N  N   . SER B 1 161 ? 9.07400   24.15800  53.74900  1.000 60.17982  ?  161 SER B N   1 
ATOM   2975 C  CA  . SER B 1 161 ? 9.89200   25.22900  54.29900  1.000 60.19652  ?  161 SER B CA  1 
ATOM   2976 C  C   . SER B 1 161 ? 9.17900   26.56900  54.15100  1.000 60.53120  ?  161 SER B C   1 
ATOM   2977 O  O   . SER B 1 161 ? 8.31100   26.75300  53.29600  1.000 65.32824  ?  161 SER B O   1 
ATOM   2978 C  CB  . SER B 1 161 ? 11.25300  25.27900  53.60400  1.000 60.18580  ?  161 SER B CB  1 
ATOM   2979 O  OG  . SER B 1 161 ? 11.16500  25.95100  52.36000  1.000 71.20956  ?  161 SER B OG  1 
ATOM   2980 N  N   . THR B 1 162 ? 9.56800   27.52200  54.99900  1.000 65.73297  ?  162 THR B N   1 
ATOM   2981 C  CA  . THR B 1 162 ? 8.92300   28.83000  54.96900  1.000 70.64186  ?  162 THR B CA  1 
ATOM   2982 C  C   . THR B 1 162 ? 9.21100   29.57200  53.67200  1.000 69.95954  ?  162 THR B C   1 
ATOM   2983 O  O   . THR B 1 162 ? 8.37800   30.36600  53.22100  1.000 78.53025  ?  162 THR B O   1 
ATOM   2984 C  CB  . THR B 1 162 ? 9.35600   29.66300  56.17500  1.000 70.38864  ?  162 THR B CB  1 
ATOM   2985 O  OG1 . THR B 1 162 ? 10.77800  29.84500  56.15000  1.000 70.93029  ?  162 THR B OG1 1 
ATOM   2986 C  CG2 . THR B 1 162 ? 8.95600   28.97000  57.46600  1.000 57.18095  ?  162 THR B CG2 1 
ATOM   2987 N  N   . ILE B 1 163 ? 10.37500  29.33500  53.06200  1.000 69.11355  ?  163 ILE B N   1 
ATOM   2988 C  CA  . ILE B 1 163 ? 10.70800  30.00200  51.80400  1.000 74.09764  ?  163 ILE B CA  1 
ATOM   2989 C  C   . ILE B 1 163 ? 9.68600   29.65400  50.73000  1.000 66.52625  ?  163 ILE B C   1 
ATOM   2990 O  O   . ILE B 1 163 ? 9.10200   30.53800  50.09300  1.000 68.85781  ?  163 ILE B O   1 
ATOM   2991 C  CB  . ILE B 1 163 ? 12.12800  29.61900  51.35400  1.000 70.69511  ?  163 ILE B CB  1 
ATOM   2992 C  CG1 . ILE B 1 163 ? 13.14400  29.94400  52.44800  1.000 70.85358  ?  163 ILE B CG1 1 
ATOM   2993 C  CG2 . ILE B 1 163 ? 12.47000  30.31900  50.04900  1.000 66.22844  ?  163 ILE B CG2 1 
ATOM   2994 C  CD1 . ILE B 1 163 ? 14.44200  29.20000  52.28500  1.000 65.30044  ?  163 ILE B CD1 1 
ATOM   2995 N  N   . MET B 1 164 ? 9.44400   28.35700  50.52700  1.000 61.79988  ?  164 MET B N   1 
ATOM   2996 C  CA  . MET B 1 164 ? 8.48000   27.92500  49.52000  1.000 66.78654  ?  164 MET B CA  1 
ATOM   2997 C  C   . MET B 1 164 ? 7.05800   28.30800  49.90500  1.000 67.79118  ?  164 MET B C   1 
ATOM   2998 O  O   . MET B 1 164 ? 6.29000   28.78500  49.06200  1.000 71.48629  ?  164 MET B O   1 
ATOM   2999 C  CB  . MET B 1 164 ? 8.59300   26.41700  49.30200  1.000 66.13549  ?  164 MET B CB  1 
ATOM   3000 C  CG  . MET B 1 164 ? 9.83000   25.99300  48.52800  1.000 68.14843  ?  164 MET B CG  1 
ATOM   3001 S  SD  . MET B 1 164 ? 9.94800   26.84400  46.94500  1.000 68.47470  ?  164 MET B SD  1 
ATOM   3002 C  CE  . MET B 1 164 ? 8.38600   26.36400  46.21000  1.000 63.57910  ?  164 MET B CE  1 
ATOM   3003 N  N   . GLN B 1 165 ? 6.68500   28.09400  51.16700  1.000 72.00931  ?  165 GLN B N   1 
ATOM   3004 C  CA  . GLN B 1 165 ? 5.33600   28.43400  51.60500  1.000 75.10458  ?  165 GLN B CA  1 
ATOM   3005 C  C   . GLN B 1 165 ? 5.05800   29.92200  51.42600  1.000 78.27699  ?  165 GLN B C   1 
ATOM   3006 O  O   . GLN B 1 165 ? 3.94400   30.31100  51.05400  1.000 80.61274  ?  165 GLN B O   1 
ATOM   3007 C  CB  . GLN B 1 165 ? 5.13200   28.00300  53.05600  1.000 72.39980  ?  165 GLN B CB  1 
ATOM   3008 C  CG  . GLN B 1 165 ? 5.22400   26.49400  53.24600  1.000 74.30801  ?  165 GLN B CG  1 
ATOM   3009 C  CD  . GLN B 1 165 ? 3.94000   25.77600  52.88100  1.000 84.41459  ?  165 GLN B CD  1 
ATOM   3010 O  OE1 . GLN B 1 165 ? 2.86200   26.14600  53.34200  1.000 92.93081  ?  165 GLN B OE1 1 
ATOM   3011 N  NE2 . GLN B 1 165 ? 4.04700   24.75500  52.03600  1.000 76.11801  ?  165 GLN B NE2 1 
ATOM   3012 N  N   . SER B 1 166 ? 6.05800   30.77100  51.68300  1.000 73.67896  ?  166 SER B N   1 
ATOM   3013 C  CA  . SER B 1 166 ? 5.87400   32.20900  51.50600  1.000 75.00423  ?  166 SER B CA  1 
ATOM   3014 C  C   . SER B 1 166 ? 5.64500   32.56600  50.04300  1.000 78.37567  ?  166 SER B C   1 
ATOM   3015 O  O   . SER B 1 166 ? 4.75600   33.36500  49.72400  1.000 75.16356  ?  166 SER B O   1 
ATOM   3016 C  CB  . SER B 1 166 ? 7.08700   32.96800  52.04400  1.000 69.91224  ?  166 SER B CB  1 
ATOM   3017 O  OG  . SER B 1 166 ? 7.30700   32.68700  53.41300  1.000 89.59273  ?  166 SER B OG  1 
ATOM   3018 N  N   . ALA B 1 167 ? 6.43400   31.98200  49.13800  1.000 76.35019  ?  167 ALA B N   1 
ATOM   3019 C  CA  . ALA B 1 167 ? 6.31800   32.31600  47.72100  1.000 75.66362  ?  167 ALA B CA  1 
ATOM   3020 C  C   . ALA B 1 167 ? 4.95800   31.91300  47.16600  1.000 73.47917  ?  167 ALA B C   1 
ATOM   3021 O  O   . ALA B 1 167 ? 4.30900   32.69000  46.45500  1.000 72.30813  ?  167 ALA B O   1 
ATOM   3022 C  CB  . ALA B 1 167 ? 7.44300   31.64600  46.93000  1.000 70.62425  ?  167 ALA B CB  1 
ATOM   3023 N  N   . TRP B 1 168 ? 4.51000   30.69700  47.48300  1.000 72.74687  ?  168 TRP B N   1 
ATOM   3024 C  CA  . TRP B 1 168 ? 3.21800   30.23400  46.98900  1.000 69.80616  ?  168 TRP B CA  1 
ATOM   3025 C  C   . TRP B 1 168 ? 2.07400   31.08800  47.52000  1.000 72.43581  ?  168 TRP B C   1 
ATOM   3026 O  O   . TRP B 1 168 ? 1.09700   31.34100  46.80500  1.000 72.58219  ?  168 TRP B O   1 
ATOM   3027 C  CB  . TRP B 1 168 ? 3.01300   28.77200  47.37900  1.000 74.17554  ?  168 TRP B CB  1 
ATOM   3028 C  CG  . TRP B 1 168 ? 3.80200   27.81300  46.55200  1.000 72.86691  ?  168 TRP B CG  1 
ATOM   3029 C  CD1 . TRP B 1 168 ? 4.34400   28.04100  45.32200  1.000 63.02921  ?  168 TRP B CD1 1 
ATOM   3030 C  CD2 . TRP B 1 168 ? 4.14800   26.46900  46.90200  1.000 73.35227  ?  168 TRP B CD2 1 
ATOM   3031 N  NE1 . TRP B 1 168 ? 5.00300   26.91800  44.88100  1.000 69.08862  ?  168 TRP B NE1 1 
ATOM   3032 C  CE2 . TRP B 1 168 ? 4.89600   25.93800  45.83200  1.000 72.43897  ?  168 TRP B CE2 1 
ATOM   3033 C  CE3 . TRP B 1 168 ? 3.89400   25.66100  48.01400  1.000 66.76277  ?  168 TRP B CE3 1 
ATOM   3034 C  CZ2 . TRP B 1 168 ? 5.39100   24.63500  45.84300  1.000 69.94361  ?  168 TRP B CZ2 1 
ATOM   3035 C  CZ3 . TRP B 1 168 ? 4.38600   24.37000  48.02300  1.000 71.06492  ?  168 TRP B CZ3 1 
ATOM   3036 C  CH2 . TRP B 1 168 ? 5.12600   23.86900  46.94500  1.000 69.95996  ?  168 TRP B CH2 1 
ATOM   3037 N  N   . LYS B 1 169 ? 2.16900   31.53800  48.77400  1.000 79.62130  ?  169 LYS B N   1 
ATOM   3038 C  CA  . LYS B 1 169 ? 1.08700   32.34300  49.33100  1.000 75.34181  ?  169 LYS B CA  1 
ATOM   3039 C  C   . LYS B 1 169 ? 1.08000   33.75700  48.76200  1.000 77.11793  ?  169 LYS B C   1 
ATOM   3040 O  O   . LYS B 1 169 ? 0.01700   34.38400  48.69100  1.000 75.09449  ?  169 LYS B O   1 
ATOM   3041 C  CB  . LYS B 1 169 ? 1.16300   32.37300  50.85600  1.000 75.09669  ?  169 LYS B CB  1 
ATOM   3042 C  CG  . LYS B 1 169 ? 0.00400   33.14600  51.48000  1.000 82.16547  ?  169 LYS B CG  1 
ATOM   3043 C  CD  . LYS B 1 169 ? 0.02800   33.15100  53.00300  1.000 88.21019  ?  169 LYS B CD  1 
ATOM   3044 C  CE  . LYS B 1 169 ? -1.12400  33.94900  53.59500  1.000 95.18181  ?  169 LYS B CE  1 
ATOM   3045 N  NZ  . LYS B 1 169 ? -1.10800  33.95900  55.08500  1.000 88.26246  ?  169 LYS B NZ  1 
ATOM   3046 N  N   . ARG B 1 170 ? 2.24000   34.28400  48.36700  1.000 78.45398  ?  170 ARG B N   1 
ATOM   3047 C  CA  . ARG B 1 170 ? 2.28800   35.58500  47.71300  1.000 73.64670  ?  170 ARG B CA  1 
ATOM   3048 C  C   . ARG B 1 170 ? 2.08600   35.48400  46.20600  1.000 77.36551  ?  170 ARG B C   1 
ATOM   3049 O  O   . ARG B 1 170 ? 2.22000   36.49200  45.50400  1.000 78.09769  ?  170 ARG B O   1 
ATOM   3050 C  CB  . ARG B 1 170 ? 3.60500   36.31200  48.01900  1.000 75.87091  ?  170 ARG B CB  1 
ATOM   3051 C  CG  . ARG B 1 170 ? 4.86000   35.73300  47.38100  1.000 73.95801  ?  170 ARG B CG  1 
ATOM   3052 C  CD  . ARG B 1 170 ? 6.08500   36.52300  47.83500  1.000 84.44788  ?  170 ARG B CD  1 
ATOM   3053 N  NE  . ARG B 1 170 ? 7.32400   36.06200  47.22000  1.000 85.69508  ?  170 ARG B NE  1 
ATOM   3054 C  CZ  . ARG B 1 170 ? 8.30200   35.44900  47.87400  1.000 91.74509  ?  170 ARG B CZ  1 
ATOM   3055 N  NH1 . ARG B 1 170 ? 8.21500   35.19600  49.17000  1.000 76.96102  ?  170 ARG B NH1 1 
ATOM   3056 N  NH2 . ARG B 1 170 ? 9.39800   35.08700  47.21200  1.000 84.38196  ?  170 ARG B NH2 1 
ATOM   3057 N  N   . GLY B 1 171 ? 1.77300   34.29300  45.69700  1.000 77.14556  ?  171 GLY B N   1 
ATOM   3058 C  CA  . GLY B 1 171 ? 1.41500   34.10400  44.30800  1.000 72.31203  ?  171 GLY B CA  1 
ATOM   3059 C  C   . GLY B 1 171 ? 2.55700   33.82900  43.35400  1.000 70.65736  ?  171 GLY B C   1 
ATOM   3060 O  O   . GLY B 1 171 ? 2.30300   33.64300  42.15600  1.000 75.19930  ?  171 GLY B O   1 
ATOM   3061 N  N   . GLN B 1 172 ? 3.79900   33.79700  43.83300  1.000 62.91522  ?  172 GLN B N   1 
ATOM   3062 C  CA  . GLN B 1 172 ? 4.92500   33.51900  42.95100  1.000 68.06215  ?  172 GLN B CA  1 
ATOM   3063 C  C   . GLN B 1 172 ? 4.79100   32.13100  42.33300  1.000 74.21516  ?  172 GLN B C   1 
ATOM   3064 O  O   . GLN B 1 172 ? 4.33400   31.18500  42.97900  1.000 73.31237  ?  172 GLN B O   1 
ATOM   3065 C  CB  . GLN B 1 172 ? 6.24300   33.63400  43.71900  1.000 65.89898  ?  172 GLN B CB  1 
ATOM   3066 C  CG  . GLN B 1 172 ? 7.48300   33.47900  42.84900  1.000 69.49147  ?  172 GLN B CG  1 
ATOM   3067 C  CD  . GLN B 1 172 ? 8.73600   34.01000  43.51500  1.000 74.48607  ?  172 GLN B CD  1 
ATOM   3068 O  OE1 . GLN B 1 172 ? 8.67800   34.93300  44.32700  1.000 86.06828  ?  172 GLN B OE1 1 
ATOM   3069 N  NE2 . GLN B 1 172 ? 9.88000   33.42700  43.17400  1.000 70.62218  ?  172 GLN B NE2 1 
ATOM   3070 N  N   . LYS B 1 173 ? 5.18600   32.01800  41.06600  1.000 71.74075  ?  173 LYS B N   1 
ATOM   3071 C  CA  . LYS B 1 173 ? 5.10900   30.75800  40.32800  1.000 72.32504  ?  173 LYS B CA  1 
ATOM   3072 C  C   . LYS B 1 173 ? 6.42200   30.00400  40.51300  1.000 71.94754  ?  173 LYS B C   1 
ATOM   3073 O  O   . LYS B 1 173 ? 7.43500   30.34000  39.89500  1.000 72.32904  ?  173 LYS B O   1 
ATOM   3074 C  CB  . LYS B 1 173 ? 4.82600   31.01700  38.85200  1.000 76.26800  ?  173 LYS B CB  1 
ATOM   3075 C  CG  . LYS B 1 173 ? 3.45700   31.61700  38.55300  1.000 87.98953  ?  173 LYS B CG  1 
ATOM   3076 C  CD  . LYS B 1 173 ? 2.31700   30.77300  39.09800  1.000 88.95121  ?  173 LYS B CD  1 
ATOM   3077 C  CE  . LYS B 1 173 ? 0.97200   31.36300  38.69500  1.000 92.74364  ?  173 LYS B CE  1 
ATOM   3078 N  NZ  . LYS B 1 173 ? 0.85200   32.80300  39.06200  1.000 91.17846  ?  173 LYS B NZ  1 
ATOM   3079 N  N   . VAL B 1 174 ? 6.41000   28.98100  41.36900  1.000 66.73405  ?  174 VAL B N   1 
ATOM   3080 C  CA  . VAL B 1 174 ? 7.55000   28.08900  41.55900  1.000 58.87866  ?  174 VAL B CA  1 
ATOM   3081 C  C   . VAL B 1 174 ? 7.03800   26.65600  41.54800  1.000 59.71110  ?  174 VAL B C   1 
ATOM   3082 O  O   . VAL B 1 174 ? 5.96000   26.36900  42.07800  1.000 64.62978  ?  174 VAL B O   1 
ATOM   3083 C  CB  . VAL B 1 174 ? 8.31800   28.37800  42.86800  1.000 64.90863  ?  174 VAL B CB  1 
ATOM   3084 C  CG1 . VAL B 1 174 ? 9.63500   27.61000  42.88800  1.000 60.38170  ?  174 VAL B CG1 1 
ATOM   3085 C  CG2 . VAL B 1 174 ? 8.57200   29.86900  43.03600  1.000 68.74659  ?  174 VAL B CG2 1 
ATOM   3086 N  N   . THR B 1 175 ? 7.80300   25.76000  40.92500  1.000 58.89655  ?  175 THR B N   1 
ATOM   3087 C  CA  . THR B 1 175 ? 7.41800   24.36200  40.77900  1.000 62.24353  ?  175 THR B CA  1 
ATOM   3088 C  C   . THR B 1 175 ? 8.57300   23.46100  41.19500  1.000 63.67740  ?  175 THR B C   1 
ATOM   3089 O  O   . THR B 1 175 ? 9.70800   23.66000  40.74900  1.000 65.68517  ?  175 THR B O   1 
ATOM   3090 C  CB  . THR B 1 175 ? 7.00400   24.06400  39.33400  1.000 68.64681  ?  175 THR B CB  1 
ATOM   3091 O  OG1 . THR B 1 175 ? 5.99200   24.99400  38.92800  1.000 74.05619  ?  175 THR B OG1 1 
ATOM   3092 C  CG2 . THR B 1 175 ? 6.45000   22.66100  39.22000  1.000 68.24515  ?  175 THR B CG2 1 
ATOM   3093 N  N   . ILE B 1 176 ? 8.28500   22.47700  42.04900  1.000 60.25733  ?  176 ILE B N   1 
ATOM   3094 C  CA  . ILE B 1 176 ? 9.28400   21.54100  42.55600  1.000 64.22621  ?  176 ILE B CA  1 
ATOM   3095 C  C   . ILE B 1 176 ? 9.09300   20.18400  41.89100  1.000 60.34028  ?  176 ILE B C   1 
ATOM   3096 O  O   . ILE B 1 176 ? 7.96300   19.69800  41.76100  1.000 61.38248  ?  176 ILE B O   1 
ATOM   3097 C  CB  . ILE B 1 176 ? 9.22400   21.40900  44.09200  1.000 59.75435  ?  176 ILE B CB  1 
ATOM   3098 C  CG1 . ILE B 1 176 ? 9.62200   22.72400  44.76700  1.000 53.37061  ?  176 ILE B CG1 1 
ATOM   3099 C  CG2 . ILE B 1 176 ? 10.08800  20.25300  44.56400  1.000 55.27830  ?  176 ILE B CG2 1 
ATOM   3100 C  CD1 . ILE B 1 176 ? 9.33800   22.75700  46.24700  1.000 62.82381  ?  176 ILE B CD1 1 
ATOM   3101 N  N   . HIS B 1 177 ? 10.20500  19.57300  41.47500  1.000 56.28525  ?  177 HIS B N   1 
ATOM   3102 C  CA  . HIS B 1 177 ? 10.20500  18.29800  40.76900  1.000 61.73652  ?  177 HIS B CA  1 
ATOM   3103 C  C   . HIS B 1 177 ? 11.19000  17.34100  41.42200  1.000 57.82514  ?  177 HIS B C   1 
ATOM   3104 O  O   . HIS B 1 177 ? 12.27500  17.75000  41.84600  1.000 56.73910  ?  177 HIS B O   1 
ATOM   3105 C  CB  . HIS B 1 177 ? 10.59100  18.47200  39.29600  1.000 61.06839  ?  177 HIS B CB  1 
ATOM   3106 C  CG  . HIS B 1 177 ? 9.83300   19.55100  38.59200  1.000 61.47084  ?  177 HIS B CG  1 
ATOM   3107 N  ND1 . HIS B 1 177 ? 8.71000   19.29900  37.83400  1.000 67.93193  ?  177 HIS B ND1 1 
ATOM   3108 C  CD2 . HIS B 1 177 ? 10.03300  20.88900  38.53600  1.000 64.41609  ?  177 HIS B CD2 1 
ATOM   3109 C  CE1 . HIS B 1 177 ? 8.25700   20.43400  37.33200  1.000 71.77774  ?  177 HIS B CE1 1 
ATOM   3110 N  NE2 . HIS B 1 177 ? 9.04000   21.41400  37.74600  1.000 71.54792  ?  177 HIS B NE2 1 
ATOM   3111 N  N   . GLY B 1 178 ? 10.82400  16.06200  41.46700  1.000 56.73253  ?  178 GLY B N   1 
ATOM   3112 C  CA  . GLY B 1 178 ? 11.71800  15.04000  41.97600  1.000 54.97418  ?  178 GLY B CA  1 
ATOM   3113 C  C   . GLY B 1 178 ? 12.08200  14.01700  40.92000  1.000 51.72486  ?  178 GLY B C   1 
ATOM   3114 O  O   . GLY B 1 178 ? 11.21500  13.28400  40.43600  1.000 52.94798  ?  178 GLY B O   1 
ATOM   3115 N  N   . TRP B 1 179 ? 13.36200  13.94300  40.56800  1.000 54.92530  ?  179 TRP B N   1 
ATOM   3116 C  CA  . TRP B 1 179 ? 13.84100  13.08800  39.49200  1.000 58.95834  ?  179 TRP B CA  1 
ATOM   3117 C  C   . TRP B 1 179 ? 14.90200  12.12800  40.01000  1.000 56.06694  ?  179 TRP B C   1 
ATOM   3118 O  O   . TRP B 1 179 ? 15.42700  12.27300  41.11600  1.000 58.46637  ?  179 TRP B O   1 
ATOM   3119 C  CB  . TRP B 1 179 ? 14.44200  13.91500  38.34900  1.000 55.78689  ?  179 TRP B CB  1 
ATOM   3120 C  CG  . TRP B 1 179 ? 13.48700  14.80000  37.62400  1.000 56.09734  ?  179 TRP B CG  1 
ATOM   3121 C  CD1 . TRP B 1 179 ? 12.12600  14.81400  37.72700  1.000 57.34857  ?  179 TRP B CD1 1 
ATOM   3122 C  CD2 . TRP B 1 179 ? 13.83000  15.83000  36.69500  1.000 56.55680  ?  179 TRP B CD2 1 
ATOM   3123 N  NE1 . TRP B 1 179 ? 11.60000  15.78400  36.90500  1.000 56.11781  ?  179 TRP B NE1 1 
ATOM   3124 C  CE2 . TRP B 1 179 ? 12.62800  16.42300  36.26200  1.000 57.84659  ?  179 TRP B CE2 1 
ATOM   3125 C  CE3 . TRP B 1 179 ? 15.04100  16.30600  36.18200  1.000 55.32094  ?  179 TRP B CE3 1 
ATOM   3126 C  CZ2 . TRP B 1 179 ? 12.60200  17.46800  35.34100  1.000 64.62351  ?  179 TRP B CZ2 1 
ATOM   3127 C  CZ3 . TRP B 1 179 ? 15.01400  17.34200  35.27200  1.000 59.54989  ?  179 TRP B CZ3 1 
ATOM   3128 C  CH2 . TRP B 1 179 ? 13.80300  17.91200  34.85800  1.000 62.16189  ?  179 TRP B CH2 1 
ATOM   3129 N  N   . ALA B 1 180 ? 15.22800  11.14900  39.17100  1.000 60.24973  ?  180 ALA B N   1 
ATOM   3130 C  CA  . ALA B 1 180 ? 16.34100  10.25100  39.42900  1.000 61.98660  ?  180 ALA B CA  1 
ATOM   3131 C  C   . ALA B 1 180 ? 16.85900  9.72100   38.10000  1.000 64.43485  ?  180 ALA B C   1 
ATOM   3132 O  O   . ALA B 1 180 ? 16.11200  9.61300   37.12400  1.000 62.04921  ?  180 ALA B O   1 
ATOM   3133 C  CB  . ALA B 1 180 ? 15.93400  9.09300   40.34800  1.000 59.14595  ?  180 ALA B CB  1 
ATOM   3134 N  N   . TYR B 1 181 ? 18.14900  9.39300   38.07400  1.000 62.10649  ?  181 TYR B N   1 
ATOM   3135 C  CA  . TYR B 1 181 ? 18.77800  8.80900   36.90100  1.000 65.05021  ?  181 TYR B CA  1 
ATOM   3136 C  C   . TYR B 1 181 ? 19.74400  7.72800   37.35900  1.000 70.81724  ?  181 TYR B C   1 
ATOM   3137 O  O   . TYR B 1 181 ? 20.24400  7.76200   38.48500  1.000 65.44211  ?  181 TYR B O   1 
ATOM   3138 C  CB  . TYR B 1 181 ? 19.51300  9.87000   36.06300  1.000 68.57080  ?  181 TYR B CB  1 
ATOM   3139 C  CG  . TYR B 1 181 ? 20.80000  10.38100  36.68000  1.000 68.48176  ?  181 TYR B CG  1 
ATOM   3140 C  CD1 . TYR B 1 181 ? 20.79000  11.43500  37.58800  1.000 70.08220  ?  181 TYR B CD1 1 
ATOM   3141 C  CD2 . TYR B 1 181 ? 22.02900  9.83100   36.32900  1.000 69.14986  ?  181 TYR B CD2 1 
ATOM   3142 C  CE1 . TYR B 1 181 ? 21.96500  11.90800  38.15000  1.000 66.21464  ?  181 TYR B CE1 1 
ATOM   3143 C  CE2 . TYR B 1 181 ? 23.20700  10.30000  36.88200  1.000 75.17497  ?  181 TYR B CE2 1 
ATOM   3144 C  CZ  . TYR B 1 181 ? 23.16900  11.33900  37.79000  1.000 72.00006  ?  181 TYR B CZ  1 
ATOM   3145 O  OH  . TYR B 1 181 ? 24.34100  11.80700  38.34100  1.000 77.55290  ?  181 TYR B OH  1 
ATOM   3146 N  N   . GLY B 1 182 ? 19.98900  6.75900   36.48400  1.000 77.42695  ?  182 GLY B N   1 
ATOM   3147 C  CA  . GLY B 1 182 ? 20.88300  5.65600   36.77800  1.000 79.52478  ?  182 GLY B CA  1 
ATOM   3148 C  C   . GLY B 1 182 ? 22.13400  5.73000   35.92600  1.000 80.54977  ?  182 GLY B C   1 
ATOM   3149 O  O   . GLY B 1 182 ? 22.11700  6.29200   34.83000  1.000 86.47655  ?  182 GLY B O   1 
ATOM   3150 N  N   . ILE B 1 183 ? 23.23200  5.16400   36.43700  1.000 84.68089  ?  183 ILE B N   1 
ATOM   3151 C  CA  . ILE B 1 183 ? 24.45700  5.08700   35.64400  1.000 90.53974  ?  183 ILE B CA  1 
ATOM   3152 C  C   . ILE B 1 183 ? 24.40500  3.94900   34.64500  1.000 98.18012  ?  183 ILE B C   1 
ATOM   3153 O  O   . ILE B 1 183 ? 25.36600  3.75300   33.89200  1.000 100.71194 ?  183 ILE B O   1 
ATOM   3154 C  CB  . ILE B 1 183 ? 25.73300  4.91400   36.49300  1.000 97.08014  ?  183 ILE B CB  1 
ATOM   3155 C  CG1 . ILE B 1 183 ? 25.62500  3.68300   37.39300  1.000 95.42287  ?  183 ILE B CG1 1 
ATOM   3156 C  CG2 . ILE B 1 183 ? 26.01600  6.17300   37.29900  1.000 102.69597 ?  183 ILE B CG2 1 
ATOM   3157 C  CD1 . ILE B 1 183 ? 26.93100  3.31100   38.06300  1.000 102.77473 ?  183 ILE B CD1 1 
ATOM   3158 N  N   . HIS B 1 184 ? 23.31800  3.17500   34.63200  1.000 99.90477  ?  184 HIS B N   1 
ATOM   3159 C  CA  . HIS B 1 184 ? 23.15800  2.12200   33.63900  1.000 93.06890  ?  184 HIS B CA  1 
ATOM   3160 C  C   . HIS B 1 184 ? 22.72600  2.68000   32.28800  1.000 90.05214  ?  184 HIS B C   1 
ATOM   3161 O  O   . HIS B 1 184 ? 23.09100  2.12100   31.24900  1.000 93.41704  ?  184 HIS B O   1 
ATOM   3162 C  CB  . HIS B 1 184 ? 22.17400  1.06200   34.14700  1.000 91.64353  ?  184 HIS B CB  1 
ATOM   3163 C  CG  . HIS B 1 184 ? 20.88400  1.61900   34.67000  1.000 97.67280  ?  184 HIS B CG  1 
ATOM   3164 N  ND1 . HIS B 1 184 ? 20.80000  2.30800   35.86200  1.000 95.93186  ?  184 HIS B ND1 1 
ATOM   3165 C  CD2 . HIS B 1 184 ? 19.62400  1.56700   34.17800  1.000 97.08520  ?  184 HIS B CD2 1 
ATOM   3166 C  CE1 . HIS B 1 184 ? 19.54700  2.66700   36.07400  1.000 93.41735  ?  184 HIS B CE1 1 
ATOM   3167 N  NE2 . HIS B 1 184 ? 18.81200  2.23000   35.06700  1.000 98.41844  ?  184 HIS B NE2 1 
ATOM   3168 N  N   . ASP B 1 185 ? 21.95500  3.76900   32.27700  1.000 86.79848  ?  185 ASP B N   1 
ATOM   3169 C  CA  . ASP B 1 185 ? 21.55600  4.39400   31.02000  1.000 86.62378  ?  185 ASP B CA  1 
ATOM   3170 C  C   . ASP B 1 185 ? 21.56800  5.91500   31.04700  1.000 86.07205  ?  185 ASP B C   1 
ATOM   3171 O  O   . ASP B 1 185 ? 21.48600  6.52200   29.97500  1.000 82.40355  ?  185 ASP B O   1 
ATOM   3172 C  CB  . ASP B 1 185 ? 20.15600  3.91700   30.59600  1.000 80.38644  ?  185 ASP B CB  1 
ATOM   3173 C  CG  . ASP B 1 185 ? 19.08600  4.23100   31.63000  1.000 87.82681  ?  185 ASP B CG  1 
ATOM   3174 O  OD1 . ASP B 1 185 ? 19.39400  4.88000   32.65300  1.000 93.06463  ?  185 ASP B OD1 1 
ATOM   3175 O  OD2 . ASP B 1 185 ? 17.92400  3.82700   31.41400  1.000 86.34662  -1 185 ASP B OD2 1 
ATOM   3176 N  N   . GLY B 1 186 ? 21.66400  6.55400   32.21200  1.000 84.36936  ?  186 GLY B N   1 
ATOM   3177 C  CA  . GLY B 1 186 ? 21.63700  8.00200   32.27500  1.000 74.87137  ?  186 GLY B CA  1 
ATOM   3178 C  C   . GLY B 1 186 ? 20.28900  8.61300   31.97500  1.000 73.43567  ?  186 GLY B C   1 
ATOM   3179 O  O   . GLY B 1 186 ? 20.21000  9.81000   31.68900  1.000 74.04900  ?  186 GLY B O   1 
ATOM   3180 N  N   . LEU B 1 187 ? 19.22000  7.82400   32.04600  1.000 69.99533  ?  187 LEU B N   1 
ATOM   3181 C  CA  . LEU B 1 187 ? 17.88100  8.28300   31.70300  1.000 69.49032  ?  187 LEU B CA  1 
ATOM   3182 C  C   . LEU B 1 187 ? 17.19000  8.84600   32.94000  1.000 71.53544  ?  187 LEU B C   1 
ATOM   3183 O  O   . LEU B 1 187 ? 17.06800  8.15800   33.96000  1.000 73.19160  ?  187 LEU B O   1 
ATOM   3184 C  CB  . LEU B 1 187 ? 17.06200  7.14100   31.10200  1.000 74.18559  ?  187 LEU B CB  1 
ATOM   3185 C  CG  . LEU B 1 187 ? 15.75700  7.53900   30.41000  1.000 71.05462  ?  187 LEU B CG  1 
ATOM   3186 C  CD1 . LEU B 1 187 ? 16.03700  8.45700   29.23100  1.000 69.50540  ?  187 LEU B CD1 1 
ATOM   3187 C  CD2 . LEU B 1 187 ? 14.98900  6.30700   29.96400  1.000 65.91058  ?  187 LEU B CD2 1 
ATOM   3188 N  N   . LEU B 1 188 ? 16.74400  10.09700  32.84600  1.000 67.11146  ?  188 LEU B N   1 
ATOM   3189 C  CA  . LEU B 1 188 ? 16.01500  10.72500  33.93800  1.000 63.31653  ?  188 LEU B CA  1 
ATOM   3190 C  C   . LEU B 1 188 ? 14.63100  10.10000  34.07800  1.000 66.08194  ?  188 LEU B C   1 
ATOM   3191 O  O   . LEU B 1 188 ? 13.87500  10.02100  33.10600  1.000 67.42166  ?  188 LEU B O   1 
ATOM   3192 C  CB  . LEU B 1 188 ? 15.89000  12.22600  33.68500  1.000 58.06894  ?  188 LEU B CB  1 
ATOM   3193 C  CG  . LEU B 1 188 ? 17.16000  13.06000  33.85000  1.000 65.14925  ?  188 LEU B CG  1 
ATOM   3194 C  CD1 . LEU B 1 188 ? 16.91000  14.49200  33.41800  1.000 64.93211  ?  188 LEU B CD1 1 
ATOM   3195 C  CD2 . LEU B 1 188 ? 17.64200  13.01200  35.29000  1.000 68.70641  ?  188 LEU B CD2 1 
ATOM   3196 N  N   . ARG B 1 189 ? 14.30400  9.64800   35.28600  1.000 69.66455  ?  189 ARG B N   1 
ATOM   3197 C  CA  . ARG B 1 189 ? 12.97500  9.14700   35.60900  1.000 65.61008  ?  189 ARG B CA  1 
ATOM   3198 C  C   . ARG B 1 189 ? 12.24500  10.17300  36.46500  1.000 56.94811  ?  189 ARG B C   1 
ATOM   3199 O  O   . ARG B 1 189 ? 12.77500  10.61900  37.48800  1.000 61.55064  ?  189 ARG B O   1 
ATOM   3200 C  CB  . ARG B 1 189 ? 13.05300  7.80900   36.34700  1.000 62.88286  ?  189 ARG B CB  1 
ATOM   3201 C  CG  . ARG B 1 189 ? 11.70700  7.30300   36.84100  1.000 61.49779  ?  189 ARG B CG  1 
ATOM   3202 C  CD  . ARG B 1 189 ? 11.83500  5.97900   37.58500  1.000 76.66669  ?  189 ARG B CD  1 
ATOM   3203 N  NE  . ARG B 1 189 ? 12.02300  4.83900   36.69500  1.000 78.77636  ?  189 ARG B NE  1 
ATOM   3204 C  CZ  . ARG B 1 189 ? 13.18400  4.22700   36.50100  1.000 79.81389  ?  189 ARG B CZ  1 
ATOM   3205 N  NH1 . ARG B 1 189 ? 14.28700  4.62700   37.11400  1.000 83.48731  ?  189 ARG B NH1 1 
ATOM   3206 N  NH2 . ARG B 1 189 ? 13.24000  3.18400   35.67800  1.000 77.08436  ?  189 ARG B NH2 1 
ATOM   3207 N  N   . ASP B 1 190 ? 11.04500  10.56300  36.03900  1.000 54.38797  ?  190 ASP B N   1 
ATOM   3208 C  CA  . ASP B 1 190 ? 10.22300  11.49100  36.80700  1.000 57.79629  ?  190 ASP B CA  1 
ATOM   3209 C  C   . ASP B 1 190 ? 9.42000   10.70900  37.83900  1.000 59.90989  ?  190 ASP B C   1 
ATOM   3210 O  O   . ASP B 1 190 ? 8.62000   9.83700   37.48100  1.000 59.85610  ?  190 ASP B O   1 
ATOM   3211 C  CB  . ASP B 1 190 ? 9.29400   12.29800  35.90000  1.000 58.51587  ?  190 ASP B CB  1 
ATOM   3212 C  CG  . ASP B 1 190 ? 8.66200   13.48700  36.61800  1.000 65.14042  ?  190 ASP B CG  1 
ATOM   3213 O  OD1 . ASP B 1 190 ? 8.44500   13.41200  37.84500  1.000 62.93733  ?  190 ASP B OD1 1 
ATOM   3214 O  OD2 . ASP B 1 190 ? 8.39200   14.51000  35.95600  1.000 71.94981  -1 190 ASP B OD2 1 
ATOM   3215 N  N   . LEU B 1 191 ? 9.65100   11.01300  39.11700  1.000 59.40162  ?  191 LEU B N   1 
ATOM   3216 C  CA  . LEU B 1 191 ? 9.00600   10.34400  40.24100  1.000 57.20127  ?  191 LEU B CA  1 
ATOM   3217 C  C   . LEU B 1 191 ? 7.58100   10.82000  40.50400  1.000 55.53960  ?  191 LEU B C   1 
ATOM   3218 O  O   . LEU B 1 191 ? 6.94200   10.30300  41.42800  1.000 52.97076  ?  191 LEU B O   1 
ATOM   3219 C  CB  . LEU B 1 191 ? 9.85100   10.53800  41.50100  1.000 51.90359  ?  191 LEU B CB  1 
ATOM   3220 C  CG  . LEU B 1 191 ? 11.25000  9.92900   41.43800  1.000 53.49623  ?  191 LEU B CG  1 
ATOM   3221 C  CD1 . LEU B 1 191 ? 12.01800  10.22400  42.71200  1.000 53.81663  ?  191 LEU B CD1 1 
ATOM   3222 C  CD2 . LEU B 1 191 ? 11.15300  8.43100   41.20900  1.000 54.08341  ?  191 LEU B CD2 1 
ATOM   3223 N  N   . ASP B 1 192 ? 7.07900   11.79600  39.74300  1.000 60.23348  ?  192 ASP B N   1 
ATOM   3224 C  CA  . ASP B 1 192 ? 5.67000   12.20200  39.79100  1.000 56.22234  ?  192 ASP B CA  1 
ATOM   3225 C  C   . ASP B 1 192 ? 5.29800   12.80800  41.14300  1.000 61.00913  ?  192 ASP B C   1 
ATOM   3226 O  O   . ASP B 1 192 ? 4.28500   12.45400  41.75000  1.000 64.75350  ?  192 ASP B O   1 
ATOM   3227 C  CB  . ASP B 1 192 ? 4.73000   11.04500  39.44400  1.000 57.29691  ?  192 ASP B CB  1 
ATOM   3228 C  CG  . ASP B 1 192 ? 3.41500   11.52500  38.85700  1.000 61.98816  ?  192 ASP B CG  1 
ATOM   3229 O  OD1 . ASP B 1 192 ? 3.29400   12.74200  38.59400  1.000 64.03145  ?  192 ASP B OD1 1 
ATOM   3230 O  OD2 . ASP B 1 192 ? 2.49900   10.69500  38.67100  1.000 61.80963  -1 192 ASP B OD2 1 
ATOM   3231 N  N   . VAL B 1 193 ? 6.13800   13.72100  41.62500  1.000 61.19005  ?  193 VAL B N   1 
ATOM   3232 C  CA  . VAL B 1 193 ? 5.83000   14.45600  42.84700  1.000 59.46290  ?  193 VAL B CA  1 
ATOM   3233 C  C   . VAL B 1 193 ? 5.87200   15.94800  42.54500  1.000 64.42753  ?  193 VAL B C   1 
ATOM   3234 O  O   . VAL B 1 193 ? 6.12700   16.76700  43.43500  1.000 66.02938  ?  193 VAL B O   1 
ATOM   3235 C  CB  . VAL B 1 193 ? 6.79800   14.08700  43.98700  1.000 50.03775  ?  193 VAL B CB  1 
ATOM   3236 C  CG1 . VAL B 1 193 ? 6.59300   12.64100  44.41000  1.000 46.22389  ?  193 VAL B CG1 1 
ATOM   3237 C  CG2 . VAL B 1 193 ? 8.24000   14.32500  43.56200  1.000 50.08855  ?  193 VAL B CG2 1 
ATOM   3238 N  N   . THR B 1 194 ? 5.61700   16.30600  41.28600  1.000 66.19589  ?  194 THR B N   1 
ATOM   3239 C  CA  . THR B 1 194 ? 5.71300   17.69400  40.84900  1.000 66.22522  ?  194 THR B CA  1 
ATOM   3240 C  C   . THR B 1 194 ? 4.63300   18.54000  41.51500  1.000 68.86688  ?  194 THR B C   1 
ATOM   3241 O  O   . THR B 1 194 ? 3.43800   18.26500  41.36100  1.000 64.50465  ?  194 THR B O   1 
ATOM   3242 C  CB  . THR B 1 194 ? 5.59400   17.77100  39.33000  1.000 64.48120  ?  194 THR B CB  1 
ATOM   3243 O  OG1 . THR B 1 194 ? 6.75100   17.17700  38.72900  1.000 80.08070  ?  194 THR B OG1 1 
ATOM   3244 C  CG2 . THR B 1 194 ? 5.47600   19.21300  38.87800  1.000 68.57160  ?  194 THR B CG2 1 
ATOM   3245 N  N   . ALA B 1 195 ? 5.05200   19.58200  42.23200  1.000 68.65923  ?  195 ALA B N   1 
ATOM   3246 C  CA  . ALA B 1 195 ? 4.16000   20.41400  43.02800  1.000 67.10276  ?  195 ALA B CA  1 
ATOM   3247 C  C   . ALA B 1 195 ? 4.28100   21.87700  42.62600  1.000 69.03070  ?  195 ALA B C   1 
ATOM   3248 O  O   . ALA B 1 195 ? 5.38300   22.36800  42.35800  1.000 67.56159  ?  195 ALA B O   1 
ATOM   3249 C  CB  . ALA B 1 195 ? 4.46000   20.26600  44.52200  1.000 69.60040  ?  195 ALA B CB  1 
ATOM   3250 N  N   . THR B 1 196 ? 3.13900   22.57100  42.59100  1.000 65.33434  ?  196 THR B N   1 
ATOM   3251 C  CA  . THR B 1 196 ? 3.10200   23.99800  42.29900  1.000 67.74098  ?  196 THR B CA  1 
ATOM   3252 C  C   . THR B 1 196 ? 2.48500   24.84200  43.40900  1.000 74.80362  ?  196 THR B C   1 
ATOM   3253 O  O   . THR B 1 196 ? 2.53600   26.07400  43.31700  1.000 77.04634  ?  196 THR B O   1 
ATOM   3254 C  CB  . THR B 1 196 ? 2.34200   24.26800  40.98900  1.000 73.54226  ?  196 THR B CB  1 
ATOM   3255 O  OG1 . THR B 1 196 ? 0.97900   23.84300  41.12100  1.000 71.61525  ?  196 THR B OG1 1 
ATOM   3256 C  CG2 . THR B 1 196 ? 2.99200   23.53100  39.82700  1.000 65.87853  ?  196 THR B CG2 1 
ATOM   3257 N  N   . ASN B 1 197 ? 1.90400   24.23000  44.44100  1.000 74.12367  ?  197 ASN B N   1 
ATOM   3258 C  CA  . ASN B 1 197 ? 1.35700   24.95700  45.58400  1.000 68.15127  ?  197 ASN B CA  1 
ATOM   3259 C  C   . ASN B 1 197 ? 1.29400   24.00000  46.77200  1.000 74.51106  ?  197 ASN B C   1 
ATOM   3260 O  O   . ASN B 1 197 ? 1.74700   22.85500  46.69300  1.000 70.69530  ?  197 ASN B O   1 
ATOM   3261 C  CB  . ASN B 1 197 ? -0.00900  25.58100  45.26600  1.000 70.72500  ?  197 ASN B CB  1 
ATOM   3262 C  CG  . ASN B 1 197 ? -1.01400  24.57400  44.74500  1.000 71.77977  ?  197 ASN B CG  1 
ATOM   3263 O  OD1 . ASN B 1 197 ? -1.16300  23.48200  45.29200  1.000 69.64594  ?  197 ASN B OD1 1 
ATOM   3264 N  ND2 . ASN B 1 197 ? -1.73200  24.95100  43.69400  1.000 75.34533  ?  197 ASN B ND2 1 
ATOM   3265 N  N   . ARG B 1 198 ? 0.71900   24.47900  47.88200  1.000 77.41577  ?  198 ARG B N   1 
ATOM   3266 C  CA  . ARG B 1 198 ? 0.72400   23.69500  49.11600  1.000 71.05180  ?  198 ARG B CA  1 
ATOM   3267 C  C   . ARG B 1 198 ? -0.12000  22.43300  48.97800  1.000 70.54879  ?  198 ARG B C   1 
ATOM   3268 O  O   . ARG B 1 198 ? 0.26700   21.36400  49.46300  1.000 71.45491  ?  198 ARG B O   1 
ATOM   3269 C  CB  . ARG B 1 198 ? 0.18300   24.52700  50.27600  1.000 78.12603  ?  198 ARG B CB  1 
ATOM   3270 C  CG  . ARG B 1 198 ? 0.89000   25.84000  50.53200  1.000 83.44948  ?  198 ARG B CG  1 
ATOM   3271 C  CD  . ARG B 1 198 ? 0.27500   26.51100  51.74700  1.000 86.94712  ?  198 ARG B CD  1 
ATOM   3272 N  NE  . ARG B 1 198 ? -1.14100  26.17500  51.85100  1.000 97.09233  ?  198 ARG B NE  1 
ATOM   3273 C  CZ  . ARG B 1 198 ? -1.99400  26.73000  52.70100  1.000 105.47658 ?  198 ARG B CZ  1 
ATOM   3274 N  NH1 . ARG B 1 198 ? -1.63500  27.73000  53.49200  1.000 102.95226 ?  198 ARG B NH1 1 
ATOM   3275 N  NH2 . ARG B 1 198 ? -3.21500  26.21500  52.81800  1.000 105.85211 ?  198 ARG B NH2 1 
ATOM   3276 N  N   . GLU B 1 199 ? -1.28100  22.53900  48.32500  1.000 70.78374  ?  199 GLU B N   1 
ATOM   3277 C  CA  . GLU B 1 199 ? -2.18400  21.39400  48.23900  1.000 68.73475  ?  199 GLU B CA  1 
ATOM   3278 C  C   . GLU B 1 199 ? -1.63300  20.31400  47.32000  1.000 66.25882  ?  199 GLU B C   1 
ATOM   3279 O  O   . GLU B 1 199 ? -1.69900  19.12300  47.64600  1.000 65.56682  ?  199 GLU B O   1 
ATOM   3280 C  CB  . GLU B 1 199 ? -3.57200  21.83900  47.77600  1.000 69.79111  ?  199 GLU B CB  1 
ATOM   3281 C  CG  . GLU B 1 199 ? -4.23600  22.87700  48.67500  1.000 70.64627  ?  199 GLU B CG  1 
ATOM   3282 C  CD  . GLU B 1 199 ? -3.81800  24.30000  48.35400  1.000 87.06042  ?  199 GLU B CD  1 
ATOM   3283 O  OE1 . GLU B 1 199 ? -2.63900  24.52000  48.00000  1.000 85.08984  ?  199 GLU B OE1 1 
ATOM   3284 O  OE2 . GLU B 1 199 ? -4.67300  25.20400  48.46400  1.000 97.84428  -1 199 GLU B OE2 1 
ATOM   3285 N  N   . THR B 1 200 ? -1.08200  20.70500  46.16900  1.000 65.43467  ?  200 THR B N   1 
ATOM   3286 C  CA  . THR B 1 200 ? -0.50100  19.71200  45.27200  1.000 68.65223  ?  200 THR B CA  1 
ATOM   3287 C  C   . THR B 1 200 ? 0.68100   19.00900  45.92300  1.000 65.45688  ?  200 THR B C   1 
ATOM   3288 O  O   . THR B 1 200 ? 0.88800   17.81200  45.69600  1.000 64.82197  ?  200 THR B O   1 
ATOM   3289 C  CB  . THR B 1 200 ? -0.09000  20.36300  43.95000  1.000 66.16130  ?  200 THR B CB  1 
ATOM   3290 O  OG1 . THR B 1 200 ? 0.79100   21.46400  44.20400  1.000 71.54365  ?  200 THR B OG1 1 
ATOM   3291 C  CG2 . THR B 1 200 ? -1.32100  20.86400  43.20600  1.000 57.76709  ?  200 THR B CG2 1 
ATOM   3292 N  N   . LEU B 1 201 ? 1.46500   19.73100  46.72700  1.000 67.44502  ?  201 LEU B N   1 
ATOM   3293 C  CA  . LEU B 1 201 ? 2.57700   19.10600  47.43800  1.000 67.17598  ?  201 LEU B CA  1 
ATOM   3294 C  C   . LEU B 1 201 ? 2.10900   17.92800  48.28300  1.000 62.33308  ?  201 LEU B C   1 
ATOM   3295 O  O   . LEU B 1 201 ? 2.74700   16.86900  48.29300  1.000 60.77383  ?  201 LEU B O   1 
ATOM   3296 C  CB  . LEU B 1 201 ? 3.27900   20.13200  48.32400  1.000 65.86136  ?  201 LEU B CB  1 
ATOM   3297 C  CG  . LEU B 1 201 ? 4.43400   19.57200  49.15400  1.000 66.11849  ?  201 LEU B CG  1 
ATOM   3298 C  CD1 . LEU B 1 201 ? 5.66400   19.34500  48.28500  1.000 63.33348  ?  201 LEU B CD1 1 
ATOM   3299 C  CD2 . LEU B 1 201 ? 4.74300   20.46200  50.34700  1.000 67.26939  ?  201 LEU B CD2 1 
ATOM   3300 N  N   . GLU B 1 202 ? 0.99700   18.07900  48.96200  1.000 65.69206  ?  202 GLU B N   1 
ATOM   3301 C  CA  . GLU B 1 202 ? 0.51000   16.99900  49.76700  1.000 67.95330  ?  202 GLU B CA  1 
ATOM   3302 C  C   . GLU B 1 202 ? 0.02600   15.87600  48.89400  1.000 64.76631  ?  202 GLU B C   1 
ATOM   3303 O  O   . GLU B 1 202 ? 0.53600   14.76900  48.97600  1.000 64.37153  ?  202 GLU B O   1 
ATOM   3304 C  CB  . GLU B 1 202 ? -0.62800  17.48000  50.64200  1.000 64.03269  ?  202 GLU B CB  1 
ATOM   3305 C  CG  . GLU B 1 202 ? -1.03600  16.48000  51.70200  1.000 70.51406  ?  202 GLU B CG  1 
ATOM   3306 C  CD  . GLU B 1 202 ? 0.08400   16.21500  52.67700  1.000 78.10651  ?  202 GLU B CD  1 
ATOM   3307 O  OE1 . GLU B 1 202 ? 0.62700   17.19500  53.22200  1.000 77.83794  ?  202 GLU B OE1 1 
ATOM   3308 O  OE2 . GLU B 1 202 ? 0.43000   15.03600  52.89200  1.000 73.54944  -1 202 GLU B OE2 1 
ATOM   3309 N  N   . GLN B 1 203 ? -0.95200  16.15200  48.04800  1.000 61.97786  ?  203 GLN B N   1 
ATOM   3310 C  CA  . GLN B 1 203 ? -1.53900  15.09400  47.23100  1.000 65.51963  ?  203 GLN B CA  1 
ATOM   3311 C  C   . GLN B 1 203 ? -0.46800  14.34400  46.45200  1.000 62.46433  ?  203 GLN B C   1 
ATOM   3312 O  O   . GLN B 1 203 ? -0.50000  13.11000  46.37200  1.000 59.56008  ?  203 GLN B O   1 
ATOM   3313 C  CB  . GLN B 1 203 ? -2.59800  15.66400  46.28600  1.000 64.64722  ?  203 GLN B CB  1 
ATOM   3314 C  CG  . GLN B 1 203 ? -3.27600  14.58600  45.44700  1.000 75.81494  ?  203 GLN B CG  1 
ATOM   3315 C  CD  . GLN B 1 203 ? -4.47200  15.08700  44.65400  1.000 82.74438  ?  203 GLN B CD  1 
ATOM   3316 O  OE1 . GLN B 1 203 ? -5.37200  14.31400  44.31500  1.000 75.60670  ?  203 GLN B OE1 1 
ATOM   3317 N  NE2 . GLN B 1 203 ? -4.48500  16.37900  44.34900  1.000 78.21615  ?  203 GLN B NE2 1 
ATOM   3318 N  N   . ARG B 1 204 ? 0.47300   15.07100  45.84500  1.000 58.33918  ?  204 ARG B N   1 
ATOM   3319 C  CA  . ARG B 1 204 ? 1.53600   14.40900  45.09700  1.000 54.82014  ?  204 ARG B CA  1 
ATOM   3320 C  C   . ARG B 1 204 ? 2.34200   13.46400  45.98300  1.000 59.70455  ?  204 ARG B C   1 
ATOM   3321 O  O   . ARG B 1 204 ? 2.61100   12.32100  45.59900  1.000 65.11979  ?  204 ARG B O   1 
ATOM   3322 C  CB  . ARG B 1 204 ? 2.45900   15.43000  44.42400  1.000 58.21296  ?  204 ARG B CB  1 
ATOM   3323 C  CG  . ARG B 1 204 ? 1.81800   16.18300  43.26000  1.000 69.98676  ?  204 ARG B CG  1 
ATOM   3324 C  CD  . ARG B 1 204 ? 0.80900   15.28900  42.57000  1.000 57.71383  ?  204 ARG B CD  1 
ATOM   3325 N  NE  . ARG B 1 204 ? 1.42000   14.08900  42.01800  1.000 52.05797  ?  204 ARG B NE  1 
ATOM   3326 C  CZ  . ARG B 1 204 ? 0.74900   12.97100  41.78700  1.000 56.00387  ?  204 ARG B CZ  1 
ATOM   3327 N  NH1 . ARG B 1 204 ? -0.54600  12.87900  42.04600  1.000 49.36461  ?  204 ARG B NH1 1 
ATOM   3328 N  NH2 . ARG B 1 204 ? 1.39800   11.90800  41.32200  1.000 67.37943  ?  204 ARG B NH2 1 
ATOM   3329 N  N   . TYR B 1 205 ? 2.75000   13.92800  47.16800  1.000 64.71865  ?  205 TYR B N   1 
ATOM   3330 C  CA  . TYR B 1 205 ? 3.54000   13.08200  48.05900  1.000 63.39667  ?  205 TYR B CA  1 
ATOM   3331 C  C   . TYR B 1 205 ? 2.77700   11.83000  48.48700  1.000 64.78198  ?  205 TYR B C   1 
ATOM   3332 O  O   . TYR B 1 205 ? 3.30000   10.71300  48.38900  1.000 66.03953  ?  205 TYR B O   1 
ATOM   3333 C  CB  . TYR B 1 205 ? 3.98800   13.87200  49.28700  1.000 64.87141  ?  205 TYR B CB  1 
ATOM   3334 C  CG  . TYR B 1 205 ? 4.61100   12.98500  50.34100  1.000 64.66456  ?  205 TYR B CG  1 
ATOM   3335 C  CD1 . TYR B 1 205 ? 5.85400   12.39900  50.13700  1.000 64.21080  ?  205 TYR B CD1 1 
ATOM   3336 C  CD2 . TYR B 1 205 ? 3.94900   12.71900  51.53200  1.000 66.51115  ?  205 TYR B CD2 1 
ATOM   3337 C  CE1 . TYR B 1 205 ? 6.42400   11.57800  51.09300  1.000 62.02157  ?  205 TYR B CE1 1 
ATOM   3338 C  CE2 . TYR B 1 205 ? 4.51000   11.90000  52.49400  1.000 63.43706  ?  205 TYR B CE2 1 
ATOM   3339 C  CZ  . TYR B 1 205 ? 5.74700   11.33300  52.27000  1.000 62.24405  ?  205 TYR B CZ  1 
ATOM   3340 O  OH  . TYR B 1 205 ? 6.30900   10.51800  53.22800  1.000 56.20284  ?  205 TYR B OH  1 
ATOM   3341 N  N   . ARG B 1 206 ? 1.54600   11.99600  48.98200  1.000 61.50245  ?  206 ARG B N   1 
ATOM   3342 C  CA  . ARG B 1 206 ? 0.75500   10.84100  49.40500  1.000 60.49314  ?  206 ARG B CA  1 
ATOM   3343 C  C   . ARG B 1 206 ? 0.52900   9.85800   48.26400  1.000 64.39749  ?  206 ARG B C   1 
ATOM   3344 O  O   . ARG B 1 206 ? 0.73000   8.64900   48.42500  1.000 61.67041  ?  206 ARG B O   1 
ATOM   3345 C  CB  . ARG B 1 206 ? -0.58000  11.30200  49.99200  1.000 65.03313  ?  206 ARG B CB  1 
ATOM   3346 C  CG  . ARG B 1 206 ? -0.44600  12.27900  51.14300  1.000 69.84717  ?  206 ARG B CG  1 
ATOM   3347 C  CD  . ARG B 1 206 ? 0.17200   11.56600  52.33600  1.000 75.39751  ?  206 ARG B CD  1 
ATOM   3348 N  NE  . ARG B 1 206 ? 0.31700   12.42100  53.50700  1.000 77.70358  ?  206 ARG B NE  1 
ATOM   3349 C  CZ  . ARG B 1 206 ? 0.91500   12.04200  54.62800  1.000 78.68335  ?  206 ARG B CZ  1 
ATOM   3350 N  NH1 . ARG B 1 206 ? 1.43000   10.83100  54.75800  1.000 80.25624  ?  206 ARG B NH1 1 
ATOM   3351 N  NH2 . ARG B 1 206 ? 0.99100   12.89600  55.64500  1.000 76.35275  ?  206 ARG B NH2 1 
ATOM   3352 N  N   . HIS B 1 207 ? 0.09200   10.35700  47.10600  1.000 66.52428  ?  207 HIS B N   1 
ATOM   3353 C  CA  . HIS B 1 207 ? -0.11000  9.47600   45.96100  1.000 63.21153  ?  207 HIS B CA  1 
ATOM   3354 C  C   . HIS B 1 207 ? 1.19900   8.83600   45.51700  1.000 60.73666  ?  207 HIS B C   1 
ATOM   3355 O  O   . HIS B 1 207 ? 1.21400   7.67900   45.07900  1.000 57.12984  ?  207 HIS B O   1 
ATOM   3356 C  CB  . HIS B 1 207 ? -0.78100  10.22900  44.81800  1.000 59.34401  ?  207 HIS B CB  1 
ATOM   3357 C  CG  . HIS B 1 207 ? -2.26200  10.36400  44.99200  1.000 58.53773  ?  207 HIS B CG  1 
ATOM   3358 N  ND1 . HIS B 1 207 ? -2.83900  11.41400  45.67200  1.000 65.97339  ?  207 HIS B ND1 1 
ATOM   3359 C  CD2 . HIS B 1 207 ? -3.28200  9.56700   44.59600  1.000 57.68973  ?  207 HIS B CD2 1 
ATOM   3360 C  CE1 . HIS B 1 207 ? -4.15200  11.26600  45.67500  1.000 68.78177  ?  207 HIS B CE1 1 
ATOM   3361 N  NE2 . HIS B 1 207 ? -4.44700  10.15300  45.02800  1.000 63.54632  ?  207 HIS B NE2 1 
ATOM   3362 N  N   . GLY B 1 208 ? 2.30200   9.58300   45.58900  1.000 56.37500  ?  208 GLY B N   1 
ATOM   3363 C  CA  . GLY B 1 208 ? 3.59800   9.00500   45.26900  1.000 58.00677  ?  208 GLY B CA  1 
ATOM   3364 C  C   . GLY B 1 208 ? 3.91400   7.76900   46.09100  1.000 65.65060  ?  208 GLY B C   1 
ATOM   3365 O  O   . GLY B 1 208 ? 4.36200   6.75100   45.55800  1.000 69.20484  ?  208 GLY B O   1 
ATOM   3366 N  N   . ILE B 1 209 ? 3.66700   7.83400   47.40200  1.000 63.36436  ?  209 ILE B N   1 
ATOM   3367 C  CA  . ILE B 1 209 ? 3.95700   6.69600   48.26900  1.000 64.74312  ?  209 ILE B CA  1 
ATOM   3368 C  C   . ILE B 1 209 ? 2.99200   5.55000   47.98900  1.000 65.79605  ?  209 ILE B C   1 
ATOM   3369 O  O   . ILE B 1 209 ? 3.40800   4.40200   47.78800  1.000 68.79151  ?  209 ILE B O   1 
ATOM   3370 C  CB  . ILE B 1 209 ? 3.91100   7.11900   49.74800  1.000 62.49225  ?  209 ILE B CB  1 
ATOM   3371 C  CG1 . ILE B 1 209 ? 4.85300   8.29800   49.99800  1.000 58.10983  ?  209 ILE B CG1 1 
ATOM   3372 C  CG2 . ILE B 1 209 ? 4.27400   5.94700   50.64600  1.000 51.46736  ?  209 ILE B CG2 1 
ATOM   3373 C  CD1 . ILE B 1 209 ? 6.30300   7.99300   49.70000  1.000 50.83357  ?  209 ILE B CD1 1 
ATOM   3374 N  N   . SER B 1 210 ? 1.68900   5.84500   47.97500  1.000 58.49413  ?  210 SER B N   1 
ATOM   3375 C  CA  . SER B 1 210 ? 0.68800   4.80900   47.73900  1.000 56.44175  ?  210 SER B CA  1 
ATOM   3376 C  C   . SER B 1 210 ? 0.89400   4.12700   46.38700  1.000 72.74503  ?  210 SER B C   1 
ATOM   3377 O  O   . SER B 1 210 ? 0.67000   2.91800   46.26000  1.000 76.50831  ?  210 SER B O   1 
ATOM   3378 C  CB  . SER B 1 210 ? -0.71900  5.39500   47.87000  1.000 51.78239  ?  210 SER B CB  1 
ATOM   3379 O  OG  . SER B 1 210 ? -0.98300  6.36600   46.87600  1.000 73.86979  ?  210 SER B OG  1 
ATOM   3380 N  N   . ASN B 1 211 ? 1.29000   4.88500   45.35900  1.000 68.04681  ?  211 ASN B N   1 
ATOM   3381 C  CA  . ASN B 1 211 ? 1.53900   4.26600   44.05900  1.000 73.34563  ?  211 ASN B CA  1 
ATOM   3382 C  C   . ASN B 1 211 ? 2.68500   3.26400   44.12800  1.000 76.77668  ?  211 ASN B C   1 
ATOM   3383 O  O   . ASN B 1 211 ? 2.65900   2.24600   43.42700  1.000 84.33078  ?  211 ASN B O   1 
ATOM   3384 C  CB  . ASN B 1 211 ? 1.84600   5.32300   42.99500  1.000 75.59631  ?  211 ASN B CB  1 
ATOM   3385 C  CG  . ASN B 1 211 ? 0.61000   6.06000   42.52200  1.000 71.27827  ?  211 ASN B CG  1 
ATOM   3386 O  OD1 . ASN B 1 211 ? -0.47800  5.49000   42.44100  1.000 69.88234  ?  211 ASN B OD1 1 
ATOM   3387 N  ND2 . ASN B 1 211 ? 0.78000   7.33100   42.16900  1.000 58.64651  ?  211 ASN B ND2 1 
ATOM   3388 N  N   . LEU B 1 212 ? 3.70000   3.53700   44.95500  1.000 72.83899  ?  212 LEU B N   1 
ATOM   3389 C  CA  . LEU B 1 212 ? 4.80600   2.59500   45.10500  1.000 74.11945  ?  212 LEU B CA  1 
ATOM   3390 C  C   . LEU B 1 212 ? 4.34800   1.29000   45.74100  1.000 78.93854  ?  212 LEU B C   1 
ATOM   3391 O  O   . LEU B 1 212 ? 4.95600   0.24100   45.50300  1.000 80.32985  ?  212 LEU B O   1 
ATOM   3392 C  CB  . LEU B 1 212 ? 5.93300   3.21700   45.93000  1.000 73.37352  ?  212 LEU B CB  1 
ATOM   3393 C  CG  . LEU B 1 212 ? 6.62300   4.45200   45.35000  1.000 75.94255  ?  212 LEU B CG  1 
ATOM   3394 C  CD1 . LEU B 1 212 ? 7.37200   5.20300   46.44100  1.000 72.69873  ?  212 LEU B CD1 1 
ATOM   3395 C  CD2 . LEU B 1 212 ? 7.56500   4.06400   44.21900  1.000 75.46662  ?  212 LEU B CD2 1 
ATOM   3396 N  N   . LYS B 1 213 ? 3.28900   1.33700   46.55700  1.000 79.61316  ?  213 LYS B N   1 
ATOM   3397 C  CA  . LYS B 1 213 ? 2.73800   0.12800   47.16000  1.000 84.00054  ?  213 LYS B CA  1 
ATOM   3398 C  C   . LYS B 1 213 ? 2.31100   -0.89300  46.11200  1.000 88.19028  ?  213 LYS B C   1 
ATOM   3399 O  O   . LYS B 1 213 ? 2.09600   -2.06200  46.45100  1.000 95.82901  ?  213 LYS B O   1 
ATOM   3400 C  CB  . LYS B 1 213 ? 1.53500   0.48500   48.03800  1.000 82.23089  ?  213 LYS B CB  1 
ATOM   3401 C  CG  . LYS B 1 213 ? 1.80700   1.54000   49.10200  1.000 77.63223  ?  213 LYS B CG  1 
ATOM   3402 C  CD  . LYS B 1 213 ? 2.47800   0.96500   50.33500  1.000 85.02968  ?  213 LYS B CD  1 
ATOM   3403 C  CE  . LYS B 1 213 ? 1.56500   -0.02600  51.04000  1.000 103.56895 ?  213 LYS B CE  1 
ATOM   3404 N  NZ  . LYS B 1 213 ? 2.11900   -0.45800  52.35600  1.000 88.82623  ?  213 LYS B NZ  1 
ATOM   3405 N  N   . LEU B 1 214 ? 2.18500   -0.47800  44.85400  1.000 85.87562  ?  214 LEU B N   1 
ATOM   3406 C  CA  . LEU B 1 214 ? 1.70900   -1.34200  43.78200  1.000 83.25474  ?  214 LEU B CA  1 
ATOM   3407 C  C   . LEU B 1 214 ? 2.83300   -1.69100  42.81200  1.000 77.54514  ?  214 LEU B C   1 
ATOM   3408 O  O   . LEU B 1 214 ? 3.81600   -2.33000  43.18600  1.000 79.08078  ?  214 LEU B O   1 
ATOM   3409 C  CB  . LEU B 1 214 ? 0.56300   -0.66200  43.03300  1.000 87.90036  ?  214 LEU B CB  1 
ATOM   3410 C  CG  . LEU B 1 214 ? -0.36200  0.22000   43.87900  1.000 82.25098  ?  214 LEU B CG  1 
ATOM   3411 C  CD1 . LEU B 1 214 ? -1.30700  1.01500   42.99000  1.000 80.89345  ?  214 LEU B CD1 1 
ATOM   3412 C  CD2 . LEU B 1 214 ? -1.14100  -0.61200  44.88700  1.000 78.07385  ?  214 LEU B CD2 1 
ATOM   3413 N  N   . MET C 1 1   ? 10.14600  30.24800  26.99500  1.000 113.95501 ?  1   MET C N   1 
ATOM   3414 C  CA  . MET C 1 1   ? 11.53600  29.83300  27.13600  1.000 104.75842 ?  1   MET C CA  1 
ATOM   3415 C  C   . MET C 1 1   ? 11.66400  28.30800  27.13900  1.000 98.13678  ?  1   MET C C   1 
ATOM   3416 O  O   . MET C 1 1   ? 10.69900  27.59400  26.86100  1.000 99.55676  ?  1   MET C O   1 
ATOM   3417 C  CB  . MET C 1 1   ? 12.14000  30.40800  28.42100  1.000 103.53021 ?  1   MET C CB  1 
ATOM   3418 C  CG  . MET C 1 1   ? 12.16100  31.93100  28.49500  1.000 111.91465 ?  1   MET C CG  1 
ATOM   3419 S  SD  . MET C 1 1   ? 13.29800  32.69500  27.32200  1.000 133.62470 ?  1   MET C SD  1 
ATOM   3420 C  CE  . MET C 1 1   ? 12.15800  33.29000  26.07600  1.000 124.98425 ?  1   MET C CE  1 
ATOM   3421 N  N   . LYS C 1 2   ? 12.86900  27.82800  27.43900  1.000 93.90953  ?  2   LYS C N   1 
ATOM   3422 C  CA  . LYS C 1 2   ? 13.10300  26.40200  27.63900  1.000 92.90558  ?  2   LYS C CA  1 
ATOM   3423 C  C   . LYS C 1 2   ? 12.27400  25.88200  28.80900  1.000 90.92127  ?  2   LYS C C   1 
ATOM   3424 O  O   . LYS C 1 2   ? 12.27800  26.46600  29.89300  1.000 93.39609  ?  2   LYS C O   1 
ATOM   3425 C  CB  . LYS C 1 2   ? 14.58500  26.12900  27.90000  1.000 86.25424  ?  2   LYS C CB  1 
ATOM   3426 C  CG  . LYS C 1 2   ? 15.44800  26.36700  26.67800  1.000 85.07778  ?  2   LYS C CG  1 
ATOM   3427 C  CD  . LYS C 1 2   ? 16.92500  26.23100  27.00100  1.000 72.78398  ?  2   LYS C CD  1 
ATOM   3428 C  CE  . LYS C 1 2   ? 17.33100  24.83400  27.41300  1.000 73.99782  ?  2   LYS C CE  1 
ATOM   3429 N  NZ  . LYS C 1 2   ? 18.79600  24.71200  27.60600  1.000 88.82679  ?  2   LYS C NZ  1 
ATOM   3430 N  N   . ASP C 1 3   ? 11.55500  24.78700  28.58500  1.000 83.43985  ?  3   ASP C N   1 
ATOM   3431 C  CA  . ASP C 1 3   ? 10.69700  24.20800  29.61000  1.000 88.60789  ?  3   ASP C CA  1 
ATOM   3432 C  C   . ASP C 1 3   ? 11.23000  22.84800  30.06600  1.000 87.91067  ?  3   ASP C C   1 
ATOM   3433 O  O   . ASP C 1 3   ? 12.24600  22.34700  29.57900  1.000 87.93372  ?  3   ASP C O   1 
ATOM   3434 C  CB  . ASP C 1 3   ? 9.26100   24.07400  29.09000  1.000 90.95341  ?  3   ASP C CB  1 
ATOM   3435 C  CG  . ASP C 1 3   ? 9.10700   22.98400  28.02900  1.000 99.30726  ?  3   ASP C CG  1 
ATOM   3436 O  OD1 . ASP C 1 3   ? 10.11800  22.52000  27.44900  1.000 96.79771  ?  3   ASP C OD1 1 
ATOM   3437 O  OD2 . ASP C 1 3   ? 7.95200   22.59800  27.76300  1.000 101.52928 -1 3   ASP C OD2 1 
ATOM   3438 N  N   . ILE C 1 4   ? 10.52300  22.26900  31.04300  1.000 83.19984  ?  4   ILE C N   1 
ATOM   3439 C  CA  . ILE C 1 4   ? 10.88600  20.95700  31.56900  1.000 81.78437  ?  4   ILE C CA  1 
ATOM   3440 C  C   . ILE C 1 4   ? 10.85800  19.91900  30.46000  1.000 80.93685  ?  4   ILE C C   1 
ATOM   3441 O  O   . ILE C 1 4   ? 11.74000  19.05500  30.37000  1.000 76.29284  ?  4   ILE C O   1 
ATOM   3442 C  CB  . ILE C 1 4   ? 9.95500   20.56800  32.74100  1.000 85.58543  ?  4   ILE C CB  1 
ATOM   3443 C  CG1 . ILE C 1 4   ? 10.30400  21.34800  34.00800  1.000 81.92895  ?  4   ILE C CG1 1 
ATOM   3444 C  CG2 . ILE C 1 4   ? 10.02800  19.06900  33.00500  1.000 83.12393  ?  4   ILE C CG2 1 
ATOM   3445 C  CD1 . ILE C 1 4   ? 11.68800  21.06200  34.54200  1.000 75.00770  ?  4   ILE C CD1 1 
ATOM   3446 N  N   . ASP C 1 5   ? 9.83800   19.98900  29.59700  1.000 86.39538  ?  5   ASP C N   1 
ATOM   3447 C  CA  . ASP C 1 5   ? 9.70600   19.02100  28.51100  1.000 87.06510  ?  5   ASP C CA  1 
ATOM   3448 C  C   . ASP C 1 5   ? 10.95200  18.99100  27.63800  1.000 76.32750  ?  5   ASP C C   1 
ATOM   3449 O  O   . ASP C 1 5   ? 11.37700  17.91900  27.18800  1.000 68.60774  ?  5   ASP C O   1 
ATOM   3450 C  CB  . ASP C 1 5   ? 8.48100   19.35300  27.65600  1.000 86.69495  ?  5   ASP C CB  1 
ATOM   3451 C  CG  . ASP C 1 5   ? 7.19700   19.40500  28.46200  1.000 100.78319 ?  5   ASP C CG  1 
ATOM   3452 O  OD1 . ASP C 1 5   ? 7.14700   18.78200  29.54600  1.000 105.60880 ?  5   ASP C OD1 1 
ATOM   3453 O  OD2 . ASP C 1 5   ? 6.24100   20.07400  28.01700  1.000 104.45278 -1 5   ASP C OD2 1 
ATOM   3454 N  N   . THR C 1 6   ? 11.54600  20.15800  27.38100  1.000 75.71461  ?  6   THR C N   1 
ATOM   3455 C  CA  . THR C 1 6   ? 12.80900  20.20400  26.65200  1.000 75.10093  ?  6   THR C CA  1 
