data_9J1D
# 
_entry.id   9J1D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9J1D         pdb_00009j1d 10.2210/pdb9j1d/pdb 
WWPDB D_1300050151 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J1D 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              guosong@fudan.edu.cn 
_pdbx_contact_author.name_first         Guosong 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7089-911X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, L.'   1 ? 
'Chen, G.' 2 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of ConA/PHE-Man' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, L.'   1 ? 
primary 'Chen, G.' 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 Concanavalin-A 25622.385 2 ? ? ? ? 
2 non-polymer syn 
;~{N}2,~{N}9-bis[2-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethoxy]ethyl]-1,10-phenanthroline-2,9-dicarboxamide
;
766.746   1 ? ? ? ? 
3 non-polymer syn 'CALCIUM ION' 40.078    2 ? ? ? ? 
4 non-polymer syn 'MANGANESE (II) ION' 54.938    2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Con A' 
# 
_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       
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;~{N}2,~{N}9-bis[2-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethoxy]ethyl]-1,10-phenanthroline-2,9-dicarboxamide
;
A1EAW 
3 'CALCIUM ION' CA    
4 'MANGANESE (II) ION' MN    
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   THR n 
1 4   ILE n 
1 5   VAL n 
1 6   ALA n 
1 7   VAL n 
1 8   GLU n 
1 9   LEU n 
1 10  ASP n 
1 11  THR n 
1 12  TYR n 
1 13  PRO n 
1 14  ASN n 
1 15  THR n 
1 16  ASP n 
1 17  ILE n 
1 18  GLY n 
1 19  ASP n 
1 20  PRO n 
1 21  SER n 
1 22  TYR n 
1 23  PRO n 
1 24  HIS n 
1 25  ILE n 
1 26  GLY n 
1 27  ILE n 
1 28  ASP n 
1 29  ILE n 
1 30  LYS n 
1 31  SER n 
1 32  VAL n 
1 33  ARG n 
1 34  SER n 
1 35  LYS n 
1 36  LYS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TRP n 
1 41  ASN n 
1 42  MET n 
1 43  GLN n 
1 44  ASN n 
1 45  GLY n 
1 46  LYS n 
1 47  VAL n 
1 48  GLY n 
1 49  THR n 
1 50  ALA n 
1 51  HIS n 
1 52  ILE n 
1 53  ILE n 
1 54  TYR n 
1 55  ASN n 
1 56  SER n 
1 57  VAL n 
1 58  ASP n 
1 59  LYS n 
1 60  ARG n 
1 61  LEU n 
1 62  SER n 
1 63  ALA n 
1 64  VAL n 
1 65  VAL n 
1 66  SER n 
1 67  TYR n 
1 68  PRO n 
1 69  ASN n 
1 70  ALA n 
1 71  ASP n 
1 72  SER n 
1 73  ALA n 
1 74  THR n 
1 75  VAL n 
1 76  SER n 
1 77  TYR n 
1 78  ASP n 
1 79  VAL n 
1 80  ASP n 
1 81  LEU n 
1 82  ASP n 
1 83  ASN n 
1 84  VAL n 
1 85  LEU n 
1 86  PRO n 
1 87  GLU n 
1 88  TRP n 
1 89  VAL n 
1 90  ARG n 
1 91  VAL n 
1 92  GLY n 
1 93  LEU n 
1 94  SER n 
1 95  ALA n 
1 96  SER n 
1 97  THR n 
1 98  GLY n 
1 99  LEU n 
1 100 TYR n 
1 101 LYS n 
1 102 GLU n 
1 103 THR n 
1 104 ASN n 
1 105 THR n 
1 106 ILE n 
1 107 LEU n 
1 108 SER n 
1 109 TRP n 
1 110 SER n 
1 111 PHE n 
1 112 THR n 
1 113 SER n 
1 114 LYS n 
1 115 LEU n 
1 116 LYS n 
1 117 SER n 
1 118 ASN n 
1 119 SER n 
1 120 THR n 
1 121 HIS n 
1 122 GLU n 
1 123 THR n 
1 124 ASN n 
1 125 ALA n 
1 126 LEU n 
1 127 HIS n 
1 128 PHE n 
1 129 MET n 
1 130 PHE n 
1 131 ASN n 
1 132 GLN n 
1 133 PHE n 
1 134 SER n 
1 135 LYS n 
1 136 ASP n 
1 137 GLN n 
1 138 LYS n 
1 139 ASP n 
1 140 LEU n 
1 141 ILE n 
1 142 LEU n 
1 143 GLN n 
1 144 GLY n 
1 145 ASP n 
1 146 ALA n 
1 147 THR n 
1 148 THR n 
1 149 GLY n 
1 150 THR n 
1 151 ASP n 
1 152 GLY n 
1 153 ASN n 
1 154 LEU n 
1 155 GLU n 
1 156 LEU n 
1 157 THR n 
1 158 ARG n 
1 159 VAL n 
1 160 SER n 
1 161 SER n 
1 162 ASN n 
1 163 GLY n 
1 164 SER n 
1 165 PRO n 
1 166 GLN n 
1 167 GLY n 
1 168 SER n 
1 169 SER n 
1 170 VAL n 
1 171 GLY n 
1 172 ARG n 
1 173 ALA n 
1 174 LEU n 
1 175 PHE n 
1 176 TYR n 
1 177 ALA n 
1 178 PRO n 
1 179 VAL n 
1 180 HIS n 
1 181 ILE n 
1 182 TRP n 
1 183 GLU n 
1 184 SER n 
1 185 SER n 
1 186 ALA n 
1 187 VAL n 
1 188 VAL n 
1 189 ALA n 
1 190 SER n 
1 191 PHE n 
1 192 GLU n 
1 193 ALA n 
1 194 THR n 
1 195 PHE n 
1 196 THR n 
1 197 PHE n 
1 198 LEU n 
1 199 ILE n 
1 200 LYS n 
1 201 SER n 
1 202 PRO n 
1 203 ASP n 
1 204 SER n 
1 205 HIS n 
1 206 PRO n 
1 207 ALA n 
1 208 ASP n 
1 209 GLY n 
1 210 ILE n 
1 211 ALA n 
1 212 PHE n 
1 213 PHE n 
1 214 ILE n 
1 215 SER n 
1 216 ASN n 
1 217 ILE n 
1 218 ASP n 
1 219 SER n 
1 220 SER n 
1 221 ILE n 
1 222 PRO n 
1 223 SER n 
1 224 GLY n 
1 225 SER n 
1 226 THR n 
1 227 GLY n 
1 228 ARG n 
1 229 LEU n 
1 230 LEU n 
1 231 GLY n 
1 232 LEU n 
1 233 PHE n 
1 234 PRO n 
1 235 ASP n 
1 236 ALA n 
1 237 ASN n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_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 
1 1 sample 1   118 'jack bean' 'Canavalia ensiformis' 3823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 119 237 'jack bean' 'Canavalia ensiformis' 3823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1EAW non-polymer         . 
;~{N}2,~{N}9-bis[2-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethoxy]ethyl]-1,10-phenanthroline-2,9-dicarboxamide
;
1,6-DI-O-PHOSPHONO-D-MANNITOL 'C34 H46 N4 O16' 766.746 
ALA   'L-peptide linking' y ALANINE ?                             'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ?                             'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                             'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                             'C4 H7 N O4'     133.103 
CA    non-polymer         . 'CALCIUM ION' ?                             'Ca 2'           40.078  
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 
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 
MN    non-polymer         . 'MANGANESE (II) ION' ?                             'Mn 2'           54.938  
PHE   'L-peptide linking' y PHENYLALANINE ?                             'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ?                             'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ?                             'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ?                             'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                             'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ?                             'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ?                             'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  TYR 12  12  12  TYR TYR A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  ASN 41  41  41  ASN ASN A . n 
A 1 42  MET 42  42  42  MET MET A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  TRP 88  88  88  TRP TRP A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 TRP 109 109 109 TRP TRP A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 PHE 111 111 111 PHE PHE A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   ASP 2   2   2   ASP ASP B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  THR 11  11  11  THR THR B . n 
B 1 12  TYR 12  12  12  TYR TYR B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  THR 15  15  15  THR THR B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  HIS 24  24  24  HIS HIS B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ILE 27  27  27  ILE ILE B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  ILE 29  29  29  ILE ILE B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TRP 40  40  40  TRP TRP B . n 
B 1 41  ASN 41  41  41  ASN ASN B . n 
B 1 42  MET 42  42  42  MET MET B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  HIS 51  51  51  HIS HIS B . n 
B 1 52  ILE 52  52  52  ILE ILE B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ASP 58  58  58  ASP ASP B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  TRP 88  88  88  TRP TRP B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  THR 97  97  97  THR THR B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 TYR 100 100 100 TYR TYR B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 THR 103 103 103 THR THR B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 TRP 109 109 109 TRP TRP B . n 
B 1 110 SER 110 110 110 SER SER B . n 
B 1 111 PHE 111 111 111 PHE PHE B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 SER 119 119 119 SER SER B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 HIS 127 127 127 HIS HIS B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 MET 129 129 129 MET MET B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLN 132 132 132 GLN GLN B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 GLN 137 137 137 GLN GLN B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 GLN 143 143 143 GLN GLN B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 THR 150 150 150 THR THR B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 ASN 153 153 153 ASN ASN B . n 
B 1 154 LEU 154 154 154 LEU LEU B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 ARG 158 158 158 ARG ARG B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 SER 161 161 161 SER SER B . n 
B 1 162 ASN 162 162 162 ASN ASN B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 GLN 166 166 166 GLN GLN B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 VAL 170 170 170 VAL VAL B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 TYR 176 176 176 TYR TYR B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 PRO 178 178 178 PRO PRO B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 HIS 180 180 180 HIS HIS B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 TRP 182 182 182 TRP TRP B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 PHE 191 191 191 PHE PHE B . n 
B 1 192 GLU 192 192 192 GLU GLU B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 PHE 195 195 195 PHE PHE B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 PHE 197 197 197 PHE PHE B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 LYS 200 200 200 LYS LYS B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 HIS 205 205 205 HIS HIS B . n 
B 1 206 PRO 206 206 206 PRO PRO B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 PHE 212 212 212 PHE PHE B . n 
B 1 213 PHE 213 213 213 PHE PHE B . n 
B 1 214 ILE 214 214 214 ILE ILE B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 PRO 222 222 222 PRO PRO B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 PHE 233 233 233 PHE PHE B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ALA 236 236 236 ALA ALA B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EAW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EAW 
_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 
C 2 A1EAW 1 301 301 A1EAW M2P A . 
D 3 CA    1 302 1   CA    CA  A . 
E 4 MN    1 303 1   MN    MN  A . 
F 3 CA    1 301 2   CA    CA  B . 
G 4 MN    1 302 2   MN    MN  B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.18.2-3874-000)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                   2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .                   3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                   4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J1D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     141.430 
_cell.length_a_esd                 ? 
_cell.length_b                     141.430 
_cell.length_b_esd                 ? 
_cell.length_c                     80.410 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9J1D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_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                   9J1D 
_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             3.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          68.65 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Tris-HCl pH 8.5, 2.0M Ammonium phosphate monobasic' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-13 
_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   0.979 
_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                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9J1D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.49 
_reflns.d_resolution_low                               63.25 
_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                                     10870 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                24.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.190 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       264888 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.186 
_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                                    3.49 
_reflns_shell.d_res_low                                     3.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           20492 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             782 
_reflns_shell.percent_possible_obs                          99.9 
_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                               26.2 
_reflns_shell.pdbx_chi_squared                              0.93 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     4.1 
_reflns_shell.pdbx_Rrim_I_all                               1.090 
_reflns_shell.pdbx_Rpim_I_all                               0.212 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.880 
_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                                  1.069 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9J1D 
_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                            3.49 
_refine.ls_d_res_low                             53.10 
_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                     10822 
_refine.ls_number_reflns_R_free                  535 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1979 
_refine.ls_R_factor_R_free                       0.2291 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1963 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4P9W 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.52 
_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                            0.44 
_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                       3.49 
_refine_hist.d_res_low                        53.10 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3676 
_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        3618 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_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' ? 0.012  ? 3760 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.833  ? 5128 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.039 ? 532  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.075  ? 590  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 655  ? f_plane_restr      ? ? 
# 
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' 3.49 3.84  . . 133 2507 100.00 . . . . 0.2640 . . . . . . . . . . . 0.3106 
'X-RAY DIFFRACTION' 3.84 4.40  . . 135 2526 100.00 . . . . 0.2231 . . . . . . . . . . . 0.2751 
'X-RAY DIFFRACTION' 4.40 5.54  . . 130 2562 100.00 . . . . 0.1761 . . . . . . . . . . . 0.1930 
'X-RAY DIFFRACTION' 5.54 53.10 . . 137 2692 99.00  . . . . 0.1796 . . . . . . . . . . . 0.2103 
# 
_struct.entry_id                     9J1D 
_struct.title                        'Structure of ConA/PHE-Man' 
_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        9J1D 
_struct_keywords.text            'Complex, Lectin, Ligand, SUGAR BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'SUGAR BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CONA_CANEN P02866 ? 1 
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSN
;
164 
2 UNP CONA_CANEN P02866 ? 1 
;STHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFL
IKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
30  
# 
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 9J1D A 1   ? 118 ? P02866 164 ? 281 ? 1   118 
2 2 9J1D A 119 ? 237 ? P02866 30  ? 148 ? 119 237 
3 1 9J1D B 1   ? 118 ? P02866 164 ? 281 ? 1   118 
4 2 9J1D B 119 ? 237 ? P02866 30  ? 148 ? 119 237 
# 
_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)' 10070 ? 
1 MORE         -89   ? 
1 'SSA (A^2)'  34220 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z  1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASN A 14  ? GLY A 18  ? ASN A 14  GLY A 18  5 ? 5 
HELX_P HELX_P2 AA2 ASP A 80  ? LEU A 85  ? ASP A 80  LEU A 85  1 ? 6 
HELX_P HELX_P3 AA3 THR A 150 ? GLY A 152 ? THR A 150 GLY A 152 5 ? 3 
HELX_P HELX_P4 AA4 ASP B 80  ? LEU B 85  ? ASP B 80  LEU B 85  1 ? 6 
# 
_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 GLU 8  OE2 ? ? ? 1_555 E MN . MN ? ? A GLU 8  A MN 303 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc2  metalc ? ? A ASP 10 OD1 ? ? ? 1_555 D CA . CA ? ? A ASP 10 A CA 302 1_555 ? ? ? ? ? ? ? 3.185 ? ? 
metalc3  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 E MN . MN ? ? A ASP 10 A MN 303 1_555 ? ? ? ? ? ? ? 1.849 ? ? 
metalc4  metalc ? ? A TYR 12 O   ? ? ? 1_555 D CA . CA ? ? A TYR 12 A CA 302 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
metalc5  metalc ? ? A ASN 14 OD1 ? ? ? 1_555 D CA . CA ? ? A ASN 14 A CA 302 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc6  metalc ? ? A ASP 19 OD2 ? ? ? 1_555 D CA . CA ? ? A ASP 19 A CA 302 1_555 ? ? ? ? ? ? ? 2.484 ? ? 
metalc7  metalc ? ? A ASP 19 OD1 ? ? ? 1_555 E MN . MN ? ? A ASP 19 A MN 303 1_555 ? ? ? ? ? ? ? 1.907 ? ? 
metalc8  metalc ? ? A HIS 24 NE2 ? ? ? 1_555 E MN . MN ? ? A HIS 24 A MN 303 1_555 ? ? ? ? ? ? ? 2.411 ? ? 
metalc9  metalc ? ? B GLU 8  OE1 ? ? ? 1_555 G MN . MN ? ? B GLU 8  B MN 302 1_555 ? ? ? ? ? ? ? 2.680 ? ? 
metalc10 metalc ? ? B GLU 8  OE2 ? ? ? 1_555 G MN . MN ? ? B GLU 8  B MN 302 1_555 ? ? ? ? ? ? ? 2.597 ? ? 
metalc11 metalc ? ? B ASP 10 OD1 ? ? ? 1_555 F CA . CA ? ? B ASP 10 B CA 301 1_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc12 metalc ? ? B ASP 10 OD2 ? ? ? 1_555 G MN . MN ? ? B ASP 10 B MN 302 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc13 metalc ? ? B TYR 12 O   ? ? ? 1_555 F CA . CA ? ? B TYR 12 B CA 301 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc14 metalc ? ? B ASP 19 OD2 ? ? ? 1_555 F CA . CA ? ? B ASP 19 B CA 301 1_555 ? ? ? ? ? ? ? 3.114 ? ? 
metalc15 metalc ? ? B ASP 19 OD1 ? ? ? 1_555 G MN . MN ? ? B ASP 19 B MN 302 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc16 metalc ? ? B ASP 19 OD2 ? ? ? 1_555 G MN . MN ? ? B ASP 19 B MN 302 1_555 ? ? ? ? ? ? ? 2.553 ? ? 
# 
_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  OE2 ? A GLU 8  ? A GLU 8  ? 1_555 MN ? E MN . ? A MN 303 ? 1_555 OD2 ? A ASP 10 ? A ASP 10 ? 1_555 96.8  ? 
2  OE2 ? A GLU 8  ? A GLU 8  ? 1_555 MN ? E MN . ? A MN 303 ? 1_555 OD1 ? A ASP 19 ? A ASP 19 ? 1_555 159.7 ? 
3  OD2 ? A ASP 10 ? A ASP 10 ? 1_555 MN ? E MN . ? A MN 303 ? 1_555 OD1 ? A ASP 19 ? A ASP 19 ? 1_555 96.5  ? 
4  OE2 ? A GLU 8  ? A GLU 8  ? 1_555 MN ? E MN . ? A MN 303 ? 1_555 NE2 ? A HIS 24 ? A HIS 24 ? 1_555 95.3  ? 
5  OD2 ? A ASP 10 ? A ASP 10 ? 1_555 MN ? E MN . ? A MN 303 ? 1_555 NE2 ? A HIS 24 ? A HIS 24 ? 1_555 70.1  ? 
6  OD1 ? A ASP 19 ? A ASP 19 ? 1_555 MN ? E MN . ? A MN 303 ? 1_555 NE2 ? A HIS 24 ? A HIS 24 ? 1_555 75.1  ? 
7  OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12 ? 1_555 103.6 ? 
8  OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 166.2 ? 
9  O   ? A TYR 12 ? A TYR 12 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 86.4  ? 
10 OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 95.0  ? 
11 O   ? A TYR 12 ? A TYR 12 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 82.6  ? 
12 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 95.8  ? 
13 OE1 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OE2 ? B GLU 8  ? B GLU 8  ? 1_555 49.0  ? 
14 OE1 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD2 ? B ASP 10 ? B ASP 10 ? 1_555 97.4  ? 
15 OE2 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD2 ? B ASP 10 ? B ASP 10 ? 1_555 73.3  ? 
16 OE1 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19 ? 1_555 130.7 ? 
17 OE2 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19 ? 1_555 82.6  ? 
18 OD2 ? B ASP 10 ? B ASP 10 ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19 ? 1_555 73.2  ? 
19 OE1 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD2 ? B ASP 19 ? B ASP 19 ? 1_555 158.7 ? 
20 OE2 ? B GLU 8  ? B GLU 8  ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD2 ? B ASP 19 ? B ASP 19 ? 1_555 124.1 ? 
21 OD2 ? B ASP 10 ? B ASP 10 ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD2 ? B ASP 19 ? B ASP 19 ? 1_555 62.6  ? 
22 OD1 ? B ASP 19 ? B ASP 19 ? 1_555 MN ? G MN . ? B MN 302 ? 1_555 OD2 ? B ASP 19 ? B ASP 19 ? 1_555 53.8  ? 
23 OD1 ? B ASP 10 ? B ASP 10 ? 1_555 CA ? F CA . ? B CA 301 ? 1_555 O   ? B TYR 12 ? B TYR 12 ? 1_555 106.9 ? 
24 OD1 ? B ASP 10 ? B ASP 10 ? 1_555 CA ? F CA . ? B CA 301 ? 1_555 OD2 ? B ASP 19 ? B ASP 19 ? 1_555 87.5  ? 
25 O   ? B TYR 12 ? B TYR 12 ? 1_555 CA ? F CA . ? B CA 301 ? 1_555 OD2 ? B ASP 19 ? B ASP 19 ? 1_555 86.7  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 207 A . ? ALA 207 A ASP 208 A ? ASP 208 A 1 -6.30 
2 ALA 207 B . ? ALA 207 B ASP 208 B ? ASP 208 B 1 -5.82 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 6 ? 
AA7 ? 6 ? 
AA8 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 36  ? LYS A 39  ? LYS A 36  LYS A 39  
AA1 2 HIS A 24  ? ILE A 29  ? HIS A 24  ILE A 29  
AA1 3 ILE A 4   ? ASP A 10  ? ILE A 4   ASP A 10  
AA1 4 GLY A 209 ? ASN A 216 ? GLY A 209 ASN A 216 
AA1 5 TRP A 88  ? SER A 96  ? TRP A 88  SER A 96  
AA1 6 VAL A 170 ? PHE A 175 ? VAL A 170 PHE A 175 
AA1 7 LEU A 140 ? GLY A 144 ? LEU A 140 GLY A 144 
AA2 1 LYS A 36  ? LYS A 39  ? LYS A 36  LYS A 39  
AA2 2 HIS A 24  ? ILE A 29  ? HIS A 24  ILE A 29  
AA2 3 ILE A 4   ? ASP A 10  ? ILE A 4   ASP A 10  
AA2 4 GLY A 209 ? ASN A 216 ? GLY A 209 ASN A 216 
AA2 5 TRP A 88  ? SER A 96  ? TRP A 88  SER A 96  
AA2 6 VAL A 179 ? HIS A 180 ? VAL A 179 HIS A 180 
AA3 1 ALA A 73  ? ASP A 78  ? ALA A 73  ASP A 78  
AA3 2 ARG A 60  ? SER A 66  ? ARG A 60  SER A 66  
AA3 3 VAL A 47  ? ASN A 55  ? VAL A 47  ASN A 55  
AA3 4 PHE A 191 ? LEU A 198 ? PHE A 191 LEU A 198 
AA3 5 THR A 105 ? LYS A 114 ? THR A 105 LYS A 114 
AA3 6 ALA A 125 ? PHE A 130 ? ALA A 125 PHE A 130 
AA4 1 ALA A 73  ? ASP A 78  ? ALA A 73  ASP A 78  
AA4 2 ARG A 60  ? SER A 66  ? ARG A 60  SER A 66  
AA4 3 VAL A 47  ? ASN A 55  ? VAL A 47  ASN A 55  
AA4 4 PHE A 191 ? LEU A 198 ? PHE A 191 LEU A 198 
AA4 5 THR A 105 ? LYS A 114 ? THR A 105 LYS A 114 
AA4 6 LEU A 154 ? GLU A 155 ? LEU A 154 GLU A 155 
AA4 7 THR A 147 ? THR A 148 ? THR A 147 THR A 148 
AA5 1 SER B 34  ? LYS B 39  ? SER B 34  LYS B 39  
AA5 2 HIS B 24  ? ILE B 29  ? HIS B 24  ILE B 29  
AA5 3 ILE B 4   ? ASP B 10  ? ILE B 4   ASP B 10  
AA5 4 GLY B 209 ? ASN B 216 ? GLY B 209 ASN B 216 
AA5 5 TRP B 88  ? SER B 96  ? TRP B 88  SER B 96  
AA5 6 VAL B 170 ? PHE B 175 ? VAL B 170 PHE B 175 
AA5 7 LEU B 140 ? GLY B 144 ? LEU B 140 GLY B 144 
AA6 1 SER B 34  ? LYS B 39  ? SER B 34  LYS B 39  
AA6 2 HIS B 24  ? ILE B 29  ? HIS B 24  ILE B 29  
AA6 3 ILE B 4   ? ASP B 10  ? ILE B 4   ASP B 10  
AA6 4 GLY B 209 ? ASN B 216 ? GLY B 209 ASN B 216 
AA6 5 TRP B 88  ? SER B 96  ? TRP B 88  SER B 96  
AA6 6 VAL B 179 ? HIS B 180 ? VAL B 179 HIS B 180 
AA7 1 SER B 72  ? ASP B 78  ? SER B 72  ASP B 78  
AA7 2 ARG B 60  ? SER B 66  ? ARG B 60  SER B 66  
AA7 3 LYS B 46  ? ASN B 55  ? LYS B 46  ASN B 55  
AA7 4 VAL B 188 ? ILE B 199 ? VAL B 188 ILE B 199 
AA7 5 THR B 105 ? LYS B 116 ? THR B 105 LYS B 116 
AA7 6 ALA B 125 ? PHE B 130 ? ALA B 125 PHE B 130 
AA8 1 SER B 72  ? ASP B 78  ? SER B 72  ASP B 78  
AA8 2 ARG B 60  ? SER B 66  ? ARG B 60  SER B 66  
AA8 3 LYS B 46  ? ASN B 55  ? LYS B 46  ASN B 55  
AA8 4 VAL B 188 ? ILE B 199 ? VAL B 188 ILE B 199 
AA8 5 THR B 105 ? LYS B 116 ? THR B 105 LYS B 116 
AA8 6 ASN B 153 ? GLU B 155 ? ASN B 153 GLU B 155 
AA8 7 THR B 147 ? THR B 150 ? THR B 147 THR B 150 
# 
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 LYS A 36  ? O LYS A 36  N ILE A 27  ? N ILE A 27  
AA1 2 3 O GLY A 26  ? O GLY A 26  N GLU A 8   ? N GLU A 8   
AA1 3 4 N VAL A 5   ? N VAL A 5   O ILE A 214 ? O ILE A 214 
AA1 4 5 O ALA A 211 ? O ALA A 211 N SER A 94  ? N SER A 94  
AA1 5 6 N VAL A 91  ? N VAL A 91  O PHE A 175 ? O PHE A 175 
AA1 6 7 O ARG A 172 ? O ARG A 172 N GLN A 143 ? N GLN A 143 
AA2 1 2 O LYS A 36  ? O LYS A 36  N ILE A 27  ? N ILE A 27  
AA2 2 3 O GLY A 26  ? O GLY A 26  N GLU A 8   ? N GLU A 8   
AA2 3 4 N VAL A 5   ? N VAL A 5   O ILE A 214 ? O ILE A 214 
AA2 4 5 O ALA A 211 ? O ALA A 211 N SER A 94  ? N SER A 94  
AA2 5 6 N VAL A 89  ? N VAL A 89  O VAL A 179 ? O VAL A 179 
AA3 1 2 O ALA A 73  ? O ALA A 73  N VAL A 65  ? N VAL A 65  
AA3 2 3 O SER A 62  ? O SER A 62  N ILE A 53  ? N ILE A 53  
AA3 3 4 N ALA A 50  ? N ALA A 50  O PHE A 195 ? O PHE A 195 
AA3 4 5 O GLU A 192 ? O GLU A 192 N THR A 112 ? N THR A 112 
AA3 5 6 N TRP A 109 ? N TRP A 109 O PHE A 130 ? O PHE A 130 
AA4 1 2 O ALA A 73  ? O ALA A 73  N VAL A 65  ? N VAL A 65  
AA4 2 3 O SER A 62  ? O SER A 62  N ILE A 53  ? N ILE A 53  
AA4 3 4 N ALA A 50  ? N ALA A 50  O PHE A 195 ? O PHE A 195 
AA4 4 5 O GLU A 192 ? O GLU A 192 N THR A 112 ? N THR A 112 
AA4 5 6 N ILE A 106 ? N ILE A 106 O LEU A 154 ? O LEU A 154 
AA4 6 7 O GLU A 155 ? O GLU A 155 N THR A 147 ? N THR A 147 
AA5 1 2 O LYS B 35  ? O LYS B 35  N ILE B 27  ? N ILE B 27  
AA5 2 3 O ASP B 28  ? O ASP B 28  N ALA B 6   ? N ALA B 6   
AA5 3 4 N VAL B 5   ? N VAL B 5   O ILE B 214 ? O ILE B 214 
AA5 4 5 O ALA B 211 ? O ALA B 211 N SER B 94  ? N SER B 94  
AA5 5 6 N LEU B 93  ? N LEU B 93  O ALA B 173 ? O ALA B 173 
AA5 6 7 O ARG B 172 ? O ARG B 172 N GLN B 143 ? N GLN B 143 
AA6 1 2 O LYS B 35  ? O LYS B 35  N ILE B 27  ? N ILE B 27  
AA6 2 3 O ASP B 28  ? O ASP B 28  N ALA B 6   ? N ALA B 6   
AA6 3 4 N VAL B 5   ? N VAL B 5   O ILE B 214 ? O ILE B 214 
AA6 4 5 O ALA B 211 ? O ALA B 211 N SER B 94  ? N SER B 94  
AA6 5 6 N VAL B 89  ? N VAL B 89  O VAL B 179 ? O VAL B 179 
AA7 1 2 O ALA B 73  ? O ALA B 73  N VAL B 65  ? N VAL B 65  
AA7 2 3 O SER B 62  ? O SER B 62  N ILE B 53  ? N ILE B 53  
AA7 3 4 N ILE B 52  ? N ILE B 52  O ALA B 193 ? O ALA B 193 
AA7 4 5 O THR B 194 ? O THR B 194 N SER B 110 ? N SER B 110 
AA7 5 6 N PHE B 111 ? N PHE B 111 O PHE B 128 ? O PHE B 128 
AA8 1 2 O ALA B 73  ? O ALA B 73  N VAL B 65  ? N VAL B 65  
AA8 2 3 O SER B 62  ? O SER B 62  N ILE B 53  ? N ILE B 53  
AA8 3 4 N ILE B 52  ? N ILE B 52  O ALA B 193 ? O ALA B 193 
AA8 4 5 O THR B 194 ? O THR B 194 N SER B 110 ? N SER B 110 
AA8 5 6 N ILE B 106 ? N ILE B 106 O LEU B 154 ? O LEU B 154 
AA8 6 7 O GLU B 155 ? O GLU B 155 N THR B 147 ? N THR B 147 
# 
_pdbx_entry_details.entry_id                   9J1D 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              90 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              90 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              90 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                125.08 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            4.78 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN B 14  ? ? -141.64 57.43  
2 1 SER B 108 ? ? -170.37 147.80 
3 1 PHE B 191 ? ? -172.39 132.35 
4 1 ALA B 207 ? ? -171.82 147.81 
# 
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 
A1EAW C1   C  Y N 1   
A1EAW C5   C  Y N 2   
A1EAW C6   C  Y N 3   
A1EAW C3   C  Y N 4   
A1EAW C2   C  Y N 5   
A1EAW N    N  Y N 6   
A1EAW C    C  Y N 7   
A1EAW O    O  N N 8   
A1EAW C10  C  Y N 9   
A1EAW C11  C  Y N 10  
A1EAW C12  C  Y N 11  
A1EAW C13  C  N N 12  
A1EAW C15  C  N N 13  
A1EAW C7   C  Y N 14  
A1EAW C8   C  Y N 15  
A1EAW C9   C  Y N 16  
A1EAW N1   N  Y N 17  
A1EAW O7   O  N N 18  
A1EAW C33  C  N N 19  
A1EAW C20  C  N N 20  
A1EAW C18  C  N N 21  
A1EAW C17  C  N N 22  
A1EAW N2   N  N N 23  
A1EAW O1   O  N N 24  
A1EAW O1M2 O  N N 25  
A1EAW C1M2 C  N S 26  
A1EAW C2M2 C  N S 27  
A1EAW C3M2 C  N S 28  
A1EAW C4M2 C  N S 29  
A1EAW C5M2 C  N R 30  
A1EAW C6M2 C  N N 31  
A1EAW O2M2 O  N N 32  
A1EAW O3M2 O  N N 33  
A1EAW O4M2 O  N N 34  
A1EAW O5M2 O  N N 35  
A1EAW O6M2 O  N N 36  
A1EAW C21  C  N N 37  
A1EAW C22  C  N N 38  
A1EAW C19  C  N N 39  
A1EAW C16  C  N N 40  
A1EAW N3   N  N N 41  
A1EAW O8   O  N N 42  
A1EAW O1M  O  N N 43  
A1EAW C1M  C  N S 44  
A1EAW C2M  C  N S 45  
A1EAW C3M  C  N S 46  
A1EAW C4M  C  N S 47  
A1EAW C5M  C  N R 48  
A1EAW C6M  C  N N 49  
A1EAW O2M  O  N N 50  
A1EAW O3M  O  N N 51  
A1EAW O4M  O  N N 52  
A1EAW O5M  O  N N 53  
A1EAW O6M  O  N N 54  
A1EAW H1   H  N N 55  
A1EAW H2   H  N N 56  
A1EAW H3   H  N N 57  
A1EAW H4   H  N N 58  
A1EAW H5   H  N N 59  
A1EAW H29  H  N N 60  
A1EAW H22  H  N N 61  
A1EAW H23  H  N N 62  
A1EAW H15  H  N N 63  
A1EAW H16  H  N N 64  
A1EAW H10  H  N N 65  
A1EAW H11  H  N N 66  
A1EAW H8   H  N N 67  
A1EAW H9   H  N N 68  
A1EAW H30  H  N N 69  
A1EAW H36  H  N N 70  
A1EAW H37  H  N N 71  
A1EAW H38  H  N N 72  
A1EAW H39  H  N N 73  
A1EAW H40  H  N N 74  
A1EAW H41  H  N N 75  
A1EAW H42  H  N N 76  
A1EAW H43  H  N N 77  
A1EAW H44  H  N N 78  
A1EAW H45  H  N N 79  
A1EAW H46  H  N N 80  
A1EAW H17  H  N N 81  
A1EAW H18  H  N N 82  
A1EAW H19  H  N N 83  
A1EAW H20  H  N N 84  
A1EAW H12  H  N N 85  
A1EAW H13  H  N N 86  
A1EAW H6   H  N N 87  
A1EAW H7   H  N N 88  
A1EAW H31  H  N N 89  
A1EAW H14  H  N N 90  
A1EAW H21  H  N N 91  
A1EAW H24  H  N N 92  
A1EAW H25  H  N N 93  
A1EAW H26  H  N N 94  
A1EAW H27  H  N N 95  
A1EAW H28  H  N N 96  
A1EAW H32  H  N N 97  
A1EAW H33  H  N N 98  
A1EAW H34  H  N N 99  
A1EAW H35  H  N N 100 
ALA   N    N  N N 101 
ALA   CA   C  N S 102 
ALA   C    C  N N 103 
ALA   O    O  N N 104 
ALA   CB   C  N N 105 
ALA   OXT  O  N N 106 
ALA   H    H  N N 107 
ALA   H2   H  N N 108 
ALA   HA   H  N N 109 
ALA   HB1  H  N N 110 
ALA   HB2  H  N N 111 
ALA   HB3  H  N N 112 
ALA   HXT  H  N N 113 
ARG   N    N  N N 114 
ARG   CA   C  N S 115 
ARG   C    C  N N 116 
ARG   O    O  N N 117 
ARG   CB   C  N N 118 
ARG   CG   C  N N 119 
ARG   CD   C  N N 120 
ARG   NE   N  N N 121 
ARG   CZ   C  N N 122 
ARG   NH1  N  N N 123 
ARG   NH2  N  N N 124 
ARG   OXT  O  N N 125 
ARG   H    H  N N 126 
ARG   H2   H  N N 127 
ARG   HA   H  N N 128 
ARG   HB2  H  N N 129 
ARG   HB3  H  N N 130 
ARG   HG2  H  N N 131 
ARG   HG3  H  N N 132 
ARG   HD2  H  N N 133 
ARG   HD3  H  N N 134 
ARG   HE   H  N N 135 
ARG   HH11 H  N N 136 
ARG   HH12 H  N N 137 
ARG   HH21 H  N N 138 
ARG   HH22 H  N N 139 
ARG   HXT  H  N N 140 
ASN   N    N  N N 141 
ASN   CA   C  N S 142 
ASN   C    C  N N 143 
ASN   O    O  N N 144 
ASN   CB   C  N N 145 
ASN   CG   C  N N 146 
ASN   OD1  O  N N 147 
ASN   ND2  N  N N 148 
ASN   OXT  O  N N 149 
ASN   H    H  N N 150 
ASN   H2   H  N N 151 
ASN   HA   H  N N 152 
ASN   HB2  H  N N 153 
ASN   HB3  H  N N 154 
ASN   HD21 H  N N 155 
ASN   HD22 H  N N 156 
ASN   HXT  H  N N 157 
ASP   N    N  N N 158 
ASP   CA   C  N S 159 
ASP   C    C  N N 160 
ASP   O    O  N N 161 
ASP   CB   C  N N 162 
ASP   CG   C  N N 163 
ASP   OD1  O  N N 164 
ASP   OD2  O  N N 165 
ASP   OXT  O  N N 166 
ASP   H    H  N N 167 
ASP   H2   H  N N 168 
ASP   HA   H  N N 169 
ASP   HB2  H  N N 170 
ASP   HB3  H  N N 171 
ASP   HD2  H  N N 172 
ASP   HXT  H  N N 173 
CA    CA   CA N N 174 
GLN   N    N  N N 175 
GLN   CA   C  N S 176 
GLN   C    C  N N 177 
GLN   O    O  N N 178 
GLN   CB   C  N N 179 
GLN   CG   C  N N 180 
GLN   CD   C  N N 181 
GLN   OE1  O  N N 182 
GLN   NE2  N  N N 183 
GLN   OXT  O  N N 184 
GLN   H    H  N N 185 
GLN   H2   H  N N 186 
GLN   HA   H  N N 187 
GLN   HB2  H  N N 188 
GLN   HB3  H  N N 189 
GLN   HG2  H  N N 190 
GLN   HG3  H  N N 191 
GLN   HE21 H  N N 192 
GLN   HE22 H  N N 193 
GLN   HXT  H  N N 194 
GLU   N    N  N N 195 
GLU   CA   C  N S 196 
GLU   C    C  N N 197 
GLU   O    O  N N 198 
GLU   CB   C  N N 199 
GLU   CG   C  N N 200 
GLU   CD   C  N N 201 
GLU   OE1  O  N N 202 
GLU   OE2  O  N N 203 
GLU   OXT  O  N N 204 
GLU   H    H  N N 205 
GLU   H2   H  N N 206 
GLU   HA   H  N N 207 
GLU   HB2  H  N N 208 
GLU   HB3  H  N N 209 
GLU   HG2  H  N N 210 
GLU   HG3  H  N N 211 
GLU   HE2  H  N N 212 
GLU   HXT  H  N N 213 
GLY   N    N  N N 214 
GLY   CA   C  N N 215 
GLY   C    C  N N 216 
GLY   O    O  N N 217 
GLY   OXT  O  N N 218 
GLY   H    H  N N 219 
GLY   H2   H  N N 220 
GLY   HA2  H  N N 221 
GLY   HA3  H  N N 222 
GLY   HXT  H  N N 223 
HIS   N    N  N N 224 
HIS   CA   C  N S 225 
HIS   C    C  N N 226 
HIS   O    O  N N 227 
HIS   CB   C  N N 228 
HIS   CG   C  Y N 229 
HIS   ND1  N  Y N 230 
HIS   CD2  C  Y N 231 
HIS   CE1  C  Y N 232 
HIS   NE2  N  Y N 233 
HIS   OXT  O  N N 234 
HIS   H    H  N N 235 
HIS   H2   H  N N 236 
HIS   HA   H  N N 237 
HIS   HB2  H  N N 238 
HIS   HB3  H  N N 239 
HIS   HD1  H  N N 240 
HIS   HD2  H  N N 241 
HIS   HE1  H  N N 242 
HIS   HE2  H  N N 243 
HIS   HXT  H  N N 244 
ILE   N    N  N N 245 
ILE   CA   C  N S 246 
ILE   C    C  N N 247 
ILE   O    O  N N 248 
ILE   CB   C  N S 249 
ILE   CG1  C  N N 250 
ILE   CG2  C  N N 251 
ILE   CD1  C  N N 252 
ILE   OXT  O  N N 253 
ILE   H    H  N N 254 
ILE   H2   H  N N 255 
ILE   HA   H  N N 256 
ILE   HB   H  N N 257 
ILE   HG12 H  N N 258 
ILE   HG13 H  N N 259 
ILE   HG21 H  N N 260 
ILE   HG22 H  N N 261 
ILE   HG23 H  N N 262 
ILE   HD11 H  N N 263 
ILE   HD12 H  N N 264 
ILE   HD13 H  N N 265 
ILE   HXT  H  N N 266 
LEU   N    N  N N 267 
LEU   CA   C  N S 268 
LEU   C    C  N N 269 
LEU   O    O  N N 270 
LEU   CB   C  N N 271 
LEU   CG   C  N N 272 
LEU   CD1  C  N N 273 
LEU   CD2  C  N N 274 
LEU   OXT  O  N N 275 
LEU   H    H  N N 276 
LEU   H2   H  N N 277 
LEU   HA   H  N N 278 
LEU   HB2  H  N N 279 
LEU   HB3  H  N N 280 
LEU   HG   H  N N 281 
LEU   HD11 H  N N 282 
LEU   HD12 H  N N 283 
LEU   HD13 H  N N 284 
LEU   HD21 H  N N 285 
LEU   HD22 H  N N 286 
LEU   HD23 H  N N 287 
LEU   HXT  H  N N 288 
LYS   N    N  N N 289 
LYS   CA   C  N S 290 
LYS   C    C  N N 291 
LYS   O    O  N N 292 
LYS   CB   C  N N 293 
LYS   CG   C  N N 294 
LYS   CD   C  N N 295 
LYS   CE   C  N N 296 
LYS   NZ   N  N N 297 
LYS   OXT  O  N N 298 
LYS   H    H  N N 299 
LYS   H2   H  N N 300 
LYS   HA   H  N N 301 
LYS   HB2  H  N N 302 
LYS   HB3  H  N N 303 
LYS   HG2  H  N N 304 
LYS   HG3  H  N N 305 
LYS   HD2  H  N N 306 
LYS   HD3  H  N N 307 
LYS   HE2  H  N N 308 
LYS   HE3  H  N N 309 
LYS   HZ1  H  N N 310 
LYS   HZ2  H  N N 311 
LYS   HZ3  H  N N 312 
LYS   HXT  H  N N 313 
MET   N    N  N N 314 
MET   CA   C  N S 315 
MET   C    C  N N 316 
MET   O    O  N N 317 
MET   CB   C  N N 318 
MET   CG   C  N N 319 
MET   SD   S  N N 320 
MET   CE   C  N N 321 
MET   OXT  O  N N 322 
MET   H    H  N N 323 
MET   H2   H  N N 324 
MET   HA   H  N N 325 
MET   HB2  H  N N 326 
MET   HB3  H  N N 327 
MET   HG2  H  N N 328 
MET   HG3  H  N N 329 
MET   HE1  H  N N 330 
MET   HE2  H  N N 331 
MET   HE3  H  N N 332 
MET   HXT  H  N N 333 
MN    MN   MN N N 334 
PHE   N    N  N N 335 
PHE   CA   C  N S 336 
PHE   C    C  N N 337 
PHE   O    O  N N 338 
PHE   CB   C  N N 339 
PHE   CG   C  Y N 340 
PHE   CD1  C  Y N 341 
PHE   CD2  C  Y N 342 
PHE   CE1  C  Y N 343 
PHE   CE2  C  Y N 344 
PHE   CZ   C  Y N 345 
PHE   OXT  O  N N 346 
PHE   H    H  N N 347 
PHE   H2   H  N N 348 
PHE   HA   H  N N 349 
PHE   HB2  H  N N 350 
PHE   HB3  H  N N 351 
PHE   HD1  H  N N 352 
PHE   HD2  H  N N 353 
PHE   HE1  H  N N 354 
PHE   HE2  H  N N 355 
PHE   HZ   H  N N 356 
PHE   HXT  H  N N 357 
PRO   N    N  N N 358 
PRO   CA   C  N S 359 
PRO   C    C  N N 360 
PRO   O    O  N N 361 
PRO   CB   C  N N 362 
PRO   CG   C  N N 363 
PRO   CD   C  N N 364 
PRO   OXT  O  N N 365 
PRO   H    H  N N 366 
PRO   HA   H  N N 367 
PRO   HB2  H  N N 368 
PRO   HB3  H  N N 369 
PRO   HG2  H  N N 370 
PRO   HG3  H  N N 371 
PRO   HD2  H  N N 372 
PRO   HD3  H  N N 373 
PRO   HXT  H  N N 374 
SER   N    N  N N 375 
SER   CA   C  N S 376 
SER   C    C  N N 377 
SER   O    O  N N 378 
SER   CB   C  N N 379 
SER   OG   O  N N 380 
SER   OXT  O  N N 381 
SER   H    H  N N 382 
SER   H2   H  N N 383 
SER   HA   H  N N 384 
SER   HB2  H  N N 385 
SER   HB3  H  N N 386 
SER   HG   H  N N 387 
SER   HXT  H  N N 388 
THR   N    N  N N 389 
THR   CA   C  N S 390 
THR   C    C  N N 391 
THR   O    O  N N 392 
THR   CB   C  N R 393 
THR   OG1  O  N N 394 
THR   CG2  C  N N 395 
THR   OXT  O  N N 396 
THR   H    H  N N 397 
THR   H2   H  N N 398 
THR   HA   H  N N 399 
THR   HB   H  N N 400 
THR   HG1  H  N N 401 
THR   HG21 H  N N 402 
THR   HG22 H  N N 403 
THR   HG23 H  N N 404 
THR   HXT  H  N N 405 
TRP   N    N  N N 406 
TRP   CA   C  N S 407 
TRP   C    C  N N 408 
TRP   O    O  N N 409 
TRP   CB   C  N N 410 
TRP   CG   C  Y N 411 
TRP   CD1  C  Y N 412 
TRP   CD2  C  Y N 413 
TRP   NE1  N  Y N 414 
TRP   CE2  C  Y N 415 
TRP   CE3  C  Y N 416 
TRP   CZ2  C  Y N 417 
TRP   CZ3  C  Y N 418 
TRP   CH2  C  Y N 419 
TRP   OXT  O  N N 420 
TRP   H    H  N N 421 
TRP   H2   H  N N 422 
TRP   HA   H  N N 423 
TRP   HB2  H  N N 424 
TRP   HB3  H  N N 425 
TRP   HD1  H  N N 426 
TRP   HE1  H  N N 427 
TRP   HE3  H  N N 428 
TRP   HZ2  H  N N 429 
TRP   HZ3  H  N N 430 
TRP   HH2  H  N N 431 
TRP   HXT  H  N N 432 
TYR   N    N  N N 433 
TYR   CA   C  N S 434 
TYR   C    C  N N 435 
TYR   O    O  N N 436 
TYR   CB   C  N N 437 
TYR   CG   C  Y N 438 
TYR   CD1  C  Y N 439 
TYR   CD2  C  Y N 440 
TYR   CE1  C  Y N 441 
TYR   CE2  C  Y N 442 
TYR   CZ   C  Y N 443 
TYR   OH   O  N N 444 
TYR   OXT  O  N N 445 
TYR   H    H  N N 446 
TYR   H2   H  N N 447 
TYR   HA   H  N N 448 
TYR   HB2  H  N N 449 
TYR   HB3  H  N N 450 
TYR   HD1  H  N N 451 
TYR   HD2  H  N N 452 
TYR   HE1  H  N N 453 
TYR   HE2  H  N N 454 
TYR   HH   H  N N 455 
TYR   HXT  H  N N 456 
VAL   N    N  N N 457 
VAL   CA   C  N S 458 
VAL   C    C  N N 459 
VAL   O    O  N N 460 
VAL   CB   C  N N 461 
VAL   CG1  C  N N 462 
VAL   CG2  C  N N 463 
VAL   OXT  O  N N 464 
VAL   H    H  N N 465 
VAL   H2   H  N N 466 
VAL   HA   H  N N 467 
VAL   HB   H  N N 468 
VAL   HG11 H  N N 469 
VAL   HG12 H  N N 470 
VAL   HG13 H  N N 471 
VAL   HG21 H  N N 472 
VAL   HG22 H  N N 473 
VAL   HG23 H  N N 474 
VAL   HXT  H  N N 475 
# 
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 
A1EAW O3M  C3M  sing N N 1   
A1EAW O2M  C2M  sing N N 2   
A1EAW O6M  C6M  sing N N 3   
A1EAW C4M  O4M  sing N N 4   
A1EAW C4M  C3M  sing N N 5   
A1EAW C4M  C5M  sing N N 6   
A1EAW C3M  C2M  sing N N 7   
A1EAW C2M  C1M  sing N N 8   
A1EAW C6M  C5M  sing N N 9   
A1EAW O5M  C5M  sing N N 10  
A1EAW O5M  C1M  sing N N 11  
A1EAW O3M2 C3M2 sing N N 12  
A1EAW C1M  O1M  sing N N 13  
A1EAW C33  C20  sing N N 14  
A1EAW C33  O1M2 sing N N 15  
A1EAW C3M2 C2M2 sing N N 16  
A1EAW C3M2 C4M2 sing N N 17  
A1EAW C18  C17  sing N N 18  
A1EAW C18  O1   sing N N 19  
A1EAW C2M2 O2M2 sing N N 20  
A1EAW C2M2 C1M2 sing N N 21  
A1EAW C20  O1   sing N N 22  
A1EAW O1M2 C1M2 sing N N 23  
A1EAW C17  N2   sing N N 24  
A1EAW O1M  C21  sing N N 25  
A1EAW O4M2 C4M2 sing N N 26  
A1EAW C1M2 O5M2 sing N N 27  
A1EAW C22  C21  sing N N 28  
A1EAW C22  O8   sing N N 29  
A1EAW C4M2 C5M2 sing N N 30  
A1EAW C19  O8   sing N N 31  
A1EAW C19  C16  sing N N 32  
A1EAW N2   C15  sing N N 33  
A1EAW C5M2 O5M2 sing N N 34  
A1EAW C5M2 C6M2 sing N N 35  
A1EAW O    C15  doub N N 36  
A1EAW C16  N3   sing N N 37  
A1EAW C15  C5   sing N N 38  
A1EAW O6M2 C6M2 sing N N 39  
A1EAW O7   C13  doub N N 40  
A1EAW N3   C13  sing N N 41  
A1EAW C5   N    doub Y N 42  
A1EAW C5   C    sing Y N 43  
A1EAW C13  C12  sing N N 44  
A1EAW N    C3   sing Y N 45  
A1EAW C    C1   doub Y N 46  
A1EAW N1   C12  doub Y N 47  
A1EAW N1   C9   sing Y N 48  
A1EAW C12  C11  sing Y N 49  
A1EAW C3   C9   doub Y N 50  
A1EAW C3   C2   sing Y N 51  
A1EAW C9   C8   sing Y N 52  
A1EAW C1   C2   sing Y N 53  
A1EAW C2   C6   doub Y N 54  
A1EAW C11  C10  doub Y N 55  
A1EAW C8   C10  sing Y N 56  
A1EAW C8   C7   doub Y N 57  
A1EAW C6   C7   sing Y N 58  
A1EAW C1   H1   sing N N 59  
A1EAW C6   H2   sing N N 60  
A1EAW C    H3   sing N N 61  
A1EAW C10  H4   sing N N 62  
A1EAW C11  H5   sing N N 63  
A1EAW C16  H6   sing N N 64  
A1EAW C16  H7   sing N N 65  
A1EAW C17  H8   sing N N 66  
A1EAW C17  H9   sing N N 67  
A1EAW C18  H10  sing N N 68  
A1EAW C18  H11  sing N N 69  
A1EAW C19  H12  sing N N 70  
A1EAW C19  H13  sing N N 71  
A1EAW C1M  H14  sing N N 72  
A1EAW C20  H15  sing N N 73  
A1EAW C20  H16  sing N N 74  
A1EAW C21  H17  sing N N 75  
A1EAW C21  H18  sing N N 76  
A1EAW C22  H19  sing N N 77  