ATOM   3456 C  C   . THR C 1 6   ? 13.89000  19.40100  27.36700  1.000 77.26785  ?  6   THR C C   1 
ATOM   3457 O  O   . THR C 1 6   ? 14.56000  18.56200  26.75600  1.000 75.92983  ?  6   THR C O   1 
ATOM   3458 C  CB  . THR C 1 6   ? 13.25600  21.65400  26.46000  1.000 76.80899  ?  6   THR C CB  1 
ATOM   3459 O  OG1 . THR C 1 6   ? 12.26100  22.37000  25.71700  1.000 78.82329  ?  6   THR C OG1 1 
ATOM   3460 C  CG2 . THR C 1 6   ? 14.57600  21.70100  25.70800  1.000 73.55033  ?  6   THR C CG2 1 
ATOM   3461 N  N   . LEU C 1 7   ? 14.06300  19.63700  28.67300  1.000 78.93903  ?  7   LEU C N   1 
ATOM   3462 C  CA  . LEU C 1 7   ? 15.11500  18.94900  29.42000  1.000 73.91615  ?  7   LEU C CA  1 
ATOM   3463 C  C   . LEU C 1 7   ? 14.89100  17.44400  29.44500  1.000 71.37891  ?  7   LEU C C   1 
ATOM   3464 O  O   . LEU C 1 7   ? 15.83900  16.66500  29.28800  1.000 70.83943  ?  7   LEU C O   1 
ATOM   3465 C  CB  . LEU C 1 7   ? 15.19000  19.49000  30.84700  1.000 76.76843  ?  7   LEU C CB  1 
ATOM   3466 C  CG  . LEU C 1 7   ? 15.16300  21.00700  30.99400  1.000 79.40998  ?  7   LEU C CG  1 
ATOM   3467 C  CD1 . LEU C 1 7   ? 15.47200  21.41100  32.42200  1.000 79.54432  ?  7   LEU C CD1 1 
ATOM   3468 C  CD2 . LEU C 1 7   ? 16.17800  21.59700  30.04700  1.000 81.62816  ?  7   LEU C CD2 1 
ATOM   3469 N  N   . ILE C 1 8   ? 13.64400  17.01600  29.64400  1.000 71.81869  ?  8   ILE C N   1 
ATOM   3470 C  CA  . ILE C 1 8   ? 13.34000  15.58900  29.63200  1.000 71.45896  ?  8   ILE C CA  1 
ATOM   3471 C  C   . ILE C 1 8   ? 13.66300  15.00300  28.26300  1.000 73.14575  ?  8   ILE C C   1 
ATOM   3472 O  O   . ILE C 1 8   ? 14.30900  13.95400  28.15000  1.000 69.60585  ?  8   ILE C O   1 
ATOM   3473 C  CB  . ILE C 1 8   ? 11.87000  15.35000  30.02100  1.000 70.88506  ?  8   ILE C CB  1 
ATOM   3474 C  CG1 . ILE C 1 8   ? 11.65600  15.63900  31.51000  1.000 69.52126  ?  8   ILE C CG1 1 
ATOM   3475 C  CG2 . ILE C 1 8   ? 11.45300  13.92500  29.68600  1.000 58.20503  ?  8   ILE C CG2 1 
ATOM   3476 C  CD1 . ILE C 1 8   ? 12.50500  14.79100  32.43400  1.000 65.19068  ?  8   ILE C CD1 1 
ATOM   3477 N  N   . SER C 1 9   ? 13.22200  15.68700  27.20300  1.000 75.58776  ?  9   SER C N   1 
ATOM   3478 C  CA  . SER C 1 9   ? 13.46900  15.21500  25.84400  1.000 70.70939  ?  9   SER C CA  1 
ATOM   3479 C  C   . SER C 1 9   ? 14.95900  15.20900  25.51700  1.000 68.62982  ?  9   SER C C   1 
ATOM   3480 O  O   . SER C 1 9   ? 15.46000  14.26100  24.90200  1.000 70.98759  ?  9   SER C O   1 
ATOM   3481 C  CB  . SER C 1 9   ? 12.70200  16.08200  24.84600  1.000 68.00271  ?  9   SER C CB  1 
ATOM   3482 O  OG  . SER C 1 9   ? 12.96500  15.68200  23.51500  1.000 82.32053  ?  9   SER C OG  1 
ATOM   3483 N  N   . ASN C 1 10  ? 15.67900  16.26800  25.90200  1.000 67.01676  ?  10  ASN C N   1 
ATOM   3484 C  CA  . ASN C 1 10  ? 17.12700  16.29300  25.70100  1.000 67.20533  ?  10  ASN C CA  1 
ATOM   3485 C  C   . ASN C 1 10  ? 17.79800  15.09400  26.36000  1.000 74.76308  ?  10  ASN C C   1 
ATOM   3486 O  O   . ASN C 1 10  ? 18.76100  14.53700  25.82000  1.000 79.58566  ?  10  ASN C O   1 
ATOM   3487 C  CB  . ASN C 1 10  ? 17.72200  17.59200  26.24700  1.000 69.65625  ?  10  ASN C CB  1 
ATOM   3488 C  CG  . ASN C 1 10  ? 17.19800  18.82300  25.53700  1.000 75.78677  ?  10  ASN C CG  1 
ATOM   3489 O  OD1 . ASN C 1 10  ? 16.52300  18.72400  24.51300  1.000 84.22325  ?  10  ASN C OD1 1 
ATOM   3490 N  ND2 . ASN C 1 10  ? 17.50400  19.99500  26.08300  1.000 80.51383  ?  10  ASN C ND2 1 
ATOM   3491 N  N   . ASN C 1 11  ? 17.30500  14.68600  27.53200  1.000 72.91858  ?  11  ASN C N   1 
ATOM   3492 C  CA  . ASN C 1 11  ? 17.90000  13.55900  28.24300  1.000 70.98342  ?  11  ASN C CA  1 
ATOM   3493 C  C   . ASN C 1 11  ? 17.70100  12.24900  27.49000  1.000 70.62880  ?  11  ASN C C   1 
ATOM   3494 O  O   . ASN C 1 11  ? 18.64000  11.45600  27.35000  1.000 72.06277  ?  11  ASN C O   1 
ATOM   3495 C  CB  . ASN C 1 11  ? 17.31100  13.45400  29.64700  1.000 68.40348  ?  11  ASN C CB  1 
ATOM   3496 C  CG  . ASN C 1 11  ? 17.78900  12.22000  30.38100  1.000 65.41130  ?  11  ASN C CG  1 
ATOM   3497 O  OD1 . ASN C 1 11  ? 17.03700  11.26300  30.56300  1.000 61.72241  ?  11  ASN C OD1 1 
ATOM   3498 N  ND2 . ASN C 1 11  ? 19.05100  12.22900  30.79300  1.000 65.10867  ?  11  ASN C ND2 1 
ATOM   3499 N  N   . ALA C 1 12  ? 16.48100  11.99700  27.00800  1.000 73.45145  ?  12  ALA C N   1 
ATOM   3500 C  CA  . ALA C 1 12  ? 16.22000  10.75300  26.29100  1.000 78.33749  ?  12  ALA C CA  1 
ATOM   3501 C  C   . ALA C 1 12  ? 17.06400  10.66000  25.02700  1.000 83.17758  ?  12  ALA C C   1 
ATOM   3502 O  O   . ALA C 1 12  ? 17.63900  9.60500   24.73100  1.000 85.57670  ?  12  ALA C O   1 
ATOM   3503 C  CB  . ALA C 1 12  ? 14.73200  10.64200  25.95700  1.000 78.34891  ?  12  ALA C CB  1 
ATOM   3504 N  N   . LEU C 1 13  ? 17.14100  11.75300  24.26600  1.000 82.25776  ?  13  LEU C N   1 
ATOM   3505 C  CA  . LEU C 1 13  ? 17.98800  11.79000  23.07800  1.000 86.54298  ?  13  LEU C CA  1 
ATOM   3506 C  C   . LEU C 1 13  ? 19.45000  11.53800  23.42900  1.000 89.34470  ?  13  LEU C C   1 
ATOM   3507 O  O   . LEU C 1 13  ? 20.07300  10.60200  22.91500  1.000 94.40654  ?  13  LEU C O   1 
ATOM   3508 C  CB  . LEU C 1 13  ? 17.82700  13.13300  22.36700  1.000 83.23050  ?  13  LEU C CB  1 
ATOM   3509 C  CG  . LEU C 1 13  ? 18.39900  13.17300  20.95000  1.000 91.36566  ?  13  LEU C CG  1 
ATOM   3510 C  CD1 . LEU C 1 13  ? 17.75500  12.10600  20.07700  1.000 91.79730  ?  13  LEU C CD1 1 
ATOM   3511 C  CD2 . LEU C 1 13  ? 18.23300  14.55500  20.33700  1.000 80.51734  ?  13  LEU C CD2 1 
ATOM   3512 N  N   . TRP C 1 14  ? 20.01800  12.38500  24.29500  1.000 84.64148  ?  14  TRP C N   1 
ATOM   3513 C  CA  . TRP C 1 14  ? 21.40500  12.22400  24.73000  1.000 81.08154  ?  14  TRP C CA  1 
ATOM   3514 C  C   . TRP C 1 14  ? 21.68500  10.80200  25.20500  1.000 82.10253  ?  14  TRP C C   1 
ATOM   3515 O  O   . TRP C 1 14  ? 22.76900  10.25900  24.96500  1.000 80.49465  ?  14  TRP C O   1 
ATOM   3516 C  CB  . TRP C 1 14  ? 21.71000  13.24100  25.83400  1.000 78.64564  ?  14  TRP C CB  1 
ATOM   3517 C  CG  . TRP C 1 14  ? 23.00200  13.03200  26.57400  1.000 85.47076  ?  14  TRP C CG  1 
ATOM   3518 C  CD1 . TRP C 1 14  ? 24.23300  13.50400  26.22400  1.000 84.36644  ?  14  TRP C CD1 1 
ATOM   3519 C  CD2 . TRP C 1 14  ? 23.18000  12.32800  27.81100  1.000 82.52686  ?  14  TRP C CD2 1 
ATOM   3520 N  NE1 . TRP C 1 14  ? 25.16900  13.12400  27.15500  1.000 85.14539  ?  14  TRP C NE1 1 
ATOM   3521 C  CE2 . TRP C 1 14  ? 24.54800  12.40200  28.14000  1.000 80.59742  ?  14  TRP C CE2 1 
ATOM   3522 C  CE3 . TRP C 1 14  ? 22.31800  11.63500  28.66600  1.000 81.06731  ?  14  TRP C CE3 1 
ATOM   3523 C  CZ2 . TRP C 1 14  ? 25.07400  11.80900  29.28600  1.000 83.49526  ?  14  TRP C CZ2 1 
ATOM   3524 C  CZ3 . TRP C 1 14  ? 22.84200  11.04800  29.80400  1.000 86.09982  ?  14  TRP C CZ3 1 
ATOM   3525 C  CH2 . TRP C 1 14  ? 24.20700  11.13800  30.10300  1.000 85.72316  ?  14  TRP C CH2 1 
ATOM   3526 N  N   . SER C 1 15  ? 20.71100  10.18200  25.87600  1.000 85.21913  ?  15  SER C N   1 
ATOM   3527 C  CA  . SER C 1 15  ? 20.88900  8.82300   26.38000  1.000 90.83398  ?  15  SER C CA  1 
ATOM   3528 C  C   . SER C 1 15  ? 20.99900  7.81300   25.24300  1.000 92.69012  ?  15  SER C C   1 
ATOM   3529 O  O   . SER C 1 15  ? 21.94200  7.01200   25.19900  1.000 97.19229  ?  15  SER C O   1 
ATOM   3530 C  CB  . SER C 1 15  ? 19.73200  8.46000   27.31000  1.000 82.74207  ?  15  SER C CB  1 
ATOM   3531 O  OG  . SER C 1 15  ? 20.01000  7.27600   28.03600  1.000 78.13927  ?  15  SER C OG  1 
ATOM   3532 N  N   . LYS C 1 16  ? 20.03300  7.82800   24.32200  1.000 93.46416  ?  16  LYS C N   1 
ATOM   3533 C  CA  . LYS C 1 16  ? 20.03700  6.87600   23.21500  1.000 101.43787 ?  16  LYS C CA  1 
ATOM   3534 C  C   . LYS C 1 16  ? 21.27500  7.05300   22.34600  1.000 100.97525 ?  16  LYS C C   1 
ATOM   3535 O  O   . LYS C 1 16  ? 21.96200  6.07900   22.02000  1.000 100.44141 ?  16  LYS C O   1 
ATOM   3536 C  CB  . LYS C 1 16  ? 18.76200  7.05400   22.38900  1.000 92.48608  ?  16  LYS C CB  1 
ATOM   3537 C  CG  . LYS C 1 16  ? 17.50100  6.72400   23.16000  1.000 101.02923 ?  16  LYS C CG  1 
ATOM   3538 C  CD  . LYS C 1 16  ? 16.25300  7.21600   22.45000  1.000 94.24873  ?  16  LYS C CD  1 
ATOM   3539 C  CE  . LYS C 1 16  ? 15.03200  7.03200   23.33600  1.000 92.07959  ?  16  LYS C CE  1 
ATOM   3540 N  NZ  . LYS C 1 16  ? 14.85500  5.61400   23.75000  1.000 101.97306 ?  16  LYS C NZ  1 
ATOM   3541 N  N   . MET C 1 17  ? 21.55400  8.29700   21.93800  1.000 99.68360  ?  17  MET C N   1 
ATOM   3542 C  CA  . MET C 1 17  ? 22.74800  8.61200   21.15600  1.000 98.93644  ?  17  MET C CA  1 
ATOM   3543 C  C   . MET C 1 17  ? 24.00100  8.02200   21.79600  1.000 100.32474 ?  17  MET C C   1 
ATOM   3544 O  O   . MET C 1 17  ? 24.85300  7.45400   21.10600  1.000 104.39934 ?  17  MET C O   1 
ATOM   3545 C  CB  . MET C 1 17  ? 22.89700  10.12200  20.99100  1.000 101.10579 ?  17  MET C CB  1 
ATOM   3546 C  CG  . MET C 1 17  ? 21.79400  10.71000  20.15100  1.000 103.45634 ?  17  MET C CG  1 
ATOM   3547 S  SD  . MET C 1 17  ? 21.77400  12.50700  20.12800  1.000 124.73205 ?  17  MET C SD  1 
ATOM   3548 C  CE  . MET C 1 17  ? 22.99700  12.87800  18.87400  1.000 94.52322  ?  17  MET C CE  1 
ATOM   3549 N  N   . LEU C 1 18  ? 24.11700  8.11200   23.10500  1.000 102.66160 ?  18  LEU C N   1 
ATOM   3550 C  CA  . LEU C 1 18  ? 25.31300  7.59800   23.73700  1.000 105.54651 ?  18  LEU C CA  1 
ATOM   3551 C  C   . LEU C 1 18  ? 25.36300  6.09500   23.57700  1.000 108.44039 ?  18  LEU C C   1 
ATOM   3552 O  O   . LEU C 1 18  ? 26.39400  5.53900   23.21900  1.000 113.96656 ?  18  LEU C O   1 
ATOM   3553 C  CB  . LEU C 1 18  ? 25.36500  7.97200   25.21000  1.000 96.05685  ?  18  LEU C CB  1 
ATOM   3554 C  CG  . LEU C 1 18  ? 26.33100  9.09900   25.55900  1.000 92.43865  ?  18  LEU C CG  1 
ATOM   3555 C  CD1 . LEU C 1 18  ? 26.03000  10.33100  24.72100  1.000 90.29052  ?  18  LEU C CD1 1 
ATOM   3556 C  CD2 . LEU C 1 18  ? 26.24700  9.42900   27.03700  1.000 97.72991  ?  18  LEU C CD2 1 
ATOM   3557 N  N   . VAL C 1 19  ? 24.25400  5.43000   23.84700  1.000 106.00030 ?  19  VAL C N   1 
ATOM   3558 C  CA  . VAL C 1 19  ? 24.22100  3.98700   23.62200  1.000 107.58253 ?  19  VAL C CA  1 
ATOM   3559 C  C   . VAL C 1 19  ? 24.73100  3.66500   22.22300  1.000 112.34388 ?  19  VAL C C   1 
ATOM   3560 O  O   . VAL C 1 19  ? 25.46300  2.68900   22.01500  1.000 116.41761 ?  19  VAL C O   1 
ATOM   3561 C  CB  . VAL C 1 19  ? 22.79700  3.44400   23.84700  1.000 107.35004 ?  19  VAL C CB  1 
ATOM   3562 C  CG1 . VAL C 1 19  ? 22.73400  1.96100   23.51400  1.000 106.72371 ?  19  VAL C CG1 1 
ATOM   3563 C  CG2 . VAL C 1 19  ? 22.35900  3.69100   25.28000  1.000 107.84679 ?  19  VAL C CG2 1 
ATOM   3564 N  N   . GLU C 1 20  ? 24.34700  4.48900   21.24600  1.000 113.48018 ?  20  GLU C N   1 
ATOM   3565 C  CA  . GLU C 1 20  ? 24.80000  4.32000   19.87000  1.000 115.14863 ?  20  GLU C CA  1 
ATOM   3566 C  C   . GLU C 1 20  ? 26.31100  4.46900   19.75100  1.000 116.11358 ?  20  GLU C C   1 
ATOM   3567 O  O   . GLU C 1 20  ? 26.97700  3.65300   19.10200  1.000 120.65120 ?  20  GLU C O   1 
ATOM   3568 C  CB  . GLU C 1 20  ? 24.10500  5.35100   18.98300  1.000 113.19261 ?  20  GLU C CB  1 
ATOM   3569 C  CG  . GLU C 1 20  ? 24.51100  5.33300   17.52600  1.000 116.60285 ?  20  GLU C CG  1 
ATOM   3570 C  CD  . GLU C 1 20  ? 23.85200  6.45000   16.74700  1.000 122.87529 ?  20  GLU C CD  1 
ATOM   3571 O  OE1 . GLU C 1 20  ? 23.16200  7.29400   17.36800  1.000 116.90510 ?  20  GLU C OE1 1 
ATOM   3572 O  OE2 . GLU C 1 20  ? 24.04100  6.49900   15.51300  1.000 132.29836 -1 20  GLU C OE2 1 
ATOM   3573 N  N   . GLU C 1 21  ? 26.87500  5.50700   20.36900  1.000 113.75470 ?  21  GLU C N   1 
ATOM   3574 C  CA  . GLU C 1 21  ? 28.28700  5.79400   20.15000  1.000 113.31379 ?  21  GLU C CA  1 
ATOM   3575 C  C   . GLU C 1 21  ? 29.16000  4.92200   21.04600  1.000 112.68861 ?  21  GLU C C   1 
ATOM   3576 O  O   . GLU C 1 21  ? 29.97700  4.13500   20.55700  1.000 115.00192 ?  21  GLU C O   1 
ATOM   3577 C  CB  . GLU C 1 21  ? 28.56400  7.27400   20.41100  1.000 114.05753 ?  21  GLU C CB  1 
ATOM   3578 C  CG  . GLU C 1 21  ? 27.77400  8.22000   19.51300  1.000 119.55415 ?  21  GLU C CG  1 
ATOM   3579 C  CD  . GLU C 1 21  ? 27.98600  7.97600   18.02900  1.000 125.77126 ?  21  GLU C CD  1 
ATOM   3580 O  OE1 . GLU C 1 21  ? 29.12700  7.68800   17.61200  1.000 131.13203 ?  21  GLU C OE1 1 
ATOM   3581 O  OE2 . GLU C 1 21  ? 26.99700  8.08600   17.27300  1.000 123.32907 -1 21  GLU C OE2 1 
ATOM   3582 N  N   . ASP C 1 22  ? 28.99000  5.04300   22.36200  1.000 115.00775 ?  22  ASP C N   1 
ATOM   3583 C  CA  . ASP C 1 22  ? 29.76200  4.27900   23.33700  1.000 112.90997 ?  22  ASP C CA  1 
ATOM   3584 C  C   . ASP C 1 22  ? 28.79100  3.62800   24.31200  1.000 111.66470 ?  22  ASP C C   1 
ATOM   3585 O  O   . ASP C 1 22  ? 28.39600  4.24200   25.31200  1.000 111.78840 ?  22  ASP C O   1 
ATOM   3586 C  CB  . ASP C 1 22  ? 30.77400  5.16500   24.05800  1.000 112.58302 ?  22  ASP C CB  1 
ATOM   3587 C  CG  . ASP C 1 22  ? 31.59200  4.40400   25.08400  1.000 114.31737 ?  22  ASP C CG  1 
ATOM   3588 O  OD1 . ASP C 1 22  ? 31.58900  3.15700   25.04700  1.000 112.79632 ?  22  ASP C OD1 1 
ATOM   3589 O  OD2 . ASP C 1 22  ? 32.25800  5.05800   25.91400  1.000 117.34906 -1 22  ASP C OD2 1 
ATOM   3590 N  N   . PRO C 1 23  ? 28.38000  2.38200   24.05500  1.000 109.93528 ?  23  PRO C N   1 
ATOM   3591 C  CA  . PRO C 1 23  ? 27.50800  1.69000   25.01400  1.000 113.05972 ?  23  PRO C CA  1 
ATOM   3592 C  C   . PRO C 1 23  ? 28.23900  1.24600   26.26800  1.000 112.84116 ?  23  PRO C C   1 
ATOM   3593 O  O   . PRO C 1 23  ? 27.58700  0.80200   27.22200  1.000 107.48909 ?  23  PRO C O   1 
ATOM   3594 C  CB  . PRO C 1 23  ? 26.99600  0.48600   24.21500  1.000 100.90335 ?  23  PRO C CB  1 
ATOM   3595 C  CG  . PRO C 1 23  ? 28.09200  0.20300   23.23600  1.000 106.01742 ?  23  PRO C CG  1 
ATOM   3596 C  CD  . PRO C 1 23  ? 28.78700  1.51100   22.93800  1.000 111.98271 ?  23  PRO C CD  1 
ATOM   3597 N  N   . GLY C 1 24  ? 29.56500  1.34700   26.28800  1.000 112.60063 ?  24  GLY C N   1 
ATOM   3598 C  CA  . GLY C 1 24  ? 30.36100  1.04100   27.45900  1.000 110.75116 ?  24  GLY C CA  1 
ATOM   3599 C  C   . GLY C 1 24  ? 30.56300  2.23600   28.36900  1.000 113.72799 ?  24  GLY C C   1 
ATOM   3600 O  O   . GLY C 1 24  ? 30.99800  2.08100   29.51400  1.000 113.01490 ?  24  GLY C O   1 
ATOM   3601 N  N   . PHE C 1 25  ? 30.27000  3.43600   27.85400  1.000 112.36967 ?  25  PHE C N   1 
ATOM   3602 C  CA  . PHE C 1 25  ? 30.42400  4.66100   28.63700  1.000 110.61378 ?  25  PHE C CA  1 
ATOM   3603 C  C   . PHE C 1 25  ? 29.72200  4.56400   29.98600  1.000 108.12443 ?  25  PHE C C   1 
ATOM   3604 O  O   . PHE C 1 25  ? 30.29200  4.92200   31.02300  1.000 108.45432 ?  25  PHE C O   1 
ATOM   3605 C  CB  . PHE C 1 25  ? 29.89600  5.85900   27.84500  1.000 107.21702 ?  25  PHE C CB  1 
ATOM   3606 C  CG  . PHE C 1 25  ? 29.68500  7.09100   28.68200  1.000 105.01688 ?  25  PHE C CG  1 
ATOM   3607 C  CD1 . PHE C 1 25  ? 30.76000  7.87000   29.07800  1.000 105.07212 ?  25  PHE C CD1 1 
ATOM   3608 C  CD2 . PHE C 1 25  ? 28.41000  7.47400   29.06400  1.000 104.67683 ?  25  PHE C CD2 1 
ATOM   3609 C  CE1 . PHE C 1 25  ? 30.56800  9.00300   29.84900  1.000 100.30458 ?  25  PHE C CE1 1 
ATOM   3610 C  CE2 . PHE C 1 25  ? 28.21200  8.60700   29.83400  1.000 101.79258 ?  25  PHE C CE2 1 
ATOM   3611 C  CZ  . PHE C 1 25  ? 29.29200  9.37200   30.22500  1.000 100.24662 ?  25  PHE C CZ  1 
ATOM   3612 N  N   . PHE C 1 26  ? 28.47400  4.09300   29.99000  1.000 105.86655 ?  26  PHE C N   1 
ATOM   3613 C  CA  . PHE C 1 26  ? 27.75500  3.94500   31.25100  1.000 107.19834 ?  26  PHE C CA  1 
ATOM   3614 C  C   . PHE C 1 26  ? 28.33900  2.83700   32.12100  1.000 111.23571 ?  26  PHE C C   1 
ATOM   3615 O  O   . PHE C 1 26  ? 28.19300  2.88000   33.34800  1.000 114.85394 ?  26  PHE C O   1 
ATOM   3616 C  CB  . PHE C 1 26  ? 26.27100  3.70800   30.97500  1.000 100.34757 ?  26  PHE C CB  1 
ATOM   3617 C  CG  . PHE C 1 26  ? 25.64500  4.76100   30.10500  1.000 96.25654  ?  26  PHE C CG  1 
ATOM   3618 C  CD1 . PHE C 1 26  ? 25.39700  6.02700   30.61400  1.000 92.35943  ?  26  PHE C CD1 1 
ATOM   3619 C  CD2 . PHE C 1 26  ? 25.31400  4.49700   28.78700  1.000 104.40576 ?  26  PHE C CD2 1 
ATOM   3620 C  CE1 . PHE C 1 26  ? 24.82300  7.00700   29.82900  1.000 92.97790  ?  26  PHE C CE1 1 
ATOM   3621 C  CE2 . PHE C 1 26  ? 24.73900  5.47500   27.99300  1.000 105.24537 ?  26  PHE C CE2 1 
ATOM   3622 C  CZ  . PHE C 1 26  ? 24.49400  6.73200   28.51600  1.000 102.21290 ?  26  PHE C CZ  1 
ATOM   3623 N  N   . GLU C 1 27  ? 29.00100  1.84500   31.52100  1.000 113.30955 ?  27  GLU C N   1 
ATOM   3624 C  CA  . GLU C 1 27  ? 29.71200  0.85000   32.32100  1.000 114.64052 ?  27  GLU C CA  1 
ATOM   3625 C  C   . GLU C 1 27  ? 30.95600  1.45100   32.96600  1.000 116.88291 ?  27  GLU C C   1 
ATOM   3626 O  O   . GLU C 1 27  ? 31.31400  1.09200   34.09400  1.000 117.61430 ?  27  GLU C O   1 
ATOM   3627 C  CB  . GLU C 1 27  ? 30.06300  -0.37300  31.47600  1.000 113.81054 ?  27  GLU C CB  1 
ATOM   3628 C  CG  . GLU C 1 27  ? 28.84200  -1.11100  30.95100  1.000 117.46821 ?  27  GLU C CG  1 
ATOM   3629 C  CD  . GLU C 1 27  ? 29.19900  -2.29100  30.07100  1.000 118.70626 ?  27  GLU C CD  1 
ATOM   3630 O  OE1 . GLU C 1 27  ? 30.37400  -2.39600  29.66200  1.000 118.12174 ?  27  GLU C OE1 1 
ATOM   3631 O  OE2 . GLU C 1 27  ? 28.30300  -3.11700  29.79400  1.000 115.83655 -1 27  GLU C OE2 1 
ATOM   3632 N  N   . LYS C 1 28  ? 31.61200  2.34000   32.24600  1.000 118.42318 ?  28  LYS C N   1 
ATOM   3633 C  CA  . LYS C 1 28  ? 32.79300  2.96900   32.78400  1.000 117.48147 ?  28  LYS C CA  1 
ATOM   3634 C  C   . LYS C 1 28  ? 32.43000  3.65400   34.07400  1.000 112.88860 ?  28  LYS C C   1 
ATOM   3635 O  O   . LYS C 1 28  ? 33.16600  3.58500   35.05100  1.000 114.35099 ?  28  LYS C O   1 
ATOM   3636 C  CB  . LYS C 1 28  ? 33.34400  3.97000   31.77900  1.000 112.48806 ?  28  LYS C CB  1 
ATOM   3637 C  CG  . LYS C 1 28  ? 33.92400  3.31500   30.54200  1.000 111.08581 ?  28  LYS C CG  1 
ATOM   3638 C  CD  . LYS C 1 28  ? 33.74600  4.18600   29.31400  1.000 114.18254 ?  28  LYS C CD  1 
ATOM   3639 C  CE  . LYS C 1 28  ? 33.83400  3.35500   28.04600  1.000 113.41248 ?  28  LYS C CE  1 
ATOM   3640 N  NZ  . LYS C 1 28  ? 34.58000  4.05800   26.96700  1.000 116.99785 ?  28  LYS C NZ  1 
ATOM   3641 N  N   . LEU C 1 29  ? 31.28300  4.30800   34.08400  1.000 111.40164 ?  29  LEU C N   1 
ATOM   3642 C  CA  . LEU C 1 29  ? 30.87500  5.02100   35.26400  1.000 112.01950 ?  29  LEU C CA  1 
ATOM   3643 C  C   . LEU C 1 29  ? 31.06400  4.11700   36.44500  1.000 112.79496 ?  29  LEU C C   1 
ATOM   3644 O  O   . LEU C 1 29  ? 31.66600  4.49700   37.43800  1.000 115.01371 ?  29  LEU C O   1 
ATOM   3645 C  CB  . LEU C 1 29  ? 29.41900  5.43300   35.15500  1.000 110.70611 ?  29  LEU C CB  1 
ATOM   3646 C  CG  . LEU C 1 29  ? 29.14800  6.69000   34.33600  1.000 107.26617 ?  29  LEU C CG  1 
ATOM   3647 C  CD1 . LEU C 1 29  ? 27.76300  6.63300   33.71500  1.000 105.80532 ?  29  LEU C CD1 1 
ATOM   3648 C  CD2 . LEU C 1 29  ? 29.29800  7.92200   35.21300  1.000 94.70799  ?  29  LEU C CD2 1 
ATOM   3649 N  N   . ALA C 1 30  ? 30.55100  2.90700   36.33800  1.000 112.57046 ?  30  ALA C N   1 
ATOM   3650 C  CA  . ALA C 1 30  ? 30.67700  1.97400   37.43300  1.000 113.35788 ?  30  ALA C CA  1 
ATOM   3651 C  C   . ALA C 1 30  ? 32.13000  1.80100   37.80000  1.000 115.11862 ?  30  ALA C C   1 
ATOM   3652 O  O   . ALA C 1 30  ? 32.55000  2.19600   38.88300  1.000 111.70504 ?  30  ALA C O   1 
ATOM   3653 C  CB  . ALA C 1 30  ? 30.07300  0.64400   37.05300  1.000 112.06454 ?  30  ALA C CB  1 
ATOM   3654 N  N   . GLN C 1 31  ? 32.90400  1.21700   36.89800  1.000 116.72723 ?  31  GLN C N   1 
ATOM   3655 C  CA  . GLN C 1 31  ? 34.31300  0.97100   37.17100  1.000 116.03872 ?  31  GLN C CA  1 
ATOM   3656 C  C   . GLN C 1 31  ? 34.97900  2.17300   37.79000  1.000 117.95382 ?  31  GLN C C   1 
ATOM   3657 O  O   . GLN C 1 31  ? 35.81500  2.03500   38.67600  1.000 118.43555 ?  31  GLN C O   1 
ATOM   3658 C  CB  . GLN C 1 31  ? 35.04200  0.61200   35.88600  1.000 114.54204 ?  31  GLN C CB  1 
ATOM   3659 C  CG  . GLN C 1 31  ? 34.65300  -0.73900  35.32000  1.000 119.38797 ?  31  GLN C CG  1 
ATOM   3660 C  CD  . GLN C 1 31  ? 33.63100  -0.62400  34.21200  1.000 121.42083 ?  31  GLN C CD  1 
ATOM   3661 O  OE1 . GLN C 1 31  ? 33.87800  0.01300   33.18800  1.000 117.70856 ?  31  GLN C OE1 1 
ATOM   3662 N  NE2 . GLN C 1 31  ? 32.46900  -1.23600  34.41200  1.000 118.95220 ?  31  GLN C NE2 1 
ATOM   3663 N  N   . ALA C 1 32  ? 34.62000  3.35700   37.31800  1.000 117.83764 ?  32  ALA C N   1 
ATOM   3664 C  CA  . ALA C 1 32  ? 35.22000  4.57100   37.83900  1.000 118.47607 ?  32  ALA C CA  1 
ATOM   3665 C  C   . ALA C 1 32  ? 35.31700  4.48100   39.33700  1.000 119.28444 ?  32  ALA C C   1 
ATOM   3666 O  O   . ALA C 1 32  ? 34.31100  4.32600   40.02400  1.000 115.95984 ?  32  ALA C O   1 
ATOM   3667 C  CB  . ALA C 1 32  ? 34.41000  5.78400   37.43300  1.000 114.86754 ?  32  ALA C CB  1 
ATOM   3668 N  N   . GLN C 1 33  ? 36.52800  4.57700   39.85200  1.000 118.88355 ?  33  GLN C N   1 
ATOM   3669 C  CA  . GLN C 1 33  ? 36.72000  4.44300   41.27500  1.000 113.01472 ?  33  GLN C CA  1 
ATOM   3670 C  C   . GLN C 1 33  ? 36.35900  5.71800   41.96100  1.000 109.61364 ?  33  GLN C C   1 
ATOM   3671 O  O   . GLN C 1 33  ? 35.87200  6.65700   41.34100  1.000 108.63785 ?  33  GLN C O   1 
ATOM   3672 C  CB  . GLN C 1 33  ? 38.17100  4.11400   41.57600  1.000 115.35993 ?  33  GLN C CB  1 
ATOM   3673 C  CG  . GLN C 1 33  ? 39.15800  4.94100   40.77600  1.000 119.82220 ?  33  GLN C CG  1 
ATOM   3674 C  CD  . GLN C 1 33  ? 39.62500  4.23100   39.52100  1.000 124.79909 ?  33  GLN C CD  1 
ATOM   3675 O  OE1 . GLN C 1 33  ? 38.82000  3.68900   38.76400  1.000 124.47491 ?  33  GLN C OE1 1 
ATOM   3676 N  NE2 . GLN C 1 33  ? 40.93200  4.23100   39.29400  1.000 127.98281 ?  33  GLN C NE2 1 
ATOM   3677 N  N   . LYS C 1 34  ? 36.60900  5.76200   43.25500  1.000 110.27742 ?  34  LYS C N   1 
ATOM   3678 C  CA  . LYS C 1 34  ? 36.26700  6.93700   44.01800  1.000 103.19373 ?  34  LYS C CA  1 
ATOM   3679 C  C   . LYS C 1 34  ? 36.90800  8.15300   43.40000  1.000 97.15791  ?  34  LYS C C   1 
ATOM   3680 O  O   . LYS C 1 34  ? 37.96100  8.06700   42.77900  1.000 93.01583  ?  34  LYS C O   1 
ATOM   3681 C  CB  . LYS C 1 34  ? 36.71900  6.76400   45.46100  1.000 94.35651  ?  34  LYS C CB  1 
ATOM   3682 C  CG  . LYS C 1 34  ? 35.96900  5.68700   46.22000  1.000 95.83232  ?  34  LYS C CG  1 
ATOM   3683 C  CD  . LYS C 1 34  ? 36.49400  5.56100   47.63900  1.000 105.86842 ?  34  LYS C CD  1 
ATOM   3684 C  CE  . LYS C 1 34  ? 35.73200  4.50000   48.41400  1.000 104.02764 ?  34  LYS C CE  1 
ATOM   3685 N  NZ  . LYS C 1 34  ? 36.25500  4.35300   49.80000  1.000 94.35858  ?  34  LYS C NZ  1 
ATOM   3686 N  N   . PRO C 1 35  ? 36.26200  9.29700   43.56300  1.000 93.15450  ?  35  PRO C N   1 
ATOM   3687 C  CA  . PRO C 1 35  ? 36.81800  10.52600  43.01900  1.000 94.61627  ?  35  PRO C CA  1 
ATOM   3688 C  C   . PRO C 1 35  ? 38.15100  10.89200  43.65100  1.000 93.42722  ?  35  PRO C C   1 
ATOM   3689 O  O   . PRO C 1 35  ? 38.50100  10.35800  44.69500  1.000 98.03415  ?  35  PRO C O   1 
ATOM   3690 C  CB  . PRO C 1 35  ? 35.76200  11.56600  43.39000  1.000 94.65538  ?  35  PRO C CB  1 
ATOM   3691 C  CG  . PRO C 1 35  ? 34.50000  10.79600  43.53000  1.000 94.66376  ?  35  PRO C CG  1 
ATOM   3692 C  CD  . PRO C 1 35  ? 34.92700  9.50100   44.14300  1.000 94.21437  ?  35  PRO C CD  1 
ATOM   3693 N  N   . ARG C 1 36  ? 38.89300  11.78800  43.01900  1.000 94.19453  ?  36  ARG C N   1 
ATOM   3694 C  CA  . ARG C 1 36  ? 40.16000  12.24900  43.56900  1.000 90.38982  ?  36  ARG C CA  1 
ATOM   3695 C  C   . ARG C 1 36  ? 40.14600  13.70800  43.96300  1.000 90.30595  ?  36  ARG C C   1 
ATOM   3696 O  O   . ARG C 1 36  ? 41.08200  14.16500  44.62800  1.000 87.77260  ?  36  ARG C O   1 
ATOM   3697 C  CB  . ARG C 1 36  ? 41.27300  12.06100  42.52500  1.000 98.95948  ?  36  ARG C CB  1 
ATOM   3698 C  CG  . ARG C 1 36  ? 41.58500  10.65500  42.21500  1.000 106.97407 ?  36  ARG C CG  1 
ATOM   3699 C  CD  . ARG C 1 36  ? 42.72800  10.49800  41.21100  1.000 125.70097 ?  36  ARG C CD  1 
ATOM   3700 N  NE  . ARG C 1 36  ? 43.00400  9.12800   40.84200  1.000 136.47044 ?  36  ARG C NE  1 
ATOM   3701 C  CZ  . ARG C 1 36  ? 43.88100  8.79200   39.89700  1.000 133.55454 ?  36  ARG C CZ  1 
ATOM   3702 N  NH1 . ARG C 1 36  ? 44.53600  9.70900   39.20900  1.000 125.55944 ?  36  ARG C NH1 1 
ATOM   3703 N  NH2 . ARG C 1 36  ? 44.18800  7.50200   39.70800  1.000 135.19748 ?  36  ARG C NH2 1 
ATOM   3704 N  N   . PHE C 1 37  ? 39.11200  14.43700  43.59300  1.000 89.33542  ?  37  PHE C N   1 
ATOM   3705 C  CA  . PHE C 1 37  ? 39.03100  15.85800  43.85400  1.000 85.16055  ?  37  PHE C CA  1 
ATOM   3706 C  C   . PHE C 1 37  ? 37.74900  16.18200  44.55900  1.000 81.09857  ?  37  PHE C C   1 
ATOM   3707 O  O   . PHE C 1 37  ? 36.70600  15.58300  44.27900  1.000 85.00934  ?  37  PHE C O   1 
ATOM   3708 C  CB  . PHE C 1 37  ? 39.00100  16.70000  42.61000  1.000 85.04302  ?  37  PHE C CB  1 
ATOM   3709 C  CG  . PHE C 1 37  ? 40.21900  16.58300  41.78800  1.000 80.26153  ?  37  PHE C CG  1 
ATOM   3710 C  CD1 . PHE C 1 37  ? 40.38300  15.49600  40.87100  1.000 89.39566  ?  37  PHE C CD1 1 
ATOM   3711 C  CD2 . PHE C 1 37  ? 41.27000  17.51400  41.95000  1.000 80.87051  ?  37  PHE C CD2 1 
ATOM   3712 C  CE1 . PHE C 1 37  ? 41.52300  15.41600  40.13400  1.000 94.12706  ?  37  PHE C CE1 1 
ATOM   3713 C  CE2 . PHE C 1 37  ? 42.41000  17.35900  41.20800  1.000 89.11586  ?  37  PHE C CE2 1 
ATOM   3714 C  CZ  . PHE C 1 37  ? 42.50100  16.39900  40.24200  1.000 94.53709  ?  37  PHE C CZ  1 
ATOM   3715 N  N   . LEU C 1 38  ? 37.82400  17.18700  45.40300  1.000 73.57042  ?  38  LEU C N   1 
ATOM   3716 C  CA  . LEU C 1 38  ? 36.63800  17.83100  45.92500  1.000 72.45340  ?  38  LEU C CA  1 
ATOM   3717 C  C   . LEU C 1 38  ? 36.57800  19.24000  45.35200  1.000 63.22610  ?  38  LEU C C   1 
ATOM   3718 O  O   . LEU C 1 38  ? 37.52700  20.01900  45.50100  1.000 63.50289  ?  38  LEU C O   1 
ATOM   3719 C  CB  . LEU C 1 38  ? 36.66300  17.85000  47.44800  1.000 78.33062  ?  38  LEU C CB  1 
ATOM   3720 C  CG  . LEU C 1 38  ? 35.58900  18.67500  48.15500  1.000 72.88257  ?  38  LEU C CG  1 
ATOM   3721 C  CD1 . LEU C 1 38  ? 34.19300  18.18900  47.79400  1.000 72.82727  ?  38  LEU C CD1 1 
ATOM   3722 C  CD2 . LEU C 1 38  ? 35.79800  18.63300  49.65900  1.000 65.44406  ?  38  LEU C CD2 1 
ATOM   3723 N  N   . TRP C 1 39  ? 35.46900  19.56600  44.69900  1.000 58.61799  ?  39  TRP C N   1 
ATOM   3724 C  CA  . TRP C 1 39  ? 35.26700  20.89400  44.13800  1.000 63.67994  ?  39  TRP C CA  1 
ATOM   3725 C  C   . TRP C 1 39  ? 34.24300  21.60400  45.00800  1.000 60.93592  ?  39  TRP C C   1 
ATOM   3726 O  O   . TRP C 1 39  ? 33.07600  21.19900  45.06700  1.000 62.58682  ?  39  TRP C O   1 
ATOM   3727 C  CB  . TRP C 1 39  ? 34.81000  20.83200  42.68300  1.000 68.78851  ?  39  TRP C CB  1 
ATOM   3728 C  CG  . TRP C 1 39  ? 34.87900  22.16700  42.00500  1.000 65.30840  ?  39  TRP C CG  1 
ATOM   3729 C  CD1 . TRP C 1 39  ? 33.92500  23.14500  42.00800  1.000 65.64982  ?  39  TRP C CD1 1 
ATOM   3730 C  CD2 . TRP C 1 39  ? 35.97900  22.68300  41.24800  1.000 65.88737  ?  39  TRP C CD2 1 
ATOM   3731 N  NE1 . TRP C 1 39  ? 34.35900  24.23100  41.28500  1.000 67.57106  ?  39  TRP C NE1 1 
ATOM   3732 C  CE2 . TRP C 1 39  ? 35.61800  23.97300  40.81000  1.000 69.88423  ?  39  TRP C CE2 1 
ATOM   3733 C  CE3 . TRP C 1 39  ? 37.23200  22.17500  40.89200  1.000 65.55061  ?  39  TRP C CE3 1 
ATOM   3734 C  CZ2 . TRP C 1 39  ? 36.46400  24.76000  40.03300  1.000 67.32757  ?  39  TRP C CZ2 1 
ATOM   3735 C  CZ3 . TRP C 1 39  ? 38.07100  22.95900  40.12400  1.000 67.88328  ?  39  TRP C CZ3 1 
ATOM   3736 C  CH2 . TRP C 1 39  ? 37.68500  24.23900  39.70500  1.000 67.51574  ?  39  TRP C CH2 1 
ATOM   3737 N  N   . ILE C 1 40  ? 34.68600  22.65500  45.68300  1.000 57.57926  ?  40  ILE C N   1 
ATOM   3738 C  CA  . ILE C 1 40  ? 33.81400  23.52100  46.45900  1.000 66.22398  ?  40  ILE C CA  1 
ATOM   3739 C  C   . ILE C 1 40  ? 33.70500  24.82600  45.68800  1.000 60.47060  ?  40  ILE C C   1 
ATOM   3740 O  O   . ILE C 1 40  ? 34.66600  25.60200  45.62200  1.000 61.96389  ?  40  ILE C O   1 
ATOM   3741 C  CB  . ILE C 1 40  ? 34.34100  23.74100  47.88400  1.000 67.35272  ?  40  ILE C CB  1 
ATOM   3742 C  CG1 . ILE C 1 40  ? 34.46100  22.40100  48.61500  1.000 60.16125  ?  40  ILE C CG1 1 
ATOM   3743 C  CG2 . ILE C 1 40  ? 33.41700  24.66700  48.65400  1.000 56.24448  ?  40  ILE C CG2 1 
ATOM   3744 C  CD1 . ILE C 1 40  ? 35.09300  22.49900  49.98100  1.000 67.09234  ?  40  ILE C CD1 1 
ATOM   3745 N  N   . GLY C 1 41  ? 32.54400  25.05300  45.07400  1.000 54.06672  ?  41  GLY C N   1 
ATOM   3746 C  CA  . GLY C 1 41  ? 32.33200  26.21400  44.23800  1.000 59.97436  ?  41  GLY C CA  1 
ATOM   3747 C  C   . GLY C 1 41  ? 31.03100  26.91700  44.58000  1.000 60.23729  ?  41  GLY C C   1 
ATOM   3748 O  O   . GLY C 1 41  ? 30.27400  26.48300  45.44900  1.000 65.79061  ?  41  GLY C O   1 
ATOM   3749 N  N   . CYS C 1 42  ? 30.80300  28.02400  43.88300  1.000 66.74134  ?  42  CYS C N   1 
ATOM   3750 C  CA  . CYS C 1 42  ? 29.61300  28.83400  44.09100  1.000 65.77048  ?  42  CYS C CA  1 
ATOM   3751 C  C   . CYS C 1 42  ? 28.40700  28.22500  43.38400  1.000 70.93076  ?  42  CYS C C   1 
ATOM   3752 O  O   . CYS C 1 42  ? 28.53400  27.53300  42.36900  1.000 73.00513  ?  42  CYS C O   1 
ATOM   3753 C  CB  . CYS C 1 42  ? 29.84200  30.26200  43.59500  1.000 66.18226  ?  42  CYS C CB  1 
ATOM   3754 S  SG  . CYS C 1 42  ? 28.41200  31.34900  43.78300  1.000 73.94000  ?  42  CYS C SG  1 
ATOM   3755 N  N   . SER C 1 43  ? 27.22100  28.48600  43.94200  1.000 67.84846  ?  43  SER C N   1 
ATOM   3756 C  CA  . SER C 1 43  ? 25.98500  28.01700  43.32600  1.000 72.13139  ?  43  SER C CA  1 
ATOM   3757 C  C   . SER C 1 43  ? 25.68000  28.71800  42.00900  1.000 69.63740  ?  43  SER C C   1 
ATOM   3758 O  O   . SER C 1 43  ? 24.84400  28.22400  41.24400  1.000 66.70759  ?  43  SER C O   1 
ATOM   3759 C  CB  . SER C 1 43  ? 24.81100  28.19800  44.28700  1.000 67.71171  ?  43  SER C CB  1 
ATOM   3760 O  OG  . SER C 1 43  ? 24.86100  27.24600  45.33400  1.000 71.82967  ?  43  SER C OG  1 
ATOM   3761 N  N   . ASP C 1 44  ? 26.32200  29.85600  41.73000  1.000 70.24094  ?  44  ASP C N   1 
ATOM   3762 C  CA  . ASP C 1 44  ? 26.15900  30.48200  40.42200  1.000 73.08699  ?  44  ASP C CA  1 
ATOM   3763 C  C   . ASP C 1 44  ? 26.54100  29.51500  39.31100  1.000 75.27432  ?  44  ASP C C   1 
ATOM   3764 O  O   . ASP C 1 44  ? 25.83600  29.41200  38.30000  1.000 72.23654  ?  44  ASP C O   1 
ATOM   3765 C  CB  . ASP C 1 44  ? 26.99700  31.75700  40.33600  1.000 70.94774  ?  44  ASP C CB  1 
ATOM   3766 C  CG  . ASP C 1 44  ? 26.37900  32.91600  41.09300  1.000 69.48414  ?  44  ASP C CG  1 
ATOM   3767 O  OD1 . ASP C 1 44  ? 25.14400  33.08300  41.02800  1.000 60.74813  ?  44  ASP C OD1 1 
ATOM   3768 O  OD2 . ASP C 1 44  ? 27.13100  33.66500  41.75100  1.000 72.89917  -1 44  ASP C OD2 1 
ATOM   3769 N  N   . SER C 1 45  ? 27.64000  28.78500  39.49900  1.000 75.07285  ?  45  SER C N   1 
ATOM   3770 C  CA  . SER C 1 45  ? 28.13100  27.79800  38.53900  1.000 76.17593  ?  45  SER C CA  1 
ATOM   3771 C  C   . SER C 1 45  ? 28.09100  28.36600  37.12400  1.000 83.47869  ?  45  SER C C   1 
ATOM   3772 O  O   . SER C 1 45  ? 27.55200  27.76500  36.19200  1.000 84.80446  ?  45  SER C O   1 
ATOM   3773 C  CB  . SER C 1 45  ? 27.33500  26.49800  38.64500  1.000 75.77210  ?  45  SER C CB  1 
ATOM   3774 O  OG  . SER C 1 45  ? 28.02300  25.42000  38.03500  1.000 78.40739  ?  45  SER C OG  1 
ATOM   3775 N  N   . ARG C 1 46  ? 28.66500  29.56500  36.98600  1.000 84.14685  ?  46  ARG C N   1 
ATOM   3776 C  CA  . ARG C 1 46  ? 28.63200  30.27700  35.71200  1.000 84.27236  ?  46  ARG C CA  1 
ATOM   3777 C  C   . ARG C 1 46  ? 29.26200  29.44600  34.60300  1.000 89.20469  ?  46  ARG C C   1 
ATOM   3778 O  O   . ARG C 1 46  ? 28.78900  29.46000  33.46100  1.000 92.85125  ?  46  ARG C O   1 
ATOM   3779 C  CB  . ARG C 1 46  ? 29.33800  31.62300  35.85900  1.000 85.05480  ?  46  ARG C CB  1 
ATOM   3780 C  CG  . ARG C 1 46  ? 28.67300  32.53700  36.88000  1.000 83.91877  ?  46  ARG C CG  1 
ATOM   3781 C  CD  . ARG C 1 46  ? 27.18800  32.72400  36.60900  1.000 87.31037  ?  46  ARG C CD  1 
ATOM   3782 N  NE  . ARG C 1 46  ? 26.95000  33.61300  35.48000  1.000 93.58442  ?  46  ARG C NE  1 
ATOM   3783 C  CZ  . ARG C 1 46  ? 25.76200  33.83900  34.93900  1.000 95.83416  ?  46  ARG C CZ  1 
ATOM   3784 N  NH1 . ARG C 1 46  ? 24.67000  33.24100  35.39000  1.000 90.23678  ?  46  ARG C NH1 1 
ATOM   3785 N  NH2 . ARG C 1 46  ? 25.66300  34.70300  33.93500  1.000 111.94504 ?  46  ARG C NH2 1 
ATOM   3786 N  N   . VAL C 1 47  ? 30.34700  28.73700  34.91300  1.000 83.33554  ?  47  VAL C N   1 
ATOM   3787 C  CA  . VAL C 1 47  ? 30.90600  27.72500  34.03200  1.000 84.18150  ?  47  VAL C CA  1 
ATOM   3788 C  C   . VAL C 1 47  ? 31.06200  26.47000  34.88100  1.000 84.42549  ?  47  VAL C C   1 
ATOM   3789 O  O   . VAL C 1 47  ? 31.74800  26.50300  35.90600  1.000 84.85838  ?  47  VAL C O   1 
ATOM   3790 C  CB  . VAL C 1 47  ? 32.26000  28.13200  33.42600  1.000 85.49204  ?  47  VAL C CB  1 
ATOM   3791 C  CG1 . VAL C 1 47  ? 32.67400  27.13500  32.35200  1.000 87.28000  ?  47  VAL C CG1 1 
ATOM   3792 C  CG2 . VAL C 1 47  ? 32.20600  29.54400  32.87200  1.000 85.03654  ?  47  VAL C CG2 1 
ATOM   3793 N  N   . PRO C 1 48  ? 30.42800  25.35200  34.52400  1.000 84.87933  ?  48  PRO C N   1 
ATOM   3794 C  CA  . PRO C 1 48  ? 30.57200  24.13700  35.33300  1.000 86.86038  ?  48  PRO C CA  1 
ATOM   3795 C  C   . PRO C 1 48  ? 32.03100  23.72900  35.47700  1.000 87.29976  ?  48  PRO C C   1 
ATOM   3796 O  O   . PRO C 1 48  ? 32.86500  23.98900  34.60700  1.000 86.98283  ?  48  PRO C O   1 
ATOM   3797 C  CB  . PRO C 1 48  ? 29.77100  23.09300  34.54800  1.000 87.46178  ?  48  PRO C CB  1 
ATOM   3798 C  CG  . PRO C 1 48  ? 28.75300  23.89800  33.81300  1.000 86.92048  ?  48  PRO C CG  1 
ATOM   3799 C  CD  . PRO C 1 48  ? 29.43600  25.18600  33.45000  1.000 85.37298  ?  48  PRO C CD  1 
ATOM   3800 N  N   . ALA C 1 49  ? 32.32800  23.07700  36.60300  1.000 87.81197  ?  49  ALA C N   1 
ATOM   3801 C  CA  . ALA C 1 49  ? 33.70900  22.74400  36.93200  1.000 87.79843  ?  49  ALA C CA  1 
ATOM   3802 C  C   . ALA C 1 49  ? 34.29800  21.72300  35.96900  1.000 86.75049  ?  49  ALA C C   1 
ATOM   3803 O  O   . ALA C 1 49  ? 35.50600  21.74900  35.70600  1.000 83.74870  ?  49  ALA C O   1 
ATOM   3804 C  CB  . ALA C 1 49  ? 33.79400  22.22600  38.36800  1.000 82.31733  ?  49  ALA C CB  1 
ATOM   3805 N  N   . GLU C 1 50  ? 33.47000  20.82300  35.43600  1.000 89.93773  ?  50  GLU C N   1 
ATOM   3806 C  CA  . GLU C 1 50  ? 33.98200  19.77700  34.55600  1.000 90.35090  ?  50  GLU C CA  1 
ATOM   3807 C  C   . GLU C 1 50  ? 34.50100  20.34700  33.24000  1.000 93.07523  ?  50  GLU C C   1 
ATOM   3808 O  O   . GLU C 1 50  ? 35.50000  19.85500  32.70100  1.000 93.52961  ?  50  GLU C O   1 
ATOM   3809 C  CB  . GLU C 1 50  ? 32.90000  18.72500  34.31100  1.000 90.06709  ?  50  GLU C CB  1 
ATOM   3810 C  CG  . GLU C 1 50  ? 32.49700  17.93800  35.55800  1.000 94.05044  ?  50  GLU C CG  1 
ATOM   3811 C  CD  . GLU C 1 50  ? 31.55400  18.70000  36.47400  1.000 93.63130  ?  50  GLU C CD  1 
ATOM   3812 O  OE1 . GLU C 1 50  ? 31.17700  19.84100  36.13000  1.000 91.41527  ?  50  GLU C OE1 1 
ATOM   3813 O  OE2 . GLU C 1 50  ? 31.19500  18.15800  37.54200  1.000 92.37161  -1 50  GLU C OE2 1 
ATOM   3814 N  N   . ARG C 1 51  ? 33.83900  21.37100  32.69700  1.000 91.08756  ?  51  ARG C N   1 
ATOM   3815 C  CA  . ARG C 1 51  ? 34.35300  21.99700  31.48100  1.000 90.70181  ?  51  ARG C CA  1 
ATOM   3816 C  C   . ARG C 1 51  ? 35.58900  22.83800  31.77200  1.000 92.18182  ?  51  ARG C C   1 
ATOM   3817 O  O   . ARG C 1 51  ? 36.52900  22.86800  30.96800  1.000 92.27518  ?  51  ARG C O   1 
ATOM   3818 C  CB  . ARG C 1 51  ? 33.28200  22.85500  30.81400  1.000 86.79726  ?  51  ARG C CB  1 
ATOM   3819 C  CG  . ARG C 1 51  ? 32.07500  22.08900  30.33600  1.000 88.49080  ?  51  ARG C CG  1 
ATOM   3820 C  CD  . ARG C 1 51  ? 31.20900  22.98600  29.48200  1.000 80.80476  ?  51  ARG C CD  1 
ATOM   3821 N  NE  . ARG C 1 51  ? 29.97500  22.32900  29.07400  1.000 91.16034  ?  51  ARG C NE  1 
ATOM   3822 C  CZ  . ARG C 1 51  ? 28.93400  22.96000  28.55200  1.000 102.00547 ?  51  ARG C CZ  1 
ATOM   3823 N  NH1 . ARG C 1 51  ? 28.96000  24.26200  28.32300  1.000 103.88002 ?  51  ARG C NH1 1 
ATOM   3824 N  NH2 . ARG C 1 51  ? 27.84400  22.26500  28.24000  1.000 104.00436 ?  51  ARG C NH2 1 
ATOM   3825 N  N   . LEU C 1 52  ? 35.60100  23.53800  32.91100  1.000 91.48887  ?  52  LEU C N   1 
ATOM   3826 C  CA  . LEU C 1 52  ? 36.72400  24.41300  33.23600  1.000 85.73981  ?  52  LEU C CA  1 
ATOM   3827 C  C   . LEU C 1 52  ? 38.01500  23.62500  33.39800  1.000 82.81597  ?  52  LEU C C   1 
ATOM   3828 O  O   . LEU C 1 52  ? 39.09000  24.09300  33.00900  1.000 81.54833  ?  52  LEU C O   1 
ATOM   3829 C  CB  . LEU C 1 52  ? 36.42800  25.20000  34.51100  1.000 88.58746  ?  52  LEU C CB  1 
ATOM   3830 C  CG  . LEU C 1 52  ? 35.46700  26.37900  34.39700  1.000 92.18915  ?  52  LEU C CG  1 
ATOM   3831 C  CD1 . LEU C 1 52  ? 35.03200  26.84400  35.77800  1.000 89.09990  ?  52  LEU C CD1 1 
ATOM   3832 C  CD2 . LEU C 1 52  ? 36.10900  27.51600  33.62100  1.000 90.70693  ?  52  LEU C CD2 1 
ATOM   3833 N  N   . THR C 1 53  ? 37.93400  22.43200  33.97800  1.000 87.23292  ?  53  THR C N   1 
ATOM   3834 C  CA  . THR C 1 53  ? 39.11800  21.65500  34.30900  1.000 90.46155  ?  53  THR C CA  1 
ATOM   3835 C  C   . THR C 1 53  ? 39.32400  20.45300  33.40000  1.000 85.75087  ?  53  THR C C   1 
ATOM   3836 O  O   . THR C 1 53  ? 40.37300  19.80500  33.48800  1.000 81.88896  ?  53  THR C O   1 
ATOM   3837 C  CB  . THR C 1 53  ? 39.04600  21.18000  35.76700  1.000 87.65659  ?  53  THR C CB  1 
ATOM   3838 O  OG1 . THR C 1 53  ? 37.85900  20.39900  35.95800  1.000 81.25627  ?  53  THR C OG1 1 
ATOM   3839 C  CG2 . THR C 1 53  ? 39.01000  22.37600  36.70500  1.000 82.73549  ?  53  THR C CG2 1 
ATOM   3840 N  N   . GLY C 1 54  ? 38.36800  20.14800  32.52700  1.000 84.01586  ?  54  GLY C N   1 
ATOM   3841 C  CA  . GLY C 1 54  ? 38.45500  18.95300  31.71200  1.000 85.52439  ?  54  GLY C CA  1 
ATOM   3842 C  C   . GLY C 1 54  ? 38.33100  17.65900  32.47900  1.000 91.17914  ?  54  GLY C C   1 
ATOM   3843 O  O   . GLY C 1 54  ? 38.80200  16.62200  32.00500  1.000 95.39965  ?  54  GLY C O   1 
ATOM   3844 N  N   . LEU C 1 55  ? 37.71800  17.69000  33.65900  1.000 97.13858  ?  55  LEU C N   1 
ATOM   3845 C  CA  . LEU C 1 55  ? 37.50800  16.49000  34.45400  1.000 94.58506  ?  55  LEU C CA  1 
ATOM   3846 C  C   . LEU C 1 55  ? 36.19900  15.83500  34.03000  1.000 95.35403  ?  55  LEU C C   1 
ATOM   3847 O  O   . LEU C 1 55  ? 35.18000  16.51800  33.88200  1.000 94.12064  ?  55  LEU C O   1 
ATOM   3848 C  CB  . LEU C 1 55  ? 37.46100  16.83800  35.94300  1.000 91.41240  ?  55  LEU C CB  1 
ATOM   3849 C  CG  . LEU C 1 55  ? 38.77200  17.20000  36.64500  1.000 87.17142  ?  55  LEU C CG  1 
ATOM   3850 C  CD1 . LEU C 1 55  ? 38.49600  17.78300  38.02100  1.000 84.58451  ?  55  LEU C CD1 1 
ATOM   3851 C  CD2 . LEU C 1 55  ? 39.67100  15.98200  36.75500  1.000 91.54995  ?  55  LEU C CD2 1 
ATOM   3852 N  N   . GLU C 1 56  ? 36.22600  14.52600  33.84300  1.000 96.55754  ?  56  GLU C N   1 
ATOM   3853 C  CA  . GLU C 1 56  ? 35.02500  13.84900  33.38900  1.000 101.13537 ?  56  GLU C CA  1 
ATOM   3854 C  C   . GLU C 1 56  ? 34.20400  13.36900  34.57900  1.000 104.42688 ?  56  GLU C C   1 
ATOM   3855 O  O   . GLU C 1 56  ? 34.72800  13.21000  35.68600  1.000 105.00672 ?  56  GLU C O   1 
ATOM   3856 C  CB  . GLU C 1 56  ? 35.37900  12.68400  32.46300  1.000 107.37429 ?  56  GLU C CB  1 
ATOM   3857 C  CG  . GLU C 1 56  ? 36.16700  11.55800  33.08700  1.000 110.33847 ?  56  GLU C CG  1 
ATOM   3858 C  CD  . GLU C 1 56  ? 36.64500  10.56700  32.04400  1.000 116.04798 ?  56  GLU C CD  1 
ATOM   3859 O  OE1 . GLU C 1 56  ? 36.26700  10.72400  30.86200  1.000 115.63557 ?  56  GLU C OE1 1 
ATOM   3860 O  OE2 . GLU C 1 56  ? 37.39800  9.63700   32.39900  1.000 121.93109 -1 56  GLU C OE2 1 
ATOM   3861 N  N   . PRO C 1 57  ? 32.89500  13.14700  34.38100  1.000 102.73379 ?  57  PRO C N   1 
ATOM   3862 C  CA  . PRO C 1 57  ? 32.03600  12.66900  35.47200  1.000 98.02939  ?  57  PRO C CA  1 
ATOM   3863 C  C   . PRO C 1 57  ? 32.58000  11.43100  36.15900  1.000 94.77059  ?  57  PRO C C   1 
ATOM   3864 O  O   . PRO C 1 57  ? 32.82000  10.39600  35.53100  1.000 95.99260  ?  57  PRO C O   1 
ATOM   3865 C  CB  . PRO C 1 57  ? 30.70700  12.37800  34.76300  1.000 95.94192  ?  57  PRO C CB  1 
ATOM   3866 C  CG  . PRO C 1 57  ? 31.02700  12.35100  33.30200  1.000 98.60541  ?  57  PRO C CG  1 
ATOM   3867 C  CD  . PRO C 1 57  ? 32.13300  13.33000  33.14200  1.000 99.98086  ?  57  PRO C CD  1 
ATOM   3868 N  N   . GLY C 1 58  ? 32.77900  11.54500  37.46800  1.000 97.97285  ?  58  GLY C N   1 
ATOM   3869 C  CA  . GLY C 1 58  ? 33.29200  10.47100  38.29000  1.000 101.19447 ?  58  GLY C CA  1 
ATOM   3870 C  C   . GLY C 1 58  ? 34.59500  10.81400  38.97700  1.000 97.73708  ?  58  GLY C C   1 
ATOM   3871 O  O   . GLY C 1 58  ? 34.99400  10.11800  39.92000  1.000 101.11919 ?  58  GLY C O   1 
ATOM   3872 N  N   . GLU C 1 59  ? 35.27500  11.86700  38.52500  1.000 95.26260  ?  59  GLU C N   1 
ATOM   3873 C  CA  . GLU C 1 59  ? 36.50900  12.33100  39.14000  1.000 96.28046  ?  59  GLU C CA  1 
ATOM   3874 C  C   . GLU C 1 59  ? 36.30100  13.58400  39.97700  1.000 96.71152  ?  59  GLU C C   1 
ATOM   3875 O  O   . GLU C 1 59  ? 37.28100  14.22400  40.36900  1.000 92.66408  ?  59  GLU C O   1 
ATOM   3876 C  CB  . GLU C 1 59  ? 37.56100  12.62300  38.06500  1.000 97.05074  ?  59  GLU C CB  1 
ATOM   3877 C  CG  . GLU C 1 59  ? 37.92100  11.44900  37.17400  1.000 102.30850 ?  59  GLU C CG  1 
ATOM   3878 C  CD  . GLU C 1 59  ? 38.57900  11.88100  35.87300  1.000 104.13948 ?  59  GLU C CD  1 
ATOM   3879 O  OE1 . GLU C 1 59  ? 38.58200  13.09500  35.57600  1.000 103.08778 ?  59  GLU C OE1 1 
ATOM   3880 O  OE2 . GLU C 1 59  ? 39.09000  11.00300  35.14600  1.000 105.18196 -1 59  GLU C OE2 1 
ATOM   3881 N  N   . LEU C 1 60  ? 35.05300  13.94400  40.26900  1.000 92.63994  ?  60  LEU C N   1 
ATOM   3882 C  CA  . LEU C 1 60  ? 34.75400  15.15400  41.02300  1.000 81.54234  ?  60  LEU C CA  1 
ATOM   3883 C  C   . LEU C 1 60  ? 33.71000  14.87900  42.09000  1.000 84.88402  ?  60  LEU C C   1 
ATOM   3884 O  O   . LEU C 1 60  ? 32.60700  14.41600  41.78000  1.000 85.84236  ?  60  LEU C O   1 
ATOM   3885 C  CB  . LEU C 1 60  ? 34.27400  16.27700  40.09800  1.000 75.76861  ?  60  LEU C CB  1 
ATOM   3886 C  CG  . LEU C 1 60  ? 35.31700  17.34400  39.76800  1.000 80.89818  ?  60  LEU C CG  1 
ATOM   3887 C  CD1 . LEU C 1 60  ? 34.66800  18.54900  39.10500  1.000 84.81775  ?  60  LEU C CD1 1 
ATOM   3888 C  CD2 . LEU C 1 60  ? 36.06400  17.76200  41.02100  1.000 78.65936  ?  60  LEU C CD2 1 
ATOM   3889 N  N   . PHE C 1 61  ? 34.06400  15.15300  43.34100  1.000 81.46028  ?  61  PHE C N   1 
ATOM   3890 C  CA  . PHE C 1 61  ? 33.07900  15.33500  44.39300  1.000 71.06845  ?  61  PHE C CA  1 
ATOM   3891 C  C   . PHE C 1 61  ? 32.77700  16.82600  44.45000  1.000 64.49329  ?  61  PHE C C   1 
ATOM   3892 O  O   . PHE C 1 61  ? 33.69300  17.64200  44.58600  1.000 64.32673  ?  61  PHE C O   1 
ATOM   3893 C  CB  . PHE C 1 61  ? 33.59900  14.82900  45.73900  1.000 77.78191  ?  61  PHE C CB  1 
ATOM   3894 C  CG  . PHE C 1 61  ? 32.53600  14.22400  46.61300  1.000 80.50159  ?  61  PHE C CG  1 
ATOM   3895 C  CD1 . PHE C 1 61  ? 31.78900  13.14500  46.17200  1.000 79.55164  ?  61  PHE C CD1 1 
ATOM   3896 C  CD2 . PHE C 1 61  ? 32.28600  14.73400  47.87800  1.000 71.49060  ?  61  PHE C CD2 1 
ATOM   3897 C  CE1 . PHE C 1 61  ? 30.81200  12.58500  46.97500  1.000 73.95097  ?  61  PHE C CE1 1 
ATOM   3898 C  CE2 . PHE C 1 61  ? 31.31000  14.17900  48.68600  1.000 68.83068  ?  61  PHE C CE2 1 
ATOM   3899 C  CZ  . PHE C 1 61  ? 30.57300  13.10300  48.23400  1.000 69.36205  ?  61  PHE C CZ  1 
ATOM   3900 N  N   . VAL C 1 62  ? 31.50200  17.18400  44.32800  1.000 63.47336  ?  62  VAL C N   1 
ATOM   3901 C  CA  . VAL C 1 62  ? 31.10800  18.56500  44.07900  1.000 68.31220  ?  62  VAL C CA  1 
ATOM   3902 C  C   . VAL C 1 62  ? 30.18300  19.02900  45.19200  1.000 65.24808  ?  62  VAL C C   1 
ATOM   3903 O  O   . VAL C 1 62  ? 29.18600  18.36600  45.49900  1.000 68.56125  ?  62  VAL C O   1 
ATOM   3904 C  CB  . VAL C 1 62  ? 30.42500  18.71900  42.70700  1.000 68.07202  ?  62  VAL C CB  1 
ATOM   3905 C  CG1 . VAL C 1 62  ? 30.01700  20.16600  42.47300  1.000 67.01120  ?  62  VAL C CG1 1 
ATOM   3906 C  CG2 . VAL C 1 62  ? 31.34600  18.23400  41.59600  1.000 71.03495  ?  62  VAL C CG2 1 
ATOM   3907 N  N   . HIS C 1 63  ? 30.50700  20.17600  45.77800  1.000 62.33863  ?  63  HIS C N   1 
ATOM   3908 C  CA  . HIS C 1 63  ? 29.63100  20.87900  46.70000  1.000 67.95839  ?  63  HIS C CA  1 
ATOM   3909 C  C   . HIS C 1 63  ? 29.51900  22.32400  46.24100  1.000 68.32461  ?  63  HIS C C   1 
ATOM   3910 O  O   . HIS C 1 63  ? 30.50900  22.91600  45.80100  1.000 65.95131  ?  63  HIS C O   1 
ATOM   3911 C  CB  . HIS C 1 63  ? 30.17300  20.81300  48.13600  1.000 68.60436  ?  63  HIS C CB  1 
ATOM   3912 C  CG  . HIS C 1 63  ? 29.46000  21.71200  49.09700  1.000 66.13177  ?  63  HIS C CG  1 
ATOM   3913 N  ND1 . HIS C 1 63  ? 28.17400  21.46800  49.52600  1.000 67.90004  ?  63  HIS C ND1 1 
ATOM   3914 C  CD2 . HIS C 1 63  ? 29.85200  22.85200  49.71200  1.000 64.12224  ?  63  HIS C CD2 1 
ATOM   3915 C  CE1 . HIS C 1 63  ? 27.80400  22.41800  50.36600  1.000 68.38391  ?  63  HIS C CE1 1 
ATOM   3916 N  NE2 . HIS C 1 63  ? 28.80400  23.27100  50.49500  1.000 64.60296  ?  63  HIS C NE2 1 
ATOM   3917 N  N   . ARG C 1 64  ? 28.31600  22.88700  46.32600  1.000 66.96428  ?  64  ARG C N   1 
ATOM   3918 C  CA  . ARG C 1 64  ? 28.10500  24.26500  45.90000  1.000 67.24122  ?  64  ARG C CA  1 
ATOM   3919 C  C   . ARG C 1 64  ? 27.15100  24.97300  46.85000  1.000 66.34379  ?  64  ARG C C   1 
ATOM   3920 O  O   . ARG C 1 64  ? 26.07200  24.45600  47.15300  1.000 67.73719  ?  64  ARG C O   1 
ATOM   3921 C  CB  . ARG C 1 64  ? 27.56500  24.32300  44.46400  1.000 67.95188  ?  64  ARG C CB  1 
ATOM   3922 C  CG  . ARG C 1 64  ? 28.58500  23.90000  43.41500  1.000 69.63375  ?  64  ARG C CG  1 
ATOM   3923 C  CD  . ARG C 1 64  ? 28.04200  23.98300  42.00000  1.000 70.67015  ?  64  ARG C CD  1 
ATOM   3924 N  NE  . ARG C 1 64  ? 29.05500  23.59500  41.02600  1.000 71.88638  ?  64  ARG C NE  1 
ATOM   3925 C  CZ  . ARG C 1 64  ? 29.97100  24.41300  40.52500  1.000 72.72322  ?  64  ARG C CZ  1 
ATOM   3926 N  NH1 . ARG C 1 64  ? 30.01200  25.69300  40.85900  1.000 69.40510  ?  64  ARG C NH1 1 
ATOM   3927 N  NH2 . ARG C 1 64  ? 30.86600  23.93600  39.66600  1.000 79.71213  ?  64  ARG C NH2 1 
ATOM   3928 N  N   . ASN C 1 65  ? 27.56000  26.15100  47.32100  1.000 63.66161  ?  65  ASN C N   1 
ATOM   3929 C  CA  . ASN C 1 65  ? 26.70700  27.03900  48.09800  1.000 62.59875  ?  65  ASN C CA  1 
ATOM   3930 C  C   . ASN C 1 65  ? 26.94300  28.46300  47.60800  1.000 60.59514  ?  65  ASN C C   1 
ATOM   3931 O  O   . ASN C 1 65  ? 27.80300  28.71100  46.75700  1.000 70.44405  ?  65  ASN C O   1 
ATOM   3932 C  CB  . ASN C 1 65  ? 26.96500  26.88900  49.60400  1.000 69.76598  ?  65  ASN C CB  1 
ATOM   3933 C  CG  . ASN C 1 65  ? 28.40800  27.16300  49.98700  1.000 66.04745  ?  65  ASN C CG  1 
ATOM   3934 O  OD1 . ASN C 1 65  ? 28.89600  28.28500  49.85800  1.000 67.14602  ?  65  ASN C OD1 1 
ATOM   3935 N  ND2 . ASN C 1 65  ? 29.09800  26.13400  50.46300  1.000 60.47587  ?  65  ASN C ND2 1 
ATOM   3936 N  N   . VAL C 1 66  ? 26.17800  29.41000  48.14900  1.000 58.45752  ?  66  VAL C N   1 
ATOM   3937 C  CA  . VAL C 1 66  ? 26.28700  30.79700  47.70700  1.000 59.64498  ?  66  VAL C CA  1 
ATOM   3938 C  C   . VAL C 1 66  ? 27.65000  31.34400  48.10900  1.000 64.59285  ?  66  VAL C C   1 
ATOM   3939 O  O   . VAL C 1 66  ? 28.00000  31.37200  49.29500  1.000 68.12550  ?  66  VAL C O   1 
ATOM   3940 C  CB  . VAL C 1 66  ? 25.15200  31.65200  48.28400  1.000 65.47809  ?  66  VAL C CB  1 
ATOM   3941 C  CG1 . VAL C 1 66  ? 25.23400  33.07000  47.74100  1.000 62.77856  ?  66  VAL C CG1 1 
ATOM   3942 C  CG2 . VAL C 1 66  ? 23.80200  31.03300  47.95500  1.000 64.54111  ?  66  VAL C CG2 1 
ATOM   3943 N  N   . ALA C 1 67  ? 28.43800  31.75000  47.11100  1.000 65.44380  ?  67  ALA C N   1 
ATOM   3944 C  CA  . ALA C 1 67  ? 29.74500  32.37700  47.30000  1.000 64.21586  ?  67  ALA C CA  1 
ATOM   3945 C  C   . ALA C 1 67  ? 30.76400  31.41700  47.90700  1.000 67.90322  ?  67  ALA C C   1 
ATOM   3946 O  O   . ALA C 1 67  ? 31.72800  31.85400  48.54100  1.000 71.79182  ?  67  ALA C O   1 
ATOM   3947 C  CB  . ALA C 1 67  ? 29.64300  33.65300  48.14100  1.000 65.63636  ?  67  ALA C CB  1 
ATOM   3948 N  N   . ASN C 1 68  ? 30.55700  30.11700  47.70000  1.000 65.67201  ?  68  ASN C N   1 
ATOM   3949 C  CA  . ASN C 1 68  ? 31.50000  29.04600  48.04500  1.000 71.50789  ?  68  ASN C CA  1 
ATOM   3950 C  C   . ASN C 1 68  ? 32.13500  29.24400  49.42600  1.000 75.03687  ?  68  ASN C C   1 
ATOM   3951 O  O   . ASN C 1 68  ? 33.35000  29.38000  49.57100  1.000 74.87758  ?  68  ASN C O   1 
ATOM   3952 C  CB  . ASN C 1 68  ? 32.57300  28.89100  46.96100  1.000 71.74819  ?  68  ASN C CB  1 
ATOM   3953 C  CG  . ASN C 1 68  ? 33.27600  30.19700  46.62800  1.000 73.08853  ?  68  ASN C CG  1 
ATOM   3954 O  OD1 . ASN C 1 68  ? 32.86000  30.92600  45.72600  1.000 76.02935  ?  68  ASN C OD1 1 
ATOM   3955 N  ND2 . ASN C 1 68  ? 34.34400  30.49900  47.35700  1.000 67.67118  ?  68  ASN C ND2 1 
ATOM   3956 N  N   . LEU C 1 69  ? 31.28900  29.22300  50.45400  1.000 72.95823  ?  69  LEU C N   1 
ATOM   3957 C  CA  . LEU C 1 69  ? 31.74900  29.46300  51.81400  1.000 73.28331  ?  69  LEU C CA  1 
ATOM   3958 C  C   . LEU C 1 69  ? 32.08600  28.16200  52.53000  1.000 73.77021  ?  69  LEU C C   1 
ATOM   3959 O  O   . LEU C 1 69  ? 31.47800  27.11500  52.28900  1.000 74.04904  ?  69  LEU C O   1 
ATOM   3960 C  CB  . LEU C 1 69  ? 30.70500  30.22400  52.63500  1.000 66.42721  ?  69  LEU C CB  1 
ATOM   3961 C  CG  . LEU C 1 69  ? 30.38500  31.67300  52.27700  1.000 74.19088  ?  69  LEU C CG  1 
ATOM   3962 C  CD1 . LEU C 1 69  ? 29.52300  32.30000  53.36500  1.000 69.74727  ?  69  LEU C CD1 1 
ATOM   3963 C  CD2 . LEU C 1 69  ? 31.66000  32.47100  52.07000  1.000 78.66907  ?  69  LEU C CD2 1 
ATOM   3964 N  N   . VAL C 1 70  ? 33.05800  28.24900  53.42900  1.000 77.59614  ?  70  VAL C N   1 
ATOM   3965 C  CA  . VAL C 1 70  ? 33.41100  27.16200  54.33900  1.000 72.46607  ?  70  VAL C CA  1 
ATOM   3966 C  C   . VAL C 1 70  ? 33.32700  27.75100  55.74200  1.000 71.08992  ?  70  VAL C C   1 
ATOM   3967 O  O   . VAL C 1 70  ? 34.31700  28.22900  56.30300  1.000 70.18091  ?  70  VAL C O   1 
ATOM   3968 C  CB  . VAL C 1 70  ? 34.79800  26.57900  54.05400  1.000 70.48019  ?  70  VAL C CB  1 
ATOM   3969 C  CG1 . VAL C 1 70  ? 35.10600  25.43700  55.01300  1.000 74.26930  ?  70  VAL C CG1 1 
ATOM   3970 C  CG2 . VAL C 1 70  ? 34.89300  26.10700  52.61000  1.000 74.40764  ?  70  VAL C CG2 1 
ATOM   3971 N  N   . ILE C 1 71  ? 32.12900  27.72900  56.31500  1.000 71.36310  ?  71  ILE C N   1 
ATOM   3972 C  CA  . ILE C 1 71  ? 31.89500  28.27000  57.64900  1.000 76.66991  ?  71  ILE C CA  1 
ATOM   3973 C  C   . ILE C 1 71  ? 32.29700  27.21900  58.67300  1.000 71.48597  ?  71  ILE C C   1 
ATOM   3974 O  O   . ILE C 1 71  ? 32.07300  26.02100  58.46500  1.000 75.23882  ?  71  ILE C O   1 
ATOM   3975 C  CB  . ILE C 1 71  ? 30.41900  28.67900  57.80800  1.000 75.99973  ?  71  ILE C CB  1 
ATOM   3976 C  CG1 . ILE C 1 71  ? 30.03500  29.71600  56.75000  1.000 67.47975  ?  71  ILE C CG1 1 
ATOM   3977 C  CG2 . ILE C 1 71  ? 30.15300  29.22100  59.20600  1.000 75.93743  ?  71  ILE C CG2 1 
ATOM   3978 C  CD1 . ILE C 1 71  ? 28.54100  29.87500  56.57200  1.000 69.36941  ?  71  ILE C CD1 1 
ATOM   3979 N  N   . HIS C 1 72  ? 32.91400  27.65800  59.77900  1.000 73.63051  ?  72  HIS C N   1 
ATOM   3980 C  CA  . HIS C 1 72  ? 33.40700  26.70800  60.77600  1.000 70.93879  ?  72  HIS C CA  1 
ATOM   3981 C  C   . HIS C 1 72  ? 32.32100  25.75800  61.26500  1.000 67.34824  ?  72  HIS C C   1 
ATOM   3982 O  O   . HIS C 1 72  ? 32.61600  24.60900  61.61000  1.000 66.75972  ?  72  HIS C O   1 
ATOM   3983 C  CB  . HIS C 1 72  ? 33.99400  27.42800  61.99600  1.000 72.21533  ?  72  HIS C CB  1 
ATOM   3984 C  CG  . HIS C 1 72  ? 35.05300  28.43900  61.67900  1.000 76.50457  ?  72  HIS C CG  1 
ATOM   3985 N  ND1 . HIS C 1 72  ? 36.25700  28.10100  61.10000  1.000 78.58180  ?  72  HIS C ND1 1 
ATOM   3986 C  CD2 . HIS C 1 72  ? 35.10900  29.77200  61.91200  1.000 74.98239  ?  72  HIS C CD2 1 
ATOM   3987 C  CE1 . HIS C 1 72  ? 36.99900  29.18600  60.96700  1.000 78.80546  ?  72  HIS C CE1 1 
ATOM   3988 N  NE2 . HIS C 1 72  ? 36.32500  30.21400  61.45200  1.000 76.80289  ?  72  HIS C NE2 1 
ATOM   3989 N  N   . THR C 1 73  ? 31.06400  26.20500  61.29200  1.000 68.78367  ?  73  THR C N   1 
ATOM   3990 C  CA  . THR C 1 73  ? 29.98900  25.44600  61.92400  1.000 74.11640  ?  73  THR C CA  1 
ATOM   3991 C  C   . THR C 1 73  ? 28.87900  25.04600  60.95500  1.000 73.11850  ?  73  THR C C   1 
ATOM   3992 O  O   . THR C 1 73  ? 27.75300  24.78500  61.39200  1.000 74.83663  ?  73  THR C O   1 
ATOM   3993 C  CB  . THR C 1 73  ? 29.40700  26.23200  63.10000  1.000 79.29063  ?  73  THR C CB  1 
ATOM   3994 O  OG1 . THR C 1 73  ? 29.18700  27.59300  62.70800  1.000 76.99195  ?  73  THR C OG1 1 
ATOM   3995 C  CG2 . THR C 1 73  ? 30.35900  26.18900  64.28700  1.000 70.80296  ?  73  THR C CG2 1 
ATOM   3996 N  N   . ASP C 1 74  ? 29.15700  24.99100  59.65400  1.000 73.59636  ?  74  ASP C N   1 
ATOM   3997 C  CA  . ASP C 1 74  ? 28.16300  24.55400  58.67300  1.000 70.96476  ?  74  ASP C CA  1 
ATOM   3998 C  C   . ASP C 1 74  ? 28.34000  23.05600  58.45800  1.000 70.86299  ?  74  ASP C C   1 
ATOM   3999 O  O   . ASP C 1 74  ? 29.25900  22.62000  57.76200  1.000 75.39018  ?  74  ASP C O   1 
ATOM   4000 C  CB  . ASP C 1 74  ? 28.30300  25.32000  57.36300  1.000 71.24162  ?  74  ASP C CB  1 
ATOM   4001 C  CG  . ASP C 1 74  ? 27.37500  24.79400  56.28200  1.000 78.09247  ?  74  ASP C CG  1 
ATOM   4002 O  OD1 . ASP C 1 74  ? 26.29400  24.27000  56.63100  1.000 76.84657  ?  74  ASP C OD1 1 
ATOM   4003 O  OD2 . ASP C 1 74  ? 27.72900  24.89300  55.08700  1.000 80.44807  -1 74  ASP C OD2 1 
ATOM   4004 N  N   . LEU C 1 75  ? 27.44400  22.26100  59.04800  1.000 65.40555  ?  75  LEU C N   1 
ATOM   4005 C  CA  . LEU C 1 75  ? 27.57500  20.81000  58.96800  1.000 64.55285  ?  75  LEU C CA  1 
ATOM   4006 C  C   . LEU C 1 75  ? 27.43300  20.29400  57.54100  1.000 70.44330  ?  75  LEU C C   1 
ATOM   4007 O  O   . LEU C 1 75  ? 27.97100  19.23000  57.21700  1.000 66.33535  ?  75  LEU C O   1 
ATOM   4008 C  CB  . LEU C 1 75  ? 26.54500  20.13900  59.87700  1.000 59.20985  ?  75  LEU C CB  1 
ATOM   4009 C  CG  . LEU C 1 75  ? 26.87100  18.71000  60.31600  1.000 56.29523  ?  75  LEU C CG  1 
ATOM   4010 C  CD1 . LEU C 1 75  ? 28.33800  18.58300  60.69300  1.000 54.84921  ?  75  LEU C CD1 1 
ATOM   4011 C  CD2 . LEU C 1 75  ? 25.98900  18.30000  61.48000  1.000 63.90128  ?  75  LEU C CD2 1 
ATOM   4012 N  N   . ASN C 1 76  ? 26.71500  21.01800  56.68100  1.000 70.99084  ?  76  ASN C N   1 
ATOM   4013 C  CA  . ASN C 1 76  ? 26.59200  20.63300  55.27700  1.000 69.75634  ?  76  ASN C CA  1 
ATOM   4014 C  C   . ASN C 1 76  ? 27.96300  20.48500  54.62800  1.000 69.34567  ?  76  ASN C C   1 
ATOM   4015 O  O   . ASN C 1 76  ? 28.37400  19.37100  54.28400  1.000 65.49160  ?  76  ASN C O   1 
ATOM   4016 C  CB  . ASN C 1 76  ? 25.74600  21.65600  54.51200  1.000 69.54145  ?  76  ASN C CB  1 
ATOM   4017 C  CG  . ASN C 1 76  ? 25.38500  21.19500  53.10200  1.000 67.28688  ?  76  ASN C CG  1 
ATOM   4018 O  OD1 . ASN C 1 76  ? 26.18000  20.55300  52.41400  1.000 65.28649  ?  76  ASN C OD1 1 
ATOM   4019 N  ND2 . ASN C 1 76  ? 24.17500  21.52800  52.66800  1.000 68.14370  ?  76  ASN C ND2 1 
ATOM   4020 N  N   . CYS C 1 77  ? 28.67400  21.60200  54.45500  1.000 69.76344  ?  77  CYS C N   1 
ATOM   4021 C  CA  . CYS C 1 77  ? 29.98600  21.55400  53.81600  1.000 67.25503  ?  77  CYS C CA  1 
ATOM   4022 C  C   . CYS C 1 77  ? 30.94300  20.64400  54.57300  1.000 68.21091  ?  77  CYS C C   1 
ATOM   4023 O  O   . CYS C 1 77  ? 31.72800  19.90900  53.96100  1.000 61.79844  ?  77  CYS C O   1 
ATOM   4024 C  CB  . CYS C 1 77  ? 30.57100  22.96000  53.70100  1.000 66.43268  ?  77  CYS C CB  1 
ATOM   4025 S  SG  . CYS C 1 77  ? 32.19800  23.01100  52.91000  1.000 58.56077  ?  77  CYS C SG  1 
ATOM   4026 N  N   . LEU C 1 78  ? 30.89300  20.67900  55.90700  1.000 67.13061  ?  78  LEU C N   1 
ATOM   4027 C  CA  . LEU C 1 78  ? 31.82300  19.88500  56.70300  1.000 63.02255  ?  78  LEU C CA  1 
ATOM   4028 C  C   . LEU C 1 78  ? 31.56700  18.39300  56.52900  1.000 61.49644  ?  78  LEU C C   1 
ATOM   4029 O  O   . LEU C 1 78  ? 32.51100  17.59300  56.52400  1.000 58.28718  ?  78  LEU C O   1 
ATOM   4030 C  CB  . LEU C 1 78  ? 31.71600  20.28500  58.17000  1.000 70.94579  ?  78  LEU C CB  1 
ATOM   4031 C  CG  . LEU C 1 78  ? 32.17000  21.71800  58.44000  1.000 71.46784  ?  78  LEU C CG  1 
ATOM   4032 C  CD1 . LEU C 1 78  ? 31.87300  22.10300  59.87600  1.000 70.25837  ?  78  LEU C CD1 1 
ATOM   4033 C  CD2 . LEU C 1 78  ? 33.64100  21.90700  58.10500  1.000 72.71928  ?  78  LEU C CD2 1 
ATOM   4034 N  N   . SER C 1 79  ? 30.29800  18.00100  56.38500  1.000 58.20405  ?  79  SER C N   1 
ATOM   4035 C  CA  . SER C 1 79  ? 29.99000  16.59600  56.13900  1.000 60.08126  ?  79  SER C CA  1 
ATOM   4036 C  C   . SER C 1 79  ? 30.51600  16.15300  54.78000  1.000 69.13583  ?  79  SER C C   1 
ATOM   4037 O  O   . SER C 1 79  ? 31.00500  15.02700  54.63200  1.000 71.32969  ?  79  SER C O   1 
ATOM   4038 C  CB  . SER C 1 79  ? 28.48200  16.36600  56.22500  1.000 62.03619  ?  79  SER C CB  1 
ATOM   4039 O  OG  . SER C 1 79  ? 27.99200  16.67000  57.51700  1.000 55.47022  ?  79  SER C OG  1 
ATOM   4040 N  N   . VAL C 1 80  ? 30.41000  17.02600  53.77500  1.000 68.24907  ?  80  VAL C N   1 
ATOM   4041 C  CA  . VAL C 1 80  ? 30.95300  16.73000  52.45200  1.000 63.80055  ?  80  VAL C CA  1 
ATOM   4042 C  C   . VAL C 1 80  ? 32.46000  16.51500  52.52700  1.000 64.52587  ?  80  VAL C C   1 
ATOM   4043 O  O   . VAL C 1 80  ? 32.98800  15.51300  52.03100  1.000 67.88885  ?  80  VAL C O   1 
ATOM   4044 C  CB  . VAL C 1 80  ? 30.59500  17.85600  51.46600  1.000 62.91200  ?  80  VAL C CB  1 
ATOM   4045 C  CG1 . VAL C 1 80  ? 31.23400  17.59800  50.11300  1.000 65.48076  ?  80  VAL C CG1 1 
ATOM   4046 C  CG2 . VAL C 1 80  ? 29.08500  17.99200  51.34200  1.000 66.33743  ?  80  VAL C CG2 1 
ATOM   4047 N  N   . VAL C 1 81  ? 33.17400  17.45700  53.15100  1.000 60.20672  ?  81  VAL C N   1 
ATOM   4048 C  CA  . VAL C 1 81  ? 34.63100  17.36900  53.21700  1.000 62.59648  ?  81  VAL C CA  1 
ATOM   4049 C  C   . VAL C 1 81  ? 35.05800  16.11600  53.97400  1.000 71.08099  ?  81  VAL C C   1 
ATOM   4050 O  O   . VAL C 1 81  ? 35.98100  15.40700  53.55500  1.000 72.91128  ?  81  VAL C O   1 
ATOM   4051 C  CB  . VAL C 1 81  ? 35.21900  18.64300  53.85200  1.000 61.38194  ?  81  VAL C CB  1 
ATOM   4052 C  CG1 . VAL C 1 81  ? 36.73900  18.54500  53.93100  1.000 65.26953  ?  81  VAL C CG1 1 
ATOM   4053 C  CG2 . VAL C 1 81  ? 34.78500  19.87900  53.08000  1.000 57.12268  ?  81  VAL C CG2 1 
ATOM   4054 N  N   . GLN C 1 82  ? 34.39100  15.82100  55.09500  1.000 71.77522  ?  82  GLN C N   1 
ATOM   4055 C  CA  . GLN C 1 82  ? 34.75700  14.64900  55.88600  1.000 70.14461  ?  82  GLN C CA  1 
ATOM   4056 C  C   . GLN C 1 82  ? 34.53500  13.36100  55.10600  1.000 72.33332  ?  82  GLN C C   1 
ATOM   4057 O  O   . GLN C 1 82  ? 35.37400  12.45300  55.14300  1.000 72.40119  ?  82  GLN C O   1 
ATOM   4058 C  CB  . GLN C 1 82  ? 33.96500  14.62300  57.19200  1.000 66.28900  ?  82  GLN C CB  1 
ATOM   4059 C  CG  . GLN C 1 82  ? 34.49400  13.61600  58.19900  1.000 65.08294  ?  82  GLN C CG  1 
ATOM   4060 C  CD  . GLN C 1 82  ? 33.84500  12.25300  58.05500  1.000 63.69483  ?  82  GLN C CD  1 
ATOM   4061 O  OE1 . GLN C 1 82  ? 32.68600  12.14600  57.65700  1.000 62.22561  ?  82  GLN C OE1 1 
ATOM   4062 N  NE2 . GLN C 1 82  ? 34.59600  11.20200  58.36000  1.000 68.00862  ?  82  GLN C NE2 1 
ATOM   4063 N  N   . TYR C 1 83  ? 33.41000  13.26100  54.39600  1.000 73.92464  ?  83  TYR C N   1 
ATOM   4064 C  CA  . TYR C 1 83  ? 33.16200  12.07900  53.57900  1.000 74.20231  ?  83  TYR C CA  1 
ATOM   4065 C  C   . TYR C 1 83  ? 34.20900  11.96000  52.47900  1.000 77.65937  ?  83  TYR C C   1 
ATOM   4066 O  O   . TYR C 1 83  ? 34.69200  10.86100  52.18400  1.000 79.29621  ?  83  TYR C O   1 
ATOM   4067 C  CB  . TYR C 1 83  ? 31.75100  12.14200  52.99100  1.000 68.99379  ?  83  TYR C CB  1 
ATOM   4068 C  CG  . TYR C 1 83  ? 31.31300  10.89600  52.25300  1.000 71.44601  ?  83  TYR C CG  1 
ATOM   4069 C  CD1 . TYR C 1 83  ? 31.08400  9.70700   52.93500  1.000 70.40504  ?  83  TYR C CD1 1 
ATOM   4070 C  CD2 . TYR C 1 83  ? 31.10200  10.91600  50.88000  1.000 69.36153  ?  83  TYR C CD2 1 
ATOM   4071 C  CE1 . TYR C 1 83  ? 30.67300  8.56700   52.26700  1.000 74.64212  ?  83  TYR C CE1 1 
ATOM   4072 C  CE2 . TYR C 1 83  ? 30.69000  9.78200   50.20300  1.000 66.37829  ?  83  TYR C CE2 1 
ATOM   4073 C  CZ  . TYR C 1 83  ? 30.47700  8.61000   50.90100  1.000 68.51423  ?  83  TYR C CZ  1 
ATOM   4074 O  OH  . TYR C 1 83  ? 30.06700  7.47700   50.23600  1.000 60.83141  ?  83  TYR C OH  1 
ATOM   4075 N  N   . ALA C 1 84  ? 34.58200  13.08700  51.87100  1.000 76.61673  ?  84  ALA C N   1 
ATOM   4076 C  CA  . ALA C 1 84  ? 35.61300  13.07100  50.83900  1.000 72.10023  ?  84  ALA C CA  1 
ATOM   4077 C  C   . ALA C 1 84  ? 36.97100  12.68300  51.41600  1.000 79.35319  ?  84  ALA C C   1 
ATOM   4078 O  O   . ALA C 1 84  ? 37.65200  11.79900  50.88400  1.000 80.87958  ?  84  ALA C O   1 
ATOM   4079 C  CB  . ALA C 1 84  ? 35.68700  14.43600  50.15500  1.000 70.46272  ?  84  ALA C CB  1 
ATOM   4080 N  N   . VAL C 1 85  ? 37.37900  13.32900  52.51000  1.000 81.10657  ?  85  VAL C N   1 
ATOM   4081 C  CA  . VAL C 1 85  ? 38.73200  13.13700  53.02500  1.000 80.93902  ?  85  VAL C CA  1 
ATOM   4082 C  C   . VAL C 1 85  ? 38.87000  11.80100  53.74500  1.000 83.00267  ?  85  VAL C C   1 
ATOM   4083 O  O   . VAL C 1 85  ? 39.85800  11.08300  53.55700  1.000 86.78886  ?  85  VAL C O   1 
ATOM   4084 C  CB  . VAL C 1 85  ? 39.12400  14.31400  53.93700  1.000 79.27126  ?  85  VAL C CB  1 
ATOM   4085 C  CG1 . VAL C 1 85  ? 40.48000  14.06100  54.57700  1.000 86.86354  ?  85  VAL C CG1 1 
ATOM   4086 C  CG2 . VAL C 1 85  ? 39.14400  15.61200  53.14600  1.000 73.70515  ?  85  VAL C CG2 1 
ATOM   4087 N  N   . ASP C 1 86  ? 37.89100  11.43600  54.57200  1.000 83.16231  ?  86  ASP C N   1 
ATOM   4088 C  CA  . ASP C 1 86  ? 38.03100  10.24600  55.40200  1.000 86.53842  ?  86  ASP C CA  1 
ATOM   4089 C  C   . ASP C 1 86  ? 37.51200  8.98200   54.73300  1.000 86.52968  ?  86  ASP C C   1 
ATOM   4090 O  O   . ASP C 1 86  ? 38.06200  7.89900   54.96500  1.000 85.53278  ?  86  ASP C O   1 
ATOM   4091 C  CB  . ASP C 1 86  ? 37.30400  10.44200  56.73500  1.000 83.40873  ?  86  ASP C CB  1 
ATOM   4092 C  CG  . ASP C 1 86  ? 37.89900  11.56100  57.56600  1.000 90.21893  ?  86  ASP C CG  1 
ATOM   4093 O  OD1 . ASP C 1 86  ? 38.94000  12.11800  57.15700  1.000 97.56954  ?  86  ASP C OD1 1 
ATOM   4094 O  OD2 . ASP C 1 86  ? 37.32500  11.88400  58.62800  1.000 88.26812  -1 86  ASP C OD2 1 
ATOM   4095 N  N   . VAL C 1 87  ? 36.48100  9.09000   53.89800  1.000 83.26477  ?  87  VAL C N   1 
ATOM   4096 C  CA  . VAL C 1 87  ? 35.86900  7.91300   53.29400  1.000 80.95743  ?  87  VAL C CA  1 
ATOM   4097 C  C   . VAL C 1 87  ? 36.35200  7.77500   51.85700  1.000 88.45770  ?  87  VAL C C   1 
ATOM   4098 O  O   . VAL C 1 87  ? 36.89500  6.73400   51.47000  1.000 90.33138  ?  87  VAL C O   1 
ATOM   4099 C  CB  . VAL C 1 87  ? 34.33200  7.98800   53.36100  1.000 77.18348  ?  87  VAL C CB  1 
ATOM   4100 C  CG1 . VAL C 1 87  ? 33.71100  6.67900   52.89700  1.000 82.64977  ?  87  VAL C CG1 1 
ATOM   4101 C  CG2 . VAL C 1 87  ? 33.87600  8.34300   54.77000  1.000 77.39322  ?  87  VAL C CG2 1 
ATOM   4102 N  N   . LEU C 1 88  ? 36.15000  8.82100   51.05300  1.000 89.80360  ?  88  LEU C N   1 
ATOM   4103 C  CA  . LEU C 1 88  ? 36.57800  8.79300   49.66000  1.000 83.42969  ?  88  LEU C CA  1 
ATOM   4104 C  C   . LEU C 1 88  ? 38.07800  9.00500   49.49300  1.000 85.73158  ?  88  LEU C C   1 
ATOM   4105 O  O   . LEU C 1 88  ? 38.63100  8.61100   48.46000  1.000 88.51135  ?  88  LEU C O   1 
ATOM   4106 C  CB  . LEU C 1 88  ? 35.81400  9.85000   48.86300  1.000 82.90903  ?  88  LEU C CB  1 
ATOM   4107 C  CG  . LEU C 1 88  ? 34.29500  9.66500   48.87000  1.000 78.44455  ?  88  LEU C CG  1 
ATOM   4108 C  CD1 . LEU C 1 88  ? 33.62500  10.70300  47.98900  1.000 74.68738  ?  88  LEU C CD1 1 
ATOM   4109 C  CD2 . LEU C 1 88  ? 33.91100  8.25500   48.44500  1.000 73.79393  ?  88  LEU C CD2 1 
ATOM   4110 N  N   . GLU C 1 89  ? 38.74100  9.61500   50.48000  1.000 87.05804  ?  89  GLU C N   1 
ATOM   4111 C  CA  . GLU C 1 89  ? 40.19100  9.83300   50.46200  1.000 85.73881  ?  89  GLU C CA  1 
ATOM   4112 C  C   . GLU C 1 89  ? 40.63400  10.64400  49.24300  1.000 92.03869  ?  89  GLU C C   1 
ATOM   4113 O  O   . GLU C 1 89  ? 41.52100  10.24200  48.48700  1.000 91.95048  ?  89  GLU C O   1 
ATOM   4114 C  CB  . GLU C 1 89  ? 40.95200  8.50800   50.55100  1.000 81.98449  ?  89  GLU C CB  1 
ATOM   4115 C  CG  . GLU C 1 89  ? 40.80000  7.82100   51.89700  1.000 92.14866  ?  89  GLU C CG  1 
ATOM   4116 C  CD  . GLU C 1 89  ? 41.57700  6.52600   51.98800  1.000 96.65934  ?  89  GLU C CD  1 
ATOM   4117 O  OE1 . GLU C 1 89  ? 41.96000  5.98400   50.93000  1.000 79.38817  ?  89  GLU C OE1 1 
ATOM   4118 O  OE2 . GLU C 1 89  ? 41.81400  6.05600   53.12200  1.000 110.99770 -1 89  GLU C OE2 1 
ATOM   4119 N  N   . VAL C 1 90  ? 39.99400  11.79800  49.04900  1.000 90.98494  ?  90  VAL C N   1 
ATOM   4120 C  CA  . VAL C 1 90  ? 40.43100  12.72100  48.01000  1.000 87.59679  ?  90  VAL C CA  1 
ATOM   4121 C  C   . VAL C 1 90  ? 41.82000  13.24800  48.35200  1.000 88.75355  ?  90  VAL C C   1 
ATOM   4122 O  O   . VAL C 1 90  ? 42.17500  13.42300  49.52600  1.000 89.37715  ?  90  VAL C O   1 
ATOM   4123 C  CB  . VAL C 1 90  ? 39.42500  13.87500  47.84900  1.000 84.29261  ?  90  VAL C CB  1 
ATOM   4124 C  CG1 . VAL C 1 90  ? 38.05800  13.33800  47.45700  1.000 84.03678  ?  90  VAL C CG1 1 
ATOM   4125 C  CG2 . VAL C 1 90  ? 39.33200  14.69100  49.13500  1.000 76.45405  ?  90  VAL C CG2 1 
ATOM   4126 N  N   . GLU C 1 91  ? 42.62400  13.49500  47.31800  1.000 89.41496  ?  91  GLU C N   1 
ATOM   4127 C  CA  . GLU C 1 91  ? 43.97000  14.00800  47.51700  1.000 86.19959  ?  91  GLU C CA  1 
ATOM   4128 C  C   . GLU C 1 91  ? 44.10200  15.48200  47.16900  1.000 85.04237  ?  91  GLU C C   1 
ATOM   4129 O  O   . GLU C 1 91  ? 45.16000  16.06800  47.42300  1.000 86.70801  ?  91  GLU C O   1 
ATOM   4130 C  CB  . GLU C 1 91  ? 44.99000  13.19300  46.70700  1.000 86.68849  ?  91  GLU C CB  1 
ATOM   4131 C  CG  . GLU C 1 91  ? 44.73500  11.69400  46.73200  1.000 96.91560  ?  91  GLU C CG  1 
ATOM   4132 C  CD  . GLU C 1 91  ? 45.86000  10.89600  46.09800  1.000 105.96248 ?  91  GLU C CD  1 
ATOM   4133 O  OE1 . GLU C 1 91  ? 46.78400  11.51700  45.53200  1.000 114.21324 ?  91  GLU C OE1 1 
ATOM   4134 O  OE2 . GLU C 1 91  ? 45.80200  9.64600   46.14400  1.000 106.71908 -1 91  GLU C OE2 1 
ATOM   4135 N  N   . HIS C 1 92  ? 43.07500  16.08900  46.57700  1.000 81.98647  ?  92  HIS C N   1 
ATOM   4136 C  CA  . HIS C 1 92  ? 43.08600  17.51300  46.27100  1.000 82.31950  ?  92  HIS C CA  1 
ATOM   4137 C  C   . HIS C 1 92  ? 41.70200  18.07500  46.52600  1.000 79.28770  ?  92  HIS C C   1 
ATOM   4138 O  O   . HIS C 1 92  ? 40.70500  17.51800  46.05900  1.000 78.74714  ?  92  HIS C O   1 
ATOM   4139 C  CB  . HIS C 1 92  ? 43.49300  17.78600  44.82000  1.000 85.84475  ?  92  HIS C CB  1 
ATOM   4140 C  CG  . HIS C 1 92  ? 44.89500  17.38600  44.50700  1.000 84.66195  ?  92  HIS C CG  1 
ATOM   4141 N  ND1 . HIS C 1 92  ? 45.99400  18.11300  44.90500  1.000 88.59053  ?  92  HIS C ND1 1 
ATOM   4142 C  CD2 . HIS C 1 92  ? 45.37700  16.29200  43.88500  1.000 81.50774  ?  92  HIS C CD2 1 
ATOM   4143 C  CE1 . HIS C 1 92  ? 47.09500  17.49900  44.50200  1.000 95.84293  ?  92  HIS C CE1 1 
ATOM   4144 N  NE2 . HIS C 1 92  ? 46.74500  16.38600  43.88400  1.000 89.13725  ?  92  HIS C NE2 1 
ATOM   4145 N  N   . ILE C 1 93  ? 41.65600  19.19300  47.24000  1.000 75.54253  ?  93  ILE C N   1 
ATOM   4146 C  CA  . ILE C 1 93  ? 40.43200  19.94700  47.46300  1.000 76.23254  ?  93  ILE C CA  1 
ATOM   4147 C  C   . ILE C 1 93  ? 40.64100  21.32800  46.86800  1.000 73.19293  ?  93  ILE C C   1 
ATOM   4148 O  O   . ILE C 1 93  ? 41.61000  22.01600  47.21200  1.000 76.08673  ?  93  ILE C O   1 
ATOM   4149 C  CB  . ILE C 1 93  ? 40.08100  20.03800  48.95400  1.000 77.93734  ?  93  ILE C CB  1 
ATOM   4150 C  CG1 . ILE C 1 93  ? 40.01500  18.64200  49.57300  1.000 75.95625  ?  93  ILE C CG1 1 
ATOM   4151 C  CG2 . ILE C 1 93  ? 38.77000  20.77200  49.14000  1.000 70.15902  ?  93  ILE C CG2 1 
ATOM   4152 C  CD1 . ILE C 1 93  ? 39.71800  18.65200  51.05800  1.000 81.25341  ?  93  ILE C CD1 1 
ATOM   4153 N  N   . ILE C 1 94  ? 39.74800  21.72600  45.97000  1.000 71.42355  ?  94  ILE C N   1 
ATOM   4154 C  CA  . ILE C 1 94  ? 39.87000  22.98700  45.25200  1.000 72.61890  ?  94  ILE C CA  1 
ATOM   4155 C  C   . ILE C 1 94  ? 38.69400  23.87300  45.63400  1.000 68.02384  ?  94  ILE C C   1 
ATOM   4156 O  O   . ILE C 1 94  ? 37.53400  23.52000  45.38400  1.000 64.89543  ?  94  ILE C O   1 
ATOM   4157 C  CB  . ILE C 1 94  ? 39.93700  22.77000  43.73300  1.000 66.79295  ?  94  ILE C CB  1 
ATOM   4158 C  CG1 . ILE C 1 94  ? 41.21300  22.00300  43.37700  1.000 65.48962  ?  94  ILE C CG1 1 
ATOM   4159 C  CG2 . ILE C 1 94  ? 39.89700  24.10200  43.01200  1.000 65.72921  ?  94  ILE C CG2 1 
ATOM   4160 C  CD1 . ILE C 1 94  ? 41.05200  21.04000  42.22500  1.000 77.20544  ?  94  ILE C CD1 1 
ATOM   4161 N  N   . ILE C 1 95  ? 38.99400  25.01700  46.24000  1.000 69.07501  ?  95  ILE C N   1 
ATOM   4162 C  CA  . ILE C 1 95  ? 38.00700  26.05300  46.51400  1.000 73.89103  ?  95  ILE C CA  1 
ATOM   4163 C  C   . ILE C 1 95  ? 38.14900  27.10700  45.42800  1.000 73.01821  ?  95  ILE C C   1 
ATOM   4164 O  O   . ILE C 1 95  ? 39.20800  27.73100  45.29100  1.000 74.94978  ?  95  ILE C O   1 
ATOM   4165 C  CB  . ILE C 1 95  ? 38.19400  26.66400  47.91100  1.000 75.73776  ?  95  ILE C CB  1 
ATOM   4166 C  CG1 . ILE C 1 95  ? 38.03700  25.58900  48.99000  1.000 74.18759  ?  95  ILE C CG1 1 
ATOM   4167 C  CG2 . ILE C 1 95  ? 37.20200  27.79800  48.13400  1.000 71.36335  ?  95  ILE C CG2 1 
ATOM   4168 C  CD1 . ILE C 1 95  ? 38.18000  26.11200  50.40300  1.000 72.14996  ?  95  ILE C CD1 1 
ATOM   4169 N  N   . CYS C 1 96  ? 37.08500  27.30600  44.65500  1.000 69.80212  ?  96  CYS C N   1 
ATOM   4170 C  CA  . CYS C 1 96  ? 37.13100  28.15100  43.47000  1.000 74.75306  ?  96  CYS C CA  1 
ATOM   4171 C  C   . CYS C 1 96  ? 36.00800  29.17400  43.53000  1.000 68.88560  ?  96  CYS C C   1 
ATOM   4172 O  O   . CYS C 1 96  ? 34.82900  28.80700  43.56600  1.000 67.83276  ?  96  CYS C O   1 
ATOM   4173 C  CB  . CYS C 1 96  ? 37.01400  27.30200  42.20200  1.000 78.69701  ?  96  CYS C CB  1 
ATOM   4174 S  SG  . CYS C 1 96  ? 37.23900  28.19200  40.64900  1.000 78.23496  ?  96  CYS C SG  1 
ATOM   4175 N  N   . GLY C 1 97  ? 36.37700  30.45500  43.53700  1.000 70.04224  ?  97  GLY C N   1 
ATOM   4176 C  CA  . GLY C 1 97  ? 35.42900  31.53300  43.37600  1.000 74.87485  ?  97  GLY C CA  1 
ATOM   4177 C  C   . GLY C 1 97  ? 35.43600  32.06600  41.95000  1.000 83.93831  ?  97  GLY C C   1 
ATOM   4178 O  O   . GLY C 1 97  ? 36.16000  31.59700  41.07600  1.000 81.08618  ?  97  GLY C O   1 
ATOM   4179 N  N   . HIS C 1 98  ? 34.59700  33.07200  41.72300  1.000 81.88763  ?  98  HIS C N   1 
ATOM   4180 C  CA  . HIS C 1 98  ? 34.47900  33.64800  40.39100  1.000 79.87326  ?  98  HIS C CA  1 
ATOM   4181 C  C   . HIS C 1 98  ? 34.20200  35.13900  40.49300  1.000 80.04753  ?  98  HIS C C   1 
ATOM   4182 O  O   . HIS C 1 98  ? 33.29100  35.55600  41.21300  1.000 79.16755  ?  98  HIS C O   1 
ATOM   4183 C  CB  . HIS C 1 98  ? 33.38000  32.94300  39.58500  1.000 83.01919  ?  98  HIS C CB  1 
ATOM   4184 C  CG  . HIS C 1 98  ? 32.03200  32.98500  40.23300  1.000 80.65117  ?  98  HIS C CG  1 
ATOM   4185 N  ND1 . HIS C 1 98  ? 30.99000  33.73700  39.73600  1.000 78.60806  ?  98  HIS C ND1 1 
ATOM   4186 C  CD2 . HIS C 1 98  ? 31.55200  32.35900  41.33400  1.000 81.53128  ?  98  HIS C CD2 1 
ATOM   4187 C  CE1 . HIS C 1 98  ? 29.92800  33.57800  40.50600  1.000 79.52309  ?  98  HIS C CE1 1 
ATOM   4188 N  NE2 . HIS C 1 98  ? 30.24200  32.74600  41.48200  1.000 80.63315  ?  98  HIS C NE2 1 
ATOM   4189 N  N   . TYR C 1 99  ? 34.99300  35.92700  39.76500  1.000 81.67456  ?  99  TYR C N   1 
ATOM   4190 C  CA  . TYR C 1 99  ? 34.81900  37.37300  39.74800  1.000 74.49151  ?  99  TYR C CA  1 
ATOM   4191 C  C   . TYR C 1 99  ? 33.43800  37.72700  39.21100  1.000 69.14224  ?  99  TYR C C   1 
ATOM   4192 O  O   . TYR C 1 99  ? 32.94900  37.11900  38.25600  1.000 84.70054  ?  99  TYR C O   1 
ATOM   4193 C  CB  . TYR C 1 99  ? 35.90000  38.02300  38.88700  1.000 82.98557  ?  99  TYR C CB  1 
ATOM   4194 C  CG  . TYR C 1 99  ? 37.31100  37.60800  39.24000  1.000 81.77792  ?  99  TYR C CG  1 
ATOM   4195 C  CD1 . TYR C 1 99  ? 38.01700  38.24700  40.25100  1.000 78.75999  ?  99  TYR C CD1 1 
ATOM   4196 C  CD2 . TYR C 1 99  ? 37.93600  36.56900  38.56300  1.000 87.57924  ?  99  TYR C CD2 1 
ATOM   4197 C  CE1 . TYR C 1 99  ? 39.30800  37.86600  40.57000  1.000 84.26410  ?  99  TYR C CE1 1 
ATOM   4198 C  CE2 . TYR C 1 99  ? 39.22300  36.18000  38.87500  1.000 85.09079  ?  99  TYR C CE2 1 
ATOM   4199 C  CZ  . TYR C 1 99  ? 39.90500  36.83100  39.87900  1.000 86.49875  ?  99  TYR C CZ  1 
ATOM   4200 O  OH  . TYR C 1 99  ? 41.18900  36.44400  40.19000  1.000 93.10270  ?  99  TYR C OH  1 
ATOM   4201 N  N   . GLY C 1 100 ? 32.80400  38.71100  39.83900  1.000 65.19209  ?  100 GLY C N   1 
ATOM   4202 C  CA  . GLY C 1 100 ? 31.45400  39.08100  39.47900  1.000 71.78673  ?  100 GLY C CA  1 
ATOM   4203 C  C   . GLY C 1 100 ? 30.37700  38.34300  40.23500  1.000 76.91798  ?  100 GLY C C   1 
ATOM   4204 O  O   . GLY C 1 100 ? 29.19800  38.46900  39.88000  1.000 76.00634  ?  100 GLY C O   1 
ATOM   4205 N  N   . CYS C 1 101 ? 30.74600  37.55700  41.24700  1.000 78.22707  ?  101 CYS C N   1 
ATOM   4206 C  CA  . CYS C 1 101 ? 29.78600  36.76600  42.00600  1.000 79.99057  ?  101 CYS C CA  1 
ATOM   4207 C  C   . CYS C 1 101 ? 28.66500  37.63200  42.56100  1.000 77.73331  ?  101 CYS C C   1 
ATOM   4208 O  O   . CYS C 1 101 ? 28.91000  38.68100  43.16500  1.000 74.91856  ?  101 CYS C O   1 
ATOM   4209 C  CB  . CYS C 1 101 ? 30.49400  36.03800  43.15000  1.000 76.39928  ?  101 CYS C CB  1 
ATOM   4210 S  SG  . CYS C 1 101 ? 29.37500  35.10200  44.21800  1.000 65.25880  ?  101 CYS C SG  1 
ATOM   4211 N  N   . GLY C 1 102 ? 27.42800  37.18400  42.34800  1.000 77.10823  ?  102 GLY C N   1 
ATOM   4212 C  CA  . GLY C 1 102 ? 26.28700  37.92100  42.85900  1.000 77.45202  ?  102 GLY C CA  1 
ATOM   4213 C  C   . GLY C 1 102 ? 26.26000  37.98100  44.37300  1.000 79.68405  ?  102 GLY C C   1 
ATOM   4214 O  O   . GLY C 1 102 ? 25.83500  38.98400  44.94900  1.000 83.44680  ?  102 GLY C O   1 
ATOM   4215 N  N   . GLY C 1 103 ? 26.70700  36.91300  45.03600  1.000 75.67263  ?  103 GLY C N   1 
ATOM   4216 C  CA  . GLY C 1 103 ? 26.72600  36.91400  46.49000  1.000 79.64844  ?  103 GLY C CA  1 
ATOM   4217 C  C   . GLY C 1 103 ? 27.73800  37.89000  47.06000  1.000 77.56863  ?  103 GLY C C   1 
ATOM   4218 O  O   . GLY C 1 103 ? 27.43500  38.64500  47.98700  1.000 80.07966  ?  103 GLY C O   1 
ATOM   4219 N  N   . VAL C 1 104 ? 28.95600  37.89200  46.50800  1.000 76.05822  ?  104 VAL C N   1 
ATOM   4220 C  CA  . VAL C 1 104 ? 29.98600  38.81300  46.98200  1.000 71.93504  ?  104 VAL C CA  1 
ATOM   4221 C  C   . VAL C 1 104 ? 29.56100  40.25400  46.73400  1.000 78.44271  ?  104 VAL C C   1 
ATOM   4222 O  O   . VAL C 1 104 ? 29.80400  41.14300  47.55900  1.000 82.81386  ?  104 VAL C O   1 
ATOM   4223 C  CB  . VAL C 1 104 ? 31.33700  38.49100  46.31600  1.000 70.62486  ?  104 VAL C CB  1 
ATOM   4224 C  CG1 . VAL C 1 104 ? 32.39900  39.48000  46.75900  1.000 76.59107  ?  104 VAL C CG1 1 
ATOM   4225 C  CG2 . VAL C 1 104 ? 31.76400  37.07200  46.65100  1.000 65.17315  ?  104 VAL C CG2 1 
ATOM   4226 N  N   . GLN C 1 105 ? 28.90800  40.50400  45.59700  1.000 79.11865  ?  105 GLN C N   1 
ATOM   4227 C  CA  . GLN C 1 105 ? 28.41400  41.84500  45.30600  1.000 82.07299  ?  105 GLN C CA  1 
ATOM   4228 C  C   . GLN C 1 105 ? 27.25500  42.21100  46.22500  1.000 85.30405  ?  105 GLN C C   1 
ATOM   4229 O  O   . GLN C 1 105 ? 27.14100  43.36200  46.66200  1.000 88.04193  ?  105 GLN C O   1 
ATOM   4230 C  CB  . GLN C 1 105 ? 27.99800  41.94300  43.84000  1.000 87.95119  ?  105 GLN C CB  1 
ATOM   4231 C  CG  . GLN C 1 105 ? 27.60500  43.33700  43.39500  1.000 91.51497  ?  105 GLN C CG  1 
ATOM   4232 C  CD  . GLN C 1 105 ? 26.99100  43.35000  42.01100  1.000 103.14628 ?  105 GLN C CD  1 
ATOM   4233 O  OE1 . GLN C 1 105 ? 26.68300  42.30000  41.44600  1.000 102.19441 ?  105 GLN C OE1 1 
ATOM   4234 N  NE2 . GLN C 1 105 ? 26.80700  44.54200  41.45700  1.000 110.08878 ?  105 GLN C NE2 1 
ATOM   4235 N  N   . ALA C 1 106 ? 26.37400  41.25000  46.51500  1.000 85.76047  ?  106 ALA C N   1 
ATOM   4236 C  CA  . ALA C 1 106 ? 25.29000  41.50900  47.45600  1.000 84.71110  ?  106 ALA C CA  1 
ATOM   4237 C  C   . ALA C 1 106 ? 25.83400  41.76700  48.85400  1.000 85.28357  ?  106 ALA C C   1 
ATOM   4238 O  O   . ALA C 1 106 ? 25.28300  42.58500  49.60100  1.000 86.69982  ?  106 ALA C O   1 
ATOM   4239 C  CB  . ALA C 1 106 ? 24.30900  40.33700  47.46800  1.000 75.36153  ?  106 ALA C CB  1 
ATOM   4240 N  N   . ALA C 1 107 ? 26.90600  41.06500  49.23100  1.000 83.12575  ?  107 ALA C N   1 
ATOM   4241 C  CA  . ALA C 1 107 ? 27.55000  41.32100  50.51600  1.000 85.00466  ?  107 ALA C CA  1 
ATOM   4242 C  C   . ALA C 1 107 ? 28.00800  42.77100  50.63000  1.000 90.23293  ?  107 ALA C C   1 
ATOM   4243 O  O   . ALA C 1 107 ? 27.84200  43.40100  51.68100  1.000 91.05196  ?  107 ALA C O   1 
ATOM   4244 C  CB  . ALA C 1 107 ? 28.72900  40.36800  50.71000  1.000 72.80562  ?  107 ALA C CB  1 
ATOM   4245 N  N   . VAL C 1 108 ? 28.58100  43.31800  49.55700  1.000 82.78268  ?  108 VAL C N   1 
ATOM   4246 C  CA  . VAL C 1 108 ? 29.14500  44.66400  49.61400  1.000 83.80180  ?  108 VAL C CA  1 
ATOM   4247 C  C   . VAL C 1 108 ? 28.05000  45.72000  49.52800  1.000 85.16446  ?  108 VAL C C   1 
ATOM   4248 O  O   . VAL C 1 108 ? 28.03800  46.68400  50.30300  1.000 90.86585  ?  108 VAL C O   1 
ATOM   4249 C  CB  . VAL C 1 108 ? 30.19900  44.84700  48.50700  1.000 90.83452  ?  108 VAL C CB  1 
ATOM   4250 C  CG1 . VAL C 1 108 ? 30.69900  46.28100  48.48200  1.000 94.09757  ?  108 VAL C CG1 1 
ATOM   4251 C  CG2 . VAL C 1 108 ? 31.35600  43.89200  48.72900  1.000 86.86183  ?  108 VAL C CG2 1 
ATOM   4252 N  N   . GLU C 1 109 ? 27.11400  45.56700  48.58900  1.000 83.58416  ?  109 GLU C N   1 
ATOM   4253 C  CA  . GLU C 1 109 ? 26.05200  46.55600  48.44700  1.000 89.37316  ?  109 GLU C CA  1 
ATOM   4254 C  C   . GLU C 1 109 ? 24.99300  46.43500  49.53400  1.000 87.72328  ?  109 GLU C C   1 
ATOM   4255 O  O   . GLU C 1 109 ? 24.21900  47.37800  49.73100  1.000 82.92531  ?  109 GLU C O   1 
ATOM   4256 C  CB  . GLU C 1 109 ? 25.40200  46.45500  47.06300  1.000 92.31752  ?  109 GLU C CB  1 
ATOM   4257 C  CG  . GLU C 1 109 ? 26.38600  46.60900  45.91100  1.000 96.10664  ?  109 GLU C CG  1 
ATOM   4258 C  CD  . GLU C 1 109 ? 25.84000  46.09200  44.59500  1.000 105.53079 ?  109 GLU C CD  1 
ATOM   4259 O  OE1 . GLU C 1 109 ? 24.97500  45.19100  44.61700  1.000 106.97099 ?  109 GLU C OE1 1 
ATOM   4260 O  OE2 . GLU C 1 109 ? 26.27500  46.59300  43.53600  1.000 105.97983 -1 109 GLU C OE2 1 
ATOM   4261 N  N   . ASN C 1 110 ? 24.96300  45.31000  50.24500  1.000 90.86192  ?  110 ASN C N   1 
ATOM   4262 C  CA  . ASN C 1 110 ? 24.05800  45.08600  51.36900  1.000 89.05272  ?  110 ASN C CA  1 
ATOM   4263 C  C   . ASN C 1 110 ? 22.60100  45.46700  51.09000  1.000 88.30300  ?  110 ASN C C   1 
ATOM   4264 O  O   . ASN C 1 110 ? 22.04000  46.33500  51.77300  1.000 87.41529  ?  110 ASN C O   1 
ATOM   4265 C  CB  . ASN C 1 110 ? 24.57900  45.82400  52.59500  1.000 82.40110  ?  110 ASN C CB  1 
ATOM   4266 C  CG  . ASN C 1 110 ? 23.98600  45.30500  53.89100  1.000 90.81550  ?  110 ASN C CG  1 
ATOM   4267 O  OD1 . ASN C 1 110 ? 23.14900  44.40300  53.89100  1.000 91.97314  ?  110 ASN C OD1 1 
ATOM   4268 N  ND2 . ASN C 1 110 ? 24.42700  45.87100  55.00900  1.000 94.32785  ?  110 ASN C ND2 1 
ATOM   4269 N  N   . PRO C 1 111 ? 21.95900  44.85100  50.10100  1.000 83.97944  ?  111 PRO C N   1 
ATOM   4270 C  CA  . PRO C 1 111 ? 20.51400  45.02300  49.94400  1.000 84.86861  ?  111 PRO C CA  1 
ATOM   4271 C  C   . PRO C 1 111 ? 19.73800  44.08100  50.85500  1.000 85.39658  ?  111 PRO C C   1 
ATOM   4272 O  O   . PRO C 1 111 ? 20.23800  43.05000  51.30800  1.000 85.80227  ?  111 PRO C O   1 
ATOM   4273 C  CB  . PRO C 1 111 ? 20.27600  44.68400  48.47000  1.000 82.64756  ?  111 PRO C CB  1 
ATOM   4274 C  CG  . PRO C 1 111 ? 21.33800  43.69500  48.15100  1.000 82.14012  ?  111 PRO C CG  1 
ATOM   4275 C  CD  . PRO C 1 111 ? 22.51800  43.98200  49.04800  1.000 82.88313  ?  111 PRO C CD  1 
ATOM   4276 N  N   . GLU C 1 112 ? 18.49300  44.46500  51.12600  1.000 79.63791  ?  112 GLU C N   1 
ATOM   4277 C  CA  . GLU C 1 112 ? 17.59300  43.64800  51.94000  1.000 84.23663  ?  112 GLU C CA  1 
ATOM   4278 C  C   . GLU C 1 112 ? 17.04800  42.52600  51.06800  1.000 79.12416  ?  112 GLU C C   1 
ATOM   4279 O  O   . GLU C 1 112 ? 16.04800  42.68200  50.36500  1.000 81.38339  ?  112 GLU C O   1 
ATOM   4280 C  CB  . GLU C 1 112 ? 16.46600  44.49400  52.51800  1.000 90.89093  ?  112 GLU C CB  1 
ATOM   4281 C  CG  . GLU C 1 112 ? 16.89400  45.42500  53.63200  1.000 90.45037  ?  112 GLU C CG  1 
ATOM   4282 C  CD  . GLU C 1 112 ? 15.77700  46.34900  54.06400  1.000 105.66173 ?  112 GLU C CD  1 
ATOM   4283 O  OE1 . GLU C 1 112 ? 14.60600  45.91500  54.03600  1.000 106.27979 ?  112 GLU C OE1 1 
ATOM   4284 O  OE2 . GLU C 1 112 ? 16.06700  47.50800  54.42900  1.000 116.79931 -1 112 GLU C OE2 1 
ATOM   4285 N  N   . LEU C 1 113 ? 17.70900  41.37100  51.12000  1.000 80.06554  ?  113 LEU C N   1 
ATOM   4286 C  CA  . LEU C 1 113 ? 17.32800  40.23100  50.29900  1.000 75.84910  ?  113 LEU C CA  1 
ATOM   4287 C  C   . LEU C 1 113 ? 16.59200  39.15000  51.07700  1.000 74.29285  ?  113 LEU C C   1 
ATOM   4288 O  O   . LEU C 1 113 ? 16.03800  38.23500  50.45900  1.000 68.72080  ?  113 LEU C O   1 
ATOM   4289 C  CB  . LEU C 1 113 ? 18.56700  39.61400  49.64000  1.000 72.10210  ?  113 LEU C CB  1 
ATOM   4290 C  CG  . LEU C 1 113 ? 19.49000  40.55900  48.87700  1.000 68.37108  ?  113 LEU C CG  1 
ATOM   4291 C  CD1 . LEU C 1 113 ? 20.69900  39.80300  48.34700  1.000 64.74123  ?  113 LEU C CD1 1 
ATOM   4292 C  CD2 . LEU C 1 113 ? 18.73400  41.23800  47.74900  1.000 78.95878  ?  113 LEU C CD2 1 
ATOM   4293 N  N   . GLY C 1 114 ? 16.56700  39.23100  52.40400  1.000 80.73628  ?  114 GLY C N   1 
ATOM   4294 C  CA  . GLY C 1 114 ? 15.89100  38.22200  53.19100  1.000 71.48702  ?  114 GLY C CA  1 
ATOM   4295 C  C   . GLY C 1 114 ? 16.84200  37.27600  53.89400  1.000 67.86729  ?  114 GLY C C   1 
ATOM   4296 O  O   . GLY C 1 114 ? 17.88700  37.69400  54.40300  1.000 69.76005  ?  114 GLY C O   1 
ATOM   4297 N  N   . LEU C 1 115 ? 16.47300  35.99300  53.92700  1.000 64.86985  ?  115 LEU C N   1 
ATOM   4298 C  CA  . LEU C 1 115 ? 17.22900  34.99100  54.67500  1.000 63.47934  ?  115 LEU C CA  1 
ATOM   4299 C  C   . LEU C 1 115 ? 18.69300  34.91400  54.25000  1.000 66.40322  ?  115 LEU C C   1 
ATOM   4300 O  O   . LEU C 1 115 ? 19.56200  34.62500  55.08100  1.000 65.45006  ?  115 LEU C O   1 
ATOM   4301 C  CB  . LEU C 1 115 ? 16.56800  33.62500  54.50200  1.000 58.47404  ?  115 LEU C CB  1 
ATOM   4302 C  CG  . LEU C 1 115 ? 17.25600  32.41600  55.13400  1.000 68.76631  ?  115 LEU C CG  1 
ATOM   4303 C  CD1 . LEU C 1 115 ? 17.32100  32.56400  56.64900  1.000 73.06915  ?  115 LEU C CD1 1 
ATOM   4304 C  CD2 . LEU C 1 115 ? 16.56500  31.12100  54.73000  1.000 69.16299  ?  115 LEU C CD2 1 
ATOM   4305 N  N   . ILE C 1 116 ? 18.98700  35.16700  52.97100  1.000 71.28208  ?  116 ILE C N   1 
ATOM   4306 C  CA  . ILE C 1 116 ? 20.34700  34.99100  52.46500  1.000 67.77230  ?  116 ILE C CA  1 
ATOM   4307 C  C   . ILE C 1 116 ? 21.32000  35.97300  53.10900  1.000 66.50007  ?  116 ILE C C   1 
ATOM   4308 O  O   . ILE C 1 116 ? 22.52200  35.69000  53.20200  1.000 63.28779  ?  116 ILE C O   1 
ATOM   4309 C  CB  . ILE C 1 116 ? 20.35400  35.10000  50.92600  1.000 66.13218  ?  116 ILE C CB  1 
ATOM   4310 C  CG1 . ILE C 1 116 ? 21.76300  34.88900  50.36100  1.000 61.38704  ?  116 ILE C CG1 1 
ATOM   4311 C  CG2 . ILE C 1 116 ? 19.78900  36.43500  50.48300  1.000 67.19189  ?  116 ILE C CG2 1 
ATOM   4312 C  CD1 . ILE C 1 116 ? 22.31900  33.50800  50.59100  1.000 64.48201  ?  116 ILE C CD1 1 
ATOM   4313 N  N   . ASN C 1 117 ? 20.83100  37.12900  53.57300  1.000 61.52476  ?  117 ASN C N   1 
ATOM   4314 C  CA  . ASN C 1 117 ? 21.72500  38.13900  54.13500  1.000 64.88073  ?  117 ASN C CA  1 
ATOM   4315 C  C   . ASN C 1 117 ? 22.54500  37.59300  55.29800  1.000 76.41530  ?  117 ASN C C   1 
ATOM   4316 O  O   . ASN C 1 117 ? 23.70100  37.99400  55.48000  1.000 77.10501  ?  117 ASN C O   1 
ATOM   4317 C  CB  . ASN C 1 117 ? 20.92400  39.36100  54.58700  1.000 67.78869  ?  117 ASN C CB  1 
ATOM   4318 C  CG  . ASN C 1 117 ? 20.58200  40.29500  53.44500  1.000 72.79179  ?  117 ASN C CG  1 
ATOM   4319 O  OD1 . ASN C 1 117 ? 20.57800  39.89800  52.28100  1.000 79.41136  ?  117 ASN C OD1 1 
ATOM   4320 N  ND2 . ASN C 1 117 ? 20.28000  41.54500  53.77600  1.000 76.21254  ?  117 ASN C ND2 1 
ATOM   4321 N  N   . ASN C 1 118 ? 21.97400  36.68000  56.09100  1.000 73.96310  ?  118 ASN C N   1 
ATOM   4322 C  CA  . ASN C 1 118 ? 22.72400  36.10600  57.20600  1.000 67.92072  ?  118 ASN C CA  1 
ATOM   4323 C  C   . ASN C 1 118 ? 23.89000  35.25800  56.71200  1.000 67.71963  ?  118 ASN C C   1 
ATOM   4324 O  O   . ASN C 1 118 ? 24.99000  35.32000  57.27400  1.000 67.63300  ?  118 ASN C O   1 
ATOM   4325 C  CB  . ASN C 1 118 ? 21.80300  35.27100  58.09500  1.000 69.14560  ?  118 ASN C CB  1 
ATOM   4326 C  CG  . ASN C 1 118 ? 20.62700  36.06300  58.62200  1.000 71.84024  ?  118 ASN C CG  1 
ATOM   4327 O  OD1 . ASN C 1 118 ? 20.78600  36.95100  59.46200  1.000 73.80862  ?  118 ASN C OD1 1 
ATOM   4328 N  ND2 . ASN C 1 118 ? 19.43200  35.73500  58.14400  1.000 63.77852  ?  118 ASN C ND2 1 
ATOM   4329 N  N   . TRP C 1 119 ? 23.67000  34.46100  55.66300  1.000 72.27398  ?  119 TRP C N   1 
ATOM   4330 C  CA  . TRP C 1 119 ? 24.76000  33.68200  55.08400  1.000 75.50193  ?  119 TRP C CA  1 
ATOM   4331 C  C   . TRP C 1 119 ? 25.88000  34.58800  54.58600  1.000 78.65615  ?  119 TRP C C   1 
ATOM   4332 O  O   . TRP C 1 119 ? 27.06500  34.28300  54.76800  1.000 76.44663  ?  119 TRP C O   1 
ATOM   4333 C  CB  . TRP C 1 119 ? 24.23200  32.80700  53.94500  1.000 74.40452  ?  119 TRP C CB  1 
ATOM   4334 C  CG  . TRP C 1 119 ? 25.25300  31.85600  53.38100  1.000 72.81853  ?  119 TRP C CG  1 
ATOM   4335 C  CD1 . TRP C 1 119 ? 26.09000  32.08200  52.32400  1.000 64.02644  ?  119 TRP C CD1 1 
ATOM   4336 C  CD2 . TRP C 1 119 ? 25.52900  30.52200  53.83000  1.000 73.76511  ?  119 TRP C CD2 1 
ATOM   4337 N  NE1 . TRP C 1 119 ? 26.87500  30.97700  52.09600  1.000 58.53561  ?  119 TRP C NE1 1 
ATOM   4338 C  CE2 . TRP C 1 119 ? 26.55100  30.00600  53.00600  1.000 63.64913  ?  119 TRP C CE2 1 
ATOM   4339 C  CE3 . TRP C 1 119 ? 25.01400  29.71500  54.85000  1.000 69.67553  ?  119 TRP C CE3 1 
ATOM   4340 C  CZ2 . TRP C 1 119 ? 27.06800  28.72200  53.17100  1.000 66.56097  ?  119 TRP C CZ2 1 
ATOM   4341 C  CZ3 . TRP C 1 119 ? 25.53000  28.44100  55.01400  1.000 68.84423  ?  119 TRP C CZ3 1 
ATOM   4342 C  CH2 . TRP C 1 119 ? 26.54500  27.95600  54.17700  1.000 70.38104  ?  119 TRP C CH2 1 
ATOM   4343 N  N   . LEU C 1 120 ? 25.52300  35.70800  53.95100  1.000 73.00259  ?  120 LEU C N   1 
ATOM   4344 C  CA  . LEU C 1 120 ? 26.51300  36.61500  53.38600  1.000 72.88676  ?  120 LEU C CA  1 
ATOM   4345 C  C   . LEU C 1 120 ? 27.24900  37.44000  54.43600  1.000 77.27591  ?  120 LEU C C   1 
ATOM   4346 O  O   . LEU C 1 120 ? 28.25100  38.07900  54.09300  1.000 73.45314  ?  120 LEU C O   1 
ATOM   4347 C  CB  . LEU C 1 120 ? 25.84400  37.54800  52.37500  1.000 74.77631  ?  120 LEU C CB  1 
ATOM   4348 C  CG  . LEU C 1 120 ? 25.12200  36.85200  51.22100  1.000 68.47988  ?  120 LEU C CG  1 
ATOM   4349 C  CD1 . LEU C 1 120 ? 24.50400  37.87200  50.28400  1.000 66.05298  ?  120 LEU C CD1 1 
ATOM   4350 C  CD2 . LEU C 1 120 ? 26.07900  35.94200  50.47100  1.000 67.52502  ?  120 LEU C CD2 1 
ATOM   4351 N  N   . LEU C 1 121 ? 26.79300  37.44700  55.69400  1.000 78.30106  ?  121 LEU C N   1 
ATOM   4352 C  CA  . LEU C 1 121 ? 27.50300  38.21200  56.71800  1.000 75.10634  ?  121 LEU C CA  1 
ATOM   4353 C  C   . LEU C 1 121 ? 28.90300  37.66700  56.95600  1.000 73.20875  ?  121 LEU C C   1 
ATOM   4354 O  O   . LEU C 1 121 ? 29.78900  38.40700  57.39800  1.000 77.04594  ?  121 LEU C O   1 
ATOM   4355 C  CB  . LEU C 1 121 ? 26.71400  38.23000  58.02800  1.000 69.90668  ?  121 LEU C CB  1 
ATOM   4356 C  CG  . LEU C 1 121 ? 25.54900  39.21800  58.09800  1.000 69.98302  ?  121 LEU C CG  1 
ATOM   4357 C  CD1 . LEU C 1 121 ? 24.73000  38.99300  59.35900  1.000 71.22718  ?  121 LEU C CD1 1 
ATOM   4358 C  CD2 . LEU C 1 121 ? 26.06300  40.64900  58.02900  1.000 69.75080  ?  121 LEU C CD2 1 
ATOM   4359 N  N   . HIS C 1 122 ? 29.12300  36.38200  56.67400  1.000 67.01964  ?  122 HIS C N   1 
ATOM   4360 C  CA  . HIS C 1 122 ? 30.47100  35.83600  56.76400  1.000 68.71826  ?  122 HIS C CA  1 
ATOM   4361 C  C   . HIS C 1 122 ? 31.40100  36.49100  55.75100  1.000 79.22805  ?  122 HIS C C   1 
ATOM   4362 O  O   . HIS C 1 122 ? 32.60900  36.59500  55.99400  1.000 79.98959  ?  122 HIS C O   1 
ATOM   4363 C  CB  . HIS C 1 122 ? 30.43400  34.32000  56.57100  1.000 68.45179  ?  122 HIS C CB  1 
ATOM   4364 C  CG  . HIS C 1 122 ? 29.75700  33.58800  57.68900  1.000 80.56552  ?  122 HIS C CG  1 
ATOM   4365 N  ND1 . HIS C 1 122 ? 30.39200  33.28800  58.87500  1.000 84.06525  ?  122 HIS C ND1 1 
ATOM   4366 C  CD2 . HIS C 1 122 ? 28.49500  33.11200  57.80800  1.000 81.17545  ?  122 HIS C CD2 1 
ATOM   4367 C  CE1 . HIS C 1 122 ? 29.55400  32.65000  59.67200  1.000 79.67996  ?  122 HIS C CE1 1 
ATOM   4368 N  NE2 . HIS C 1 122 ? 28.39500  32.53100  59.04800  1.000 81.58547  ?  122 HIS C NE2 1 
ATOM   4369 N  N   . ILE C 1 123 ? 30.85900  36.94100  54.61800  1.000 80.84282  ?  123 ILE C N   1 
ATOM   4370 C  CA  . ILE C 1 123 ? 31.66600  37.65600  53.63500  1.000 80.87984  ?  123 ILE C CA  1 
ATOM   4371 C  C   . ILE C 1 123 ? 31.93200  39.08600  54.08700  1.000 84.58141  ?  123 ILE C C   1 
ATOM   4372 O  O   . ILE C 1 123 ? 33.05000  39.59300  53.94200  1.000 88.89873  ?  123 ILE C O   1 
ATOM   4373 C  CB  . ILE C 1 123 ? 30.98300  37.61900  52.25700  1.000 78.09189  ?  123 ILE C CB  1 
ATOM   4374 C  CG1 . ILE C 1 123 ? 30.73100  36.17600  51.82700  1.000 75.90289  ?  123 ILE C CG1 1 
ATOM   4375 C  CG2 . ILE C 1 123 ? 31.82900  38.34200  51.22000  1.000 71.04818  ?  123 ILE C CG2 1 
ATOM   4376 C  CD1 . ILE C 1 123 ? 29.65500  36.04900  50.78700  1.000 65.47480  ?  123 ILE C CD1 1 
ATOM   4377 N  N   . ARG C 1 124 ? 30.91200  39.76300  54.62800  1.000 78.91166  ?  124 ARG C N   1 
ATOM   4378 C  CA  . ARG C 1 124 ? 31.11700  41.11000  55.15300  1.000 80.47892  ?  124 ARG C CA  1 
ATOM   4379 C  C   . ARG C 1 124 ? 32.17100  41.12500  56.25000  1.000 85.41517  ?  124 ARG C C   1 
ATOM   4380 O  O   . ARG C 1 124 ? 32.90800  42.10800  56.38900  1.000 87.64201  ?  124 ARG C O   1 
ATOM   4381 C  CB  . ARG C 1 124 ? 29.79900  41.67900  55.68300  1.000 74.60722  ?  124 ARG C CB  1 
ATOM   4382 C  CG  . ARG C 1 124 ? 28.76700  41.99200  54.61100  1.000 82.09494  ?  124 ARG C CG  1 
ATOM   4383 C  CD  . ARG C 1 124 ? 27.53500  42.66700  55.20500  1.000 80.58553  ?  124 ARG C CD  1 
ATOM   4384 N  NE  . ARG C 1 124 ? 27.83500  43.95000  55.83100  1.000 81.03649  ?  124 ARG C NE  1 
ATOM   4385 C  CZ  . ARG C 1 124 ? 27.75800  45.12000  55.21200  1.000 81.75037  ?  124 ARG C CZ  1 
ATOM   4386 N  NH1 . ARG C 1 124 ? 27.40300  45.20700  53.94100  1.000 85.18141  ?  124 ARG C NH1 1 
ATOM   4387 N  NH2 . ARG C 1 124 ? 28.04100  46.23200  55.88600  1.000 77.14371  ?  124 ARG C NH2 1 
ATOM   4388 N  N   . ASP C 1 125 ? 32.25000  40.05600  57.04500  1.000 91.08811  ?  125 ASP C N   1 
ATOM   4389 C  CA  . ASP C 1 125 ? 33.33800  39.92900  58.00800  1.000 91.89335  ?  125 ASP C CA  1 
ATOM   4390 C  C   . ASP C 1 125 ? 34.69400  39.91800  57.30900  1.000 94.35489  ?  125 ASP C C   1 
ATOM   4391 O  O   . ASP C 1 125 ? 35.66200  40.50600  57.80500  1.000 100.59529 ?  125 ASP C O   1 
ATOM   4392 C  CB  . ASP C 1 125 ? 33.14300  38.67000  58.85200  1.000 88.45779  ?  125 ASP C CB  1 
ATOM   4393 C  CG  . ASP C 1 125 ? 31.99700  38.80500  59.83800  1.000 90.76540  ?  125 ASP C CG  1 
ATOM   4394 O  OD1 . ASP C 1 125 ? 31.48300  39.93400  59.99900  1.000 90.38987  ?  125 ASP C OD1 1 
ATOM   4395 O  OD2 . ASP C 1 125 ? 31.61200  37.78700  60.45100  1.000 88.92702  -1 125 ASP C OD2 1 
ATOM   4396 N  N   . ILE C 1 126 ? 34.78200  39.25300  56.15400  1.000 87.71770  ?  126 ILE C N   1 
ATOM   4397 C  CA  . ILE C 1 126 ? 36.01500  39.28100  55.37200  1.000 97.78069  ?  126 ILE C CA  1 
ATOM   4398 C  C   . ILE C 1 126 ? 36.22800  40.66200  54.76200  1.000 98.06284  ?  126 ILE C C   1 
ATOM   4399 O  O   . ILE C 1 126 ? 37.36800  41.06400  54.49600  1.000 93.68765  ?  126 ILE C O   1 
ATOM   4400 C  CB  . ILE C 1 126 ? 35.98600  38.17800  54.29400  1.000 98.70063  ?  126 ILE C CB  1 
ATOM   4401 C  CG1 . ILE C 1 126 ? 35.66700  36.82000  54.92400  1.000 91.59022  ?  126 ILE C CG1 1 
ATOM   4402 C  CG2 . ILE C 1 126 ? 37.31000  38.11200  53.54300  1.000 86.74380  ?  126 ILE C CG2 1 
ATOM   4403 C  CD1 . ILE C 1 126 ? 36.65900  36.38200  55.97700  1.000 84.90264  ?  126 ILE C CD1 1 
ATOM   4404 N  N   . TRP C 1 127 ? 35.14600  41.41200  54.53800  1.000 94.26703  ?  127 TRP C N   1 
ATOM   4405 C  CA  . TRP C 1 127 ? 35.26600  42.76600  54.00500  1.000 89.16199  ?  127 TRP C CA  1 
ATOM   4406 C  C   . TRP C 1 127 ? 35.95100  43.70200  54.99300  1.000 94.76401  ?  127 TRP C C   1 
ATOM   4407 O  O   . TRP C 1 127 ? 36.84600  44.46800  54.61800  1.000 96.84909  ?  127 TRP C O   1 
ATOM   4408 C  CB  . TRP C 1 127 ? 33.88500  43.30700  53.63600  1.000 85.96457  ?  127 TRP C CB  1 
ATOM   4409 C  CG  . TRP C 1 127 ? 33.91600  44.68900  53.05400  1.000 95.33900  ?  127 TRP C CG  1 
ATOM   4410 C  CD1 . TRP C 1 127 ? 33.54900  45.84300  53.68300  1.000 94.16779  ?  127 TRP C CD1 1 
ATOM   4411 C  CD2 . TRP C 1 127 ? 34.33400  45.06700  51.73600  1.000 99.85914  ?  127 TRP C CD2 1 
ATOM   4412 N  NE1 . TRP C 1 127 ? 33.71200  46.91500  52.84100  1.000 95.79082  ?  127 TRP C NE1 1 
ATOM   4413 C  CE2 . TRP C 1 127 ? 34.19200  46.46600  51.63900  1.000 100.42967 ?  127 TRP C CE2 1 
ATOM   4414 C  CE3 . TRP C 1 127 ? 34.81100  44.36000  50.62900  1.000 97.08852  ?  127 TRP C CE3 1 
ATOM   4415 C  CZ2 . TRP C 1 127 ? 34.51300  47.17000  50.47900  1.000 102.42130 ?  127 TRP C CZ2 1 
ATOM   4416 C  CZ3 . TRP C 1 127 ? 35.12700  45.06000  49.47700  1.000 95.80043  ?  127 TRP C CZ3 1 
ATOM   4417 C  CH2 . TRP C 1 127 ? 34.97800  46.45100  49.41200  1.000 94.57695  ?  127 TRP C CH2 1 
ATOM   4418 N  N   . PHE C 1 128 ? 35.54100  43.65900  56.26100  1.000 96.36061  ?  128 PHE C N   1 
ATOM   4419 C  CA  . PHE C 1 128 ? 36.11900  44.56400  57.24700  1.000 87.02941  ?  128 PHE C CA  1 
ATOM   4420 C  C   . PHE C 1 128 ? 37.46900  44.07700  57.75400  1.000 85.22591  ?  128 PHE C C   1 