A1EAW C22  H20  sing N N 78  
A1EAW C2M  H21  sing N N 79  
A1EAW C33  H22  sing N N 80  
A1EAW C33  H23  sing N N 81  
A1EAW C3M  H24  sing N N 82  
A1EAW C4M  H25  sing N N 83  
A1EAW C5M  H26  sing N N 84  
A1EAW C6M  H27  sing N N 85  
A1EAW C6M  H28  sing N N 86  
A1EAW C7   H29  sing N N 87  
A1EAW N2   H30  sing N N 88  
A1EAW N3   H31  sing N N 89  
A1EAW O2M  H32  sing N N 90  
A1EAW O3M  H33  sing N N 91  
A1EAW O4M  H34  sing N N 92  
A1EAW O6M  H35  sing N N 93  
A1EAW C1M2 H36  sing N N 94  
A1EAW C2M2 H37  sing N N 95  
A1EAW C3M2 H38  sing N N 96  
A1EAW C4M2 H39  sing N N 97  
A1EAW C5M2 H40  sing N N 98  
A1EAW C6M2 H41  sing N N 99  
A1EAW C6M2 H42  sing N N 100 
A1EAW O2M2 H43  sing N N 101 
A1EAW O3M2 H44  sing N N 102 
A1EAW O4M2 H45  sing N N 103 
A1EAW O6M2 H46  sing N N 104 
ALA   N    CA   sing N N 105 
ALA   N    H    sing N N 106 
ALA   N    H2   sing N N 107 
ALA   CA   C    sing N N 108 
ALA   CA   CB   sing N N 109 
ALA   CA   HA   sing N N 110 
ALA   C    O    doub N N 111 
ALA   C    OXT  sing N N 112 
ALA   CB   HB1  sing N N 113 
ALA   CB   HB2  sing N N 114 
ALA   CB   HB3  sing N N 115 
ALA   OXT  HXT  sing N N 116 
ARG   N    CA   sing N N 117 
ARG   N    H    sing N N 118 
ARG   N    H2   sing N N 119 
ARG   CA   C    sing N N 120 
ARG   CA   CB   sing N N 121 
ARG   CA   HA   sing N N 122 
ARG   C    O    doub N N 123 
ARG   C    OXT  sing N N 124 
ARG   CB   CG   sing N N 125 
ARG   CB   HB2  sing N N 126 
ARG   CB   HB3  sing N N 127 
ARG   CG   CD   sing N N 128 
ARG   CG   HG2  sing N N 129 
ARG   CG   HG3  sing N N 130 
ARG   CD   NE   sing N N 131 
ARG   CD   HD2  sing N N 132 
ARG   CD   HD3  sing N N 133 
ARG   NE   CZ   sing N N 134 
ARG   NE   HE   sing N N 135 
ARG   CZ   NH1  sing N N 136 
ARG   CZ   NH2  doub N N 137 
ARG   NH1  HH11 sing N N 138 
ARG   NH1  HH12 sing N N 139 
ARG   NH2  HH21 sing N N 140 
ARG   NH2  HH22 sing N N 141 
ARG   OXT  HXT  sing N N 142 
ASN   N    CA   sing N N 143 
ASN   N    H    sing N N 144 
ASN   N    H2   sing N N 145 
ASN   CA   C    sing N N 146 
ASN   CA   CB   sing N N 147 
ASN   CA   HA   sing N N 148 
ASN   C    O    doub N N 149 
ASN   C    OXT  sing N N 150 
ASN   CB   CG   sing N N 151 
ASN   CB   HB2  sing N N 152 
ASN   CB   HB3  sing N N 153 
ASN   CG   OD1  doub N N 154 
ASN   CG   ND2  sing N N 155 
ASN   ND2  HD21 sing N N 156 
ASN   ND2  HD22 sing N N 157 
ASN   OXT  HXT  sing N N 158 
ASP   N    CA   sing N N 159 
ASP   N    H    sing N N 160 
ASP   N    H2   sing N N 161 
ASP   CA   C    sing N N 162 
ASP   CA   CB   sing N N 163 
ASP   CA   HA   sing N N 164 
ASP   C    O    doub N N 165 
ASP   C    OXT  sing N N 166 
ASP   CB   CG   sing N N 167 
ASP   CB   HB2  sing N N 168 
ASP   CB   HB3  sing N N 169 
ASP   CG   OD1  doub N N 170 
ASP   CG   OD2  sing N N 171 
ASP   OD2  HD2  sing N N 172 
ASP   OXT  HXT  sing N N 173 
GLN   N    CA   sing N N 174 
GLN   N    H    sing N N 175 
GLN   N    H2   sing N N 176 
GLN   CA   C    sing N N 177 
GLN   CA   CB   sing N N 178 
GLN   CA   HA   sing N N 179 
GLN   C    O    doub N N 180 
GLN   C    OXT  sing N N 181 
GLN   CB   CG   sing N N 182 
GLN   CB   HB2  sing N N 183 
GLN   CB   HB3  sing N N 184 
GLN   CG   CD   sing N N 185 
GLN   CG   HG2  sing N N 186 
GLN   CG   HG3  sing N N 187 
GLN   CD   OE1  doub N N 188 
GLN   CD   NE2  sing N N 189 
GLN   NE2  HE21 sing N N 190 
GLN   NE2  HE22 sing N N 191 
GLN   OXT  HXT  sing N N 192 
GLU   N    CA   sing N N 193 
GLU   N    H    sing N N 194 
GLU   N    H2   sing N N 195 
GLU   CA   C    sing N N 196 
GLU   CA   CB   sing N N 197 
GLU   CA   HA   sing N N 198 
GLU   C    O    doub N N 199 
GLU   C    OXT  sing N N 200 
GLU   CB   CG   sing N N 201 
GLU   CB   HB2  sing N N 202 
GLU   CB   HB3  sing N N 203 
GLU   CG   CD   sing N N 204 
GLU   CG   HG2  sing N N 205 
GLU   CG   HG3  sing N N 206 
GLU   CD   OE1  doub N N 207 
GLU   CD   OE2  sing N N 208 
GLU   OE2  HE2  sing N N 209 
GLU   OXT  HXT  sing N N 210 
GLY   N    CA   sing N N 211 
GLY   N    H    sing N N 212 
GLY   N    H2   sing N N 213 
GLY   CA   C    sing N N 214 
GLY   CA   HA2  sing N N 215 
GLY   CA   HA3  sing N N 216 
GLY   C    O    doub N N 217 
GLY   C    OXT  sing N N 218 
GLY   OXT  HXT  sing N N 219 
HIS   N    CA   sing N N 220 
HIS   N    H    sing N N 221 
HIS   N    H2   sing N N 222 
HIS   CA   C    sing N N 223 
HIS   CA   CB   sing N N 224 
HIS   CA   HA   sing N N 225 
HIS   C    O    doub N N 226 
HIS   C    OXT  sing N N 227 
HIS   CB   CG   sing N N 228 
HIS   CB   HB2  sing N N 229 
HIS   CB   HB3  sing N N 230 
HIS   CG   ND1  sing Y N 231 
HIS   CG   CD2  doub Y N 232 
HIS   ND1  CE1  doub Y N 233 
HIS   ND1  HD1  sing N N 234 
HIS   CD2  NE2  sing Y N 235 
HIS   CD2  HD2  sing N N 236 
HIS   CE1  NE2  sing Y N 237 
HIS   CE1  HE1  sing N N 238 
HIS   NE2  HE2  sing N N 239 
HIS   OXT  HXT  sing N N 240 
ILE   N    CA   sing N N 241 
ILE   N    H    sing N N 242 
ILE   N    H2   sing N N 243 
ILE   CA   C    sing N N 244 
ILE   CA   CB   sing N N 245 
ILE   CA   HA   sing N N 246 
ILE   C    O    doub N N 247 
ILE   C    OXT  sing N N 248 
ILE   CB   CG1  sing N N 249 
ILE   CB   CG2  sing N N 250 
ILE   CB   HB   sing N N 251 
ILE   CG1  CD1  sing N N 252 
ILE   CG1  HG12 sing N N 253 
ILE   CG1  HG13 sing N N 254 
ILE   CG2  HG21 sing N N 255 
ILE   CG2  HG22 sing N N 256 
ILE   CG2  HG23 sing N N 257 
ILE   CD1  HD11 sing N N 258 
ILE   CD1  HD12 sing N N 259 
ILE   CD1  HD13 sing N N 260 
ILE   OXT  HXT  sing N N 261 
LEU   N    CA   sing N N 262 
LEU   N    H    sing N N 263 
LEU   N    H2   sing N N 264 
LEU   CA   C    sing N N 265 
LEU   CA   CB   sing N N 266 
LEU   CA   HA   sing N N 267 
LEU   C    O    doub N N 268 
LEU   C    OXT  sing N N 269 
LEU   CB   CG   sing N N 270 
LEU   CB   HB2  sing N N 271 
LEU   CB   HB3  sing N N 272 
LEU   CG   CD1  sing N N 273 
LEU   CG   CD2  sing N N 274 
LEU   CG   HG   sing N N 275 
LEU   CD1  HD11 sing N N 276 
LEU   CD1  HD12 sing N N 277 
LEU   CD1  HD13 sing N N 278 
LEU   CD2  HD21 sing N N 279 
LEU   CD2  HD22 sing N N 280 
LEU   CD2  HD23 sing N N 281 
LEU   OXT  HXT  sing N N 282 
LYS   N    CA   sing N N 283 
LYS   N    H    sing N N 284 
LYS   N    H2   sing N N 285 
LYS   CA   C    sing N N 286 
LYS   CA   CB   sing N N 287 
LYS   CA   HA   sing N N 288 
LYS   C    O    doub N N 289 
LYS   C    OXT  sing N N 290 
LYS   CB   CG   sing N N 291 
LYS   CB   HB2  sing N N 292 
LYS   CB   HB3  sing N N 293 
LYS   CG   CD   sing N N 294 
LYS   CG   HG2  sing N N 295 
LYS   CG   HG3  sing N N 296 
LYS   CD   CE   sing N N 297 
LYS   CD   HD2  sing N N 298 
LYS   CD   HD3  sing N N 299 
LYS   CE   NZ   sing N N 300 
LYS   CE   HE2  sing N N 301 
LYS   CE   HE3  sing N N 302 
LYS   NZ   HZ1  sing N N 303 
LYS   NZ   HZ2  sing N N 304 
LYS   NZ   HZ3  sing N N 305 
LYS   OXT  HXT  sing N N 306 
MET   N    CA   sing N N 307 
MET   N    H    sing N N 308 
MET   N    H2   sing N N 309 
MET   CA   C    sing N N 310 
MET   CA   CB   sing N N 311 
MET   CA   HA   sing N N 312 
MET   C    O    doub N N 313 
MET   C    OXT  sing N N 314 
MET   CB   CG   sing N N 315 
MET   CB   HB2  sing N N 316 
MET   CB   HB3  sing N N 317 
MET   CG   SD   sing N N 318 
MET   CG   HG2  sing N N 319 
MET   CG   HG3  sing N N 320 
MET   SD   CE   sing N N 321 
MET   CE   HE1  sing N N 322 
MET   CE   HE2  sing N N 323 
MET   CE   HE3  sing N N 324 
MET   OXT  HXT  sing N N 325 
PHE   N    CA   sing N N 326 
PHE   N    H    sing N N 327 
PHE   N    H2   sing N N 328 
PHE   CA   C    sing N N 329 
PHE   CA   CB   sing N N 330 
PHE   CA   HA   sing N N 331 
PHE   C    O    doub N N 332 
PHE   C    OXT  sing N N 333 
PHE   CB   CG   sing N N 334 
PHE   CB   HB2  sing N N 335 
PHE   CB   HB3  sing N N 336 
PHE   CG   CD1  doub Y N 337 
PHE   CG   CD2  sing Y N 338 
PHE   CD1  CE1  sing Y N 339 
PHE   CD1  HD1  sing N N 340 
PHE   CD2  CE2  doub Y N 341 
PHE   CD2  HD2  sing N N 342 
PHE   CE1  CZ   doub Y N 343 
PHE   CE1  HE1  sing N N 344 
PHE   CE2  CZ   sing Y N 345 
PHE   CE2  HE2  sing N N 346 
PHE   CZ   HZ   sing N N 347 
PHE   OXT  HXT  sing N N 348 
PRO   N    CA   sing N N 349 
PRO   N    CD   sing N N 350 
PRO   N    H    sing N N 351 
PRO   CA   C    sing N N 352 
PRO   CA   CB   sing N N 353 
PRO   CA   HA   sing N N 354 
PRO   C    O    doub N N 355 
PRO   C    OXT  sing N N 356 
PRO   CB   CG   sing N N 357 
PRO   CB   HB2  sing N N 358 
PRO   CB   HB3  sing N N 359 
PRO   CG   CD   sing N N 360 
PRO   CG   HG2  sing N N 361 
PRO   CG   HG3  sing N N 362 
PRO   CD   HD2  sing N N 363 
PRO   CD   HD3  sing N N 364 
PRO   OXT  HXT  sing N N 365 
SER   N    CA   sing N N 366 
SER   N    H    sing N N 367 
SER   N    H2   sing N N 368 
SER   CA   C    sing N N 369 
SER   CA   CB   sing N N 370 
SER   CA   HA   sing N N 371 
SER   C    O    doub N N 372 
SER   C    OXT  sing N N 373 
SER   CB   OG   sing N N 374 
SER   CB   HB2  sing N N 375 
SER   CB   HB3  sing N N 376 
SER   OG   HG   sing N N 377 
SER   OXT  HXT  sing N N 378 
THR   N    CA   sing N N 379 
THR   N    H    sing N N 380 
THR   N    H2   sing N N 381 
THR   CA   C    sing N N 382 
THR   CA   CB   sing N N 383 
THR   CA   HA   sing N N 384 
THR   C    O    doub N N 385 
THR   C    OXT  sing N N 386 
THR   CB   OG1  sing N N 387 
THR   CB   CG2  sing N N 388 
THR   CB   HB   sing N N 389 
THR   OG1  HG1  sing N N 390 
THR   CG2  HG21 sing N N 391 
THR   CG2  HG22 sing N N 392 
THR   CG2  HG23 sing N N 393 
THR   OXT  HXT  sing N N 394 
TRP   N    CA   sing N N 395 
TRP   N    H    sing N N 396 
TRP   N    H2   sing N N 397 
TRP   CA   C    sing N N 398 
TRP   CA   CB   sing N N 399 
TRP   CA   HA   sing N N 400 
TRP   C    O    doub N N 401 
TRP   C    OXT  sing N N 402 
TRP   CB   CG   sing N N 403 
TRP   CB   HB2  sing N N 404 
TRP   CB   HB3  sing N N 405 
TRP   CG   CD1  doub Y N 406 
TRP   CG   CD2  sing Y N 407 
TRP   CD1  NE1  sing Y N 408 
TRP   CD1  HD1  sing N N 409 
TRP   CD2  CE2  doub Y N 410 
TRP   CD2  CE3  sing Y N 411 
TRP   NE1  CE2  sing Y N 412 
TRP   NE1  HE1  sing N N 413 
TRP   CE2  CZ2  sing Y N 414 
TRP   CE3  CZ3  doub Y N 415 
TRP   CE3  HE3  sing N N 416 
TRP   CZ2  CH2  doub Y N 417 
TRP   CZ2  HZ2  sing N N 418 
TRP   CZ3  CH2  sing Y N 419 
TRP   CZ3  HZ3  sing N N 420 
TRP   CH2  HH2  sing N N 421 
TRP   OXT  HXT  sing N N 422 
TYR   N    CA   sing N N 423 
TYR   N    H    sing N N 424 
TYR   N    H2   sing N N 425 
TYR   CA   C    sing N N 426 
TYR   CA   CB   sing N N 427 
TYR   CA   HA   sing N N 428 
TYR   C    O    doub N N 429 
TYR   C    OXT  sing N N 430 
TYR   CB   CG   sing N N 431 
TYR   CB   HB2  sing N N 432 
TYR   CB   HB3  sing N N 433 
TYR   CG   CD1  doub Y N 434 
TYR   CG   CD2  sing Y N 435 
TYR   CD1  CE1  sing Y N 436 
TYR   CD1  HD1  sing N N 437 
TYR   CD2  CE2  doub Y N 438 
TYR   CD2  HD2  sing N N 439 
TYR   CE1  CZ   doub Y N 440 
TYR   CE1  HE1  sing N N 441 
TYR   CE2  CZ   sing Y N 442 
TYR   CE2  HE2  sing N N 443 
TYR   CZ   OH   sing N N 444 
TYR   OH   HH   sing N N 445 
TYR   OXT  HXT  sing N N 446 
VAL   N    CA   sing N N 447 
VAL   N    H    sing N N 448 
VAL   N    H2   sing N N 449 
VAL   CA   C    sing N N 450 
VAL   CA   CB   sing N N 451 
VAL   CA   HA   sing N N 452 
VAL   C    O    doub N N 453 
VAL   C    OXT  sing N N 454 
VAL   CB   CG1  sing N N 455 
VAL   CB   CG2  sing N N 456 
VAL   CB   HB   sing N N 457 
VAL   CG1  HG11 sing N N 458 
VAL   CG1  HG12 sing N N 459 
VAL   CG1  HG13 sing N N 460 
VAL   CG2  HG21 sing N N 461 
VAL   CG2  HG22 sing N N 462 
VAL   CG2  HG23 sing N N 463 
VAL   OXT  HXT  sing N N 464 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4P9W 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9J1D 
_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]   0.007071 
_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]   0.007071 
_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]   0.012436 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
MN 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ALA   A 1 1   ? -11.324 8.727   -14.839 1.00 144.73 ? 1   ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 1   ? -12.480 8.043   -15.390 1.00 138.14 ? 1   ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 1   ? -12.387 6.529   -15.136 1.00 137.01 ? 1   ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 1   ? -12.352 5.756   -16.095 1.00 137.14 ? 1   ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 1   ? -12.648 8.355   -16.894 1.00 132.06 ? 1   ALA   A CB   1 
ATOM   6    N  N    . ASP   A 1 2   ? -12.416 6.108   -13.875 1.00 133.84 ? 2   ASP   A N    1 
ATOM   7    C  CA   . ASP   A 1 2   ? -12.588 4.697   -13.615 1.00 127.40 ? 2   ASP   A CA   1 
ATOM   8    C  C    . ASP   A 1 2   ? -13.952 4.201   -14.126 1.00 127.77 ? 2   ASP   A C    1 
ATOM   9    O  O    . ASP   A 1 2   ? -14.989 4.866   -13.977 1.00 128.94 ? 2   ASP   A O    1 
ATOM   10   C  CB   . ASP   A 1 2   ? -12.543 4.294   -12.106 1.00 124.48 ? 2   ASP   A CB   1 
ATOM   11   C  CG   . ASP   A 1 2   ? -13.549 5.069   -11.203 1.00 128.04 ? 2   ASP   A CG   1 
ATOM   12   O  OD1  . ASP   A 1 2   ? -14.081 6.174   -11.660 1.00 124.31 ? 2   ASP   A OD1  1 
ATOM   13   O  OD2  . ASP   A 1 2   ? -13.849 4.478   -10.128 1.00 128.51 ? 2   ASP   A OD2  1 
ATOM   14   N  N    . THR   A 1 3   ? -13.945 2.955   -14.606 1.00 122.59 ? 3   THR   A N    1 
ATOM   15   C  CA   . THR   A 1 3   ? -15.142 2.293   -15.109 1.00 116.22 ? 3   THR   A CA   1 
ATOM   16   C  C    . THR   A 1 3   ? -15.999 1.802   -13.950 1.00 109.03 ? 3   THR   A C    1 
ATOM   17   O  O    . THR   A 1 3   ? -15.479 1.289   -12.950 1.00 107.97 ? 3   THR   A O    1 
ATOM   18   C  CB   . THR   A 1 3   ? -14.745 1.114   -15.975 1.00 110.50 ? 3   THR   A CB   1 
ATOM   19   O  OG1  . THR   A 1 3   ? -13.915 1.557   -17.054 1.00 117.01 ? 3   THR   A OG1  1 
ATOM   20   C  CG2  . THR   A 1 3   ? -16.006 0.485   -16.535 1.00 102.10 ? 3   THR   A CG2  1 
ATOM   21   N  N    . ILE   A 1 4   ? -17.326 1.922   -14.097 1.00 102.56 ? 4   ILE   A N    1 
ATOM   22   C  CA   . ILE   A 1 4   ? -18.195 1.680   -12.944 1.00 97.91  ? 4   ILE   A CA   1 
ATOM   23   C  C    . ILE   A 1 4   ? -19.618 1.241   -13.340 1.00 93.76  ? 4   ILE   A C    1 
ATOM   24   O  O    . ILE   A 1 4   ? -20.269 1.850   -14.191 1.00 92.32  ? 4   ILE   A O    1 
ATOM   25   C  CB   . ILE   A 1 4   ? -18.173 2.961   -12.079 1.00 91.60  ? 4   ILE   A CB   1 
ATOM   26   C  CG1  . ILE   A 1 4   ? -18.657 2.738   -10.666 1.00 89.44  ? 4   ILE   A CG1  1 
ATOM   27   C  CG2  . ILE   A 1 4   ? -19.122 3.970   -12.601 1.00 93.98  ? 4   ILE   A CG2  1 
ATOM   28   C  CD1  . ILE   A 1 4   ? -18.297 3.916   -9.776  1.00 91.11  ? 4   ILE   A CD1  1 
ATOM   29   N  N    . VAL   A 1 5   ? -20.121 0.165   -12.739 1.00 94.34  ? 5   VAL   A N    1 
ATOM   30   C  CA   . VAL   A 1 5   ? -21.480 -0.302  -13.009 1.00 88.18  ? 5   VAL   A CA   1 
ATOM   31   C  C    . VAL   A 1 5   ? -22.233 -0.385  -11.684 1.00 81.78  ? 5   VAL   A C    1 
ATOM   32   O  O    . VAL   A 1 5   ? -21.643 -0.722  -10.647 1.00 76.51  ? 5   VAL   A O    1 
ATOM   33   C  CB   . VAL   A 1 5   ? -21.481 -1.677  -13.701 1.00 84.49  ? 5   VAL   A CB   1 
ATOM   34   C  CG1  . VAL   A 1 5   ? -22.898 -2.034  -14.109 1.00 81.87  ? 5   VAL   A CG1  1 
ATOM   35   C  CG2  . VAL   A 1 5   ? -20.486 -1.715  -14.837 1.00 79.64  ? 5   VAL   A CG2  1 
ATOM   36   N  N    . ALA   A 1 6   ? -23.534 -0.085  -11.705 1.00 74.56  ? 6   ALA   A N    1 
ATOM   37   C  CA   . ALA   A 1 6   ? -24.176 0.086   -10.407 1.00 75.91  ? 6   ALA   A CA   1 
ATOM   38   C  C    . ALA   A 1 6   ? -25.676 -0.091  -10.483 1.00 76.24  ? 6   ALA   A C    1 
ATOM   39   O  O    . ALA   A 1 6   ? -26.295 0.140   -11.520 1.00 82.09  ? 6   ALA   A O    1 
ATOM   40   C  CB   . ALA   A 1 6   ? -23.893 1.463   -9.793  1.00 75.55  ? 6   ALA   A CB   1 
ATOM   41   N  N    . VAL   A 1 7   ? -26.248 -0.468  -9.347  1.00 74.35  ? 7   VAL   A N    1 
ATOM   42   C  CA   . VAL   A 1 7   ? -27.688 -0.489  -9.135  1.00 77.20  ? 7   VAL   A CA   1 
ATOM   43   C  C    . VAL   A 1 7   ? -28.009 0.607   -8.139  1.00 79.08  ? 7   VAL   A C    1 
ATOM   44   O  O    . VAL   A 1 7   ? -27.606 0.532   -6.973  1.00 78.22  ? 7   VAL   A O    1 
ATOM   45   C  CB   . VAL   A 1 7   ? -28.172 -1.853  -8.623  1.00 78.93  ? 7   VAL   A CB   1 
ATOM   46   C  CG1  . VAL   A 1 7   ? -29.647 -1.799  -8.270  1.00 71.67  ? 7   VAL   A CG1  1 
ATOM   47   C  CG2  . VAL   A 1 7   ? -27.914 -2.937  -9.669  1.00 72.65  ? 7   VAL   A CG2  1 
ATOM   48   N  N    . GLU   A 1 8   ? -28.743 1.610   -8.590  1.00 80.02  ? 8   GLU   A N    1 
ATOM   49   C  CA   . GLU   A 1 8   ? -28.977 2.800   -7.799  1.00 78.75  ? 8   GLU   A CA   1 
ATOM   50   C  C    . GLU   A 1 8   ? -30.385 2.768   -7.227  1.00 80.49  ? 8   GLU   A C    1 
ATOM   51   O  O    . GLU   A 1 8   ? -31.291 2.131   -7.775  1.00 78.20  ? 8   GLU   A O    1 
ATOM   52   C  CB   . GLU   A 1 8   ? -28.782 4.061   -8.643  1.00 83.59  ? 8   GLU   A CB   1 
ATOM   53   C  CG   . GLU   A 1 8   ? -29.853 4.281   -9.711  1.00 89.86  ? 8   GLU   A CG   1 
ATOM   54   C  CD   . GLU   A 1 8   ? -29.925 5.729   -10.183 1.00 95.01  ? 8   GLU   A CD   1 
ATOM   55   O  OE1  . GLU   A 1 8   ? -29.046 6.515   -9.805  1.00 98.50  ? 8   GLU   A OE1  1 
ATOM   56   O  OE2  . GLU   A 1 8   ? -30.877 6.107   -10.898 1.00 101.22 ? 8   GLU   A OE2  1 
ATOM   57   N  N    . LEU   A 1 9   ? -30.547 3.457   -6.098  1.00 84.03  ? 9   LEU   A N    1 
ATOM   58   C  CA   . LEU   A 1 9   ? -31.826 3.628   -5.408  1.00 87.61  ? 9   LEU   A CA   1 
ATOM   59   C  C    . LEU   A 1 9   ? -32.040 5.113   -5.083  1.00 96.44  ? 9   LEU   A C    1 
ATOM   60   O  O    . LEU   A 1 9   ? -31.647 5.538   -3.993  1.00 96.01  ? 9   LEU   A O    1 
ATOM   61   C  CB   . LEU   A 1 9   ? -31.857 2.790   -4.130  1.00 85.13  ? 9   LEU   A CB   1 
ATOM   62   C  CG   . LEU   A 1 9   ? -32.046 1.274   -4.080  1.00 81.09  ? 9   LEU   A CG   1 
ATOM   63   C  CD1  . LEU   A 1 9   ? -30.974 0.530   -4.861  1.00 80.76  ? 9   LEU   A CD1  1 
ATOM   64   C  CD2  . LEU   A 1 9   ? -32.089 0.840   -2.632  1.00 75.74  ? 9   LEU   A CD2  1 
ATOM   65   N  N    . ASP   A 1 10  ? -32.683 5.878   -5.989  1.00 101.64 ? 10  ASP   A N    1 
ATOM   66   C  CA   . ASP   A 1 10  ? -32.914 7.320   -5.809  1.00 103.43 ? 10  ASP   A CA   1 
ATOM   67   C  C    . ASP   A 1 10  ? -34.138 7.626   -4.965  1.00 105.92 ? 10  ASP   A C    1 
ATOM   68   O  O    . ASP   A 1 10  ? -35.275 7.373   -5.384  1.00 108.19 ? 10  ASP   A O    1 
ATOM   69   C  CB   . ASP   A 1 10  ? -33.087 8.048   -7.134  1.00 102.91 ? 10  ASP   A CB   1 
ATOM   70   C  CG   . ASP   A 1 10  ? -31.812 8.211   -7.856  1.00 108.44 ? 10  ASP   A CG   1 
ATOM   71   O  OD1  . ASP   A 1 10  ? -30.789 8.322   -7.144  1.00 113.31 ? 10  ASP   A OD1  1 
ATOM   72   O  OD2  . ASP   A 1 10  ? -31.823 8.210   -9.107  1.00 108.06 ? 10  ASP   A OD2  1 
ATOM   73   N  N    . THR   A 1 11  ? -33.901 8.241   -3.811  1.00 108.39 ? 11  THR   A N    1 
ATOM   74   C  CA   . THR   A 1 11  ? -34.950 8.927   -3.076  1.00 111.52 ? 11  THR   A CA   1 
ATOM   75   C  C    . THR   A 1 11  ? -35.165 10.350  -3.555  1.00 114.11 ? 11  THR   A C    1 
ATOM   76   O  O    . THR   A 1 11  ? -36.212 10.944  -3.241  1.00 107.68 ? 11  THR   A O    1 