ATOM   4421 O  O   . PHE C 1 128 ? 38.32200  44.89900  58.11000  1.000 88.04495  ?  128 PHE C O   1 
ATOM   4422 C  CB  . PHE C 1 128 ? 35.15400  44.75400  58.41500  1.000 84.79501  ?  128 PHE C CB  1 
ATOM   4423 C  CG  . PHE C 1 128 ? 33.82000  45.30900  58.00900  1.000 86.11580  ?  128 PHE C CG  1 
ATOM   4424 C  CD1 . PHE C 1 128 ? 33.71900  46.55500  57.41300  1.000 84.53495  ?  128 PHE C CD1 1 
ATOM   4425 C  CD2 . PHE C 1 128 ? 32.66200  44.58700  58.23800  1.000 93.20638  ?  128 PHE C CD2 1 
ATOM   4426 C  CE1 . PHE C 1 128 ? 32.48600  47.06200  57.03900  1.000 82.65323  ?  128 PHE C CE1 1 
ATOM   4427 C  CE2 . PHE C 1 128 ? 31.42900  45.08800  57.87000  1.000 93.21222  ?  128 PHE C CE2 1 
ATOM   4428 C  CZ  . PHE C 1 128 ? 31.34000  46.32700  57.27100  1.000 87.04178  ?  128 PHE C CZ  1 
ATOM   4429 N  N   . LYS C 1 129 ? 37.67600  42.75700  57.80800  1.000 88.77475  ?  129 LYS C N   1 
ATOM   4430 C  CA  . LYS C 1 129 ? 38.96700  42.22300  58.23400  1.000 90.86215  ?  129 LYS C CA  1 
ATOM   4431 C  C   . LYS C 1 129 ? 40.10000  42.78300  57.38300  1.000 92.09345  ?  129 LYS C C   1 
ATOM   4432 O  O   . LYS C 1 129 ? 41.16800  43.12500  57.90400  1.000 96.11854  ?  129 LYS C O   1 
ATOM   4433 C  CB  . LYS C 1 129 ? 38.94600  40.69400  58.17600  1.000 87.78355  ?  129 LYS C CB  1 
ATOM   4434 C  CG  . LYS C 1 129 ? 40.29300  40.03900  58.43900  1.000 82.69354  ?  129 LYS C CG  1 
ATOM   4435 C  CD  . LYS C 1 129 ? 40.19100  38.52300  58.38400  1.000 86.59098  ?  129 LYS C CD  1 
ATOM   4436 C  CE  . LYS C 1 129 ? 41.51700  37.86700  58.73700  1.000 89.99807  ?  129 LYS C CE  1 
ATOM   4437 N  NZ  . LYS C 1 129 ? 41.40500  36.38400  58.81900  1.000 96.07638  ?  129 LYS C NZ  1 
ATOM   4438 N  N   . HIS C 1 130 ? 39.88700  42.88200  56.07000  1.000 93.29438  ?  130 HIS C N   1 
ATOM   4439 C  CA  . HIS C 1 130 ? 40.85500  43.46900  55.15300  1.000 94.72257  ?  130 HIS C CA  1 
ATOM   4440 C  C   . HIS C 1 130 ? 40.41700  44.85300  54.67800  1.000 101.81121 ?  130 HIS C C   1 
ATOM   4441 O  O   . HIS C 1 130 ? 40.73500  45.25800  53.55700  1.000 105.44906 ?  130 HIS C O   1 
ATOM   4442 C  CB  . HIS C 1 130 ? 41.08200  42.54800  53.95500  1.000 93.20918  ?  130 HIS C CB  1 
ATOM   4443 C  CG  . HIS C 1 130 ? 41.48400  41.15500  54.32500  1.000 87.31625  ?  130 HIS C CG  1 
ATOM   4444 N  ND1 . HIS C 1 130 ? 42.77300  40.82200  54.68300  1.000 81.49879  ?  130 HIS C ND1 1 
ATOM   4445 C  CD2 . HIS C 1 130 ? 40.76800  40.00700  54.39000  1.000 84.56037  ?  130 HIS C CD2 1 
ATOM   4446 C  CE1 . HIS C 1 130 ? 42.83400  39.53000  54.95100  1.000 83.10181  ?  130 HIS C CE1 1 
ATOM   4447 N  NE2 . HIS C 1 130 ? 41.63000  39.01200  54.78100  1.000 84.25513  ?  130 HIS C NE2 1 
ATOM   4448 N  N   . SER C 1 131 ? 39.67900  45.58500  55.52200  1.000 100.29607 ?  131 SER C N   1 
ATOM   4449 C  CA  . SER C 1 131 ? 39.24400  46.93400  55.16300  1.000 103.24882 ?  131 SER C CA  1 
ATOM   4450 C  C   . SER C 1 131 ? 40.42200  47.84600  54.84500  1.000 107.26050 ?  131 SER C C   1 
ATOM   4451 O  O   . SER C 1 131 ? 40.29700  48.75500  54.01600  1.000 107.56131 ?  131 SER C O   1 
ATOM   4452 C  CB  . SER C 1 131 ? 38.39600  47.53600  56.28300  1.000 101.67233 ?  131 SER C CB  1 
ATOM   4453 O  OG  . SER C 1 131 ? 38.18300  48.92200  56.07000  1.000 102.91722 ?  131 SER C OG  1 
ATOM   4454 N  N   . SER C 1 132 ? 41.56500  47.62900  55.49900  1.000 103.73090 ?  132 SER C N   1 
ATOM   4455 C  CA  . SER C 1 132 ? 42.75000  48.43200  55.21600  1.000 105.48232 ?  132 SER C CA  1 
ATOM   4456 C  C   . SER C 1 132 ? 43.24000  48.19100  53.79300  1.000 112.37863 ?  132 SER C C   1 
ATOM   4457 O  O   . SER C 1 132 ? 43.47700  49.14200  53.03800  1.000 117.24683 ?  132 SER C O   1 
ATOM   4458 C  CB  . SER C 1 132 ? 43.84900  48.12100  56.23100  1.000 111.98578 ?  132 SER C CB  1 
ATOM   4459 O  OG  . SER C 1 132 ? 45.06900  48.74500  55.87100  1.000 111.84431 ?  132 SER C OG  1 
ATOM   4460 N  N   . LEU C 1 133 ? 43.41600  46.92000  53.42200  1.000 113.55484 ?  133 LEU C N   1 
ATOM   4461 C  CA  . LEU C 1 133 ? 43.87100  46.56200  52.08000  1.000 111.06047 ?  133 LEU C CA  1 
ATOM   4462 C  C   . LEU C 1 133 ? 43.00900  47.21100  51.00300  1.000 110.52473 ?  133 LEU C C   1 
ATOM   4463 O  O   . LEU C 1 133 ? 43.52200  47.86900  50.09100  1.000 111.08788 ?  133 LEU C O   1 
ATOM   4464 C  CB  . LEU C 1 133 ? 43.87300  45.03800  51.92400  1.000 103.28376 ?  133 LEU C CB  1 
ATOM   4465 C  CG  . LEU C 1 133 ? 44.17700  44.43700  50.54800  1.000 108.23564 ?  133 LEU C CG  1 
ATOM   4466 C  CD1 . LEU C 1 133 ? 44.99200  43.16600  50.68100  1.000 114.08416 ?  133 LEU C CD1 1 
ATOM   4467 C  CD2 . LEU C 1 133 ? 42.88500  44.13400  49.80300  1.000 103.49271 ?  133 LEU C CD2 1 
ATOM   4468 N  N   . LEU C 1 134 ? 41.69000  47.01800  51.08800  1.000 109.92588 ?  134 LEU C N   1 
ATOM   4469 C  CA  . LEU C 1 134 ? 40.78200  47.54200  50.07100  1.000 110.41826 ?  134 LEU C CA  1 
ATOM   4470 C  C   . LEU C 1 134 ? 40.87400  49.05900  49.94400  1.000 114.33120 ?  134 LEU C C   1 
ATOM   4471 O  O   . LEU C 1 134 ? 40.61100  49.60700  48.86700  1.000 119.57567 ?  134 LEU C O   1 
ATOM   4472 C  CB  . LEU C 1 134 ? 39.35100  47.12400  50.40200  1.000 109.45315 ?  134 LEU C CB  1 
ATOM   4473 C  CG  . LEU C 1 134 ? 39.15100  45.61800  50.56400  1.000 107.76692 ?  134 LEU C CG  1 
ATOM   4474 C  CD1 . LEU C 1 134 ? 37.97200  45.34300  51.47500  1.000 100.84256 ?  134 LEU C CD1 1 
ATOM   4475 C  CD2 . LEU C 1 134 ? 38.94700  44.95900  49.20900  1.000 95.58669  ?  134 LEU C CD2 1 
ATOM   4476 N  N   . GLY C 1 135 ? 41.23500  49.75100  51.02600  1.000 112.80899 ?  135 GLY C N   1 
ATOM   4477 C  CA  . GLY C 1 135 ? 41.38300  51.19700  50.95400  1.000 112.85105 ?  135 GLY C CA  1 
ATOM   4478 C  C   . GLY C 1 135 ? 42.51300  51.63000  50.03900  1.000 116.40062 ?  135 GLY C C   1 
ATOM   4479 O  O   . GLY C 1 135 ? 42.40700  52.64400  49.34300  1.000 118.15945 ?  135 GLY C O   1 
ATOM   4480 N  N   . GLU C 1 136 ? 43.60700  50.86700  50.02300  1.000 117.52958 ?  136 GLU C N   1 
ATOM   4481 C  CA  . GLU C 1 136 ? 44.78100  51.21200  49.23000  1.000 119.21242 ?  136 GLU C CA  1 
ATOM   4482 C  C   . GLU C 1 136 ? 44.54800  51.04400  47.73200  1.000 116.46643 ?  136 GLU C C   1 
ATOM   4483 O  O   . GLU C 1 136 ? 45.33900  51.55800  46.93100  1.000 117.54081 ?  136 GLU C O   1 
ATOM   4484 C  CB  . GLU C 1 136 ? 45.96000  50.34400  49.69200  1.000 120.42494 ?  136 GLU C CB  1 
ATOM   4485 C  CG  . GLU C 1 136 ? 47.28900  50.58100  48.98500  1.000 125.05355 ?  136 GLU C CG  1 
ATOM   4486 C  CD  . GLU C 1 136 ? 48.34200  49.55400  49.36100  1.000 131.22234 ?  136 GLU C CD  1 
ATOM   4487 O  OE1 . GLU C 1 136 ? 48.08200  48.73600  50.26900  1.000 129.66930 ?  136 GLU C OE1 1 
ATOM   4488 O  OE2 . GLU C 1 136 ? 49.42700  49.55900  48.74100  1.000 130.69991 -1 136 GLU C OE2 1 
ATOM   4489 N  N   . MET C 1 137 ? 43.47400  50.37200  47.33400  1.000 114.87946 ?  137 MET C N   1 
ATOM   4490 C  CA  . MET C 1 137 ? 43.21600  50.09400  45.92700  1.000 116.95610 ?  137 MET C CA  1 
ATOM   4491 C  C   . MET C 1 137 ? 42.13000  51.00600  45.35400  1.000 118.43469 ?  137 MET C C   1 
ATOM   4492 O  O   . MET C 1 137 ? 41.25400  51.47100  46.08500  1.000 114.93292 ?  137 MET C O   1 
ATOM   4493 C  CB  . MET C 1 137 ? 42.78900  48.62900  45.78000  1.000 112.56636 ?  137 MET C CB  1 
ATOM   4494 C  CG  . MET C 1 137 ? 43.86500  47.62800  46.21800  1.000 110.95942 ?  137 MET C CG  1 
ATOM   4495 S  SD  . MET C 1 137 ? 43.32200  45.90700  46.21500  1.000 110.80680 ?  137 MET C SD  1 
ATOM   4496 C  CE  . MET C 1 137 ? 41.58400  46.13400  46.57400  1.000 102.40208 ?  137 MET C CE  1 
ATOM   4497 N  N   . PRO C 1 138 ? 42.17400  51.28600  44.05300  1.000 115.22254 ?  138 PRO C N   1 
ATOM   4498 C  CA  . PRO C 1 138 ? 41.06000  51.98200  43.40600  1.000 108.50404 ?  138 PRO C CA  1 
ATOM   4499 C  C   . PRO C 1 138 ? 39.77400  51.17300  43.41800  1.000 105.83067 ?  138 PRO C C   1 
ATOM   4500 O  O   . PRO C 1 138 ? 39.77800  49.94200  43.34500  1.000 103.83282 ?  138 PRO C O   1 
ATOM   4501 C  CB  . PRO C 1 138 ? 41.56700  52.20000  41.97600  1.000 110.83722 ?  138 PRO C CB  1 
ATOM   4502 C  CG  . PRO C 1 138 ? 43.02100  52.34700  42.13400  1.000 115.59282 ?  138 PRO C CG  1 
ATOM   4503 C  CD  . PRO C 1 138 ? 43.40600  51.41500  43.25600  1.000 114.87163 ?  138 PRO C CD  1 
ATOM   4504 N  N   . GLN C 1 139 ? 38.65900  51.90700  43.51400  1.000 105.36586 ?  139 GLN C N   1 
ATOM   4505 C  CA  . GLN C 1 139 ? 37.34300  51.30400  43.71700  1.000 107.31300 ?  139 GLN C CA  1 
ATOM   4506 C  C   . GLN C 1 139 ? 37.10300  50.12700  42.77200  1.000 108.79386 ?  139 GLN C C   1 
ATOM   4507 O  O   . GLN C 1 139 ? 36.59600  49.08100  43.19400  1.000 111.10940 ?  139 GLN C O   1 
ATOM   4508 C  CB  . GLN C 1 139 ? 36.27100  52.38100  43.53900  1.000 103.54007 ?  139 GLN C CB  1 
ATOM   4509 C  CG  . GLN C 1 139 ? 34.87000  51.99200  44.00500  1.000 103.46663 ?  139 GLN C CG  1 
ATOM   4510 C  CD  . GLN C 1 139 ? 34.14700  51.11400  43.00600  1.000 110.80478 ?  139 GLN C CD  1 
ATOM   4511 O  OE1 . GLN C 1 139 ? 33.67300  50.02900  43.34500  1.000 112.98342 ?  139 GLN C OE1 1 
ATOM   4512 N  NE2 . GLN C 1 139 ? 34.08000  51.56700  41.76000  1.000 113.08269 ?  139 GLN C NE2 1 
ATOM   4513 N  N   . GLU C 1 140 ? 37.44500  50.29300  41.49100  1.000 112.62672 ?  140 GLU C N   1 
ATOM   4514 C  CA  . GLU C 1 140 ? 37.25200  49.23300  40.50400  1.000 115.38927 ?  140 GLU C CA  1 
ATOM   4515 C  C   . GLU C 1 140 ? 37.99300  47.96800  40.88900  1.000 113.02711 ?  140 GLU C C   1 
ATOM   4516 O  O   . GLU C 1 140 ? 37.55000  46.85800  40.59200  1.000 113.32975 ?  140 GLU C O   1 
ATOM   4517 C  CB  . GLU C 1 140 ? 37.73600  49.70600  39.13100  1.000 110.19575 ?  140 GLU C CB  1 
ATOM   4518 C  CG  . GLU C 1 140 ? 39.01300  50.50400  39.27500  1.000 110.90878 ?  140 GLU C CG  1 
ATOM   4519 C  CD  . GLU C 1 140 ? 38.76500  51.99200  39.44700  1.000 112.01744 ?  140 GLU C CD  1 
ATOM   4520 O  OE1 . GLU C 1 140 ? 37.67300  52.36500  39.92100  1.000 113.22597 ?  140 GLU C OE1 1 
ATOM   4521 O  OE2 . GLU C 1 140 ? 39.68500  52.78200  39.15000  1.000 108.68859 -1 140 GLU C OE2 1 
ATOM   4522 N  N   . ARG C 1 141 ? 39.14000  48.12800  41.55100  1.000 112.73660 ?  141 ARG C N   1 
ATOM   4523 C  CA  . ARG C 1 141 ? 40.06300  47.05200  41.85300  1.000 112.82278 ?  141 ARG C CA  1 
ATOM   4524 C  C   . ARG C 1 141 ? 39.75100  46.38500  43.18800  1.000 109.29211 ?  141 ARG C C   1 
ATOM   4525 O  O   . ARG C 1 141 ? 40.59800  45.64800  43.71300  1.000 108.41953 ?  141 ARG C O   1 
ATOM   4526 C  CB  . ARG C 1 141 ? 41.49300  47.61600  41.88500  1.000 112.70141 ?  141 ARG C CB  1 
ATOM   4527 C  CG  . ARG C 1 141 ? 41.97700  48.13800  40.53000  1.000 120.87497 ?  141 ARG C CG  1 
ATOM   4528 C  CD  . ARG C 1 141 ? 43.36200  48.78400  40.60000  1.000 128.95336 ?  141 ARG C CD  1 
ATOM   4529 N  NE  . ARG C 1 141 ? 44.43800  47.87000  40.97100  1.000 138.33856 ?  141 ARG C NE  1 
ATOM   4530 C  CZ  . ARG C 1 141 ? 45.69300  48.24100  41.20100  1.000 139.14992 ?  141 ARG C CZ  1 
ATOM   4531 N  NH1 . ARG C 1 141 ? 46.05900  49.51200  41.16000  1.000 134.91070 ?  141 ARG C NH1 1 
ATOM   4532 N  NH2 . ARG C 1 141 ? 46.61600  47.30700  41.42800  1.000 143.29373 ?  141 ARG C NH2 1 
ATOM   4533 N  N   . ARG C 1 142 ? 38.56600  46.62400  43.74200  1.000 108.54231 ?  142 ARG C N   1 
ATOM   4534 C  CA  . ARG C 1 142 ? 38.17500  46.09400  45.04100  1.000 103.94817 ?  142 ARG C CA  1 
ATOM   4535 C  C   . ARG C 1 142 ? 37.24800  44.87300  44.98400  1.000 101.59224 ?  142 ARG C C   1 
ATOM   4536 O  O   . ARG C 1 142 ? 37.48400  43.88400  45.69100  1.000 98.21328  ?  142 ARG C O   1 
ATOM   4537 C  CB  . ARG C 1 142 ? 37.50900  47.20800  45.84200  1.000 96.53993  ?  142 ARG C CB  1 
ATOM   4538 C  CG  . ARG C 1 142 ? 38.50900  48.11900  46.51000  1.000 99.49413  ?  142 ARG C CG  1 
ATOM   4539 C  CD  . ARG C 1 142 ? 37.84500  49.37800  47.00700  1.000 104.03700 ?  142 ARG C CD  1 
ATOM   4540 N  NE  . ARG C 1 142 ? 38.82500  50.37000  47.42900  1.000 109.56878 ?  142 ARG C NE  1 
ATOM   4541 C  CZ  . ARG C 1 142 ? 38.55200  51.65500  47.59900  1.000 109.48555 ?  142 ARG C CZ  1 
ATOM   4542 N  NH1 . ARG C 1 142 ? 37.33400  52.13300  47.40100  1.000 103.43012 ?  142 ARG C NH1 1 
ATOM   4543 N  NH2 . ARG C 1 142 ? 39.52500  52.48200  47.96700  1.000 111.53393 ?  142 ARG C NH2 1 
ATOM   4544 N  N   . LEU C 1 143 ? 36.19700  44.93200  44.16400  1.000 102.58935 ?  143 LEU C N   1 
ATOM   4545 C  CA  . LEU C 1 143 ? 35.20700  43.85200  44.14400  1.000 91.97931  ?  143 LEU C CA  1 
ATOM   4546 C  C   . LEU C 1 143 ? 35.82000  42.53100  43.70000  1.000 87.44463  ?  143 LEU C C   1 
ATOM   4547 O  O   . LEU C 1 143 ? 35.41100  41.46400  44.17100  1.000 86.19022  ?  143 LEU C O   1 
ATOM   4548 C  CB  . LEU C 1 143 ? 34.03600  44.22500  43.23400  1.000 87.70877  ?  143 LEU C CB  1 
ATOM   4549 C  CG  . LEU C 1 143 ? 33.13000  45.36300  43.71100  1.000 97.10929  ?  143 LEU C CG  1 
ATOM   4550 C  CD1 . LEU C 1 143 ? 31.92800  45.51500  42.79000  1.000 92.36354  ?  143 LEU C CD1 1 
ATOM   4551 C  CD2 . LEU C 1 143 ? 32.68200  45.14300  45.14800  1.000 94.12979  ?  143 LEU C CD2 1 
ATOM   4552 N  N   . ASP C 1 144 ? 36.79100  42.58400  42.78800  1.000 91.28055  ?  144 ASP C N   1 
ATOM   4553 C  CA  . ASP C 1 144 ? 37.50500  41.37500  42.39600  1.000 92.56299  ?  144 ASP C CA  1 
ATOM   4554 C  C   . ASP C 1 144 ? 38.43300  40.89900  43.50800  1.000 88.66395  ?  144 ASP C C   1 
ATOM   4555 O  O   . ASP C 1 144 ? 38.61500  39.69100  43.70000  1.000 82.41755  ?  144 ASP C O   1 
ATOM   4556 C  CB  . ASP C 1 144 ? 38.28600  41.63100  41.10900  1.000 92.39089  ?  144 ASP C CB  1 
ATOM   4557 C  CG  . ASP C 1 144 ? 37.39300  41.65400  39.88500  1.000 91.70888  ?  144 ASP C CG  1 
ATOM   4558 O  OD1 . ASP C 1 144 ? 36.15400  41.66700  40.05400  1.000 85.36498  ?  144 ASP C OD1 1 
ATOM   4559 O  OD2 . ASP C 1 144 ? 37.92900  41.67000  38.75700  1.000 101.24978 -1 144 ASP C OD2 1 
ATOM   4560 N  N   . THR C 1 145 ? 39.03200  41.83700  44.24600  1.000 93.86737  ?  145 THR C N   1 
ATOM   4561 C  CA  . THR C 1 145 ? 39.97200  41.46700  45.29900  1.000 96.24929  ?  145 THR C CA  1 
ATOM   4562 C  C   . THR C 1 145 ? 39.26800  40.78600  46.46700  1.000 92.35537  ?  145 THR C C   1 
ATOM   4563 O  O   . THR C 1 145 ? 39.75700  39.77400  46.98300  1.000 90.35708  ?  145 THR C O   1 
ATOM   4564 C  CB  . THR C 1 145 ? 40.73500  42.69900  45.78000  1.000 99.89830  ?  145 THR C CB  1 
ATOM   4565 O  OG1 . THR C 1 145 ? 41.29800  43.38200  44.65300  1.000 106.64643 ?  145 THR C OG1 1 
ATOM   4566 C  CG2 . THR C 1 145 ? 41.85500  42.28900  46.72300  1.000 94.97349  ?  145 THR C CG2 1 
ATOM   4567 N  N   . LEU C 1 146 ? 38.13400  41.33600  46.91500  1.000 88.75879  ?  146 LEU C N   1 
ATOM   4568 C  CA  . LEU C 1 146 ? 37.35100  40.66600  47.95000  1.000 87.85550  ?  146 LEU C CA  1 
ATOM   4569 C  C   . LEU C 1 146 ? 37.00100  39.24400  47.53600  1.000 87.46826  ?  146 LEU C C   1 
ATOM   4570 O  O   . LEU C 1 146 ? 37.04600  38.31700  48.35500  1.000 87.76717  ?  146 LEU C O   1 
ATOM   4571 C  CB  . LEU C 1 146 ? 36.07200  41.44800  48.25100  1.000 85.42291  ?  146 LEU C CB  1 
ATOM   4572 C  CG  . LEU C 1 146 ? 35.15400  40.71000  49.23100  1.000 82.49791  ?  146 LEU C CG  1 
ATOM   4573 C  CD1 . LEU C 1 146 ? 35.85000  40.52000  50.57300  1.000 88.40195  ?  146 LEU C CD1 1 
ATOM   4574 C  CD2 . LEU C 1 146 ? 33.81400  41.40000  49.40300  1.000 85.62478  ?  146 LEU C CD2 1 
ATOM   4575 N  N   . CYS C 1 147 ? 36.65000  39.05600  46.26100  1.000 88.79839  ?  147 CYS C N   1 
ATOM   4576 C  CA  . CYS C 1 147 ? 36.37100  37.72000  45.74800  1.000 83.74842  ?  147 CYS C CA  1 
ATOM   4577 C  C   . CYS C 1 147 ? 37.57500  36.80100  45.92300  1.000 86.24855  ?  147 CYS C C   1 
ATOM   4578 O  O   . CYS C 1 147 ? 37.42000  35.62000  46.25200  1.000 82.99438  ?  147 CYS C O   1 
ATOM   4579 C  CB  . CYS C 1 147 ? 35.95900  37.80500  44.27800  1.000 84.56189  ?  147 CYS C CB  1 
ATOM   4580 S  SG  . CYS C 1 147 ? 35.69100  36.21300  43.47300  1.000 101.91684 ?  147 CYS C SG  1 
ATOM   4581 N  N   . GLU C 1 148 ? 38.78400  37.32300  45.70100  1.000 90.55487  ?  148 GLU C N   1 
ATOM   4582 C  CA  . GLU C 1 148 ? 39.98200  36.52500  45.94600  1.000 91.51037  ?  148 GLU C CA  1 
ATOM   4583 C  C   . GLU C 1 148 ? 40.26100  36.38000  47.43700  1.000 91.72982  ?  148 GLU C C   1 
ATOM   4584 O  O   . GLU C 1 148 ? 40.72300  35.32300  47.88500  1.000 94.87100  ?  148 GLU C O   1 
ATOM   4585 C  CB  . GLU C 1 148 ? 41.18900  37.14100  45.24000  1.000 94.91804  ?  148 GLU C CB  1 
ATOM   4586 C  CG  . GLU C 1 148 ? 41.05300  37.25500  43.73300  1.000 97.88067  ?  148 GLU C CG  1 
ATOM   4587 C  CD  . GLU C 1 148 ? 42.26700  37.90200  43.09600  1.000 102.19323 ?  148 GLU C CD  1 
ATOM   4588 O  OE1 . GLU C 1 148 ? 43.14900  38.37500  43.84400  1.000 104.05948 ?  148 GLU C OE1 1 
ATOM   4589 O  OE2 . GLU C 1 148 ? 42.34400  37.93500  41.85000  1.000 101.66533 -1 148 GLU C OE2 1 
ATOM   4590 N  N   . LEU C 1 149 ? 40.00500  37.43200  48.22000  1.000 91.65455  ?  149 LEU C N   1 
ATOM   4591 C  CA  . LEU C 1 149 ? 40.18900  37.33900  49.66600  1.000 86.76360  ?  149 LEU C CA  1 
ATOM   4592 C  C   . LEU C 1 149 ? 39.26500  36.29100  50.26900  1.000 83.79420  ?  149 LEU C C   1 
ATOM   4593 O  O   . LEU C 1 149 ? 39.68400  35.48100  51.10300  1.000 82.78685  ?  149 LEU C O   1 
ATOM   4594 C  CB  . LEU C 1 149 ? 39.94100  38.69800  50.32300  1.000 78.78768  ?  149 LEU C CB  1 
ATOM   4595 C  CG  . LEU C 1 149 ? 40.99200  39.79200  50.14100  1.000 79.04721  ?  149 LEU C CG  1 
ATOM   4596 C  CD1 . LEU C 1 149 ? 40.43300  41.13800  50.58100  1.000 75.41466  ?  149 LEU C CD1 1 
ATOM   4597 C  CD2 . LEU C 1 149 ? 42.26900  39.45500  50.89400  1.000 79.10487  ?  149 LEU C CD2 1 
ATOM   4598 N  N   . ASN C 1 150 ? 37.99800  36.29200  49.84800  1.000 85.92709  ?  150 ASN C N   1 
ATOM   4599 C  CA  . ASN C 1 150 ? 37.03100  35.33900  50.38000  1.000 81.19243  ?  150 ASN C CA  1 
ATOM   4600 C  C   . ASN C 1 150 ? 37.48800  33.90500  50.14500  1.000 78.79004  ?  150 ASN C C   1 
ATOM   4601 O  O   . ASN C 1 150 ? 37.37800  33.05800  51.03700  1.000 82.89755  ?  150 ASN C O   1 
ATOM   4602 C  CB  . ASN C 1 150 ? 35.66200  35.58700  49.74400  1.000 78.02069  ?  150 ASN C CB  1 
ATOM   4603 C  CG  . ASN C 1 150 ? 34.58400  34.67900  50.30100  1.000 77.04328  ?  150 ASN C CG  1 
ATOM   4604 O  OD1 . ASN C 1 150 ? 34.65000  34.25000  51.45200  1.000 84.49968  ?  150 ASN C OD1 1 
ATOM   4605 N  ND2 . ASN C 1 150 ? 33.57700  34.38700  49.48500  1.000 69.91487  ?  150 ASN C ND2 1 
ATOM   4606 N  N   . VAL C 1 151 ? 38.02900  33.62100  48.95800  1.000 80.33250  ?  151 VAL C N   1 
ATOM   4607 C  CA  . VAL C 1 151 ? 38.46000  32.26300  48.63800  1.000 83.26618  ?  151 VAL C CA  1 
ATOM   4608 C  C   . VAL C 1 151 ? 39.64300  31.85200  49.50900  1.000 78.25445  ?  151 VAL C C   1 
ATOM   4609 O  O   . VAL C 1 151 ? 39.71600  30.71100  49.98100  1.000 79.01749  ?  151 VAL C O   1 
ATOM   4610 C  CB  . VAL C 1 151 ? 38.79300  32.15600  47.13900  1.000 81.33786  ?  151 VAL C CB  1 
ATOM   4611 C  CG1 . VAL C 1 151 ? 39.37300  30.78700  46.81200  1.000 75.70450  ?  151 VAL C CG1 1 
ATOM   4612 C  CG2 . VAL C 1 151 ? 37.55700  32.43500  46.30100  1.000 64.91136  ?  151 VAL C CG2 1 
ATOM   4613 N  N   . MET C 1 152 ? 40.58300  32.77300  49.74300  1.000 78.17599  ?  152 MET C N   1 
ATOM   4614 C  CA  . MET C 1 152 ? 41.72600  32.46200  50.59800  1.000 87.66288  ?  152 MET C CA  1 
ATOM   4615 C  C   . MET C 1 152 ? 41.29100  32.20200  52.03300  1.000 84.58207  ?  152 MET C C   1 
ATOM   4616 O  O   . MET C 1 152 ? 41.83700  31.31700  52.70300  1.000 77.31060  ?  152 MET C O   1 
ATOM   4617 C  CB  . MET C 1 152 ? 42.74900  33.59200  50.54000  1.000 91.49676  ?  152 MET C CB  1 
ATOM   4618 C  CG  . MET C 1 152 ? 43.27000  33.85600  49.14600  1.000 90.00608  ?  152 MET C CG  1 
ATOM   4619 S  SD  . MET C 1 152 ? 44.47900  35.18500  49.07300  1.000 95.99903  ?  152 MET C SD  1 
ATOM   4620 C  CE  . MET C 1 152 ? 44.73500  35.26800  47.30400  1.000 106.49333 ?  152 MET C CE  1 
ATOM   4621 N  N   . GLU C 1 153 ? 40.33100  32.98000  52.53200  1.000 81.21859  ?  153 GLU C N   1 
ATOM   4622 C  CA  . GLU C 1 153 ? 39.84300  32.75800  53.88700  1.000 79.76650  ?  153 GLU C CA  1 
ATOM   4623 C  C   . GLU C 1 153 ? 39.15200  31.40500  54.00300  1.000 79.51993  ?  153 GLU C C   1 
ATOM   4624 O  O   . GLU C 1 153 ? 39.30200  30.71000  55.01500  1.000 84.38195  ?  153 GLU C O   1 
ATOM   4625 C  CB  . GLU C 1 153 ? 38.91000  33.89500  54.30100  1.000 79.88294  ?  153 GLU C CB  1 
ATOM   4626 C  CG  . GLU C 1 153 ? 39.59800  35.25300  54.35500  1.000 83.58948  ?  153 GLU C CG  1 
ATOM   4627 C  CD  . GLU C 1 153 ? 40.54000  35.39200  55.53800  1.000 93.27996  ?  153 GLU C CD  1 
ATOM   4628 O  OE1 . GLU C 1 153 ? 40.48100  34.54700  56.45600  1.000 93.22421  ?  153 GLU C OE1 1 
ATOM   4629 O  OE2 . GLU C 1 153 ? 41.34500  36.34900  55.54700  1.000 94.50804  -1 153 GLU C OE2 1 
ATOM   4630 N  N   . GLN C 1 154 ? 38.38900  31.01100  52.97700  1.000 75.83110  ?  154 GLN C N   1 
ATOM   4631 C  CA  . GLN C 1 154 ? 37.72200  29.71300  53.02300  1.000 69.22781  ?  154 GLN C CA  1 
ATOM   4632 C  C   . GLN C 1 154 ? 38.73600  28.57700  52.98200  1.000 74.25721  ?  154 GLN C C   1 
ATOM   4633 O  O   . GLN C 1 154 ? 38.55000  27.54700  53.64000  1.000 73.49784  ?  154 GLN C O   1 
ATOM   4634 C  CB  . GLN C 1 154 ? 36.72600  29.57600  51.87000  1.000 77.10421  ?  154 GLN C CB  1 
ATOM   4635 C  CG  . GLN C 1 154 ? 35.69500  30.68600  51.79000  1.000 78.09496  ?  154 GLN C CG  1 
ATOM   4636 C  CD  . GLN C 1 154 ? 35.16200  31.09000  53.14700  1.000 77.23444  ?  154 GLN C CD  1 
ATOM   4637 O  OE1 . GLN C 1 154 ? 34.63400  30.26700  53.89300  1.000 77.34731  ?  154 GLN C OE1 1 
ATOM   4638 N  NE2 . GLN C 1 154 ? 35.30500  32.36900  53.47700  1.000 74.49586  ?  154 GLN C NE2 1 
ATOM   4639 N  N   . VAL C 1 155 ? 39.81100  28.74500  52.20700  1.000 78.88650  ?  155 VAL C N   1 
ATOM   4640 C  CA  . VAL C 1 155 ? 40.91200  27.78700  52.24400  1.000 82.50460  ?  155 VAL C CA  1 
ATOM   4641 C  C   . VAL C 1 155 ? 41.51600  27.74000  53.64000  1.000 78.55616  ?  155 VAL C C   1 
ATOM   4642 O  O   . VAL C 1 155 ? 41.82900  26.66500  54.16600  1.000 75.13316  ?  155 VAL C O   1 
ATOM   4643 C  CB  . VAL C 1 155 ? 41.96700  28.14500  51.18000  1.000 78.04225  ?  155 VAL C CB  1 
ATOM   4644 C  CG1 . VAL C 1 155 ? 43.22000  27.30200  51.36200  1.000 82.16582  ?  155 VAL C CG1 1 
ATOM   4645 C  CG2 . VAL C 1 155 ? 41.39600  27.95400  49.78400  1.000 81.07790  ?  155 VAL C CG2 1 
ATOM   4646 N  N   . TYR C 1 156 ? 41.67900  28.91000  54.26100  1.000 82.09664  ?  156 TYR C N   1 
ATOM   4647 C  CA  . TYR C 1 156 ? 42.16200  28.98400  55.63600  1.000 81.98063  ?  156 TYR C CA  1 
ATOM   4648 C  C   . TYR C 1 156 ? 41.21900  28.25900  56.58800  1.000 78.51343  ?  156 TYR C C   1 
ATOM   4649 O  O   . TYR C 1 156 ? 41.64800  27.41700  57.38700  1.000 78.37929  ?  156 TYR C O   1 
ATOM   4650 C  CB  . TYR C 1 156 ? 42.31500  30.45200  56.03400  1.000 84.63352  ?  156 TYR C CB  1 
ATOM   4651 C  CG  . TYR C 1 156 ? 43.28500  30.71800  57.15800  1.000 89.57438  ?  156 TYR C CG  1 
ATOM   4652 C  CD1 . TYR C 1 156 ? 44.55200  30.15000  57.15800  1.000 94.47713  ?  156 TYR C CD1 1 
ATOM   4653 C  CD2 . TYR C 1 156 ? 42.94600  31.56900  58.20000  1.000 89.03803  ?  156 TYR C CD2 1 
ATOM   4654 C  CE1 . TYR C 1 156 ? 45.44500  30.40300  58.17600  1.000 97.32215  ?  156 TYR C CE1 1 
ATOM   4655 C  CE2 . TYR C 1 156 ? 43.83300  31.83000  59.22300  1.000 99.22359  ?  156 TYR C CE2 1 
ATOM   4656 C  CZ  . TYR C 1 156 ? 45.08200  31.24600  59.20700  1.000 101.60159 ?  156 TYR C CZ  1 
ATOM   4657 O  OH  . TYR C 1 156 ? 45.96900  31.50300  60.22700  1.000 102.90280 ?  156 TYR C OH  1 
ATOM   4658 N  N   . ASN C 1 157 ? 39.92100  28.56500  56.50300  1.000 72.07924  ?  157 ASN C N   1 
ATOM   4659 C  CA  . ASN C 1 157 ? 38.93300  27.90900  57.35500  1.000 65.88215  ?  157 ASN C CA  1 
ATOM   4660 C  C   . ASN C 1 157 ? 38.96100  26.39700  57.17200  1.000 68.62421  ?  157 ASN C C   1 
ATOM   4661 O  O   . ASN C 1 157 ? 38.90100  25.64500  58.15100  1.000 83.44444  ?  157 ASN C O   1 
ATOM   4662 C  CB  . ASN C 1 157 ? 37.53700  28.45100  57.05100  1.000 63.93624  ?  157 ASN C CB  1 
ATOM   4663 C  CG  . ASN C 1 157 ? 37.43300  29.94600  57.26300  1.000 66.71515  ?  157 ASN C CG  1 
ATOM   4664 O  OD1 . ASN C 1 157 ? 38.35000  30.57500  57.79000  1.000 68.67561  ?  157 ASN C OD1 1 
ATOM   4665 N  ND2 . ASN C 1 157 ? 36.31000  30.52600  56.85400  1.000 68.48191  ?  157 ASN C ND2 1 
ATOM   4666 N  N   . LEU C 1 158 ? 39.02800  25.93600  55.92300  1.000 78.77929  ?  158 LEU C N   1 
ATOM   4667 C  CA  . LEU C 1 158 ? 39.03300  24.50200  55.65800  1.000 83.60829  ?  158 LEU C CA  1 
ATOM   4668 C  C   . LEU C 1 158 ? 40.19500  23.81400  56.36400  1.000 78.28125  ?  158 LEU C C   1 
ATOM   4669 O  O   . LEU C 1 158 ? 40.02000  22.75600  56.97800  1.000 74.49881  ?  158 LEU C O   1 
ATOM   4670 C  CB  . LEU C 1 158 ? 39.09400  24.26000  54.14900  1.000 72.24563  ?  158 LEU C CB  1 
ATOM   4671 C  CG  . LEU C 1 158 ? 39.16500  22.80600  53.68600  1.000 76.50091  ?  158 LEU C CG  1 
ATOM   4672 C  CD1 . LEU C 1 158 ? 38.07100  21.98300  54.34300  1.000 79.92502  ?  158 LEU C CD1 1 
ATOM   4673 C  CD2 . LEU C 1 158 ? 39.06300  22.72800  52.17300  1.000 86.29876  ?  158 LEU C CD2 1 
ATOM   4674 N  N   . GLY C 1 159 ? 41.38800  24.40800  56.29800  1.000 79.91905  ?  159 GLY C N   1 
ATOM   4675 C  CA  . GLY C 1 159 ? 42.54900  23.82500  56.94300  1.000 79.28482  ?  159 GLY C CA  1 
ATOM   4676 C  C   . GLY C 1 159 ? 42.50400  23.84700  58.45700  1.000 89.71638  ?  159 GLY C C   1 
ATOM   4677 O  O   . GLY C 1 159 ? 43.21400  23.06400  59.09600  1.000 90.58679  ?  159 GLY C O   1 
ATOM   4678 N  N   . HIS C 1 160 ? 41.69700  24.73000  59.04700  1.000 89.82377  ?  160 HIS C N   1 
ATOM   4679 C  CA  . HIS C 1 160 ? 41.61400  24.82000  60.49900  1.000 78.90509  ?  160 HIS C CA  1 
ATOM   4680 C  C   . HIS C 1 160 ? 40.59600  23.86500  61.10600  1.000 79.35950  ?  160 HIS C C   1 
ATOM   4681 O  O   . HIS C 1 160 ? 40.67600  23.58400  62.30700  1.000 90.65647  ?  160 HIS C O   1 
ATOM   4682 C  CB  . HIS C 1 160 ? 41.28100  26.25300  60.92400  1.000 77.16301  ?  160 HIS C CB  1 
ATOM   4683 C  CG  . HIS C 1 160 ? 42.44800  27.18900  60.84900  1.000 85.57581  ?  160 HIS C CG  1 
ATOM   4684 N  ND1 . HIS C 1 160 ? 43.75200  26.76400  60.97900  1.000 89.26749  ?  160 HIS C ND1 1 
ATOM   4685 C  CD2 . HIS C 1 160 ? 42.50500  28.52800  60.66100  1.000 82.19332  ?  160 HIS C CD2 1 
ATOM   4686 C  CE1 . HIS C 1 160 ? 44.56400  27.80100  60.87200  1.000 86.44337  ?  160 HIS C CE1 1 
ATOM   4687 N  NE2 . HIS C 1 160 ? 43.83200  28.88300  60.67900  1.000 84.94502  ?  160 HIS C NE2 1 
ATOM   4688 N  N   . SER C 1 161 ? 39.64200  23.37300  60.31800  1.000 73.67170  ?  161 SER C N   1 
ATOM   4689 C  CA  . SER C 1 161 ? 38.65700  22.43300  60.82900  1.000 74.34413  ?  161 SER C CA  1 
ATOM   4690 C  C   . SER C 1 161 ? 39.34200  21.16300  61.32600  1.000 77.32294  ?  161 SER C C   1 
ATOM   4691 O  O   . SER C 1 161 ? 40.46000  20.83000  60.92700  1.000 78.26885  ?  161 SER C O   1 
ATOM   4692 C  CB  . SER C 1 161 ? 37.63500  22.08300  59.74800  1.000 76.79725  ?  161 SER C CB  1 
ATOM   4693 O  OG  . SER C 1 161 ? 38.15100  21.10100  58.86600  1.000 77.78387  ?  161 SER C OG  1 
ATOM   4694 N  N   . THR C 1 162 ? 38.64500  20.43800  62.20200  1.000 75.99608  ?  162 THR C N   1 
ATOM   4695 C  CA  . THR C 1 162 ? 39.22000  19.22000  62.76200  1.000 80.05116  ?  162 THR C CA  1 
ATOM   4696 C  C   . THR C 1 162 ? 39.41300  18.14200  61.70400  1.000 76.76546  ?  162 THR C C   1 
ATOM   4697 O  O   . THR C 1 162 ? 40.34300  17.33500  61.81200  1.000 77.57670  ?  162 THR C O   1 
ATOM   4698 C  CB  . THR C 1 162 ? 38.33700  18.68600  63.88800  1.000 73.97096  ?  162 THR C CB  1 
ATOM   4699 O  OG1 . THR C 1 162 ? 37.03700  18.37400  63.37000  1.000 73.12201  ?  162 THR C OG1 1 
ATOM   4700 C  CG2 . THR C 1 162 ? 38.19600  19.72200  64.97700  1.000 69.29089  ?  162 THR C CG2 1 
ATOM   4701 N  N   . ILE C 1 163 ? 38.55400  18.11400  60.68300  1.000 77.04962  ?  163 ILE C N   1 
ATOM   4702 C  CA  . ILE C 1 163 ? 38.65300  17.09500  59.64000  1.000 80.76274  ?  163 ILE C CA  1 
ATOM   4703 C  C   . ILE C 1 163 ? 40.00000  17.18000  58.93200  1.000 80.62828  ?  163 ILE C C   1 
ATOM   4704 O  O   . ILE C 1 163 ? 40.70500  16.17500  58.77600  1.000 81.01524  ?  163 ILE C O   1 
ATOM   4705 C  CB  . ILE C 1 163 ? 37.48400  17.23400  58.65000  1.000 74.69509  ?  163 ILE C CB  1 
ATOM   4706 C  CG1 . ILE C 1 163 ? 36.15500  17.17200  59.40500  1.000 70.74800  ?  163 ILE C CG1 1 
ATOM   4707 C  CG2 . ILE C 1 163 ? 37.55400  16.13800  57.60400  1.000 81.53962  ?  163 ILE C CG2 1 
ATOM   4708 C  CD1 . ILE C 1 163 ? 34.99000  17.73900  58.63500  1.000 75.78416  ?  163 ILE C CD1 1 
ATOM   4709 N  N   . MET C 1 164 ? 40.37200  18.37900  58.47800  1.000 77.06811  ?  164 MET C N   1 
ATOM   4710 C  CA  . MET C 1 164 ? 41.66700  18.54100  57.82400  1.000 80.98928  ?  164 MET C CA  1 
ATOM   4711 C  C   . MET C 1 164 ? 42.81200  18.38000  58.81500  1.000 86.13729  ?  164 MET C C   1 
ATOM   4712 O  O   . MET C 1 164 ? 43.81900  17.73200  58.50500  1.000 82.52971  ?  164 MET C O   1 
ATOM   4713 C  CB  . MET C 1 164 ? 41.74500  19.89500  57.12200  1.000 82.00067  ?  164 MET C CB  1 
ATOM   4714 C  CG  . MET C 1 164 ? 40.90100  19.96400  55.86600  1.000 78.32345  ?  164 MET C CG  1 
ATOM   4715 S  SD  . MET C 1 164 ? 41.28600  18.59200  54.76400  1.000 80.54407  ?  164 MET C SD  1 
ATOM   4716 C  CE  . MET C 1 164 ? 43.04600  18.82700  54.53400  1.000 77.62921  ?  164 MET C CE  1 
ATOM   4717 N  N   . GLN C 1 165 ? 42.68500  18.98000  60.00100  1.000 89.46854  ?  165 GLN C N   1 
ATOM   4718 C  CA  . GLN C 1 165 ? 43.73900  18.87100  61.00300  1.000 85.46807  ?  165 GLN C CA  1 
ATOM   4719 C  C   . GLN C 1 165 ? 43.98500  17.42000  61.39600  1.000 85.34112  ?  165 GLN C C   1 
ATOM   4720 O  O   . GLN C 1 165 ? 45.13700  17.00100  61.54800  1.000 90.74442  ?  165 GLN C O   1 
ATOM   4721 C  CB  . GLN C 1 165 ? 43.38000  19.70800  62.23100  1.000 83.01831  ?  165 GLN C CB  1 
ATOM   4722 C  CG  . GLN C 1 165 ? 43.30700  21.20400  61.96500  1.000 86.62715  ?  165 GLN C CG  1 
ATOM   4723 C  CD  . GLN C 1 165 ? 44.66200  21.87100  62.00200  1.000 94.22236  ?  165 GLN C CD  1 
ATOM   4724 O  OE1 . GLN C 1 165 ? 45.42200  21.69200  62.95000  1.000 102.03784 ?  165 GLN C OE1 1 
ATOM   4725 N  NE2 . GLN C 1 165 ? 44.97400  22.64400  60.96900  1.000 95.04775  ?  165 GLN C NE2 1 
ATOM   4726 N  N   . SER C 1 166 ? 42.91600  16.63100  61.54600  1.000 79.24038  ?  166 SER C N   1 
ATOM   4727 C  CA  . SER C 1 166 ? 43.08500  15.22200  61.89200  1.000 86.13770  ?  166 SER C CA  1 
ATOM   4728 C  C   . SER C 1 166 ? 43.76400  14.45200  60.76700  1.000 91.50049  ?  166 SER C C   1 
ATOM   4729 O  O   . SER C 1 166 ? 44.65600  13.63400  61.02000  1.000 93.31700  ?  166 SER C O   1 
ATOM   4730 C  CB  . SER C 1 166 ? 41.73600  14.58800  62.23400  1.000 83.79593  ?  166 SER C CB  1 
ATOM   4731 O  OG  . SER C 1 166 ? 41.11500  15.25800  63.31800  1.000 85.70315  ?  166 SER C OG  1 
ATOM   4732 N  N   . ALA C 1 167 ? 43.35200  14.69400  59.52000  1.000 90.53508  ?  167 ALA C N   1 
ATOM   4733 C  CA  . ALA C 1 167 ? 43.94300  13.97900  58.39300  1.000 92.43099  ?  167 ALA C CA  1 
ATOM   4734 C  C   . ALA C 1 167 ? 45.42200  14.31700  58.24900  1.000 92.84835  ?  167 ALA C C   1 
ATOM   4735 O  O   . ALA C 1 167 ? 46.26200  13.42600  58.08000  1.000 91.74681  ?  167 ALA C O   1 
ATOM   4736 C  CB  . ALA C 1 167 ? 43.18400  14.30700  57.10700  1.000 96.91901  ?  167 ALA C CB  1 
ATOM   4737 N  N   . TRP C 1 168 ? 45.75700  15.60800  58.31000  1.000 92.00955  ?  168 TRP C N   1 
ATOM   4738 C  CA  . TRP C 1 168 ? 47.15700  16.01300  58.24600  1.000 93.39957  ?  168 TRP C CA  1 
ATOM   4739 C  C   . TRP C 1 168 ? 47.94400  15.47900  59.43500  1.000 97.25221  ?  168 TRP C C   1 
ATOM   4740 O  O   . TRP C 1 168 ? 49.12400  15.13700  59.29800  1.000 97.50612  ?  168 TRP C O   1 
ATOM   4741 C  CB  . TRP C 1 168 ? 47.25900  17.53600  58.17400  1.000 90.11272  ?  168 TRP C CB  1 
ATOM   4742 C  CG  . TRP C 1 168 ? 46.94700  18.08600  56.81800  1.000 90.77172  ?  168 TRP C CG  1 
ATOM   4743 C  CD1 . TRP C 1 168 ? 46.96700  17.40600  55.63400  1.000 92.29950  ?  168 TRP C CD1 1 
ATOM   4744 C  CD2 . TRP C 1 168 ? 46.57100  19.43200  56.50200  1.000 91.99905  ?  168 TRP C CD2 1 
ATOM   4745 N  NE1 . TRP C 1 168 ? 46.62700  18.24500  54.60100  1.000 86.79570  ?  168 TRP C NE1 1 
ATOM   4746 C  CE2 . TRP C 1 168 ? 46.38000  19.49500  55.10700  1.000 87.07068  ?  168 TRP C CE2 1 
ATOM   4747 C  CE3 . TRP C 1 168 ? 46.37800  20.59000  57.26100  1.000 92.82331  ?  168 TRP C CE3 1 
ATOM   4748 C  CZ2 . TRP C 1 168 ? 46.00500  20.66800  54.45700  1.000 87.39638  ?  168 TRP C CZ2 1 
ATOM   4749 C  CZ3 . TRP C 1 168 ? 46.00600  21.75500  56.61400  1.000 89.39523  ?  168 TRP C CZ3 1 
ATOM   4750 C  CH2 . TRP C 1 168 ? 45.82300  21.78500  55.22600  1.000 92.43035  ?  168 TRP C CH2 1 
ATOM   4751 N  N   . LYS C 1 169 ? 47.30400  15.39000  60.60300  1.000 94.83124  ?  169 LYS C N   1 
ATOM   4752 C  CA  . LYS C 1 169 ? 47.98400  14.90600  61.79900  1.000 95.29523  ?  169 LYS C CA  1 
ATOM   4753 C  C   . LYS C 1 169 ? 48.27200  13.41300  61.72400  1.000 94.37196  ?  169 LYS C C   1 
ATOM   4754 O  O   . LYS C 1 169 ? 49.27900  12.95100  62.27100  1.000 95.22614  ?  169 LYS C O   1 
ATOM   4755 C  CB  . LYS C 1 169 ? 47.12500  15.21700  63.02400  1.000 94.99347  ?  169 LYS C CB  1 
ATOM   4756 C  CG  . LYS C 1 169 ? 47.71700  14.87300  64.37000  1.000 98.46732  ?  169 LYS C CG  1 
ATOM   4757 C  CD  . LYS C 1 169 ? 46.63100  15.00900  65.42600  1.000 108.46786 ?  169 LYS C CD  1 
ATOM   4758 C  CE  . LYS C 1 169 ? 45.48900  14.03800  65.14600  1.000 106.36301 ?  169 LYS C CE  1 
ATOM   4759 N  NZ  . LYS C 1 169 ? 44.67700  13.72800  66.35500  1.000 113.99179 ?  169 LYS C NZ  1 
ATOM   4760 N  N   . ARG C 1 170 ? 47.41400  12.64900  61.05200  1.000 93.28958  ?  170 ARG C N   1 
ATOM   4761 C  CA  . ARG C 1 170 ? 47.62800  11.22400  60.84100  1.000 93.93870  ?  170 ARG C CA  1 
ATOM   4762 C  C   . ARG C 1 170 ? 48.42100  10.91700  59.57400  1.000 98.46974  ?  170 ARG C C   1 
ATOM   4763 O  O   . ARG C 1 170 ? 48.58200  9.74200   59.23000  1.000 97.77785  ?  170 ARG C O   1 
ATOM   4764 C  CB  . ARG C 1 170 ? 46.28100  10.49500  60.83500  1.000 94.14515  ?  170 ARG C CB  1 
ATOM   4765 C  CG  . ARG C 1 170 ? 45.37600  10.81500  59.65800  1.000 99.62099  ?  170 ARG C CG  1 
ATOM   4766 C  CD  . ARG C 1 170 ? 44.02500  10.13900  59.83000  1.000 99.56043  ?  170 ARG C CD  1 
ATOM   4767 N  NE  . ARG C 1 170 ? 43.12400  10.40100  58.71400  1.000 96.17345  ?  170 ARG C NE  1 
ATOM   4768 C  CZ  . ARG C 1 170 ? 42.04000  11.16000  58.79500  1.000 95.39086  ?  170 ARG C CZ  1 
ATOM   4769 N  NH1 . ARG C 1 170 ? 41.69900  11.76100  59.92400  1.000 93.60948  ?  170 ARG C NH1 1 
ATOM   4770 N  NH2 . ARG C 1 170 ? 41.28200  11.32500  57.71500  1.000 97.21166  ?  170 ARG C NH2 1 
ATOM   4771 N  N   . GLY C 1 171 ? 48.92100  11.93800  58.87800  1.000 93.50069  ?  171 GLY C N   1 
ATOM   4772 C  CA  . GLY C 1 171 ? 49.79900  11.73600  57.74500  1.000 90.17256  ?  171 GLY C CA  1 
ATOM   4773 C  C   . GLY C 1 171 ? 49.12000  11.57100  56.40300  1.000 99.60938  ?  171 GLY C C   1 
ATOM   4774 O  O   . GLY C 1 171 ? 49.81900  11.38900  55.39600  1.000 91.33845  ?  171 GLY C O   1 
ATOM   4775 N  N   . GLN C 1 172 ? 47.79000  11.60900  56.35100  1.000 99.40770  ?  172 GLN C N   1 
ATOM   4776 C  CA  . GLN C 1 172 ? 47.09100  11.48200  55.08000  1.000 83.50940  ?  172 GLN C CA  1 
ATOM   4777 C  C   . GLN C 1 172 ? 47.47400  12.62400  54.14600  1.000 87.01648  ?  172 GLN C C   1 
ATOM   4778 O  O   . GLN C 1 172 ? 47.67600  13.76100  54.58100  1.000 83.43647  ?  172 GLN C O   1 
ATOM   4779 C  CB  . GLN C 1 172 ? 45.57800  11.46500  55.31400  1.000 89.87434  ?  172 GLN C CB  1 
ATOM   4780 C  CG  . GLN C 1 172 ? 44.74300  11.20200  54.06700  1.000 89.92349  ?  172 GLN C CG  1 
ATOM   4781 C  CD  . GLN C 1 172 ? 43.32400  10.76800  54.39900  1.000 94.74573  ?  172 GLN C CD  1 
ATOM   4782 O  OE1 . GLN C 1 172 ? 43.07600  10.16100  55.44100  1.000 100.05594 ?  172 GLN C OE1 1 
ATOM   4783 N  NE2 . GLN C 1 172 ? 42.38500  11.08200  53.51300  1.000 92.75470  ?  172 GLN C NE2 1 
ATOM   4784 N  N   . LYS C 1 173 ? 47.58200  12.31300  52.85500  1.000 95.54638  ?  173 LYS C N   1 
ATOM   4785 C  CA  . LYS C 1 173 ? 47.93500  13.30200  51.83500  1.000 80.14052  ?  173 LYS C CA  1 
ATOM   4786 C  C   . LYS C 1 173 ? 46.66900  13.96300  51.30500  1.000 78.65556  ?  173 LYS C C   1 
ATOM   4787 O  O   . LYS C 1 173 ? 45.91000  13.36500  50.54000  1.000 84.20059  ?  173 LYS C O   1 
ATOM   4788 C  CB  . LYS C 1 173 ? 48.74100  12.67900  50.69800  1.000 81.50493  ?  173 LYS C CB  1 
ATOM   4789 C  CG  . LYS C 1 173 ? 50.19500  12.33100  51.01400  1.000 83.24410  ?  173 LYS C CG  1 
ATOM   4790 C  CD  . LYS C 1 173 ? 50.39300  11.16200  51.95200  1.000 90.67096  ?  173 LYS C CD  1 
ATOM   4791 C  CE  . LYS C 1 173 ? 51.88000  10.98900  52.23500  1.000 94.39053  ?  173 LYS C CE  1 
ATOM   4792 N  NZ  . LYS C 1 173 ? 52.16600  9.92300   53.23000  1.000 102.41204 ?  173 LYS C NZ  1 
ATOM   4793 N  N   . VAL C 1 174 ? 46.43100  15.19900  51.73700  1.000 73.99644  ?  174 VAL C N   1 
ATOM   4794 C  CA  . VAL C 1 174 ? 45.36400  16.04100  51.21300  1.000 78.31581  ?  174 VAL C CA  1 
ATOM   4795 C  C   . VAL C 1 174 ? 45.95900  17.41600  50.95500  1.000 84.41193  ?  174 VAL C C   1 
ATOM   4796 O  O   . VAL C 1 174 ? 46.76100  17.91200  51.75300  1.000 86.18314  ?  174 VAL C O   1 
ATOM   4797 C  CB  . VAL C 1 174 ? 44.15900  16.14100  52.17400  1.000 84.78293  ?  174 VAL C CB  1 
ATOM   4798 C  CG1 . VAL C 1 174 ? 42.98200  16.80800  51.47600  1.000 78.72444  ?  174 VAL C CG1 1 
ATOM   4799 C  CG2 . VAL C 1 174 ? 43.75900  14.76800  52.69100  1.000 87.68096  ?  174 VAL C CG2 1 
ATOM   4800 N  N   . THR C 1 175 ? 45.57200  18.03300  49.84100  1.000 91.05824  ?  175 THR C N   1 
ATOM   4801 C  CA  . THR C 1 175 ? 46.11200  19.32800  49.45000  1.000 88.11065  ?  175 THR C CA  1 
ATOM   4802 C  C   . THR C 1 175 ? 44.95700  20.26000  49.12100  1.000 85.22315  ?  175 THR C C   1 
ATOM   4803 O  O   . THR C 1 175 ? 44.07700  19.90700  48.32900  1.000 86.18617  ?  175 THR C O   1 
ATOM   4804 C  CB  . THR C 1 175 ? 47.04800  19.19700  48.24300  1.000 89.07694  ?  175 THR C CB  1 
ATOM   4805 O  OG1 . THR C 1 175 ? 48.03600  18.19400  48.50900  1.000 90.80751  ?  175 THR C OG1 1 
ATOM   4806 C  CG2 . THR C 1 175 ? 47.75800  20.51000  47.99100  1.000 88.74736  ?  175 THR C CG2 1 
ATOM   4807 N  N   . ILE C 1 176 ? 44.96900  21.45200  49.71200  1.000 81.83644  ?  176 ILE C N   1 
ATOM   4808 C  CA  . ILE C 1 176 ? 43.90600  22.43300  49.52500  1.000 81.48588  ?  176 ILE C CA  1 
ATOM   4809 C  C   . ILE C 1 176 ? 44.41900  23.52900  48.60300  1.000 85.81979  ?  176 ILE C C   1 
ATOM   4810 O  O   . ILE C 1 176 ? 45.53900  24.02500  48.77900  1.000 87.10582  ?  176 ILE C O   1 
ATOM   4811 C  CB  . ILE C 1 176 ? 43.44000  23.01500  50.87100  1.000 78.98720  ?  176 ILE C CB  1 
ATOM   4812 C  CG1 . ILE C 1 176 ? 43.07900  21.89300  51.84500  1.000 82.17471  ?  176 ILE C CG1 1 
ATOM   4813 C  CG2 . ILE C 1 176 ? 42.24500  23.92800  50.66800  1.000 74.25621  ?  176 ILE C CG2 1 
ATOM   4814 C  CD1 . ILE C 1 176 ? 42.74700  22.38400  53.24000  1.000 82.39316  ?  176 ILE C CD1 1 
ATOM   4815 N  N   . HIS C 1 177 ? 43.59500  23.91600  47.62800  1.000 84.35504  ?  177 HIS C N   1 
ATOM   4816 C  CA  . HIS C 1 177 ? 43.96300  24.90500  46.62400  1.000 76.69821  ?  177 HIS C CA  1 
ATOM   4817 C  C   . HIS C 1 177 ? 42.87900  25.96900  46.53000  1.000 76.34362  ?  177 HIS C C   1 
ATOM   4818 O  O   . HIS C 1 177 ? 41.68900  25.66800  46.65500  1.000 74.94321  ?  177 HIS C O   1 
ATOM   4819 C  CB  . HIS C 1 177 ? 44.16000  24.26400  45.24700  1.000 72.84752  ?  177 HIS C CB  1 
ATOM   4820 C  CG  . HIS C 1 177 ? 45.02600  23.04500  45.25900  1.000 75.18321  ?  177 HIS C CG  1 
ATOM   4821 N  ND1 . HIS C 1 177 ? 46.37800  23.08700  44.99800  1.000 77.73229  ?  177 HIS C ND1 1 
ATOM   4822 C  CD2 . HIS C 1 177 ? 44.72500  21.74200  45.47700  1.000 79.75471  ?  177 HIS C CD2 1 
ATOM   4823 C  CE1 . HIS C 1 177 ? 46.87600  21.86500  45.06400  1.000 81.63015  ?  177 HIS C CE1 1 
ATOM   4824 N  NE2 . HIS C 1 177 ? 45.89300  21.03100  45.35300  1.000 81.78204  ?  177 HIS C NE2 1 
ATOM   4825 N  N   . GLY C 1 178 ? 43.29800  27.21200  46.30400  1.000 74.68840  ?  178 GLY C N   1 
ATOM   4826 C  CA  . GLY C 1 178 ? 42.36700  28.30600  46.10100  1.000 75.13104  ?  178 GLY C CA  1 
ATOM   4827 C  C   . GLY C 1 178 ? 42.48300  28.94000  44.72900  1.000 89.23211  ?  178 GLY C C   1 
ATOM   4828 O  O   . GLY C 1 178 ? 43.53100  29.49700  44.38800  1.000 92.82556  ?  178 GLY C O   1 
ATOM   4829 N  N   . TRP C 1 179 ? 41.41900  28.86500  43.93200  1.000 87.85377  ?  179 TRP C N   1 
ATOM   4830 C  CA  . TRP C 1 179 ? 41.41100  29.35100  42.55900  1.000 81.07897  ?  179 TRP C CA  1 
ATOM   4831 C  C   . TRP C 1 179 ? 40.30500  30.37900  42.35900  1.000 82.90437  ?  179 TRP C C   1 
ATOM   4832 O  O   . TRP C 1 179 ? 39.42900  30.56600  43.20700  1.000 81.19029  ?  179 TRP C O   1 
ATOM   4833 C  CB  . TRP C 1 179 ? 41.21100  28.20400  41.55900  1.000 74.50055  ?  179 TRP C CB  1 
ATOM   4834 C  CG  . TRP C 1 179 ? 42.31900  27.20800  41.49500  1.000 75.98562  ?  179 TRP C CG  1 
ATOM   4835 C  CD1 . TRP C 1 179 ? 43.55300  27.30400  42.07100  1.000 79.51601  ?  179 TRP C CD1 1 
ATOM   4836 C  CD2 . TRP C 1 179 ? 42.28600  25.94500  40.82300  1.000 72.55721  ?  179 TRP C CD2 1 
ATOM   4837 N  NE1 . TRP C 1 179 ? 44.29400  26.18000  41.79000  1.000 81.08114  ?  179 TRP C NE1 1 
ATOM   4838 C  CE2 . TRP C 1 179 ? 43.53700  25.33000  41.02600  1.000 76.81165  ?  179 TRP C CE2 1 
ATOM   4839 C  CE3 . TRP C 1 179 ? 41.31900  25.27600  40.06700  1.000 71.77503  ?  179 TRP C CE3 1 
ATOM   4840 C  CZ2 . TRP C 1 179 ? 43.84500  24.07700  40.50100  1.000 80.95541  ?  179 TRP C CZ2 1 
ATOM   4841 C  CZ3 . TRP C 1 179 ? 41.62600  24.03300  39.54600  1.000 75.83529  ?  179 TRP C CZ3 1 
ATOM   4842 C  CH2 . TRP C 1 179 ? 42.87900  23.44600  39.76400  1.000 79.98710  ?  179 TRP C CH2 1 
ATOM   4843 N  N   . ALA C 1 180 ? 40.36400  31.04800  41.20900  1.000 86.93403  ?  180 ALA C N   1 
ATOM   4844 C  CA  . ALA C 1 180 ? 39.29800  31.93200  40.75900  1.000 87.72293  ?  180 ALA C CA  1 
ATOM   4845 C  C   . ALA C 1 180 ? 39.34600  32.02000  39.24000  1.000 93.27270  ?  180 ALA C C   1 
ATOM   4846 O  O   . ALA C 1 180 ? 40.40900  31.87500  38.63100  1.000 97.04040  ?  180 ALA C O   1 
ATOM   4847 C  CB  . ALA C 1 180 ? 39.41300  33.32800  41.38200  1.000 84.15693  ?  180 ALA C CB  1 
ATOM   4848 N  N   . TYR C 1 181 ? 38.18400  32.26300  38.63400  1.000 94.10268  ?  181 TYR C N   1 
ATOM   4849 C  CA  . TYR C 1 181 ? 38.08400  32.43100  37.19100  1.000 92.56664  ?  181 TYR C CA  1 
ATOM   4850 C  C   . TYR C 1 181 ? 37.09200  33.54100  36.88200  1.000 93.85965  ?  181 TYR C C   1 
ATOM   4851 O  O   . TYR C 1 181 ? 36.19900  33.84300  37.67600  1.000 90.38808  ?  181 TYR C O   1 
ATOM   4852 C  CB  . TYR C 1 181 ? 37.65800  31.13300  36.48700  1.000 86.55517  ?  181 TYR C CB  1 
ATOM   4853 C  CG  . TYR C 1 181 ? 36.20800  30.74600  36.69600  1.000 85.48770  ?  181 TYR C CG  1 
ATOM   4854 C  CD1 . TYR C 1 181 ? 35.82400  29.98500  37.79100  1.000 85.69113  ?  181 TYR C CD1 1 
ATOM   4855 C  CD2 . TYR C 1 181 ? 35.22700  31.13000  35.78900  1.000 91.86981  ?  181 TYR C CD2 1 
ATOM   4856 C  CE1 . TYR C 1 181 ? 34.50200  29.62500  37.98300  1.000 88.15324  ?  181 TYR C CE1 1 
ATOM   4857 C  CE2 . TYR C 1 181 ? 33.90300  30.77700  35.97400  1.000 93.88720  ?  181 TYR C CE2 1 
ATOM   4858 C  CZ  . TYR C 1 181 ? 33.54600  30.02400  37.07300  1.000 89.94943  ?  181 TYR C CZ  1 
ATOM   4859 O  OH  . TYR C 1 181 ? 32.22900  29.66800  37.25800  1.000 86.54206  ?  181 TYR C OH  1 
ATOM   4860 N  N   . GLY C 1 182 ? 37.26000  34.15200  35.71300  1.000 94.58460  ?  182 GLY C N   1 
ATOM   4861 C  CA  . GLY C 1 182 ? 36.39600  35.22800  35.26800  1.000 95.80188  ?  182 GLY C CA  1 
ATOM   4862 C  C   . GLY C 1 182 ? 35.54100  34.78300  34.09800  1.000 99.73538  ?  182 GLY C C   1 
ATOM   4863 O  O   . GLY C 1 182 ? 35.93300  33.90600  33.32500  1.000 101.77810 ?  182 GLY C O   1 
ATOM   4864 N  N   . ILE C 1 183 ? 34.36200  35.40000  33.96700  1.000 101.98333 ?  183 ILE C N   1 
ATOM   4865 C  CA  . ILE C 1 183 ? 33.48400  35.11200  32.83500  1.000 105.25378 ?  183 ILE C CA  1 
ATOM   4866 C  C   . ILE C 1 183 ? 33.91300  35.84700  31.57900  1.000 105.80913 ?  183 ILE C C   1 
ATOM   4867 O  O   . ILE C 1 183 ? 33.24800  35.72000  30.54400  1.000 113.52611 ?  183 ILE C O   1 
ATOM   4868 C  CB  . ILE C 1 183 ? 32.00700  35.44800  33.13200  1.000 112.48138 ?  183 ILE C CB  1 
ATOM   4869 C  CG1 . ILE C 1 183 ? 31.85200  36.90300  33.57300  1.000 105.14529 ?  183 ILE C CG1 1 
ATOM   4870 C  CG2 . ILE C 1 183 ? 31.44100  34.49500  34.17600  1.000 110.02426 ?  183 ILE C CG2 1 
ATOM   4871 C  CD1 . ILE C 1 183 ? 30.41000  37.35900  33.64600  1.000 104.34284 ?  183 ILE C CD1 1 
ATOM   4872 N  N   . HIS C 1 184 ? 34.98700  36.63700  31.64600  1.000 104.90131 ?  184 HIS C N   1 
ATOM   4873 C  CA  . HIS C 1 184 ? 35.49700  37.31600  30.46100  1.000 104.89349 ?  184 HIS C CA  1 
ATOM   4874 C  C   . HIS C 1 184 ? 36.30700  36.38200  29.57100  1.000 106.65440 ?  184 HIS C C   1 
ATOM   4875 O  O   . HIS C 1 184 ? 36.32100  36.56000  28.34800  1.000 108.97631 ?  184 HIS C O   1 
ATOM   4876 C  CB  . HIS C 1 184 ? 36.36200  38.51100  30.86600  1.000 101.19763 ?  184 HIS C CB  1 
ATOM   4877 C  CG  . HIS C 1 184 ? 37.45000  38.16600  31.83400  1.000 109.58873 ?  184 HIS C CG  1 
ATOM   4878 N  ND1 . HIS C 1 184 ? 37.20600  37.85800  33.15600  1.000 110.39861 ?  184 HIS C ND1 1 
ATOM   4879 C  CD2 . HIS C 1 184 ? 38.79100  38.07200  31.66900  1.000 110.99455 ?  184 HIS C CD2 1 
ATOM   4880 C  CE1 . HIS C 1 184 ? 38.34900  37.59500  33.76300  1.000 110.94930 ?  184 HIS C CE1 1 
ATOM   4881 N  NE2 . HIS C 1 184 ? 39.32600  37.71700  32.88300  1.000 109.41269 ?  184 HIS C NE2 1 
ATOM   4882 N  N   . ASP C 1 185 ? 37.01500  35.41400  30.15700  1.000 101.56412 ?  185 ASP C N   1 
ATOM   4883 C  CA  . ASP C 1 185 ? 37.78500  34.45700  29.36900  1.000 102.09894 ?  185 ASP C CA  1 
ATOM   4884 C  C   . ASP C 1 185 ? 37.75500  33.03000  29.90100  1.000 103.82917 ?  185 ASP C C   1 
ATOM   4885 O  O   . ASP C 1 185 ? 38.19600  32.12700  29.18400  1.000 106.90717 ?  185 ASP C O   1 
ATOM   4886 C  CB  . ASP C 1 185 ? 39.24800  34.91300  29.23400  1.000 99.35557  ?  185 ASP C CB  1 
ATOM   4887 C  CG  . ASP C 1 185 ? 39.94100  35.08400  30.57200  1.000 106.09246 ?  185 ASP C CG  1 
ATOM   4888 O  OD1 . ASP C 1 185 ? 39.33000  34.78800  31.62000  1.000 109.04182 ?  185 ASP C OD1 1 
ATOM   4889 O  OD2 . ASP C 1 185 ? 41.11300  35.51700  30.57200  1.000 109.28673 -1 185 ASP C OD2 1 
ATOM   4890 N  N   . GLY C 1 186 ? 37.26500  32.78900  31.11600  1.000 98.21976  ?  186 GLY C N   1 
ATOM   4891 C  CA  . GLY C 1 186 ? 37.24500  31.44700  31.66400  1.000 91.60853  ?  186 GLY C CA  1 
ATOM   4892 C  C   . GLY C 1 186 ? 38.58800  30.89700  32.08600  1.000 90.55546  ?  186 GLY C C   1 
ATOM   4893 O  O   . GLY C 1 186 ? 38.73000  29.68000  32.22400  1.000 82.84303  ?  186 GLY C O   1 
ATOM   4894 N  N   . LEU C 1 187 ? 39.58400  31.75300  32.29300  1.000 94.76276  ?  187 LEU C N   1 
ATOM   4895 C  CA  . LEU C 1 187 ? 40.91900  31.30500  32.66800  1.000 95.60342  ?  187 LEU C CA  1 
ATOM   4896 C  C   . LEU C 1 187 ? 41.02300  31.25000  34.18900  1.000 96.16068  ?  187 LEU C C   1 
ATOM   4897 O  O   . LEU C 1 187 ? 40.80900  32.26000  34.86800  1.000 94.92337  ?  187 LEU C O   1 
ATOM   4898 C  CB  . LEU C 1 187 ? 41.98500  32.23100  32.08500  1.000 100.87237 ?  187 LEU C CB  1 
ATOM   4899 C  CG  . LEU C 1 187 ? 43.42000  31.70400  32.13600  1.000 102.24895 ?  187 LEU C CG  1 
ATOM   4900 C  CD1 . LEU C 1 187 ? 43.53300  30.42000  31.33000  1.000 95.01107  ?  187 LEU C CD1 1 
ATOM   4901 C  CD2 . LEU C 1 187 ? 44.39700  32.74900  31.62100  1.000 96.87844  ?  187 LEU C CD2 1 
ATOM   4902 N  N   . LEU C 1 188 ? 41.35200  30.07200  34.71900  1.000 97.22549  ?  188 LEU C N   1 