ATOM   77   C  CB   . THR   A 1 11  ? -34.639 8.905   -1.574  1.00 110.90 ? 11  THR   A CB   1 
ATOM   78   O  OG1  . THR   A 1 11  ? -33.363 9.519   -1.322  1.00 104.72 ? 11  THR   A OG1  1 
ATOM   79   C  CG2  . THR   A 1 11  ? -34.712 7.485   -1.012  1.00 108.66 ? 11  THR   A CG2  1 
ATOM   80   N  N    . TYR   A 1 12  ? -34.217 10.898  -4.323  1.00 116.56 ? 12  TYR   A N    1 
ATOM   81   C  CA   . TYR   A 1 12  ? -34.350 12.262  -4.798  1.00 112.69 ? 12  TYR   A CA   1 
ATOM   82   C  C    . TYR   A 1 12  ? -34.271 12.281  -6.313  1.00 107.46 ? 12  TYR   A C    1 
ATOM   83   O  O    . TYR   A 1 12  ? -33.214 11.961  -6.888  1.00 100.91 ? 12  TYR   A O    1 
ATOM   84   C  CB   . TYR   A 1 12  ? -33.294 13.182  -4.227  1.00 114.23 ? 12  TYR   A CB   1 
ATOM   85   C  CG   . TYR   A 1 12  ? -33.732 14.606  -4.386  1.00 120.21 ? 12  TYR   A CG   1 
ATOM   86   C  CD1  . TYR   A 1 12  ? -34.898 15.049  -3.768  1.00 121.43 ? 12  TYR   A CD1  1 
ATOM   87   C  CD2  . TYR   A 1 12  ? -33.043 15.490  -5.193  1.00 122.22 ? 12  TYR   A CD2  1 
ATOM   88   C  CE1  . TYR   A 1 12  ? -35.329 16.344  -3.904  1.00 122.32 ? 12  TYR   A CE1  1 
ATOM   89   C  CE2  . TYR   A 1 12  ? -33.468 16.794  -5.338  1.00 118.81 ? 12  TYR   A CE2  1 
ATOM   90   C  CZ   . TYR   A 1 12  ? -34.613 17.212  -4.692  1.00 122.50 ? 12  TYR   A CZ   1 
ATOM   91   O  OH   . TYR   A 1 12  ? -35.053 18.507  -4.833  1.00 133.63 ? 12  TYR   A OH   1 
ATOM   92   N  N    . PRO   A 1 13  ? -35.349 12.665  -6.963  1.00 110.75 ? 13  PRO   A N    1 
ATOM   93   C  CA   . PRO   A 1 13  ? -35.378 12.749  -8.420  1.00 110.65 ? 13  PRO   A CA   1 
ATOM   94   C  C    . PRO   A 1 13  ? -34.789 14.040  -8.934  1.00 109.06 ? 13  PRO   A C    1 
ATOM   95   O  O    . PRO   A 1 13  ? -35.275 15.132  -8.629  1.00 108.67 ? 13  PRO   A O    1 
ATOM   96   C  CB   . PRO   A 1 13  ? -36.869 12.685  -8.710  1.00 110.67 ? 13  PRO   A CB   1 
ATOM   97   C  CG   . PRO   A 1 13  ? -37.450 13.497  -7.570  1.00 106.32 ? 13  PRO   A CG   1 
ATOM   98   C  CD   . PRO   A 1 13  ? -36.600 13.166  -6.366  1.00 109.54 ? 13  PRO   A CD   1 
ATOM   99   N  N    . ASN   A 1 14  ? -33.755 13.918  -9.747  1.00 110.13 ? 14  ASN   A N    1 
ATOM   100  C  CA   . ASN   A 1 14  ? -33.025 15.054  -10.285 1.00 115.21 ? 14  ASN   A CA   1 
ATOM   101  C  C    . ASN   A 1 14  ? -33.388 15.188  -11.770 1.00 119.21 ? 14  ASN   A C    1 
ATOM   102  O  O    . ASN   A 1 14  ? -32.647 14.745  -12.648 1.00 121.32 ? 14  ASN   A O    1 
ATOM   103  C  CB   . ASN   A 1 14  ? -31.517 14.811  -10.036 1.00 115.29 ? 14  ASN   A CB   1 
ATOM   104  C  CG   . ASN   A 1 14  ? -31.172 14.766  -8.543  1.00 116.57 ? 14  ASN   A CG   1 
ATOM   105  O  OD1  . ASN   A 1 14  ? -30.784 13.728  -7.994  1.00 119.90 ? 14  ASN   A OD1  1 
ATOM   106  N  ND2  . ASN   A 1 14  ? -31.298 15.902  -7.889  1.00 117.20 ? 14  ASN   A ND2  1 
ATOM   107  N  N    . THR   A 1 15  ? -34.540 15.835  -12.042 1.00 115.52 ? 15  THR   A N    1 
ATOM   108  C  CA   . THR   A 1 15  ? -35.255 15.693  -13.317 1.00 113.08 ? 15  THR   A CA   1 
ATOM   109  C  C    . THR   A 1 15  ? -34.428 16.125  -14.526 1.00 119.85 ? 15  THR   A C    1 
ATOM   110  O  O    . THR   A 1 15  ? -34.691 15.669  -15.652 1.00 118.56 ? 15  THR   A O    1 
ATOM   111  C  CB   . THR   A 1 15  ? -36.546 16.506  -13.272 1.00 111.87 ? 15  THR   A CB   1 
ATOM   112  O  OG1  . THR   A 1 15  ? -37.335 16.064  -12.170 1.00 113.86 ? 15  THR   A OG1  1 
ATOM   113  C  CG2  . THR   A 1 15  ? -37.358 16.266  -14.517 1.00 125.86 ? 15  THR   A CG2  1 
ATOM   114  N  N    . ASP   A 1 16  ? -33.423 16.975  -14.306 1.00 122.37 ? 16  ASP   A N    1 
ATOM   115  C  CA   . ASP   A 1 16  ? -32.628 17.538  -15.392 1.00 125.27 ? 16  ASP   A CA   1 
ATOM   116  C  C    . ASP   A 1 16  ? -31.646 16.526  -16.001 1.00 126.86 ? 16  ASP   A C    1 
ATOM   117  O  O    . ASP   A 1 16  ? -31.321 16.638  -17.192 1.00 123.11 ? 16  ASP   A O    1 
ATOM   118  C  CB   . ASP   A 1 16  ? -31.947 18.811  -14.863 1.00 130.50 ? 16  ASP   A CB   1 
ATOM   119  C  CG   . ASP   A 1 16  ? -30.894 18.533  -13.780 1.00 135.53 ? 16  ASP   A CG   1 
ATOM   120  O  OD1  . ASP   A 1 16  ? -29.937 17.765  -14.032 1.00 139.71 ? 16  ASP   A OD1  1 
ATOM   121  O  OD2  . ASP   A 1 16  ? -30.991 19.149  -12.687 1.00 134.94 ? 16  ASP   A OD2  1 
ATOM   122  N  N    . ILE   A 1 17  ? -31.188 15.527  -15.224 1.00 128.75 ? 17  ILE   A N    1 
ATOM   123  C  CA   . ILE   A 1 17  ? -30.316 14.446  -15.708 1.00 125.81 ? 17  ILE   A CA   1 
ATOM   124  C  C    . ILE   A 1 17  ? -31.099 13.170  -16.022 1.00 123.92 ? 17  ILE   A C    1 
ATOM   125  O  O    . ILE   A 1 17  ? -30.513 12.139  -16.381 1.00 123.66 ? 17  ILE   A O    1 
ATOM   126  C  CB   . ILE   A 1 17  ? -29.185 14.123  -14.709 1.00 118.57 ? 17  ILE   A CB   1 
ATOM   127  C  CG1  . ILE   A 1 17  ? -29.787 13.705  -13.364 1.00 119.06 ? 17  ILE   A CG1  1 
ATOM   128  C  CG2  . ILE   A 1 17  ? -28.157 15.241  -14.629 1.00 116.42 ? 17  ILE   A CG2  1 
ATOM   129  C  CD1  . ILE   A 1 17  ? -28.790 13.158  -12.391 1.00 120.99 ? 17  ILE   A CD1  1 
ATOM   130  N  N    . GLY   A 1 18  ? -32.416 13.212  -15.884 1.00 121.25 ? 18  GLY   A N    1 
ATOM   131  C  CA   . GLY   A 1 18  ? -33.253 12.139  -16.375 1.00 120.29 ? 18  GLY   A CA   1 
ATOM   132  C  C    . GLY   A 1 18  ? -33.994 11.366  -15.317 1.00 109.67 ? 18  GLY   A C    1 
ATOM   133  O  O    . GLY   A 1 18  ? -34.870 10.562  -15.669 1.00 104.49 ? 18  GLY   A O    1 
ATOM   134  N  N    . ASP   A 1 19  ? -33.672 11.559  -14.046 1.00 108.52 ? 19  ASP   A N    1 
ATOM   135  C  CA   . ASP   A 1 19  ? -34.430 10.922  -12.980 1.00 111.22 ? 19  ASP   A CA   1 
ATOM   136  C  C    . ASP   A 1 19  ? -35.929 11.163  -13.215 1.00 105.99 ? 19  ASP   A C    1 
ATOM   137  O  O    . ASP   A 1 19  ? -36.342 12.321  -13.363 1.00 111.21 ? 19  ASP   A O    1 
ATOM   138  C  CB   . ASP   A 1 19  ? -34.020 11.479  -11.604 1.00 113.06 ? 19  ASP   A CB   1 
ATOM   139  C  CG   . ASP   A 1 19  ? -32.864 10.692  -10.930 1.00 112.05 ? 19  ASP   A CG   1 
ATOM   140  O  OD1  . ASP   A 1 19  ? -32.486 9.614   -11.441 1.00 111.72 ? 19  ASP   A OD1  1 
ATOM   141  O  OD2  . ASP   A 1 19  ? -32.370 11.125  -9.851  1.00 106.31 ? 19  ASP   A OD2  1 
ATOM   142  N  N    . PRO   A 1 20  ? -36.756 10.121  -13.289 1.00 103.49 ? 20  PRO   A N    1 
ATOM   143  C  CA   . PRO   A 1 20  ? -38.199 10.357  -13.306 1.00 108.73 ? 20  PRO   A CA   1 
ATOM   144  C  C    . PRO   A 1 20  ? -38.614 11.111  -12.062 1.00 112.32 ? 20  PRO   A C    1 
ATOM   145  O  O    . PRO   A 1 20  ? -37.861 11.224  -11.098 1.00 115.64 ? 20  PRO   A O    1 
ATOM   146  C  CB   . PRO   A 1 20  ? -38.801 8.946   -13.328 1.00 110.29 ? 20  PRO   A CB   1 
ATOM   147  C  CG   . PRO   A 1 20  ? -37.692 8.062   -13.759 1.00 109.11 ? 20  PRO   A CG   1 
ATOM   148  C  CD   . PRO   A 1 20  ? -36.466 8.686   -13.174 1.00 107.85 ? 20  PRO   A CD   1 
ATOM   149  N  N    . SER   A 1 21  ? -39.836 11.631  -12.094 1.00 117.86 ? 21  SER   A N    1 
ATOM   150  C  CA   . SER   A 1 21  ? -40.367 12.378  -10.959 1.00 118.89 ? 21  SER   A CA   1 
ATOM   151  C  C    . SER   A 1 21  ? -40.354 11.539  -9.678  1.00 120.46 ? 21  SER   A C    1 
ATOM   152  O  O    . SER   A 1 21  ? -39.710 11.897  -8.690  1.00 121.97 ? 21  SER   A O    1 
ATOM   153  C  CB   . SER   A 1 21  ? -41.784 12.854  -11.293 1.00 123.03 ? 21  SER   A CB   1 
ATOM   154  O  OG   . SER   A 1 21  ? -42.364 13.555  -10.211 1.00 120.68 ? 21  SER   A OG   1 
ATOM   155  N  N    . TYR   A 1 22  ? -41.071 10.414  -9.678  1.00 123.49 ? 22  TYR   A N    1 
ATOM   156  C  CA   . TYR   A 1 22  ? -41.144 9.441   -8.584  1.00 123.66 ? 22  TYR   A CA   1 
ATOM   157  C  C    . TYR   A 1 22  ? -39.810 8.826   -8.121  1.00 122.42 ? 22  TYR   A C    1 
ATOM   158  O  O    . TYR   A 1 22  ? -38.836 8.767   -8.896  1.00 120.22 ? 22  TYR   A O    1 
ATOM   159  C  CB   . TYR   A 1 22  ? -42.163 8.357   -8.972  1.00 120.84 ? 22  TYR   A CB   1 
ATOM   160  C  CG   . TYR   A 1 22  ? -41.924 7.743   -10.340 1.00 118.92 ? 22  TYR   A CG   1 
ATOM   161  C  CD1  . TYR   A 1 22  ? -40.901 6.853   -10.565 1.00 118.51 ? 22  TYR   A CD1  1 
ATOM   162  C  CD2  . TYR   A 1 22  ? -42.651 8.185   -11.440 1.00 123.39 ? 22  TYR   A CD2  1 
ATOM   163  C  CE1  . TYR   A 1 22  ? -40.660 6.341   -11.834 1.00 120.51 ? 22  TYR   A CE1  1 
ATOM   164  C  CE2  . TYR   A 1 22  ? -42.434 7.671   -12.703 1.00 127.02 ? 22  TYR   A CE2  1 
ATOM   165  C  CZ   . TYR   A 1 22  ? -41.428 6.752   -12.897 1.00 125.33 ? 22  TYR   A CZ   1 
ATOM   166  O  OH   . TYR   A 1 22  ? -41.189 6.235   -14.156 1.00 133.99 ? 22  TYR   A OH   1 
ATOM   167  N  N    . PRO   A 1 23  ? -39.717 8.400   -6.847  1.00 117.40 ? 23  PRO   A N    1 
ATOM   168  C  CA   . PRO   A 1 23  ? -38.490 7.737   -6.368  1.00 109.91 ? 23  PRO   A CA   1 
ATOM   169  C  C    . PRO   A 1 23  ? -38.348 6.364   -7.006  1.00 108.99 ? 23  PRO   A C    1 
ATOM   170  O  O    . PRO   A 1 23  ? -39.279 5.555   -6.995  1.00 111.98 ? 23  PRO   A O    1 
ATOM   171  C  CB   . PRO   A 1 23  ? -38.706 7.624   -4.856  1.00 103.16 ? 23  PRO   A CB   1 
ATOM   172  C  CG   . PRO   A 1 23  ? -39.767 8.588   -4.536  1.00 112.40 ? 23  PRO   A CG   1 
ATOM   173  C  CD   . PRO   A 1 23  ? -40.659 8.660   -5.744  1.00 111.71 ? 23  PRO   A CD   1 
ATOM   174  N  N    . HIS   A 1 24  ? -37.162 6.090   -7.526  1.00 102.77 ? 24  HIS   A N    1 
ATOM   175  C  CA   . HIS   A 1 24  ? -36.959 4.977   -8.433  1.00 98.47  ? 24  HIS   A CA   1 
ATOM   176  C  C    . HIS   A 1 24  ? -35.724 4.180   -8.047  1.00 96.20  ? 24  HIS   A C    1 
ATOM   177  O  O    . HIS   A 1 24  ? -34.859 4.655   -7.311  1.00 99.18  ? 24  HIS   A O    1 
ATOM   178  C  CB   . HIS   A 1 24  ? -36.829 5.511   -9.856  1.00 102.14 ? 24  HIS   A CB   1 
ATOM   179  C  CG   . HIS   A 1 24  ? -35.695 6.478   -10.028 1.00 101.82 ? 24  HIS   A CG   1 
ATOM   180  N  ND1  . HIS   A 1 24  ? -35.814 7.811   -9.698  1.00 100.52 ? 24  HIS   A ND1  1 
ATOM   181  C  CD2  . HIS   A 1 24  ? -34.433 6.316   -10.496 1.00 98.21  ? 24  HIS   A CD2  1 
ATOM   182  C  CE1  . HIS   A 1 24  ? -34.675 8.425   -9.953  1.00 100.49 ? 24  HIS   A CE1  1 
ATOM   183  N  NE2  . HIS   A 1 24  ? -33.819 7.542   -10.436 1.00 93.32  ? 24  HIS   A NE2  1 
ATOM   184  N  N    . ILE   A 1 25  ? -35.659 2.953   -8.554  1.00 89.91  ? 25  ILE   A N    1 
ATOM   185  C  CA   . ILE   A 1 25  ? -34.425 2.178   -8.609  1.00 83.59  ? 25  ILE   A CA   1 
ATOM   186  C  C    . ILE   A 1 25  ? -34.008 2.100   -10.061 1.00 84.54  ? 25  ILE   A C    1 
ATOM   187  O  O    . ILE   A 1 25  ? -34.844 2.193   -10.965 1.00 88.76  ? 25  ILE   A O    1 
ATOM   188  C  CB   . ILE   A 1 25  ? -34.607 0.773   -8.016  1.00 82.07  ? 25  ILE   A CB   1 
ATOM   189  C  CG1  . ILE   A 1 25  ? -35.604 -0.009  -8.835  1.00 83.38  ? 25  ILE   A CG1  1 
ATOM   190  C  CG2  . ILE   A 1 25  ? -35.169 0.833   -6.634  1.00 91.79  ? 25  ILE   A CG2  1 
ATOM   191  C  CD1  . ILE   A 1 25  ? -35.649 -1.422  -8.431  1.00 84.42  ? 25  ILE   A CD1  1 
ATOM   192  N  N    . GLY   A 1 26  ? -32.717 1.926   -10.298 1.00 81.86  ? 26  GLY   A N    1 
ATOM   193  C  CA   . GLY   A 1 26  ? -32.275 1.938   -11.679 1.00 84.15  ? 26  GLY   A CA   1 
ATOM   194  C  C    . GLY   A 1 26  ? -30.930 1.287   -11.884 1.00 84.53  ? 26  GLY   A C    1 
ATOM   195  O  O    . GLY   A 1 26  ? -30.137 1.133   -10.948 1.00 82.37  ? 26  GLY   A O    1 
ATOM   196  N  N    . ILE   A 1 27  ? -30.679 0.906   -13.135 1.00 84.23  ? 27  ILE   A N    1 
ATOM   197  C  CA   . ILE   A 1 27  ? -29.377 0.389   -13.559 1.00 88.47  ? 27  ILE   A CA   1 
ATOM   198  C  C    . ILE   A 1 27  ? -28.580 1.516   -14.204 1.00 89.57  ? 27  ILE   A C    1 
ATOM   199  O  O    . ILE   A 1 27  ? -29.067 2.199   -15.114 1.00 93.64  ? 27  ILE   A O    1 
ATOM   200  C  CB   . ILE   A 1 27  ? -29.524 -0.820  -14.507 1.00 85.67  ? 27  ILE   A CB   1 
ATOM   201  C  CG1  . ILE   A 1 27  ? -30.193 -1.984  -13.782 1.00 84.81  ? 27  ILE   A CG1  1 
ATOM   202  C  CG2  . ILE   A 1 27  ? -28.179 -1.269  -15.074 1.00 78.17  ? 27  ILE   A CG2  1 
ATOM   203  C  CD1  . ILE   A 1 27  ? -31.653 -1.979  -13.875 1.00 86.08  ? 27  ILE   A CD1  1 
ATOM   204  N  N    . ASP   A 1 28  ? -27.402 1.780   -13.645 1.00 83.43  ? 28  ASP   A N    1 
ATOM   205  C  CA   . ASP   A 1 28  ? -26.518 2.853   -14.159 1.00 83.98  ? 28  ASP   A CA   1 
ATOM   206  C  C    . ASP   A 1 28  ? -25.287 2.173   -14.750 1.00 85.27  ? 28  ASP   A C    1 
ATOM   207  O  O    . ASP   A 1 28  ? -24.427 1.761   -13.973 1.00 85.12  ? 28  ASP   A O    1 
ATOM   208  C  CB   . ASP   A 1 28  ? -26.167 3.841   -13.046 1.00 86.62  ? 28  ASP   A CB   1 
ATOM   209  C  CG   . ASP   A 1 28  ? -27.385 4.414   -12.343 1.00 93.56  ? 28  ASP   A CG   1 
ATOM   210  O  OD1  . ASP   A 1 28  ? -28.441 4.483   -12.977 1.00 96.98  ? 28  ASP   A OD1  1 
ATOM   211  O  OD2  . ASP   A 1 28  ? -27.267 4.790   -11.171 1.00 91.89  ? 28  ASP   A OD2  1 
ATOM   212  N  N    . ILE   A 1 29  ? -25.237 2.024   -16.073 1.00 88.85  ? 29  ILE   A N    1 
ATOM   213  C  CA   . ILE   A 1 29  ? -24.091 1.314   -16.707 1.00 91.69  ? 29  ILE   A CA   1 
ATOM   214  C  C    . ILE   A 1 29  ? -23.146 2.324   -17.348 1.00 91.88  ? 29  ILE   A C    1 
ATOM   215  O  O    . ILE   A 1 29  ? -23.481 2.813   -18.420 1.00 96.43  ? 29  ILE   A O    1 
ATOM   216  C  CB   . ILE   A 1 29  ? -24.624 0.340   -17.768 1.00 89.34  ? 29  ILE   A CB   1 
ATOM   217  C  CG1  . ILE   A 1 29  ? -25.036 -0.995  -17.154 1.00 89.29  ? 29  ILE   A CG1  1 
ATOM   218  C  CG2  . ILE   A 1 29  ? -23.605 0.152   -18.872 1.00 85.02  ? 29  ILE   A CG2  1 
ATOM   219  C  CD1  . ILE   A 1 29  ? -24.875 -2.157  -18.093 1.00 89.02  ? 29  ILE   A CD1  1 
ATOM   220  N  N    . LYS   A 1 30  ? -22.060 2.671   -16.649 1.00 93.50  ? 30  LYS   A N    1 
ATOM   221  C  CA   . LYS   A 1 30  ? -20.951 3.568   -17.093 1.00 97.59  ? 30  LYS   A CA   1 
ATOM   222  C  C    . LYS   A 1 30  ? -21.347 5.052   -17.125 1.00 100.76 ? 30  LYS   A C    1 
ATOM   223  O  O    . LYS   A 1 30  ? -20.503 5.849   -17.541 1.00 106.41 ? 30  LYS   A O    1 
ATOM   224  C  CB   . LYS   A 1 30  ? -20.296 3.091   -18.392 1.00 86.71  ? 30  LYS   A CB   1 
ATOM   225  C  CG   . LYS   A 1 30  ? -18.820 3.423   -18.543 1.00 99.89  ? 30  LYS   A CG   1 
ATOM   226  C  CD   . LYS   A 1 30  ? -18.176 2.692   -19.697 1.00 107.86 ? 30  LYS   A CD   1 
ATOM   227  C  CE   . LYS   A 1 30  ? -16.978 1.867   -19.281 1.00 103.20 ? 30  LYS   A CE   1 
ATOM   228  N  NZ   . LYS   A 1 30  ? -16.034 1.666   -20.404 1.00 99.98  ? 30  LYS   A NZ   1 
ATOM   229  N  N    . SER   A 1 31  ? -22.554 5.414   -16.685 1.00 97.36  ? 31  SER   A N    1 
ATOM   230  C  CA   . SER   A 1 31  ? -23.006 6.826   -16.667 1.00 102.74 ? 31  SER   A CA   1 
ATOM   231  C  C    . SER   A 1 31  ? -24.076 6.979   -15.590 1.00 103.62 ? 31  SER   A C    1 
ATOM   232  O  O    . SER   A 1 31  ? -24.860 6.047   -15.421 1.00 105.24 ? 31  SER   A O    1 
ATOM   233  C  CB   . SER   A 1 31  ? -23.535 7.229   -18.009 1.00 110.09 ? 31  SER   A CB   1 
ATOM   234  O  OG   . SER   A 1 31  ? -24.571 8.188   -17.875 1.00 114.83 ? 31  SER   A OG   1 
ATOM   235  N  N    . VAL   A 1 32  ? -24.160 8.147   -14.961 1.00 103.49 ? 32  VAL   A N    1 
ATOM   236  C  CA   . VAL   A 1 32  ? -25.165 8.359   -13.881 1.00 104.70 ? 32  VAL   A CA   1 
ATOM   237  C  C    . VAL   A 1 32  ? -26.576 8.249   -14.456 1.00 102.46 ? 32  VAL   A C    1 
ATOM   238  O  O    . VAL   A 1 32  ? -27.452 7.782   -13.733 1.00 96.36  ? 32  VAL   A O    1 
ATOM   239  C  CB   . VAL   A 1 32  ? -24.972 9.687   -13.137 1.00 110.08 ? 32  VAL   A CB   1 
ATOM   240  C  CG1  . VAL   A 1 32  ? -24.511 10.788  -14.073 1.00 117.25 ? 32  VAL   A CG1  1 
ATOM   241  C  CG2  . VAL   A 1 32  ? -26.250 10.084  -12.423 1.00 104.34 ? 32  VAL   A CG2  1 
ATOM   242  N  N    . ARG   A 1 33  ? -26.804 8.733   -15.675 1.00 107.10 ? 33  ARG   A N    1 
ATOM   243  C  CA   . ARG   A 1 33  ? -28.175 8.616   -16.229 1.00 109.21 ? 33  ARG   A CA   1 
ATOM   244  C  C    . ARG   A 1 33  ? -28.498 7.124   -16.284 1.00 100.36 ? 33  ARG   A C    1 
ATOM   245  O  O    . ARG   A 1 33  ? -27.688 6.368   -16.824 1.00 92.67  ? 33  ARG   A O    1 
ATOM   246  C  CB   . ARG   A 1 33  ? -28.255 9.271   -17.609 1.00 115.02 ? 33  ARG   A CB   1 
ATOM   247  C  CG   . ARG   A 1 33  ? -28.422 10.783  -17.566 1.00 112.35 ? 33  ARG   A CG   1 
ATOM   248  C  CD   . ARG   A 1 33  ? -27.412 11.485  -18.449 1.00 120.56 ? 33  ARG   A CD   1 
ATOM   249  N  NE   . ARG   A 1 33  ? -27.818 12.838  -18.789 1.00 123.49 ? 33  ARG   A NE   1 
ATOM   250  C  CZ   . ARG   A 1 33  ? -29.046 13.194  -19.136 1.00 124.78 ? 33  ARG   A CZ   1 
ATOM   251  N  NH1  . ARG   A 1 33  ? -30.009 12.292  -19.191 1.00 119.35 ? 33  ARG   A NH1  1 
ATOM   252  N  NH2  . ARG   A 1 33  ? -29.309 14.453  -19.427 1.00 123.94 ? 33  ARG   A NH2  1 
ATOM   253  N  N    . SER   A 1 34  ? -29.665 6.744   -15.773 1.00 97.60  ? 34  SER   A N    1 
ATOM   254  C  CA   . SER   A 1 34  ? -30.045 5.315   -15.682 1.00 96.19  ? 34  SER   A CA   1 
ATOM   255  C  C    . SER   A 1 34  ? -30.496 4.791   -17.041 1.00 99.79  ? 34  SER   A C    1 
ATOM   256  O  O    . SER   A 1 34  ? -31.224 5.512   -17.734 1.00 100.61 ? 34  SER   A O    1 
ATOM   257  C  CB   . SER   A 1 34  ? -31.113 5.134   -14.649 1.00 95.69  ? 34  SER   A CB   1 
ATOM   258  O  OG   . SER   A 1 34  ? -30.911 6.024   -13.562 1.00 95.29  ? 34  SER   A OG   1 
ATOM   259  N  N    . LYS   A 1 35  ? -30.065 3.578   -17.391 1.00 97.29  ? 35  LYS   A N    1 
ATOM   260  C  CA   . LYS   A 1 35  ? -30.476 2.957   -18.643 1.00 94.03  ? 35  LYS   A CA   1 
ATOM   261  C  C    . LYS   A 1 35  ? -31.918 2.454   -18.553 1.00 94.60  ? 35  LYS   A C    1 
ATOM   262  O  O    . LYS   A 1 35  ? -32.680 2.589   -19.515 1.00 103.46 ? 35  LYS   A O    1 
ATOM   263  C  CB   . LYS   A 1 35  ? -29.506 1.833   -19.004 1.00 90.12  ? 35  LYS   A CB   1 
ATOM   264  C  CG   . LYS   A 1 35  ? -28.025 2.262   -18.988 1.00 90.18  ? 35  LYS   A CG   1 
ATOM   265  C  CD   . LYS   A 1 35  ? -27.694 3.469   -19.871 1.00 98.84  ? 35  LYS   A CD   1 
ATOM   266  C  CE   . LYS   A 1 35  ? -26.208 3.891   -19.713 1.00 100.96 ? 35  LYS   A CE   1 
ATOM   267  N  NZ   . LYS   A 1 35  ? -25.441 4.278   -20.961 1.00 94.40  ? 35  LYS   A NZ   1 
ATOM   268  N  N    . LYS   A 1 36  ? -32.328 1.909   -17.403 1.00 93.13  ? 36  LYS   A N    1 
ATOM   269  C  CA   . LYS   A 1 36  ? -33.733 1.590   -17.159 1.00 94.12  ? 36  LYS   A CA   1 
ATOM   270  C  C    . LYS   A 1 36  ? -34.024 1.798   -15.670 1.00 96.48  ? 36  LYS   A C    1 
ATOM   271  O  O    . LYS   A 1 36  ? -33.116 1.697   -14.832 1.00 93.11  ? 36  LYS   A O    1 
ATOM   272  C  CB   . LYS   A 1 36  ? -34.057 0.157   -17.616 1.00 91.37  ? 36  LYS   A CB   1 
ATOM   273  C  CG   . LYS   A 1 36  ? -35.530 -0.236  -17.558 1.00 97.56  ? 36  LYS   A CG   1 
ATOM   274  C  CD   . LYS   A 1 36  ? -35.816 -1.462  -18.450 1.00 107.21 ? 36  LYS   A CD   1 
ATOM   275  C  CE   . LYS   A 1 36  ? -37.054 -2.282  -17.987 1.00 112.85 ? 36  LYS   A CE   1 
ATOM   276  N  NZ   . LYS   A 1 36  ? -36.910 -3.239  -16.827 1.00 97.99  ? 36  LYS   A NZ   1 
ATOM   277  N  N    . THR   A 1 37  ? -35.287 2.123   -15.346 1.00 96.38  ? 37  THR   A N    1 
ATOM   278  C  CA   . THR   A 1 37  ? -35.716 2.366   -13.964 1.00 93.52  ? 37  THR   A CA   1 
ATOM   279  C  C    . THR   A 1 37  ? -37.108 1.785   -13.732 1.00 95.78  ? 37  THR   A C    1 
ATOM   280  O  O    . THR   A 1 37  ? -37.785 1.340   -14.665 1.00 98.91  ? 37  THR   A O    1 
ATOM   281  C  CB   . THR   A 1 37  ? -35.782 3.858   -13.604 1.00 92.94  ? 37  THR   A CB   1 
ATOM   282  O  OG1  . THR   A 1 37  ? -36.783 4.506   -14.398 1.00 102.99 ? 37  THR   A OG1  1 
ATOM   283  C  CG2  . THR   A 1 37  ? -34.472 4.529   -13.857 1.00 91.10  ? 37  THR   A CG2  1 
ATOM   284  N  N    . ALA   A 1 38  ? -37.546 1.827   -12.470 1.00 90.47  ? 38  ALA   A N    1 
ATOM   285  C  CA   . ALA   A 1 38  ? -38.897 1.432   -12.093 1.00 88.68  ? 38  ALA   A CA   1 
ATOM   286  C  C    . ALA   A 1 38  ? -39.305 2.152   -10.818 1.00 93.51  ? 38  ALA   A C    1 
ATOM   287  O  O    . ALA   A 1 38  ? -38.486 2.384   -9.925  1.00 93.45  ? 38  ALA   A O    1 
ATOM   288  C  CB   . ALA   A 1 38  ? -39.029 -0.076  -11.883 1.00 90.38  ? 38  ALA   A CB   1 
ATOM   289  N  N    . LYS   A 1 39  ? -40.590 2.497   -10.741 1.00 100.94 ? 39  LYS   A N    1 
ATOM   290  C  CA   . LYS   A 1 39  ? -41.114 3.192   -9.573  1.00 102.65 ? 39  LYS   A CA   1 
ATOM   291  C  C    . LYS   A 1 39  ? -40.919 2.353   -8.326  1.00 102.69 ? 39  LYS   A C    1 
ATOM   292  O  O    . LYS   A 1 39  ? -41.132 1.135   -8.334  1.00 102.77 ? 39  LYS   A O    1 
ATOM   293  C  CB   . LYS   A 1 39  ? -42.606 3.530   -9.739  1.00 111.44 ? 39  LYS   A CB   1 
ATOM   294  C  CG   . LYS   A 1 39  ? -43.217 4.281   -8.513  1.00 113.79 ? 39  LYS   A CG   1 
ATOM   295  C  CD   . LYS   A 1 39  ? -44.676 4.730   -8.705  1.00 117.77 ? 39  LYS   A CD   1 
ATOM   296  C  CE   . LYS   A 1 39  ? -45.265 5.276   -7.411  1.00 117.99 ? 39  LYS   A CE   1 
ATOM   297  N  NZ   . LYS   A 1 39  ? -44.575 6.521   -6.985  1.00 114.99 ? 39  LYS   A NZ   1 
ATOM   298  N  N    . TRP   A 1 40  ? -40.553 3.033   -7.241  1.00 107.74 ? 40  TRP   A N    1 
ATOM   299  C  CA   . TRP   A 1 40  ? -40.258 2.406   -5.959  1.00 106.94 ? 40  TRP   A CA   1 
ATOM   300  C  C    . TRP   A 1 40  ? -41.046 3.122   -4.863  1.00 106.02 ? 40  TRP   A C    1 
ATOM   301  O  O    . TRP   A 1 40  ? -40.745 4.276   -4.540  1.00 100.86 ? 40  TRP   A O    1 
ATOM   302  C  CB   . TRP   A 1 40  ? -38.759 2.473   -5.694  1.00 101.53 ? 40  TRP   A CB   1 
ATOM   303  C  CG   . TRP   A 1 40  ? -38.350 2.148   -4.297  1.00 105.97 ? 40  TRP   A CG   1 
ATOM   304  C  CD1  . TRP   A 1 40  ? -39.000 1.335   -3.401  1.00 109.46 ? 40  TRP   A CD1  1 
ATOM   305  C  CD2  . TRP   A 1 40  ? -37.167 2.587   -3.648  1.00 99.57  ? 40  TRP   A CD2  1 
ATOM   306  N  NE1  . TRP   A 1 40  ? -38.294 1.265   -2.228  1.00 103.64 ? 40  TRP   A NE1  1 
ATOM   307  C  CE2  . TRP   A 1 40  ? -37.164 2.026   -2.359  1.00 99.61  ? 40  TRP   A CE2  1 
ATOM   308  C  CE3  . TRP   A 1 40  ? -36.112 3.409   -4.029  1.00 93.71  ? 40  TRP   A CE3  1 
ATOM   309  C  CZ2  . TRP   A 1 40  ? -36.154 2.262   -1.463  1.00 98.19  ? 40  TRP   A CZ2  1 
ATOM   310  C  CZ3  . TRP   A 1 40  ? -35.122 3.634   -3.147  1.00 91.76  ? 40  TRP   A CZ3  1 
ATOM   311  C  CH2  . TRP   A 1 40  ? -35.140 3.066   -1.875  1.00 93.77  ? 40  TRP   A CH2  1 
ATOM   312  N  N    . ASN   A 1 41  ? -42.045 2.435   -4.290  1.00 107.90 ? 41  ASN   A N    1 
ATOM   313  C  CA   . ASN   A 1 41  ? -42.855 2.969   -3.187  1.00 110.13 ? 41  ASN   A CA   1 
ATOM   314  C  C    . ASN   A 1 41  ? -42.038 2.887   -1.903  1.00 108.25 ? 41  ASN   A C    1 
ATOM   315  O  O    . ASN   A 1 41  ? -42.228 2.019   -1.045  1.00 105.40 ? 41  ASN   A O    1 
ATOM   316  C  CB   . ASN   A 1 41  ? -44.186 2.237   -3.062  1.00 117.19 ? 41  ASN   A CB   1 
ATOM   317  C  CG   . ASN   A 1 41  ? -45.123 2.519   -4.236  1.00 128.94 ? 41  ASN   A CG   1 
ATOM   318  O  OD1  . ASN   A 1 41  ? -45.195 1.748   -5.203  1.00 129.35 ? 41  ASN   A OD1  1 
ATOM   319  N  ND2  . ASN   A 1 41  ? -45.838 3.644   -4.160  1.00 131.92 ? 41  ASN   A ND2  1 
ATOM   320  N  N    . MET   A 1 42  ? -41.109 3.833   -1.796  1.00 110.99 ? 42  MET   A N    1 
ATOM   321  C  CA   . MET   A 1 42  ? -40.160 3.896   -0.695  1.00 106.64 ? 42  MET   A CA   1 
ATOM   322  C  C    . MET   A 1 42  ? -40.878 4.002   0.641   1.00 106.55 ? 42  MET   A C    1 
ATOM   323  O  O    . MET   A 1 42  ? -41.939 4.624   0.746   1.00 111.10 ? 42  MET   A O    1 
ATOM   324  C  CB   . MET   A 1 42  ? -39.236 5.095   -0.901  1.00 102.46 ? 42  MET   A CB   1 
ATOM   325  C  CG   . MET   A 1 42  ? -37.926 4.999   -0.166  1.00 108.89 ? 42  MET   A CG   1 
ATOM   326  S  SD   . MET   A 1 42  ? -38.016 5.756   1.465   1.00 131.33 ? 42  MET   A SD   1 
ATOM   327  C  CE   . MET   A 1 42  ? -38.280 7.477   1.017   1.00 121.34 ? 42  MET   A CE   1 
ATOM   328  N  N    . GLN   A 1 43  ? -40.301 3.383   1.665   1.00 102.33 ? 43  GLN   A N    1 
ATOM   329  C  CA   . GLN   A 1 43  ? -40.869 3.421   3.000   1.00 100.72 ? 43  GLN   A CA   1 
ATOM   330  C  C    . GLN   A 1 43  ? -39.844 4.020   3.937   1.00 101.61 ? 43  GLN   A C    1 
ATOM   331  O  O    . GLN   A 1 43  ? -38.719 3.519   4.031   1.00 99.98  ? 43  GLN   A O    1 
ATOM   332  C  CB   . GLN   A 1 43  ? -41.284 2.035   3.470   1.00 102.57 ? 43  GLN   A CB   1 
ATOM   333  C  CG   . GLN   A 1 43  ? -42.248 1.367   2.510   1.00 108.18 ? 43  GLN   A CG   1 
ATOM   334  C  CD   . GLN   A 1 43  ? -43.173 0.391   3.195   1.00 112.23 ? 43  GLN   A CD   1 
ATOM   335  O  OE1  . GLN   A 1 43  ? -43.216 0.319   4.428   1.00 113.44 ? 43  GLN   A OE1  1 
ATOM   336  N  NE2  . GLN   A 1 43  ? -43.891 -0.401  2.398   1.00 108.21 ? 43  GLN   A NE2  1 
ATOM   337  N  N    . ASN   A 1 44  ? -40.240 5.100   4.613   1.00 110.17 ? 44  ASN   A N    1 
ATOM   338  C  CA   . ASN   A 1 44  ? -39.357 5.845   5.505   1.00 116.06 ? 44  ASN   A CA   1 
ATOM   339  C  C    . ASN   A 1 44  ? -39.274 5.138   6.857   1.00 114.92 ? 44  ASN   A C    1 
ATOM   340  O  O    . ASN   A 1 44  ? -40.301 4.782   7.449   1.00 112.59 ? 44  ASN   A O    1 
ATOM   341  C  CB   . ASN   A 1 44  ? -39.862 7.290   5.672   1.00 114.20 ? 44  ASN   A CB   1 
ATOM   342  C  CG   . ASN   A 1 44  ? -38.981 8.152   6.614   1.00 113.34 ? 44  ASN   A CG   1 
ATOM   343  O  OD1  . ASN   A 1 44  ? -38.459 7.686   7.624   1.00 114.04 ? 44  ASN   A OD1  1 
ATOM   344  N  ND2  . ASN   A 1 44  ? -38.853 9.427   6.282   1.00 113.65 ? 44  ASN   A ND2  1 
ATOM   345  N  N    . GLY   A 1 45  ? -38.043 4.937   7.338   1.00 112.93 ? 45  GLY   A N    1 
ATOM   346  C  CA   . GLY   A 1 45  ? -37.797 4.352   8.641   1.00 111.59 ? 45  GLY   A CA   1 
ATOM   347  C  C    . GLY   A 1 45  ? -37.957 2.853   8.723   1.00 110.53 ? 45  GLY   A C    1 
ATOM   348  O  O    . GLY   A 1 45  ? -37.808 2.283   9.813   1.00 108.27 ? 45  GLY   A O    1 
ATOM   349  N  N    . LYS   A 1 46  ? -38.266 2.192   7.618   1.00 109.75 ? 46  LYS   A N    1 
ATOM   350  C  CA   . LYS   A 1 46  ? -38.429 0.751   7.610   1.00 105.86 ? 46  LYS   A CA   1 
ATOM   351  C  C    . LYS   A 1 46  ? -37.227 0.129   6.912   1.00 100.99 ? 46  LYS   A C    1 
ATOM   352  O  O    . LYS   A 1 46  ? -36.716 0.669   5.921   1.00 100.36 ? 46  LYS   A O    1 
ATOM   353  C  CB   . LYS   A 1 46  ? -39.755 0.357   6.941   1.00 102.69 ? 46  LYS   A CB   1 
ATOM   354  C  CG   . LYS   A 1 46  ? -40.957 1.107   7.543   1.00 104.21 ? 46  LYS   A CG   1 
ATOM   355  C  CD   . LYS   A 1 46  ? -41.464 0.422   8.820   1.00 107.91 ? 46  LYS   A CD   1 
ATOM   356  C  CE   . LYS   A 1 46  ? -42.708 1.095   9.392   1.00 108.70 ? 46  LYS   A CE   1 
ATOM   357  N  NZ   . LYS   A 1 46  ? -42.442 1.894   10.636  1.00 116.70 ? 46  LYS   A NZ   1 
ATOM   358  N  N    . VAL   A 1 47  ? -36.737 -0.977  7.466   1.00 94.96  ? 47  VAL   A N    1 
ATOM   359  C  CA   . VAL   A 1 47  ? -35.623 -1.663  6.833   1.00 90.71  ? 47  VAL   A CA   1 
ATOM   360  C  C    . VAL   A 1 47  ? -36.123 -2.334  5.564   1.00 90.31  ? 47  VAL   A C    1 
ATOM   361  O  O    . VAL   A 1 47  ? -37.207 -2.933  5.542   1.00 97.11  ? 47  VAL   A O    1 
ATOM   362  C  CB   . VAL   A 1 47  ? -35.001 -2.696  7.785   1.00 89.16  ? 47  VAL   A CB   1 
ATOM   363  C  CG1  . VAL   A 1 47  ? -33.850 -3.438  7.090   1.00 85.44  ? 47  VAL   A CG1  1 
ATOM   364  C  CG2  . VAL   A 1 47  ? -34.569 -2.039  9.067   1.00 91.89  ? 47  VAL   A CG2  1 
ATOM   365  N  N    . GLY   A 1 48  ? -35.341 -2.238  4.495   1.00 81.59  ? 48  GLY   A N    1 
ATOM   366  C  CA   . GLY   A 1 48  ? -35.696 -2.867  3.248   1.00 86.03  ? 48  GLY   A CA   1 
ATOM   367  C  C    . GLY   A 1 48  ? -34.560 -3.746  2.767   1.00 81.77  ? 48  GLY   A C    1 
ATOM   368  O  O    . GLY   A 1 48  ? -33.455 -3.700  3.290   1.00 80.72  ? 48  GLY   A O    1 
ATOM   369  N  N    . THR   A 1 49  ? -34.858 -4.545  1.758   1.00 82.64  ? 49  THR   A N    1 
ATOM   370  C  CA   . THR   A 1 49  ? -33.913 -5.517  1.249   1.00 80.42  ? 49  THR   A CA   1 
ATOM   371  C  C    . THR   A 1 49  ? -33.713 -5.306  -0.226  1.00 82.37  ? 49  THR   A C    1 
ATOM   372  O  O    . THR   A 1 49  ? -34.683 -5.247  -0.983  1.00 89.95  ? 49  THR   A O    1 
ATOM   373  C  CB   . THR   A 1 49  ? -34.402 -6.927  1.446   1.00 101.46 ? 49  THR   A CB   1 
ATOM   374  O  OG1  . THR   A 1 49  ? -34.600 -7.169  2.837   1.00 115.70 ? 49  THR   A OG1  1 
ATOM   375  C  CG2  . THR   A 1 49  ? -33.381 -7.869  0.893   1.00 103.10 ? 49  THR   A CG2  1 
ATOM   376  N  N    . ALA   A 1 50  ? -32.465 -5.250  -0.637  1.00 78.09  ? 50  ALA   A N    1 
ATOM   377  C  CA   . ALA   A 1 50  ? -32.128 -5.191  -2.044  1.00 79.32  ? 50  ALA   A CA   1 
ATOM   378  C  C    . ALA   A 1 50  ? -31.526 -6.522  -2.445  1.00 82.88  ? 50  ALA   A C    1 
ATOM   379  O  O    . ALA   A 1 50  ? -30.694 -7.074  -1.714  1.00 83.78  ? 50  ALA   A O    1 
ATOM   380  C  CB   . ALA   A 1 50  ? -31.156 -4.053  -2.330  1.00 73.22  ? 50  ALA   A CB   1 
ATOM   381  N  N    . HIS   A 1 51  ? -31.975 -7.046  -3.583  1.00 81.86  ? 51  HIS   A N    1 
ATOM   382  C  CA   . HIS   A 1 51  ? -31.420 -8.242  -4.200  1.00 81.23  ? 51  HIS   A CA   1 
ATOM   383  C  C    . HIS   A 1 51  ? -30.925 -7.840  -5.580  1.00 76.66  ? 51  HIS   A C    1 
ATOM   384  O  O    . HIS   A 1 51  ? -31.527 -6.986  -6.229  1.00 75.93  ? 51  HIS   A O    1 
ATOM   385  C  CB   . HIS   A 1 51  ? -32.478 -9.358  -4.300  1.00 84.21  ? 51  HIS   A CB   1 
ATOM   386  C  CG   . HIS   A 1 51  ? -32.896 -9.950  -2.981  1.00 90.88  ? 51  HIS   A CG   1 
ATOM   387  N  ND1  . HIS   A 1 51  ? -32.101 -10.817 -2.257  1.00 91.39  ? 51  HIS   A ND1  1 
ATOM   388  C  CD2  . HIS   A 1 51  ? -34.022 -9.774  -2.245  1.00 90.69  ? 51  HIS   A CD2  1 
ATOM   389  C  CE1  . HIS   A 1 51  ? -32.727 -11.166 -1.145  1.00 94.56  ? 51  HIS   A CE1  1 
ATOM   390  N  NE2  . HIS   A 1 51  ? -33.893 -10.545 -1.113  1.00 97.51  ? 51  HIS   A NE2  1 
ATOM   391  N  N    . ILE   A 1 52  ? -29.811 -8.415  -6.018  1.00 75.62  ? 52  ILE   A N    1 
ATOM   392  C  CA   . ILE   A 1 52  ? -29.182 -8.041  -7.288  1.00 74.18  ? 52  ILE   A CA   1 
ATOM   393  C  C    . ILE   A 1 52  ? -28.559 -9.293  -7.879  1.00 78.76  ? 52  ILE   A C    1 
ATOM   394  O  O    . ILE   A 1 52  ? -27.827 -10.011 -7.189  1.00 84.76  ? 52  ILE   A O    1 
ATOM   395  C  CB   . ILE   A 1 52  ? -28.091 -6.966  -7.106  1.00 73.51  ? 52  ILE   A CB   1 
ATOM   396  C  CG1  . ILE   A 1 52  ? -28.667 -5.664  -6.574  1.00 71.49  ? 52  ILE   A CG1  1 
ATOM   397  C  CG2  . ILE   A 1 52  ? -27.371 -6.701  -8.409  1.00 69.55  ? 52  ILE   A CG2  1 
ATOM   398  C  CD1  . ILE   A 1 52  ? -27.598 -4.734  -6.139  1.00 70.49  ? 52  ILE   A CD1  1 
ATOM   399  N  N    . ILE   A 1 53  ? -28.825 -9.557  -9.154  1.00 75.69  ? 53  ILE   A N    1 
ATOM   400  C  CA   . ILE   A 1 53  ? -28.493 -10.852 -9.732  1.00 74.26  ? 53  ILE   A CA   1 
ATOM   401  C  C    . ILE   A 1 53  ? -28.249 -10.730 -11.226 1.00 76.33  ? 53  ILE   A C    1 
ATOM   402  O  O    . ILE   A 1 53  ? -29.046 -10.141 -11.962 1.00 86.20  ? 53  ILE   A O    1 
ATOM   403  C  CB   . ILE   A 1 53  ? -29.590 -11.881 -9.367  1.00 79.76  ? 53  ILE   A CB   1 
ATOM   404  C  CG1  . ILE   A 1 53  ? -30.961 -11.426 -9.832  1.00 83.04  ? 53  ILE   A CG1  1 
ATOM   405  C  CG2  . ILE   A 1 53  ? -29.633 -12.270 -7.867  1.00 91.54  ? 53  ILE   A CG2  1 
ATOM   406  C  CD1  . ILE   A 1 53  ? -32.005 -12.481 -9.634  1.00 94.86  ? 53  ILE   A CD1  1 
ATOM   407  N  N    . TYR   A 1 54  ? -27.114 -11.246 -11.672 1.00 73.67  ? 54  TYR   A N    1 
ATOM   408  C  CA   . TYR   A 1 54  ? -26.731 -11.210 -13.074 1.00 80.14  ? 54  TYR   A CA   1 
ATOM   409  C  C    . TYR   A 1 54  ? -25.898 -12.423 -13.402 1.00 82.03  ? 54  TYR   A C    1 
ATOM   410  O  O    . TYR   A 1 54  ? -25.168 -12.926 -12.549 1.00 80.40  ? 54  TYR   A O    1 
ATOM   411  C  CB   . TYR   A 1 54  ? -25.916 -9.975  -13.410 1.00 80.03  ? 54  TYR   A CB   1 
ATOM   412  C  CG   . TYR   A 1 54  ? -25.090 -10.063 -14.691 1.00 82.21  ? 54  TYR   A CG   1 
ATOM   413  C  CD1  . TYR   A 1 54  ? -23.797 -10.562 -14.665 1.00 75.15  ? 54  TYR   A CD1  1 
ATOM   414  C  CD2  . TYR   A 1 54  ? -25.598 -9.653  -15.912 1.00 90.36  ? 54  TYR   A CD2  1 
ATOM   415  C  CE1  . TYR   A 1 54  ? -23.037 -10.639 -15.792 1.00 82.02  ? 54  TYR   A CE1  1 
ATOM   416  C  CE2  . TYR   A 1 54  ? -24.834 -9.725  -17.066 1.00 90.45  ? 54  TYR   A CE2  1 
ATOM   417  C  CZ   . TYR   A 1 54  ? -23.551 -10.222 -16.997 1.00 89.79  ? 54  TYR   A CZ   1 
ATOM   418  O  OH   . TYR   A 1 54  ? -22.791 -10.308 -18.147 1.00 96.18  ? 54  TYR   A OH   1 
ATOM   419  N  N    . ASN   A 1 55  ? -25.960 -12.845 -14.665 1.00 79.94  ? 55  ASN   A N    1 
ATOM   420  C  CA   . ASN   A 1 55  ? -25.293 -14.069 -15.077 1.00 82.73  ? 55  ASN   A CA   1 
ATOM   421  C  C    . ASN   A 1 55  ? -24.945 -13.977 -16.548 1.00 84.78  ? 55  ASN   A C    1 
ATOM   422  O  O    . ASN   A 1 55  ? -25.591 -13.263 -17.312 1.00 85.60  ? 55  ASN   A O    1 
ATOM   423  C  CB   . ASN   A 1 55  ? -26.185 -15.264 -14.765 1.00 88.13  ? 55  ASN   A CB   1 
ATOM   424  C  CG   . ASN   A 1 55  ? -27.453 -15.254 -15.583 1.00 93.12  ? 55  ASN   A CG   1 
ATOM   425  O  OD1  . ASN   A 1 55  ? -27.404 -15.384 -16.792 1.00 100.79 ? 55  ASN   A OD1  1 
ATOM   426  N  ND2  . ASN   A 1 55  ? -28.583 -14.957 -14.937 1.00 90.68  ? 55  ASN   A ND2  1 
ATOM   427  N  N    . SER   A 1 56  ? -23.914 -14.723 -16.936 1.00 86.76  ? 56  SER   A N    1 
ATOM   428  C  CA   . SER   A 1 56  ? -23.405 -14.627 -18.297 1.00 88.18  ? 56  SER   A CA   1 
ATOM   429  C  C    . SER   A 1 56  ? -24.351 -15.249 -19.320 1.00 92.57  ? 56  SER   A C    1 
ATOM   430  O  O    . SER   A 1 56  ? -24.288 -14.916 -20.507 1.00 99.66  ? 56  SER   A O    1 
ATOM   431  C  CB   . SER   A 1 56  ? -22.043 -15.291 -18.378 1.00 87.72  ? 56  SER   A CB   1 
ATOM   432  O  OG   . SER   A 1 56  ? -21.586 -15.236 -19.708 1.00 100.53 ? 56  SER   A OG   1 
ATOM   433  N  N    . VAL   A 1 57  ? -25.235 -16.139 -18.891 1.00 91.39  ? 57  VAL   A N    1 
ATOM   434  C  CA   . VAL   A 1 57  ? -26.108 -16.833 -19.828 1.00 88.12  ? 57  VAL   A CA   1 
ATOM   435  C  C    . VAL   A 1 57  ? -27.230 -15.913 -20.307 1.00 95.85  ? 57  VAL   A C    1 
ATOM   436  O  O    . VAL   A 1 57  ? -27.385 -15.679 -21.507 1.00 99.98  ? 57  VAL   A O    1 
ATOM   437  C  CB   . VAL   A 1 57  ? -26.684 -18.085 -19.162 1.00 89.29  ? 57  VAL   A CB   1 
ATOM   438  C  CG1  . VAL   A 1 57  ? -27.652 -18.779 -20.095 1.00 87.51  ? 57  VAL   A CG1  1 
ATOM   439  C  CG2  . VAL   A 1 57  ? -25.584 -18.949 -18.668 1.00 91.90  ? 57  VAL   A CG2  1 
ATOM   440  N  N    . ASP   A 1 58  ? -28.077 -15.440 -19.374 1.00 99.37  ? 58  ASP   A N    1 
ATOM   441  C  CA   . ASP   A 1 58  ? -29.104 -14.437 -19.685 1.00 94.89  ? 58  ASP   A CA   1 
ATOM   442  C  C    . ASP   A 1 58  ? -28.494 -13.227 -20.339 1.00 97.61  ? 58  ASP   A C    1 
ATOM   443  O  O    . ASP   A 1 58  ? -29.083 -12.641 -21.255 1.00 105.23 ? 58  ASP   A O    1 
ATOM   444  C  CB   . ASP   A 1 58  ? -29.804 -13.913 -18.420 1.00 101.80 ? 58  ASP   A CB   1 
ATOM   445  C  CG   . ASP   A 1 58  ? -30.605 -14.949 -17.679 1.00 109.27 ? 58  ASP   A CG   1 
ATOM   446  O  OD1  . ASP   A 1 58  ? -31.066 -15.939 -18.294 1.00 112.60 ? 58  ASP   A OD1  1 
ATOM   447  O  OD2  . ASP   A 1 58  ? -30.741 -14.771 -16.446 1.00 105.02 ? 58  ASP   A OD2  1 
ATOM   448  N  N    . LYS   A 1 59  ? -27.334 -12.810 -19.826 1.00 96.97  ? 59  LYS   A N    1 
ATOM   449  C  CA   . LYS   A 1 59  ? -26.802 -11.460 -19.985 1.00 97.95  ? 59  LYS   A CA   1 
ATOM   450  C  C    . LYS   A 1 59  ? -27.857 -10.423 -19.591 1.00 100.29 ? 59  LYS   A C    1 
ATOM   451  O  O    . LYS   A 1 59  ? -28.051 -9.429  -20.289 1.00 108.19 ? 59  LYS   A O    1 
ATOM   452  C  CB   . LYS   A 1 59  ? -26.288 -11.223 -21.412 1.00 99.11  ? 59  LYS   A CB   1 
ATOM   453  C  CG   . LYS   A 1 59  ? -25.086 -12.095 -21.802 1.00 101.82 ? 59  LYS   A CG   1 
ATOM   454  C  CD   . LYS   A 1 59  ? -24.604 -11.783 -23.209 1.00 112.01 ? 59  LYS   A CD   1 
ATOM   455  C  CE   . LYS   A 1 59  ? -23.356 -12.595 -23.585 1.00 128.83 ? 59  LYS   A CE   1 
ATOM   456  N  NZ   . LYS   A 1 59  ? -23.609 -14.066 -23.724 1.00 126.74 ? 59  LYS   A NZ   1 
ATOM   457  N  N    . ARG   A 1 60  ? -28.579 -10.667 -18.485 1.00 97.82  ? 60  ARG   A N    1 
ATOM   458  C  CA   . ARG   A 1 60  ? -29.466 -9.663  -17.899 1.00 92.42  ? 60  ARG   A CA   1 
ATOM   459  C  C    . ARG   A 1 60  ? -29.058 -9.401  -16.462 1.00 91.21  ? 60  ARG   A C    1 
ATOM   460  O  O    . ARG   A 1 60  ? -29.014 -10.321 -15.632 1.00 92.28  ? 60  ARG   A O    1 
ATOM   461  C  CB   . ARG   A 1 60  ? -30.964 -10.021 -17.909 1.00 96.78  ? 60  ARG   A CB   1 
ATOM   462  C  CG   . ARG   A 1 60  ? -31.487 -10.196 -19.272 1.00 98.86  ? 60  ARG   A CG   1 
ATOM   463  C  CD   . ARG   A 1 60  ? -32.971 -10.422 -19.417 1.00 109.32 ? 60  ARG   A CD   1 
ATOM   464  N  NE   . ARG   A 1 60  ? -33.771 -9.226  -19.191 1.00 117.91 ? 60  ARG   A NE   1 
ATOM   465  C  CZ   . ARG   A 1 60  ? -35.101 -9.214  -19.115 1.00 127.99 ? 60  ARG   A CZ   1 
ATOM   466  N  NH1  . ARG   A 1 60  ? -35.735 -8.058  -18.919 1.00 124.72 ? 60  ARG   A NH1  1 
ATOM   467  N  NH2  . ARG   A 1 60  ? -35.802 -10.344 -19.260 1.00 126.54 ? 60  ARG   A NH2  1 
ATOM   468  N  N    . LEU   A 1 61  ? -28.765 -8.138  -16.201 1.00 87.88  ? 61  LEU   A N    1 
ATOM   469  C  CA   . LEU   A 1 61  ? -28.595 -7.571  -14.877 1.00 85.81  ? 61  LEU   A CA   1 
ATOM   470  C  C    . LEU   A 1 61  ? -29.934 -7.141  -14.313 1.00 85.06  ? 61  LEU   A C    1 
ATOM   471  O  O    . LEU   A 1 61  ? -30.700 -6.453  -14.988 1.00 91.20  ? 61  LEU   A O    1 
ATOM   472  C  CB   . LEU   A 1 61  ? -27.680 -6.359  -14.959 1.00 82.44  ? 61  LEU   A CB   1 
ATOM   473  C  CG   . LEU   A 1 61  ? -27.463 -5.709  -13.615 1.00 81.35  ? 61  LEU   A CG   1 
ATOM   474  C  CD1  . LEU   A 1 61  ? -26.783 -6.709  -12.716 1.00 81.86  ? 61  LEU   A CD1  1 
ATOM   475  C  CD2  . LEU   A 1 61  ? -26.615 -4.493  -13.810 1.00 85.61  ? 61  LEU   A CD2  1 
ATOM   476  N  N    . SER   A 1 62  ? -30.188 -7.469  -13.059 1.00 80.08  ? 62  SER   A N    1 
ATOM   477  C  CA   . SER   A 1 62  ? -31.513 -7.192  -12.535 1.00 85.13  ? 62  SER   A CA   1 
ATOM   478  C  C    . SER   A 1 62  ? -31.495 -7.114  -11.013 1.00 81.19  ? 62  SER   A C    1 
ATOM   479  O  O    . SER   A 1 62  ? -30.498 -7.452  -10.368 1.00 82.87  ? 62  SER   A O    1 