ATOM   4903 C  CA  . LEU C 1 188 ? 41.52700  29.91300  36.15700  1.000 91.52745  ?  188 LEU C CA  1 
ATOM   4904 C  C   . LEU C 1 188 ? 42.80100  30.60300  36.62500  1.000 92.32445  ?  188 LEU C C   1 
ATOM   4905 O  O   . LEU C 1 188 ? 43.88400  30.37200  36.08000  1.000 96.06397  ?  188 LEU C O   1 
ATOM   4906 C  CB  . LEU C 1 188 ? 41.57100  28.43100  36.53100  1.000 83.07798  ?  188 LEU C CB  1 
ATOM   4907 C  CG  . LEU C 1 188 ? 40.26800  27.63400  36.48700  1.000 81.71826  ?  188 LEU C CG  1 
ATOM   4908 C  CD1 . LEU C 1 188 ? 40.54700  26.16300  36.74200  1.000 74.20274  ?  188 LEU C CD1 1 
ATOM   4909 C  CD2 . LEU C 1 188 ? 39.27700  28.16800  37.50300  1.000 77.65092  ?  188 LEU C CD2 1 
ATOM   4910 N  N   . ARG C 1 189 ? 42.66900  31.45100  37.63900  1.000 95.50539  ?  189 ARG C N   1 
ATOM   4911 C  CA  . ARG C 1 189 ? 43.81100  32.07000  38.29600  1.000 97.59234  ?  189 ARG C CA  1 
ATOM   4912 C  C   . ARG C 1 189 ? 44.04100  31.38600  39.63600  1.000 88.80121  ?  189 ARG C C   1 
ATOM   4913 O  O   . ARG C 1 189 ? 43.12500  31.30200  40.46100  1.000 88.97773  ?  189 ARG C O   1 
ATOM   4914 C  CB  . ARG C 1 189 ? 43.58900  33.57200  38.48500  1.000 99.08857  ?  189 ARG C CB  1 
ATOM   4915 C  CG  . ARG C 1 189 ? 44.64900  34.26200  39.33200  1.000 98.88505  ?  189 ARG C CG  1 
ATOM   4916 C  CD  . ARG C 1 189 ? 44.38100  35.75700  39.45100  1.000 104.10664 ?  189 ARG C CD  1 
ATOM   4917 N  NE  . ARG C 1 189 ? 44.78500  36.47900  38.24900  1.000 108.94842 ?  189 ARG C NE  1 
ATOM   4918 C  CZ  . ARG C 1 189 ? 43.94900  36.92600  37.32100  1.000 107.69850 ?  189 ARG C CZ  1 
ATOM   4919 N  NH1 . ARG C 1 189 ? 42.64300  36.73500  37.41600  1.000 108.17591 ?  189 ARG C NH1 1 
ATOM   4920 N  NH2 . ARG C 1 189 ? 44.43600  37.57700  36.26900  1.000 106.14002 ?  189 ARG C NH2 1 
ATOM   4921 N  N   . ASP C 1 190 ? 45.26300  30.90400  39.84900  1.000 87.02586  ?  190 ASP C N   1 
ATOM   4922 C  CA  . ASP C 1 190 ? 45.62200  30.25400  41.10200  1.000 90.71098  ?  190 ASP C CA  1 
ATOM   4923 C  C   . ASP C 1 190 ? 45.98200  31.32800  42.12000  1.000 93.14812  ?  190 ASP C C   1 
ATOM   4924 O  O   . ASP C 1 190 ? 46.94100  32.08200  41.92400  1.000 93.39777  ?  190 ASP C O   1 
ATOM   4925 C  CB  . ASP C 1 190 ? 46.78800  29.28900  40.88800  1.000 88.14752  ?  190 ASP C CB  1 
ATOM   4926 C  CG  . ASP C 1 190 ? 47.00100  28.34500  42.06300  1.000 93.66685  ?  190 ASP C CG  1 
ATOM   4927 O  OD1 . ASP C 1 190 ? 46.69800  28.72600  43.21400  1.000 96.42554  ?  190 ASP C OD1 1 
ATOM   4928 O  OD2 . ASP C 1 190 ? 47.47900  27.21300  41.83200  1.000 93.07420  -1 190 ASP C OD2 1 
ATOM   4929 N  N   . LEU C 1 191 ? 45.22000  31.38900  43.21200  1.000 90.11815  ?  191 LEU C N   1 
ATOM   4930 C  CA  . LEU C 1 191 ? 45.42000  32.42000  44.22000  1.000 93.18707  ?  191 LEU C CA  1 
ATOM   4931 C  C   . LEU C 1 191 ? 46.63900  32.16600  45.09700  1.000 94.44451  ?  191 LEU C C   1 
ATOM   4932 O  O   . LEU C 1 191 ? 46.91000  32.97200  45.99500  1.000 90.19427  ?  191 LEU C O   1 
ATOM   4933 C  CB  . LEU C 1 191 ? 44.16200  32.56700  45.07900  1.000 90.88861  ?  191 LEU C CB  1 
ATOM   4934 C  CG  . LEU C 1 191 ? 42.93800  33.03600  44.28800  1.000 95.30356  ?  191 LEU C CG  1 
ATOM   4935 C  CD1 . LEU C 1 191 ? 41.71400  33.15100  45.18100  1.000 88.62839  ?  191 LEU C CD1 1 
ATOM   4936 C  CD2 . LEU C 1 191 ? 43.22900  34.35700  43.59200  1.000 97.03086  ?  191 LEU C CD2 1 
ATOM   4937 N  N   . ASP C 1 192 ? 47.35600  31.06100  44.87200  1.000 95.28641  ?  192 ASP C N   1 
ATOM   4938 C  CA  . ASP C 1 192 ? 48.68400  30.83500  45.45100  1.000 94.92853  ?  192 ASP C CA  1 
ATOM   4939 C  C   . ASP C 1 192 ? 48.63500  30.69400  46.97600  1.000 99.99865  ?  192 ASP C C   1 
ATOM   4940 O  O   . ASP C 1 192 ? 49.43800  31.28600  47.69900  1.000 100.98672 ?  192 ASP C O   1 
ATOM   4941 C  CB  . ASP C 1 192 ? 49.64300  31.95400  45.03200  1.000 92.29646  ?  192 ASP C CB  1 
ATOM   4942 C  CG  . ASP C 1 192 ? 51.08000  31.49300  44.94600  1.000 95.27746  ?  192 ASP C CG  1 
ATOM   4943 O  OD1 . ASP C 1 192 ? 51.32500  30.27600  45.07800  1.000 91.85576  ?  192 ASP C OD1 1 
ATOM   4944 O  OD2 . ASP C 1 192 ? 51.96400  32.35000  44.73600  1.000 103.60984 -1 192 ASP C OD2 1 
ATOM   4945 N  N   . VAL C 1 193 ? 47.67800  29.90200  47.46200  1.000 97.69546  ?  193 VAL C N   1 
ATOM   4946 C  CA  . VAL C 1 193 ? 47.57100  29.59500  48.88600  1.000 93.70360  ?  193 VAL C CA  1 
ATOM   4947 C  C   . VAL C 1 193 ? 47.56000  28.08400  49.09100  1.000 91.54490  ?  193 VAL C C   1 
ATOM   4948 O  O   . VAL C 1 193 ? 46.98200  27.58400  50.06300  1.000 95.87819  ?  193 VAL C O   1 
ATOM   4949 C  CB  . VAL C 1 193 ? 46.32100  30.24400  49.50900  1.000 90.21786  ?  193 VAL C CB  1 
ATOM   4950 C  CG1 . VAL C 1 193 ? 46.45100  31.76100  49.50900  1.000 92.46442  ?  193 VAL C CG1 1 
ATOM   4951 C  CG2 . VAL C 1 193 ? 45.06900  29.80900  48.76500  1.000 91.37373  ?  193 VAL C CG2 1 
ATOM   4952 N  N   . THR C 1 194 ? 48.20400  27.34900  48.18500  1.000 92.63004  ?  194 THR C N   1 
ATOM   4953 C  CA  . THR C 1 194 ? 48.15800  25.89000  48.20700  1.000 91.18844  ?  194 THR C CA  1 
ATOM   4954 C  C   . THR C 1 194 ? 48.82400  25.34100  49.46600  1.000 95.98478  ?  194 THR C C   1 
ATOM   4955 O  O   . THR C 1 194 ? 49.99600  25.62700  49.73500  1.000 100.11430 ?  194 THR C O   1 
ATOM   4956 C  CB  . THR C 1 194 ? 48.83300  25.32400  46.95900  1.000 91.43332  ?  194 THR C CB  1 
ATOM   4957 O  OG1 . THR C 1 194 ? 48.04500  25.63500  45.80300  1.000 93.07881  ?  194 THR C OG1 1 
ATOM   4958 C  CG2 . THR C 1 194 ? 48.99200  23.81600  47.07400  1.000 91.67706  ?  194 THR C CG2 1 
ATOM   4959 N  N   . ALA C 1 195 ? 48.08200  24.53600  50.22100  1.000 94.06139  ?  195 ALA C N   1 
ATOM   4960 C  CA  . ALA C 1 195 ? 48.51500  24.02300  51.51200  1.000 93.23672  ?  195 ALA C CA  1 
ATOM   4961 C  C   . ALA C 1 195 ? 48.49000  22.50100  51.51800  1.000 92.96912  ?  195 ALA C C   1 
ATOM   4962 O  O   . ALA C 1 195 ? 47.56300  21.88400  50.98300  1.000 91.83202  ?  195 ALA C O   1 
ATOM   4963 C  CB  . ALA C 1 195 ? 47.62000  24.55200  52.63100  1.000 90.61852  ?  195 ALA C CB  1 
ATOM   4964 N  N   . THR C 1 196 ? 49.50900  21.90100  52.14000  1.000 92.56028  ?  196 THR C N   1 
ATOM   4965 C  CA  . THR C 1 196 ? 49.58500  20.45400  52.28700  1.000 94.07903  ?  196 THR C CA  1 
ATOM   4966 C  C   . THR C 1 196 ? 49.64600  19.98000  53.73400  1.000 94.86741  ?  196 THR C C   1 
ATOM   4967 O  O   . THR C 1 196 ? 49.53700  18.77200  53.97100  1.000 91.52973  ?  196 THR C O   1 
ATOM   4968 C  CB  . THR C 1 196 ? 50.81500  19.89900  51.55000  1.000 90.43839  ?  196 THR C CB  1 
ATOM   4969 O  OG1 . THR C 1 196 ? 52.00800  20.42400  52.14500  1.000 88.00703  ?  196 THR C OG1 1 
ATOM   4970 C  CG2 . THR C 1 196 ? 50.78200  20.28700  50.07800  1.000 93.90152  ?  196 THR C CG2 1 
ATOM   4971 N  N   . ASN C 1 197 ? 49.81400  20.88000  54.69800  1.000 94.64467  ?  197 ASN C N   1 
ATOM   4972 C  CA  . ASN C 1 197 ? 49.84700  20.53100  56.11600  1.000 97.63641  ?  197 ASN C CA  1 
ATOM   4973 C  C   . ASN C 1 197 ? 49.53200  21.78900  56.92200  1.000 97.36370  ?  197 ASN C C   1 
ATOM   4974 O  O   . ASN C 1 197 ? 49.20700  22.83900  56.35700  1.000 94.52317  ?  197 ASN C O   1 
ATOM   4975 C  CB  . ASN C 1 197 ? 51.19600  19.90000  56.49000  1.000 99.04253  ?  197 ASN C CB  1 
ATOM   4976 C  CG  . ASN C 1 197 ? 52.38000  20.75400  56.07800  1.000 95.16596  ?  197 ASN C CG  1 
ATOM   4977 O  OD1 . ASN C 1 197 ? 52.39800  21.96300  56.30200  1.000 92.63166  ?  197 ASN C OD1 1 
ATOM   4978 N  ND2 . ASN C 1 197 ? 53.38300  20.12300  55.47800  1.000 91.59914  ?  197 ASN C ND2 1 
ATOM   4979 N  N   . ARG C 1 198 ? 49.62300  21.68300  58.25100  1.000 99.34660  ?  198 ARG C N   1 
ATOM   4980 C  CA  . ARG C 1 198 ? 49.28300  22.82000  59.10000  1.000 100.37274 ?  198 ARG C CA  1 
ATOM   4981 C  C   . ARG C 1 198 ? 50.26000  23.96900  58.90800  1.000 102.83449 ?  198 ARG C C   1 
ATOM   4982 O  O   . ARG C 1 198 ? 49.86400  25.14000  58.90900  1.000 100.17362 ?  198 ARG C O   1 
ATOM   4983 C  CB  . ARG C 1 198 ? 49.27800  22.41500  60.57200  1.000 98.24309  ?  198 ARG C CB  1 
ATOM   4984 C  CG  . ARG C 1 198 ? 48.29000  21.35200  60.98400  1.000 97.81834  ?  198 ARG C CG  1 
ATOM   4985 C  CD  . ARG C 1 198 ? 48.37900  21.19500  62.49200  1.000 109.73463 ?  198 ARG C CD  1 
ATOM   4986 N  NE  . ARG C 1 198 ? 48.09900  22.47800  63.13000  1.000 107.53422 ?  198 ARG C NE  1 
ATOM   4987 C  CZ  . ARG C 1 198 ? 48.22100  22.72700  64.42700  1.000 114.15996 ?  198 ARG C CZ  1 
ATOM   4988 N  NH1 . ARG C 1 198 ? 48.63200  21.79800  65.27400  1.000 119.77847 ?  198 ARG C NH1 1 
ATOM   4989 N  NH2 . ARG C 1 198 ? 47.93200  23.94200  64.88300  1.000 115.47633 ?  198 ARG C NH2 1 
ATOM   4990 N  N   . GLU C 1 199 ? 51.54700  23.65400  58.77000  1.000 106.66338 ?  199 GLU C N   1 
ATOM   4991 C  CA  . GLU C 1 199 ? 52.54000  24.71100  58.65400  1.000 107.93593 ?  199 GLU C CA  1 
ATOM   4992 C  C   . GLU C 1 199 ? 52.42400  25.42400  57.31500  1.000 106.27751 ?  199 GLU C C   1 
ATOM   4993 O  O   . GLU C 1 199 ? 52.41600  26.65900  57.26600  1.000 104.28226 ?  199 GLU C O   1 
ATOM   4994 C  CB  . GLU C 1 199 ? 53.94300  24.13100  58.84400  1.000 105.79892 ?  199 GLU C CB  1 
ATOM   4995 C  CG  . GLU C 1 199 ? 54.22000  23.61500  60.25100  1.000 113.35564 ?  199 GLU C CG  1 
ATOM   4996 C  CD  . GLU C 1 199 ? 55.59200  22.98100  60.39000  1.000 125.36087 ?  199 GLU C CD  1 
ATOM   4997 O  OE1 . GLU C 1 199 ? 56.26400  22.76500  59.35800  1.000 114.74659 ?  199 GLU C OE1 1 
ATOM   4998 O  OE2 . GLU C 1 199 ? 56.00100  22.69700  61.53400  1.000 131.68429 -1 199 GLU C OE2 1 
ATOM   4999 N  N   . THR C 1 200 ? 52.27100  24.66400  56.22700  1.000 102.80717 ?  200 THR C N   1 
ATOM   5000 C  CA  . THR C 1 200 ? 52.12000  25.27600  54.91000  1.000 104.00301 ?  200 THR C CA  1 
ATOM   5001 C  C   . THR C 1 200 ? 50.83800  26.09200  54.81900  1.000 102.36162 ?  200 THR C C   1 
ATOM   5002 O  O   . THR C 1 200 ? 50.80900  27.14300  54.16800  1.000 99.43311  ?  200 THR C O   1 
ATOM   5003 C  CB  . THR C 1 200 ? 52.15000  24.20700  53.81800  1.000 102.89391 ?  200 THR C CB  1 
ATOM   5004 O  OG1 . THR C 1 200 ? 51.16200  23.20800  54.10000  1.000 104.47526 ?  200 THR C OG1 1 
ATOM   5005 C  CG2 . THR C 1 200 ? 53.52500  23.56300  53.73400  1.000 100.06145 ?  200 THR C CG2 1 
ATOM   5006 N  N   . LEU C 1 201 ? 49.76300  25.62300  55.45900  1.000 100.40195 ?  201 LEU C N   1 
ATOM   5007 C  CA  . LEU C 1 201 ? 48.51200  26.37700  55.45100  1.000 99.54024  ?  201 LEU C CA  1 
ATOM   5008 C  C   . LEU C 1 201 ? 48.72100  27.79200  55.97600  1.000 102.35530 ?  201 LEU C C   1 
ATOM   5009 O  O   . LEU C 1 201 ? 48.20000  28.75700  55.40200  1.000 102.59688 ?  201 LEU C O   1 
ATOM   5010 C  CB  . LEU C 1 201 ? 47.46000  25.66600  56.29400  1.000 94.10547  ?  201 LEU C CB  1 
ATOM   5011 C  CG  . LEU C 1 201 ? 46.13000  26.40400  56.42400  1.000 89.39008  ?  201 LEU C CG  1 
ATOM   5012 C  CD1 . LEU C 1 201 ? 45.33000  26.31100  55.13500  1.000 93.35852  ?  201 LEU C CD1 1 
ATOM   5013 C  CD2 . LEU C 1 201 ? 45.34200  25.85800  57.59500  1.000 93.77112  ?  201 LEU C CD2 1 
ATOM   5014 N  N   . GLU C 1 202 ? 49.54600  27.93400  56.99200  1.000 104.96831 ?  202 GLU C N   1 
ATOM   5015 C  CA  . GLU C 1 202 ? 49.77000  29.24800  57.54900  1.000 107.67979 ?  202 GLU C CA  1 
ATOM   5016 C  C   . GLU C 1 202 ? 50.75800  30.01000  56.71100  1.000 113.54554 ?  202 GLU C C   1 
ATOM   5017 O  O   . GLU C 1 202 ? 50.52700  31.16200  56.37500  1.000 116.89442 ?  202 GLU C O   1 
ATOM   5018 C  CB  . GLU C 1 202 ? 50.30500  29.12700  58.96300  1.000 111.31607 ?  202 GLU C CB  1 
ATOM   5019 C  CG  . GLU C 1 202 ? 50.25000  30.42800  59.73100  1.000 112.91706 ?  202 GLU C CG  1 
ATOM   5020 C  CD  . GLU C 1 202 ? 48.82900  30.90000  59.91300  1.000 114.15597 ?  202 GLU C CD  1 
ATOM   5021 O  OE1 . GLU C 1 202 ? 47.97300  30.05500  60.24300  1.000 108.56522 ?  202 GLU C OE1 1 
ATOM   5022 O  OE2 . GLU C 1 202 ? 48.56800  32.10400  59.72100  1.000 114.84933 -1 202 GLU C OE2 1 
ATOM   5023 N  N   . GLN C 1 203 ? 51.85200  29.36800  56.35000  1.000 112.78374 ?  203 GLN C N   1 
ATOM   5024 C  CA  . GLN C 1 203 ? 52.91600  30.02800  55.59600  1.000 112.88954 ?  203 GLN C CA  1 
ATOM   5025 C  C   . GLN C 1 203 ? 52.38400  30.59100  54.28600  1.000 110.74412 ?  203 GLN C C   1 
ATOM   5026 O  O   . GLN C 1 203 ? 52.61000  31.76500  53.96600  1.000 112.10789 ?  203 GLN C O   1 
ATOM   5027 C  CB  . GLN C 1 203 ? 54.03200  29.02900  55.28400  1.000 113.00915 ?  203 GLN C CB  1 
ATOM   5028 C  CG  . GLN C 1 203 ? 54.72600  28.42000  56.48800  1.000 116.45881 ?  203 GLN C CG  1 
ATOM   5029 C  CD  . GLN C 1 203 ? 55.69200  27.31100  56.10100  1.000 116.14122 ?  203 GLN C CD  1 
ATOM   5030 O  OE1 . GLN C 1 203 ? 55.75100  26.90800  54.93900  1.000 113.16784 ?  203 GLN C OE1 1 
ATOM   5031 N  NE2 . GLN C 1 203 ? 56.40100  26.76500  57.08700  1.000 116.54688 ?  203 GLN C NE2 1 
ATOM   5032 N  N   . ARG C 1 204 ? 51.67700  29.76700  53.51100  1.000 108.74927 ?  204 ARG C N   1 
ATOM   5033 C  CA  . ARG C 1 204 ? 51.09800  30.22900  52.25100  1.000 110.15781 ?  204 ARG C CA  1 
ATOM   5034 C  C   . ARG C 1 204 ? 50.09400  31.35800  52.48700  1.000 109.07687 ?  204 ARG C C   1 
ATOM   5035 O  O   . ARG C 1 204 ? 50.09200  32.36200  51.76600  1.000 109.46519 ?  204 ARG C O   1 
ATOM   5036 C  CB  . ARG C 1 204 ? 50.45300  29.04900  51.53100  1.000 104.00008 ?  204 ARG C CB  1 
ATOM   5037 C  CG  . ARG C 1 204 ? 51.45600  28.01600  51.00600  1.000 103.18212 ?  204 ARG C CG  1 
ATOM   5038 C  CD  . ARG C 1 204 ? 52.62100  28.59700  50.19400  1.000 111.38440 ?  204 ARG C CD  1 
ATOM   5039 N  NE  . ARG C 1 204 ? 53.76900  28.98900  51.00600  1.000 113.61340 ?  204 ARG C NE  1 
ATOM   5040 C  CZ  . ARG C 1 204 ? 54.64500  29.92500  50.66700  1.000 115.89128 ?  204 ARG C CZ  1 
ATOM   5041 N  NH1 . ARG C 1 204 ? 54.54800  30.58500  49.52300  1.000 111.76694 ?  204 ARG C NH1 1 
ATOM   5042 N  NH2 . ARG C 1 204 ? 55.64900  30.20200  51.49400  1.000 114.48000 ?  204 ARG C NH2 1 
ATOM   5043 N  N   . TYR C 1 205 ? 49.21100  31.19200  53.47900  1.000 107.09833 ?  205 TYR C N   1 
ATOM   5044 C  CA  . TYR C 1 205 ? 48.27000  32.25400  53.82000  1.000 107.61395 ?  205 TYR C CA  1 
ATOM   5045 C  C   . TYR C 1 205 ? 49.03200  33.51000  54.21500  1.000 111.97676 ?  205 TYR C C   1 
ATOM   5046 O  O   . TYR C 1 205 ? 48.69400  34.61900  53.79200  1.000 113.18400 ?  205 TYR C O   1 
ATOM   5047 C  CB  . TYR C 1 205 ? 47.31900  31.79400  54.93000  1.000 99.73123  ?  205 TYR C CB  1 
ATOM   5048 C  CG  . TYR C 1 205 ? 46.37200  32.86900  55.43100  1.000 97.56378  ?  205 TYR C CG  1 
ATOM   5049 C  CD1 . TYR C 1 205 ? 45.30700  33.30500  54.65000  1.000 97.82387  ?  205 TYR C CD1 1 
ATOM   5050 C  CD2 . TYR C 1 205 ? 46.54300  33.44600  56.67900  1.000 100.64903 ?  205 TYR C CD2 1 
ATOM   5051 C  CE1 . TYR C 1 205 ? 44.43500  34.28200  55.10600  1.000 97.17899  ?  205 TYR C CE1 1 
ATOM   5052 C  CE2 . TYR C 1 205 ? 45.68100  34.42500  57.14200  1.000 98.88912  ?  205 TYR C CE2 1 
ATOM   5053 C  CZ  . TYR C 1 205 ? 44.62800  34.83900  56.35200  1.000 92.23623  ?  205 TYR C CZ  1 
ATOM   5054 O  OH  . TYR C 1 205 ? 43.76600  35.81400  56.80700  1.000 81.19384  ?  205 TYR C OH  1 
ATOM   5055 N  N   . ARG C 1 206 ? 50.05800  33.34300  55.05500  1.000 112.48707 ?  206 ARG C N   1 
ATOM   5056 C  CA  . ARG C 1 206 ? 50.96300  34.44200  55.37700  1.000 115.68336 ?  206 ARG C CA  1 
ATOM   5057 C  C   . ARG C 1 206 ? 51.57300  35.02800  54.11000  1.000 118.90321 ?  206 ARG C C   1 
ATOM   5058 O  O   . ARG C 1 206 ? 51.60700  36.25300  53.93000  1.000 120.11141 ?  206 ARG C O   1 
ATOM   5059 C  CB  . ARG C 1 206 ? 52.08900  33.94600  56.29000  1.000 115.88977 ?  206 ARG C CB  1 
ATOM   5060 C  CG  . ARG C 1 206 ? 51.72400  33.54600  57.69900  1.000 119.14500 ?  206 ARG C CG  1 
ATOM   5061 C  CD  . ARG C 1 206 ? 51.43600  34.78400  58.52300  1.000 123.90459 ?  206 ARG C CD  1 
ATOM   5062 N  NE  . ARG C 1 206 ? 52.62000  35.64100  58.53100  1.000 126.00775 ?  206 ARG C NE  1 
ATOM   5063 C  CZ  . ARG C 1 206 ? 52.69800  36.82400  59.12300  1.000 125.59655 ?  206 ARG C CZ  1 
ATOM   5064 N  NH1 . ARG C 1 206 ? 51.66600  37.34200  59.76700  1.000 124.27092 ?  206 ARG C NH1 1 
ATOM   5065 N  NH2 . ARG C 1 206 ? 53.84100  37.50300  59.07000  1.000 119.35807 ?  206 ARG C NH2 1 
ATOM   5066 N  N   . HIS C 1 207 ? 52.06800  34.16000  53.22300  1.000 115.44577 ?  207 HIS C N   1 
ATOM   5067 C  CA  . HIS C 1 207 ? 52.66800  34.59900  51.96500  1.000 118.07144 ?  207 HIS C CA  1 
ATOM   5068 C  C   . HIS C 1 207 ? 51.66200  35.29100  51.04800  1.000 120.35926 ?  207 HIS C C   1 
ATOM   5069 O  O   . HIS C 1 207 ? 51.98500  36.30600  50.42100  1.000 120.46891 ?  207 HIS C O   1 
ATOM   5070 C  CB  . HIS C 1 207 ? 53.28800  33.38500  51.26100  1.000 118.89179 ?  207 HIS C CB  1 
ATOM   5071 C  CG  . HIS C 1 207 ? 54.08100  33.72500  50.03800  1.000 115.62736 ?  207 HIS C CG  1 
ATOM   5072 N  ND1 . HIS C 1 207 ? 55.44700  33.90400  50.06700  1.000 114.23735 ?  207 HIS C ND1 1 
ATOM   5073 C  CD2 . HIS C 1 207 ? 53.70900  33.87700  48.74600  1.000 109.70308 ?  207 HIS C CD2 1 
ATOM   5074 C  CE1 . HIS C 1 207 ? 55.87900  34.17900  48.84900  1.000 115.84674 ?  207 HIS C CE1 1 
ATOM   5075 N  NE2 . HIS C 1 207 ? 54.84400  34.16600  48.02900  1.000 117.38568 ?  207 HIS C NE2 1 
ATOM   5076 N  N   . GLY C 1 208 ? 50.44800  34.75600  50.95200  1.000 117.74379 ?  208 GLY C N   1 
ATOM   5077 C  CA  . GLY C 1 208 ? 49.40400  35.34500  50.13500  1.000 115.21042 ?  208 GLY C CA  1 
ATOM   5078 C  C   . GLY C 1 208 ? 49.03100  36.77800  50.45700  1.000 115.55733 ?  208 GLY C C   1 
ATOM   5079 O  O   . GLY C 1 208 ? 49.04100  37.64200  49.57600  1.000 120.53955 ?  208 GLY C O   1 
ATOM   5080 N  N   . ILE C 1 209 ? 48.69800  37.02600  51.72900  1.000 115.27874 ?  209 ILE C N   1 
ATOM   5081 C  CA  . ILE C 1 209 ? 48.22900  38.34700  52.14800  1.000 117.70380 ?  209 ILE C CA  1 
ATOM   5082 C  C   . ILE C 1 209 ? 49.21600  39.42600  51.72400  1.000 123.53753 ?  209 ILE C C   1 
ATOM   5083 O  O   . ILE C 1 209 ? 48.84300  40.42400  51.09700  1.000 125.89780 ?  209 ILE C O   1 
ATOM   5084 C  CB  . ILE C 1 209 ? 47.99300  38.37400  53.66800  1.000 110.25567 ?  209 ILE C CB  1 
ATOM   5085 C  CG1 . ILE C 1 209 ? 47.00600  37.28000  54.08100  1.000 106.56141 ?  209 ILE C CG1 1 
ATOM   5086 C  CG2 . ILE C 1 209 ? 47.49500  39.74000  54.10800  1.000 109.49197 ?  209 ILE C CG2 1 
ATOM   5087 C  CD1 . ILE C 1 209 ? 45.65700  37.38500  53.41100  1.000 97.33855  ?  209 ILE C CD1 1 
ATOM   5088 N  N   . SER C 1 210 ? 50.49600  39.23100  52.05100  1.000 124.14443 ?  210 SER C N   1 
ATOM   5089 C  CA  . SER C 1 210 ? 51.49400  40.27400  51.83600  1.000 123.51762 ?  210 SER C CA  1 
ATOM   5090 C  C   . SER C 1 210 ? 51.65800  40.62500  50.36100  1.000 123.57990 ?  210 SER C C   1 
ATOM   5091 O  O   . SER C 1 210 ? 51.77700  41.80500  50.01200  1.000 124.34624 ?  210 SER C O   1 
ATOM   5092 C  CB  . SER C 1 210 ? 52.83400  39.84000  52.42900  1.000 124.25702 ?  210 SER C CB  1 
ATOM   5093 O  OG  . SER C 1 210 ? 53.35500  38.71400  51.74200  1.000 123.98444 ?  210 SER C OG  1 
ATOM   5094 N  N   . ASN C 1 211 ? 51.67100  39.62300  49.48000  1.000 122.48205 ?  211 ASN C N   1 
ATOM   5095 C  CA  . ASN C 1 211 ? 51.85600  39.91200  48.06200  1.000 121.37584 ?  211 ASN C CA  1 
ATOM   5096 C  C   . ASN C 1 211 ? 50.69100  40.72200  47.50300  1.000 123.86315 ?  211 ASN C C   1 
ATOM   5097 O  O   . ASN C 1 211 ? 50.88400  41.58300  46.63700  1.000 123.33737 ?  211 ASN C O   1 
ATOM   5098 C  CB  . ASN C 1 211 ? 52.04100  38.61500  47.27500  1.000 118.23064 ?  211 ASN C CB  1 
ATOM   5099 C  CG  . ASN C 1 211 ? 53.41600  38.00700  47.47000  1.000 118.80303 ?  211 ASN C CG  1 
ATOM   5100 O  OD1 . ASN C 1 211 ? 54.41100  38.71500  47.61500  1.000 116.99898 ?  211 ASN C OD1 1 
ATOM   5101 N  ND2 . ASN C 1 211 ? 53.47800  36.68200  47.45800  1.000 117.61689 ?  211 ASN C ND2 1 
ATOM   5102 N  N   . LEU C 1 212 ? 49.46900  40.44800  47.96900  1.000 125.46820 ?  212 LEU C N   1 
ATOM   5103 C  CA  . LEU C 1 212 ? 48.32000  41.22800  47.51700  1.000 128.11771 ?  212 LEU C CA  1 
ATOM   5104 C  C   . LEU C 1 212 ? 48.33700  42.65500  48.05600  1.000 126.10614 ?  212 LEU C C   1 
ATOM   5105 O  O   . LEU C 1 212 ? 47.83200  43.56600  47.39000  1.000 125.06597 ?  212 LEU C O   1 
ATOM   5106 C  CB  . LEU C 1 212 ? 47.01600  40.54500  47.92500  1.000 128.45729 ?  212 LEU C CB  1 
ATOM   5107 C  CG  . LEU C 1 212 ? 46.71300  39.15500  47.37200  1.000 127.56840 ?  212 LEU C CG  1 
ATOM   5108 C  CD1 . LEU C 1 212 ? 45.63400  38.52000  48.22400  1.000 124.93287 ?  212 LEU C CD1 1 
ATOM   5109 C  CD2 . LEU C 1 212 ? 46.29500  39.21500  45.90900  1.000 125.91469 ?  212 LEU C CD2 1 
ATOM   5110 N  N   . LYS C 1 213 ? 48.89400  42.86900  49.24700  1.000 124.22157 ?  213 LYS C N   1 
ATOM   5111 C  CA  . LYS C 1 213 ? 48.95400  44.20900  49.83600  1.000 124.83702 ?  213 LYS C CA  1 
ATOM   5112 C  C   . LYS C 1 213 ? 49.71100  45.18600  48.94200  1.000 124.75465 ?  213 LYS C C   1 
ATOM   5113 O  O   . LYS C 1 213 ? 49.46900  46.39200  48.98500  1.000 123.66355 ?  213 LYS C O   1 
ATOM   5114 C  CB  . LYS C 1 213 ? 49.60200  44.17800  51.22700  1.000 124.84887 ?  213 LYS C CB  1 
ATOM   5115 C  CG  . LYS C 1 213 ? 48.95200  43.22500  52.22400  1.000 128.16549 ?  213 LYS C CG  1 
ATOM   5116 C  CD  . LYS C 1 213 ? 47.67200  43.78300  52.83600  1.000 128.74640 ?  213 LYS C CD  1 
ATOM   5117 C  CE  . LYS C 1 213 ? 47.91700  45.02800  53.66800  1.000 123.79692 ?  213 LYS C CE  1 
ATOM   5118 N  NZ  . LYS C 1 213 ? 46.68100  45.43700  54.39500  1.000 122.79439 ?  213 LYS C NZ  1 
ATOM   5119 N  N   . LYS D 1 2   ? 25.25600  13.27100  94.59300  1.000 93.44948  ?  2   LYS D N   1 
ATOM   5120 C  CA  . LYS D 1 2   ? 23.91200  13.43900  94.05500  1.000 92.67062  ?  2   LYS D CA  1 
ATOM   5121 C  C   . LYS D 1 2   ? 23.73500  12.62100  92.77500  1.000 83.82699  ?  2   LYS D C   1 
ATOM   5122 O  O   . LYS D 1 2   ? 24.49000  12.78700  91.81600  1.000 82.90441  ?  2   LYS D O   1 
ATOM   5123 C  CB  . LYS D 1 2   ? 23.63800  14.92100  93.78300  1.000 91.16203  ?  2   LYS D CB  1 
ATOM   5124 C  CG  . LYS D 1 2   ? 23.55500  15.77100  95.04300  1.000 92.79561  ?  2   LYS D CG  1 
ATOM   5125 C  CD  . LYS D 1 2   ? 23.25600  17.22900  94.72500  1.000 93.96735  ?  2   LYS D CD  1 
ATOM   5126 C  CE  . LYS D 1 2   ? 23.23700  18.07800  95.99000  1.000 103.80440 ?  2   LYS D CE  1 
ATOM   5127 N  NZ  . LYS D 1 2   ? 22.92900  19.50900  95.71000  1.000 102.66567 ?  2   LYS D NZ  1 
ATOM   5128 N  N   . ASP D 1 3   ? 22.74600  11.73300  92.77100  1.000 82.41642  ?  3   ASP D N   1 
ATOM   5129 C  CA  . ASP D 1 3   ? 22.43000  10.88100  91.63000  1.000 81.73154  ?  3   ASP D CA  1 
ATOM   5130 C  C   . ASP D 1 3   ? 21.02500  11.19000  91.10700  1.000 80.66451  ?  3   ASP D C   1 
ATOM   5131 O  O   . ASP D 1 3   ? 20.33600  12.08500  91.60100  1.000 80.87440  ?  3   ASP D O   1 
ATOM   5132 C  CB  . ASP D 1 3   ? 22.59200  9.40000   91.99400  1.000 82.48040  ?  3   ASP D CB  1 
ATOM   5133 C  CG  . ASP D 1 3   ? 21.56500  8.92200   92.99900  1.000 92.98623  ?  3   ASP D CG  1 
ATOM   5134 O  OD1 . ASP D 1 3   ? 20.94500  9.76800   93.67700  1.000 93.14642  ?  3   ASP D OD1 1 
ATOM   5135 O  OD2 . ASP D 1 3   ? 21.37700  7.69300   93.10800  1.000 104.91456 -1 3   ASP D OD2 1 
ATOM   5136 N  N   . ILE D 1 4   ? 20.60900  10.42700  90.09000  1.000 80.52454  ?  4   ILE D N   1 
ATOM   5137 C  CA  . ILE D 1 4   ? 19.30900  10.64300  89.45400  1.000 79.46807  ?  4   ILE D CA  1 
ATOM   5138 C  C   . ILE D 1 4   ? 18.17200  10.46800  90.45500  1.000 80.27449  ?  4   ILE D C   1 
ATOM   5139 O  O   . ILE D 1 4   ? 17.25000  11.29000  90.52200  1.000 77.21744  ?  4   ILE D O   1 
ATOM   5140 C  CB  . ILE D 1 4   ? 19.14000  9.69800   88.25000  1.000 71.08545  ?  4   ILE D CB  1 
ATOM   5141 C  CG1 . ILE D 1 4   ? 19.99300  10.17200  87.07200  1.000 69.12712  ?  4   ILE D CG1 1 
ATOM   5142 C  CG2 . ILE D 1 4   ? 17.67600  9.60100   87.84600  1.000 64.80380  ?  4   ILE D CG2 1 
ATOM   5143 C  CD1 . ILE D 1 4   ? 19.58500  11.53100  86.54200  1.000 62.36619  ?  4   ILE D CD1 1 
ATOM   5144 N  N   . ASP D 1 5   ? 18.22100  9.39300   91.24800  1.000 85.94239  ?  5   ASP D N   1 
ATOM   5145 C  CA  . ASP D 1 5   ? 17.16100  9.13800   92.22200  1.000 84.28073  ?  5   ASP D CA  1 
ATOM   5146 C  C   . ASP D 1 5   ? 17.01600  10.29900  93.19800  1.000 78.38703  ?  5   ASP D C   1 
ATOM   5147 O  O   . ASP D 1 5   ? 15.90100  10.63600  93.61400  1.000 73.90152  ?  5   ASP D O   1 
ATOM   5148 C  CB  . ASP D 1 5   ? 17.43300  7.83000   92.96300  1.000 83.42934  ?  5   ASP D CB  1 
ATOM   5149 C  CG  . ASP D 1 5   ? 17.54000  6.64300   92.02400  1.000 101.07104 ?  5   ASP D CG  1 
ATOM   5150 O  OD1 . ASP D 1 5   ? 17.00800  6.72400   90.89600  1.000 98.99663  ?  5   ASP D OD1 1 
ATOM   5151 O  OD2 . ASP D 1 5   ? 18.15500  5.62800   92.41400  1.000 103.73396 -1 5   ASP D OD2 1 
ATOM   5152 N  N   . THR D 1 6   ? 18.13700  10.90900  93.58700  1.000 78.69110  ?  6   THR D N   1 
ATOM   5153 C  CA  . THR D 1 6   ? 18.09400  12.11400  94.40800  1.000 75.22656  ?  6   THR D CA  1 
ATOM   5154 C  C   . THR D 1 6   ? 17.28500  13.21400  93.73000  1.000 79.55254  ?  6   THR D C   1 
ATOM   5155 O  O   . THR D 1 6   ? 16.40900  13.82900  94.35000  1.000 74.81200  ?  6   THR D O   1 
ATOM   5156 C  CB  . THR D 1 6   ? 19.51400  12.60000  94.70000  1.000 77.47254  ?  6   THR D CB  1 
ATOM   5157 O  OG1 . THR D 1 6   ? 20.23600  11.58500  95.41000  1.000 85.50729  ?  6   THR D OG1 1 
ATOM   5158 C  CG2 . THR D 1 6   ? 19.48800  13.88000  95.52300  1.000 77.91055  ?  6   THR D CG2 1 
ATOM   5159 N  N   . LEU D 1 7   ? 17.56600  13.46900  92.44800  1.000 80.93850  ?  7   LEU D N   1 
ATOM   5160 C  CA  . LEU D 1 7   ? 16.90200  14.56000  91.73800  1.000 68.72703  ?  7   LEU D CA  1 
ATOM   5161 C  C   . LEU D 1 7   ? 15.39900  14.33500  91.64800  1.000 67.78422  ?  7   LEU D C   1 
ATOM   5162 O  O   . LEU D 1 7   ? 14.61400  15.28000  91.79500  1.000 65.04375  ?  7   LEU D O   1 
ATOM   5163 C  CB  . LEU D 1 7   ? 17.50000  14.71900  90.34100  1.000 73.15131  ?  7   LEU D CB  1 
ATOM   5164 C  CG  . LEU D 1 7   ? 19.02400  14.64600  90.26300  1.000 75.91598  ?  7   LEU D CG  1 
ATOM   5165 C  CD1 . LEU D 1 7   ? 19.53900  15.09400  88.89800  1.000 75.24521  ?  7   LEU D CD1 1 
ATOM   5166 C  CD2 . LEU D 1 7   ? 19.63800  15.44400  91.38700  1.000 78.79571  ?  7   LEU D CD2 1 
ATOM   5167 N  N   . ILE D 1 8   ? 14.97800  13.09600  91.38500  1.000 66.31141  ?  8   ILE D N   1 
ATOM   5168 C  CA  . ILE D 1 8   ? 13.55000  12.79200  91.35900  1.000 71.44117  ?  8   ILE D CA  1 
ATOM   5169 C  C   . ILE D 1 8   ? 12.93400  13.04600  92.72900  1.000 76.48061  ?  8   ILE D C   1 
ATOM   5170 O  O   . ILE D 1 8   ? 11.88300  13.68800  92.85000  1.000 77.54346  ?  8   ILE D O   1 
ATOM   5171 C  CB  . ILE D 1 8   ? 13.31500  11.34500  90.88700  1.000 73.65189  ?  8   ILE D CB  1 
ATOM   5172 C  CG1 . ILE D 1 8   ? 13.58000  11.22200  89.38500  1.000 71.28027  ?  8   ILE D CG1 1 
ATOM   5173 C  CG2 . ILE D 1 8   ? 11.90100  10.88900  91.22800  1.000 59.68412  ?  8   ILE D CG2 1 
ATOM   5174 C  CD1 . ILE D 1 8   ? 12.69600  12.11800  88.53600  1.000 60.58224  ?  8   ILE D CD1 1 
ATOM   5175 N  N   . SER D 1 9   ? 13.58300  12.54400  93.78500  1.000 77.07626  ?  9   SER D N   1 
ATOM   5176 C  CA  . SER D 1 9   ? 13.06000  12.72300  95.13600  1.000 75.67895  ?  9   SER D CA  1 
ATOM   5177 C  C   . SER D 1 9   ? 13.06800  14.19000  95.55300  1.000 75.18748  ?  9   SER D C   1 
ATOM   5178 O  O   . SER D 1 9   ? 12.09900  14.67000  96.15100  1.000 72.03464  ?  9   SER D O   1 
ATOM   5179 C  CB  . SER D 1 9   ? 13.85600  11.87500  96.12800  1.000 75.81042  ?  9   SER D CB  1 
ATOM   5180 O  OG  . SER D 1 9   ? 15.12700  12.44400  96.38600  1.000 77.67639  ?  9   SER D OG  1 
ATOM   5181 N  N   . ASN D 1 10  ? 14.15500  14.91600  95.26100  1.000 73.88116  ?  10  ASN D N   1 
ATOM   5182 C  CA  . ASN D 1 10  ? 14.19000  16.34500  95.56900  1.000 71.63669  ?  10  ASN D CA  1 
ATOM   5183 C  C   . ASN D 1 10  ? 13.01900  17.07700  94.92800  1.000 72.62775  ?  10  ASN D C   1 
ATOM   5184 O  O   . ASN D 1 10  ? 12.46500  18.01500  95.51500  1.000 73.75346  ?  10  ASN D O   1 
ATOM   5185 C  CB  . ASN D 1 10  ? 15.50900  16.97100  95.10700  1.000 67.27291  ?  10  ASN D CB  1 
ATOM   5186 C  CG  . ASN D 1 10  ? 16.71800  16.39800  95.81900  1.000 74.96643  ?  10  ASN D CG  1 
ATOM   5187 O  OD1 . ASN D 1 10  ? 16.58900  15.64500  96.78400  1.000 87.99556  ?  10  ASN D OD1 1 
ATOM   5188 N  ND2 . ASN D 1 10  ? 17.90700  16.77400  95.35700  1.000 71.17345  ?  10  ASN D ND2 1 
ATOM   5189 N  N   . ASN D 1 11  ? 12.63700  16.66900  93.71800  1.000 74.76216  ?  11  ASN D N   1 
ATOM   5190 C  CA  . ASN D 1 11  ? 11.54400  17.33100  93.01500  1.000 72.92503  ?  11  ASN D CA  1 
ATOM   5191 C  C   . ASN D 1 11  ? 10.20300  17.10800  93.70500  1.000 73.65838  ?  11  ASN D C   1 
ATOM   5192 O  O   . ASN D 1 11  ? 9.40400   18.04400  93.82900  1.000 74.16407  ?  11  ASN D O   1 
ATOM   5193 C  CB  . ASN D 1 11  ? 11.47900  16.84900  91.57100  1.000 62.52424  ?  11  ASN D CB  1 
ATOM   5194 C  CG  . ASN D 1 11  ? 10.29100  17.41500  90.83500  1.000 64.63749  ?  11  ASN D CG  1 
ATOM   5195 O  OD1 . ASN D 1 11  ? 9.32600   16.70800  90.55400  1.000 66.92953  ?  11  ASN D OD1 1 
ATOM   5196 N  ND2 . ASN D 1 11  ? 10.34700  18.70900  90.52900  1.000 63.77456  ?  11  ASN D ND2 1 
ATOM   5197 N  N   . ALA D 1 12  ? 9.92200   15.87100  94.12700  1.000 76.85456  ?  12  ALA D N   1 
ATOM   5198 C  CA  . ALA D 1 12  ? 8.64300   15.57600  94.76900  1.000 74.71666  ?  12  ALA D CA  1 
ATOM   5199 C  C   . ALA D 1 12  ? 8.46400   16.37400  96.05600  1.000 79.24519  ?  12  ALA D C   1 
ATOM   5200 O  O   . ALA D 1 12  ? 7.38000   16.90900  96.31600  1.000 84.19187  ?  12  ALA D O   1 
ATOM   5201 C  CB  . ALA D 1 12  ? 8.52800   14.07800  95.04500  1.000 67.82215  ?  12  ALA D CB  1 
ATOM   5202 N  N   . LEU D 1 13  ? 9.51200   16.44900  96.88000  1.000 82.58490  ?  13  LEU D N   1 
ATOM   5203 C  CA  . LEU D 1 13  ? 9.45800   17.26000  98.09300  1.000 82.47685  ?  13  LEU D CA  1 
ATOM   5204 C  C   . LEU D 1 13  ? 9.14800   18.71300  97.75600  1.000 87.42912  ?  13  LEU D C   1 
ATOM   5205 O  O   . LEU D 1 13  ? 8.17500   19.29100  98.25200  1.000 90.57010  ?  13  LEU D O   1 
ATOM   5206 C  CB  . LEU D 1 13  ? 10.78400  17.15700  98.84900  1.000 78.12027  ?  13  LEU D CB  1 
ATOM   5207 C  CG  . LEU D 1 13  ? 11.37300  15.75800  99.03400  1.000 82.42943  ?  13  LEU D CG  1 
ATOM   5208 C  CD1 . LEU D 1 13  ? 12.73300  15.83600  99.71200  1.000 77.44785  ?  13  LEU D CD1 1 
ATOM   5209 C  CD2 . LEU D 1 13  ? 10.42600  14.86300  99.81400  1.000 78.85135  ?  13  LEU D CD2 1 
ATOM   5210 N  N   . TRP D 1 14  ? 9.99100   19.31800  96.91500  1.000 80.83872  ?  14  TRP D N   1 
ATOM   5211 C  CA  . TRP D 1 14  ? 9.79200   20.69000  96.45500  1.000 77.01080  ?  14  TRP D CA  1 
ATOM   5212 C  C   . TRP D 1 14  ? 8.37800   20.91600  95.92700  1.000 75.99128  ?  14  TRP D C   1 
ATOM   5213 O  O   . TRP D 1 14  ? 7.81000   22.00100  96.09600  1.000 80.37325  ?  14  TRP D O   1 
ATOM   5214 C  CB  . TRP D 1 14  ? 10.84100  21.00600  95.38700  1.000 75.06002  ?  14  TRP D CB  1 
ATOM   5215 C  CG  . TRP D 1 14  ? 10.63900  22.26800  94.60600  1.000 75.73642  ?  14  TRP D CG  1 
ATOM   5216 C  CD1 . TRP D 1 14  ? 11.06900  23.51900  94.94300  1.000 73.34054  ?  14  TRP D CD1 1 
ATOM   5217 C  CD2 . TRP D 1 14  ? 10.00000  22.39400  93.32900  1.000 84.39729  ?  14  TRP D CD2 1 
ATOM   5218 N  NE1 . TRP D 1 14  ? 10.71800  24.41900  93.96600  1.000 77.68345  ?  14  TRP D NE1 1 
ATOM   5219 C  CE2 . TRP D 1 14  ? 10.06500  23.75300  92.96200  1.000 85.40288  ?  14  TRP D CE2 1 
ATOM   5220 C  CE3 . TRP D 1 14  ? 9.37200   21.49100  92.46500  1.000 78.03784  ?  14  TRP D CE3 1 
ATOM   5221 C  CZ2 . TRP D 1 14  ? 9.52200   24.23200  91.77000  1.000 75.29043  ?  14  TRP D CZ2 1 
ATOM   5222 C  CZ3 . TRP D 1 14  ? 8.83400   21.96800  91.28400  1.000 73.55910  ?  14  TRP D CZ3 1 
ATOM   5223 C  CH2 . TRP D 1 14  ? 8.91100   23.32600  90.94800  1.000 75.43478  ?  14  TRP D CH2 1 
ATOM   5224 N  N   . SER D 1 15  ? 7.79300   19.90500  95.27900  1.000 75.78203  ?  15  SER D N   1 
ATOM   5225 C  CA  . SER D 1 15  ? 6.46000   20.06200  94.70300  1.000 84.63664  ?  15  SER D CA  1 
ATOM   5226 C  C   . SER D 1 15  ? 5.39500   20.24900  95.78300  1.000 87.76560  ?  15  SER D C   1 
ATOM   5227 O  O   . SER D 1 15  ? 4.65000   21.23600  95.76900  1.000 92.56621  ?  15  SER D O   1 
ATOM   5228 C  CB  . SER D 1 15  ? 6.13500   18.85300  93.82200  1.000 82.72670  ?  15  SER D CB  1 
ATOM   5229 O  OG  . SER D 1 15  ? 4.99100   19.09200  93.02000  1.000 82.85063  ?  15  SER D OG  1 
ATOM   5230 N  N   . LYS D 1 16  ? 5.29600   19.30400  96.72400  1.000 90.76077  ?  16  LYS D N   1 
ATOM   5231 C  CA  . LYS D 1 16  ? 4.29200   19.41600  97.78500  1.000 94.33585  ?  16  LYS D CA  1 
ATOM   5232 C  C   . LYS D 1 16  ? 4.57100   20.59100  98.71700  1.000 97.38527  ?  16  LYS D C   1 
ATOM   5233 O  O   . LYS D 1 16  ? 3.64600   21.32100  99.09200  1.000 102.72681 ?  16  LYS D O   1 
ATOM   5234 C  CB  . LYS D 1 16  ? 4.15100   18.10100  98.54800  1.000 90.81462  ?  16  LYS D CB  1 
ATOM   5235 C  CG  . LYS D 1 16  ? 3.45800   17.04200  97.70500  1.000 99.09927  ?  16  LYS D CG  1 
ATOM   5236 C  CD  . LYS D 1 16  ? 3.52000   15.65500  98.29900  1.000 100.84916 ?  16  LYS D CD  1 
ATOM   5237 C  CE  . LYS D 1 16  ? 2.91500   14.65800  97.32800  1.000 112.15253 ?  16  LYS D CE  1 
ATOM   5238 N  NZ  . LYS D 1 16  ? 1.50800   15.03000  96.99100  1.000 110.09042 ?  16  LYS D NZ  1 
ATOM   5239 N  N   . MET D 1 17  ? 5.82700   20.74800  99.15500  1.000 92.95837  ?  17  MET D N   1 
ATOM   5240 C  CA  . MET D 1 17  ? 6.21400   21.90700  99.95800  1.000 97.91852  ?  17  MET D CA  1 
ATOM   5241 C  C   . MET D 1 17  ? 5.61500   23.18200  99.37900  1.000 101.83496 ?  17  MET D C   1 
ATOM   5242 O  O   . MET D 1 17  ? 5.04000   24.00200  100.10300 1.000 107.80799 ?  17  MET D O   1 
ATOM   5243 C  CB  . MET D 1 17  ? 7.74100   22.01200  100.01800 1.000 95.15876  ?  17  MET D CB  1 
ATOM   5244 C  CG  . MET D 1 17  ? 8.44900   20.96400  100.86500 1.000 102.18086 ?  17  MET D CG  1 
ATOM   5245 S  SD  . MET D 1 17  ? 9.97000   21.56300  101.65000 1.000 116.18891 ?  17  MET D SD  1 
ATOM   5246 C  CE  . MET D 1 17  ? 9.68500   23.32800  101.76700 1.000 107.05841 ?  17  MET D CE  1 
ATOM   5247 N  N   . LEU D 1 18  ? 5.74300   23.35900  98.06200  1.000 99.52489  ?  18  LEU D N   1 
ATOM   5248 C  CA  . LEU D 1 18  ? 5.14500   24.52000  97.41500  1.000 100.28813 ?  18  LEU D CA  1 
ATOM   5249 C  C   . LEU D 1 18  ? 3.63100   24.50800  97.57500  1.000 105.46414 ?  18  LEU D C   1 
ATOM   5250 O  O   . LEU D 1 18  ? 3.03800   25.50200  98.00300  1.000 110.74159 ?  18  LEU D O   1 
ATOM   5251 C  CB  . LEU D 1 18  ? 5.52100   24.54500  95.93700  1.000 96.44306  ?  18  LEU D CB  1 
ATOM   5252 C  CG  . LEU D 1 18  ? 6.89100   25.10900  95.58400  1.000 97.38052  ?  18  LEU D CG  1 
ATOM   5253 C  CD1 . LEU D 1 18  ? 7.14100   24.87600  94.12200  1.000 89.39851  ?  18  LEU D CD1 1 
ATOM   5254 C  CD2 . LEU D 1 18  ? 6.94000   26.59100  95.90200  1.000 100.61027 ?  18  LEU D CD2 1 
ATOM   5255 N  N   . VAL D 1 19  ? 2.98900   23.37800  97.26700  1.000 103.82418 ?  19  VAL D N   1 
ATOM   5256 C  CA  . VAL D 1 19  ? 1.54500   23.26900  97.46300  1.000 106.45760 ?  19  VAL D CA  1 
ATOM   5257 C  C   . VAL D 1 19  ? 1.18300   23.58100  98.91000  1.000 106.49662 ?  19  VAL D C   1 
ATOM   5258 O  O   . VAL D 1 19  ? 0.20400   24.28600  99.18400  1.000 108.12065 ?  19  VAL D O   1 
ATOM   5259 C  CB  . VAL D 1 19  ? 1.05200   21.87400  97.03400  1.000 108.00454 ?  19  VAL D CB  1 
ATOM   5260 C  CG1 . VAL D 1 19  ? -0.43100  21.71900  97.32800  1.000 111.30738 ?  19  VAL D CG1 1 
ATOM   5261 C  CG2 . VAL D 1 19  ? 1.33600   21.64300  95.55700  1.000 94.76282  ?  19  VAL D CG2 1 
ATOM   5262 N  N   . GLU D 1 20  ? 1.97000   23.06400  99.85400  1.000 107.93328 ?  20  GLU D N   1 
ATOM   5263 C  CA  . GLU D 1 20  ? 1.73500   23.34100  101.26800 1.000 110.06074 ?  20  GLU D CA  1 
ATOM   5264 C  C   . GLU D 1 20  ? 1.94600   24.81400  101.59900 1.000 108.52909 ?  20  GLU D C   1 
ATOM   5265 O  O   . GLU D 1 20  ? 1.07500   25.46400  102.18900 1.000 109.40073 ?  20  GLU D O   1 
ATOM   5266 C  CB  . GLU D 1 20  ? 2.67600   22.48100  102.11200 1.000 112.18528 ?  20  GLU D CB  1 
ATOM   5267 C  CG  . GLU D 1 20  ? 2.56500   22.69800  103.61100 1.000 117.90278 ?  20  GLU D CG  1 
ATOM   5268 C  CD  . GLU D 1 20  ? 3.60200   21.90800  104.38400 1.000 129.22278 ?  20  GLU D CD  1 
ATOM   5269 O  OE1 . GLU D 1 20  ? 4.47500   21.28600  103.74100 1.000 130.02070 ?  20  GLU D OE1 1 
ATOM   5270 O  OE2 . GLU D 1 20  ? 3.55400   21.91800  105.63200 1.000 131.39212 -1 20  GLU D OE2 1 
ATOM   5271 N  N   . GLU D 1 21  ? 3.09800   25.36100  101.21100 1.000 106.95743 ?  21  GLU D N   1 
ATOM   5272 C  CA  . GLU D 1 21  ? 3.50600   26.70800  101.60200 1.000 103.72671 ?  21  GLU D CA  1 
ATOM   5273 C  C   . GLU D 1 21  ? 2.97900   27.79400  100.66600 1.000 108.17474 ?  21  GLU D C   1 
ATOM   5274 O  O   . GLU D 1 21  ? 2.27900   28.71300  101.10200 1.000 107.55938 ?  21  GLU D O   1 
ATOM   5275 C  CB  . GLU D 1 21  ? 5.03400   26.76200  101.71000 1.000 102.88696 ?  21  GLU D CB  1 
ATOM   5276 C  CG  . GLU D 1 21  ? 5.58200   25.89400  102.83300 1.000 104.98757 ?  21  GLU D CG  1 
ATOM   5277 C  CD  . GLU D 1 21  ? 7.06100   25.60100  102.68900 1.000 109.26652 ?  21  GLU D CD  1 
ATOM   5278 O  OE1 . GLU D 1 21  ? 7.65400   25.99100  101.66100 1.000 115.33890 ?  21  GLU D OE1 1 
ATOM   5279 O  OE2 . GLU D 1 21  ? 7.63400   24.98500  103.61300 1.000 105.20865 -1 21  GLU D OE2 1 
ATOM   5280 N  N   . ASP D 1 22  ? 3.30800   27.70400  99.37900  1.000 110.57581 ?  22  ASP D N   1 
ATOM   5281 C  CA  . ASP D 1 22  ? 2.91600   28.71200  98.39600  1.000 107.49528 ?  22  ASP D CA  1 
ATOM   5282 C  C   . ASP D 1 22  ? 2.17200   28.03600  97.25400  1.000 108.62399 ?  22  ASP D C   1 
ATOM   5283 O  O   . ASP D 1 22  ? 2.77600   27.63500  96.24800  1.000 108.03854 ?  22  ASP D O   1 
ATOM   5284 C  CB  . ASP D 1 22  ? 4.14100   29.46700  97.87600  1.000 106.29744 ?  22  ASP D CB  1 
ATOM   5285 C  CG  . ASP D 1 22  ? 3.79500   30.50200  96.81700  1.000 110.33865 ?  22  ASP D CG  1 
ATOM   5286 O  OD1 . ASP D 1 22  ? 2.60600   30.86500  96.68300  1.000 110.66608 ?  22  ASP D OD1 1 
ATOM   5287 O  OD2 . ASP D 1 22  ? 4.72000   30.94600  96.10400  1.000 104.02533 -1 22  ASP D OD2 1 
ATOM   5288 N  N   . PRO D 1 23  ? 0.84700   27.90200  97.36800  1.000 109.31633 ?  23  PRO D N   1 
ATOM   5289 C  CA  . PRO D 1 23  ? 0.06100   27.35000  96.25900  1.000 103.52322 ?  23  PRO D CA  1 
ATOM   5290 C  C   . PRO D 1 23  ? -0.12900  28.33000  95.12000  1.000 111.38932 ?  23  PRO D C   1 
ATOM   5291 O  O   . PRO D 1 23  ? -0.67300  27.94600  94.07500  1.000 114.44770 ?  23  PRO D O   1 
ATOM   5292 C  CB  . PRO D 1 23  ? -1.27600  27.00000  96.92300  1.000 105.78707 ?  23  PRO D CB  1 
ATOM   5293 C  CG  . PRO D 1 23  ? -1.39700  27.96600  98.05000  1.000 114.23827 ?  23  PRO D CG  1 
ATOM   5294 C  CD  . PRO D 1 23  ? 0.00200   28.31300  98.50400  1.000 113.13684 ?  23  PRO D CD  1 
ATOM   5295 N  N   . GLY D 1 24  ? 0.30100   29.57800  95.29000  1.000 111.83331 ?  24  GLY D N   1 
ATOM   5296 C  CA  . GLY D 1 24  ? 0.20300   30.57500  94.24600  1.000 111.09279 ?  24  GLY D CA  1 
ATOM   5297 C  C   . GLY D 1 24  ? 1.36600   30.55400  93.27800  1.000 107.12274 ?  24  GLY D C   1 
ATOM   5298 O  O   . GLY D 1 24  ? 1.29700   31.17500  92.21400  1.000 108.33349 ?  24  GLY D O   1 
ATOM   5299 N  N   . PHE D 1 25  ? 2.45700   29.87900  93.65500  1.000 106.19062 ?  25  PHE D N   1 
ATOM   5300 C  CA  . PHE D 1 25  ? 3.60000   29.74900  92.75600  1.000 107.79341 ?  25  PHE D CA  1 
ATOM   5301 C  C   . PHE D 1 25  ? 3.16500   29.18300  91.40900  1.000 106.15860 ?  25  PHE D C   1 
ATOM   5302 O  O   . PHE D 1 25  ? 3.51300   29.71800  90.35000  1.000 103.47306 ?  25  PHE D O   1 
ATOM   5303 C  CB  . PHE D 1 25  ? 4.67100   28.86600  93.39900  1.000 105.12217 ?  25  PHE D CB  1 
ATOM   5304 C  CG  . PHE D 1 25  ? 5.74000   28.41000  92.44500  1.000 101.59202 ?  25  PHE D CG  1 
ATOM   5305 C  CD1 . PHE D 1 25  ? 6.75200   29.27400  92.05800  1.000 98.38058  ?  25  PHE D CD1 1 
ATOM   5306 C  CD2 . PHE D 1 25  ? 5.74000   27.11900  91.94300  1.000 98.01920  ?  25  PHE D CD2 1 
ATOM   5307 C  CE1 . PHE D 1 25  ? 7.74200   28.86000  91.18700  1.000 101.05721 ?  25  PHE D CE1 1 
ATOM   5308 C  CE2 . PHE D 1 25  ? 6.72900   26.69700  91.07500  1.000 93.65458  ?  25  PHE D CE2 1 
ATOM   5309 C  CZ  . PHE D 1 25  ? 7.73000   27.57000  90.69400  1.000 97.23586  ?  25  PHE D CZ  1 
ATOM   5310 N  N   . PHE D 1 26  ? 2.39500   28.09200  91.43600  1.000 107.67652 ?  26  PHE D N   1 
ATOM   5311 C  CA  . PHE D 1 26  ? 1.86500   27.50700  90.21200  1.000 101.75632 ?  26  PHE D CA  1 
ATOM   5312 C  C   . PHE D 1 26  ? 0.79300   28.38000  89.57800  1.000 100.62202 ?  26  PHE D C   1 
ATOM   5313 O  O   . PHE D 1 26  ? 0.53700   28.25100  88.37600  1.000 102.89277 ?  26  PHE D O   1 
ATOM   5314 C  CB  . PHE D 1 26  ? 1.31400   26.10900  90.48700  1.000 99.12513  ?  26  PHE D CB  1 
ATOM   5315 C  CG  . PHE D 1 26  ? 2.26800   25.23000  91.23200  1.000 96.75341  ?  26  PHE D CG  1 
ATOM   5316 C  CD1 . PHE D 1 26  ? 3.41100   24.75000  90.61600  1.000 92.80914  ?  26  PHE D CD1 1 
ATOM   5317 C  CD2 . PHE D 1 26  ? 2.02000   24.87900  92.54600  1.000 100.35530 ?  26  PHE D CD2 1 
ATOM   5318 C  CE1 . PHE D 1 26  ? 4.29600   23.94800  91.30400  1.000 86.79501  ?  26  PHE D CE1 1 
ATOM   5319 C  CE2 . PHE D 1 26  ? 2.89700   24.07100  93.23600  1.000 101.71760 ?  26  PHE D CE2 1 
ATOM   5320 C  CZ  . PHE D 1 26  ? 4.03700   23.60200  92.61300  1.000 95.74648  ?  26  PHE D CZ  1 
ATOM   5321 N  N   . GLU D 1 27  ? 0.15900   29.26300  90.35600  1.000 106.96624 ?  27  GLU D N   1 
ATOM   5322 C  CA  . GLU D 1 27  ? -0.80500  30.19000  89.77300  1.000 105.67687 ?  27  GLU D CA  1 
ATOM   5323 C  C   . GLU D 1 27  ? -0.11800  31.19400  88.86000  1.000 107.75278 ?  27  GLU D C   1 
ATOM   5324 O  O   . GLU D 1 27  ? -0.60700  31.46700  87.75800  1.000 106.28734 ?  27  GLU D O   1 
ATOM   5325 C  CB  . GLU D 1 27  ? -1.54300  30.95100  90.87300  1.000 109.16048 ?  27  GLU D CB  1 
ATOM   5326 C  CG  . GLU D 1 27  ? -2.35700  30.13100  91.84000  1.000 116.27935 ?  27  GLU D CG  1 
ATOM   5327 C  CD  . GLU D 1 27  ? -2.93500  30.99800  92.94500  1.000 119.87830 ?  27  GLU D CD  1 
ATOM   5328 O  OE1 . GLU D 1 27  ? -2.49200  32.16100  93.07900  1.000 122.57453 ?  27  GLU D OE1 1 
ATOM   5329 O  OE2 . GLU D 1 27  ? -3.81800  30.51900  93.68500  1.000 118.37895 -1 27  GLU D OE2 1 
ATOM   5330 N  N   . LYS D 1 28  ? 1.01900   31.74600  89.29500  1.000 109.78095 ?  28  LYS D N   1 
ATOM   5331 C  CA  . LYS D 1 28  ? 1.77300   32.65700  88.43700  1.000 109.82003 ?  28  LYS D CA  1 
ATOM   5332 C  C   . LYS D 1 28  ? 2.23100   31.94300  87.17800  1.000 107.62768 ?  28  LYS D C   1 
ATOM   5333 O  O   . LYS D 1 28  ? 2.11600   32.47000  86.06800  1.000 112.80879 ?  28  LYS D O   1 
ATOM   5334 C  CB  . LYS D 1 28  ? 2.98800   33.22700  89.17400  1.000 110.22471 ?  28  LYS D CB  1 
ATOM   5335 C  CG  . LYS D 1 28  ? 2.70100   33.90400  90.49900  1.000 107.84130 ?  28  LYS D CG  1 
ATOM   5336 C  CD  . LYS D 1 28  ? 3.91000   33.77200  91.42800  1.000 107.71993 ?  28  LYS D CD  1 
ATOM   5337 C  CE  . LYS D 1 28  ? 3.65300   34.37700  92.80700  1.000 110.54802 ?  28  LYS D CE  1 
ATOM   5338 N  NZ  . LYS D 1 28  ? 2.48800   33.72200  93.48700  1.000 110.27191 ?  28  LYS D NZ  1 
ATOM   5339 N  N   . LEU D 1 29  ? 2.76000   30.73000  87.34500  1.000 105.27624 ?  29  LEU D N   1 
ATOM   5340 C  CA  . LEU D 1 29  ? 3.20100   29.93200  86.21100  1.000 103.92923 ?  29  LEU D CA  1 
ATOM   5341 C  C   . LEU D 1 29  ? 2.04700   29.65400  85.25400  1.000 102.60853 ?  29  LEU D C   1 
ATOM   5342 O  O   . LEU D 1 29  ? 2.24900   29.57500  84.03600  1.000 104.59539 ?  29  LEU D O   1 
ATOM   5343 C  CB  . LEU D 1 29  ? 3.79200   28.62200  86.72300  1.000 98.74956  ?  29  LEU D CB  1 
ATOM   5344 C  CG  . LEU D 1 29  ? 5.21500   28.63900  87.29200  1.000 96.87181  ?  29  LEU D CG  1 
ATOM   5345 C  CD1 . LEU D 1 29  ? 5.55100   27.27300  87.87800  1.000 93.41879  ?  29  LEU D CD1 1 
ATOM   5346 C  CD2 . LEU D 1 29  ? 6.27000   29.10600  86.29900  1.000 97.61078  ?  29  LEU D CD2 1 
ATOM   5347 N  N   . ALA D 1 30  ? 0.83200   29.52200  85.79500  1.000 102.89387 ?  30  ALA D N   1 
ATOM   5348 C  CA  . ALA D 1 30  ? -0.36700  29.26800  84.99900  1.000 102.05431 ?  30  ALA D CA  1 
ATOM   5349 C  C   . ALA D 1 30  ? -0.73300  30.44600  84.10000  1.000 105.12307 ?  30  ALA D C   1 
ATOM   5350 O  O   . ALA D 1 30  ? -1.15300  30.22800  82.95400  1.000 107.26613 ?  30  ALA D O   1 
ATOM   5351 C  CB  . ALA D 1 30  ? -1.53600  28.92000  85.91700  1.000 99.38208  ?  30  ALA D CB  1 
ATOM   5352 N  N   . GLN D 1 31  ? -0.61100  31.68100  84.58300  1.000 106.95148 ?  31  GLN D N   1 
ATOM   5353 C  CA  . GLN D 1 31  ? -0.94800  32.81100  83.72800  1.000 112.31229 ?  31  GLN D CA  1 
ATOM   5354 C  C   . GLN D 1 31  ? 0.04200   32.93400  82.56800  1.000 112.87286 ?  31  GLN D C   1 
ATOM   5355 O  O   . GLN D 1 31  ? 1.06500   32.24200  82.49900  1.000 111.89498 ?  31  GLN D O   1 
ATOM   5356 C  CB  . GLN D 1 31  ? -0.99700  34.12200  84.51800  1.000 112.64586 ?  31  GLN D CB  1 
ATOM   5357 C  CG  . GLN D 1 31  ? -2.23400  34.31600  85.39700  1.000 110.90566 ?  31  GLN D CG  1 
ATOM   5358 C  CD  . GLN D 1 31  ? -2.08500  35.47900  86.36400  1.000 120.68126 ?  31  GLN D CD  1 
ATOM   5359 O  OE1 . GLN D 1 31  ? -1.07400  36.18000  86.35700  1.000 122.45303 ?  31  GLN D OE1 1 
ATOM   5360 N  NE2 . GLN D 1 31  ? -3.12400  35.72900  87.15500  1.000 125.43129 ?  31  GLN D NE2 1 
ATOM   5361 N  N   . ALA D 1 32  ? -0.30500  33.82800  81.64000  1.000 111.15631 ?  32  ALA D N   1 
ATOM   5362 C  CA  . ALA D 1 32  ? 0.45700   34.03800  80.41000  1.000 114.10504 ?  32  ALA D CA  1 
ATOM   5363 C  C   . ALA D 1 32  ? 1.95700   34.11600  80.66600  1.000 113.45576 ?  32  ALA D C   1 
ATOM   5364 O  O   . ALA D 1 32  ? 2.72700   33.27100  80.19200  1.000 113.43332 ?  32  ALA D O   1 
ATOM   5365 C  CB  . ALA D 1 32  ? -0.03700  35.31200  79.72200  1.000 113.53664 ?  32  ALA D CB  1 
ATOM   5366 N  N   . GLN D 1 33  ? 2.37800   35.13000  81.40500  1.000 113.81390 ?  33  GLN D N   1 
ATOM   5367 C  CA  . GLN D 1 33  ? 3.77900   35.36000  81.73800  1.000 110.64158 ?  33  GLN D CA  1 
ATOM   5368 C  C   . GLN D 1 33  ? 4.62200   35.44000  80.46900  1.000 109.32126 ?  33  GLN D C   1 
ATOM   5369 O  O   . GLN D 1 33  ? 5.65800   34.78500  80.33900  1.000 106.41463 ?  33  GLN D O   1 
ATOM   5370 C  CB  . GLN D 1 33  ? 4.31600   34.27700  82.67000  1.000 105.93953 ?  33  GLN D CB  1 
ATOM   5371 C  CG  . GLN D 1 33  ? 3.50200   34.13400  83.92000  1.000 109.62488 ?  33  GLN D CG  1 
ATOM   5372 C  CD  . GLN D 1 33  ? 3.35400   35.43400  84.66700  1.000 117.22635 ?  33  GLN D CD  1 
ATOM   5373 O  OE1 . GLN D 1 33  ? 2.28100   36.03500  84.65500  1.000 118.76537 ?  33  GLN D OE1 1 
ATOM   5374 N  NE2 . GLN D 1 33  ? 4.43100   35.89900  85.28700  1.000 117.57448 ?  33  GLN D NE2 1 
ATOM   5375 N  N   . LYS D 1 34  ? 4.15600   36.24000  79.51600  1.000 99.93082  ?  34  LYS D N   1 
ATOM   5376 C  CA  . LYS D 1 34  ? 4.90800   36.41500  78.28400  1.000 94.00477  ?  34  LYS D CA  1 
ATOM   5377 C  C   . LYS D 1 34  ? 6.26100   37.02800  78.61800  1.000 89.85632  ?  34  LYS D C   1 
ATOM   5378 O  O   . LYS D 1 34  ? 6.30800   38.11500  79.20900  1.000 92.13944  ?  34  LYS D O   1 
ATOM   5379 C  CB  . LYS D 1 34  ? 4.14600   37.32200  77.32600  1.000 98.05594  ?  34  LYS D CB  1 
ATOM   5380 C  CG  . LYS D 1 34  ? 2.85400   36.72700  76.79700  1.000 101.47047 ?  34  LYS D CG  1 
ATOM   5381 C  CD  . LYS D 1 34  ? 2.13100   37.68500  75.86900  1.000 108.01610 ?  34  LYS D CD  1 
ATOM   5382 C  CE  . LYS D 1 34  ? 0.85800   37.04800  75.34000  1.000 106.41402 ?  34  LYS D CE  1 
ATOM   5383 N  NZ  . LYS D 1 34  ? 0.13000   37.99300  74.44700  1.000 95.94821  ?  34  LYS D NZ  1 
ATOM   5384 N  N   . PRO D 1 35  ? 7.36900   36.38000  78.26500  1.000 88.48014  ?  35  PRO D N   1 