ATOM   480  C  CB   . SER   A 1 62  ? -32.465 -8.228  -13.087 1.00 86.99  ? 62  SER   A CB   1 
ATOM   481  O  OG   . SER   A 1 62  ? -32.071 -9.490  -12.610 1.00 93.69  ? 62  SER   A OG   1 
ATOM   482  N  N    . ALA   A 1 63  ? -32.605 -6.632  -10.441 1.00 73.37  ? 63  ALA   A N    1 
ATOM   483  C  CA   . ALA   A 1 63  ? -32.615 -6.222  -9.040  1.00 73.04  ? 63  ALA   A CA   1 
ATOM   484  C  C    . ALA   A 1 63  ? -34.041 -6.036  -8.545  1.00 74.24  ? 63  ALA   A C    1 
ATOM   485  O  O    . ALA   A 1 63  ? -34.915 -5.636  -9.310  1.00 78.71  ? 63  ALA   A O    1 
ATOM   486  C  CB   . ALA   A 1 63  ? -31.834 -4.923  -8.850  1.00 75.48  ? 63  ALA   A CB   1 
ATOM   487  N  N    . VAL   A 1 64  ? -34.270 -6.329  -7.253  1.00 78.94  ? 64  VAL   A N    1 
ATOM   488  C  CA   . VAL   A 1 64  ? -35.573 -6.135  -6.610  1.00 85.01  ? 64  VAL   A CA   1 
ATOM   489  C  C    . VAL   A 1 64  ? -35.380 -5.530  -5.223  1.00 90.19  ? 64  VAL   A C    1 
ATOM   490  O  O    . VAL   A 1 64  ? -34.585 -6.031  -4.414  1.00 91.36  ? 64  VAL   A O    1 
ATOM   491  C  CB   . VAL   A 1 64  ? -36.385 -7.439  -6.468  1.00 80.59  ? 64  VAL   A CB   1 
ATOM   492  C  CG1  . VAL   A 1 64  ? -36.605 -8.018  -7.779  1.00 86.86  ? 64  VAL   A CG1  1 
ATOM   493  C  CG2  . VAL   A 1 64  ? -35.712 -8.445  -5.569  1.00 84.03  ? 64  VAL   A CG2  1 
ATOM   494  N  N    . VAL   A 1 65  ? -36.139 -4.473  -4.940  1.00 87.08  ? 65  VAL   A N    1 
ATOM   495  C  CA   . VAL   A 1 65  ? -36.175 -3.846  -3.629  1.00 86.69  ? 65  VAL   A CA   1 
ATOM   496  C  C    . VAL   A 1 65  ? -37.523 -4.152  -3.023  1.00 90.17  ? 65  VAL   A C    1 
ATOM   497  O  O    . VAL   A 1 65  ? -38.532 -4.160  -3.729  1.00 94.80  ? 65  VAL   A O    1 
ATOM   498  C  CB   . VAL   A 1 65  ? -35.959 -2.329  -3.702  1.00 90.19  ? 65  VAL   A CB   1 
ATOM   499  C  CG1  . VAL   A 1 65  ? -36.138 -1.739  -2.337  1.00 97.89  ? 65  VAL   A CG1  1 
ATOM   500  C  CG2  . VAL   A 1 65  ? -34.583 -2.031  -4.205  1.00 85.67  ? 65  VAL   A CG2  1 
ATOM   501  N  N    . SER   A 1 66  ? -37.549 -4.376  -1.720  1.00 92.71  ? 66  SER   A N    1 
ATOM   502  C  CA   . SER   A 1 66  ? -38.700 -5.047  -1.152  1.00 100.72 ? 66  SER   A CA   1 
ATOM   503  C  C    . SER   A 1 66  ? -38.796 -4.766  0.329   1.00 102.04 ? 66  SER   A C    1 
ATOM   504  O  O    . SER   A 1 66  ? -37.830 -4.950  1.070   1.00 102.65 ? 66  SER   A O    1 
ATOM   505  C  CB   . SER   A 1 66  ? -38.613 -6.555  -1.402  1.00 110.27 ? 66  SER   A CB   1 
ATOM   506  O  OG   . SER   A 1 66  ? -37.385 -7.097  -0.936  1.00 105.89 ? 66  SER   A OG   1 
ATOM   507  N  N    . TYR   A 1 67  ? -39.972 -4.349  0.744   1.00 104.31 ? 67  TYR   A N    1 
ATOM   508  C  CA   . TYR   A 1 67  ? -40.256 -4.126  2.137   1.00 109.19 ? 67  TYR   A CA   1 
ATOM   509  C  C    . TYR   A 1 67  ? -41.219 -5.212  2.591   1.00 120.56 ? 67  TYR   A C    1 
ATOM   510  O  O    . TYR   A 1 67  ? -41.935 -5.779  1.759   1.00 123.89 ? 67  TYR   A O    1 
ATOM   511  C  CB   . TYR   A 1 67  ? -40.893 -2.748  2.344   1.00 108.09 ? 67  TYR   A CB   1 
ATOM   512  C  CG   . TYR   A 1 67  ? -39.902 -1.628  2.194   1.00 103.08 ? 67  TYR   A CG   1 
ATOM   513  C  CD1  . TYR   A 1 67  ? -38.892 -1.444  3.110   1.00 100.32 ? 67  TYR   A CD1  1 
ATOM   514  C  CD2  . TYR   A 1 67  ? -39.974 -0.756  1.110   1.00 105.60 ? 67  TYR   A CD2  1 
ATOM   515  C  CE1  . TYR   A 1 67  ? -37.971 -0.420  2.958   1.00 99.67  ? 67  TYR   A CE1  1 
ATOM   516  C  CE2  . TYR   A 1 67  ? -39.058 0.270   0.950   1.00 103.44 ? 67  TYR   A CE2  1 
ATOM   517  C  CZ   . TYR   A 1 67  ? -38.056 0.431   1.878   1.00 99.26  ? 67  TYR   A CZ   1 
ATOM   518  O  OH   . TYR   A 1 67  ? -37.136 1.443   1.740   1.00 95.28  ? 67  TYR   A OH   1 
ATOM   519  N  N    . PRO   A 1 68  ? -41.249 -5.549  3.881   1.00 125.37 ? 68  PRO   A N    1 
ATOM   520  C  CA   . PRO   A 1 68  ? -42.223 -6.543  4.344   1.00 124.46 ? 68  PRO   A CA   1 
ATOM   521  C  C    . PRO   A 1 68  ? -43.634 -6.046  4.087   1.00 119.85 ? 68  PRO   A C    1 
ATOM   522  O  O    . PRO   A 1 68  ? -43.905 -4.849  4.162   1.00 119.63 ? 68  PRO   A O    1 
ATOM   523  C  CB   . PRO   A 1 68  ? -41.926 -6.659  5.841   1.00 121.88 ? 68  PRO   A CB   1 
ATOM   524  C  CG   . PRO   A 1 68  ? -40.516 -6.191  5.981   1.00 131.68 ? 68  PRO   A CG   1 
ATOM   525  C  CD   . PRO   A 1 68  ? -40.386 -5.081  4.979   1.00 121.57 ? 68  PRO   A CD   1 
ATOM   526  N  N    . ASN   A 1 69  ? -44.524 -6.973  3.742   1.00 123.69 ? 69  ASN   A N    1 
ATOM   527  C  CA   . ASN   A 1 69  ? -45.936 -6.658  3.515   1.00 125.08 ? 69  ASN   A CA   1 
ATOM   528  C  C    . ASN   A 1 69  ? -46.108 -5.490  2.543   1.00 118.79 ? 69  ASN   A C    1 
ATOM   529  O  O    . ASN   A 1 69  ? -46.865 -4.553  2.792   1.00 120.38 ? 69  ASN   A O    1 
ATOM   530  C  CB   . ASN   A 1 69  ? -46.650 -6.352  4.837   1.00 130.71 ? 69  ASN   A CB   1 
ATOM   531  C  CG   . ASN   A 1 69  ? -47.302 -7.579  5.461   1.00 140.17 ? 69  ASN   A CG   1 
ATOM   532  O  OD1  . ASN   A 1 69  ? -47.301 -8.676  4.885   1.00 138.20 ? 69  ASN   A OD1  1 
ATOM   533  N  ND2  . ASN   A 1 69  ? -47.902 -7.385  6.636   1.00 143.60 ? 69  ASN   A ND2  1 
ATOM   534  N  N    . ALA   A 1 70  ? -45.389 -5.540  1.428   1.00 117.52 ? 70  ALA   A N    1 
ATOM   535  C  CA   . ALA   A 1 70  ? -45.505 -4.490  0.424   1.00 117.67 ? 70  ALA   A CA   1 
ATOM   536  C  C    . ALA   A 1 70  ? -44.953 -5.011  -0.891  1.00 116.08 ? 70  ALA   A C    1 
ATOM   537  O  O    . ALA   A 1 70  ? -43.980 -5.770  -0.906  1.00 118.39 ? 70  ALA   A O    1 
ATOM   538  C  CB   . ALA   A 1 70  ? -44.759 -3.216  0.840   1.00 119.36 ? 70  ALA   A CB   1 
ATOM   539  N  N    . ASP   A 1 71  ? -45.585 -4.603  -1.991  1.00 111.93 ? 71  ASP   A N    1 
ATOM   540  C  CA   . ASP   A 1 71  ? -45.080 -4.971  -3.306  1.00 113.11 ? 71  ASP   A CA   1 
ATOM   541  C  C    . ASP   A 1 71  ? -43.619 -4.568  -3.440  1.00 110.39 ? 71  ASP   A C    1 
ATOM   542  O  O    . ASP   A 1 71  ? -43.127 -3.671  -2.749  1.00 115.01 ? 71  ASP   A O    1 
ATOM   543  C  CB   . ASP   A 1 71  ? -45.922 -4.335  -4.424  1.00 119.72 ? 71  ASP   A CB   1 
ATOM   544  C  CG   . ASP   A 1 71  ? -47.299 -5.009  -4.604  1.00 127.55 ? 71  ASP   A CG   1 
ATOM   545  O  OD1  . ASP   A 1 71  ? -47.386 -6.236  -4.352  1.00 131.33 ? 71  ASP   A OD1  1 
ATOM   546  O  OD2  . ASP   A 1 71  ? -48.282 -4.330  -5.008  1.00 121.57 ? 71  ASP   A OD2  1 
ATOM   547  N  N    . SER   A 1 72  ? -42.920 -5.276  -4.313  1.00 104.02 ? 72  SER   A N    1 
ATOM   548  C  CA   . SER   A 1 72  ? -41.490 -5.120  -4.478  1.00 101.46 ? 72  SER   A CA   1 
ATOM   549  C  C    . SER   A 1 72  ? -41.206 -4.534  -5.846  1.00 101.84 ? 72  SER   A C    1 
ATOM   550  O  O    . SER   A 1 72  ? -41.725 -5.014  -6.867  1.00 105.26 ? 72  SER   A O    1 
ATOM   551  C  CB   . SER   A 1 72  ? -40.753 -6.448  -4.270  1.00 106.60 ? 72  SER   A CB   1 
ATOM   552  O  OG   . SER   A 1 72  ? -41.068 -7.430  -5.245  1.00 109.94 ? 72  SER   A OG   1 
ATOM   553  N  N    . ALA   A 1 73  ? -40.407 -3.472  -5.846  1.00 98.23  ? 73  ALA   A N    1 
ATOM   554  C  CA   . ALA   A 1 73  ? -40.030 -2.802  -7.074  1.00 95.05  ? 73  ALA   A CA   1 
ATOM   555  C  C    . ALA   A 1 73  ? -38.833 -3.498  -7.693  1.00 88.31  ? 73  ALA   A C    1 
ATOM   556  O  O    . ALA   A 1 73  ? -37.848 -3.783  -7.006  1.00 87.17  ? 73  ALA   A O    1 
ATOM   557  C  CB   . ALA   A 1 73  ? -39.727 -1.331  -6.813  1.00 98.61  ? 73  ALA   A CB   1 
ATOM   558  N  N    . THR   A 1 74  ? -38.951 -3.785  -9.000  1.00 93.41  ? 74  THR   A N    1 
ATOM   559  C  CA   . THR   A 1 74  ? -38.074 -4.657  -9.782  1.00 90.06  ? 74  THR   A CA   1 
ATOM   560  C  C    . THR   A 1 74  ? -37.582 -3.930  -11.024 1.00 85.63  ? 74  THR   A C    1 
ATOM   561  O  O    . THR   A 1 74  ? -38.241 -3.021  -11.529 1.00 89.09  ? 74  THR   A O    1 
ATOM   562  C  CB   . THR   A 1 74  ? -38.794 -5.897  -10.238 1.00 93.67  ? 74  THR   A CB   1 
ATOM   563  O  OG1  . THR   A 1 74  ? -39.903 -5.497  -11.090 1.00 113.18 ? 74  THR   A OG1  1 
ATOM   564  C  CG2  . THR   A 1 74  ? -39.356 -6.696  -8.996  1.00 92.58  ? 74  THR   A CG2  1 
ATOM   565  N  N    . VAL   A 1 75  ? -36.434 -4.357  -11.541 1.00 84.76  ? 75  VAL   A N    1 
ATOM   566  C  CA   . VAL   A 1 75  ? -35.952 -3.762  -12.769 1.00 88.34  ? 75  VAL   A CA   1 
ATOM   567  C  C    . VAL   A 1 75  ? -34.953 -4.706  -13.438 1.00 90.83  ? 75  VAL   A C    1 
ATOM   568  O  O    . VAL   A 1 75  ? -34.283 -5.490  -12.773 1.00 89.04  ? 75  VAL   A O    1 
ATOM   569  C  CB   . VAL   A 1 75  ? -35.358 -2.351  -12.491 1.00 79.27  ? 75  VAL   A CB   1 
ATOM   570  C  CG1  . VAL   A 1 75  ? -34.194 -2.404  -11.542 1.00 77.36  ? 75  VAL   A CG1  1 
ATOM   571  C  CG2  . VAL   A 1 75  ? -35.060 -1.619  -13.767 1.00 89.46  ? 75  VAL   A CG2  1 
ATOM   572  N  N    . SER   A 1 76  ? -34.899 -4.662  -14.780 1.00 97.63  ? 76  SER   A N    1 
ATOM   573  C  CA   . SER   A 1 76  ? -33.960 -5.470  -15.563 1.00 94.20  ? 76  SER   A CA   1 
ATOM   574  C  C    . SER   A 1 76  ? -33.423 -4.701  -16.758 1.00 97.45  ? 76  SER   A C    1 
ATOM   575  O  O    . SER   A 1 76  ? -34.072 -3.793  -17.285 1.00 103.75 ? 76  SER   A O    1 
ATOM   576  C  CB   . SER   A 1 76  ? -34.564 -6.757  -16.130 1.00 96.23  ? 76  SER   A CB   1 
ATOM   577  O  OG   . SER   A 1 76  ? -35.028 -7.604  -15.117 1.00 100.95 ? 76  SER   A OG   1 
ATOM   578  N  N    . TYR   A 1 77  ? -32.263 -5.142  -17.233 1.00 94.76  ? 77  TYR   A N    1 
ATOM   579  C  CA   . TYR   A 1 77  ? -31.569 -4.492  -18.338 1.00 102.93 ? 77  TYR   A CA   1 
ATOM   580  C  C    . TYR   A 1 77  ? -30.610 -5.505  -18.953 1.00 99.64  ? 77  TYR   A C    1 
ATOM   581  O  O    . TYR   A 1 77  ? -29.775 -6.074  -18.248 1.00 99.00  ? 77  TYR   A O    1 
ATOM   582  C  CB   . TYR   A 1 77  ? -30.816 -3.232  -17.852 1.00 104.56 ? 77  TYR   A CB   1 
ATOM   583  C  CG   . TYR   A 1 77  ? -30.059 -2.458  -18.927 1.00 99.25  ? 77  TYR   A CG   1 
ATOM   584  C  CD1  . TYR   A 1 77  ? -30.585 -2.284  -20.203 1.00 101.59 ? 77  TYR   A CD1  1 
ATOM   585  C  CD2  . TYR   A 1 77  ? -28.774 -1.988  -18.684 1.00 93.93  ? 77  TYR   A CD2  1 
ATOM   586  C  CE1  . TYR   A 1 77  ? -29.875 -1.615  -21.189 1.00 101.46 ? 77  TYR   A CE1  1 
ATOM   587  C  CE2  . TYR   A 1 77  ? -28.058 -1.330  -19.664 1.00 97.20  ? 77  TYR   A CE2  1 
ATOM   588  C  CZ   . TYR   A 1 77  ? -28.605 -1.142  -20.915 1.00 101.10 ? 77  TYR   A CZ   1 
ATOM   589  O  OH   . TYR   A 1 77  ? -27.868 -0.475  -21.883 1.00 101.60 ? 77  TYR   A OH   1 
ATOM   590  N  N    . ASP   A 1 78  ? -30.733 -5.727  -20.260 1.00 104.20 ? 78  ASP   A N    1 
ATOM   591  C  CA   . ASP   A 1 78  ? -29.875 -6.665  -20.982 1.00 105.69 ? 78  ASP   A CA   1 
ATOM   592  C  C    . ASP   A 1 78  ? -28.541 -5.990  -21.273 1.00 101.82 ? 78  ASP   A C    1 
ATOM   593  O  O    . ASP   A 1 78  ? -28.475 -5.071  -22.093 1.00 108.20 ? 78  ASP   A O    1 
ATOM   594  C  CB   . ASP   A 1 78  ? -30.546 -7.128  -22.279 1.00 116.90 ? 78  ASP   A CB   1 
ATOM   595  C  CG   . ASP   A 1 78  ? -31.745 -8.077  -22.037 1.00 127.97 ? 78  ASP   A CG   1 
ATOM   596  O  OD1  . ASP   A 1 78  ? -32.861 -7.573  -21.729 1.00 134.23 ? 78  ASP   A OD1  1 
ATOM   597  O  OD2  . ASP   A 1 78  ? -31.571 -9.322  -22.150 1.00 123.88 ? 78  ASP   A OD2  1 
ATOM   598  N  N    . VAL   A 1 79  ? -27.477 -6.449  -20.618 1.00 99.22  ? 79  VAL   A N    1 
ATOM   599  C  CA   . VAL   A 1 79  ? -26.145 -5.871  -20.765 1.00 94.44  ? 79  VAL   A CA   1 
ATOM   600  C  C    . VAL   A 1 79  ? -25.090 -6.964  -20.605 1.00 95.71  ? 79  VAL   A C    1 
ATOM   601  O  O    . VAL   A 1 79  ? -25.223 -7.868  -19.776 1.00 98.18  ? 79  VAL   A O    1 
ATOM   602  C  CB   . VAL   A 1 79  ? -25.965 -4.702  -19.777 1.00 88.41  ? 79  VAL   A CB   1 
ATOM   603  C  CG1  . VAL   A 1 79  ? -26.158 -5.156  -18.372 1.00 84.55  ? 79  VAL   A CG1  1 
ATOM   604  C  CG2  . VAL   A 1 79  ? -24.581 -4.100  -19.937 1.00 99.07  ? 79  VAL   A CG2  1 
ATOM   605  N  N    . ASP   A 1 80  ? -24.050 -6.908  -21.424 1.00 97.92  ? 80  ASP   A N    1 
ATOM   606  C  CA   . ASP   A 1 80  ? -22.982 -7.899  -21.352 1.00 100.96 ? 80  ASP   A CA   1 
ATOM   607  C  C    . ASP   A 1 80  ? -21.841 -7.233  -20.594 1.00 102.03 ? 80  ASP   A C    1 
ATOM   608  O  O    . ASP   A 1 80  ? -21.087 -6.451  -21.170 1.00 108.30 ? 80  ASP   A O    1 
ATOM   609  C  CB   . ASP   A 1 80  ? -22.532 -8.355  -22.738 1.00 110.91 ? 80  ASP   A CB   1 
ATOM   610  C  CG   . ASP   A 1 80  ? -21.491 -9.480  -22.677 1.00 119.39 ? 80  ASP   A CG   1 
ATOM   611  O  OD1  . ASP   A 1 80  ? -20.782 -9.599  -21.646 1.00 121.08 ? 80  ASP   A OD1  1 
ATOM   612  O  OD2  . ASP   A 1 80  ? -21.375 -10.240 -23.671 1.00 120.31 ? 80  ASP   A OD2  1 
ATOM   613  N  N    . LEU   A 1 81  ? -21.706 -7.558  -19.308 1.00 99.77  ? 81  LEU   A N    1 
ATOM   614  C  CA   . LEU   A 1 81  ? -20.783 -6.871  -18.415 1.00 96.45  ? 81  LEU   A CA   1 
ATOM   615  C  C    . LEU   A 1 81  ? -19.311 -7.118  -18.733 1.00 101.50 ? 81  LEU   A C    1 
ATOM   616  O  O    . LEU   A 1 81  ? -18.474 -6.384  -18.195 1.00 101.04 ? 81  LEU   A O    1 
ATOM   617  C  CB   . LEU   A 1 81  ? -21.046 -7.274  -16.958 1.00 90.37  ? 81  LEU   A CB   1 
ATOM   618  C  CG   . LEU   A 1 81  ? -22.103 -6.544  -16.120 1.00 88.39  ? 81  LEU   A CG   1 
ATOM   619  C  CD1  . LEU   A 1 81  ? -21.682 -5.128  -15.857 1.00 100.10 ? 81  LEU   A CD1  1 
ATOM   620  C  CD2  . LEU   A 1 81  ? -23.437 -6.529  -16.768 1.00 91.13  ? 81  LEU   A CD2  1 
ATOM   621  N  N    . ASP   A 1 82  ? -18.949 -8.124  -19.551 1.00 98.90  ? 82  ASP   A N    1 
ATOM   622  C  CA   . ASP   A 1 82  ? -17.515 -8.312  -19.794 1.00 104.61 ? 82  ASP   A CA   1 
ATOM   623  C  C    . ASP   A 1 82  ? -17.009 -7.357  -20.870 1.00 108.57 ? 82  ASP   A C    1 
ATOM   624  O  O    . ASP   A 1 82  ? -15.800 -7.095  -20.959 1.00 107.17 ? 82  ASP   A O    1 
ATOM   625  C  CB   . ASP   A 1 82  ? -17.189 -9.786  -20.120 1.00 110.13 ? 82  ASP   A CB   1 
ATOM   626  C  CG   . ASP   A 1 82  ? -17.720 -10.281 -21.477 1.00 118.66 ? 82  ASP   A CG   1 
ATOM   627  O  OD1  . ASP   A 1 82  ? -18.330 -9.508  -22.242 1.00 127.21 ? 82  ASP   A OD1  1 
ATOM   628  O  OD2  . ASP   A 1 82  ? -17.564 -11.499 -21.752 1.00 117.19 ? 82  ASP   A OD2  1 
ATOM   629  N  N    . ASN   A 1 83  ? -17.931 -6.853  -21.693 1.00 112.85 ? 83  ASN   A N    1 
ATOM   630  C  CA   . ASN   A 1 83  ? -17.670 -5.687  -22.531 1.00 111.10 ? 83  ASN   A CA   1 
ATOM   631  C  C    . ASN   A 1 83  ? -17.394 -4.461  -21.673 1.00 111.77 ? 83  ASN   A C    1 
ATOM   632  O  O    . ASN   A 1 83  ? -16.402 -3.748  -21.878 1.00 114.15 ? 83  ASN   A O    1 
ATOM   633  C  CB   . ASN   A 1 83  ? -18.876 -5.414  -23.435 1.00 108.71 ? 83  ASN   A CB   1 
ATOM   634  C  CG   . ASN   A 1 83  ? -18.785 -6.117  -24.766 1.00 117.87 ? 83  ASN   A CG   1 
ATOM   635  O  OD1  . ASN   A 1 83  ? -17.691 -6.410  -25.253 1.00 127.87 ? 83  ASN   A OD1  1 
ATOM   636  N  ND2  . ASN   A 1 83  ? -19.937 -6.376  -25.378 1.00 113.51 ? 83  ASN   A ND2  1 
ATOM   637  N  N    . VAL   A 1 84  ? -18.263 -4.224  -20.686 1.00 108.49 ? 84  VAL   A N    1 
ATOM   638  C  CA   . VAL   A 1 84  ? -18.302 -2.979  -19.927 1.00 101.52 ? 84  VAL   A CA   1 
ATOM   639  C  C    . VAL   A 1 84  ? -17.217 -2.943  -18.855 1.00 100.54 ? 84  VAL   A C    1 
ATOM   640  O  O    . VAL   A 1 84  ? -16.547 -1.920  -18.672 1.00 102.39 ? 84  VAL   A O    1 
ATOM   641  C  CB   . VAL   A 1 84  ? -19.705 -2.815  -19.316 1.00 94.84  ? 84  VAL   A CB   1 
ATOM   642  C  CG1  . VAL   A 1 84  ? -19.714 -1.728  -18.257 1.00 88.81  ? 84  VAL   A CG1  1 
ATOM   643  C  CG2  . VAL   A 1 84  ? -20.740 -2.572  -20.415 1.00 101.37 ? 84  VAL   A CG2  1 
ATOM   644  N  N    . LEU   A 1 85  ? -17.024 -4.048  -18.134 1.00 95.45  ? 85  LEU   A N    1 
ATOM   645  C  CA   . LEU   A 1 85  ? -16.215 -4.041  -16.932 1.00 85.48  ? 85  LEU   A CA   1 
ATOM   646  C  C    . LEU   A 1 85  ? -14.847 -4.625  -17.208 1.00 88.78  ? 85  LEU   A C    1 
ATOM   647  O  O    . LEU   A 1 85  ? -14.667 -5.380  -18.168 1.00 92.55  ? 85  LEU   A O    1 
ATOM   648  C  CB   . LEU   A 1 85  ? -16.909 -4.855  -15.852 1.00 80.18  ? 85  LEU   A CB   1 
ATOM   649  C  CG   . LEU   A 1 85  ? -17.751 -3.922  -15.005 1.00 84.20  ? 85  LEU   A CG   1 
ATOM   650  C  CD1  . LEU   A 1 85  ? -18.695 -4.724  -14.201 1.00 83.59  ? 85  LEU   A CD1  1 
ATOM   651  C  CD2  . LEU   A 1 85  ? -16.941 -3.046  -14.096 1.00 89.37  ? 85  LEU   A CD2  1 
ATOM   652  N  N    . PRO   A 1 86  ? -13.844 -4.299  -16.397 1.00 90.34  ? 86  PRO   A N    1 
ATOM   653  C  CA   . PRO   A 1 86  ? -12.560 -5.000  -16.508 1.00 90.65  ? 86  PRO   A CA   1 
ATOM   654  C  C    . PRO   A 1 86  ? -12.674 -6.424  -15.996 1.00 90.54  ? 86  PRO   A C    1 
ATOM   655  O  O    . PRO   A 1 86  ? -13.650 -6.810  -15.356 1.00 94.41  ? 86  PRO   A O    1 
ATOM   656  C  CB   . PRO   A 1 86  ? -11.615 -4.149  -15.656 1.00 93.42  ? 86  PRO   A CB   1 
ATOM   657  C  CG   . PRO   A 1 86  ? -12.497 -3.567  -14.604 1.00 89.72  ? 86  PRO   A CG   1 
ATOM   658  C  CD   . PRO   A 1 86  ? -13.815 -3.289  -15.324 1.00 90.36  ? 86  PRO   A CD   1 
ATOM   659  N  N    . GLU   A 1 87  ? -11.653 -7.222  -16.310 1.00 94.58  ? 87  GLU   A N    1 
ATOM   660  C  CA   . GLU   A 1 87  ? -11.659 -8.616  -15.875 1.00 95.59  ? 87  GLU   A CA   1 
ATOM   661  C  C    . GLU   A 1 87  ? -11.660 -8.723  -14.358 1.00 87.46  ? 87  GLU   A C    1 
ATOM   662  O  O    . GLU   A 1 87  ? -12.093 -9.736  -13.810 1.00 91.74  ? 87  GLU   A O    1 
ATOM   663  C  CB   . GLU   A 1 87  ? -10.451 -9.369  -16.447 1.00 95.54  ? 87  GLU   A CB   1 
ATOM   664  C  CG   . GLU   A 1 87  ? -10.546 -10.885 -16.355 1.00 100.20 ? 87  GLU   A CG   1 
ATOM   665  C  CD   . GLU   A 1 87  ? -9.791  -11.592 -17.474 1.00 117.19 ? 87  GLU   A CD   1 
ATOM   666  O  OE1  . GLU   A 1 87  ? -9.450  -10.891 -18.459 1.00 120.63 ? 87  GLU   A OE1  1 
ATOM   667  O  OE2  . GLU   A 1 87  ? -9.543  -12.833 -17.366 1.00 121.91 ? 87  GLU   A OE2  1 
ATOM   668  N  N    . TRP   A 1 88  ? -11.185 -7.703  -13.662 1.00 84.22  ? 88  TRP   A N    1 
ATOM   669  C  CA   . TRP   A 1 88  ? -11.000 -7.782  -12.224 1.00 78.83  ? 88  TRP   A CA   1 
ATOM   670  C  C    . TRP   A 1 88  ? -11.480 -6.484  -11.610 1.00 79.41  ? 88  TRP   A C    1 
ATOM   671  O  O    . TRP   A 1 88  ? -11.070 -5.404  -12.034 1.00 91.09  ? 88  TRP   A O    1 
ATOM   672  C  CB   . TRP   A 1 88  ? -9.540  -8.046  -11.875 1.00 76.54  ? 88  TRP   A CB   1 
ATOM   673  C  CG   . TRP   A 1 88  ? -9.045  -9.470  -11.972 1.00 85.15  ? 88  TRP   A CG   1 
ATOM   674  C  CD1  . TRP   A 1 88  ? -8.503  -10.070 -13.051 1.00 89.38  ? 88  TRP   A CD1  1 
ATOM   675  C  CD2  . TRP   A 1 88  ? -8.973  -10.424 -10.911 1.00 89.28  ? 88  TRP   A CD2  1 
ATOM   676  N  NE1  . TRP   A 1 88  ? -8.105  -11.344 -12.750 1.00 91.56  ? 88  TRP   A NE1  1 
ATOM   677  C  CE2  . TRP   A 1 88  ? -8.390  -11.588 -11.438 1.00 89.98  ? 88  TRP   A CE2  1 
ATOM   678  C  CE3  . TRP   A 1 88  ? -9.367  -10.411 -9.570  1.00 89.16  ? 88  TRP   A CE3  1 
ATOM   679  C  CZ2  . TRP   A 1 88  ? -8.194  -12.724 -10.681 1.00 98.26  ? 88  TRP   A CZ2  1 
ATOM   680  C  CZ3  . TRP   A 1 88  ? -9.162  -11.531 -8.817  1.00 89.25  ? 88  TRP   A CZ3  1 
ATOM   681  C  CH2  . TRP   A 1 88  ? -8.580  -12.682 -9.372  1.00 93.81  ? 88  TRP   A CH2  1 
ATOM   682  N  N    . VAL   A 1 89  ? -12.374 -6.584  -10.648 1.00 76.52  ? 89  VAL   A N    1 
ATOM   683  C  CA   . VAL   A 1 89  ? -13.086 -5.435  -10.132 1.00 80.66  ? 89  VAL   A CA   1 
ATOM   684  C  C    . VAL   A 1 89  ? -13.040 -5.465  -8.604  1.00 79.16  ? 89  VAL   A C    1 
ATOM   685  O  O    . VAL   A 1 89  ? -12.492 -6.375  -7.997  1.00 77.98  ? 89  VAL   A O    1 
ATOM   686  C  CB   . VAL   A 1 89  ? -14.537 -5.381  -10.651 1.00 80.24  ? 89  VAL   A CB   1 
ATOM   687  C  CG1  . VAL   A 1 89  ? -14.546 -5.462  -12.158 1.00 79.76  ? 89  VAL   A CG1  1 
ATOM   688  C  CG2  . VAL   A 1 89  ? -15.333 -6.517  -10.066 1.00 79.22  ? 89  VAL   A CG2  1 
ATOM   689  N  N    . ARG   A 1 90  ? -13.592 -4.438  -7.982  1.00 80.46  ? 90  ARG   A N    1 
ATOM   690  C  CA   . ARG   A 1 90  ? -13.949 -4.508  -6.577  1.00 77.66  ? 90  ARG   A CA   1 
ATOM   691  C  C    . ARG   A 1 90  ? -15.411 -4.169  -6.511  1.00 80.17  ? 90  ARG   A C    1 
ATOM   692  O  O    . ARG   A 1 90  ? -15.913 -3.388  -7.321  1.00 83.13  ? 90  ARG   A O    1 
ATOM   693  C  CB   . ARG   A 1 90  ? -13.244 -3.528  -5.703  1.00 81.39  ? 90  ARG   A CB   1 
ATOM   694  C  CG   . ARG   A 1 90  ? -11.803 -3.723  -5.604  1.00 87.70  ? 90  ARG   A CG   1 
ATOM   695  C  CD   . ARG   A 1 90  ? -11.296 -2.667  -4.658  1.00 85.04  ? 90  ARG   A CD   1 
ATOM   696  N  NE   . ARG   A 1 90  ? -9.839  -2.703  -4.573  1.00 91.69  ? 90  ARG   A NE   1 
ATOM   697  C  CZ   . ARG   A 1 90  ? -9.072  -3.377  -3.696  1.00 91.39  ? 90  ARG   A CZ   1 
ATOM   698  N  NH1  . ARG   A 1 90  ? -7.760  -3.324  -3.804  1.00 94.19  ? 90  ARG   A NH1  1 
ATOM   699  N  NH2  . ARG   A 1 90  ? -9.527  -4.140  -2.721  1.00 90.18  ? 90  ARG   A NH2  1 
ATOM   700  N  N    . VAL   A 1 91  ? -16.077 -4.741  -5.536  1.00 77.51  ? 91  VAL   A N    1 
ATOM   701  C  CA   . VAL   A 1 91  ? -17.496 -4.537  -5.386  1.00 73.55  ? 91  VAL   A CA   1 
ATOM   702  C  C    . VAL   A 1 91  ? -17.682 -3.736  -4.120  1.00 72.08  ? 91  VAL   A C    1 
ATOM   703  O  O    . VAL   A 1 91  ? -16.783 -3.634  -3.286  1.00 75.31  ? 91  VAL   A O    1 
ATOM   704  C  CB   . VAL   A 1 91  ? -18.250 -5.875  -5.350  1.00 74.78  ? 91  VAL   A CB   1 
ATOM   705  C  CG1  . VAL   A 1 91  ? -17.879 -6.706  -6.571  1.00 75.61  ? 91  VAL   A CG1  1 
ATOM   706  C  CG2  . VAL   A 1 91  ? -17.866 -6.654  -4.117  1.00 74.69  ? 91  VAL   A CG2  1 
ATOM   707  N  N    . GLY   A 1 92  ? -18.844 -3.122  -3.988  1.00 69.83  ? 92  GLY   A N    1 
ATOM   708  C  CA   . GLY   A 1 92  ? -19.075 -2.354  -2.788  1.00 72.62  ? 92  GLY   A CA   1 
ATOM   709  C  C    . GLY   A 1 92  ? -20.335 -1.524  -2.877  1.00 76.04  ? 92  GLY   A C    1 
ATOM   710  O  O    . GLY   A 1 92  ? -21.102 -1.588  -3.843  1.00 76.55  ? 92  GLY   A O    1 
ATOM   711  N  N    . LEU   A 1 93  ? -20.512 -0.734  -1.835  1.00 76.37  ? 93  LEU   A N    1 
ATOM   712  C  CA   . LEU   A 1 93  ? -21.716 0.028   -1.604  1.00 79.41  ? 93  LEU   A CA   1 
ATOM   713  C  C    . LEU   A 1 93  ? -21.363 1.497   -1.523  1.00 81.94  ? 93  LEU   A C    1 
ATOM   714  O  O    . LEU   A 1 93  ? -20.291 1.867   -1.043  1.00 86.24  ? 93  LEU   A O    1 
ATOM   715  C  CB   . LEU   A 1 93  ? -22.373 -0.377  -0.304  1.00 82.94  ? 93  LEU   A CB   1 
ATOM   716  C  CG   . LEU   A 1 93  ? -22.886 -1.804  -0.297  1.00 80.55  ? 93  LEU   A CG   1 
ATOM   717  C  CD1  . LEU   A 1 93  ? -23.420 -2.135  1.089   1.00 78.52  ? 93  LEU   A CD1  1 
ATOM   718  C  CD2  . LEU   A 1 93  ? -23.942 -1.997  -1.388  1.00 81.89  ? 93  LEU   A CD2  1 
ATOM   719  N  N    . SER   A 1 94  ? -22.294 2.333   -1.945  1.00 82.12  ? 94  SER   A N    1 
ATOM   720  C  CA   . SER   A 1 94  ? -22.072 3.763   -1.939  1.00 81.90  ? 94  SER   A CA   1 
ATOM   721  C  C    . SER   A 1 94  ? -23.393 4.450   -1.635  1.00 85.04  ? 94  SER   A C    1 
ATOM   722  O  O    . SER   A 1 94  ? -24.464 3.884   -1.855  1.00 91.29  ? 94  SER   A O    1 
ATOM   723  C  CB   . SER   A 1 94  ? -21.507 4.220   -3.273  1.00 78.43  ? 94  SER   A CB   1 
ATOM   724  O  OG   . SER   A 1 94  ? -21.323 5.609   -3.246  1.00 86.66  ? 94  SER   A OG   1 
ATOM   725  N  N    . ALA   A 1 95  ? -23.312 5.665   -1.112  1.00 83.21  ? 95  ALA   A N    1 
ATOM   726  C  CA   . ALA   A 1 95  ? -24.504 6.436   -0.798  1.00 86.11  ? 95  ALA   A CA   1 
ATOM   727  C  C    . ALA   A 1 95  ? -24.062 7.863   -0.518  1.00 92.20  ? 95  ALA   A C    1 
ATOM   728  O  O    . ALA   A 1 95  ? -22.875 8.128   -0.315  1.00 88.62  ? 95  ALA   A O    1 
ATOM   729  C  CB   . ALA   A 1 95  ? -25.260 5.838   0.385   1.00 87.29  ? 95  ALA   A CB   1 
ATOM   730  N  N    . SER   A 1 96  ? -25.027 8.783   -0.503  1.00 99.35  ? 96  SER   A N    1 
ATOM   731  C  CA   . SER   A 1 96  ? -24.684 10.200  -0.428  1.00 101.51 ? 96  SER   A CA   1 
ATOM   732  C  C    . SER   A 1 96  ? -25.928 11.070  -0.252  1.00 102.20 ? 96  SER   A C    1 
ATOM   733  O  O    . SER   A 1 96  ? -27.028 10.714  -0.680  1.00 96.81  ? 96  SER   A O    1 
ATOM   734  C  CB   . SER   A 1 96  ? -23.900 10.617  -1.672  1.00 102.44 ? 96  SER   A CB   1 
ATOM   735  O  OG   . SER   A 1 96  ? -24.799 10.918  -2.714  1.00 106.24 ? 96  SER   A OG   1 
ATOM   736  N  N    . THR   A 1 97  ? -25.725 12.228  0.392   1.00 107.88 ? 97  THR   A N    1 
ATOM   737  C  CA   . THR   A 1 97  ? -26.748 13.255  0.563   1.00 110.68 ? 97  THR   A CA   1 
ATOM   738  C  C    . THR   A 1 97  ? -26.232 14.573  -0.006  1.00 110.30 ? 97  THR   A C    1 
ATOM   739  O  O    . THR   A 1 97  ? -25.033 14.749  -0.219  1.00 110.01 ? 97  THR   A O    1 
ATOM   740  C  CB   . THR   A 1 97  ? -27.136 13.472  2.032   1.00 106.04 ? 97  THR   A CB   1 
ATOM   741  O  OG1  . THR   A 1 97  ? -26.003 13.953  2.745   1.00 107.99 ? 97  THR   A OG1  1 
ATOM   742  C  CG2  . THR   A 1 97  ? -27.550 12.174  2.664   1.00 106.80 ? 97  THR   A CG2  1 
ATOM   743  N  N    . GLY   A 1 98  ? -27.156 15.499  -0.260  1.00 114.71 ? 98  GLY   A N    1 
ATOM   744  C  CA   . GLY   A 1 98  ? -26.804 16.818  -0.752  1.00 115.24 ? 98  GLY   A CA   1 
ATOM   745  C  C    . GLY   A 1 98  ? -27.347 17.910  0.146   1.00 121.35 ? 98  GLY   A C    1 
ATOM   746  O  O    . GLY   A 1 98  ? -27.151 17.863  1.362   1.00 125.69 ? 98  GLY   A O    1 
ATOM   747  N  N    . LEU   A 1 99  ? -28.004 18.912  -0.444  1.00 127.39 ? 99  LEU   A N    1 
ATOM   748  C  CA   . LEU   A 1 99  ? -28.813 19.859  0.327   1.00 130.81 ? 99  LEU   A CA   1 
ATOM   749  C  C    . LEU   A 1 99  ? -29.830 19.153  1.214   1.00 132.14 ? 99  LEU   A C    1 
ATOM   750  O  O    . LEU   A 1 99  ? -29.925 19.422  2.418   1.00 134.53 ? 99  LEU   A O    1 
ATOM   751  C  CB   . LEU   A 1 99  ? -29.531 20.818  -0.619  1.00 134.49 ? 99  LEU   A CB   1 
ATOM   752  C  CG   . LEU   A 1 99  ? -30.433 21.794  0.116   1.00 129.99 ? 99  LEU   A CG   1 
ATOM   753  C  CD1  . LEU   A 1 99  ? -29.628 22.634  1.061   1.00 144.41 ? 99  LEU   A CD1  1 
ATOM   754  C  CD2  . LEU   A 1 99  ? -31.170 22.654  -0.869  1.00 134.05 ? 99  LEU   A CD2  1 
ATOM   755  N  N    . TYR   A 1 100 ? -30.642 18.293  0.621   1.00 127.04 ? 100 TYR   A N    1 
ATOM   756  C  CA   . TYR   A 1 100 ? -31.514 17.422  1.372   1.00 123.94 ? 100 TYR   A CA   1 
ATOM   757  C  C    . TYR   A 1 100 ? -30.712 16.199  1.776   1.00 121.87 ? 100 TYR   A C    1 
ATOM   758  O  O    . TYR   A 1 100 ? -29.656 15.915  1.209   1.00 121.12 ? 100 TYR   A O    1 
ATOM   759  C  CB   . TYR   A 1 100 ? -32.706 17.043  0.519   1.00 123.89 ? 100 TYR   A CB   1 
ATOM   760  C  CG   . TYR   A 1 100 ? -33.778 18.104  0.445   1.00 131.28 ? 100 TYR   A CG   1 
ATOM   761  C  CD1  . TYR   A 1 100 ? -34.517 18.478  1.559   1.00 134.73 ? 100 TYR   A CD1  1 
ATOM   762  C  CD2  . TYR   A 1 100 ? -34.024 18.767  -0.750  1.00 136.17 ? 100 TYR   A CD2  1 
ATOM   763  C  CE1  . TYR   A 1 100 ? -35.520 19.461  1.463   1.00 140.22 ? 100 TYR   A CE1  1 
ATOM   764  C  CE2  . TYR   A 1 100 ? -35.007 19.754  -0.852  1.00 134.77 ? 100 TYR   A CE2  1 
ATOM   765  C  CZ   . TYR   A 1 100 ? -35.751 20.099  0.247   1.00 136.62 ? 100 TYR   A CZ   1 
ATOM   766  O  OH   . TYR   A 1 100 ? -36.716 21.079  0.110   1.00 132.70 ? 100 TYR   A OH   1 
ATOM   767  N  N    . LYS   A 1 101 ? -31.199 15.480  2.776   1.00 118.13 ? 101 LYS   A N    1 
ATOM   768  C  CA   . LYS   A 1 101 ? -30.334 14.515  3.432   1.00 114.04 ? 101 LYS   A CA   1 
ATOM   769  C  C    . LYS   A 1 101 ? -31.172 13.400  4.039   1.00 116.94 ? 101 LYS   A C    1 
ATOM   770  O  O    . LYS   A 1 101 ? -32.380 13.544  4.245   1.00 120.69 ? 101 LYS   A O    1 
ATOM   771  C  CB   . LYS   A 1 101 ? -29.481 15.221  4.481   1.00 115.54 ? 101 LYS   A CB   1 
ATOM   772  C  CG   . LYS   A 1 101 ? -30.371 15.810  5.533   1.00 122.33 ? 101 LYS   A CG   1 
ATOM   773  C  CD   . LYS   A 1 101 ? -29.662 16.613  6.577   1.00 125.24 ? 101 LYS   A CD   1 
ATOM   774  C  CE   . LYS   A 1 101 ? -30.703 17.094  7.572   1.00 135.50 ? 101 LYS   A CE   1 
ATOM   775  N  NZ   . LYS   A 1 101 ? -31.649 18.060  6.936   1.00 140.72 ? 101 LYS   A NZ   1 
ATOM   776  N  N    . GLU   A 1 102 ? -30.505 12.281  4.327   1.00 115.38 ? 102 GLU   A N    1 
ATOM   777  C  CA   . GLU   A 1 102 ? -31.147 11.065  4.813   1.00 108.15 ? 102 GLU   A CA   1 
ATOM   778  C  C    . GLU   A 1 102 ? -30.100 10.209  5.510   1.00 108.67 ? 102 GLU   A C    1 
ATOM   779  O  O    . GLU   A 1 102 ? -28.897 10.394  5.311   1.00 107.50 ? 102 GLU   A O    1 
ATOM   780  C  CB   . GLU   A 1 102 ? -31.751 10.257  3.666   1.00 114.55 ? 102 GLU   A CB   1 
ATOM   781  C  CG   . GLU   A 1 102 ? -30.665 9.662   2.744   1.00 118.74 ? 102 GLU   A CG   1 
ATOM   782  C  CD   . GLU   A 1 102 ? -31.209 8.883   1.541   1.00 115.50 ? 102 GLU   A CD   1 
ATOM   783  O  OE1  . GLU   A 1 102 ? -32.446 8.836   1.371   1.00 117.61 ? 102 GLU   A OE1  1 
ATOM   784  O  OE2  . GLU   A 1 102 ? -30.396 8.285   0.789   1.00 106.79 ? 102 GLU   A OE2  1 
ATOM   785  N  N    . THR   A 1 103 ? -30.561 9.235   6.296   1.00 110.69 ? 103 THR   A N    1 
ATOM   786  C  CA   . THR   A 1 103 ? -29.659 8.300   6.975   1.00 109.81 ? 103 THR   A CA   1 
ATOM   787  C  C    . THR   A 1 103 ? -29.474 7.069   6.094   1.00 106.13 ? 103 THR   A C    1 
ATOM   788  O  O    . THR   A 1 103 ? -30.428 6.314   5.875   1.00 106.21 ? 103 THR   A O    1 
ATOM   789  C  CB   . THR   A 1 103 ? -30.196 7.898   8.351   1.00 107.24 ? 103 THR   A CB   1 
ATOM   790  O  OG1  . THR   A 1 103 ? -31.208 6.888   8.218   1.00 96.60  ? 103 THR   A OG1  1 
ATOM   791  C  CG2  . THR   A 1 103 ? -30.792 9.099   9.055   1.00 116.11 ? 103 THR   A CG2  1 
ATOM   792  N  N    . ASN   A 1 104 ? -28.249 6.863   5.590   1.00 101.10 ? 104 ASN   A N    1 
ATOM   793  C  CA   . ASN   A 1 104 ? -27.925 5.706   4.744   1.00 96.18  ? 104 ASN   A CA   1 
ATOM   794  C  C    . ASN   A 1 104 ? -27.255 4.649   5.607   1.00 95.55  ? 104 ASN   A C    1 
ATOM   795  O  O    . ASN   A 1 104 ? -26.028 4.553   5.674   1.00 96.91  ? 104 ASN   A O    1 
ATOM   796  C  CB   . ASN   A 1 104 ? -27.053 6.102   3.561   1.00 96.18  ? 104 ASN   A CB   1 
ATOM   797  C  CG   . ASN   A 1 104 ? -27.792 6.986   2.575   1.00 99.77  ? 104 ASN   A CG   1 
ATOM   798  O  OD1  . ASN   A 1 104 ? -27.213 7.863   1.945   1.00 102.21 ? 104 ASN   A OD1  1 
ATOM   799  N  ND2  . ASN   A 1 104 ? -29.088 6.764   2.448   1.00 102.97 ? 104 ASN   A ND2  1 
ATOM   800  N  N    . THR   A 1 105 ? -28.090 3.842   6.253   1.00 93.16  ? 105 THR   A N    1 
ATOM   801  C  CA   . THR   A 1 105 ? -27.666 2.835   7.209   1.00 93.23  ? 105 THR   A CA   1 
ATOM   802  C  C    . THR   A 1 105 ? -27.762 1.470   6.553   1.00 89.47  ? 105 THR   A C    1 
ATOM   803  O  O    . THR   A 1 105 ? -28.831 1.091   6.075   1.00 90.03  ? 105 THR   A O    1 
ATOM   804  C  CB   . THR   A 1 105 ? -28.542 2.862   8.456   1.00 93.33  ? 105 THR   A CB   1 
ATOM   805  O  OG1  . THR   A 1 105 ? -28.457 4.151   9.065   1.00 100.68 ? 105 THR   A OG1  1 
ATOM   806  C  CG2  . THR   A 1 105 ? -28.022 1.859   9.448   1.00 100.82 ? 105 THR   A CG2  1 
ATOM   807  N  N    . ILE   A 1 106 ? -26.654 0.739   6.539   1.00 89.43  ? 106 ILE   A N    1 
ATOM   808  C  CA   . ILE   A 1 106 ? -26.571 -0.581  5.928   1.00 86.67  ? 106 ILE   A CA   1 
ATOM   809  C  C    . ILE   A 1 106 ? -26.585 -1.600  7.062   1.00 88.65  ? 106 ILE   A C    1 
ATOM   810  O  O    . ILE   A 1 106 ? -25.651 -1.654  7.869   1.00 94.49  ? 106 ILE   A O    1 
ATOM   811  C  CB   . ILE   A 1 106 ? -25.307 -0.720  5.067   1.00 89.02  ? 106 ILE   A CB   1 
ATOM   812  C  CG1  . ILE   A 1 106 ? -25.414 0.182   3.827   1.00 86.73  ? 106 ILE   A CG1  1 
ATOM   813  C  CG2  . ILE   A 1 106 ? -25.016 -2.197  4.745   1.00 81.90  ? 106 ILE   A CG2  1 
ATOM   814  C  CD1  . ILE   A 1 106 ? -26.494 -0.205  2.836   1.00 83.92  ? 106 ILE   A CD1  1 
ATOM   815  N  N    . LEU   A 1 107 ? -27.641 -2.404  7.153   1.00 86.03  ? 107 LEU   A N    1 
ATOM   816  C  CA   . LEU   A 1 107 ? -27.719 -3.323  8.280   1.00 82.06  ? 107 LEU   A CA   1 
ATOM   817  C  C    . LEU   A 1 107 ? -26.950 -4.605  8.027   1.00 85.27  ? 107 LEU   A C    1 
ATOM   818  O  O    . LEU   A 1 107 ? -26.418 -5.179  8.979   1.00 90.56  ? 107 LEU   A O    1 
ATOM   819  C  CB   . LEU   A 1 107 ? -29.165 -3.662  8.613   1.00 76.47  ? 107 LEU   A CB   1 
ATOM   820  C  CG   . LEU   A 1 107 ? -29.957 -2.612  9.394   1.00 84.39  ? 107 LEU   A CG   1 
ATOM   821  C  CD1  . LEU   A 1 107 ? -30.333 -1.405  8.568   1.00 84.70  ? 107 LEU   A CD1  1 
ATOM   822  C  CD2  . LEU   A 1 107 ? -31.188 -3.205  10.066  1.00 99.24  ? 107 LEU   A CD2  1 
ATOM   823  N  N    . SER   A 1 108 ? -26.876 -5.050  6.768   1.00 83.61  ? 108 SER   A N    1 
ATOM   824  C  CA   . SER   A 1 108 ? -26.339 -6.350  6.376   1.00 80.87  ? 108 SER   A CA   1 
ATOM   825  C  C    . SER   A 1 108 ? -26.071 -6.335  4.878   1.00 79.76  ? 108 SER   A C    1 
ATOM   826  O  O    . SER   A 1 108 ? -26.780 -5.668  4.126   1.00 87.61  ? 108 SER   A O    1 
ATOM   827  C  CB   . SER   A 1 108 ? -27.303 -7.505  6.717   1.00 92.26  ? 108 SER   A CB   1 
ATOM   828  O  OG   . SER   A 1 108 ? -28.457 -7.579  5.874   1.00 92.79  ? 108 SER   A OG   1 
ATOM   829  N  N    . TRP   A 1 109 ? -25.063 -7.088  4.445   1.00 73.08  ? 109 TRP   A N    1 
ATOM   830  C  CA   . TRP   A 1 109 ? -24.677 -7.106  3.034   1.00 74.38  ? 109 TRP   A CA   1 
ATOM   831  C  C    . TRP   A 1 109 ? -23.896 -8.379  2.728   1.00 78.44  ? 109 TRP   A C    1 
ATOM   832  O  O    . TRP   A 1 109 ? -22.888 -8.642  3.393   1.00 82.17  ? 109 TRP   A O    1 
ATOM   833  C  CB   . TRP   A 1 109 ? -23.835 -5.855  2.677   1.00 75.76  ? 109 TRP   A CB   1 
ATOM   834  C  CG   . TRP   A 1 109 ? -23.192 -5.876  1.286   1.00 76.77  ? 109 TRP   A CG   1 
ATOM   835  C  CD1  . TRP   A 1 109 ? -23.781 -6.263  0.120   1.00 79.15  ? 109 TRP   A CD1  1 
ATOM   836  C  CD2  . TRP   A 1 109 ? -21.845 -5.490  0.936   1.00 74.90  ? 109 TRP   A CD2  1 
ATOM   837  N  NE1  . TRP   A 1 109 ? -22.889 -6.159  -0.930  1.00 75.45  ? 109 TRP   A NE1  1 
ATOM   838  C  CE2  . TRP   A 1 109 ? -21.701 -5.683  -0.457  1.00 73.49  ? 109 TRP   A CE2  1 
ATOM   839  C  CE3  . TRP   A 1 109 ? -20.759 -4.999  1.660   1.00 77.50  ? 109 TRP   A CE3  1 
ATOM   840  C  CZ2  . TRP   A 1 109 ? -20.521 -5.403  -1.136  1.00 77.73  ? 109 TRP   A CZ2  1 
ATOM   841  C  CZ3  . TRP   A 1 109 ? -19.582 -4.716  0.978   1.00 80.14  ? 109 TRP   A CZ3  1 
ATOM   842  C  CH2  . TRP   A 1 109 ? -19.471 -4.921  -0.403  1.00 79.56  ? 109 TRP   A CH2  1 
ATOM   843  N  N    . SER   A 1 110 ? -24.334 -9.145  1.710   1.00 72.91  ? 110 SER   A N    1 
ATOM   844  C  CA   . SER   A 1 110 ? -23.619 -10.337 1.253   1.00 71.84  ? 110 SER   A CA   1 
ATOM   845  C  C    . SER   A 1 110 ? -23.478 -10.344 -0.272  1.00 68.08  ? 110 SER   A C    1 
ATOM   846  O  O    . SER   A 1 110 ? -24.174 -9.617  -0.981  1.00 68.35  ? 110 SER   A O    1 
ATOM   847  C  CB   . SER   A 1 110 ? -24.315 -11.621 1.728   1.00 79.19  ? 110 SER   A CB   1 
ATOM   848  O  OG   . SER   A 1 110 ? -25.595 -11.795 1.145   1.00 86.74  ? 110 SER   A OG   1 
ATOM   849  N  N    . PHE   A 1 111 ? -22.584 -11.204 -0.779  1.00 64.21  ? 111 PHE   A N    1 
ATOM   850  C  CA   . PHE   A 1 111 ? -22.231 -11.194 -2.197  1.00 70.04  ? 111 PHE   A CA   1 
ATOM   851  C  C    . PHE   A 1 111 ? -21.618 -12.535 -2.607  1.00 73.81  ? 111 PHE   A C    1 
ATOM   852  O  O    . PHE   A 1 111 ? -20.714 -13.032 -1.933  1.00 76.00  ? 111 PHE   A O    1 
ATOM   853  C  CB   . PHE   A 1 111 ? -21.237 -10.050 -2.484  1.00 67.40  ? 111 PHE   A CB   1 
ATOM   854  C  CG   . PHE   A 1 111 ? -20.644 -10.078 -3.875  1.00 70.86  ? 111 PHE   A CG   1 
ATOM   855  C  CD1  . PHE   A 1 111 ? -19.457 -10.753 -4.139  1.00 75.20  ? 111 PHE   A CD1  1 
ATOM   856  C  CD2  . PHE   A 1 111 ? -21.246 -9.390  -4.913  1.00 71.69  ? 111 PHE   A CD2  1 
ATOM   857  C  CE1  . PHE   A 1 111 ? -18.915 -10.774 -5.428  1.00 75.13  ? 111 PHE   A CE1  1 
ATOM   858  C  CE2  . PHE   A 1 111 ? -20.701 -9.402  -6.185  1.00 69.94  ? 111 PHE   A CE2  1 
ATOM   859  C  CZ   . PHE   A 1 111 ? -19.543 -10.092 -6.444  1.00 69.97  ? 111 PHE   A CZ   1 
ATOM   860  N  N    . THR   A 1 112 ? -22.065 -13.092 -3.737  1.00 73.08  ? 112 THR   A N    1 
ATOM   861  C  CA   . THR   A 1 112 ? -21.517 -14.331 -4.283  1.00 71.56  ? 112 THR   A CA   1 
ATOM   862  C  C    . THR   A 1 112 ? -21.029 -14.099 -5.714  1.00 76.24  ? 112 THR   A C    1 
ATOM   863  O  O    . THR   A 1 112 ? -21.582 -13.272 -6.440  1.00 81.10  ? 112 THR   A O    1 
ATOM   864  C  CB   . THR   A 1 112 ? -22.573 -15.447 -4.280  1.00 80.25  ? 112 THR   A CB   1 
ATOM   865  O  OG1  . THR   A 1 112 ? -23.021 -15.724 -2.944  1.00 83.20  ? 112 THR   A OG1  1 
ATOM   866  C  CG2  . THR   A 1 112 ? -22.014 -16.720 -4.879  1.00 84.17  ? 112 THR   A CG2  1 
ATOM   867  N  N    . SER   A 1 113 ? -19.992 -14.827 -6.122  1.00 76.56  ? 113 SER   A N    1 
ATOM   868  C  CA   . SER   A 1 113 ? -19.402 -14.743 -7.456  1.00 75.04  ? 113 SER   A CA   1 
ATOM   869  C  C    . SER   A 1 113 ? -18.844 -16.082 -7.881  1.00 78.36  ? 113 SER   A C    1 
ATOM   870  O  O    . SER   A 1 113 ? -17.880 -16.551 -7.281  1.00 78.76  ? 113 SER   A O    1 
ATOM   871  C  CB   . SER   A 1 113 ? -18.249 -13.753 -7.524  1.00 78.78  ? 113 SER   A CB   1 
ATOM   872  O  OG   . SER   A 1 113 ? -17.656 -13.841 -8.819  1.00 87.59  ? 113 SER   A OG   1 
ATOM   873  N  N    . LYS   A 1 114 ? -19.374 -16.652 -8.955  1.00 82.08  ? 114 LYS   A N    1 
ATOM   874  C  CA   . LYS   A 1 114 ? -18.916 -17.944 -9.436  1.00 75.73  ? 114 LYS   A CA   1 
ATOM   875  C  C    . LYS   A 1 114 ? -18.479 -17.797 -10.884 1.00 79.13  ? 114 LYS   A C    1 
ATOM   876  O  O    . LYS   A 1 114 ? -19.079 -17.025 -11.633 1.00 81.21  ? 114 LYS   A O    1 
ATOM   877  C  CB   . LYS   A 1 114 ? -20.029 -18.962 -9.313  1.00 88.07  ? 114 LYS   A CB   1 
ATOM   878  C  CG   . LYS   A 1 114 ? -20.467 -19.290 -7.874  1.00 87.05  ? 114 LYS   A CG   1 
ATOM   879  C  CD   . LYS   A 1 114 ? -21.574 -20.329 -7.912  1.00 99.95  ? 114 LYS   A CD   1 
ATOM   880  C  CE   . LYS   A 1 114 ? -22.092 -20.719 -6.555  1.00 105.24 ? 114 LYS   A CE   1 
ATOM   881  N  NZ   . LYS   A 1 114 ? -23.151 -21.780 -6.740  1.00 125.27 ? 114 LYS   A NZ   1 
ATOM   882  N  N    . LEU   A 1 115 ? -17.427 -18.518 -11.271 1.00 88.00  ? 115 LEU   A N    1 
ATOM   883  C  CA   . LEU   A 1 115 ? -16.972 -18.620 -12.667 1.00 92.16  ? 115 LEU   A CA   1 