ATOM   5385 C  CA  . PRO D 1 35  ? 8.67900   36.92400  78.62600  1.000 88.03749  ?  35  PRO D CA  1 
ATOM   5386 C  C   . PRO D 1 35  ? 9.00100   38.22400  77.92000  1.000 90.27570  ?  35  PRO D C   1 
ATOM   5387 O  O   . PRO D 1 35  ? 8.53700   38.48700  76.80900  1.000 94.26913  ?  35  PRO D O   1 
ATOM   5388 C  CB  . PRO D 1 35  ? 9.65400   35.81000  78.23400  1.000 87.36368  ?  35  PRO D CB  1 
ATOM   5389 C  CG  . PRO D 1 35  ? 8.91000   34.97800  77.25500  1.000 86.76296  ?  35  PRO D CG  1 
ATOM   5390 C  CD  . PRO D 1 35  ? 7.47400   35.04300  77.66200  1.000 85.84690  ?  35  PRO D CD  1 
ATOM   5391 N  N   . ARG D 1 36  ? 9.81600   39.03300  78.59000  1.000 82.13920  ?  36  ARG D N   1 
ATOM   5392 C  CA  . ARG D 1 36  ? 10.34900  40.26700  78.05000  1.000 87.80786  ?  36  ARG D CA  1 
ATOM   5393 C  C   . ARG D 1 36  ? 11.85300  40.22400  77.87800  1.000 87.37675  ?  36  ARG D C   1 
ATOM   5394 O  O   . ARG D 1 36  ? 12.41700  41.11100  77.22700  1.000 90.39329  ?  36  ARG D O   1 
ATOM   5395 C  CB  . ARG D 1 36  ? 9.98500   41.44500  78.95100  1.000 90.89669  ?  36  ARG D CB  1 
ATOM   5396 C  CG  . ARG D 1 36  ? 10.04700  42.76600  78.25900  1.000 101.56588 ?  36  ARG D CG  1 
ATOM   5397 C  CD  . ARG D 1 36  ? 9.59200   43.85100  79.18600  1.000 103.95567 ?  36  ARG D CD  1 
ATOM   5398 N  NE  . ARG D 1 36  ? 10.44500  43.98300  80.35700  1.000 95.22243  ?  36  ARG D NE  1 
ATOM   5399 C  CZ  . ARG D 1 36  ? 11.46500  44.82400  80.44500  1.000 101.33533 ?  36  ARG D CZ  1 
ATOM   5400 N  NH1 . ARG D 1 36  ? 11.78600  45.62700  79.44400  1.000 102.49273 ?  36  ARG D NH1 1 
ATOM   5401 N  NH2 . ARG D 1 36  ? 12.15900  44.88200  81.57300  1.000 102.29590 ?  36  ARG D NH2 1 
ATOM   5402 N  N   . PHE D 1 37  ? 12.50300  39.19000  78.38300  1.000 81.99941  ?  37  PHE D N   1 
ATOM   5403 C  CA  . PHE D 1 37  ? 13.94900  39.09100  78.34500  1.000 82.63753  ?  37  PHE D CA  1 
ATOM   5404 C  C   . PHE D 1 37  ? 14.34100  37.80900  77.63700  1.000 75.29656  ?  37  PHE D C   1 
ATOM   5405 O  O   . PHE D 1 37  ? 13.70100  36.76900  77.80200  1.000 76.19061  ?  37  PHE D O   1 
ATOM   5406 C  CB  . PHE D 1 37  ? 14.55500  39.07500  79.74600  1.000 87.87770  ?  37  PHE D CB  1 
ATOM   5407 C  CG  . PHE D 1 37  ? 14.29400  40.31100  80.55000  1.000 87.47612  ?  37  PHE D CG  1 
ATOM   5408 C  CD1 . PHE D 1 37  ? 13.12300  40.45600  81.28200  1.000 90.92780  ?  37  PHE D CD1 1 
ATOM   5409 C  CD2 . PHE D 1 37  ? 15.24700  41.31100  80.61700  1.000 89.62718  ?  37  PHE D CD2 1 
ATOM   5410 C  CE1 . PHE D 1 37  ? 12.90500  41.59000  82.04300  1.000 95.27427  ?  37  PHE D CE1 1 
ATOM   5411 C  CE2 . PHE D 1 37  ? 15.03400  42.44100  81.37100  1.000 91.95017  ?  37  PHE D CE2 1 
ATOM   5412 C  CZ  . PHE D 1 37  ? 13.86700  42.58000  82.08800  1.000 95.01043  ?  37  PHE D CZ  1 
ATOM   5413 N  N   . LEU D 1 38  ? 15.40300  37.89900  76.84600  1.000 76.33026  ?  38  LEU D N   1 
ATOM   5414 C  CA  . LEU D 1 38  ? 16.06400  36.74100  76.26900  1.000 76.75338  ?  38  LEU D CA  1 
ATOM   5415 C  C   . LEU D 1 38  ? 17.47200  36.65800  76.83900  1.000 73.19886  ?  38  LEU D C   1 
ATOM   5416 O  O   . LEU D 1 38  ? 18.23100  37.63100  76.77000  1.000 73.65454  ?  38  LEU D O   1 
ATOM   5417 C  CB  . LEU D 1 38  ? 16.09400  36.82800  74.74200  1.000 76.37961  ?  38  LEU D CB  1 
ATOM   5418 C  CG  . LEU D 1 38  ? 16.94200  35.79800  73.99800  1.000 76.23972  ?  38  LEU D CG  1 
ATOM   5419 C  CD1 . LEU D 1 38  ? 16.47900  34.38900  74.31600  1.000 74.54344  ?  38  LEU D CD1 1 
ATOM   5420 C  CD2 . LEU D 1 38  ? 16.86900  36.05900  72.50500  1.000 67.52970  ?  38  LEU D CD2 1 
ATOM   5421 N  N   . TRP D 1 39  ? 17.81400  35.51000  77.41300  1.000 69.80283  ?  39  TRP D N   1 
ATOM   5422 C  CA  . TRP D 1 39  ? 19.13700  35.28700  77.98100  1.000 71.13658  ?  39  TRP D CA  1 
ATOM   5423 C  C   . TRP D 1 39  ? 19.89600  34.34600  77.05600  1.000 67.45930  ?  39  TRP D C   1 
ATOM   5424 O  O   . TRP D 1 39  ? 19.51600  33.18100  76.89800  1.000 68.00701  ?  39  TRP D O   1 
ATOM   5425 C  CB  . TRP D 1 39  ? 19.04700  34.71200  79.39400  1.000 73.14250  ?  39  TRP D CB  1 
ATOM   5426 C  CG  . TRP D 1 39  ? 20.35900  34.73100  80.12000  1.000 71.15930  ?  39  TRP D CG  1 
ATOM   5427 C  CD1 . TRP D 1 39  ? 21.35200  33.79700  80.04600  1.000 70.00746  ?  39  TRP D CD1 1 
ATOM   5428 C  CD2 . TRP D 1 39  ? 20.81700  35.73200  81.03700  1.000 70.15953  ?  39  TRP D CD2 1 
ATOM   5429 N  NE1 . TRP D 1 39  ? 22.40300  34.15800  80.85500  1.000 70.61207  ?  39  TRP D NE1 1 
ATOM   5430 C  CE2 . TRP D 1 39  ? 22.09900  35.34100  81.47600  1.000 71.48379  ?  39  TRP D CE2 1 
ATOM   5431 C  CE3 . TRP D 1 39  ? 20.26800  36.92000  81.53000  1.000 71.31671  ?  39  TRP D CE3 1 
ATOM   5432 C  CZ2 . TRP D 1 39  ? 22.84000  36.09600  82.38300  1.000 69.52937  ?  39  TRP D CZ2 1 
ATOM   5433 C  CZ3 . TRP D 1 39  ? 21.00700  37.66900  82.43000  1.000 73.56326  ?  39  TRP D CZ3 1 
ATOM   5434 C  CH2 . TRP D 1 39  ? 22.27900  37.25400  82.84700  1.000 72.12795  ?  39  TRP D CH2 1 
ATOM   5435 N  N   . ILE D 1 40  ? 20.96100  34.85200  76.44700  1.000 65.63287  ?  40  ILE D N   1 
ATOM   5436 C  CA  . ILE D 1 40  ? 21.87400  34.04500  75.64800  1.000 67.70386  ?  40  ILE D CA  1 
ATOM   5437 C  C   . ILE D 1 40  ? 23.14400  33.91100  76.47500  1.000 63.79429  ?  40  ILE D C   1 
ATOM   5438 O  O   . ILE D 1 40  ? 23.93900  34.85200  76.57400  1.000 69.65390  ?  40  ILE D O   1 
ATOM   5439 C  CB  . ILE D 1 40  ? 22.14800  34.66900  74.27500  1.000 70.16621  ?  40  ILE D CB  1 
ATOM   5440 C  CG1 . ILE D 1 40  ? 20.84500  34.80800  73.48300  1.000 66.50823  ?  40  ILE D CG1 1 
ATOM   5441 C  CG2 . ILE D 1 40  ? 23.16100  33.83900  73.50200  1.000 64.23823  ?  40  ILE D CG2 1 
ATOM   5442 C  CD1 . ILE D 1 40  ? 21.00400  35.53200  72.16200  1.000 61.81483  ?  40  ILE D CD1 1 
ATOM   5443 N  N   . GLY D 1 41  ? 23.34500  32.73100  77.06500  1.000 62.68748  ?  41  GLY D N   1 
ATOM   5444 C  CA  . GLY D 1 41  ? 24.44000  32.50700  77.98400  1.000 67.92129  ?  41  GLY D CA  1 
ATOM   5445 C  C   . GLY D 1 41  ? 25.19800  31.23000  77.66700  1.000 62.50288  ?  41  GLY D C   1 
ATOM   5446 O  O   . GLY D 1 41  ? 24.87900  30.51000  76.72100  1.000 68.44394  ?  41  GLY D O   1 
ATOM   5447 N  N   . CYS D 1 42  ? 26.22800  30.98900  78.47000  1.000 61.35021  ?  42  CYS D N   1 
ATOM   5448 C  CA  . CYS D 1 42  ? 27.07800  29.82100  78.30000  1.000 64.23151  ?  42  CYS D CA  1 
ATOM   5449 C  C   . CYS D 1 42  ? 26.42800  28.57000  78.88400  1.000 66.16285  ?  42  CYS D C   1 
ATOM   5450 O  O   . CYS D 1 42  ? 25.67000  28.62800  79.85800  1.000 65.66996  ?  42  CYS D O   1 
ATOM   5451 C  CB  . CYS D 1 42  ? 28.43600  30.05600  78.96100  1.000 67.00747  ?  42  CYS D CB  1 
ATOM   5452 S  SG  . CYS D 1 42  ? 29.56600  28.66200  78.84100  1.000 70.65585  ?  42  CYS D SG  1 
ATOM   5453 N  N   . SER D 1 43  ? 26.73900  27.42300  78.27200  1.000 68.08741  ?  43  SER D N   1 
ATOM   5454 C  CA  . SER D 1 43  ? 26.25500  26.14400  78.78000  1.000 68.12852  ?  43  SER D CA  1 
ATOM   5455 C  C   . SER D 1 43  ? 26.91600  25.75200  80.09500  1.000 74.35936  ?  43  SER D C   1 
ATOM   5456 O  O   . SER D 1 43  ? 26.41100  24.85700  80.78000  1.000 74.63922  ?  43  SER D O   1 
ATOM   5457 C  CB  . SER D 1 43  ? 26.46700  25.04300  77.74000  1.000 69.62630  ?  43  SER D CB  1 
ATOM   5458 O  OG  . SER D 1 43  ? 25.54200  25.16900  76.67500  1.000 74.32152  ?  43  SER D OG  1 
ATOM   5459 N  N   . ASP D 1 44  ? 28.03700  26.38700  80.44900  1.000 70.08359  ?  44  ASP D N   1 
ATOM   5460 C  CA  . ASP D 1 44  ? 28.63200  26.15600  81.76100  1.000 71.68160  ?  44  ASP D CA  1 
ATOM   5461 C  C   . ASP D 1 44  ? 27.62600  26.45600  82.86200  1.000 73.95937  ?  44  ASP D C   1 
ATOM   5462 O  O   . ASP D 1 44  ? 27.50000  25.69100  83.82600  1.000 77.18606  ?  44  ASP D O   1 
ATOM   5463 C  CB  . ASP D 1 44  ? 29.87800  27.02400  81.92900  1.000 75.49579  ?  44  ASP D CB  1 
ATOM   5464 C  CG  . ASP D 1 44  ? 31.06400  26.50500  81.14100  1.000 76.25265  ?  44  ASP D CG  1 
ATOM   5465 O  OD1 . ASP D 1 44  ? 31.28100  25.27700  81.12500  1.000 69.90935  ?  44  ASP D OD1 1 
ATOM   5466 O  OD2 . ASP D 1 44  ? 31.76900  27.32800  80.51800  1.000 82.37343  -1 44  ASP D OD2 1 
ATOM   5467 N  N   . SER D 1 45  ? 26.88500  27.55600  82.71300  1.000 67.45875  ?  45  SER D N   1 
ATOM   5468 C  CA  . SER D 1 45  ? 25.86100  27.98600  83.66100  1.000 70.58071  ?  45  SER D CA  1 
ATOM   5469 C  C   . SER D 1 45  ? 26.36700  27.89000  85.10000  1.000 82.53162  ?  45  SER D C   1 
ATOM   5470 O  O   . SER D 1 45  ? 25.71900  27.31900  85.98100  1.000 83.67913  ?  45  SER D O   1 
ATOM   5471 C  CB  . SER D 1 45  ? 24.57600  27.18000  83.46600  1.000 63.02582  ?  45  SER D CB  1 
ATOM   5472 O  OG  . SER D 1 45  ? 23.47000  27.82200  84.07600  1.000 75.43532  ?  45  SER D OG  1 
ATOM   5473 N  N   . ARG D 1 46  ? 27.55800  28.45300  85.32400  1.000 82.18883  ?  46  ARG D N   1 
ATOM   5474 C  CA  . ARG D 1 46  ? 28.17200  28.39700  86.64600  1.000 83.32444  ?  46  ARG D CA  1 
ATOM   5475 C  C   . ARG D 1 46  ? 27.27200  29.04100  87.69100  1.000 87.39970  ?  46  ARG D C   1 
ATOM   5476 O  O   . ARG D 1 46  ? 27.19200  28.57000  88.83100  1.000 89.47537  ?  46  ARG D O   1 
ATOM   5477 C  CB  . ARG D 1 46  ? 29.54800  29.06100  86.61900  1.000 80.13603  ?  46  ARG D CB  1 
ATOM   5478 C  CG  . ARG D 1 46  ? 30.55100  28.36200  85.70900  1.000 82.66181  ?  46  ARG D CG  1 
ATOM   5479 C  CD  . ARG D 1 46  ? 30.66900  26.87300  86.02000  1.000 83.13563  ?  46  ARG D CD  1 
ATOM   5480 N  NE  . ARG D 1 46  ? 31.40200  26.61100  87.25300  1.000 94.72997  ?  46  ARG D NE  1 
ATOM   5481 C  CZ  . ARG D 1 46  ? 31.52000  25.41500  87.81300  1.000 92.83107  ?  46  ARG D CZ  1 
ATOM   5482 N  NH1 . ARG D 1 46  ? 30.95700  24.34300  87.28000  1.000 80.74357  ?  46  ARG D NH1 1 
ATOM   5483 N  NH2 . ARG D 1 46  ? 32.22600  25.28900  88.93400  1.000 95.70783  ?  46  ARG D NH2 1 
ATOM   5484 N  N   . VAL D 1 47  ? 26.59700  30.13200  87.32500  1.000 85.20147  ?  47  VAL D N   1 
ATOM   5485 C  CA  . VAL D 1 47  ? 25.54100  30.71200  88.13700  1.000 84.78057  ?  47  VAL D CA  1 
ATOM   5486 C  C   . VAL D 1 47  ? 24.32500  30.84600  87.22800  1.000 84.04169  ?  47  VAL D C   1 
ATOM   5487 O  O   . VAL D 1 47  ? 24.39800  31.52200  86.19800  1.000 82.78601  ?  47  VAL D O   1 
ATOM   5488 C  CB  . VAL D 1 47  ? 25.91800  32.08500  88.72100  1.000 86.52298  ?  47  VAL D CB  1 
ATOM   5489 C  CG1 . VAL D 1 47  ? 24.87900  32.52700  89.74500  1.000 84.29701  ?  47  VAL D CG1 1 
ATOM   5490 C  CG2 . VAL D 1 47  ? 27.31200  32.06400  89.31500  1.000 86.70476  ?  47  VAL D CG2 1 
ATOM   5491 N  N   . PRO D 1 48  ? 23.19900  30.20400  87.54200  1.000 85.41285  ?  48  PRO D N   1 
ATOM   5492 C  CA  . PRO D 1 48  ? 22.01100  30.34100  86.69200  1.000 85.23655  ?  48  PRO D CA  1 
ATOM   5493 C  C   . PRO D 1 48  ? 21.58400  31.79500  86.55900  1.000 80.99908  ?  48  PRO D C   1 
ATOM   5494 O  O   . PRO D 1 48  ? 21.83300  32.62200  87.43800  1.000 82.86858  ?  48  PRO D O   1 
ATOM   5495 C  CB  . PRO D 1 48  ? 20.95300  29.51200  87.42700  1.000 88.04333  ?  48  PRO D CB  1 
ATOM   5496 C  CG  . PRO D 1 48  ? 21.74600  28.49700  88.18100  1.000 90.92037  ?  48  PRO D CG  1 
ATOM   5497 C  CD  . PRO D 1 48  ? 23.01000  29.19900  88.60100  1.000 88.84210  ?  48  PRO D CD  1 
ATOM   5498 N  N   . ALA D 1 49  ? 20.93700  32.10100  85.43300  1.000 83.68911  ?  49  ALA D N   1 
ATOM   5499 C  CA  . ALA D 1 49  ? 20.57600  33.48400  85.14400  1.000 81.47416  ?  49  ALA D CA  1 
ATOM   5500 C  C   . ALA D 1 49  ? 19.54700  34.01800  86.13100  1.000 75.89380  ?  49  ALA D C   1 
ATOM   5501 O  O   . ALA D 1 49  ? 19.55500  35.21300  86.44500  1.000 75.74162  ?  49  ALA D O   1 
ATOM   5502 C  CB  . ALA D 1 49  ? 20.05000  33.60200  83.71300  1.000 77.47317  ?  49  ALA D CB  1 
ATOM   5503 N  N   . GLU D 1 50  ? 18.65800  33.15500  86.62900  1.000 77.04872  ?  50  GLU D N   1 
ATOM   5504 C  CA  . GLU D 1 50  ? 17.63500  33.60300  87.56800  1.000 87.44083  ?  50  GLU D CA  1 
ATOM   5505 C  C   . GLU D 1 50  ? 18.25100  34.00700  88.90300  1.000 87.09953  ?  50  GLU D C   1 
ATOM   5506 O  O   . GLU D 1 50  ? 17.77800  34.94400  89.55500  1.000 83.00182  ?  50  GLU D O   1 
ATOM   5507 C  CB  . GLU D 1 50  ? 16.58200  32.51000  87.76000  1.000 87.19897  ?  50  GLU D CB  1 
ATOM   5508 C  CG  . GLU D 1 50  ? 15.77600  32.18300  86.50300  1.000 87.53955  ?  50  GLU D CG  1 
ATOM   5509 C  CD  . GLU D 1 50  ? 16.52000  31.28200  85.52900  1.000 95.04842  ?  50  GLU D CD  1 
ATOM   5510 O  OE1 . GLU D 1 50  ? 17.65800  30.87000  85.84500  1.000 93.23458  ?  50  GLU D OE1 1 
ATOM   5511 O  OE2 . GLU D 1 50  ? 15.96600  30.99300  84.44400  1.000 80.78357  -1 50  GLU D OE2 1 
ATOM   5512 N  N   . ARG D 1 51  ? 19.30100  33.30200  89.32800  1.000 84.99305  ?  51  ARG D N   1 
ATOM   5513 C  CA  . ARG D 1 51  ? 20.00400  33.65800  90.55700  1.000 80.79044  ?  51  ARG D CA  1 
ATOM   5514 C  C   . ARG D 1 51  ? 20.79500  34.94900  90.39400  1.000 85.95024  ?  51  ARG D C   1 
ATOM   5515 O  O   . ARG D 1 51  ? 20.82700  35.78100  91.30800  1.000 97.04808  ?  51  ARG D O   1 
ATOM   5516 C  CB  . ARG D 1 51  ? 20.91500  32.50100  90.95800  1.000 83.19049  ?  51  ARG D CB  1 
ATOM   5517 C  CG  . ARG D 1 51  ? 20.14300  31.26900  91.36900  1.000 92.76713  ?  51  ARG D CG  1 
ATOM   5518 C  CD  . ARG D 1 51  ? 21.05400  30.11000  91.68700  1.000 96.25217  ?  51  ARG D CD  1 
ATOM   5519 N  NE  . ARG D 1 51  ? 20.27600  28.93100  92.04700  1.000 99.96599  ?  51  ARG D NE  1 
ATOM   5520 C  CZ  . ARG D 1 51  ? 20.68900  27.68300  91.88000  1.000 101.01199 ?  51  ARG D CZ  1 
ATOM   5521 N  NH1 . ARG D 1 51  ? 21.84500  27.41100  91.30400  1.000 98.79925  ?  51  ARG D NH1 1 
ATOM   5522 N  NH2 . ARG D 1 51  ? 19.92300  26.68300  92.30400  1.000 99.41212  ?  51  ARG D NH2 1 
ATOM   5523 N  N   . LEU D 1 52  ? 21.43800  35.13500  89.23900  1.000 84.33651  ?  52  LEU D N   1 
ATOM   5524 C  CA  . LEU D 1 52  ? 22.22400  36.34400  89.01500  1.000 85.32628  ?  52  LEU D CA  1 
ATOM   5525 C  C   . LEU D 1 52  ? 21.34000  37.58400  88.98900  1.000 87.34584  ?  52  LEU D C   1 
ATOM   5526 O  O   . LEU D 1 52  ? 21.73200  38.64400  89.49000  1.000 90.56801  ?  52  LEU D O   1 
ATOM   5527 C  CB  . LEU D 1 52  ? 23.01000  36.23200  87.70900  1.000 88.48557  ?  52  LEU D CB  1 
ATOM   5528 C  CG  . LEU D 1 52  ? 24.26300  35.35800  87.68800  1.000 89.82615  ?  52  LEU D CG  1 
ATOM   5529 C  CD1 . LEU D 1 52  ? 24.71700  35.11800  86.25500  1.000 85.53151  ?  52  LEU D CD1 1 
ATOM   5530 C  CD2 . LEU D 1 52  ? 25.37800  35.98300  88.51100  1.000 88.98736  ?  52  LEU D CD2 1 
ATOM   5531 N  N   . THR D 1 53  ? 20.14400  37.47100  88.41400  1.000 86.17158  ?  53  THR D N   1 
ATOM   5532 C  CA  . THR D 1 53  ? 19.28700  38.62200  88.18100  1.000 87.11125  ?  53  THR D CA  1 
ATOM   5533 C  C   . THR D 1 53  ? 18.08900  38.70000  89.11500  1.000 87.04368  ?  53  THR D C   1 
ATOM   5534 O  O   . THR D 1 53  ? 17.37600  39.70900  89.09000  1.000 89.69870  ?  53  THR D O   1 
ATOM   5535 C  CB  . THR D 1 53  ? 18.78700  38.62000  86.72800  1.000 92.23182  ?  53  THR D CB  1 
ATOM   5536 O  OG1 . THR D 1 53  ? 18.08400  37.39800  86.46500  1.000 87.10309  ?  53  THR D OG1 1 
ATOM   5537 C  CG2 . THR D 1 53  ? 19.95900  38.73800  85.76500  1.000 85.45330  ?  53  THR D CG2 1 
ATOM   5538 N  N   . GLY D 1 54  ? 17.83800  37.67400  89.92600  1.000 87.72007  ?  54  GLY D N   1 
ATOM   5539 C  CA  . GLY D 1 54  ? 16.65000  37.69100  90.75400  1.000 87.84487  ?  54  GLY D CA  1 
ATOM   5540 C  C   . GLY D 1 54  ? 15.36000  37.63500  89.97100  1.000 95.88140  ?  54  GLY D C   1 
ATOM   5541 O  O   . GLY D 1 54  ? 14.31800  38.05800  90.47600  1.000 94.19116  ?  54  GLY D O   1 
ATOM   5542 N  N   . LEU D 1 55  ? 15.40100  37.11300  88.74800  1.000 97.68818  ?  55  LEU D N   1 
ATOM   5543 C  CA  . LEU D 1 55  ? 14.21600  37.02900  87.90800  1.000 95.35357  ?  55  LEU D CA  1 
ATOM   5544 C  C   . LEU D 1 55  ? 13.41500  35.77500  88.23300  1.000 97.34350  ?  55  LEU D C   1 
ATOM   5545 O  O   . LEU D 1 55  ? 13.97700  34.70900  88.49400  1.000 97.74019  ?  55  LEU D O   1 
ATOM   5546 C  CB  . LEU D 1 55  ? 14.60200  37.04900  86.43000  1.000 93.23300  ?  55  LEU D CB  1 
ATOM   5547 C  CG  . LEU D 1 55  ? 15.03400  38.41800  85.89600  1.000 96.32606  ?  55  LEU D CG  1 
ATOM   5548 C  CD1 . LEU D 1 55  ? 15.62800  38.29300  84.50500  1.000 93.65430  ?  55  LEU D CD1 1 
ATOM   5549 C  CD2 . LEU D 1 55  ? 13.86600  39.38500  85.89400  1.000 96.66964  ?  55  LEU D CD2 1 
ATOM   5550 N  N   . GLU D 1 56  ? 12.09900  35.91100  88.21200  1.000 96.87375  ?  56  GLU D N   1 
ATOM   5551 C  CA  . GLU D 1 56  ? 11.16900  34.87200  88.62800  1.000 99.40157  ?  56  GLU D CA  1 
ATOM   5552 C  C   . GLU D 1 56  ? 10.89100  33.91200  87.46800  1.000 99.62853  ?  56  GLU D C   1 
ATOM   5553 O  O   . GLU D 1 56  ? 11.04400  34.28600  86.30400  1.000 101.90401 ?  56  GLU D O   1 
ATOM   5554 C  CB  . GLU D 1 56  ? 9.87400   35.53400  89.08000  1.000 104.87180 ?  56  GLU D CB  1 
ATOM   5555 C  CG  . GLU D 1 56  ? 9.18200   36.25300  87.93200  1.000 104.43121 ?  56  GLU D CG  1 
ATOM   5556 C  CD  . GLU D 1 56  ? 8.09800   37.21200  88.37000  1.000 117.50180 ?  56  GLU D CD  1 
ATOM   5557 O  OE1 . GLU D 1 56  ? 7.80700   37.28400  89.58300  1.000 129.41507 ?  56  GLU D OE1 1 
ATOM   5558 O  OE2 . GLU D 1 56  ? 7.54900   37.90400  87.48700  1.000 113.71177 -1 56  GLU D OE2 1 
ATOM   5559 N  N   . PRO D 1 57  ? 10.50900  32.66300  87.75200  1.000 97.67041  ?  57  PRO D N   1 
ATOM   5560 C  CA  . PRO D 1 57  ? 10.22300  31.70800  86.66500  1.000 96.84102  ?  57  PRO D CA  1 
ATOM   5561 C  C   . PRO D 1 57  ? 9.12800   32.24200  85.76700  1.000 102.22835 ?  57  PRO D C   1 
ATOM   5562 O  O   . PRO D 1 57  ? 8.01600   32.52400  86.22100  1.000 99.26551  ?  57  PRO D O   1 
ATOM   5563 C  CB  . PRO D 1 57  ? 9.72000   30.45700  87.39100  1.000 94.05027  ?  57  PRO D CB  1 
ATOM   5564 C  CG  . PRO D 1 57  ? 10.07100  30.60700  88.76300  1.000 95.89306  ?  57  PRO D CG  1 
ATOM   5565 C  CD  . PRO D 1 57  ? 10.09400  32.11800  89.05000  1.000 102.25941 ?  57  PRO D CD  1 
ATOM   5566 N  N   . GLY D 1 58  ? 9.42300   32.34700  84.48800  1.000 96.51632  ?  58  GLY D N   1 
ATOM   5567 C  CA  . GLY D 1 58  ? 8.43000   32.71500  83.50800  1.000 91.40229  ?  58  GLY D CA  1 
ATOM   5568 C  C   . GLY D 1 58  ? 8.73800   33.98800  82.77600  1.000 99.95039  ?  58  GLY D C   1 
ATOM   5569 O  O   . GLY D 1 58  ? 8.13400   34.24200  81.72700  1.000 103.53469 ?  58  GLY D O   1 
ATOM   5570 N  N   . GLU D 1 59  ? 9.65700   34.80400  83.28700  1.000 98.07195  ?  59  GLU D N   1 
ATOM   5571 C  CA  . GLU D 1 59  ? 10.02800  36.03900  82.61200  1.000 97.39568  ?  59  GLU D CA  1 
ATOM   5572 C  C   . GLU D 1 59  ? 11.39300  35.96000  81.93300  1.000 90.70546  ?  59  GLU D C   1 
ATOM   5573 O  O   . GLU D 1 59  ? 11.97800  36.99800  81.61300  1.000 88.34127  ?  59  GLU D O   1 
ATOM   5574 C  CB  . GLU D 1 59  ? 9.95600   37.22600  83.57600  1.000 100.40934 ?  59  GLU D CB  1 
ATOM   5575 C  CG  . GLU D 1 59  ? 10.81700  37.14800  84.81900  1.000 104.83695 ?  59  GLU D CG  1 
ATOM   5576 C  CD  . GLU D 1 59  ? 10.58000  38.33300  85.74300  1.000 109.67846 ?  59  GLU D CD  1 
ATOM   5577 O  OE1 . GLU D 1 59  ? 9.81200   39.24200  85.36100  1.000 113.17657 ?  59  GLU D OE1 1 
ATOM   5578 O  OE2 . GLU D 1 59  ? 11.15300  38.35400  86.85200  1.000 102.86494 -1 59  GLU D OE2 1 
ATOM   5579 N  N   . LEU D 1 60  ? 11.91000  34.75300  81.70000  1.000 87.47738  ?  60  LEU D N   1 
ATOM   5580 C  CA  . LEU D 1 60  ? 13.19700  34.55800  81.03800  1.000 78.62238  ?  60  LEU D CA  1 
ATOM   5581 C  C   . LEU D 1 60  ? 13.06300  33.53000  79.92600  1.000 82.43144  ?  60  LEU D C   1 
ATOM   5582 O  O   . LEU D 1 60  ? 12.68600  32.38000  80.17500  1.000 80.12431  ?  60  LEU D O   1 
ATOM   5583 C  CB  . LEU D 1 60  ? 14.28700  34.11300  82.02000  1.000 77.27243  ?  60  LEU D CB  1 
ATOM   5584 C  CG  . LEU D 1 60  ? 15.30000  35.17800  82.42900  1.000 80.71066  ?  60  LEU D CG  1 
ATOM   5585 C  CD1 . LEU D 1 60  ? 16.47800  34.53700  83.14300  1.000 76.95976  ?  60  LEU D CD1 1 
ATOM   5586 C  CD2 . LEU D 1 60  ? 15.77200  35.93700  81.19900  1.000 79.94764  ?  60  LEU D CD2 1 
ATOM   5587 N  N   . PHE D 1 61  ? 13.36400  33.95500  78.70100  1.000 80.22837  ?  61  PHE D N   1 
ATOM   5588 C  CA  . PHE D 1 61  ? 13.63300  33.04900  77.59500  1.000 75.08475  ?  61  PHE D CA  1 
ATOM   5589 C  C   . PHE D 1 61  ? 15.13900  32.83300  77.51200  1.000 72.86081  ?  61  PHE D C   1 
ATOM   5590 O  O   . PHE D 1 61  ? 15.90600  33.79900  77.43800  1.000 74.00961  ?  61  PHE D O   1 
ATOM   5591 C  CB  . PHE D 1 61  ? 13.09100  33.62800  76.28800  1.000 77.56708  ?  61  PHE D CB  1 
ATOM   5592 C  CG  . PHE D 1 61  ? 12.55900  32.59400  75.34400  1.000 76.14378  ?  61  PHE D CG  1 
ATOM   5593 C  CD1 . PHE D 1 61  ? 11.54700  31.73700  75.73800  1.000 76.44677  ?  61  PHE D CD1 1 
ATOM   5594 C  CD2 . PHE D 1 61  ? 13.05800  32.49000  74.05600  1.000 75.04184  ?  61  PHE D CD2 1 
ATOM   5595 C  CE1 . PHE D 1 61  ? 11.04900  30.78600  74.87200  1.000 74.85110  ?  61  PHE D CE1 1 
ATOM   5596 C  CE2 . PHE D 1 61  ? 12.56400  31.54100  73.18400  1.000 73.80410  ?  61  PHE D CE2 1 
ATOM   5597 C  CZ  . PHE D 1 61  ? 11.55700  30.68900  73.59200  1.000 75.63950  ?  61  PHE D CZ  1 
ATOM   5598 N  N   . VAL D 1 62  ? 15.56600  31.57300  77.54800  1.000 69.16473  ?  62  VAL D N   1 
ATOM   5599 C  CA  . VAL D 1 62  ? 16.97200  31.23000  77.73900  1.000 68.73296  ?  62  VAL D CA  1 
ATOM   5600 C  C   . VAL D 1 62  ? 17.45100  30.34000  76.60100  1.000 72.59134  ?  62  VAL D C   1 
ATOM   5601 O  O   . VAL D 1 62  ? 16.78200  29.36700  76.23700  1.000 74.58572  ?  62  VAL D O   1 
ATOM   5602 C  CB  . VAL D 1 62  ? 17.21300  30.54400  79.09500  1.000 67.66639  ?  62  VAL D CB  1 
ATOM   5603 C  CG1 . VAL D 1 62  ? 18.68600  30.19400  79.25300  1.000 62.51103  ?  62  VAL D CG1 1 
ATOM   5604 C  CG2 . VAL D 1 62  ? 16.75500  31.44400  80.23000  1.000 77.14743  ?  62  VAL D CG2 1 
ATOM   5605 N  N   . HIS D 1 63  ? 18.60400  30.68900  76.03600  1.000 64.09432  ?  63  HIS D N   1 
ATOM   5606 C  CA  . HIS D 1 63  ? 19.36300  29.83100  75.13900  1.000 61.86359  ?  63  HIS D CA  1 
ATOM   5607 C  C   . HIS D 1 63  ? 20.78900  29.76200  75.66300  1.000 62.06970  ?  63  HIS D C   1 
ATOM   5608 O  O   . HIS D 1 63  ? 21.32700  30.76600  76.13700  1.000 66.86505  ?  63  HIS D O   1 
ATOM   5609 C  CB  . HIS D 1 63  ? 19.35000  30.35900  73.69600  1.000 70.16573  ?  63  HIS D CB  1 
ATOM   5610 C  CG  . HIS D 1 63  ? 20.33700  29.68300  72.79400  1.000 65.00862  ?  63  HIS D CG  1 
ATOM   5611 N  ND1 . HIS D 1 63  ? 20.19000  28.38000  72.37000  1.000 66.89408  ?  63  HIS D ND1 1 
ATOM   5612 C  CD2 . HIS D 1 63  ? 21.48900  30.13100  72.23900  1.000 60.38080  ?  63  HIS D CD2 1 
ATOM   5613 C  CE1 . HIS D 1 63  ? 21.20700  28.05500  71.59100  1.000 64.35265  ?  63  HIS D CE1 1 
ATOM   5614 N  NE2 . HIS D 1 63  ? 22.01000  29.09900  71.49700  1.000 55.45409  ?  63  HIS D NE2 1 
ATOM   5615 N  N   . ARG D 1 64  ? 21.39500  28.57800  75.59600  1.000 59.70819  ?  64  ARG D N   1 
ATOM   5616 C  CA  . ARG D 1 64  ? 22.75800  28.39900  76.08500  1.000 61.82130  ?  64  ARG D CA  1 
ATOM   5617 C  C   . ARG D 1 64  ? 23.54100  27.49100  75.15100  1.000 61.76182  ?  64  ARG D C   1 
ATOM   5618 O  O   . ARG D 1 64  ? 23.06600  26.41400  74.78300  1.000 67.31462  ?  64  ARG D O   1 
ATOM   5619 C  CB  . ARG D 1 64  ? 22.78300  27.81900  77.50500  1.000 65.42322  ?  64  ARG D CB  1 
ATOM   5620 C  CG  . ARG D 1 64  ? 22.30600  28.78000  78.58000  1.000 67.66795  ?  64  ARG D CG  1 
ATOM   5621 C  CD  . ARG D 1 64  ? 22.39400  28.16900  79.97000  1.000 65.71292  ?  64  ARG D CD  1 
ATOM   5622 N  NE  . ARG D 1 64  ? 21.96500  29.11800  80.99000  1.000 64.05195  ?  64  ARG D NE  1 
ATOM   5623 C  CZ  . ARG D 1 64  ? 22.74900  30.03800  81.53900  1.000 69.51895  ?  64  ARG D CZ  1 
ATOM   5624 N  NH1 . ARG D 1 64  ? 24.02700  30.14300  81.21200  1.000 68.42201  ?  64  ARG D NH1 1 
ATOM   5625 N  NH2 . ARG D 1 64  ? 22.23700  30.87200  82.43900  1.000 79.03253  ?  64  ARG D NH2 1 
ATOM   5626 N  N   . ASN D 1 65  ? 24.73500  27.93700  74.76500  1.000 59.26869  ?  65  ASN D N   1 
ATOM   5627 C  CA  . ASN D 1 65  ? 25.67300  27.12200  74.00700  1.000 61.92137  ?  65  ASN D CA  1 
ATOM   5628 C  C   . ASN D 1 65  ? 27.06500  27.34500  74.58300  1.000 61.54551  ?  65  ASN D C   1 
ATOM   5629 O  O   . ASN D 1 65  ? 27.25700  28.14900  75.50100  1.000 64.94780  ?  65  ASN D O   1 
ATOM   5630 C  CB  . ASN D 1 65  ? 25.61400  27.44300  72.50700  1.000 65.28163  ?  65  ASN D CB  1 
ATOM   5631 C  CG  . ASN D 1 65  ? 25.91900  28.89900  72.20300  1.000 62.66150  ?  65  ASN D CG  1 
ATOM   5632 O  OD1 . ASN D 1 65  ? 27.03600  29.37400  72.41400  1.000 61.34249  ?  65  ASN D OD1 1 
ATOM   5633 N  ND2 . ASN D 1 65  ? 24.92000  29.61800  71.70400  1.000 59.23115  ?  65  ASN D ND2 1 
ATOM   5634 N  N   . VAL D 1 66  ? 28.04400  26.61900  74.04700  1.000 55.99072  ?  66  VAL D N   1 
ATOM   5635 C  CA  . VAL D 1 66  ? 29.41000  26.72300  74.54700  1.000 56.46024  ?  66  VAL D CA  1 
ATOM   5636 C  C   . VAL D 1 66  ? 29.94400  28.11300  74.22100  1.000 64.96301  ?  66  VAL D C   1 
ATOM   5637 O  O   . VAL D 1 66  ? 30.00900  28.50800  73.05000  1.000 71.91434  ?  66  VAL D O   1 
ATOM   5638 C  CB  . VAL D 1 66  ? 30.30000  25.62700  73.94800  1.000 58.42476  ?  66  VAL D CB  1 
ATOM   5639 C  CG1 . VAL D 1 66  ? 31.69500  25.67900  74.55900  1.000 58.63972  ?  66  VAL D CG1 1 
ATOM   5640 C  CG2 . VAL D 1 66  ? 29.66900  24.25600  74.14900  1.000 62.45957  ?  66  VAL D CG2 1 
ATOM   5641 N  N   . ALA D 1 67  ? 30.29900  28.86900  75.26400  1.000 58.52241  ?  67  ALA D N   1 
ATOM   5642 C  CA  . ALA D 1 67  ? 30.90800  30.19500  75.14500  1.000 59.60127  ?  67  ALA D CA  1 
ATOM   5643 C  C   . ALA D 1 67  ? 29.94800  31.24000  74.57400  1.000 63.68288  ?  67  ALA D C   1 
ATOM   5644 O  O   . ALA D 1 67  ? 30.38900  32.21800  73.96600  1.000 68.24145  ?  67  ALA D O   1 
ATOM   5645 C  CB  . ALA D 1 67  ? 32.19800  30.15200  74.31800  1.000 61.20482  ?  67  ALA D CB  1 
ATOM   5646 N  N   . ASN D 1 68  ? 28.64500  31.03900  74.77200  1.000 64.42485  ?  68  ASN D N   1 
ATOM   5647 C  CA  . ASN D 1 68  ? 27.58100  32.00600  74.46100  1.000 65.83678  ?  68  ASN D CA  1 
ATOM   5648 C  C   . ASN D 1 68  ? 27.79200  32.69100  73.10700  1.000 71.00968  ?  68  ASN D C   1 
ATOM   5649 O  O   . ASN D 1 68  ? 27.96400  33.90700  73.01100  1.000 73.30680  ?  68  ASN D O   1 
ATOM   5650 C  CB  . ASN D 1 68  ? 27.43000  33.04600  75.57800  1.000 70.15732  ?  68  ASN D CB  1 
ATOM   5651 C  CG  . ASN D 1 68  ? 28.73400  33.75500  75.91500  1.000 69.01968  ?  68  ASN D CG  1 
ATOM   5652 O  OD1 . ASN D 1 68  ? 29.48000  33.32600  76.79500  1.000 62.84862  ?  68  ASN D OD1 1 
ATOM   5653 N  ND2 . ASN D 1 68  ? 29.01000  34.84700  75.21200  1.000 70.53286  ?  68  ASN D ND2 1 
ATOM   5654 N  N   . LEU D 1 69  ? 27.76600  31.88500  72.04900  1.000 72.12794  ?  69  LEU D N   1 
ATOM   5655 C  CA  . LEU D 1 69  ? 28.01400  32.37900  70.70100  1.000 72.16767  ?  69  LEU D CA  1 
ATOM   5656 C  C   . LEU D 1 69  ? 26.72100  32.71300  69.96200  1.000 66.92704  ?  69  LEU D C   1 
ATOM   5657 O  O   . LEU D 1 69  ? 25.66700  32.11400  70.19800  1.000 61.48716  ?  69  LEU D O   1 
ATOM   5658 C  CB  . LEU D 1 69  ? 28.81500  31.36000  69.88900  1.000 68.22104  ?  69  LEU D CB  1 
ATOM   5659 C  CG  . LEU D 1 69  ? 30.25700  31.11700  70.33300  1.000 69.61109  ?  69  LEU D CG  1 
ATOM   5660 C  CD1 . LEU D 1 69  ? 30.98800  30.27000  69.30400  1.000 71.51520  ?  69  LEU D CD1 1 
ATOM   5661 C  CD2 . LEU D 1 69  ? 30.97500  32.43800  70.54900  1.000 72.91414  ?  69  LEU D CD2 1 
ATOM   5662 N  N   . VAL D 1 70  ? 26.81700  33.69900  69.06900  1.000 73.53597  ?  70  VAL D N   1 
ATOM   5663 C  CA  . VAL D 1 70  ? 25.74800  34.04000  68.12800  1.000 76.82759  ?  70  VAL D CA  1 
ATOM   5664 C  C   . VAL D 1 70  ? 26.36900  34.00800  66.73300  1.000 70.41920  ?  70  VAL D C   1 
ATOM   5665 O  O   . VAL D 1 70  ? 26.87200  35.02000  66.23400  1.000 70.83939  ?  70  VAL D O   1 
ATOM   5666 C  CB  . VAL D 1 70  ? 25.10300  35.39900  68.41900  1.000 75.24503  ?  70  VAL D CB  1 
ATOM   5667 C  CG1 . VAL D 1 70  ? 24.00800  35.68900  67.40200  1.000 66.99109  ?  70  VAL D CG1 1 
ATOM   5668 C  CG2 . VAL D 1 70  ? 24.52200  35.41200  69.82100  1.000 76.93917  ?  70  VAL D CG2 1 
ATOM   5669 N  N   . ILE D 1 71  ? 26.37100  32.83400  66.11300  1.000 70.10403  ?  71  ILE D N   1 
ATOM   5670 C  CA  . ILE D 1 71  ? 26.94400  32.66100  64.78300  1.000 74.90360  ?  71  ILE D CA  1 
ATOM   5671 C  C   . ILE D 1 71  ? 25.90900  33.04700  63.73300  1.000 71.58260  ?  71  ILE D C   1 
ATOM   5672 O  O   . ILE D 1 71  ? 24.71900  32.73900  63.87000  1.000 68.25561  ?  71  ILE D O   1 
ATOM   5673 C  CB  . ILE D 1 71  ? 27.43000  31.21100  64.60900  1.000 75.96281  ?  71  ILE D CB  1 
ATOM   5674 C  CG1 . ILE D 1 71  ? 28.46000  30.88500  65.69300  1.000 73.03319  ?  71  ILE D CG1 1 
ATOM   5675 C  CG2 . ILE D 1 71  ? 28.02900  31.00000  63.22800  1.000 76.35919  ?  71  ILE D CG2 1 
ATOM   5676 C  CD1 . ILE D 1 71  ? 28.70900  29.40800  65.88500  1.000 75.53892  ?  71  ILE D CD1 1 
ATOM   5677 N  N   . HIS D 1 72  ? 26.36200  33.73700  62.67700  1.000 73.75558  ?  72  HIS D N   1 
ATOM   5678 C  CA  . HIS D 1 72  ? 25.44700  34.22800  61.64700  1.000 73.33540  ?  72  HIS D CA  1 
ATOM   5679 C  C   . HIS D 1 72  ? 24.61600  33.11000  61.02900  1.000 77.02452  ?  72  HIS D C   1 
ATOM   5680 O  O   . HIS D 1 72  ? 23.49600  33.35600  60.56800  1.000 81.60371  ?  72  HIS D O   1 
ATOM   5681 C  CB  . HIS D 1 72  ? 26.21400  34.95600  60.54200  1.000 71.41170  ?  72  HIS D CB  1 
ATOM   5682 C  CG  . HIS D 1 72  ? 27.14700  36.01300  61.04200  1.000 71.80108  ?  72  HIS D CG  1 
ATOM   5683 N  ND1 . HIS D 1 72  ? 26.71500  37.12400  61.73200  1.000 67.96253  ?  72  HIS D ND1 1 
ATOM   5684 C  CD2 . HIS D 1 72  ? 28.49000  36.14100  60.92500  1.000 70.42330  ?  72  HIS D CD2 1 
ATOM   5685 C  CE1 . HIS D 1 72  ? 27.75300  37.88400  62.03300  1.000 70.74965  ?  72  HIS D CE1 1 
ATOM   5686 N  NE2 . HIS D 1 72  ? 28.84200  37.31000  61.55400  1.000 69.05557  ?  72  HIS D NE2 1 
ATOM   5687 N  N   . THR D 1 73  ? 25.14500  31.88600  60.99500  1.000 74.76076  ?  73  THR D N   1 
ATOM   5688 C  CA  . THR D 1 73  ? 24.51100  30.79100  60.27100  1.000 76.31654  ?  73  THR D CA  1 
ATOM   5689 C  C   . THR D 1 73  ? 24.07800  29.65200  61.18800  1.000 76.35608  ?  73  THR D C   1 
ATOM   5690 O  O   . THR D 1 73  ? 23.89100  28.52300  60.72100  1.000 79.94922  ?  73  THR D O   1 
ATOM   5691 C  CB  . THR D 1 73  ? 25.44400  30.26700  59.17800  1.000 80.43695  ?  73  THR D CB  1 
ATOM   5692 O  OG1 . THR D 1 73  ? 26.76300  30.09800  59.71400  1.000 74.28179  ?  73  THR D OG1 1 
ATOM   5693 C  CG2 . THR D 1 73  ? 25.49000  31.24200  58.01300  1.000 79.74459  ?  73  THR D CG2 1 
ATOM   5694 N  N   . ASP D 1 74  ? 23.90700  29.92100  62.48100  1.000 81.30181  ?  74  ASP D N   1 
ATOM   5695 C  CA  . ASP D 1 74  ? 23.42500  28.91600  63.42700  1.000 79.65358  ?  74  ASP D CA  1 
ATOM   5696 C  C   . ASP D 1 74  ? 21.91200  29.04800  63.52600  1.000 77.64619  ?  74  ASP D C   1 
ATOM   5697 O  O   . ASP D 1 74  ? 21.39800  29.94600  64.19700  1.000 72.08940  ?  74  ASP D O   1 
ATOM   5698 C  CB  . ASP D 1 74  ? 24.07900  29.08800  64.79200  1.000 75.04439  ?  74  ASP D CB  1 
ATOM   5699 C  CG  . ASP D 1 74  ? 23.48100  28.17100  65.84100  1.000 79.89452  ?  74  ASP D CG  1 
ATOM   5700 O  OD1 . ASP D 1 74  ? 22.99600  27.07900  65.46900  1.000 77.82217  ?  74  ASP D OD1 1 
ATOM   5701 O  OD2 . ASP D 1 74  ? 23.48000  28.54600  67.03200  1.000 83.31918  -1 74  ASP D OD2 1 
ATOM   5702 N  N   . LEU D 1 75  ? 21.19000  28.14200  62.86300  1.000 78.82582  ?  75  LEU D N   1 
ATOM   5703 C  CA  . LEU D 1 75  ? 19.73500  28.23300  62.86200  1.000 78.37950  ?  75  LEU D CA  1 
ATOM   5704 C  C   . LEU D 1 75  ? 19.15300  28.00900  64.25400  1.000 73.71143  ?  75  LEU D C   1 
ATOM   5705 O  O   . LEU D 1 75  ? 18.05200  28.49200  64.54400  1.000 70.75403  ?  75  LEU D O   1 
ATOM   5706 C  CB  . LEU D 1 75  ? 19.14500  27.24300  61.85900  1.000 70.06253  ?  75  LEU D CB  1 
ATOM   5707 C  CG  . LEU D 1 75  ? 17.75100  27.62100  61.35700  1.000 70.51836  ?  75  LEU D CG  1 
ATOM   5708 C  CD1 . LEU D 1 75  ? 17.68400  29.11100  61.06400  1.000 64.83480  ?  75  LEU D CD1 1 
ATOM   5709 C  CD2 . LEU D 1 75  ? 17.39800  26.83200  60.11300  1.000 74.26324  ?  75  LEU D CD2 1 
ATOM   5710 N  N   . ASN D 1 76  ? 19.85900  27.27400  65.11800  1.000 72.43645  ?  76  ASN D N   1 
ATOM   5711 C  CA  . ASN D 1 76  ? 19.44800  27.10400  66.51000  1.000 75.53425  ?  76  ASN D CA  1 
ATOM   5712 C  C   . ASN D 1 76  ? 19.28000  28.45000  67.20300  1.000 73.77411  ?  76  ASN D C   1 
ATOM   5713 O  O   . ASN D 1 76  ? 18.16300  28.83700  67.56300  1.000 71.58182  ?  76  ASN D O   1 
ATOM   5714 C  CB  . ASN D 1 76  ? 20.46600  26.25500  67.28000  1.000 75.08744  ?  76  ASN D CB  1 
ATOM   5715 C  CG  . ASN D 1 76  ? 19.98900  25.88000  68.68500  1.000 71.93860  ?  76  ASN D CG  1 
ATOM   5716 O  OD1 . ASN D 1 76  ? 19.32800  26.66300  69.37000  1.000 68.61862  ?  76  ASN D OD1 1 
ATOM   5717 N  ND2 . ASN D 1 76  ? 20.34800  24.68000  69.12500  1.000 70.72850  ?  76  ASN D ND2 1 
ATOM   5718 N  N   . CYS D 1 77  ? 20.39400  29.15600  67.40900  1.000 70.36021  ?  77  CYS D N   1 
ATOM   5719 C  CA  . CYS D 1 77  ? 20.34400  30.44100  68.09900  1.000 69.00450  ?  77  CYS D CA  1 
ATOM   5720 C  C   . CYS D 1 77  ? 19.42700  31.42500  67.38300  1.000 71.30929  ?  77  CYS D C   1 
ATOM   5721 O  O   . CYS D 1 77  ? 18.68300  32.17100  68.03000  1.000 71.59674  ?  77  CYS D O   1 
ATOM   5722 C  CB  . CYS D 1 77  ? 21.75200  31.02300  68.22700  1.000 72.12790  ?  77  CYS D CB  1 
ATOM   5723 S  SG  . CYS D 1 77  ? 21.82400  32.61300  69.08700  1.000 92.00922  ?  77  CYS D SG  1 
ATOM   5724 N  N   . LEU D 1 78  ? 19.45900  31.43500  66.04900  1.000 76.29443  ?  78  LEU D N   1 
ATOM   5725 C  CA  . LEU D 1 78  ? 18.65600  32.39700  65.30000  1.000 70.95893  ?  78  LEU D CA  1 
ATOM   5726 C  C   . LEU D 1 78  ? 17.16300  32.13000  65.45900  1.000 72.48141  ?  78  LEU D C   1 
ATOM   5727 O  O   . LEU D 1 78  ? 16.36600  33.07200  65.54100  1.000 71.61106  ?  78  LEU D O   1 
ATOM   5728 C  CB  . LEU D 1 78  ? 19.04800  32.36200  63.82500  1.000 74.10678  ?  78  LEU D CB  1 
ATOM   5729 C  CG  . LEU D 1 78  ? 20.45000  32.85200  63.46800  1.000 75.92314  ?  78  LEU D CG  1 
ATOM   5730 C  CD1 . LEU D 1 78  ? 20.74000  32.57100  62.00600  1.000 74.00463  ?  78  LEU D CD1 1 
ATOM   5731 C  CD2 . LEU D 1 78  ? 20.59700  34.33300  63.77400  1.000 68.24912  ?  78  LEU D CD2 1 
ATOM   5732 N  N   . SER D 1 79  ? 16.76500  30.85600  65.51700  1.000 72.20096  ?  79  SER D N   1 
ATOM   5733 C  CA  . SER D 1 79  ? 15.35100  30.53500  65.69600  1.000 70.48847  ?  79  SER D CA  1 
ATOM   5734 C  C   . SER D 1 79  ? 14.85100  30.96200  67.07000  1.000 71.55524  ?  79  SER D C   1 
ATOM   5735 O  O   . SER D 1 79  ? 13.71400  31.43200  67.20200  1.000 73.44817  ?  79  SER D O   1 
ATOM   5736 C  CB  . SER D 1 79  ? 15.11500  29.04400  65.47000  1.000 70.90618  ?  79  SER D CB  1 
ATOM   5737 O  OG  . SER D 1 79  ? 15.43000  28.68400  64.13400  1.000 74.25055  ?  79  SER D OG  1 
ATOM   5738 N  N   . VAL D 1 80  ? 15.67500  30.79000  68.10600  1.000 77.94904  ?  80  VAL D N   1 
ATOM   5739 C  CA  . VAL D 1 80  ? 15.30400  31.27200  69.43500  1.000 68.90741  ?  80  VAL D CA  1 
ATOM   5740 C  C   . VAL D 1 80  ? 15.10100  32.78000  69.40500  1.000 68.35407  ?  80  VAL D C   1 
ATOM   5741 O  O   . VAL D 1 80  ? 14.08300  33.30000  69.88000  1.000 67.63583  ?  80  VAL D O   1 
ATOM   5742 C  CB  . VAL D 1 80  ? 16.36500  30.86900  70.47500  1.000 63.88569  ?  80  VAL D CB  1 
ATOM   5743 C  CG1 . VAL D 1 80  ? 16.01400  31.45100  71.83900  1.000 68.10939  ?  80  VAL D CG1 1 
ATOM   5744 C  CG2 . VAL D 1 80  ? 16.49400  29.35600  70.54900  1.000 64.86132  ?  80  VAL D CG2 1 
ATOM   5745 N  N   . VAL D 1 81  ? 16.07100  33.50400  68.84000  1.000 69.32546  ?  81  VAL D N   1 
ATOM   5746 C  CA  . VAL D 1 81  ? 15.99400  34.96100  68.78800  1.000 68.79224  ?  81  VAL D CA  1 
ATOM   5747 C  C   . VAL D 1 81  ? 14.78200  35.40700  67.97900  1.000 70.19050  ?  81  VAL D C   1 
ATOM   5748 O  O   . VAL D 1 81  ? 14.05800  36.32700  68.37700  1.000 71.78062  ?  81  VAL D O   1 
ATOM   5749 C  CB  . VAL D 1 81  ? 17.30300  35.54500  68.22300  1.000 67.82437  ?  81  VAL D CB  1 
ATOM   5750 C  CG1 . VAL D 1 81  ? 17.20900  37.05900  68.12100  1.000 70.19147  ?  81  VAL D CG1 1 
ATOM   5751 C  CG2 . VAL D 1 81  ? 18.48100  35.13800  69.09200  1.000 57.72589  ?  81  VAL D CG2 1 
ATOM   5752 N  N   . GLN D 1 82  ? 14.54000  34.76700  66.83100  1.000 67.20378  ?  82  GLN D N   1 
ATOM   5753 C  CA  . GLN D 1 82  ? 13.40000  35.15500  66.00600  1.000 67.69636  ?  82  GLN D CA  1 
ATOM   5754 C  C   . GLN D 1 82  ? 12.08900  34.88400  66.73300  1.000 67.70469  ?  82  GLN D C   1 
ATOM   5755 O  O   . GLN D 1 82  ? 11.15800  35.69600  66.67500  1.000 66.02221  ?  82  GLN D O   1 
ATOM   5756 C  CB  . GLN D 1 82  ? 13.44200  34.43200  64.65800  1.000 62.78641  ?  82  GLN D CB  1 
ATOM   5757 C  CG  . GLN D 1 82  ? 12.50900  35.03300  63.60700  1.000 57.58536  ?  82  GLN D CG  1 
ATOM   5758 C  CD  . GLN D 1 82  ? 11.12800  34.40200  63.58600  1.000 57.97082  ?  82  GLN D CD  1 
ATOM   5759 O  OE1 . GLN D 1 82  ? 10.97000  33.21700  63.87700  1.000 60.70125  ?  82  GLN D OE1 1 
ATOM   5760 N  NE2 . GLN D 1 82  ? 10.11700  35.19900  63.25800  1.000 54.89443  ?  82  GLN D NE2 1 
ATOM   5761 N  N   . TYR D 1 83  ? 11.99100  33.74100  67.41600  1.000 71.29155  ?  83  TYR D N   1 
ATOM   5762 C  CA  . TYR D 1 83  ? 10.79100  33.45600  68.19400  1.000 75.54112  ?  83  TYR D CA  1 
ATOM   5763 C  C   . TYR D 1 83  ? 10.63000  34.45900  69.33300  1.000 76.45742  ?  83  TYR D C   1 
ATOM   5764 O  O   . TYR D 1 83  ? 9.51300   34.89100  69.63900  1.000 76.08519  ?  83  TYR D O   1 
ATOM   5765 C  CB  . TYR D 1 83  ? 10.83300  32.02600  68.73400  1.000 69.56226  ?  83  TYR D CB  1 
ATOM   5766 C  CG  . TYR D 1 83  ? 9.53800   31.59600  69.38400  1.000 70.92125  ?  83  TYR D CG  1 
ATOM   5767 C  CD1 . TYR D 1 83  ? 8.39300   31.41200  68.62000  1.000 72.96608  ?  83  TYR D CD1 1 
ATOM   5768 C  CD2 . TYR D 1 83  ? 9.45400   31.37000  70.75200  1.000 68.95453  ?  83  TYR D CD2 1 
ATOM   5769 C  CE1 . TYR D 1 83  ? 7.20100   31.02000  69.19400  1.000 73.53113  ?  83  TYR D CE1 1 
ATOM   5770 C  CE2 . TYR D 1 83  ? 8.26000   30.97600  71.33800  1.000 69.26982  ?  83  TYR D CE2 1 
ATOM   5771 C  CZ  . TYR D 1 83  ? 7.13800   30.80300  70.55200  1.000 64.70337  ?  83  TYR D CZ  1 
ATOM   5772 O  OH  . TYR D 1 83  ? 5.94700   30.41100  71.11900  1.000 61.51706  ?  83  TYR D OH  1 
ATOM   5773 N  N   . ALA D 1 84  ? 11.73500  34.82700  69.98500  1.000 68.94534  ?  84  ALA D N   1 
ATOM   5774 C  CA  . ALA D 1 84  ? 11.66600  35.81200  71.06000  1.000 71.06828  ?  84  ALA D CA  1 
ATOM   5775 C  C   . ALA D 1 84  ? 11.26700  37.18700  70.53500  1.000 76.71732  ?  84  ALA D C   1 
ATOM   5776 O  O   . ALA D 1 84  ? 10.33300  37.81200  71.05000  1.000 78.30847  ?  84  ALA D O   1 
ATOM   5777 C  CB  . ALA D 1 84  ? 13.01000  35.88500  71.78500  1.000 71.98724  ?  84  ALA D CB  1 
ATOM   5778 N  N   . VAL D 1 85  ? 11.94800  37.66400  69.49100  1.000 76.65827  ?  85  VAL D N   1 
ATOM   5779 C  CA  . VAL D 1 85  ? 11.75300  39.04000  69.04200  1.000 76.17694  ?  85  VAL D CA  1 
ATOM   5780 C  C   . VAL D 1 85  ? 10.43000  39.19200  68.30100  1.000 82.11433  ?  85  VAL D C   1 
ATOM   5781 O  O   . VAL D 1 85  ? 9.70200   40.17200  68.50000  1.000 82.83106  ?  85  VAL D O   1 
ATOM   5782 C  CB  . VAL D 1 85  ? 12.94500  39.49000  68.17600  1.000 76.02754  ?  85  VAL D CB  1 
ATOM   5783 C  CG1 . VAL D 1 85  ? 12.69400  40.87400  67.59600  1.000 83.32405  ?  85  VAL D CG1 1 
ATOM   5784 C  CG2 . VAL D 1 85  ? 14.22300  39.48300  68.99600  1.000 78.86438  ?  85  VAL D CG2 1 
ATOM   5785 N  N   . ASP D 1 86  ? 10.09200  38.23400  67.43800  1.000 79.53915  ?  86  ASP D N   1 
ATOM   5786 C  CA  . ASP D 1 86  ? 8.92100   38.38900  66.58600  1.000 77.08816  ?  86  ASP D CA  1 
ATOM   5787 C  C   . ASP D 1 86  ? 7.64200   37.83700  67.20400  1.000 77.28972  ?  86  ASP D C   1 
ATOM   5788 O  O   . ASP D 1 86  ? 6.56100   38.38400  66.95300  1.000 81.11418  ?  86  ASP D O   1 
ATOM   5789 C  CB  . ASP D 1 86  ? 9.16100   37.70600  65.23700  1.000 83.24842  ?  86  ASP D CB  1 
ATOM   5790 C  CG  . ASP D 1 86  ? 10.30900  38.32800  64.46600  1.000 85.47522  ?  86  ASP D CG  1 
ATOM   5791 O  OD1 . ASP D 1 86  ? 10.85700  39.34900  64.93300  1.000 88.18868  ?  86  ASP D OD1 1 
ATOM   5792 O  OD2 . ASP D 1 86  ? 10.66000  37.79600  63.39000  1.000 83.52787  -1 86  ASP D OD2 1 
ATOM   5793 N  N   . VAL D 1 87  ? 7.73000   36.77600  68.00400  1.000 82.81172  ?  87  VAL D N   1 
ATOM   5794 C  CA  . VAL D 1 87  ? 6.53700   36.13900  68.55500  1.000 83.10407  ?  87  VAL D CA  1 
ATOM   5795 C  C   . VAL D 1 87  ? 6.35400   36.52400  70.01900  1.000 81.16092  ?  87  VAL D C   1 
ATOM   5796 O  O   . VAL D 1 87  ? 5.30000   37.04100  70.40700  1.000 82.03960  ?  87  VAL D O   1 
ATOM   5797 C  CB  . VAL D 1 87  ? 6.59900   34.61000  68.38800  1.000 81.97867  ?  87  VAL D CB  1 
ATOM   5798 C  CG1 . VAL D 1 87  ? 5.27700   33.98000  68.79600  1.000 75.56749  ?  87  VAL D CG1 1 
ATOM   5799 C  CG2 . VAL D 1 87  ? 6.95200   34.24900  66.95200  1.000 75.10998  ?  87  VAL D CG2 1 
ATOM   5800 N  N   . LEU D 1 88  ? 7.37500   36.27300  70.84400  1.000 81.02026  ?  88  LEU D N   1 
ATOM   5801 C  CA  . LEU D 1 88  ? 7.28900   36.61500  72.26100  1.000 84.30471  ?  88  LEU D CA  1 
ATOM   5802 C  C   . LEU D 1 88  ? 7.42500   38.11000  72.50800  1.000 86.50548  ?  88  LEU D C   1 
ATOM   5803 O  O   . LEU D 1 88  ? 7.01900   38.58600  73.57400  1.000 81.91890  ?  88  LEU D O   1 
ATOM   5804 C  CB  . LEU D 1 88  ? 8.35100   35.86000  73.06200  1.000 80.98697  ?  88  LEU D CB  1 
ATOM   5805 C  CG  . LEU D 1 88  ? 8.24700   34.33700  73.06700  1.000 77.39615  ?  88  LEU D CG  1 
ATOM   5806 C  CD1 . LEU D 1 88  ? 9.33400   33.74900  73.93600  1.000 68.80824  ?  88  LEU D CD1 1 
ATOM   5807 C  CD2 . LEU D 1 88  ? 6.88000   33.91600  73.58000  1.000 63.89402  ?  88  LEU D CD2 1 
ATOM   5808 N  N   . GLU D 1 89  ? 7.98800   38.85300  71.55300  1.000 88.06040  ?  89  GLU D N   1 
ATOM   5809 C  CA  . GLU D 1 89  ? 8.11000   40.30700  71.64300  1.000 87.40776  ?  89  GLU D CA  1 
ATOM   5810 C  C   . GLU D 1 89  ? 8.93400   40.72400  72.86200  1.000 83.78068  ?  89  GLU D C   1 
ATOM   5811 O  O   . GLU D 1 89  ? 8.51900   41.56400  73.66300  1.000 89.00416  ?  89  GLU D O   1 
ATOM   5812 C  CB  . GLU D 1 89  ? 6.72100   40.94900  71.68100  1.000 87.31199  ?  89  GLU D CB  1 
ATOM   5813 C  CG  . GLU D 1 89  ? 5.91900   40.75800  70.40700  1.000 88.21826  ?  89  GLU D CG  1 
ATOM   5814 C  CD  . GLU D 1 89  ? 4.54200   41.38100  70.49100  1.000 92.20761  ?  89  GLU D CD  1 
ATOM   5815 O  OE1 . GLU D 1 89  ? 4.34900   42.28800  71.32600  1.000 92.33725  ?  89  GLU D OE1 1 
ATOM   5816 O  OE2 . GLU D 1 89  ? 3.64700   40.94800  69.73500  1.000 102.27076 -1 89  GLU D OE2 1 
ATOM   5817 N  N   . VAL D 1 90  ? 10.11700  40.12200  73.00200  1.000 82.65119  ?  90  VAL D N   1 
ATOM   5818 C  CA  . VAL D 1 90  ? 11.03300  40.53600  74.05700  1.000 87.39976  ?  90  VAL D CA  1 
ATOM   5819 C  C   . VAL D 1 90  ? 11.51200  41.95900  73.79000  1.000 88.52666  ?  90  VAL D C   1 
ATOM   5820 O  O   . VAL D 1 90  ? 11.66300  42.38600  72.63700  1.000 82.09646  ?  90  VAL D O   1 
ATOM   5821 C  CB  . VAL D 1 90  ? 12.22200  39.56300  74.17100  1.000 83.05343  ?  90  VAL D CB  1 
ATOM   5822 C  CG1 . VAL D 1 90  ? 11.73500  38.15700  74.49700  1.000 81.64333  ?  90  VAL D CG1 1 
ATOM   5823 C  CG2 . VAL D 1 90  ? 13.05300  39.56700  72.89200  1.000 82.26511  ?  90  VAL D CG2 1 
ATOM   5824 N  N   . GLU D 1 91  ? 11.73300  42.71100  74.86700  1.000 95.03585  ?  91  GLU D N   1 
ATOM   5825 C  CA  . GLU D 1 91  ? 12.21400  44.08000  74.76500  1.000 93.33272  ?  91  GLU D CA  1 
ATOM   5826 C  C   . GLU D 1 91  ? 13.68000  44.21400  75.15400  1.000 92.05925  ?  91  GLU D C   1 
ATOM   5827 O  O   . GLU D 1 91  ? 14.26400  45.28300  74.94600  1.000 93.96926  ?  91  GLU D O   1 
ATOM   5828 C  CB  . GLU D 1 91  ? 11.35500  45.00500  75.64100  1.000 95.81101  ?  91  GLU D CB  1 
ATOM   5829 C  CG  . GLU D 1 91  ? 9.86400   44.70500  75.54900  1.000 100.82313 ?  91  GLU D CG  1 
ATOM   5830 C  CD  . GLU D 1 91  ? 9.01900   45.63900  76.39200  1.000 106.96177 ?  91  GLU D CD  1 
ATOM   5831 O  OE1 . GLU D 1 91  ? 9.60100   46.45400  77.13800  1.000 107.76753 ?  91  GLU D OE1 1 
ATOM   5832 O  OE2 . GLU D 1 91  ? 7.77800   45.48000  76.39100  1.000 111.45824 -1 91  GLU D OE2 1 
ATOM   5833 N  N   . HIS D 1 92  ? 14.28400  43.16400  75.71300  1.000 88.08387  ?  92  HIS D N   1 
ATOM   5834 C  CA  . HIS D 1 92  ? 15.69900  43.15200  76.06400  1.000 87.95492  ?  92  HIS D CA  1 
ATOM   5835 C  C   . HIS D 1 92  ? 16.27100  41.77900  75.75400  1.000 83.45725  ?  92  HIS D C   1 
ATOM   5836 O  O   . HIS D 1 92  ? 15.67600  40.76000  76.11700  1.000 84.07101  ?  92  HIS D O   1 
ATOM   5837 C  CB  . HIS D 1 92  ? 15.94200  43.47700  77.54400  1.000 89.47966  ?  92  HIS D CB  1 
ATOM   5838 C  CG  . HIS D 1 92  ? 15.56400  44.87000  77.93100  1.000 91.62644  ?  92  HIS D CG  1 
ATOM   5839 N  ND1 . HIS D 1 92  ? 16.30400  45.97500  77.57400  1.000 92.85367  ?  92  HIS D ND1 1 
ATOM   5840 C  CD2 . HIS D 1 92  ? 14.52200  45.33400  78.65300  1.000 90.67712  ?  92  HIS D CD2 1 
ATOM   5841 C  CE1 . HIS D 1 92  ? 15.72800  47.06300  78.05700  1.000 94.70135  ?  92  HIS D CE1 1 
ATOM   5842 N  NE2 . HIS D 1 92  ? 14.64300  46.70000  78.71600  1.000 90.85816  ?  92  HIS D NE2 1 
ATOM   5843 N  N   . ILE D 1 93  ? 17.42400  41.75800  75.09300  1.000 77.50333  ?  93  ILE D N   1 
ATOM   5844 C  CA  . ILE D 1 93  ? 18.18700  40.54100  74.85300  1.000 76.70391  ?  93  ILE D CA  1 
ATOM   5845 C  C   . ILE D 1 93  ? 19.54100  40.71100  75.51900  1.000 75.65937  ?  93  ILE D C   1 
ATOM   5846 O  O   . ILE D 1 93  ? 20.24300  41.69500  75.26200  1.000 76.59788  ?  93  ILE D O   1 
ATOM   5847 C  CB  . ILE D 1 93  ? 18.35900  40.25000  73.35200  1.000 81.43702  ?  93  ILE D CB  1 
ATOM   5848 C  CG1 . ILE D 1 93  ? 17.00500  40.20800  72.64700  1.000 83.57642  ?  93  ILE D CG1 1 
ATOM   5849 C  CG2 . ILE D 1 93  ? 19.10700  38.94300  73.15400  1.000 74.43671  ?  93  ILE D CG2 1 
ATOM   5850 C  CD1 . ILE D 1 93  ? 17.11700  39.96700  71.16000  1.000 73.84016  ?  93  ILE D CD1 1 
ATOM   5851 N  N   . ILE D 1 94  ? 19.90500  39.76600  76.37800  1.000 72.25029  ?  94  ILE D N   1 
ATOM   5852 C  CA  . ILE D 1 94  ? 21.13300  39.86000  77.15500  1.000 72.05875  ?  94  ILE D CA  1 
ATOM   5853 C  C   . ILE D 1 94  ? 22.06300  38.73300  76.72800  1.000 68.41453  ?  94  ILE D C   1 
ATOM   5854 O  O   . ILE D 1 94  ? 21.73100  37.55200  76.88800  1.000 70.21885  ?  94  ILE D O   1 
ATOM   5855 C  CB  . ILE D 1 94  ? 20.85300  39.80200  78.66400  1.000 70.96937  ?  94  ILE D CB  1 
ATOM   5856 C  CG1 . ILE D 1 94  ? 20.02500  41.01700  79.08800  1.000 70.84339  ?  94  ILE D CG1 1 
ATOM   5857 C  CG2 . ILE D 1 94  ? 22.15600  39.76200  79.44300  1.000 69.73479  ?  94  ILE D CG2 1 
ATOM   5858 C  CD1 . ILE D 1 94  ? 19.02600  40.72500  80.18600  1.000 68.35327  ?  94  ILE D CD1 1 
ATOM   5859 N  N   . ILE D 1 95  ? 23.21700  39.09900  76.17900  1.000 67.59317  ?  95  ILE D N   1 
ATOM   5860 C  CA  . ILE D 1 95  ? 24.29900  38.16100  75.90700  1.000 73.22873  ?  95  ILE D CA  1 
ATOM   5861 C  C   . ILE D 1 95  ? 25.31700  38.31700  77.02600  1.000 74.36782  ?  95  ILE D C   1 
ATOM   5862 O  O   . ILE D 1 95  ? 25.90600  39.39200  77.19500  1.000 75.73101  ?  95  ILE D O   1 
ATOM   5863 C  CB  . ILE D 1 95  ? 24.93300  38.40500  74.52900  1.000 78.61423  ?  95  ILE D CB  1 
ATOM   5864 C  CG1 . ILE D 1 95  ? 23.89100  38.22100  73.42200  1.000 70.99038  ?  95  ILE D CG1 1 
ATOM   5865 C  CG2 . ILE D 1 95  ? 26.12200  37.47700  74.31400  1.000 73.86419  ?  95  ILE D CG2 1 
ATOM   5866 C  CD1 . ILE D 1 95  ? 24.44100  38.41100  72.02500  1.000 75.89962  ?  95  ILE D CD1 1 
ATOM   5867 N  N   . CYS D 1 96  ? 25.52300  37.25000  77.79300  1.000 78.87985  ?  96  CYS D N   1 
ATOM   5868 C  CA  . CYS D 1 96  ? 26.31900  37.30100  79.01300  1.000 72.08356  ?  96  CYS D CA  1 
ATOM   5869 C  C   . CYS D 1 96  ? 27.36700  36.20000  79.00000  1.000 72.48573  ?  96  CYS D C   1 
ATOM   5870 O  O   . CYS D 1 96  ? 27.02600  35.01600  78.91000  1.000 76.24195  ?  96  CYS D O   1 
ATOM   5871 C  CB  . CYS D 1 96  ? 25.42300  37.16700  80.24800  1.000 76.06990  ?  96  CYS D CB  1 
ATOM   5872 S  SG  . CYS D 1 96  ? 26.27700  37.39400  81.82500  1.000 83.63487  ?  96  CYS D SG  1 
ATOM   5873 N  N   . GLY D 1 97  ? 28.63900  36.59000  79.09900  1.000 75.89005  ?  97  GLY D N   1 
ATOM   5874 C  CA  . GLY D 1 97  ? 29.71700  35.65400  79.31500  1.000 78.35674  ?  97  GLY D CA  1 
ATOM   5875 C  C   . GLY D 1 97  ? 30.12000  35.60400  80.78200  1.000 83.97782  ?  97  GLY D C   1 
ATOM   5876 O  O   . GLY D 1 97  ? 29.55300  36.27500  81.64100  1.000 79.21383  ?  97  GLY D O   1 
ATOM   5877 N  N   . HIS D 1 98  ? 31.11800  34.77000  81.06400  1.000 86.74575  ?  98  HIS D N   1 
ATOM   5878 C  CA  . HIS D 1 98  ? 31.56600  34.58200  82.43700  1.000 85.08813  ?  98  HIS D CA  1 
ATOM   5879 C  C   . HIS D 1 98  ? 33.06300  34.31600  82.46200  1.000 88.02735  ?  98  HIS D C   1 
ATOM   5880 O  O   . HIS D 1 98  ? 33.55900  33.47500  81.70600  1.000 87.25341  ?  98  HIS D O   1 
ATOM   5881 C  CB  . HIS D 1 98  ? 30.80900  33.43100  83.10900  1.000 80.59573  ?  98  HIS D CB  1 
ATOM   5882 C  CG  . HIS D 1 98  ? 30.96700  32.11600  82.41200  1.000 85.67818  ?  98  HIS D CG  1 
ATOM   5883 N  ND1 . HIS D 1 98  ? 31.67800  31.06900  82.95600  1.000 85.94769  ?  98  HIS D ND1 1 
ATOM   5884 C  CD2 . HIS D 1 98  ? 30.51700  31.68300  81.21100  1.000 87.19916  ?  98  HIS D CD2 1 
ATOM   5885 C  CE1 . HIS D 1 98  ? 31.65300  30.04400  82.12300  1.000 86.62632  ?  98  HIS D CE1 1 
ATOM   5886 N  NE2 . HIS D 1 98  ? 30.95600  30.39100  81.05600  1.000 90.98623  ?  98  HIS D NE2 1 
ATOM   5887 N  N   . TYR D 1 99  ? 33.77400  35.04500  83.32000  1.000 86.76048  ?  99  TYR D N   1 
ATOM   5888 C  CA  . TYR D 1 99  ? 35.21000  34.85100  83.46500  1.000 88.10423  ?  99  TYR D CA  1 
ATOM   5889 C  C   . TYR D 1 99  ? 35.51000  33.43600  83.94600  1.000 88.59613  ?  99  TYR D C   1 
ATOM   5890 O  O   . TYR D 1 99  ? 34.82300  32.89900  84.81900  1.000 93.43144  ?  99  TYR D O   1 
ATOM   5891 C  CB  . TYR D 1 99  ? 35.78200  35.88400  84.43400  1.000 88.66883  ?  99  TYR D CB  1 
ATOM   5892 C  CG  . TYR D 1 99  ? 35.40500  37.30300  84.07300  1.000 89.14393  ?  99  TYR D CG  1 
ATOM   5893 C  CD1 . TYR D 1 99  ? 36.13800  38.02300  83.13800  1.000 93.40137  ?  99  TYR D CD1 1 
ATOM   5894 C  CD2 . TYR D 1 99  ? 34.30500  37.91700  84.65600  1.000 83.20522  ?  99  TYR D CD2 1 
ATOM   5895 C  CE1 . TYR D 1 99  ? 35.79000  39.31800  82.80200  1.000 94.76898  ?  99  TYR D CE1 1 
ATOM   5896 C  CE2 . TYR D 1 99  ? 33.94800  39.21000  84.32700  1.000 83.86722  ?  99  TYR D CE2 1 
ATOM   5897 C  CZ  . TYR D 1 99  ? 34.69400  39.90600  83.39900  1.000 97.04221  ?  99  TYR D CZ  1 
ATOM   5898 O  OH  . TYR D 1 99  ? 34.34100  41.19500  83.06900  1.000 103.42587 ?  99  TYR D OH  1 
ATOM   5899 N  N   . GLY D 1 100 ? 36.54500  32.83400  83.37000  1.000 94.11980  ?  100 GLY D N   1 
ATOM   5900 C  CA  . GLY D 1 100 ? 36.88200  31.45400  83.65100  1.000 90.27166  ?  100 GLY D CA  1 
ATOM   5901 C  C   . GLY D 1 100 ? 36.23000  30.44700  82.73300  1.000 92.52848  ?  100 GLY D C   1 
ATOM   5902 O  O   . GLY D 1 100 ? 36.33500  29.24100  82.99000  1.000 90.38964  ?  100 GLY D O   1 
ATOM   5903 N  N   . CYS D 1 101 ? 35.54500  30.90700  81.68400  1.000 88.70049  ?  101 CYS D N   1 
ATOM   5904 C  CA  . CYS D 1 101 ? 34.83800  30.02400  80.76200  1.000 85.54083  ?  101 CYS D CA  1 
ATOM   5905 C  C   . CYS D 1 101 ? 35.75900  28.96000  80.17900  1.000 81.40140  ?  101 CYS D C   1 
ATOM   5906 O  O   . CYS D 1 101 ? 36.86000  29.25900  79.70800  1.000 81.21364  ?  101 CYS D O   1 
ATOM   5907 C  CB  . CYS D 1 101 ? 34.21400  30.84500  79.63500  1.000 84.27771  ?  101 CYS D CB  1 
ATOM   5908 S  SG  . CYS D 1 101 ? 33.39300  29.85600  78.36500  1.000 84.93918  ?  101 CYS D SG  1 
ATOM   5909 N  N   . GLY D 1 102 ? 35.30000  27.70800  80.22200  1.000 76.11735  ?  102 GLY D N   1 
ATOM   5910 C  CA  . GLY D 1 102 ? 36.09000  26.62000  79.67000  1.000 81.06567  ?  102 GLY D CA  1 
ATOM   5911 C  C   . GLY D 1 102 ? 36.27100  26.72400  78.16700  1.000 87.61267  ?  102 GLY D C   1 
ATOM   5912 O  O   . GLY D 1 102 ? 37.32500  26.36700  77.63500  1.000 86.93248  ?  102 GLY D O   1 
ATOM   5913 N  N   . GLY D 1 103 ? 35.25000  27.21300  77.46200  1.000 82.35410  ?  103 GLY D N   1 
ATOM   5914 C  CA  . GLY D 1 103 ? 35.35300  27.33400  76.01600  1.000 74.45491  ?  103 GLY D CA  1 
ATOM   5915 C  C   . GLY D 1 103 ? 36.37600  28.37000  75.58900  1.000 78.83931  ?  103 GLY D C   1 
ATOM   5916 O  O   . GLY D 1 103 ? 37.18500  28.12500  74.69000  1.000 86.34843  ?  103 GLY D O   1 
ATOM   5917 N  N   . VAL D 1 104 ? 36.36000  29.53800  76.23600  1.000 74.79191  ?  104 VAL D N   1 
ATOM   5918 C  CA  . VAL D 1 104 ? 37.31700  30.58900  75.89800  1.000 74.81967  ?  104 VAL D CA  1 
ATOM   5919 C  C   . VAL D 1 104 ? 38.73700  30.11500  76.17600  1.000 75.19672  ?  104 VAL D C   1 
ATOM   5920 O  O   . VAL D 1 104 ? 39.67200  30.42300  75.42700  1.000 76.44749  ?  104 VAL D O   1 
ATOM   5921 C  CB  . VAL D 1 104 ? 36.98600  31.88000  76.67000  1.000 75.60250  ?  104 VAL D CB  1 
ATOM   5922 C  CG1 . VAL D 1 104 ? 38.00400  32.96700  76.35900  1.000 80.04555  ?  104 VAL D CG1 1 
ATOM   5923 C  CG2 . VAL D 1 104 ? 35.57700  32.35200  76.34100  1.000 69.29859  ?  104 VAL D CG2 1 
ATOM   5924 N  N   . GLN D 1 105 ? 38.91700  29.34800  77.25100  1.000 83.95697  ?  105 GLN D N   1 
ATOM   5925 C  CA  . GLN D 1 105 ? 40.23700  28.81900  77.57200  1.000 89.64326  ?  105 GLN D CA  1 
ATOM   5926 C  C   . GLN D 1 105 ? 40.66900  27.76100  76.56500  1.000 82.12359  ?  105 GLN D C   1 
ATOM   5927 O  O   . GLN D 1 105 ? 41.83000  27.73900  76.14000  1.000 81.28697  ?  105 GLN D O   1 
ATOM   5928 C  CB  . GLN D 1 105 ? 40.22500  28.23400  78.98400  1.000 85.37874  ?  105 GLN D CB  1 
ATOM   5929 C  CG  . GLN D 1 105 ? 41.57300  27.76500  79.48800  1.000 88.15966  ?  105 GLN D CG  1 
ATOM   5930 C  CD  . GLN D 1 105 ? 41.46000  26.97500  80.77800  1.000 99.05063  ?  105 GLN D CD  1 
ATOM   5931 O  OE1 . GLN D 1 105 ? 40.36300  26.60800  81.20000  1.000 102.82595 ?  105 GLN D OE1 1 
ATOM   5932 N  NE2 . GLN D 1 105 ? 42.59700  26.70400  81.40800  1.000 95.06397  ?  105 GLN D NE2 1 
ATOM   5933 N  N   . ALA D 1 106 ? 39.74800  26.88200  76.16500  1.000 78.21309  ?  106 ALA D N   1 
ATOM   5934 C  CA  . ALA D 1 106 ? 40.07500  25.86200  75.17300  1.000 87.94911  ?  106 ALA D CA  1 
ATOM   5935 C  C   . ALA D 1 106 ? 40.37600  26.48200  73.81400  1.000 87.92314  ?  106 ALA D C   1 
ATOM   5936 O  O   . ALA D 1 106 ? 41.23300  25.98300  73.07500  1.000 83.85651  ?  106 ALA D O   1 
ATOM   5937 C  CB  . ALA D 1 106 ? 38.93400  24.85300  75.06200  1.000 86.44090  ?  106 ALA D CB  1 
ATOM   5938 N  N   . ALA D 1 107 ? 39.66900  27.55900  73.46000  1.000 81.57142  ?  107 ALA D N   1 
ATOM   5939 C  CA  . ALA D 1 107 ? 39.94800  28.25000  72.20600  1.000 79.08155  ?  107 ALA D CA  1 
ATOM   5940 C  C   . ALA D 1 107 ? 41.39800  28.71100  72.13100  1.000 86.09106  ?  107 ALA D C   1 
ATOM   5941 O  O   . ALA D 1 107 ? 42.04400  28.58500  71.08500  1.000 88.43895  ?  107 ALA D O   1 
ATOM   5942 C  CB  . ALA D 1 107 ? 39.00000  29.43600  72.04100  1.000 71.15319  ?  107 ALA D CB  1 
ATOM   5943 N  N   . VAL D 1 108 ? 41.92600  29.24900  73.23000  1.000 89.98058  ?  108 VAL D N   1 
ATOM   5944 C  CA  . VAL D 1 108 ? 43.27500  29.80400  73.21600  1.000 88.78394  ?  108 VAL D CA  1 
ATOM   5945 C  C   . VAL D 1 108 ? 44.32300  28.70100  73.31300  1.000 88.82121  ?  108 VAL D C   1 
ATOM   5946 O  O   . VAL D 1 108 ? 45.31100  28.70000  72.57100  1.000 93.86780  ?  108 VAL D O   1 
ATOM   5947 C  CB  . VAL D 1 108 ? 43.42900  30.84400  74.33800  1.000 89.48214  ?  108 VAL D CB  1 
ATOM   5948 C  CG1 . VAL D 1 108 ? 44.86200  31.33700  74.41300  1.000 93.11630  ?  108 VAL D CG1 1 
ATOM   5949 C  CG2 . VAL D 1 108 ? 42.48600  32.00000  74.07900  1.000 85.01125  ?  108 VAL D CG2 1 
ATOM   5950 N  N   . GLU D 1 109 ? 44.13100  27.74500  74.22500  1.000 90.40324  ?  109 GLU D N   1 
ATOM   5951 C  CA  . GLU D 1 109 ? 45.11700  26.68300  74.38300  1.000 95.11197  ?  109 GLU D CA  1 
ATOM   5952 C  C   . GLU D 1 109 ? 45.05100  25.66000  73.26100  1.000 93.63055  ?  109 GLU D C   1 
ATOM   5953 O  O   . GLU D 1 109 ? 46.02300  24.92600  73.05500  1.000 96.54448  ?  109 GLU D O   1 
ATOM   5954 C  CB  . GLU D 1 109 ? 44.92400  25.96600  75.72200  1.000 94.34298  ?  109 GLU D CB  1 
ATOM   5955 C  CG  . GLU D 1 109 ? 44.95500  26.87200  76.93700  1.000 92.85041  ?  109 GLU D CG  1 
ATOM   5956 C  CD  . GLU D 1 109 ? 44.32900  26.22000  78.15300  1.000 101.69507 ?  109 GLU D CD  1 
ATOM   5957 O  OE1 . GLU D 1 109 ? 43.45600  25.34200  77.97300  1.000 94.49453  ?  109 GLU D OE1 1 
ATOM   5958 O  OE2 . GLU D 1 109 ? 44.70600  26.58400  79.28700  1.000 109.39446 -1 109 GLU D OE2 1 
ATOM   5959 N  N   . ASN D 1 110 ? 43.94500  25.62300  72.52400  1.000 92.38035  ?  110 ASN D N   1 
ATOM   5960 C  CA  . ASN D 1 110 ? 43.76600  24.73400  71.38100  1.000 94.38151  ?  110 ASN D CA  1 
ATOM   5961 C  C   . ASN D 1 110 ? 44.19400  23.28700  71.64400  1.000 94.47111  ?  110 ASN D C   1 
ATOM   5962 O  O   . ASN D 1 110 ? 45.09600  22.77100  70.97400  1.000 88.16619  ?  110 ASN D O   1 
ATOM   5963 C  CB  . ASN D 1 110 ? 44.49000  25.29200  70.16400  1.000 95.95971  ?  110 ASN D CB  1 
ATOM   5964 C  CG  . ASN D 1 110 ? 44.00700  24.67400  68.86500  1.000 94.91291  ?  110 ASN D CG  1 
ATOM   5965 O  OD1 . ASN D 1 110 ? 43.14200  23.79600  68.86300  1.000 93.96456  ?  110 ASN D OD1 1 
ATOM   5966 N  ND2 . ASN D 1 110 ? 44.56400  25.13200  67.75000  1.000 87.66862  ?  110 ASN D ND2 1 
ATOM   5967 N  N   . PRO D 1 111 ? 43.57600  22.60600  72.60500  1.000 96.53310  ?  111 PRO D N   1 
ATOM   5968 C  CA  . PRO D 1 111 ? 43.79800  21.16500  72.73000  1.000 94.60662  ?  111 PRO D CA  1 
ATOM   5969 C  C   . PRO D 1 111 ? 42.93000  20.40400  71.73900  1.000 89.39332  ?  111 PRO D C   1 
ATOM   5970 O  O   . PRO D 1 111 ? 41.90900  20.89400  71.25400  1.000 86.91598  ?  111 PRO D O   1 
ATOM   5971 C  CB  . PRO D 1 111 ? 43.39000  20.86600  74.17600  1.000 82.73799  ?  111 PRO D CB  1 
ATOM   5972 C  CG  . PRO D 1 111 ? 42.35200  21.88700  74.48100  1.000 85.57793  ?  111 PRO D CG  1 
ATOM   5973 C  CD  . PRO D 1 111 ? 42.64400  23.10500  73.63500  1.000 90.39519  ?  111 PRO D CD  1 
ATOM   5974 N  N   . GLU D 1 112 ? 43.36900  19.18900  71.42500  1.000 87.77453  ?  112 GLU D N   1 
ATOM   5975 C  CA  . GLU D 1 112 ? 42.61800  18.32900  70.51400  1.000 88.66645  ?  112 GLU D CA  1 
ATOM   5976 C  C   . GLU D 1 112 ? 41.46100  17.72200  71.29500  1.000 81.81675  ?  112 GLU D C   1 
ATOM   5977 O  O   . GLU D 1 112 ? 41.59000  16.68100  71.94100  1.000 86.55060  ?  112 GLU D O   1 
ATOM   5978 C  CB  . GLU D 1 112 ? 43.51800  17.26000  69.90800  1.000 95.59647  ?  112 GLU D CB  1 
ATOM   5979 C  CG  . GLU D 1 112 ? 44.49700  17.79800  68.87500  1.000 99.12488  ?  112 GLU D CG  1 
ATOM   5980 C  CD  . GLU D 1 112 ? 45.47800  16.74600  68.39700  1.000 110.33005 ?  112 GLU D CD  1 
ATOM   5981 O  OE1 . GLU D 1 112 ? 45.08300  15.56500  68.30100  1.000 108.05598 ?  112 GLU D OE1 1 
ATOM   5982 O  OE2 . GLU D 1 112 ? 46.64300  17.10000  68.11500  1.000 117.15854 -1 112 GLU D OE2 1 
ATOM   5983 N  N   . LEU D 1 113 ? 40.30700  18.38400  71.22800  1.000 77.89345  ?  113 LEU D N   1 
ATOM   5984 C  CA  . LEU D 1 113 ? 39.12700  17.96100  71.96700  1.000 79.52218  ?  113 LEU D CA  1 
ATOM   5985 C  C   . LEU D 1 113 ? 38.08500  17.27800  71.09500  1.000 81.70258  ?  113 LEU D C   1 
ATOM   5986 O  O   . LEU D 1 113 ? 37.13800  16.69400  71.63400  1.000 76.65560  ?  113 LEU D O   1 
ATOM   5987 C  CB  . LEU D 1 113 ? 38.48300  19.16200  72.66800  1.000 75.28424  ?  113 LEU D CB  1 
ATOM   5988 C  CG  . LEU D 1 113 ? 39.39700  20.02000  73.53800  1.000 84.10846  ?  113 LEU D CG  1 
ATOM   5989 C  CD1 . LEU D 1 113 ? 38.63600  21.20900  74.10500  1.000 83.72122  ?  113 LEU D CD1 1 
ATOM   5990 C  CD2 . LEU D 1 113 ? 39.99500  19.18000  74.65300  1.000 82.20517  ?  113 LEU D CD2 1 
ATOM   5991 N  N   . GLY D 1 114 ? 38.22700  17.34000  69.77500  1.000 81.59435  ?  114 GLY D N   1 
ATOM   5992 C  CA  . GLY D 1 114 ? 37.26600  16.70200  68.90200  1.000 73.06200  ?  114 GLY D CA  1 
ATOM   5993 C  C   . GLY D 1 114 ? 36.31800  17.67200  68.23300  1.000 67.10966  ?  114 GLY D C   1 
ATOM   5994 O  O   . GLY D 1 114 ? 36.71500  18.77200  67.83500  1.000 69.91041  ?  114 GLY D O   1 
ATOM   5995 N  N   . LEU D 1 115 ? 35.05200  17.26100  68.11200  1.000 66.23997  ?  115 LEU D N   1 
ATOM   5996 C  CA  . LEU D 1 115 ? 34.05700  18.03700  67.37500  1.000 66.14104  ?  115 LEU D CA  1 
ATOM   5997 C  C   . LEU D 1 115 ? 33.90500  19.45900  67.91000  1.000 67.69658  ?  115 LEU D C   1 
ATOM   5998 O  O   . LEU D 1 115 ? 33.59400  20.37700  67.14300  1.000 64.96758  ?  115 LEU D O   1 
ATOM   5999 C  CB  . LEU D 1 115 ? 32.71300  17.30800  67.41000  1.000 59.16122  ?  115 LEU D CB  1 
ATOM   6000 C  CG  . LEU D 1 115 ? 31.52300  18.00800  66.75800  1.000 63.61691  ?  115 LEU D CG  1 
ATOM   6001 C  CD1 . LEU D 1 115 ? 31.78900  18.23100  65.27800  1.000 72.90475  ?  115 LEU D CD1 1 
ATOM   6002 C  CD2 . LEU D 1 115 ? 30.25100  17.20300  66.96300  1.000 61.98484  ?  115 LEU D CD2 1 
ATOM   6003 N  N   . ILE D 1 116 ? 34.11000  19.66300  69.21400  1.000 68.04243  ?  116 ILE D N   1 
ATOM   6004 C  CA  . ILE D 1 116 ? 33.88800  20.98300  69.80100  1.000 65.57598  ?  116 ILE D CA  1 
ATOM   6005 C  C   . ILE D 1 116 ? 34.87600  22.00500  69.24500  1.000 66.23300  ?  116 ILE D C   1 
ATOM   6006 O  O   . ILE D 1 116 ? 34.58100  23.20700  69.21500  1.000 61.69011  ?  116 ILE D O   1 
ATOM   6007 C  CB  . ILE D 1 116 ? 33.95600  20.89600  71.33900  1.000 65.10444  ?  116 ILE D CB  1 
ATOM   6008 C  CG1 . ILE D 1 116 ? 33.65800  22.25100  71.98700  1.000 56.40055  ?  116 ILE D CG1 1 
ATOM   6009 C  CG2 . ILE D 1 116 ? 35.31500  20.39100  71.78500  1.000 65.57765  ?  116 ILE D CG2 1 
ATOM   6010 C  CD1 . ILE D 1 116 ? 32.24900  22.74300  71.76200  1.000 59.15914  ?  116 ILE D CD1 1 
ATOM   6011 N  N   . ASN D 1 117 ? 36.05000  21.55200  68.78800  1.000 65.59850  ?  117 ASN D N   1 
ATOM   6012 C  CA  . ASN D 1 117 ? 37.07900  22.47600  68.31400  1.000 65.60258  ?  117 ASN D CA  1 
ATOM   6013 C  C   . ASN D 1 117 ? 36.56400  23.36500  67.18800  1.000 75.20326  ?  117 ASN D C   1 
ATOM   6014 O  O   . ASN D 1 117 ? 36.93900  24.54000  67.09500  1.000 78.84681  ?  117 ASN D O   1 
ATOM   6015 C  CB  . ASN D 1 117 ? 38.30100  21.69500  67.83000  1.000 69.80582  ?  117 ASN D CB  1 
ATOM   6016 C  CG  . ASN D 1 117 ? 39.19900  21.24600  68.95800  1.000 74.98652  ?  117 ASN D CG  1 
ATOM   6017 O  OD1 . ASN D 1 117 ? 38.77500  21.15300  70.10700  1.000 89.10486  ?  117 ASN D OD1 1 
ATOM   6018 N  ND2 . ASN D 1 117 ? 40.44900  20.94000  68.62900  1.000 77.69225  ?  117 ASN D ND2 1 
ATOM   6019 N  N   . ASN D 1 118 ? 35.69800  22.82400  66.32600  1.000 71.28026  ?  118 ASN D N   1 
ATOM   6020 C  CA  . ASN D 1 118 ? 35.15600  23.61900  65.22700  1.000 70.08684  ?  118 ASN D CA  1 
ATOM   6021 C  C   . ASN D 1 118 ? 34.25600  24.73700  65.74100  1.000 69.17603  ?  118 ASN D C   1 
ATOM   6022 O  O   . ASN D 1 118 ? 34.29800  25.86100  65.22500  1.000 68.80478  ?  118 ASN D O   1 
ATOM   6023 C  CB  . ASN D 1 118 ? 34.40700  22.71700  64.24800  1.000 70.03911  ?  118 ASN D CB  1 
ATOM   6024 C  CG  . ASN D 1 118 ? 35.28100  21.60000  63.70700  1.000 69.55703  ?  118 ASN D CG  1 
ATOM   6025 O  OD1 . ASN D 1 118 ? 36.20300  21.84100  62.92800  1.000 65.95507  ?  118 ASN D OD1 1 
ATOM   6026 N  ND2 . ASN D 1 118 ? 34.99800  20.37000  64.12100  1.000 71.87573  ?  118 ASN D ND2 1 
ATOM   6027 N  N   . TRP D 1 119 ? 33.43000  24.44800  66.74900  1.000 76.28796  ?  119 TRP D N   1 
ATOM   6028 C  CA  . TRP D 1 119 ? 32.61500  25.49400  67.36100  1.000 77.14111  ?  119 TRP D CA  1 
ATOM   6029 C  C   . TRP D 1 119 ? 33.49100  26.59000  67.95600  1.000 72.00866  ?  119 TRP D C   1 
ATOM   6030 O  O   . TRP D 1 119 ? 33.15500  27.77800  67.87700  1.000 70.39051  ?  119 TRP D O   1 
ATOM   6031 C  CB  . TRP D 1 119 ? 31.70100  24.89600  68.43200  1.000 70.40695  ?  119 TRP D CB  1 
ATOM   6032 C  CG  . TRP D 1 119 ? 30.71300  25.87400  69.00300  1.000 67.74211  ?  119 TRP D CG  1 
ATOM   6033 C  CD1 . TRP D 1 119 ? 30.87700  26.65000  70.11200  1.000 67.86705  ?  119 TRP D CD1 1 
ATOM   6034 C  CD2 . TRP D 1 119 ? 29.40500  26.17200  68.49500  1.000 69.38784  ?  119 TRP D CD2 1 
ATOM   6035 N  NE1 . TRP D 1 119 ? 29.75400  27.41400  70.32600  1.000 65.04311  ?  119 TRP D NE1 1 
ATOM   6036 C  CE2 . TRP D 1 119 ? 28.83700  27.14000  69.34700  1.000 66.95415  ?  119 TRP D CE2 1 
ATOM   6037 C  CE3 . TRP D 1 119 ? 28.66000  25.71200  67.40500  1.000 67.23303  ?  119 TRP D CE3 1 
ATOM   6038 C  CZ2 . TRP D 1 119 ? 27.55900  27.65800  69.14100  1.000 69.58398  ?  119 TRP D CZ2 1 
ATOM   6039 C  CZ3 . TRP D 1 119 ? 27.39200  26.23000  67.20100  1.000 64.51741  ?  119 TRP D CZ3 1 
ATOM   6040 C  CH2 . TRP D 1 119 ? 26.85500  27.19200  68.06500  1.000 70.13849  ?  119 TRP D CH2 1 
ATOM   6041 N  N   . LEU D 1 120 ? 34.60000  26.20500  68.58900  1.000 71.02996  ?  120 LEU D N   1 
ATOM   6042 C  CA  . LEU D 1 120 ? 35.49800  27.15600  69.23000  1.000 77.73033  ?  120 LEU D CA  1 
ATOM   6043 C  C   . LEU D 1 120 ? 36.35800  27.93500  68.24000  1.000 77.76335  ?  120 LEU D C   1 
ATOM   6044 O  O   . LEU D 1 120 ? 37.00100  28.91000  68.64300  1.000 81.25025  ?  120 LEU D O   1 
ATOM   6045 C  CB  . LEU D 1 120 ? 36.39500  26.42400  70.23200  1.000 72.69439  ?  120 LEU D CB  1 
ATOM   6046 C  CG  . LEU D 1 120 ? 35.62400  25.64200  71.29900  1.000 64.92690  ?  120 LEU D CG  1 
ATOM   6047 C  CD1 . LEU D 1 120 ? 36.56800  24.94500  72.26200  1.000 70.70995  ?  120 LEU D CD1 1 
ATOM   6048 C  CD2 . LEU D 1 120 ? 34.66100  26.55400  72.04600  1.000 61.05780  ?  120 LEU D CD2 1 
ATOM   6049 N  N   . LEU D 1 121 ? 36.39600  27.53100  66.96600  1.000 78.18819  ?  121 LEU D N   1 
ATOM   6050 C  CA  . LEU D 1 121 ? 37.17900  28.27100  65.97800  1.000 75.39287  ?  121 LEU D CA  1 
ATOM   6051 C  C   . LEU D 1 121 ? 36.63200  29.67400  65.75100  1.000 75.71097  ?  121 LEU D C   1 
ATOM   6052 O  O   . LEU D 1 121 ? 37.38000  30.56700  65.33500  1.000 75.33533  ?  121 LEU D O   1 
ATOM   6053 C  CB  . LEU D 1 121 ? 37.24600  27.49400  64.66500  1.000 71.13246  ?  121 LEU D CB  1 
ATOM   6054 C  CG  . LEU D 1 121 ? 38.27400  26.36100  64.69500  1.000 75.21163  ?  121 LEU D CG  1 
ATOM   6055 C  CD1 . LEU D 1 121 ? 38.16200  25.47000  63.46800  1.000 75.70655  ?  121 LEU D CD1 1 
ATOM   6056 C  CD2 . LEU D 1 121 ? 39.67700  26.94000  64.81600  1.000 70.48977  ?  121 LEU D CD2 1 
ATOM   6057 N  N   . HIS D 1 122 ? 35.33700  29.88700  66.00200  1.000 74.75018  ?  122 HIS D N   1 
ATOM   6058 C  CA  . HIS D 1 122 ? 34.79100  31.23900  65.94500  1.000 78.06017  ?  122 HIS D CA  1 
ATOM   6059 C  C   . HIS D 1 122 ? 35.41400  32.13600  67.00700  1.000 87.00509  ?  122 HIS D C   1 
ATOM   6060 O  O   . HIS D 1 122 ? 35.51600  33.35200  66.81100  1.000 89.96402  ?  122 HIS D O   1 
ATOM   6061 C  CB  . HIS D 1 122 ? 33.27300  31.20800  66.11700  1.000 77.75695  ?  122 HIS D CB  1 
ATOM   6062 C  CG  . HIS D 1 122 ? 32.54200  30.57700  64.97300  1.000 76.34842  ?  122 HIS D CG  1 
ATOM   6063 N  ND1 . HIS D 1 122 ? 32.25900  31.25400  63.80700  1.000 86.86317  ?  122 HIS D ND1 1 
ATOM   6064 C  CD2 . HIS D 1 122 ? 32.03200  29.33200  64.82000  1.000 76.24693  ?  122 HIS D CD2 1 
ATOM   6065 C  CE1 . HIS D 1 122 ? 31.60700  30.45300  62.98300  1.000 83.51278  ?  122 HIS D CE1 1 
ATOM   6066 N  NE2 . HIS D 1 122 ? 31.45600  29.28100  63.57400  1.000 79.74924  ?  122 HIS D NE2 1 
ATOM   6067 N  N   . ILE D 1 123 ? 35.83500  31.55800  68.13500  1.000 84.23152  ?  123 ILE D N   1 
ATOM   6068 C  CA  . ILE D 1 123 ? 36.49700  32.34600  69.17000  1.000 84.66897  ?  123 ILE D CA  1 
ATOM   6069 C  C   . ILE D 1 123 ? 37.92900  32.67500  68.77200  1.000 83.76523  ?  123 ILE D C   1 
ATOM   6070 O  O   . ILE D 1 123 ? 38.39200  33.80400  68.97200  1.000 88.48990  ?  123 ILE D O   1 
ATOM   6071 C  CB  . ILE D 1 123 ? 36.44700  31.60900  70.52000  1.000 79.47992  ?  123 ILE D CB  1 
ATOM   6072 C  CG1 . ILE D 1 123 ? 35.00400  31.28600  70.90500  1.000 80.63371  ?  123 ILE D CG1 1 
ATOM   6073 C  CG2 . ILE D 1 123 ? 37.10400  32.44700  71.60300  1.000 81.85751  ?  123 ILE D CG2 1 
ATOM   6074 C  CD1 . ILE D 1 123 ? 34.89300  30.16900  71.91100  1.000 81.62209  ?  123 ILE D CD1 1 
ATOM   6075 N  N   . ARG D 1 124 ? 38.65900  31.70300  68.21300  1.000 78.93480  ?  124 ARG D N   1 
ATOM   6076 C  CA  . ARG D 1 124 ? 40.00900  31.99000  67.73700  1.000 83.09152  ?  124 ARG D CA  1 
ATOM   6077 C  C   . ARG D 1 124 ? 40.00000  33.09400  66.68900  1.000 90.71264  ?  124 ARG D C   1 
ATOM   6078 O  O   . ARG D 1 124 ? 40.95600  33.87300  66.60000  1.000 92.66521  ?  124 ARG D O   1 
ATOM   6079 C  CB  . ARG D 1 124 ? 40.66700  30.72700  67.17800  1.000 77.18582  ?  124 ARG D CB  1 
ATOM   6080 C  CG  . ARG D 1 124 ? 40.99800  29.67800  68.23000  1.000 80.07319  ?  124 ARG D CG  1 
ATOM   6081 C  CD  . ARG D 1 124 ? 41.79400  28.52200  67.63600  1.000 79.14386  ?  124 ARG D CD  1 
ATOM   6082 N  NE  . ARG D 1 124 ? 43.08500  28.95300  67.11100  1.000 77.84380  ?  124 ARG D NE  1 
ATOM   6083 C  CZ  . ARG D 1 124 ? 44.21700  28.93900  67.80200  1.000 83.13845  ?  124 ARG D CZ  1 
ATOM   6084 N  NH1 . ARG D 1 124 ? 44.25600  28.52300  69.05700  1.000 90.29600  ?  124 ARG D NH1 1 
ATOM   6085 N  NH2 . ARG D 1 124 ? 45.33800  29.35600  67.22000  1.000 83.52869  ?  124 ARG D NH2 1 
ATOM   6086 N  N   . ASP D 1 125 ? 38.93300  33.17800  65.88900  1.000 91.39410  ?  125 ASP D N   1 
ATOM   6087 C  CA  . ASP D 1 125 ? 38.77200  34.31200  64.98500  1.000 94.72319  ?  125 ASP D CA  1 
ATOM   6088 C  C   . ASP D 1 125 ? 38.74900  35.62900  65.75300  1.000 89.41159  ?  125 ASP D C   1 
ATOM   6089 O  O   . ASP D 1 125 ? 39.35000  36.61900  65.31900  1.000 85.65096  ?  125 ASP D O   1 
ATOM   6090 C  CB  . ASP D 1 125 ? 37.49700  34.15000  64.15600  1.000 91.30091  ?  125 ASP D CB  1 
ATOM   6091 C  CG  . ASP D 1 125 ? 37.62600  33.08100  63.08700  1.000 95.47395  ?  125 ASP D CG  1 
ATOM   6092 O  OD1 . ASP D 1 125 ? 38.75700  32.60700  62.84900  1.000 96.39542  ?  125 ASP D OD1 1 
ATOM   6093 O  OD2 . ASP D 1 125 ? 36.59500  32.71500  62.48300  1.000 94.95100  -1 125 ASP D OD2 1 
ATOM   6094 N  N   . ILE D 1 126 ? 38.06300  35.66000  66.89800  1.000 87.57960  ?  126 ILE D N   1 
ATOM   6095 C  CA  . ILE D 1 126 ? 38.04500  36.86900  67.71700  1.000 90.46777  ?  126 ILE D CA  1 
ATOM   6096 C  C   . ILE D 1 126 ? 39.39800  37.08900  68.38000  1.000 87.23255  ?  126 ILE D C   1 
ATOM   6097 O  O   . ILE D 1 126 ? 39.77500  38.22900  68.68000  1.000 79.81842  ?  126 ILE D O   1 
ATOM   6098 C  CB  . ILE D 1 126 ? 36.91100  36.78900  68.75700  1.000 90.22906  ?  126 ILE D CB  1 
ATOM   6099 C  CG1 . ILE D 1 126 ? 35.57600  36.50300  68.06900  1.000 94.27266  ?  126 ILE D CG1 1 
ATOM   6100 C  CG2 . ILE D 1 126 ? 36.81700  38.07900  69.56100  1.000 85.52808  ?  126 ILE D CG2 1 
ATOM   6101 C  CD1 . ILE D 1 126 ? 34.41100  36.40800  69.02600  1.000 91.15486  ?  126 ILE D CD1 1 
ATOM   6102 N  N   . TRP D 1 127 ? 40.15600  36.01400  68.60600  1.000 88.71619  ?  127 TRP D N   1 
ATOM   6103 C  CA  . TRP D 1 127 ? 41.44400  36.14600  69.27700  1.000 87.15001  ?  127 TRP D CA  1 
ATOM   6104 C  C   . TRP D 1 127 ? 42.45200  36.84200  68.36700  1.000 90.63473  ?  127 TRP D C   1 
ATOM   6105 O  O   . TRP D 1 127 ? 43.18200  37.73700  68.80800  1.000 91.66715  ?  127 TRP D O   1 
ATOM   6106 C  CB  . TRP D 1 127 ? 41.93600  34.76200  69.71500  1.000 87.52545  ?  127 TRP D CB  1 
ATOM   6107 C  CG  . TRP D 1 127 ? 43.13300  34.75500  70.63100  1.000 93.79701  ?  127 TRP D CG  1 
ATOM   6108 C  CD1 . TRP D 1 127 ? 43.27000  35.45200  71.79800  1.000 94.33511  ?  127 TRP D CD1 1 
ATOM   6109 C  CD2 . TRP D 1 127 ? 44.32300  33.96300  70.49900  1.000 94.71126  ?  127 TRP D CD2 1 
ATOM   6110 N  NE1 . TRP D 1 127 ? 44.48100  35.17100  72.38200  1.000 93.81046  ?  127 TRP D NE1 1 
ATOM   6111 C  CE2 . TRP D 1 127 ? 45.14600  34.25800  71.60700  1.000 95.50264  ?  127 TRP D CE2 1 
ATOM   6112 C  CE3 . TRP D 1 127 ? 44.77900  33.04600  69.54600  1.000 93.27521  ?  127 TRP D CE3 1 
ATOM   6113 C  CZ2 . TRP D 1 127 ? 46.39800  33.67000  71.78600  1.000 97.26706  ?  127 TRP D CZ2 1 
ATOM   6114 C  CZ3 . TRP D 1 127 ? 46.02400  32.46300  69.72700  1.000 96.51670  ?  127 TRP D CZ3 1 
ATOM   6115 C  CH2 . TRP D 1 127 ? 46.81800  32.77800  70.83900  1.000 95.97218  ?  127 TRP D CH2 1 
ATOM   6116 N  N   . PHE D 1 128 ? 42.49300  36.45200  67.08900  1.000 93.50217  ?  128 PHE D N   1 
ATOM   6117 C  CA  . PHE D 1 128 ? 43.41900  37.05900  66.13700  1.000 87.72651  ?  128 PHE D CA  1 
ATOM   6118 C  C   . PHE D 1 128 ? 42.92100  38.40100  65.60900  1.000 82.16138  ?  128 PHE D C   1 
ATOM   6119 O  O   . PHE D 1 128 ? 43.73900  39.26500  65.27400  1.000 75.40714  ?  128 PHE D O   1 
ATOM   6120 C  CB  . PHE D 1 128 ? 43.67900  36.09900  64.97600  1.000 84.90161  ?  128 PHE D CB  1 
ATOM   6121 C  CG  . PHE D 1 128 ? 44.31400  34.80700  65.39600  1.000 87.15882  ?  128 PHE D CG  1 
ATOM   6122 C  CD1 . PHE D 1 128 ? 45.56900  34.80100  65.97900  1.000 91.06075  ?  128 PHE D CD1 1 
ATOM   6123 C  CD2 . PHE D 1 128 ? 43.66100  33.60100  65.21000  1.000 88.56732  ?  128 PHE D CD2 1 
ATOM   6124 C  CE1 . PHE D 1 128 ? 46.16200  33.61600  66.37100  1.000 92.37548  ?  128 PHE D CE1 1 
ATOM   6125 C  CE2 . PHE D 1 128 ? 44.24800  32.41200  65.60100  1.000 89.94468  ?  128 PHE D CE2 1 
ATOM   6126 C  CZ  . PHE D 1 128 ? 45.50100  32.42100  66.18100  1.000 91.43142  ?  128 PHE D CZ  1 
ATOM   6127 N  N   . LYS D 1 129 ? 41.60000  38.58400  65.49900  1.000 76.62982  ?  129 LYS D N   1 
ATOM   6128 C  CA  . LYS D 1 129 ? 41.06500  39.87800  65.07900  1.000 68.16854  ?  129 LYS D CA  1 
ATOM   6129 C  C   . LYS D 1 129 ? 41.55200  40.99900  65.98800  1.000 81.75858  ?  129 LYS D C   1 
ATOM   6130 O  O   . LYS D 1 129 ? 41.93600  42.07500  65.51200  1.000 72.87637  ?  129 LYS D O   1 
ATOM   6131 C  CB  . LYS D 1 129 ? 39.53700  39.84100  65.07100  1.000 66.78450  ?  129 LYS D CB  1 
ATOM   6132 C  CG  . LYS D 1 129 ? 38.89200  41.20400  64.85200  1.000 67.25166  ?  129 LYS D CG  1 
ATOM   6133 C  CD  . LYS D 1 129 ? 37.37600  41.12100  64.87200  1.000 74.71673  ?  129 LYS D CD  1 
ATOM   6134 C  CE  . LYS D 1 129 ? 36.74800  42.47500  64.58000  1.000 81.56358  ?  129 LYS D CE  1 
ATOM   6135 N  NZ  . LYS D 1 129 ? 35.26400  42.39700  64.47900  1.000 80.03182  ?  129 LYS D NZ  1 
ATOM   6136 N  N   . HIS D 1 130 ? 41.55900  40.75800  67.30000  1.000 92.14254  ?  130 HIS D N   1 
ATOM   6137 C  CA  . HIS D 1 130 ? 42.01800  41.72600  68.28700  1.000 84.54818  ?  130 HIS D CA  1 
ATOM   6138 C  C   . HIS D 1 130 ? 43.38900  41.37100  68.85400  1.000 89.87981  ?  130 HIS D C   1 
ATOM   6139 O  O   . HIS D 1 130 ? 43.67000  41.64900  70.02200  1.000 98.56168  ?  130 HIS D O   1 
ATOM   6140 C  CB  . HIS D 1 130 ? 41.00200  41.86000  69.42100  1.000 80.23808  ?  130 HIS D CB  1 
ATOM   6141 C  CG  . HIS D 1 130 ? 39.62200  42.21700  68.96500  1.000 78.51347  ?  130 HIS D CG  1 
ATOM   6142 N  ND1 . HIS D 1 130 ? 39.25700  43.50600  68.63900  1.000 79.70906  ?  130 HIS D ND1 1 
ATOM   6143 C  CD2 . HIS D 1 130 ? 38.51500  41.45800  68.78900  1.000 81.87791  ?  130 HIS D CD2 1 
ATOM   6144 C  CE1 . HIS D 1 130 ? 37.98600  43.52500  68.28000  1.000 86.05703  ?  130 HIS D CE1 1 
ATOM   6145 N  NE2 . HIS D 1 130 ? 37.51200  42.29500  68.36100  1.000 86.36239  ?  130 HIS D NE2 1 
ATOM   6146 N  N   . SER D 1 131 ? 44.24600  40.74000  68.04500  1.000 92.98967  ?  131 SER D N   1 
ATOM   6147 C  CA  . SER D 1 131 ? 45.60000  40.43100  68.49600  1.000 94.45726  ?  131 SER D CA  1 
ATOM   6148 C  C   . SER D 1 131 ? 46.34500  41.68700  68.93300  1.000 101.90865 ?  131 SER D C   1 
ATOM   6149 O  O   . SER D 1 131 ? 47.22700  41.61600  69.79600  1.000 104.22950 ?  131 SER D O   1 
ATOM   6150 C  CB  . SER D 1 131 ? 46.38000  39.70300  67.40100  1.000 95.51091  ?  131 SER D CB  1 
ATOM   6151 O  OG  . SER D 1 131 ? 47.75600  39.62500  67.73400  1.000 89.55042  ?  131 SER D OG  1 
ATOM   6152 N  N   . SER D 1 132 ? 46.01100  42.83700  68.34200  1.000 101.85806 ?  132 SER D N   1 
ATOM   6153 C  CA  . SER D 1 132 ? 46.66000  44.08900  68.72000  1.000 103.22162 ?  132 SER D CA  1 
ATOM   6154 C  C   . SER D 1 132 ? 46.36200  44.44300  70.17300  1.000 106.21436 ?  132 SER D C   1 
ATOM   6155 O  O   . SER D 1 132 ? 47.27900  44.68900  70.96400  1.000 105.45895 ?  132 SER D O   1 
ATOM   6156 C  CB  . SER D 1 132 ? 46.20200  45.21100  67.78700  1.000 101.15620 ?  132 SER D CB  1 
ATOM   6157 O  OG  . SER D 1 132 ? 46.65100  46.47400  68.24300  1.000 105.18511 ?  132 SER D OG  1 
ATOM   6158 N  N   . LEU D 1 133 ? 45.07700  44.48600  70.53500  1.000 107.57168 ?  133 LEU D N   1 
ATOM   6159 C  CA  . LEU D 1 133 ? 44.68000  44.79100  71.90800  1.000 105.36950 ?  133 LEU D CA  1 
ATOM   6160 C  C   . LEU D 1 133 ? 45.34800  43.86700  72.91700  1.000 105.71662 ?  133 LEU D C   1 
ATOM   6161 O  O   . LEU D 1 133 ? 45.99500  44.32400  73.86600  1.000 111.39655 ?  133 LEU D O   1 
ATOM   6162 C  CB  . LEU D 1 133 ? 43.16200  44.68600  72.05000  1.000 102.23814 ?  133 LEU D CB  1 
ATOM   6163 C  CG  . LEU D 1 133 ? 42.67700  44.78200  73.50000  1.000 109.38770 ?  133 LEU D CG  1 
ATOM   6164 C  CD1 . LEU D 1 133 ? 42.20100  46.16400  73.87000  1.000 117.11360 ?  133 LEU D CD1 1 
ATOM   6165 C  CD2 . LEU D 1 133 ? 41.59100  43.75300  73.76000  1.000 105.77692 ?  133 LEU D CD2 1 
ATOM   6166 N  N   . LEU D 1 134 ? 45.19100  42.55600  72.72700  1.000 102.89335 ?  134 LEU D N   1 
ATOM   6167 C  CA  . LEU D 1 134 ? 45.68100  41.58800  73.70200  1.000 108.18828 ?  134 LEU D CA  1 
ATOM   6168 C  C   . LEU D 1 134 ? 47.18800  41.68000  73.91000  1.000 112.81709 ?  134 LEU D C   1 
ATOM   6169 O  O   . LEU D 1 134 ? 47.67800  41.39100  75.00900  1.000 118.66600 ?  134 LEU D O   1 
ATOM   6170 C  CB  . LEU D 1 134 ? 45.28200  40.18100  73.25800  1.000 105.98801 ?  134 LEU D CB  1 
ATOM   6171 C  CG  . LEU D 1 134 ? 43.78000  40.00100  73.00800  1.000 103.36532 ?  134 LEU D CG  1 
ATOM   6172 C  CD1 . LEU D 1 134 ? 43.52600  38.86800  72.02500  1.000 99.16067  ?  134 LEU D CD1 1 
ATOM   6173 C  CD2 . LEU D 1 134 ? 43.03200  39.76300  74.31000  1.000 105.01907 ?  134 LEU D CD2 1 
ATOM   6174 N  N   . GLY D 1 135 ? 47.94000  42.07500  72.88100  1.000 110.91247 ?  135 GLY D N   1 
ATOM   6175 C  CA  . GLY D 1 135 ? 49.37900  42.21400  73.04900  1.000 114.04620 ?  135 GLY D CA  1 
ATOM   6176 C  C   . GLY D 1 135 ? 49.76100  43.35400  73.97600  1.000 114.03913 ?  135 GLY D C   1 
ATOM   6177 O  O   . GLY D 1 135 ? 50.68600  43.22700  74.78300  1.000 110.35137 ?  135 GLY D O   1 
ATOM   6178 N  N   . GLU D 1 136 ? 49.05100  44.48100  73.87700  1.000 115.28387 ?  136 GLU D N   1 
ATOM   6179 C  CA  . GLU D 1 136 ? 49.34500  45.66900  74.67400  1.000 119.46884 ?  136 GLU D CA  1 
ATOM   6180 C  C   . GLU D 1 136 ? 48.93000  45.52800  76.13400  1.000 121.12467 ?  136 GLU D C   1 
ATOM   6181 O  O   . GLU D 1 136 ? 49.37400  46.32600  76.96800  1.000 119.36847 ?  136 GLU D O   1 
ATOM   6182 C  CB  . GLU D 1 136 ? 48.67100  46.89000  74.03200  1.000 118.56003 ?  136 GLU D CB  1 
ATOM   6183 C  CG  . GLU D 1 136 ? 48.88500  48.21900  74.75100  1.000 125.66891 ?  136 GLU D CG  1 
ATOM   6184 C  CD  . GLU D 1 136 ? 48.05400  49.34200  74.16200  1.000 131.27990 ?  136 GLU D CD  1 
ATOM   6185 O  OE1 . GLU D 1 136 ? 47.42100  49.12500  73.10700  1.000 131.77660 ?  136 GLU D OE1 1 
ATOM   6186 O  OE2 . GLU D 1 136 ? 48.02600  50.43900  74.75800  1.000 134.99828 -1 136 GLU D OE2 1 
ATOM   6187 N  N   . MET D 1 137 ? 48.14900  44.52100  76.47700  1.000 118.84741 ?  137 MET D N   1 
ATOM   6188 C  CA  . MET D 1 137 ? 47.64700  44.37000  77.83300  1.000 117.23107 ?  137 MET D CA  1 
ATOM   6189 C  C   . MET D 1 137 ? 48.47000  43.35800  78.61500  1.000 119.39960 ?  137 MET D C   1 
ATOM   6190 O  O   . MET D 1 137 ? 49.17400  42.52700  78.03300  1.000 115.90933 ?  137 MET D O   1 
ATOM   6191 C  CB  . MET D 1 137 ? 46.17600  43.94600  77.82100  1.000 112.26671 ?  137 MET D CB  1 
ATOM   6192 C  CG  . MET D 1 137 ? 45.23300  44.94000  77.17400  1.000 112.31311 ?  137 MET D CG  1 
ATOM   6193 S  SD  . MET D 1 137 ? 43.55300  44.29600  77.20000  1.000 123.96487 ?  137 MET D SD  1 
ATOM   6194 C  CE  . MET D 1 137 ? 43.89600  42.53800  77.20600  1.000 113.07259 ?  137 MET D CE  1 
ATOM   6195 N  N   . PRO D 1 138 ? 48.41100  43.41000  79.94600  1.000 121.79274 ?  138 PRO D N   1 
ATOM   6196 C  CA  . PRO D 1 138 ? 49.16700  42.44500  80.75100  1.000 121.38463 ?  138 PRO D CA  1 
ATOM   6197 C  C   . PRO D 1 138 ? 48.71300  41.01500  80.50600  1.000 123.10164 ?  138 PRO D C   1 
ATOM   6198 O  O   . PRO D 1 138 ? 47.52800  40.73800  80.30900  1.000 121.75035 ?  138 PRO D O   1 
ATOM   6199 C  CB  . PRO D 1 138 ? 48.87400  42.88400  82.18900  1.000 116.68051 ?  138 PRO D CB  1 
ATOM   6200 C  CG  . PRO D 1 138 ? 48.51000  44.31600  82.07400  1.000 110.92546 ?  138 PRO D CG  1 
ATOM   6201 C  CD  . PRO D 1 138 ? 47.79200  44.45600  80.77800  1.000 113.47634 ?  138 PRO D CD  1 
ATOM   6202 N  N   . GLN D 1 139 ? 49.69700  40.11100  80.50100  1.000 122.98559 ?  139 GLN D N   1 
ATOM   6203 C  CA  . GLN D 1 139 ? 49.47900  38.71600  80.13100  1.000 120.92927 ?  139 GLN D CA  1 
ATOM   6204 C  C   . GLN D 1 139 ? 48.32100  38.07700  80.89500  1.000 123.07082 ?  139 GLN D C   1 
ATOM   6205 O  O   . GLN D 1 139 ? 47.47300  37.40400  80.30000  1.000 119.05277 ?  139 GLN D O   1 
ATOM   6206 C  CB  . GLN D 1 139 ? 50.77900  37.93500  80.34200  1.000 119.82743 ?  139 GLN D CB  1 
ATOM   6207 C  CG  . GLN D 1 139 ? 50.79700  36.52200  79.77800  1.000 117.40690 ?  139 GLN D CG  1 
ATOM   6208 C  CD  . GLN D 1 139 ? 50.11300  35.52100  80.68600  1.000 120.63075 ?  139 GLN D CD  1 
ATOM   6209 O  OE1 . GLN D 1 139 ? 49.20200  34.80600  80.27200  1.000 116.68472 ?  139 GLN D OE1 1 
ATOM   6210 N  NE2 . GLN D 1 139 ? 50.55500  35.46600  81.93700  1.000 119.87156 ?  139 GLN D NE2 1 
ATOM   6211 N  N   . GLU D 1 140 ? 48.27600  38.25900  82.21900  1.000 120.87816 ?  140 GLU D N   1 
ATOM   6212 C  CA  . GLU D 1 140 ? 47.24900  37.58200  83.01000  1.000 119.52858 ?  140 GLU D CA  1 
ATOM   6213 C  C   . GLU D 1 140 ? 45.83500  38.00100  82.60700  1.000 122.37640 ?  140 GLU D C   1 
ATOM   6214 O  O   . GLU D 1 140 ? 44.91200  37.17900  82.64300  1.000 122.21646 ?  140 GLU D O   1 
ATOM   6215 C  CB  . GLU D 1 140 ? 47.47600  37.78400  84.51200  1.000 122.68242 ?  140 GLU D CB  1 
ATOM   6216 C  CG  . GLU D 1 140 ? 48.01600  39.12200  84.97300  1.000 124.45582 ?  140 GLU D CG  1 
ATOM   6217 C  CD  . GLU D 1 140 ? 49.53500  39.15700  84.99100  1.000 125.02794 ?  140 GLU D CD  1 
ATOM   6218 O  OE1 . GLU D 1 140 ? 50.16500  38.48200  84.14900  1.000 125.08318 ?  140 GLU D OE1 1 
ATOM   6219 O  OE2 . GLU D 1 140 ? 50.09800  39.81600  85.89000  1.000 112.40374 -1 140 GLU D OE2 1 
ATOM   6220 N  N   . ARG D 1 141 ? 45.63700  39.26300  82.21800  1.000 121.03618 ?  141 ARG D N   1 
ATOM   6221 C  CA  . ARG D 1 141 ? 44.29800  39.76200  81.90900  1.000 118.87623 ?  141 ARG D CA  1 
ATOM   6222 C  C   . ARG D 1 141 ? 43.90000  39.58000  80.45200  1.000 117.11264 ?  141 ARG D C   1 
ATOM   6223 O  O   . ARG D 1 141 ? 43.01900  40.30000  79.97100  1.000 117.07173 ?  141 ARG D O   1 
ATOM   6224 C  CB  . ARG D 1 141 ? 44.14000  41.23500  82.28500  1.000 117.46512 ?  141 ARG D CB  1 
ATOM   6225 C  CG  . ARG D 1 141 ? 44.28100  41.54700  83.74400  1.000 124.54075 ?  141 ARG D CG  1 
ATOM   6226 C  CD  . ARG D 1 141 ? 44.14300  43.03600  83.98100  1.000 124.18872 ?  141 ARG D CD  1 
ATOM   6227 N  NE  . ARG D 1 141 ? 42.85400  43.57100  83.55900  1.000 132.04638 ?  141 ARG D NE  1 
ATOM   6228 C  CZ  . ARG D 1 141 ? 42.68500  44.38500  82.52600  1.000 130.76735 ?  141 ARG D CZ  1 
ATOM   6229 N  NH1 . ARG D 1 141 ? 43.70600  44.77900  81.78300  1.000 122.25371 ?  141 ARG D NH1 1 
ATOM   6230 N  NH2 . ARG D 1 141 ? 41.46000  44.80500  82.22400  1.000 130.61554 ?  141 ARG D NH2 1 
ATOM   6231 N  N   . ARG D 1 142 ? 44.51300  38.64300  79.73600  1.000 110.99271 ?  142 ARG D N   1 
ATOM   6232 C  CA  . ARG D 1 142 ? 44.15200  38.50200  78.33400  1.000 110.98781 ?  142 ARG D CA  1 
ATOM   6233 C  C   . ARG D 1 142 ? 42.97200  37.55100  78.15700  1.000 108.51544 ?  142 ARG D C   1 
ATOM   6234 O  O   . ARG D 1 142 ? 42.04400  37.85100  77.40000  1.000 104.85066 ?  142 ARG D O   1 
ATOM   6235 C  CB  . ARG D 1 142 ? 45.36100  38.02600  77.52600  1.000 113.51931 ?  142 ARG D CB  1 
ATOM   6236 C  CG  . ARG D 1 142 ? 46.29400  39.15000  77.11200  1.000 114.68719 ?  142 ARG D CG  1 
ATOM   6237 C  CD  . ARG D 1 142 ? 47.62100  38.61800  76.60000  1.000 115.14516 ?  142 ARG D CD  1 
ATOM   6238 N  NE  . ARG D 1 142 ? 48.58400  39.69500  76.40000  1.000 118.75591 ?  142 ARG D NE  1 
ATOM   6239 C  CZ  . ARG D 1 142 ? 49.89100  39.52000  76.26200  1.000 119.86241 ?  142 ARG D CZ  1 
ATOM   6240 N  NH1 . ARG D 1 142 ? 50.43600  38.31500  76.29000  1.000 117.21196 ?  142 ARG D NH1 1 
ATOM   6241 N  NH2 . ARG D 1 142 ? 50.67200  40.58300  76.08600  1.000 120.95046 ?  142 ARG D NH2 1 
ATOM   6242 N  N   . LEU D 1 143 ? 42.98800  36.40900  78.85100  1.000 104.34287 ?  143 LEU D N   1 
ATOM   6243 C  CA  . LEU D 1 143 ? 41.88300  35.46200  78.72800  1.000 98.47680  ?  143 LEU D CA  1 
ATOM   6244 C  C   . LEU D 1 143 ? 40.57600  36.04700  79.25000  1.000 95.44885  ?  143 LEU D C   1 
ATOM   6245 O  O   . LEU D 1 143 ? 39.50400  35.73200  78.72200  1.000 94.93905  ?  143 LEU D O   1 
ATOM   6246 C  CB  . LEU D 1 143 ? 42.21100  34.15800  79.45200  1.000 88.01449  ?  143 LEU D CB  1 
ATOM   6247 C  CG  . LEU D 1 143 ? 43.30700  33.31900  78.79900  1.000 95.05662  ?  143 LEU D CG  1 
ATOM   6248 C  CD1 . LEU D 1 143 ? 43.43100  31.96600  79.47900  1.000 85.44433  ?  143 LEU D CD1 1 
ATOM   6249 C  CD2 . LEU D 1 143 ? 43.01900  33.15700  77.32400  1.000 92.01948  ?  143 LEU D CD2 1 
ATOM   6250 N  N   . ASP D 1 144 ? 40.63600  36.89000  80.28300  1.000 96.17705  ?  144 ASP D N   1 
ATOM   6251 C  CA  . ASP D 1 144 ? 39.42200  37.55100  80.74700  1.000 98.87827  ?  144 ASP D CA  1 
ATOM   6252 C  C   . ASP D 1 144 ? 38.94400  38.58600  79.73700  1.000 97.60514  ?  144 ASP D C   1 
ATOM   6253 O  O   . ASP D 1 144 ? 37.73500  38.76600  79.54800  1.000 95.55025  ?  144 ASP D O   1 
ATOM   6254 C  CB  . ASP D 1 144 ? 39.65600  38.20200  82.11100  1.000 97.27365  ?  144 ASP D CB  1 
ATOM   6255 C  CG  . ASP D 1 144 ? 39.65700  37.19600  83.24600  1.000 102.11995 ?  144 ASP D CG  1 
ATOM   6256 O  OD1 . ASP D 1 144 ? 39.67900  35.97900  82.96600  1.000 101.36177 ?  144 ASP D OD1 1 
ATOM   6257 O  OD2 . ASP D 1 144 ? 39.63100  37.62200  84.42100  1.000 104.15658 -1 144 ASP D OD2 1 
ATOM   6258 N  N   . THR D 1 145 ? 39.87800  39.27800  79.08300  1.000 98.66551  ?  145 THR D N   1 
ATOM   6259 C  CA  . THR D 1 145 ? 39.49900  40.29300  78.10600  1.000 100.96582 ?  145 THR D CA  1 
ATOM   6260 C  C   . THR D 1 145 ? 38.89400  39.66300  76.85700  1.000 94.63902  ?  145 THR D C   1 
ATOM   6261 O  O   . THR D 1 145 ? 37.89100  40.16000  76.33200  1.000 88.11789  ?  145 THR D O   1 
ATOM   6262 C  CB  . THR D 1 145 ? 40.70500  41.15200  77.74300  1.000 103.27008 ?  145 THR D CB  1 
ATOM   6263 O  OG1 . THR D 1 145 ? 41.31800  41.64200  78.94200  1.000 106.20789 ?  145 THR D OG1 1 
ATOM   6264 C  CG2 . THR D 1 145 ? 40.27200  42.33300  76.88800  1.000 101.87134 ?  145 THR D CG2 1 
ATOM   6265 N  N   . LEU D 1 146 ? 39.50600  38.58700  76.34900  1.000 94.22648  ?  146 LEU D N   1 
ATOM   6266 C  CA  . LEU D 1 146 ? 38.91100  37.85900  75.23100  1.000 94.33504  ?  146 LEU D CA  1 
ATOM   6267 C  C   . LEU D 1 146 ? 37.48400  37.44100  75.55300  1.000 89.63330  ?  146 LEU D C   1 
ATOM   6268 O  O   . LEU D 1 146 ? 36.59700  37.50800  74.69300  1.000 90.67474  ?  146 LEU D O   1 
ATOM   6269 C  CB  . LEU D 1 146 ? 39.75700  36.63500  74.87900  1.000 91.11428  ?  146 LEU D CB  1 
ATOM   6270 C  CG  . LEU D 1 146 ? 39.13000  35.72500  73.81900  1.000 84.77419  ?  146 LEU D CG  1 
ATOM   6271 C  CD1 . LEU D 1 146 ? 38.93200  36.47300  72.51000  1.000 87.90420  ?  146 LEU D CD1 1 
ATOM   6272 C  CD2 . LEU D 1 146 ? 39.96900  34.48000  73.60300  1.000 83.66169  ?  146 LEU D CD2 1 
ATOM   6273 N  N   . CYS D 1 147 ? 37.24600  37.00400  76.79200  1.000 92.51487  ?  147 CYS D N   1 
ATOM   6274 C  CA  . CYS D 1 147 ? 35.88800  36.69300  77.22300  1.000 93.03531  ?  147 CYS D CA  1 
ATOM   6275 C  C   . CYS D 1 147 ? 34.98500  37.91000  77.08100  1.000 90.80796  ?  147 CYS D C   1 
ATOM   6276 O  O   . CYS D 1 147 ? 33.82300  37.78900  76.67700  1.000 85.76752  ?  147 CYS D O   1 
ATOM   6277 C  CB  . CYS D 1 147 ? 35.90000  36.19300  78.66700  1.000 86.74275  ?  147 CYS D CB  1 
ATOM   6278 S  SG  . CYS D 1 147 ? 34.26300  35.89600  79.37300  1.000 93.61899  ?  147 CYS D SG  1 
ATOM   6279 N  N   . GLU D 1 148 ? 35.50600  39.09500  77.40700  1.000 95.28792  ?  148 GLU D N   1 
ATOM   6280 C  CA  . GLU D 1 148 ? 34.73700  40.31800  77.20800  1.000 94.55451  ?  148 GLU D CA  1 
ATOM   6281 C  C   . GLU D 1 148 ? 34.66000  40.68300  75.73100  1.000 93.11723  ?  148 GLU D C   1 
ATOM   6282 O  O   . GLU D 1 148 ? 33.62200  41.16300  75.26000  1.000 94.71797  ?  148 GLU D O   1 
ATOM   6283 C  CB  . GLU D 1 148 ? 35.35800  41.45800  78.01400  1.000 97.40103  ?  148 GLU D CB  1 
ATOM   6284 C  CG  . GLU D 1 148 ? 35.41500  41.18900  79.50700  1.000 100.85924 ?  148 GLU D CG  1 
ATOM   6285 C  CD  . GLU D 1 148 ? 36.09000  42.30700  80.27400  1.000 104.86589 ?  148 GLU D CD  1 
ATOM   6286 O  OE1 . GLU D 1 148 ? 36.62900  43.23000  79.62800  1.000 107.21683 ?  148 GLU D OE1 1 
ATOM   6287 O  OE2 . GLU D 1 148 ? 36.08500  42.25900  81.52200  1.000 101.93240 -1 148 GLU D OE2 1 
ATOM   6288 N  N   . LEU D 1 149 ? 35.74600  40.46500  74.98300  1.000 92.25735  ?  149 LEU D N   1 
ATOM   6289 C  CA  . LEU D 1 149 ? 35.70300  40.69800  73.54300  1.000 90.25851  ?  149 LEU D CA  1 
ATOM   6290 C  C   . LEU D 1 149 ? 34.68800  39.78300  72.87600  1.000 87.16191  ?  149 LEU D C   1 
ATOM   6291 O  O   . LEU D 1 149 ? 33.91200  40.22100  72.01900  1.000 89.32178  ?  149 LEU D O   1 
ATOM   6292 C  CB  . LEU D 1 149 ? 37.08500  40.49000  72.92100  1.000 85.21376  ?  149 LEU D CB  1 
ATOM   6293 C  CG  . LEU D 1 149 ? 38.16900  41.54200  73.14600  1.000 81.77865  ?  149 LEU D CG  1 
ATOM   6294 C  CD1 . LEU D 1 149 ? 39.52100  40.98200  72.73400  1.000 78.91289  ?  149 LEU D CD1 1 
ATOM   6295 C  CD2 . LEU D 1 149 ? 37.85200  42.81400  72.37700  1.000 74.80005  ?  149 LEU D CD2 1 
ATOM   6296 N  N   . ASN D 1 150 ? 34.68200  38.50500  73.26300  1.000 85.00204  ?  150 ASN D N   1 
ATOM   6297 C  CA  . ASN D 1 150 ? 33.75800  37.54500  72.67000  1.000 84.92434  ?  150 ASN D CA  1 
ATOM   6298 C  C   . ASN D 1 150 ? 32.31100  37.98000  72.86400  1.000 83.14384  ?  150 ASN D C   1 
ATOM   6299 O  O   . ASN D 1 150 ? 31.49900  37.88100  71.93800  1.000 86.65345  ?  150 ASN D O   1 
ATOM   6300 C  CB  . ASN D 1 150 ? 34.00000  36.15900  73.26900  1.000 78.03566  ?  150 ASN D CB  1 
ATOM   6301 C  CG  . ASN D 1 150 ? 33.12300  35.09100  72.64900  1.000 81.60061  ?  150 ASN D CG  1 
ATOM   6302 O  OD1 . ASN D 1 150 ? 32.72200  35.19400  71.49000  1.000 88.08627  ?  150 ASN D OD1 1 
ATOM   6303 N  ND2 . ASN D 1 150 ? 32.83300  34.04700  73.41600  1.000 78.94472  ?  150 ASN D ND2 1 
ATOM   6304 N  N   . VAL D 1 151 ? 31.97200  38.47900  74.05500  1.000 86.18599  ?  151 VAL D N   1 
ATOM   6305 C  CA  . VAL D 1 151 ? 30.59700  38.89700  74.31500  1.000 88.57519  ?  151 VAL D CA  1 
ATOM   6306 C  C   . VAL D 1 151 ? 30.23400  40.11100  73.46700  1.000 85.17859  ?  151 VAL D C   1 
ATOM   6307 O  O   . VAL D 1 151 ? 29.12100  40.20300  72.93600  1.000 81.03396  ?  151 VAL D O   1 
ATOM   6308 C  CB  . VAL D 1 151 ? 30.39400  39.17300  75.81600  1.000 79.84072  ?  151 VAL D CB  1 
ATOM   6309 C  CG1 . VAL D 1 151 ? 29.00800  39.74900  76.07100  1.000 77.21344  ?  151 VAL D CG1 1 
ATOM   6310 C  CG2 . VAL D 1 151 ? 30.59600  37.90100  76.61700  1.000 80.43400  ?  151 VAL D CG2 1 
ATOM   6311 N  N   . MET D 1 152 ? 31.16600  41.05600  73.31700  1.000 88.09694  ?  152 MET D N   1 
ATOM   6312 C  CA  . MET D 1 152 ? 30.89600  42.22900  72.49000  1.000 90.18074  ?  152 MET D CA  1 
ATOM   6313 C  C   . MET D 1 152 ? 30.69800  41.84500  71.03100  1.000 87.31009  ?  152 MET D C   1 
ATOM   6314 O  O   . MET D 1 152 ? 29.82700  42.39900  70.34900  1.000 86.61052  ?  152 MET D O   1 
ATOM   6315 C  CB  . MET D 1 152 ? 32.02600  43.25100  72.62500  1.000 95.15810  ?  152 MET D CB  1 
ATOM   6316 C  CG  . MET D 1 152 ? 32.25800  43.75500  74.03900  1.000 93.97872  ?  152 MET D CG  1 
ATOM   6317 S  SD  . MET D 1 152 ? 33.59300  44.96500  74.12100  1.000 102.01359 ?  152 MET D SD  1 
ATOM   6318 C  CE  . MET D 1 152 ? 33.69000  45.24300  75.88800  1.000 99.48059  ?  152 MET D CE  1 
ATOM   6319 N  N   . GLU D 1 153 ? 31.49900  40.90200  70.53000  1.000 86.79027  ?  153 GLU D N   1 
ATOM   6320 C  CA  . GLU D 1 153 ? 31.36100  40.48400  69.14000  1.000 86.08442  ?  153 GLU D CA  1 
ATOM   6321 C  C   . GLU D 1 153 ? 30.01800  39.81000  68.89000  1.000 84.01945  ?  153 GLU D C   1 
ATOM   6322 O  O   . GLU D 1 153 ? 29.39300  40.03000  67.84500  1.000 83.62217  ?  153 GLU D O   1 
ATOM   6323 C  CB  . GLU D 1 153 ? 32.50900  39.55200  68.75100  1.000 82.20684  ?  153 GLU D CB  1 
ATOM   6324 C  CG  . GLU D 1 153 ? 33.87700  40.20700  68.80300  1.000 84.29269  ?  153 GLU D CG  1 
ATOM   6325 C  CD  . GLU D 1 153 ? 34.09700  41.19300  67.67300  1.000 93.97523  ?  153 GLU D CD  1 
ATOM   6326 O  OE1 . GLU D 1 153 ? 33.30000  41.18800  66.71000  1.000 96.77102  ?  153 GLU D OE1 1 
ATOM   6327 O  OE2 . GLU D 1 153 ? 35.06800  41.97700  67.74900  1.000 95.67091  -1 153 GLU D OE2 1 
ATOM   6328 N  N   . GLN D 1 154 ? 29.55600  38.98500  69.83300  1.000 83.28832  ?  154 GLN D N   1 
ATOM   6329 C  CA  . GLN D 1 154 ? 28.27800  38.30500  69.64100  1.000 80.22392  ?  154 GLN D CA  1 
ATOM   6330 C  C   . GLN D 1 154 ? 27.11900  39.29500  69.64300  1.000 80.99792  ?  154 GLN D C   1 
ATOM   6331 O  O   . GLN D 1 154 ? 26.14600  39.12100  68.90000  1.000 80.14457  ?  154 GLN D O   1 
ATOM   6332 C  CB  . GLN D 1 154 ? 28.07200  37.23500  70.71300  1.000 78.90921  ?  154 GLN D CB  1 
ATOM   6333 C  CG  . GLN D 1 154 ? 29.19800  36.21400  70.82200  1.000 79.98735  ?  154 GLN D CG  1 
ATOM   6334 C  CD  . GLN D 1 154 ? 29.73600  35.76900  69.47400  1.000 82.47118  ?  154 GLN D CD  1 
ATOM   6335 O  OE1 . GLN D 1 154 ? 28.99200  35.28800  68.61900  1.000 81.58303  ?  154 GLN D OE1 1 
ATOM   6336 N  NE2 . GLN D 1 154 ? 31.04300  35.91400  69.28500  1.000 80.56616  ?  154 GLN D NE2 1 
ATOM   6337 N  N   . VAL D 1 155 ? 27.20100  40.33400  70.47900  1.000 80.64175  ?  155 VAL D N   1 
ATOM   6338 C  CA  . VAL D 1 155 ? 26.21500  41.41100  70.42700  1.000 82.55533  ?  155 VAL D CA  1 
ATOM   6339 C  C   . VAL D 1 155 ? 26.25100  42.08900  69.06300  1.000 82.60798  ?  155 VAL D C   1 
ATOM   6340 O  O   . VAL D 1 155 ? 25.20700  42.41500  68.48300  1.000 76.33756  ?  155 VAL D O   1 
ATOM   6341 C  CB  . VAL D 1 155 ? 26.46100  42.41400  71.57000  1.000 76.55457  ?  155 VAL D CB  1 
ATOM   6342 C  CG1 . VAL D 1 155 ? 25.57300  43.63800  71.41300  1.000 77.93348  ?  155 VAL D CG1 1 
ATOM   6343 C  CG2 . VAL D 1 155 ? 26.23700  41.74900  72.91900  1.000 80.83212  ?  155 VAL D CG2 1 
ATOM   6344 N  N   . TYR D 1 156 ? 27.45600  42.31000  68.53200  1.000 79.40604  ?  156 TYR D N   1 
ATOM   6345 C  CA  . TYR D 1 156 ? 27.60500  42.86700  67.19100  1.000 84.66894  ?  156 TYR D CA  1 
ATOM   6346 C  C   . TYR D 1 156 ? 26.95100  41.96700  66.15000  1.000 85.49641  ?  156 TYR D C   1 
ATOM   6347 O  O   . TYR D 1 156 ? 26.16300  42.42900  65.31500  1.000 81.31124  ?  156 TYR D O   1 
ATOM   6348 C  CB  . TYR D 1 156 ? 29.09200  43.05800  66.88600  1.000 88.11698  ?  156 TYR D CB  1 
ATOM   6349 C  CG  . TYR D 1 156 ? 29.40700  44.06500  65.80600  1.000 94.01930  ?  156 TYR D CG  1 
ATOM   6350 C  CD1 . TYR D 1 156 ? 28.82100  45.32300  65.80600  1.000 94.03758  ?  156 TYR D CD1 1 
ATOM   6351 C  CD2 . TYR D 1 156 ? 30.31600  43.76400  64.79800  1.000 94.20824  ?  156 TYR D CD2 1 
ATOM   6352 C  CE1 . TYR D 1 156 ? 29.11900  46.24800  64.82200  1.000 97.20330  ?  156 TYR D CE1 1 
ATOM   6353 C  CE2 . TYR D 1 156 ? 30.62200  44.68200  63.81300  1.000 90.71846  ?  156 TYR D CE2 1 
ATOM   6354 C  CZ  . TYR D 1 156 ? 30.02000  45.92200  63.82900  1.000 97.05004  ?  156 TYR D CZ  1 
ATOM   6355 O  OH  . TYR D 1 156 ? 30.32100  46.83800  62.84800  1.000 100.44262 ?  156 TYR D OH  1 
ATOM   6356 N  N   . ASN D 1 157 ? 27.27400  40.67200  66.18500  1.000 81.20961  ?  157 ASN D N   1 
ATOM   6357 C  CA  . ASN D 1 157 ? 26.66800  39.72100  65.26000  1.000 68.94615  ?  157 ASN D CA  1 
ATOM   6358 C  C   . ASN D 1 157 ? 25.15200  39.70200  65.40400  1.000 70.24587  ?  157 ASN D C   1 
ATOM   6359 O  O   . ASN D 1 157 ? 24.42800  39.65700  64.40400  1.000 79.65259  ?  157 ASN D O   1 
ATOM   6360 C  CB  . ASN D 1 157 ? 27.25400  38.32800  65.48600  1.000 66.06328  ?  157 ASN D CB  1 
ATOM   6361 C  CG  . ASN D 1 157 ? 28.75800  38.29700  65.30500  1.000 66.26305  ?  157 ASN D CG  1 
ATOM   6362 O  OD1 . ASN D 1 157 ? 29.36000  39.27800  64.86800  1.000 72.33454  ?  157 ASN D OD1 1 
ATOM   6363 N  ND2 . ASN D 1 157 ? 29.37200  37.16300  65.62500  1.000 62.43853  ?  157 ASN D ND2 1 
ATOM   6364 N  N   . LEU D 1 158 ? 24.65600  39.70900  66.64400  1.000 77.92284  ?  158 LEU D N   1 
ATOM   6365 C  CA  . LEU D 1 158 ? 23.21500  39.68200  66.86800  1.000 78.77653  ?  158 LEU D CA  1 
ATOM   6366 C  C   . LEU D 1 158 ? 22.53200  40.85500  66.17900  1.000 76.76341  ?  158 LEU D C   1 
ATOM   6367 O  O   . LEU D 1 158 ? 21.49000  40.68600  65.53700  1.000 78.88362  ?  158 LEU D O   1 
ATOM   6368 C  CB  . LEU D 1 158 ? 22.92100  39.69100  68.36900  1.000 76.67565  ?  158 LEU D CB  1 
ATOM   6369 C  CG  . LEU D 1 158 ? 21.45200  39.73700  68.80000  1.000 72.30627  ?  158 LEU D CG  1 
ATOM   6370 C  CD1 . LEU D 1 158 ? 20.64100  38.66400  68.09100  1.000 79.11945  ?  158 LEU D CD1 1 
ATOM   6371 C  CD2 . LEU D 1 158 ? 21.33200  39.59000  70.30700  1.000 77.35698  ?  158 LEU D CD2 1 
ATOM   6372 N  N   . GLY D 1 159 ? 23.11100  42.05200  66.28800  1.000 80.01693  ?  159 GLY D N   1 
ATOM   6373 C  CA  . GLY D 1 159 ? 22.53400  43.21800  65.64600  1.000 81.32953  ?  159 GLY D CA  1 
ATOM   6374 C  C   . GLY D 1 159 ? 22.59300  43.18300  64.13300  1.000 86.31316  ?  159 GLY D C   1 
ATOM   6375 O  O   . GLY D 1 159 ? 21.81800  43.88700  63.47700  1.000 86.92038  ?  159 GLY D O   1 
ATOM   6376 N  N   . HIS D 1 160 ? 23.48700  42.37100  63.56500  1.000 90.14696  ?  160 HIS D N   1 
ATOM   6377 C  CA  . HIS D 1 160 ? 23.65200  42.28500  62.12000  1.000 78.80161  ?  160 HIS D CA  1 
ATOM   6378 C  C   . HIS D 1 160 ? 22.69600  41.30100  61.46200  1.000 79.23139  ?  160 HIS D C   1 
ATOM   6379 O  O   . HIS D 1 160 ? 22.49800  41.37400  60.24300  1.000 86.17867  ?  160 HIS D O   1 
ATOM   6380 C  CB  . HIS D 1 160 ? 25.08700  41.87600  61.77900  1.000 72.56563  ?  160 HIS D CB  1 
ATOM   6381 C  CG  . HIS D 1 160 ? 26.08600  42.97700  61.94400  1.000 79.69676  ?  160 HIS D CG  1 
ATOM   6382 N  ND1 . HIS D 1 160 ? 25.75700  44.30900  61.81800  1.000 82.91414  ?  160 HIS D ND1 1 
ATOM   6383 C  CD2 . HIS D 1 160 ? 27.40800  42.94200  62.23500  1.000 84.69465  ?  160 HIS D CD2 1 
ATOM   6384 C  CE1 . HIS D 1 160 ? 26.83400  45.04700  62.01900  1.000 86.23528  ?  160 HIS D CE1 1 
ATOM   6385 N  NE2 . HIS D 1 160 ? 27.84900  44.24200  62.27400  1.000 89.07456  ?  160 HIS D NE2 1 
ATOM   6386 N  N   . SER D 1 161 ? 22.11900  40.38000  62.22900  1.000 75.58704  ?  161 SER D N   1 
ATOM   6387 C  CA  . SER D 1 161 ? 21.19600  39.39900  61.67900  1.000 78.77881  ?  161 SER D CA  1 
ATOM   6388 C  C   . SER D 1 161 ? 19.98800  40.08400  61.04700  1.000 77.69805  ?  161 SER D C   1 
ATOM   6389 O  O   . SER D 1 161 ? 19.64800  41.22600  61.36300  1.000 78.42571  ?  161 SER D O   1 
ATOM   6390 C  CB  . SER D 1 161 ? 20.72700  38.44000  62.77300  1.000 80.67221  ?  161 SER D CB  1 
ATOM   6391 O  OG  . SER D 1 161 ? 19.69600  39.02900  63.55000  1.000 73.49839  ?  161 SER D OG  1 
ATOM   6392 N  N   . THR D 1 162 ? 19.33000  39.36100  60.13900  1.000 73.07781  ?  162 THR D N   1 
ATOM   6393 C  CA  . THR D 1 162 ? 18.15200  39.91800  59.48300  1.000 75.88199  ?  162 THR D CA  1 
ATOM   6394 C  C   . THR D 1 162 ? 17.01800  40.12200  60.47500  1.000 71.35361  ?  162 THR D C   1 
ATOM   6395 O  O   . THR D 1 162 ? 16.20500  41.03700  60.30700  1.000 70.41654  ?  162 THR D O   1 
ATOM   6396 C  CB  . THR D 1 162 ? 17.68900  39.00700  58.34700  1.000 77.90682  ?  162 THR D CB  1 
ATOM   6397 O  OG1 . THR D 1 162 ? 17.33800  37.72100  58.87400  1.000 68.02081  ?  162 THR D OG1 1 
ATOM   6398 C  CG2 . THR D 1 162 ? 18.79000  38.84200  57.32300  1.000 69.76147  ?  162 THR D CG2 1 
ATOM   6399 N  N   . ILE D 1 163 ? 16.95200  39.27600  61.50500  1.000 75.04134  ?  163 ILE D N   1 
ATOM   6400 C  CA  . ILE D 1 163 ? 15.89800  39.37600  62.51100  1.000 74.33767  ?  163 ILE D CA  1 
ATOM   6401 C  C   . ILE D 1 163 ? 15.96300  40.72100  63.22500  1.000 74.19823  ?  163 ILE D C   1 
ATOM   6402 O  O   . ILE D 1 163 ? 14.95600  41.42900  63.34700  1.000 74.95772  ?  163 ILE D O   1 
ATOM   6403 C  CB  . ILE D 1 163 ? 16.00500  38.20300  63.50100  1.000 70.74520  ?  163 ILE D CB  1 
ATOM   6404 C  CG1 . ILE D 1 163 ? 15.97200  36.88000  62.73300  1.000 62.71062  ?  163 ILE D CG1 1 
ATOM   6405 C  CG2 . ILE D 1 163 ? 14.87600  38.26100  64.51500  1.000 74.39080  ?  163 ILE D CG2 1 
ATOM   6406 C  CD1 . ILE D 1 163 ? 16.52100  35.70900  63.50700  1.000 67.31278  ?  163 ILE D CD1 1 
ATOM   6407 N  N   . MET D 1 164 ? 17.14500  41.08700  63.72500  1.000 71.88403  ?  164 MET D N   1 
ATOM   6408 C  CA  . MET D 1 164 ? 17.28600  42.36500  64.41700  1.000 79.68036  ?  164 MET D CA  1 
ATOM   6409 C  C   . MET D 1 164 ? 17.16900  43.53700  63.45000  1.000 78.63994  ?  164 MET D C   1 
ATOM   6410 O  O   . MET D 1 164 ? 16.48900  44.52800  63.74200  1.000 79.27229  ?  164 MET D O   1 
ATOM   6411 C  CB  . MET D 1 164 ? 18.61200  42.41300  65.17600  1.000 85.52439  ?  164 MET D CB  1 
ATOM   6412 C  CG  . MET D 1 164 ? 18.64600  41.49300  66.38900  1.000 77.43100  ?  164 MET D CG  1 
ATOM   6413 S  SD  . MET D 1 164 ? 17.24800  41.72900  67.50100  1.000 77.00489  ?  164 MET D SD  1 
ATOM   6414 C  CE  . MET D 1 164 ? 17.41000  43.46800  67.88300  1.000 88.57476  ?  164 MET D CE  1 
ATOM   6415 N  N   . GLN D 1 165 ? 17.83400  43.44400  62.29300  1.000 88.17280  ?  165 GLN D N   1 
ATOM   6416 C  CA  . GLN D 1 165 ? 17.77600  44.52800  61.31500  1.000 84.06051  ?  165 GLN D CA  1 
ATOM   6417 C  C   . GLN D 1 165 ? 16.34400  44.79000  60.86500  1.000 85.53103  ?  165 GLN D C   1 
ATOM   6418 O  O   . GLN D 1 165 ? 15.94200  45.94700  60.69900  1.000 92.52766  ?  165 GLN D O   1 
ATOM   6419 C  CB  . GLN D 1 165 ? 18.66000  44.20200  60.11000  1.000 78.94629  ?  165 GLN D CB  1 
ATOM   6420 C  CG  . GLN D 1 165 ? 20.15400  44.11700  60.40100  1.000 81.29907  ?  165 GLN D CG  1 
ATOM   6421 C  CD  . GLN D 1 165 ? 20.83400  45.47300  60.41200  1.000 91.34076  ?  165 GLN D CD  1 
ATOM   6422 O  OE1 . GLN D 1 165 ? 20.67200  46.27000  59.48800  1.000 102.66972 ?  165 GLN D OE1 1 
ATOM   6423 N  NE2 . GLN D 1 165 ? 21.61200  45.73600  61.45500  1.000 85.36497  ?  165 GLN D NE2 1 
ATOM   6424 N  N   . SER D 1 166 ? 15.55900  43.72800  60.66100  1.000 78.20598  ?  166 SER D N   1 
ATOM   6425 C  CA  . SER D 1 166 ? 14.16300  43.90600  60.27100  1.000 84.38820  ?  166 SER D CA  1 
ATOM   6426 C  C   . SER D 1 166 ? 13.34500  44.53300  61.39400  1.000 91.67052  ?  166 SER D C   1 
ATOM   6427 O  O   . SER D 1 166 ? 12.54300  45.44300  61.15000  1.000 95.90569  ?  166 SER D O   1 
ATOM   6428 C  CB  . SER D 1 166 ? 13.55600  42.56500  59.86000  1.000 83.39407  ?  166 SER D CB  1 
ATOM   6429 O  OG  . SER D 1 166 ? 14.27900  41.98400  58.78900  1.000 88.01032  ?  166 SER D OG  1 
ATOM   6430 N  N   . ALA D 1 167 ? 13.53000  44.05700  62.63000  1.000 91.01533  ?  167 ALA D N   1 
ATOM   6431 C  CA  . ALA D 1 167 ? 12.75000  44.56900  63.75400  1.000 92.10863  ?  167 ALA D CA  1 
ATOM   6432 C  C   . ALA D 1 167 ? 13.05200  46.04000  64.01200  1.000 98.89538  ?  167 ALA D C   1 
ATOM   6433 O  O   . ALA D 1 167 ? 12.13700  46.85100  64.19900  1.000 101.69759 ?  167 ALA D O   1 
ATOM   6434 C  CB  . ALA D 1 167 ? 13.02200  43.73200  65.00400  1.000 94.31604  ?  167 ALA D CB  1 
ATOM   6435 N  N   . TRP D 1 168 ? 14.33600  46.40200  64.04800  1.000 97.82109  ?  168 TRP D N   1 
ATOM   6436 C  CA  . TRP D 1 168 ? 14.70100  47.80300  64.23000  1.000 100.18952 ?  168 TRP D CA  1 
ATOM   6437 C  C   . TRP D 1 168 ? 14.22200  48.65700  63.06500  1.000 99.10866  ?  168 TRP D C   1 
ATOM   6438 O  O   . TRP D 1 168 ? 13.84400  49.81800  63.25900  1.000 101.17077 ?  168 TRP D O   1 
ATOM   6439 C  CB  . TRP D 1 168 ? 16.21100  47.93300  64.41200  1.000 94.40364  ?  168 TRP D CB  1 
ATOM   6440 C  CG  . TRP D 1 168 ? 16.67000  47.55600  65.78100  1.000 85.71532  ?  168 TRP D CG  1 
ATOM   6441 C  CD1 . TRP D 1 168 ? 15.91200  47.50700  66.91400  1.000 90.67294  ?  168 TRP D CD1 1 
ATOM   6442 C  CD2 . TRP D 1 168 ? 17.99100  47.16300  66.16300  1.000 83.21773  ?  168 TRP D CD2 1 
ATOM   6443 N  NE1 . TRP D 1 168 ? 16.68300  47.11500  67.98100  1.000 91.28201  ?  168 TRP D NE1 1 
ATOM   6444 C  CE2 . TRP D 1 168 ? 17.96400  46.89600  67.54600  1.000 88.43206  ?  168 TRP D CE2 1 
ATOM   6445 C  CE3 . TRP D 1 168 ? 19.19600  47.01200  65.47100  1.000 83.96307  ?  168 TRP D CE3 1 
ATOM   6446 C  CZ2 . TRP D 1 168 ? 19.09500  46.48900  68.25000  1.000 89.03212  ?  168 TRP D CZ2 1 
ATOM   6447 C  CZ3 . TRP D 1 168 ? 20.31700  46.60700  66.17000  1.000 89.00572  ?  168 TRP D CZ3 1 
ATOM   6448 C  CH2 . TRP D 1 168 ? 20.25900  46.34900  67.54500  1.000 85.82442  ?  168 TRP D CH2 1 
ATOM   6449 N  N   . LYS D 1 169 ? 14.23000  48.10400  61.85100  1.000 90.75497  ?  169 LYS D N   1 
ATOM   6450 C  CA  . LYS D 1 169 ? 13.77600  48.86900  60.69700  1.000 97.78333  ?  169 LYS D CA  1 
ATOM   6451 C  C   . LYS D 1 169 ? 12.26800  49.07100  60.72800  1.000 100.16081 ?  169 LYS D C   1 
ATOM   6452 O  O   . LYS D 1 169 ? 11.77100  50.08800  60.23200  1.000 101.20690 ?  169 LYS D O   1 
ATOM   6453 C  CB  . LYS D 1 169 ? 14.19700  48.16300  59.40800  1.000 98.39917  ?  169 LYS D CB  1 
ATOM   6454 C  CG  . LYS D 1 169 ? 13.84800  48.89300  58.12700  1.000 103.28833 ?  169 LYS D CG  1 
ATOM   6455 C  CD  . LYS D 1 169 ? 14.31800  48.08900  56.92800  1.000 101.99091 ?  169 LYS D CD  1 
ATOM   6456 C  CE  . LYS D 1 169 ? 13.51200  46.80700  56.79400  1.000 103.95050 ?  169 LYS D CE  1 
ATOM   6457 N  NZ  . LYS D 1 169 ? 12.07800  47.05800  56.49400  1.000 99.52863  ?  169 LYS D NZ  1 
ATOM   6458 N  N   . ARG D 1 170 ? 11.52600  48.12500  61.30200  1.000 98.94140  ?  170 ARG D N   1 
ATOM   6459 C  CA  . ARG D 1 170 ? 10.09000  48.27800  61.48300  1.000 100.19582 ?  170 ARG D CA  1 
ATOM   6460 C  C   . ARG D 1 170 ? 9.72900   48.95600  62.80300  1.000 98.82968  ?  170 ARG D C   1 
ATOM   6461 O  O   . ARG D 1 170 ? 8.54200   49.04500  63.13200  1.000 96.63600  ?  170 ARG D O   1 
ATOM   6462 C  CB  . ARG D 1 170 ? 9.38400   46.92200  61.37200  1.000 101.54351 ?  170 ARG D CB  1 
ATOM   6463 C  CG  . ARG D 1 170 ? 9.64800   45.95800  62.51100  1.000 94.89959  ?  170 ARG D CG  1 
ATOM   6464 C  CD  . ARG D 1 170 ? 8.98400   44.61600  62.24900  1.000 94.23781  ?  170 ARG D CD  1 
ATOM   6465 N  NE  . ARG D 1 170 ? 9.18600   43.68200  63.35000  1.000 105.29578 ?  170 ARG D NE  1 
ATOM   6466 C  CZ  . ARG D 1 170 ? 9.94800   42.59900  63.28200  1.000 103.01982 ?  170 ARG D CZ  1 
ATOM   6467 N  NH1 . ARG D 1 170 ? 10.60600  42.28500  62.17700  1.000 95.62543  ?  170 ARG D NH1 1 
ATOM   6468 N  NH2 . ARG D 1 170 ? 10.05700  41.81400  64.35000  1.000 99.20313  ?  170 ARG D NH2 1 
ATOM   6469 N  N   . GLY D 1 171 ? 10.71800  49.42100  63.56800  1.000 96.15144  ?  171 GLY D N   1 
ATOM   6470 C  CA  . GLY D 1 171 ? 10.45500  50.21700  64.75000  1.000 101.17056 ?  171 GLY D CA  1 
ATOM   6471 C  C   . GLY D 1 171 ? 10.25100  49.46300  66.04800  1.000 104.82483 ?  171 GLY D C   1 
ATOM   6472 O  O   . GLY D 1 171 ? 9.99800   50.10400  67.07600  1.000 107.38231 ?  171 GLY D O   1 
ATOM   6473 N  N   . GLN D 1 172 ? 10.33500  48.13400  66.04100  1.000 104.25066 ?  172 GLN D N   1 
ATOM   6474 C  CA  . GLN D 1 172 ? 10.13900  47.36700  67.26600  1.000 107.01013 ?  172 GLN D CA  1 
ATOM   6475 C  C   . GLN D 1 172 ? 11.16400  47.74900  68.32900  1.000 106.62175 ?  172 GLN D C   1 
ATOM   6476 O  O   . GLN D 1 172 ? 12.32700  48.03100  68.02300  1.000 106.87219 ?  172 GLN D O   1 
ATOM   6477 C  CB  . GLN D 1 172 ? 10.22700  45.86600  66.97300  1.000 105.13853 ?  172 GLN D CB  1 
ATOM   6478 C  CG  . GLN D 1 172 ? 9.91100   44.98200  68.17400  1.000 98.56803  ?  172 GLN D CG  1 
ATOM   6479 C  CD  . GLN D 1 172 ? 9.59500   43.54900  67.78900  1.000 102.65933 ?  172 GLN D CD  1 
ATOM   6480 O  OE1 . GLN D 1 172 ? 9.09400   43.28100  66.69600  1.000 103.99933 ?  172 GLN D OE1 1 
ATOM   6481 N  NE2 . GLN D 1 172 ? 9.88400   42.61900  68.69200  1.000 87.72879  ?  172 GLN D NE2 1 
ATOM   6482 N  N   . LYS D 1 173 ? 10.72600  47.74300  69.59000  1.000 98.92382  ?  173 LYS D N   1 
ATOM   6483 C  CA  . LYS D 1 173 ? 11.58900  48.06300  70.72700  1.000 101.80300 ?  173 LYS D CA  1 
ATOM   6484 C  C   . LYS D 1 173 ? 12.30700  46.79600  71.16600  1.000 101.32357 ?  173 LYS D C   1 
ATOM   6485 O  O   . LYS D 1 173 ? 11.73000  45.93700  71.83600  1.000 100.24748 ?  173 LYS D O   1 
ATOM   6486 C  CB  . LYS D 1 173 ? 10.78800  48.64500  71.88900  1.000 101.56705 ?  173 LYS D CB  1 
ATOM   6487 C  CG  . LYS D 1 173 ? 10.30700  50.07800  71.75500  1.000 107.02861 ?  173 LYS D CG  1 
ATOM   6488 C  CD  . LYS D 1 173 ? 11.49600  51.01500  71.57800  1.000 111.63783 ?  173 LYS D CD  1 
ATOM   6489 C  CE  . LYS D 1 173 ? 11.07400  52.47700  71.56800  1.000 115.03580 ?  173 LYS D CE  1 
ATOM   6490 N  NZ  . LYS D 1 173 ? 10.01100  52.76700  70.57300  1.000 113.29615 ?  173 LYS D NZ  1 
ATOM   6491 N  N   . VAL D 1 174 ? 13.57400  46.68000  70.78000  1.000 97.70040  ?  174 VAL D N   1 
ATOM   6492 C  CA  . VAL D 1 174 ? 14.44900  45.61200  71.24700  1.000 92.73711  ?  174 VAL D CA  1 
ATOM   6493 C  C   . VAL D 1 174 ? 15.78100  46.24200  71.62100  1.000 90.11701  ?  174 VAL D C   1 
ATOM   6494 O  O   . VAL D 1 174 ? 16.28900  47.11400  70.90800  1.000 92.00027  ?  174 VAL D O   1 
ATOM   6495 C  CB  . VAL D 1 174 ? 14.64800  44.50600  70.18700  1.000 88.81837  ?  174 VAL D CB  1 
ATOM   6496 C  CG1 . VAL D 1 174 ? 15.33900  43.30100  70.80800  1.000 88.58567  ?  174 VAL D CG1 1 
ATOM   6497 C  CG2 . VAL D 1 174 ? 13.32100  44.09800  69.56100  1.000 90.10545  ?  174 VAL D CG2 1 
ATOM   6498 N  N   . THR D 1 175 ? 16.34600  45.80200  72.74100  1.000 89.31915  ?  175 THR D N   1 
ATOM   6499 C  CA  . THR D 1 175 ? 17.61400  46.32100  73.23300  1.000 87.14020  ?  175 THR D CA  1 
ATOM   6500 C  C   . THR D 1 175 ? 18.51000  45.14400  73.57900  1.000 83.63955  ?  175 THR D C   1 
ATOM   6501 O  O   . THR D 1 175 ? 18.09200  44.23800  74.30600  1.000 83.91485  ?  175 THR D O   1 
ATOM   6502 C  CB  . THR D 1 175 ? 17.41400  47.22200  74.45700  1.000 91.31762  ?  175 THR D CB  1 
ATOM   6503 O  OG1 . THR D 1 175 ? 16.46400  48.25100  74.14900  1.000 90.53328  ?  175 THR D OG1 1 
ATOM   6504 C  CG2 . THR D 1 175 ? 18.72700  47.86800  74.85400  1.000 87.12731  ?  175 THR D CG2 1 
ATOM   6505 N  N   . ILE D 1 176 ? 19.73300  45.15600  73.06100  1.000 82.09843  ?  176 ILE D N   1 
ATOM   6506 C  CA  . ILE D 1 176 ? 20.69100  44.07800  73.27400  1.000 82.53133  ?  176 ILE D CA  1 
ATOM   6507 C  C   . ILE D 1 176 ? 21.76500  44.55400  74.24200  1.000 79.28406  ?  176 ILE D C   1 
ATOM   6508 O  O   . ILE D 1 176 ? 22.22900  45.69800  74.15700  1.000 83.41767  ?  176 ILE D O   1 
ATOM   6509 C  CB  . ILE D 1 176 ? 21.29700  43.58600  71.94400  1.000 81.72956  ?  176 ILE D CB  1 
ATOM   6510 C  CG1 . ILE D 1 176 ? 21.97500  44.72800  71.18900  1.000 82.25694  ?  176 ILE D CG1 1 
ATOM   6511 C  CG2 . ILE D 1 176 ? 20.21500  42.96000  71.07700  1.000 78.10747  ?  176 ILE D CG2 1 
ATOM   6512 C  CD1 . ILE D 1 176 ? 22.42800  44.34500  69.79500  1.000 82.91676  ?  176 ILE D CD1 1 
ATOM   6513 N  N   . HIS D 1 177 ? 22.13800  43.68500  75.18100  1.000 75.63353  ?  177 HIS D N   1 
ATOM   6514 C  CA  . HIS D 1 177 ? 23.10300  44.01900  76.22000  1.000 78.22808  ?  177 HIS D CA  1 
ATOM   6515 C  C   . HIS D 1 177 ? 24.19500  42.96300  76.28400  1.000 79.51458  ?  177 HIS D C   1 
ATOM   6516 O  O   . HIS D 1 177 ? 23.95100  41.77600  76.05600  1.000 81.40039  ?  177 HIS D O   1 
ATOM   6517 C  CB  . HIS D 1 177 ? 22.44900  44.13200  77.60300  1.000 67.52169  ?  177 HIS D CB  1 
ATOM   6518 C  CG  . HIS D 1 177 ? 21.21600  44.97700  77.62400  1.000 72.97346  ?  177 HIS D CG  1 
ATOM   6519 N  ND1 . HIS D 1 177 ? 21.23900  46.31800  77.94100  1.000 76.35875  ?  177 HIS D ND1 1 
ATOM   6520 C  CD2 . HIS D 1 177 ? 19.91800  44.66500  77.40100  1.000 75.65381  ?  177 HIS D CD2 1 
ATOM   6521 C  CE1 . HIS D 1 177 ? 20.01000  46.80000  77.89200  1.000 78.36338  ?  177 HIS D CE1 1 
ATOM   6522 N  NE2 . HIS D 1 177 ? 19.19000  45.81700  77.56800  1.000 76.71085  ?  177 HIS D NE2 1 
ATOM   6523 N  N   . GLY D 1 178 ? 25.41100  43.41600  76.58500  1.000 77.56823  ?  178 GLY D N   1 
ATOM   6524 C  CA  . GLY D 1 178 ? 26.52800  42.51500  76.79000  1.000 78.08091  ?  178 GLY D CA  1 
ATOM   6525 C  C   . GLY D 1 178 ? 27.07400  42.60000  78.20100  1.000 85.64583  ?  178 GLY D C   1 
ATOM   6526 O  O   . GLY D 1 178 ? 27.58300  43.64600  78.61200  1.000 88.38558  ?  178 GLY D O   1 
ATOM   6527 N  N   . TRP D 1 179 ? 26.98200  41.50500  78.95100  1.000 84.86686  ?  179 TRP D N   1 
ATOM   6528 C  CA  . TRP D 1 179 ? 27.38100  41.46000  80.35000  1.000 81.44707  ?  179 TRP D CA  1 
ATOM   6529 C  C   . TRP D 1 179 ? 28.43100  40.37900  80.56200  1.000 82.26393  ?  179 TRP D C   1 
ATOM   6530 O  O   . TRP D 1 179 ? 28.70800  39.55900  79.68300  1.000 84.71768  ?  179 TRP D O   1 
ATOM   6531 C  CB  . TRP D 1 179 ? 26.18300  41.19200  81.27300  1.000 74.48634  ?  179 TRP D CB  1 
ATOM   6532 C  CG  . TRP D 1 179 ? 25.14500  42.26800  81.29600  1.000 75.46842  ?  179 TRP D CG  1 
ATOM   6533 C  CD1 . TRP D 1 179 ? 25.22900  43.50800  80.73200  1.000 79.77158  ?  179 TRP D CD1 1 
ATOM   6534 C  CD2 . TRP D 1 179 ? 23.86100  42.19900  81.92600  1.000 72.53520  ?  179 TRP D CD2 1 
ATOM   6535 N  NE1 . TRP D 1 179 ? 24.07300  44.21400  80.96900  1.000 77.13228  ?  179 TRP D NE1 1 
ATOM   6536 C  CE2 . TRP D 1 179 ? 23.21700  43.43100  81.70000  1.000 72.76457  ?  179 TRP D CE2 1 
ATOM   6537 C  CE3 . TRP D 1 179 ? 23.19200  41.21300  82.65700  1.000 75.93313  ?  179 TRP D CE3 1 
ATOM   6538 C  CZ2 . TRP D 1 179 ? 21.93700  43.70300  82.17900  1.000 78.56229  ?  179 TRP D CZ2 1 
ATOM   6539 C  CZ3 . TRP D 1 179 ? 21.92200  41.48400  83.13400  1.000 76.06352  ?  179 TRP D CZ3 1 
ATOM   6540 C  CH2 . TRP D 1 179 ? 21.30800  42.71900  82.89300  1.000 82.10071  ?  179 TRP D CH2 1 
ATOM   6541 N  N   . ALA D 1 180 ? 29.02200  40.39300  81.75500  1.000 75.56818  ?  180 ALA D N   1 
ATOM   6542 C  CA  . ALA D 1 180 ? 29.91900  39.33600  82.19000  1.000 81.60914  ?  180 ALA D CA  1 
ATOM   6543 C  C   . ALA D 1 180 ? 29.89500  39.27100  83.71000  1.000 89.66194  ?  180 ALA D C   1 
ATOM   6544 O  O   . ALA D 1 180 ? 29.64200  40.27400  84.38300  1.000 87.30007  ?  180 ALA D O   1 
ATOM   6545 C  CB  . ALA D 1 180 ? 31.35000  39.55500  81.68400  1.000 77.32261  ?  180 ALA D CB  1 
ATOM   6546 N  N   . TYR D 1 181 ? 30.16400  38.08300  84.24700  1.000 85.94296  ?  181 TYR D N   1 
ATOM   6547 C  CA  . TYR D 1 181 ? 30.22700  37.89300  85.68800  1.000 83.15529  ?  181 TYR D CA  1 
ATOM   6548 C  C   . TYR D 1 181 ? 31.38800  36.97200  86.02800  1.000 87.59896  ?  181 TYR D C   1 
ATOM   6549 O  O   . TYR D 1 181 ? 31.80700  36.14500  85.21400  1.000 89.24627  ?  181 TYR D O   1 
ATOM   6550 C  CB  . TYR D 1 181 ? 28.90800  37.33000  86.24800  1.000 83.81891  ?  181 TYR D CB  1 
ATOM   6551 C  CG  . TYR D 1 181 ? 28.62300  35.88100  85.90700  1.000 86.54583  ?  181 TYR D CG  1 
ATOM   6552 C  CD1 . TYR D 1 181 ? 27.96900  35.54000  84.72800  1.000 85.30550  ?  181 TYR D CD1 1 
ATOM   6553 C  CD2 . TYR D 1 181 ? 28.98400  34.85600  86.77600  1.000 85.91871  ?  181 TYR D CD2 1 
ATOM   6554 C  CE1 . TYR D 1 181 ? 27.69600  34.21900  84.41700  1.000 84.09734  ?  181 TYR D CE1 1 
ATOM   6555 C  CE2 . TYR D 1 181 ? 28.71900  33.53300  86.47200  1.000 86.43206  ?  181 TYR D CE2 1 
ATOM   6556 C  CZ  . TYR D 1 181 ? 28.07400  33.22000  85.29200  1.000 88.77148  ?  181 TYR D CZ  1 
ATOM   6557 O  OH  . TYR D 1 181 ? 27.80700  31.90400  84.98900  1.000 88.10225  ?  181 TYR D OH  1 
ATOM   6558 N  N   . GLY D 1 182 ? 31.89900  37.12100  87.24700  1.000 90.48785  ?  182 GLY D N   1 
ATOM   6559 C  CA  . GLY D 1 182 ? 33.02800  36.34500  87.72200  1.000 95.22175  ?  182 GLY D CA  1 
ATOM   6560 C  C   . GLY D 1 182 ? 32.58500  35.36100  88.78600  1.000 96.72529  ?  182 GLY D C   1 
ATOM   6561 O  O   . GLY D 1 182 ? 31.59400  35.58600  89.48500  1.000 93.93463  ?  182 GLY D O   1 
ATOM   6562 N  N   . ILE D 1 183 ? 33.33000  34.25800  88.90700  1.000 99.09516  ?  183 ILE D N   1 
ATOM   6563 C  CA  . ILE D 1 183 ? 33.02300  33.25200  89.92200  1.000 99.14668  ?  183 ILE D CA  1 
ATOM   6564 C  C   . ILE D 1 183 ? 33.53300  33.63400  91.30100  1.000 103.90046 ?  183 ILE D C   1 
ATOM   6565 O  O   . ILE D 1 183 ? 33.23500  32.93600  92.27900  1.000 107.00522 ?  183 ILE D O   1 
ATOM   6566 C  CB  . ILE D 1 183 ? 33.59000  31.89600  89.45300  1.000 101.22468 ?  183 ILE D CB  1 
ATOM   6567 C  CG1 . ILE D 1 183 ? 35.10600  31.99000  89.29300  1.000 107.08105 ?  183 ILE D CG1 1 
ATOM   6568 C  CG2 . ILE D 1 183 ? 32.89400  31.40900  88.18300  1.000 107.78014 ?  183 ILE D CG2 1 
ATOM   6569 C  CD1 . ILE D 1 183 ? 35.75400  30.64400  89.04600  1.000 112.73098 ?  183 ILE D CD1 1 
ATOM   6570 N  N   . HIS D 1 184 ? 34.25600  34.74900  91.41700  1.000 105.45994 ?  184 HIS D N   1 
ATOM   6571 C  CA  . HIS D 1 184 ? 34.73400  35.21400  92.71300  1.000 98.80260  ?  184 HIS D CA  1 
ATOM   6572 C  C   . HIS D 1 184 ? 33.66200  35.94900  93.50800  1.000 98.54339  ?  184 HIS D C   1 
ATOM   6573 O  O   . HIS D 1 184 ? 33.64300  35.85800  94.74000  1.000 109.21685 ?  184 HIS D O   1 
ATOM   6574 C  CB  . HIS D 1 184 ? 35.94700  36.12400  92.52200  1.000 98.87119  ?  184 HIS D CB  1 
ATOM   6575 C  CG  . HIS D 1 184 ? 35.72300  37.22700  91.53500  1.000 106.42958 ?  184 HIS D CG  1 
ATOM   6576 N  ND1 . HIS D 1 184 ? 35.63900  37.00500  90.17700  1.000 108.41971 ?  184 HIS D ND1 1 
ATOM   6577 C  CD2 . HIS D 1 184 ? 35.55400  38.55900  91.70900  1.000 107.86513 ?  184 HIS D CD2 1 
ATOM   6578 C  CE1 . HIS D 1 184 ? 35.43300  38.15300  89.55600  1.000 107.70759 ?  184 HIS D CE1 1 
ATOM   6579 N  NE2 . HIS D 1 184 ? 35.37800  39.11200  90.46300  1.000 108.66849 ?  184 HIS D NE2 1 
ATOM   6580 N  N   . ASP D 1 185 ? 32.76300  36.67100  92.83600  1.000 94.61615  ?  185 ASP D N   1 
ATOM   6581 C  CA  . ASP D 1 185 ? 31.73400  37.42600  93.54200  1.000 92.22114  ?  185 ASP D CA  1 
ATOM   6582 C  C   . ASP D 1 185 ? 30.35000  37.38900  92.91000  1.000 98.89868  ?  185 ASP D C   1 
ATOM   6583 O  O   . ASP D 1 185 ? 29.40300  37.84500  93.55600  1.000 96.42666  ?  185 ASP D O   1 
ATOM   6584 C  CB  . ASP D 1 185 ? 32.16100  38.89500  93.68900  1.000 91.16694  ?  185 ASP D CB  1 
ATOM   6585 C  CG  . ASP D 1 185 ? 32.42200  39.56900  92.35000  1.000 98.92251  ?  185 ASP D CG  1 
ATOM   6586 O  OD1 . ASP D 1 185 ? 32.21700  38.92800  91.29600  1.000 103.88682 ?  185 ASP D OD1 1 
ATOM   6587 O  OD2 . ASP D 1 185 ? 32.82700  40.75000  92.35000  1.000 96.13391  -1 185 ASP D OD2 1 
ATOM   6588 N  N   . GLY D 1 186 ? 30.19300  36.90100  91.68000  1.000 99.32519  ?  186 GLY D N   1 
ATOM   6589 C  CA  . GLY D 1 186 ? 28.88100  36.89500  91.06400  1.000 88.03046  ?  186 GLY D CA  1 
ATOM   6590 C  C   . GLY D 1 186 ? 28.36900  38.25500  90.65000  1.000 88.14977  ?  186 GLY D C   1 
ATOM   6591 O  O   . GLY D 1 186 ? 27.16100  38.42100  90.46300  1.000 79.78096  ?  186 GLY D O   1 
ATOM   6592 N  N   . LEU D 1 187 ? 29.25500  39.23900  90.50500  1.000 91.93238  ?  187 LEU D N   1 
ATOM   6593 C  CA  . LEU D 1 187 ? 28.86300  40.60200  90.16600  1.000 89.38391  ?  187 LEU D CA  1 
ATOM   6594 C  C   . LEU D 1 187 ? 28.83700  40.77600  88.65100  1.000 87.95384  ?  187 LEU D C   1 
ATOM   6595 O  O   . LEU D 1 187 ? 29.85100  40.56100  87.97800  1.000 86.63971  ?  187 LEU D O   1 
ATOM   6596 C  CB  . LEU D 1 187 ? 29.82300  41.60900  90.79900  1.000 89.96545  ?  187 LEU D CB  1 
ATOM   6597 C  CG  . LEU D 1 187 ? 29.37700  43.07100  90.76500  1.000 89.00316  ?  187 LEU D CG  1 
ATOM   6598 C  CD1 . LEU D 1 187 ? 28.08400  43.25200  91.53700  1.000 92.02766  ?  187 LEU D CD1 1 
ATOM   6599 C  CD2 . LEU D 1 187 ? 30.46600  43.98000  91.31200  1.000 83.51889  ?  187 LEU D CD2 1 
ATOM   6600 N  N   . LEU D 1 188 ? 27.67800  41.16600  88.12100  1.000 87.65484  ?  188 LEU D N   1 
ATOM   6601 C  CA  . LEU D 1 188 ? 27.55000  41.43000  86.69300  1.000 83.60390  ?  188 LEU D CA  1 
ATOM   6602 C  C   . LEU D 1 188 ? 28.25200  42.73000  86.31800  1.000 84.84910  ?  188 LEU D C   1 
ATOM   6603 O  O   . LEU D 1 188 ? 27.99700  43.78200  86.91400  1.000 83.42477  ?  188 LEU D O   1 
ATOM   6604 C  CB  . LEU D 1 188 ? 26.07700  41.48700  86.29200  1.000 73.80288  ?  188 LEU D CB  1 
ATOM   6605 C  CG  . LEU D 1 188 ? 25.35900  40.13700  86.26300  1.000 75.09960  ?  188 LEU D CG  1 
ATOM   6606 C  CD1 . LEU D 1 188 ? 23.87500  40.31900  85.99400  1.000 73.87615  ?  188 LEU D CD1 1 
ATOM   6607 C  CD2 . LEU D 1 188 ? 25.98900  39.22200  85.22600  1.000 73.94786  ?  188 LEU D CD2 1 
ATOM   6608 N  N   . ARG D 1 189 ? 29.13200  42.65500  85.32500  1.000 89.97539  ?  189 ARG D N   1 
ATOM   6609 C  CA  . ARG D 1 189 ? 29.78200  43.82500  84.75100  1.000 92.90770  ?  189 ARG D CA  1 
ATOM   6610 C  C   . ARG D 1 189 ? 29.15700  44.13700  83.39700  1.000 86.26006  ?  189 ARG D C   1 
ATOM   6611 O  O   . ARG D 1 189 ? 29.08400  43.26400  82.52600  1.000 87.48564  ?  189 ARG D O   1 
ATOM   6612 C  CB  . ARG D 1 189 ? 31.28800  43.59500  84.60700  1.000 92.95934  ?  189 ARG D CB  1 
ATOM   6613 C  CG  . ARG D 1 189 ? 32.02200  44.69000  83.84900  1.000 93.88041  ?  189 ARG D CG  1 
ATOM   6614 C  CD  . ARG D 1 189 ? 33.51500  44.40400  83.75400  1.000 97.60040  ?  189 ARG D CD  1 
ATOM   6615 N  NE  . ARG D 1 189 ? 34.21500  44.70900  84.99700  1.000 99.33298  ?  189 ARG D NE  1 
ATOM   6616 C  CZ  . ARG D 1 189 ? 34.63000  43.80100  85.87000  1.000 107.22586 ?  189 ARG D CZ  1 
ATOM   6617 N  NH1 . ARG D 1 189 ? 34.42500  42.50900  85.67300  1.000 102.95116 ?  189 ARG D NH1 1 
ATOM   6618 N  NH2 . ARG D 1 189 ? 35.26400  44.20000  86.96900  1.000 113.52813 ?  189 ARG D NH2 1 
ATOM   6619 N  N   . ASP D 1 190 ? 28.70100  45.37700  83.22700  1.000 87.70300  ?  190 ASP D N   1 
ATOM   6620 C  CA  . ASP D 1 190 ? 28.11800  45.81300  81.96300  1.000 89.54322  ?  190 ASP D CA  1 
ATOM   6621 C  C   . ASP D 1 190 ? 29.23500  46.24800  81.02000  1.000 90.19715  ?  190 ASP D C   1 
ATOM   6622 O  O   . ASP D 1 190 ? 29.96600  47.20200  81.31100  1.000 86.83008  ?  190 ASP D O   1 
ATOM   6623 C  CB  . ASP D 1 190 ? 27.12500  46.95000  82.20400  1.000 91.91454  ?  190 ASP D CB  1 
ATOM   6624 C  CG  . ASP D 1 190 ? 26.23700  47.22900  81.00000  1.000 86.67585  ?  190 ASP D CG  1 
ATOM   6625 O  OD1 . ASP D 1 190 ? 26.67900  47.01200  79.85200  1.000 90.28023  ?  190 ASP D OD1 1 
ATOM   6626 O  OD2 . ASP D 1 190 ? 25.08500  47.66600  81.20600  1.000 85.14124  -1 190 ASP D OD2 1 
ATOM   6627 N  N   . LEU D 1 191 ? 29.36200  45.55600  79.88700  1.000 92.32813  ?  191 LEU D N   1 
ATOM   6628 C  CA  . LEU D 1 191 ? 30.42700  45.83100  78.93000  1.000 92.55042  ?  191 LEU D CA  1 
ATOM   6629 C  C   . LEU D 1 191 ? 30.17100  47.07600  78.09300  1.000 96.63041  ?  191 LEU D C   1 
ATOM   6630 O  O   . LEU D 1 191 ? 31.01900  47.42600  77.26200  1.000 96.27715  ?  191 LEU D O   1 
ATOM   6631 C  CB  . LEU D 1 191 ? 30.63400  44.62200  78.01500  1.000 90.36465  ?  191 LEU D CB  1 
ATOM   6632 C  CG  . LEU D 1 191 ? 31.09200  43.35400  78.73600  1.000 90.59223  ?  191 LEU D CG  1 
ATOM   6633 C  CD1 . LEU D 1 191 ? 31.23900  42.20000  77.76300  1.000 89.90501  ?  191 LEU D CD1 1 
ATOM   6634 C  CD2 . LEU D 1 191 ? 32.40000  43.60900  79.47200  1.000 97.41882  ?  191 LEU D CD2 1 
ATOM   6635 N  N   . ASP D 1 192 ? 29.02400  47.73200  78.27700  1.000 96.06998  ?  192 ASP D N   1 
ATOM   6636 C  CA  . ASP D 1 192 ? 28.76600  49.06200  77.72300  1.000 97.11443  ?  192 ASP D CA  1 
ATOM   6637 C  C   . ASP D 1 192 ? 28.73300  49.03300  76.19400  1.000 98.81377  ?  192 ASP D C   1 
ATOM   6638 O  O   . ASP D 1 192 ? 29.31500  49.89100  75.52600  1.000 103.71414 ?  192 ASP D O   1 
ATOM   6639 C  CB  . ASP D 1 192 ? 29.81000  50.06300  78.23300  1.000 97.54174  ?  192 ASP D CB  1 
ATOM   6640 C  CG  . ASP D 1 192 ? 29.25300  51.46100  78.40000  1.000 105.99691 ?  192 ASP D CG  1 
ATOM   6641 O  OD1 . ASP D 1 192 ? 28.02100  51.62700  78.28300  1.000 105.01251 ?  192 ASP D OD1 1 
ATOM   6642 O  OD2 . ASP D 1 192 ? 30.04600  52.39600  78.63900  1.000 114.33333 -1 192 ASP D OD2 1 
ATOM   6643 N  N   . VAL D 1 193 ? 28.04500  48.03700  75.63200  1.000 97.15102  ?  193 VAL D N   1 
ATOM   6644 C  CA  . VAL D 1 193 ? 27.86300  47.93200  74.18500  1.000 95.01747  ?  193 VAL D CA  1 
ATOM   6645 C  C   . VAL D 1 193 ? 26.37300  47.86400  73.87500  1.000 91.97776  ?  193 VAL D C   1 
ATOM   6646 O  O   . VAL D 1 193 ? 25.96300  47.30900  72.84900  1.000 87.10966  ?  193 VAL D O   1 
ATOM   6647 C  CB  . VAL D 1 193 ? 28.59700  46.70600  73.61100  1.000 86.55681  ?  193 VAL D CB  1 
ATOM   6648 C  CG1 . VAL D 1 193 ? 30.10300  46.87100  73.74500  1.000 90.84606  ?  193 VAL D CG1 1 
ATOM   6649 C  CG2 . VAL D 1 193 ? 28.12600  45.43200  74.29800  1.000 85.30749  ?  193 VAL D CG2 1 
ATOM   6650 N  N   . THR D 1 194 ? 25.56100  48.44500  74.75300  1.000 95.16384  ?  194 THR D N   1 
ATOM   6651 C  CA  . THR D 1 194 ? 24.11000  48.35700  74.64100  1.000 91.49271  ?  194 THR D CA  1 
ATOM   6652 C  C   . THR D 1 194 ? 23.61900  49.07800  73.38900  1.000 96.34408  ?  194 THR D C   1 
ATOM   6653 O  O   . THR D 1 194 ? 23.89600  50.26600  73.19900  1.000 99.84767  ?  194 THR D O   1 
ATOM   6654 C  CB  . THR D 1 194 ? 23.46100  48.94400  75.89200  1.000 84.34281  ?  194 THR D CB  1 
ATOM   6655 O  OG1 . THR D 1 194 ? 23.74100  48.10000  77.01600  1.000 80.78819  ?  194 THR D OG1 1 
ATOM   6656 C  CG2 . THR D 1 194 ? 21.96100  49.06400  75.71300  1.000 81.74812  ?  194 THR D CG2 1 
ATOM   6657 N  N   . ALA D 1 195 ? 22.88400  48.36000  72.54100  1.000 92.38379  ?  195 ALA D N   1 
ATOM   6658 C  CA  . ALA D 1 195 ? 22.43500  48.87300  71.25500  1.000 88.11378  ?  195 ALA D CA  1 
ATOM   6659 C  C   . ALA D 1 195 ? 20.91800  48.80300  71.15400  1.000 85.92944  ?  195 ALA D C   1 
ATOM   6660 O  O   . ALA D 1 195 ? 20.30000  47.81700  71.56700  1.000 86.10378  ?  195 ALA D O   1 
ATOM   6661 C  CB  . ALA D 1 195 ? 23.06500  48.08700  70.10400  1.000 92.24921  ?  195 ALA D CB  1 
ATOM   6662 N  N   . THR D 1 196 ? 20.32300  49.85700  70.59100  1.000 89.86972  ?  196 THR D N   1 
ATOM   6663 C  CA  . THR D 1 196 ? 18.88900  49.91800  70.35400  1.000 93.12036  ?  196 THR D CA  1 
ATOM   6664 C  C   . THR D 1 196 ? 18.53300  50.11000  68.89000  1.000 95.77651  ?  196 THR D C   1 
ATOM   6665 O  O   . THR D 1 196 ? 17.34900  50.03100  68.54200  1.000 94.02378  ?  196 THR D O   1 
ATOM   6666 C  CB  . THR D 1 196 ? 18.25200  51.05200  71.17100  1.000 94.95659  ?  196 THR D CB  1 
ATOM   6667 O  OG1 . THR D 1 196 ? 18.79600  52.31100  70.75200  1.000 103.75501 ?  196 THR D OG1 1 
ATOM   6668 C  CG2 . THR D 1 196 ? 18.52200  50.85300  72.65100  1.000 93.86882  ?  196 THR D CG2 1 
ATOM   6669 N  N   . ASN D 1 197 ? 19.51200  50.36700  68.03200  1.000 99.77125  ?  197 ASN D N   1 
ATOM   6670 C  CA  . ASN D 1 197 ? 19.27600  50.50700  66.60400  1.000 98.07262  ?  197 ASN D CA  1 
ATOM   6671 C  C   . ASN D 1 197 ? 20.59300  50.27100  65.88000  1.000 96.11214  ?  197 ASN D C   1 
ATOM   6672 O  O   . ASN D 1 197 ? 21.60900  49.92100  66.48900  1.000 88.78733  ?  197 ASN D O   1 
ATOM   6673 C  CB  . ASN D 1 197 ? 18.66700  51.87400  66.26900  1.000 98.66390  ?  197 ASN D CB  1 
ATOM   6674 C  CG  . ASN D 1 197 ? 19.47500  53.03400  66.82700  1.000 99.80559  ?  197 ASN D CG  1 
ATOM   6675 O  OD1 . ASN D 1 197 ? 20.69900  53.08200  66.69600  1.000 98.20981  ?  197 ASN D OD1 1 
ATOM   6676 N  ND2 . ASN D 1 197 ? 18.78700  53.97400  67.46400  1.000 100.22969 ?  197 ASN D ND2 1 
ATOM   6677 N  N   . ARG D 1 198 ? 20.55900  50.47000  64.56100  1.000 100.83368 ?  198 ARG D N   1 
ATOM   6678 C  CA  . ARG D 1 198 ? 21.73000  50.20900  63.73100  1.000 100.77311 ?  198 ARG D CA  1 
ATOM   6679 C  C   . ARG D 1 198 ? 22.86800  51.16300  64.06200  1.000 104.52683 ?  198 ARG D C   1 
ATOM   6680 O  O   . ARG D 1 198 ? 24.03200  50.74900  64.12200  1.000 102.45935 ?  198 ARG D O   1 
ATOM   6681 C  CB  . ARG D 1 198 ? 21.35700  50.32500  62.25600  1.000 105.35324 ?  198 ARG D CB  1 
ATOM   6682 C  CG  . ARG D 1 198 ? 20.37300  49.28600  61.77200  1.000 105.37020 ?  198 ARG D CG  1 
ATOM   6683 C  CD  . ARG D 1 198 ? 20.09100  49.49000  60.29800  1.000 111.80422 ?  198 ARG D CD  1 
ATOM   6684 N  NE  . ARG D 1 198 ? 19.88000  50.89700  59.97800  1.000 117.23559 ?  198 ARG D NE  1 
ATOM   6685 C  CZ  . ARG D 1 198 ? 19.60300  51.35000  58.76400  1.000 121.71791 ?  198 ARG D CZ  1 
ATOM   6686 N  NH1 . ARG D 1 198 ? 19.53600  50.53600  57.72300  1.000 115.81515 ?  198 ARG D NH1 1 
ATOM   6687 N  NH2 . ARG D 1 198 ? 19.30900  52.63700  58.60200  1.000 127.15057 ?  198 ARG D NH2 1 
ATOM   6688 N  N   . GLU D 1 199 ? 22.55200  52.43900  64.29700  1.000 108.39715 ?  199 GLU D N   1 
ATOM   6689 C  CA  . GLU D 1 199 ? 23.59000  53.42800  64.57400  1.000 106.57027 ?  199 GLU D CA  1 
ATOM   6690 C  C   . GLU D 1 199 ? 24.21200  53.21100  65.94800  1.000 105.83835 ?  199 GLU D C   1 
ATOM   6691 O  O   . GLU D 1 199 ? 25.43500  53.31900  66.10500  1.000 106.20529 ?  199 GLU D O   1 
ATOM   6692 C  CB  . GLU D 1 199 ? 23.00700  54.83500  64.44800  1.000 106.18425 ?  199 GLU D CB  1 
ATOM   6693 C  CG  . GLU D 1 199 ? 22.41500  55.14500  63.07100  1.000 110.48496 ?  199 GLU D CG  1 
ATOM   6694 C  CD  . GLU D 1 199 ? 20.98500  54.65500  62.89600  1.000 111.35984 ?  199 GLU D CD  1 
ATOM   6695 O  OE1 . GLU D 1 199 ? 20.64900  53.56900  63.41400  1.000 106.57356 ?  199 GLU D OE1 1 
ATOM   6696 O  OE2 . GLU D 1 199 ? 20.19700  55.35900  62.23000  1.000 115.80959 -1 199 GLU D OE2 1 
ATOM   6697 N  N   . THR D 1 200 ? 23.39200  52.91800  66.96100  1.000 102.97371 ?  200 THR D N   1 
ATOM   6698 C  CA  . THR D 1 200 ? 23.95200  52.64700  68.28000  1.000 106.72978 ?  200 THR D CA  1 
ATOM   6699 C  C   . THR D 1 200 ? 24.81600  51.39500  68.25000  1.000 107.89522 ?  200 THR D C   1 
ATOM   6700 O  O   . THR D 1 200 ? 25.90300  51.37200  68.83400  1.000 109.99941 ?  200 THR D O   1 
ATOM   6701 C  CB  . THR D 1 200 ? 22.83800  52.50200  69.32000  1.000 97.42481  ?  200 THR D CB  1 
ATOM   6702 O  OG1 . THR D 1 200 ? 21.90400  51.49900  68.89600  1.000 98.79691  ?  200 THR D OG1 1 
ATOM   6703 C  CG2 . THR D 1 200 ? 22.11100  53.82300  69.52500  1.000 99.35243  ?  200 THR D CG2 1 
ATOM   6704 N  N   . LEU D 1 201 ? 24.37900  50.36700  67.52100  1.000 102.35032 ?  201 LEU D N   1 
ATOM   6705 C  CA  . LEU D 1 201 ? 25.16700  49.14400  67.41100  1.000 99.50154  ?  201 LEU D CA  1 
ATOM   6706 C  C   . LEU D 1 201 ? 26.57200  49.42600  66.89600  1.000 100.97109 ?  201 LEU D C   1 
ATOM   6707 O  O   . LEU D 1 201 ? 27.54600  48.83300  67.37500  1.000 100.25058 ?  201 LEU D O   1 
ATOM   6708 C  CB  . LEU D 1 201 ? 24.45600  48.13500  66.51000  1.000 97.96904  ?  201 LEU D CB  1 
ATOM   6709 C  CG  . LEU D 1 201 ? 25.22000  46.82800  66.28900  1.000 96.85011  ?  201 LEU D CG  1 
ATOM   6710 C  CD1 . LEU D 1 201 ? 25.15800  45.95000  67.53000  1.000 86.61535  ?  201 LEU D CD1 1 
ATOM   6711 C  CD2 . LEU D 1 201 ? 24.68900  46.08900  65.07200  1.000 89.45962  ?  201 LEU D CD2 1 
ATOM   6712 N  N   . GLU D 1 202 ? 26.70100  50.32700  65.92100  1.000 103.63392 ?  202 GLU D N   1 
ATOM   6713 C  CA  . GLU D 1 202 ? 28.01600  50.59900  65.34800  1.000 106.91242 ?  202 GLU D CA  1 
ATOM   6714 C  C   . GLU D 1 202 ? 28.93700  51.30800  66.33600  1.000 107.83757 ?  202 GLU D C   1 
ATOM   6715 O  O   . GLU D 1 202 ? 29.98100  50.76700  66.71400  1.000 106.75786 ?  202 GLU D O   1 
ATOM   6716 C  CB  . GLU D 1 202 ? 27.86500  51.42000  64.06700  1.000 101.63664 ?  202 GLU D CB  1 
ATOM   6717 C  CG  . GLU D 1 202 ? 27.06800  50.72500  62.97800  1.000 103.14920 ?  202 GLU D CG  1 
ATOM   6718 C  CD  . GLU D 1 202 ? 27.67700  49.40100  62.56300  1.000 104.01620 ?  202 GLU D CD  1 
ATOM   6719 O  OE1 . GLU D 1 202 ? 28.91000  49.24300  62.69000  1.000 105.30048 ?  202 GLU D OE1 1 
ATOM   6720 O  OE2 . GLU D 1 202 ? 26.92000  48.51600  62.11100  1.000 98.13816  -1 202 GLU D OE2 1 
ATOM   6721 N  N   . GLN D 1 203 ? 28.56100  52.50600  66.79000  1.000 110.58415 ?  203 GLN D N   1 
ATOM   6722 C  CA  . GLN D 1 203 ? 29.44500  53.26800  67.67300  1.000 109.61543 ?  203 GLN D CA  1 
ATOM   6723 C  C   . GLN D 1 203 ? 29.73800  52.53200  68.97500  1.000 110.08760 ?  203 GLN D C   1 
ATOM   6724 O  O   . GLN D 1 203 ? 30.89200  52.46800  69.41400  1.000 111.93709 ?  203 GLN D O   1 
ATOM   6725 C  CB  . GLN D 1 203 ? 28.87300  54.65800  67.95100  1.000 108.88420 ?  203 GLN D CB  1 
ATOM   6726 C  CG  . GLN D 1 203 ? 28.91300  55.60000  66.76100  1.000 117.13277 ?  203 GLN D CG  1 
ATOM   6727 C  CD  . GLN D 1 203 ? 28.26500  56.93600  67.06600  1.000 121.08897 ?  203 GLN D CD  1 
ATOM   6728 O  OE1 . GLN D 1 203 ? 27.59400  57.09700  68.08600  1.000 120.71592 ?  203 GLN D OE1 1 
ATOM   6729 N  NE2 . GLN D 1 203 ? 28.50200  57.91800  66.20300  1.000 122.45290 ?  203 GLN D NE2 1 
ATOM   6730 N  N   . ARG D 1 204 ? 28.70500  51.96800  69.60200  1.000 109.36126 ?  204 ARG D N   1 
ATOM   6731 C  CA  . ARG D 1 204 ? 28.88200  51.26800  70.87100  1.000 106.55048 ?  204 ARG D CA  1 
ATOM   6732 C  C   . ARG D 1 204 ? 29.95300  50.18900  70.74000  1.000 108.07982 ?  204 ARG D C   1 
ATOM   6733 O  O   . ARG D 1 204 ? 30.81800  50.04600  71.61200  1.000 110.17427 ?  204 ARG D O   1 
ATOM   6734 C  CB  . ARG D 1 204 ? 27.55000  50.65200  71.30700  1.000 104.70925 ?  204 ARG D CB  1 
ATOM   6735 C  CG  . ARG D 1 204 ? 26.42100  51.65300  71.58900  1.000 107.75328 ?  204 ARG D CG  1 
ATOM   6736 C  CD  . ARG D 1 204 ? 26.58900  52.58900  72.76200  1.000 113.02587 ?  204 ARG D CD  1 
ATOM   6737 N  NE  . ARG D 1 204 ? 25.42200  53.44500  72.89400  1.000 116.15621 ?  204 ARG D NE  1 
ATOM   6738 C  CZ  . ARG D 1 204 ? 25.34700  54.51500  73.67000  1.000 120.35903 ?  204 ARG D CZ  1 
ATOM   6739 N  NH1 . ARG D 1 204 ? 26.36400  54.89900  74.42300  1.000 119.50495 ?  204 ARG D NH1 1 
ATOM   6740 N  NH2 . ARG D 1 204 ? 24.23500  55.23800  73.65900  1.000 120.07738 ?  204 ARG D NH2 1 
ATOM   6741 N  N   . TYR D 1 205 ? 29.93000  49.49800  69.61200  1.000 106.97011 ?  205 TYR D N   1 
ATOM   6742 C  CA  . TYR D 1 205 ? 30.89800  48.44800  69.39300  1.000 108.39713 ?  205 TYR D CA  1 
ATOM   6743 C  C   . TYR D 1 205 ? 32.26600  49.05600  69.39100  1.000 109.24504 ?  205 TYR D C   1 
ATOM   6744 O  O   . TYR D 1 205 ? 33.10000  48.72800  70.22600  1.000 109.72291 ?  205 TYR D O   1 
ATOM   6745 C  CB  . TYR D 1 205 ? 30.64500  47.74100  68.06700  1.000 100.66054 ?  205 TYR D CB  1 
ATOM   6746 C  CG  . TYR D 1 205 ? 31.75700  46.81000  67.67400  1.000 98.64550  ?  205 TYR D CG  1 
ATOM   6747 C  CD1 . TYR D 1 205 ? 32.22800  45.85400  68.55900  1.000 98.04677  ?  205 TYR D CD1 1 
ATOM   6748 C  CD2 . TYR D 1 205 ? 32.34700  46.89300  66.42600  1.000 105.18005 ?  205 TYR D CD2 1 
ATOM   6749 C  CE1 . TYR D 1 205 ? 33.25400  45.00200  68.20900  1.000 95.20077  ?  205 TYR D CE1 1 
ATOM   6750 C  CE2 . TYR D 1 205 ? 33.37300  46.04400  66.06700  1.000 106.92631 ?  205 TYR D CE2 1 
ATOM   6751 C  CZ  . TYR D 1 205 ? 33.82200  45.10200  66.96400  1.000 99.87058  ?  205 TYR D CZ  1 
ATOM   6752 O  OH  . TYR D 1 205 ? 34.84300  44.25700  66.61300  1.000 101.23545 ?  205 TYR D OH  1 
ATOM   6753 N  N   . ARG D 1 206 ? 32.50500  49.95200  68.45000  1.000 108.11698 ?  206 ARG D N   1 
ATOM   6754 C  CA  . ARG D 1 206 ? 33.82600  50.52500  68.34300  1.000 108.47942 ?  206 ARG D CA  1 
ATOM   6755 C  C   . ARG D 1 206 ? 34.16300  51.14100  69.67300  1.000 113.08934 ?  206 ARG D C   1 
ATOM   6756 O  O   . ARG D 1 206 ? 35.25600  50.93300  70.19900  1.000 113.30188 ?  206 ARG D O   1 
ATOM   6757 C  CB  . ARG D 1 206 ? 33.87000  51.55200  67.22800  1.000 106.69012 ?  206 ARG D CB  1 
ATOM   6758 C  CG  . ARG D 1 206 ? 33.59900  50.97000  65.85300  1.000 105.17709 ?  206 ARG D CG  1 
ATOM   6759 C  CD  . ARG D 1 206 ? 34.69300  50.01000  65.41600  1.000 107.28985 ?  206 ARG D CD  1 
ATOM   6760 N  NE  . ARG D 1 206 ? 34.45300  49.46300  64.08500  1.000 112.09527 ?  206 ARG D NE  1 
ATOM   6761 C  CZ  . ARG D 1 206 ? 35.12100  48.44200  63.56400  1.000 107.29470 ?  206 ARG D CZ  1 
ATOM   6762 N  NH1 . ARG D 1 206 ? 36.08100  47.85000  64.25900  1.000 104.62730 ?  206 ARG D NH1 1 
ATOM   6763 N  NH2 . ARG D 1 206 ? 34.83100  48.01300  62.34500  1.000 110.35476 ?  206 ARG D NH2 1 
ATOM   6764 N  N   . HIS D 1 207 ? 33.21700  51.88100  70.23500  1.000 113.47521 ?  207 HIS D N   1 
ATOM   6765 C  CA  . HIS D 1 207 ? 33.42600  52.46800  71.54100  1.000 112.77911 ?  207 HIS D CA  1 
ATOM   6766 C  C   . HIS D 1 207 ? 33.94100  51.40600  72.47500  1.000 114.80803 ?  207 HIS D C   1 
ATOM   6767 O  O   . HIS D 1 207 ? 35.05500  51.49800  72.98100  1.000 115.69322 ?  207 HIS D O   1 
ATOM   6768 C  CB  . HIS D 1 207 ? 32.11800  53.02900  72.07500  1.000 110.06971 ?  207 HIS D CB  1 
ATOM   6769 C  CG  . HIS D 1 207 ? 32.27400  53.87600  73.29600  1.000 115.28146 ?  207 HIS D CG  1 
ATOM   6770 N  ND1 . HIS D 1 207 ? 31.27000  54.69700  73.76200  1.000 111.78164 ?  207 HIS D ND1 1 
ATOM   6771 C  CD2 . HIS D 1 207 ? 33.31400  54.03100  74.14800  1.000 118.80530 ?  207 HIS D CD2 1 
ATOM   6772 C  CE1 . HIS D 1 207 ? 31.68400  55.32100  74.84900  1.000 112.37237 ?  207 HIS D CE1 1 
ATOM   6773 N  NE2 . HIS D 1 207 ? 32.92100  54.93500  75.10500  1.000 120.21406 ?  207 HIS D NE2 1 
ATOM   6774 N  N   . GLY D 1 208 ? 33.13000  50.38600  72.70200  1.000 109.10731 ?  208 GLY D N   1 
ATOM   6775 C  CA  . GLY D 1 208 ? 33.52000  49.32800  73.62300  1.000 106.34519 ?  208 GLY D CA  1 
ATOM   6776 C  C   . GLY D 1 208 ? 34.97600  48.92100  73.48400  1.000 107.17571 ?  208 GLY D C   1 
ATOM   6777 O  O   . GLY D 1 208 ? 35.67200  48.71800  74.48200  1.000 114.64098 ?  208 GLY D O   1 
ATOM   6778 N  N   . ILE D 1 209 ? 35.45500  48.79400  72.24400  1.000 110.40399 ?  209 ILE D N   1 
ATOM   6779 C  CA  . ILE D 1 209 ? 36.81100  48.30400  72.02100  1.000 112.72505 ?  209 ILE D CA  1 
ATOM   6780 C  C   . ILE D 1 209 ? 37.84700  49.33000  72.47000  1.000 113.90963 ?  209 ILE D C   1 
ATOM   6781 O  O   . ILE D 1 209 ? 38.96300  48.96500  72.85800  1.000 115.60806 ?  209 ILE D O   1 
ATOM   6782 C  CB  . ILE D 1 209 ? 37.00000  47.92600  70.53900  1.000 106.42128 ?  209 ILE D CB  1 
ATOM   6783 C  CG1 . ILE D 1 209 ? 35.90600  46.95700  70.08100  1.000 100.37529 ?  209 ILE D CG1 1 
ATOM   6784 C  CG2 . ILE D 1 209 ? 38.36400  47.29800  70.30200  1.000 101.62842 ?  209 ILE D CG2 1 
ATOM   6785 C  CD1 . ILE D 1 209 ? 35.91500  45.62600  70.80200  1.000 102.31436 ?  209 ILE D CD1 1 
ATOM   6786 N  N   . SER D 1 210 ? 37.49500  50.61900  72.45600  1.000 116.25537 ?  210 SER D N   1 
ATOM   6787 C  CA  . SER D 1 210 ? 38.51300  51.65500  72.61200  1.000 121.00116 ?  210 SER D CA  1 
ATOM   6788 C  C   . SER D 1 210 ? 38.98800  51.76900  74.06200  1.000 121.05704 ?  210 SER D C   1 
ATOM   6789 O  O   . SER D 1 210 ? 40.19500  51.89600  74.31100  1.000 122.70254 ?  210 SER D O   1 
ATOM   6790 C  CB  . SER D 1 210 ? 37.96500  52.99200  72.12500  1.000 123.48043 ?  210 SER D CB  1 
ATOM   6791 O  OG  . SER D 1 210 ? 36.88100  53.42900  72.92700  1.000 122.06756 ?  210 SER D OG  1 
ATOM   6792 N  N   . ASN D 1 211 ? 38.06500  51.72300  75.02600  1.000 122.48037 ?  211 ASN D N   1 
ATOM   6793 C  CA  . ASN D 1 211 ? 38.45600  51.79700  76.43200  1.000 120.84255 ?  211 ASN D CA  1 
ATOM   6794 C  C   . ASN D 1 211 ? 39.31200  50.61100  76.84800  1.000 117.97680 ?  211 ASN D C   1 
ATOM   6795 O  O   . ASN D 1 211 ? 40.21400  50.76100  77.67600  1.000 124.54066 ?  211 ASN D O   1 
ATOM   6796 C  CB  . ASN D 1 211 ? 37.21500  51.91300  77.31000  1.000 123.56971 ?  211 ASN D CB  1 
ATOM   6797 C  CG  . ASN D 1 211 ? 36.68400  53.32000  77.37600  1.000 130.18640 ?  211 ASN D CG  1 
ATOM   6798 O  OD1 . ASN D 1 211 ? 37.46000  54.26700  77.46200  1.000 132.65663 ?  211 ASN D OD1 1 
ATOM   6799 N  ND2 . ASN D 1 211 ? 35.36400  53.47500  77.28800  1.000 128.15372 ?  211 ASN D ND2 1 
ATOM   6800 N  N   . LEU D 1 212 ? 39.05400  49.42800  76.28000  1.000 111.91777 ?  212 LEU D N   1 
ATOM   6801 C  CA  . LEU D 1 212 ? 39.87700  48.27400  76.61800  1.000 115.32142 ?  212 LEU D CA  1 
ATOM   6802 C  C   . LEU D 1 212 ? 41.31600  48.49400  76.18000  1.000 119.07792 ?  212 LEU D C   1 
ATOM   6803 O  O   . LEU D 1 212 ? 42.24200  47.97000  76.80900  1.000 120.22740 ?  212 LEU D O   1 
ATOM   6804 C  CB  . LEU D 1 212 ? 39.31100  47.00500  75.97800  1.000 111.85864 ?  212 LEU D CB  1 
ATOM   6805 C  CG  . LEU D 1 212 ? 37.90300  46.55100  76.36000  1.000 108.41811 ?  212 LEU D CG  1 
ATOM   6806 C  CD1 . LEU D 1 212 ? 37.36500  45.58600  75.31000  1.000 111.41500 ?  212 LEU D CD1 1 
ATOM   6807 C  CD2 . LEU D 1 212 ? 37.89200  45.90800  77.73500  1.000 107.53072 ?  212 LEU D CD2 1 
ATOM   6808 N  N   . LYS D 1 213 ? 41.52400  49.25900  75.10200  1.000 123.93758 ?  213 LYS D N   1 
ATOM   6809 C  CA  . LYS D 1 213 ? 42.86900  49.61700  74.66500  1.000 126.76765 ?  213 LYS D CA  1 
ATOM   6810 C  C   . LYS D 1 213 ? 43.61800  50.42400  75.72000  1.000 129.45416 ?  213 LYS D C   1 
ATOM   6811 O  O   . LYS D 1 213 ? 44.84500  50.55400  75.63400  1.000 131.92496 ?  213 LYS D O   1 
ATOM   6812 C  CB  . LYS D 1 213 ? 42.80900  50.40400  73.35300  1.000 122.74897 ?  213 LYS D CB  1 
ATOM   6813 C  CG  . LYS D 1 213 ? 42.03000  49.71900  72.23200  1.000 123.67308 ?  213 LYS D CG  1 
ATOM   6814 C  CD  . LYS D 1 213 ? 42.83300  48.63000  71.53700  1.000 124.70979 ?  213 LYS D CD  1 
ATOM   6815 C  CE  . LYS D 1 213 ? 44.05600  49.17600  70.82600  1.000 127.19814 ?  213 LYS D CE  1 
ATOM   6816 N  NZ  . LYS D 1 213 ? 44.71200  48.11400  70.01100  1.000 121.21480 ?  213 LYS D NZ  1 
ATOM   6817 N  N   . LEU D 1 214 ? 42.91000  50.98000  76.69900  1.000 128.08311 ?  214 LEU D N   1 
ATOM   6818 C  CA  . LEU D 1 214 ? 43.51200  51.86200  77.69400  1.000 126.97152 ?  214 LEU D CA  1 
ATOM   6819 C  C   . LEU D 1 214 ? 43.76700  51.13600  79.01200  1.000 124.89929 ?  214 LEU D C   1 
ATOM   6820 O  O   . LEU D 1 214 ? 44.24500  50.00200  79.03000  1.000 124.57097 ?  214 LEU D O   1 
ATOM   6821 C  CB  . LEU D 1 214 ? 42.61600  53.07700  77.93800  1.000 128.45183 ?  214 LEU D CB  1 
ATOM   6822 C  CG  . LEU D 1 214 ? 41.85000  53.62200  76.72900  1.000 128.45804 ?  214 LEU D CG  1 
ATOM   6823 C  CD1 . LEU D 1 214 ? 40.92100  54.75300  77.14400  1.000 130.43070 ?  214 LEU D CD1 1 
ATOM   6824 C  CD2 . LEU D 1 214 ? 42.80100  54.08200  75.63200  1.000 122.78974 ?  214 LEU D CD2 1 
HETATM 6825 ZN ZN  . ZN  E 2 .   ? 8.35300   25.18500  75.73100  1.000 79.14168  ?  301 ZN  A ZN  1 
HETATM 6826 ZN ZN  . ZN  F 2 .   ? 25.12100  10.03800  45.54200  1.000 79.09399  ?  301 ZN  B ZN  1 
HETATM 6827 ZN ZN  . ZN  G 2 .   ? 28.81300  33.37600  42.77900  1.000 83.63524  ?  301 ZN  C ZN  1 
HETATM 6828 ZN ZN  . ZN  H 2 .   ? 31.64800  29.11200  79.63500  1.000 81.24974  ?  301 ZN  D ZN  1 
HETATM 6829 O  O   . HOH I 3 .   ? 12.29100  23.35400  80.83100  1.000 66.05349  ?  401 HOH A O   1 
HETATM 6830 O  O   . HOH J 3 .   ? 27.62500  23.02500  37.76800  1.000 73.11250  ?  401 HOH C O   1 
HETATM 6831 O  O   . HOH J 3 .   ? 31.55600  28.52400  39.95200  1.000 71.97291  ?  402 HOH C O   1 
# 