ATOM   884  C  C    . LEU   A 1 115 ? -16.986 -20.076 -13.113 1.00 98.44  ? 115 LEU   A C    1 
ATOM   885  O  O    . LEU   A 1 115 ? -15.933 -20.620 -13.473 1.00 103.45 ? 115 LEU   A O    1 
ATOM   886  C  CB   . LEU   A 1 115 ? -15.599 -18.050 -12.865 1.00 86.14  ? 115 LEU   A CB   1 
ATOM   887  C  CG   . LEU   A 1 115 ? -15.446 -16.562 -12.642 1.00 89.17  ? 115 LEU   A CG   1 
ATOM   888  C  CD1  . LEU   A 1 115 ? -13.970 -16.188 -12.800 1.00 95.47  ? 115 LEU   A CD1  1 
ATOM   889  C  CD2  . LEU   A 1 115 ? -16.349 -15.788 -13.592 1.00 85.15  ? 115 LEU   A CD2  1 
ATOM   890  N  N    . LYS   A 1 116 ? -18.172 -20.684 -13.111 1.00 102.35 ? 116 LYS   A N    1 
ATOM   891  C  CA   . LYS   A 1 116 ? -18.311 -22.064 -13.543 1.00 114.21 ? 116 LYS   A CA   1 
ATOM   892  C  C    . LYS   A 1 116 ? -17.694 -22.195 -14.930 1.00 117.59 ? 116 LYS   A C    1 
ATOM   893  O  O    . LYS   A 1 116 ? -17.776 -21.276 -15.742 1.00 117.62 ? 116 LYS   A O    1 
ATOM   894  C  CB   . LYS   A 1 116 ? -19.795 -22.472 -13.554 1.00 116.21 ? 116 LYS   A CB   1 
ATOM   895  C  CG   . LYS   A 1 116 ? -20.581 -22.258 -12.241 1.00 128.37 ? 116 LYS   A CG   1 
ATOM   896  C  CD   . LYS   A 1 116 ? -21.369 -23.470 -11.747 1.00 124.43 ? 116 LYS   A CD   1 
ATOM   897  C  CE   . LYS   A 1 116 ? -22.114 -23.074 -10.487 1.00 125.70 ? 116 LYS   A CE   1 
ATOM   898  N  NZ   . LYS   A 1 116 ? -22.901 -24.154 -9.857  1.00 132.69 ? 116 LYS   A NZ   1 
ATOM   899  N  N    . SER   A 1 117 ? -17.083 -23.351 -15.193 1.00 130.40 ? 117 SER   A N    1 
ATOM   900  C  CA   . SER   A 1 117 ? -16.427 -23.588 -16.504 1.00 136.73 ? 117 SER   A CA   1 
ATOM   901  C  C    . SER   A 1 117 ? -16.939 -24.874 -17.157 1.00 156.93 ? 117 SER   A C    1 
ATOM   902  O  O    . SER   A 1 117 ? -17.836 -25.522 -16.595 1.00 157.39 ? 117 SER   A O    1 
ATOM   903  C  CB   . SER   A 1 117 ? -14.934 -23.601 -16.376 1.00 137.87 ? 117 SER   A CB   1 
ATOM   904  O  OG   . SER   A 1 117 ? -14.330 -23.654 -17.657 1.00 136.66 ? 117 SER   A OG   1 
ATOM   905  N  N    . ASN   A 1 118 ? -16.314 -25.234 -18.279 1.00 166.38 ? 118 ASN   A N    1 
ATOM   906  C  CA   . ASN   A 1 118 ? -16.667 -26.389 -19.148 1.00 172.97 ? 118 ASN   A CA   1 
ATOM   907  C  C    . ASN   A 1 118 ? -16.534 -27.731 -18.419 1.00 186.10 ? 118 ASN   A C    1 
ATOM   908  O  O    . ASN   A 1 118 ? -17.362 -28.619 -18.684 1.00 188.98 ? 118 ASN   A O    1 
ATOM   909  C  CB   . ASN   A 1 118 ? -15.806 -26.381 -20.410 1.00 165.43 ? 118 ASN   A CB   1 
ATOM   910  C  CG   . ASN   A 1 118 ? -14.525 -25.601 -20.214 1.00 161.47 ? 118 ASN   A CG   1 
ATOM   911  O  OD1  . ASN   A 1 118 ? -13.915 -25.665 -19.150 1.00 168.99 ? 118 ASN   A OD1  1 
ATOM   912  N  ND2  . ASN   A 1 118 ? -14.116 -24.856 -21.227 1.00 149.79 ? 118 ASN   A ND2  1 
ATOM   913  N  N    . SER   A 1 119 ? -15.546 -27.864 -17.528 1.00 193.70 ? 119 SER   A N    1 
ATOM   914  C  CA   . SER   A 1 119 ? -15.231 -29.147 -16.836 1.00 200.28 ? 119 SER   A CA   1 
ATOM   915  C  C    . SER   A 1 119 ? -16.206 -29.492 -15.696 1.00 212.10 ? 119 SER   A C    1 
ATOM   916  O  O    . SER   A 1 119 ? -17.140 -28.707 -15.428 1.00 228.14 ? 119 SER   A O    1 
ATOM   917  C  CB   . SER   A 1 119 ? -13.798 -29.171 -16.389 1.00 198.25 ? 119 SER   A CB   1 
ATOM   918  O  OG   . SER   A 1 119 ? -12.985 -28.459 -17.307 1.00 199.96 ? 119 SER   A OG   1 
ATOM   919  N  N    . THR   A 1 120 ? -15.959 -30.618 -15.011 1.00 221.19 ? 120 THR   A N    1 
ATOM   920  C  CA   . THR   A 1 120 ? -16.882 -31.125 -13.959 1.00 209.42 ? 120 THR   A CA   1 
ATOM   921  C  C    . THR   A 1 120 ? -16.722 -30.298 -12.685 1.00 208.43 ? 120 THR   A C    1 
ATOM   922  O  O    . THR   A 1 120 ? -16.041 -30.754 -11.751 1.00 207.78 ? 120 THR   A O    1 
ATOM   923  C  CB   . THR   A 1 120 ? -16.554 -32.575 -13.584 1.00 206.79 ? 120 THR   A CB   1 
ATOM   924  O  OG1  . THR   A 1 120 ? -17.200 -32.869 -12.344 1.00 189.25 ? 120 THR   A OG1  1 
ATOM   925  C  CG2  . THR   A 1 120 ? -15.068 -32.813 -13.440 1.00 208.58 ? 120 THR   A CG2  1 
ATOM   926  N  N    . HIS   A 1 121 ? -17.354 -29.124 -12.683 1.00 207.35 ? 121 HIS   A N    1 
ATOM   927  C  CA   . HIS   A 1 121 ? -17.346 -28.166 -11.548 1.00 196.88 ? 121 HIS   A CA   1 
ATOM   928  C  C    . HIS   A 1 121 ? -15.927 -27.723 -11.176 1.00 203.37 ? 121 HIS   A C    1 
ATOM   929  O  O    . HIS   A 1 121 ? -15.664 -27.558 -9.968  1.00 200.22 ? 121 HIS   A O    1 
ATOM   930  C  CB   . HIS   A 1 121 ? -18.204 -28.662 -10.380 1.00 184.03 ? 121 HIS   A CB   1 
ATOM   931  C  CG   . HIS   A 1 121 ? -19.539 -28.005 -10.378 1.00 167.10 ? 121 HIS   A CG   1 
ATOM   932  N  ND1  . HIS   A 1 121 ? -20.441 -28.188 -11.403 1.00 156.13 ? 121 HIS   A ND1  1 
ATOM   933  C  CD2  . HIS   A 1 121 ? -20.106 -27.135 -9.518  1.00 151.51 ? 121 HIS   A CD2  1 
ATOM   934  C  CE1  . HIS   A 1 121 ? -21.520 -27.477 -11.162 1.00 139.74 ? 121 HIS   A CE1  1 
ATOM   935  N  NE2  . HIS   A 1 121 ? -21.339 -26.823 -10.013 1.00 139.44 ? 121 HIS   A NE2  1 
ATOM   936  N  N    . GLU   A 1 122 ? -15.053 -27.564 -12.176 1.00 195.10 ? 122 GLU   A N    1 
ATOM   937  C  CA   . GLU   A 1 122 ? -13.693 -27.000 -11.962 1.00 176.85 ? 122 GLU   A CA   1 
ATOM   938  C  C    . GLU   A 1 122 ? -13.848 -25.485 -12.125 1.00 157.68 ? 122 GLU   A C    1 
ATOM   939  O  O    . GLU   A 1 122 ? -13.415 -24.947 -13.157 1.00 144.06 ? 122 GLU   A O    1 
ATOM   940  C  CB   . GLU   A 1 122 ? -12.695 -27.609 -12.944 1.00 178.59 ? 122 GLU   A CB   1 
ATOM   941  C  CG   . GLU   A 1 122 ? -12.871 -29.106 -13.124 1.00 189.27 ? 122 GLU   A CG   1 
ATOM   942  C  CD   . GLU   A 1 122 ? -12.888 -29.938 -11.853 1.00 184.79 ? 122 GLU   A CD   1 
ATOM   943  O  OE1  . GLU   A 1 122 ? -13.198 -29.380 -10.785 1.00 181.22 ? 122 GLU   A OE1  1 
ATOM   944  O  OE2  . GLU   A 1 122 ? -12.591 -31.146 -11.936 1.00 184.56 ? 122 GLU   A OE2  1 
ATOM   945  N  N    . THR   A 1 123 ? -14.448 -24.846 -11.119 1.00 154.37 ? 123 THR   A N    1 
ATOM   946  C  CA   . THR   A 1 123 ? -14.802 -23.410 -11.151 1.00 129.59 ? 123 THR   A CA   1 
ATOM   947  C  C    . THR   A 1 123 ? -13.932 -22.616 -10.180 1.00 122.51 ? 123 THR   A C    1 
ATOM   948  O  O    . THR   A 1 123 ? -13.091 -23.222 -9.518  1.00 124.74 ? 123 THR   A O    1 
ATOM   949  C  CB   . THR   A 1 123 ? -16.262 -23.270 -10.718 1.00 123.66 ? 123 THR   A CB   1 
ATOM   950  O  OG1  . THR   A 1 123 ? -16.280 -23.438 -9.304  1.00 121.12 ? 123 THR   A OG1  1 
ATOM   951  C  CG2  . THR   A 1 123 ? -17.138 -24.346 -11.314 1.00 141.91 ? 123 THR   A CG2  1 
ATOM   952  N  N    . ASN   A 1 124 ? -14.140 -21.299 -10.144 1.00 110.55 ? 124 ASN   A N    1 
ATOM   953  C  CA   . ASN   A 1 124 ? -13.444 -20.366 -9.254  1.00 93.95  ? 124 ASN   A CA   1 
ATOM   954  C  C    . ASN   A 1 124 ? -14.453 -19.453 -8.583  1.00 77.77  ? 124 ASN   A C    1 
ATOM   955  O  O    . ASN   A 1 124 ? -15.277 -18.850 -9.262  1.00 85.49  ? 124 ASN   A O    1 
ATOM   956  C  CB   . ASN   A 1 124 ? -12.468 -19.535 -10.056 1.00 97.74  ? 124 ASN   A CB   1 
ATOM   957  C  CG   . ASN   A 1 124 ? -11.423 -20.386 -10.655 1.00 113.38 ? 124 ASN   A CG   1 
ATOM   958  O  OD1  . ASN   A 1 124 ? -11.385 -20.581 -11.872 1.00 127.22 ? 124 ASN   A OD1  1 
ATOM   959  N  ND2  . ASN   A 1 124 ? -10.598 -20.973 -9.810  1.00 109.00 ? 124 ASN   A ND2  1 
ATOM   960  N  N    . ALA   A 1 125 ? -14.387 -19.319 -7.267  1.00 69.61  ? 125 ALA   A N    1 
ATOM   961  C  CA   . ALA   A 1 125 ? -15.504 -18.694 -6.578  1.00 67.18  ? 125 ALA   A CA   1 
ATOM   962  C  C    . ALA   A 1 125 ? -15.076 -17.912 -5.332  1.00 71.94  ? 125 ALA   A C    1 
ATOM   963  O  O    . ALA   A 1 125 ? -13.946 -18.033 -4.840  1.00 67.85  ? 125 ALA   A O    1 
ATOM   964  C  CB   . ALA   A 1 125 ? -16.534 -19.737 -6.219  1.00 74.98  ? 125 ALA   A CB   1 
ATOM   965  N  N    . LEU   A 1 126 ? -16.028 -17.099 -4.835  1.00 67.39  ? 126 LEU   A N    1 
ATOM   966  C  CA   . LEU   A 1 126 ? -15.883 -16.140 -3.736  1.00 67.56  ? 126 LEU   A CA   1 
ATOM   967  C  C    . LEU   A 1 126 ? -17.257 -15.712 -3.227  1.00 73.63  ? 126 LEU   A C    1 
ATOM   968  O  O    . LEU   A 1 126 ? -18.126 -15.319 -4.011  1.00 81.27  ? 126 LEU   A O    1 
ATOM   969  C  CB   . LEU   A 1 126 ? -15.067 -14.902 -4.154  1.00 69.49  ? 126 LEU   A CB   1 
ATOM   970  C  CG   . LEU   A 1 126 ? -14.705 -13.757 -3.177  1.00 72.55  ? 126 LEU   A CG   1 
ATOM   971  C  CD1  . LEU   A 1 126 ? -13.397 -13.033 -3.521  1.00 84.75  ? 126 LEU   A CD1  1 
ATOM   972  C  CD2  . LEU   A 1 126 ? -15.797 -12.722 -3.228  1.00 70.13  ? 126 LEU   A CD2  1 
ATOM   973  N  N    . HIS   A 1 127 ? -17.427 -15.765 -1.909  1.00 72.08  ? 127 HIS   A N    1 
ATOM   974  C  CA   . HIS   A 1 127 ? -18.649 -15.385 -1.215  1.00 72.83  ? 127 HIS   A CA   1 
ATOM   975  C  C    . HIS   A 1 127 ? -18.324 -14.750 0.117   1.00 71.72  ? 127 HIS   A C    1 
ATOM   976  O  O    . HIS   A 1 127 ? -17.441 -15.227 0.830   1.00 74.44  ? 127 HIS   A O    1 
ATOM   977  C  CB   . HIS   A 1 127 ? -19.546 -16.586 -0.945  1.00 80.48  ? 127 HIS   A CB   1 
ATOM   978  C  CG   . HIS   A 1 127 ? -20.707 -16.278 -0.055  1.00 77.31  ? 127 HIS   A CG   1 
ATOM   979  N  ND1  . HIS   A 1 127 ? -21.776 -15.506 -0.448  1.00 81.35  ? 127 HIS   A ND1  1 
ATOM   980  C  CD2  . HIS   A 1 127 ? -20.941 -16.611 1.237   1.00 78.39  ? 127 HIS   A CD2  1 
ATOM   981  C  CE1  . HIS   A 1 127 ? -22.632 -15.398 0.555   1.00 84.26  ? 127 HIS   A CE1  1 
ATOM   982  N  NE2  . HIS   A 1 127 ? -22.148 -16.061 1.590   1.00 85.97  ? 127 HIS   A NE2  1 
ATOM   983  N  N    . PHE   A 1 128 ? -19.087 -13.725 0.486   1.00 70.95  ? 128 PHE   A N    1 
ATOM   984  C  CA   . PHE   A 1 128 ? -18.838 -13.097 1.770   1.00 70.62  ? 128 PHE   A CA   1 
ATOM   985  C  C    . PHE   A 1 128 ? -20.132 -12.511 2.310   1.00 71.19  ? 128 PHE   A C    1 
ATOM   986  O  O    . PHE   A 1 128 ? -21.000 -12.099 1.538   1.00 73.27  ? 128 PHE   A O    1 
ATOM   987  C  CB   . PHE   A 1 128 ? -17.708 -12.071 1.629   1.00 69.61  ? 128 PHE   A CB   1 
ATOM   988  C  CG   . PHE   A 1 128 ? -18.048 -10.836 0.826   1.00 70.91  ? 128 PHE   A CG   1 
ATOM   989  C  CD1  . PHE   A 1 128 ? -18.903 -9.857  1.327   1.00 74.04  ? 128 PHE   A CD1  1 
ATOM   990  C  CD2  . PHE   A 1 128 ? -17.486 -10.648 -0.437  1.00 72.84  ? 128 PHE   A CD2  1 
ATOM   991  C  CE1  . PHE   A 1 128 ? -19.177 -8.711  0.585   1.00 78.60  ? 128 PHE   A CE1  1 
ATOM   992  C  CE2  . PHE   A 1 128 ? -17.753 -9.512  -1.194  1.00 71.90  ? 128 PHE   A CE2  1 
ATOM   993  C  CZ   . PHE   A 1 128 ? -18.600 -8.545  -0.694  1.00 79.43  ? 128 PHE   A CZ   1 
ATOM   994  N  N    . MET   A 1 129 ? -20.263 -12.484 3.642   1.00 70.24  ? 129 MET   A N    1 
ATOM   995  C  CA   . MET   A 1 129 ? -21.525 -12.075 4.245   1.00 73.67  ? 129 MET   A CA   1 
ATOM   996  C  C    . MET   A 1 129 ? -21.284 -11.275 5.513   1.00 74.71  ? 129 MET   A C    1 
ATOM   997  O  O    . MET   A 1 129 ? -20.375 -11.572 6.284   1.00 78.24  ? 129 MET   A O    1 
ATOM   998  C  CB   . MET   A 1 129 ? -22.395 -13.280 4.587   1.00 78.01  ? 129 MET   A CB   1 
ATOM   999  C  CG   . MET   A 1 129 ? -23.783 -12.918 5.054   1.00 88.28  ? 129 MET   A CG   1 
ATOM   1000 S  SD   . MET   A 1 129 ? -24.755 -14.399 5.341   1.00 122.71 ? 129 MET   A SD   1 
ATOM   1001 C  CE   . MET   A 1 129 ? -26.308 -13.710 5.890   1.00 139.31 ? 129 MET   A CE   1 
ATOM   1002 N  N    . PHE   A 1 130 ? -22.124 -10.277 5.727   1.00 75.61  ? 130 PHE   A N    1 
ATOM   1003 C  CA   . PHE   A 1 130 ? -22.098 -9.463  6.928   1.00 77.73  ? 130 PHE   A CA   1 
ATOM   1004 C  C    . PHE   A 1 130 ? -23.551 -9.287  7.365   1.00 85.24  ? 130 PHE   A C    1 
ATOM   1005 O  O    . PHE   A 1 130 ? -24.323 -8.657  6.640   1.00 83.05  ? 130 PHE   A O    1 
ATOM   1006 C  CB   . PHE   A 1 130 ? -21.440 -8.107  6.656   1.00 74.99  ? 130 PHE   A CB   1 
ATOM   1007 C  CG   . PHE   A 1 130 ? -20.032 -8.184  6.127   1.00 77.26  ? 130 PHE   A CG   1 
ATOM   1008 C  CD1  . PHE   A 1 130 ? -19.052 -8.950  6.750   1.00 87.44  ? 130 PHE   A CD1  1 
ATOM   1009 C  CD2  . PHE   A 1 130 ? -19.672 -7.444  5.026   1.00 79.76  ? 130 PHE   A CD2  1 
ATOM   1010 C  CE1  . PHE   A 1 130 ? -17.737 -9.001  6.249   1.00 85.77  ? 130 PHE   A CE1  1 
ATOM   1011 C  CE2  . PHE   A 1 130 ? -18.370 -7.494  4.522   1.00 83.90  ? 130 PHE   A CE2  1 
ATOM   1012 C  CZ   . PHE   A 1 130 ? -17.406 -8.270  5.130   1.00 78.84  ? 130 PHE   A CZ   1 
ATOM   1013 N  N    . ASN   A 1 131 ? -23.947 -9.882  8.499   1.00 88.20  ? 131 ASN   A N    1 
ATOM   1014 C  CA   . ASN   A 1 131 ? -25.102 -9.401  9.257   1.00 97.87  ? 131 ASN   A CA   1 
ATOM   1015 C  C    . ASN   A 1 131 ? -24.728 -8.532  10.448  1.00 100.50 ? 131 ASN   A C    1 
ATOM   1016 O  O    . ASN   A 1 131 ? -25.619 -8.028  11.136  1.00 109.59 ? 131 ASN   A O    1 
ATOM   1017 C  CB   . ASN   A 1 131 ? -26.020 -10.533 9.753   1.00 122.62 ? 131 ASN   A CB   1 
ATOM   1018 C  CG   . ASN   A 1 131 ? -26.835 -11.196 8.649   1.00 138.90 ? 131 ASN   A CG   1 
ATOM   1019 O  OD1  . ASN   A 1 131 ? -26.614 -12.354 8.336   1.00 148.26 ? 131 ASN   A OD1  1 
ATOM   1020 N  ND2  . ASN   A 1 131 ? -27.861 -10.489 8.132   1.00 136.51 ? 131 ASN   A ND2  1 
ATOM   1021 N  N    . GLN   A 1 132 ? -23.452 -8.318  10.704  1.00 98.54  ? 132 GLN   A N    1 
ATOM   1022 C  CA   . GLN   A 1 132 ? -23.091 -7.318  11.695  1.00 106.79 ? 132 GLN   A CA   1 
ATOM   1023 C  C    . GLN   A 1 132 ? -21.765 -6.693  11.271  1.00 107.75 ? 132 GLN   A C    1 
ATOM   1024 O  O    . GLN   A 1 132 ? -20.858 -7.392  10.801  1.00 99.20  ? 132 GLN   A O    1 
ATOM   1025 C  CB   . GLN   A 1 132 ? -23.031 -7.952  13.097  1.00 116.58 ? 132 GLN   A CB   1 
ATOM   1026 C  CG   . GLN   A 1 132 ? -21.913 -9.016  13.258  1.00 129.71 ? 132 GLN   A CG   1 
ATOM   1027 C  CD   . GLN   A 1 132 ? -22.202 -10.087 14.324  1.00 135.28 ? 132 GLN   A CD   1 
ATOM   1028 O  OE1  . GLN   A 1 132 ? -22.524 -9.760  15.473  1.00 141.34 ? 132 GLN   A OE1  1 
ATOM   1029 N  NE2  . GLN   A 1 132 ? -22.087 -11.378 13.938  1.00 129.10 ? 132 GLN   A NE2  1 
ATOM   1030 N  N    . PHE   A 1 133 ? -21.663 -5.374  11.395  1.00 104.01 ? 133 PHE   A N    1 
ATOM   1031 C  CA   . PHE   A 1 133 ? -20.434 -4.675  11.044  1.00 101.74 ? 133 PHE   A CA   1 
ATOM   1032 C  C    . PHE   A 1 133 ? -19.658 -4.353  12.310  1.00 109.56 ? 133 PHE   A C    1 
ATOM   1033 O  O    . PHE   A 1 133 ? -20.192 -3.727  13.235  1.00 114.05 ? 133 PHE   A O    1 
ATOM   1034 C  CB   . PHE   A 1 133 ? -20.749 -3.427  10.232  1.00 102.50 ? 133 PHE   A CB   1 
ATOM   1035 C  CG   . PHE   A 1 133 ? -21.181 -3.745  8.847   1.00 95.04  ? 133 PHE   A CG   1 
ATOM   1036 C  CD1  . PHE   A 1 133 ? -20.266 -4.199  7.923   1.00 90.97  ? 133 PHE   A CD1  1 
ATOM   1037 C  CD2  . PHE   A 1 133 ? -22.503 -3.615  8.474   1.00 93.13  ? 133 PHE   A CD2  1 
ATOM   1038 C  CE1  . PHE   A 1 133 ? -20.651 -4.511  6.655   1.00 84.83  ? 133 PHE   A CE1  1 
ATOM   1039 C  CE2  . PHE   A 1 133 ? -22.901 -3.927  7.214   1.00 85.41  ? 133 PHE   A CE2  1 
ATOM   1040 C  CZ   . PHE   A 1 133 ? -21.968 -4.372  6.299   1.00 87.23  ? 133 PHE   A CZ   1 
ATOM   1041 N  N    . SER   A 1 134 ? -18.411 -4.810  12.357  1.00 109.13 ? 134 SER   A N    1 
ATOM   1042 C  CA   . SER   A 1 134 ? -17.652 -4.679  13.580  1.00 114.09 ? 134 SER   A CA   1 
ATOM   1043 C  C    . SER   A 1 134 ? -17.095 -3.273  13.690  1.00 112.92 ? 134 SER   A C    1 
ATOM   1044 O  O    . SER   A 1 134 ? -17.216 -2.445  12.791  1.00 109.88 ? 134 SER   A O    1 
ATOM   1045 C  CB   . SER   A 1 134 ? -16.513 -5.688  13.639  1.00 118.67 ? 134 SER   A CB   1 
ATOM   1046 O  OG   . SER   A 1 134 ? -15.541 -5.370  12.663  1.00 122.11 ? 134 SER   A OG   1 
ATOM   1047 N  N    . LYS   A 1 135 ? -16.434 -3.030  14.804  1.00 118.29 ? 135 LYS   A N    1 
ATOM   1048 C  CA   . LYS   A 1 135 ? -16.087 -1.668  15.162  1.00 119.33 ? 135 LYS   A CA   1 
ATOM   1049 C  C    . LYS   A 1 135 ? -14.932 -1.214  14.282  1.00 112.55 ? 135 LYS   A C    1 
ATOM   1050 O  O    . LYS   A 1 135 ? -14.932 -0.095  13.757  1.00 112.45 ? 135 LYS   A O    1 
ATOM   1051 C  CB   . LYS   A 1 135 ? -15.726 -1.646  16.648  1.00 128.15 ? 135 LYS   A CB   1 
ATOM   1052 C  CG   . LYS   A 1 135 ? -16.929 -1.705  17.640  1.00 129.80 ? 135 LYS   A CG   1 
ATOM   1053 C  CD   . LYS   A 1 135 ? -17.473 -3.151  17.550  1.00 124.73 ? 135 LYS   A CD   1 
ATOM   1054 C  CE   . LYS   A 1 135 ? -16.413 -4.143  18.059  1.00 121.17 ? 135 LYS   A CE   1 
ATOM   1055 N  NZ   . LYS   A 1 135 ? -16.802 -5.567  18.020  1.00 109.93 ? 135 LYS   A NZ   1 
ATOM   1056 N  N    . ASP   A 1 136 ? -13.961 -2.109  14.082  1.00 110.44 ? 136 ASP   A N    1 
ATOM   1057 C  CA   . ASP   A 1 136 ? -12.936 -2.025  13.043  1.00 116.43 ? 136 ASP   A CA   1 
ATOM   1058 C  C    . ASP   A 1 136 ? -13.117 -3.193  12.086  1.00 115.33 ? 136 ASP   A C    1 
ATOM   1059 O  O    . ASP   A 1 136 ? -12.811 -4.344  12.432  1.00 110.68 ? 136 ASP   A O    1 
ATOM   1060 C  CB   . ASP   A 1 136 ? -11.516 -2.043  13.618  1.00 119.20 ? 136 ASP   A CB   1 
ATOM   1061 C  CG   . ASP   A 1 136 ? -10.432 -1.880  12.528  1.00 115.63 ? 136 ASP   A CG   1 
ATOM   1062 O  OD1  . ASP   A 1 136 ? -10.239 -0.759  12.008  1.00 121.77 ? 136 ASP   A OD1  1 
ATOM   1063 O  OD2  . ASP   A 1 136 ? -9.779  -2.895  12.178  1.00 111.50 ? 136 ASP   A OD2  1 
ATOM   1064 N  N    . GLN   A 1 137 ? -13.569 -2.884  10.874  1.00 113.28 ? 137 GLN   A N    1 
ATOM   1065 C  CA   . GLN   A 1 137 ? -13.736 -3.879  9.820   1.00 107.39 ? 137 GLN   A CA   1 
ATOM   1066 C  C    . GLN   A 1 137 ? -12.556 -3.767  8.867   1.00 101.74 ? 137 GLN   A C    1 
ATOM   1067 O  O    . GLN   A 1 137 ? -12.541 -2.906  7.983   1.00 101.64 ? 137 GLN   A O    1 
ATOM   1068 C  CB   . GLN   A 1 137 ? -15.060 -3.685  9.091   1.00 101.82 ? 137 GLN   A CB   1 
ATOM   1069 C  CG   . GLN   A 1 137 ? -15.442 -4.932  8.334   1.00 100.70 ? 137 GLN   A CG   1 
ATOM   1070 C  CD   . GLN   A 1 137 ? -16.000 -5.990  9.275   1.00 107.09 ? 137 GLN   A CD   1 
ATOM   1071 O  OE1  . GLN   A 1 137 ? -16.674 -5.654  10.258  1.00 110.93 ? 137 GLN   A OE1  1 
ATOM   1072 N  NE2  . GLN   A 1 137 ? -15.689 -7.270  9.010   1.00 101.06 ? 137 GLN   A NE2  1 
ATOM   1073 N  N    . LYS   A 1 138 ? -11.565 -4.634  9.038   1.00 94.96  ? 138 LYS   A N    1 
ATOM   1074 C  CA   . LYS   A 1 138 ? -10.371 -4.479  8.232   1.00 94.37  ? 138 LYS   A CA   1 
ATOM   1075 C  C    . LYS   A 1 138 ? -10.405 -5.236  6.918   1.00 93.52  ? 138 LYS   A C    1 
ATOM   1076 O  O    . LYS   A 1 138 ? -9.411  -5.188  6.188   1.00 96.85  ? 138 LYS   A O    1 
ATOM   1077 C  CB   . LYS   A 1 138 ? -9.144  -4.874  9.017   1.00 92.07  ? 138 LYS   A CB   1 
ATOM   1078 C  CG   . LYS   A 1 138 ? -9.172  -6.224  9.542   1.00 97.05  ? 138 LYS   A CG   1 
ATOM   1079 C  CD   . LYS   A 1 138 ? -7.854  -6.394  10.213  1.00 95.58  ? 138 LYS   A CD   1 
ATOM   1080 C  CE   . LYS   A 1 138 ? -7.844  -5.382  11.331  1.00 99.09  ? 138 LYS   A CE   1 
ATOM   1081 N  NZ   . LYS   A 1 138 ? -8.954  -5.716  12.243  1.00 109.33 ? 138 LYS   A NZ   1 
ATOM   1082 N  N    . ASP   A 1 139 ? -11.512 -5.899  6.573   1.00 92.46  ? 139 ASP   A N    1 
ATOM   1083 C  CA   . ASP   A 1 139 ? -11.689 -6.396  5.212   1.00 91.39  ? 139 ASP   A CA   1 
ATOM   1084 C  C    . ASP   A 1 139 ? -12.688 -5.584  4.405   1.00 89.22  ? 139 ASP   A C    1 
ATOM   1085 O  O    . ASP   A 1 139 ? -12.921 -5.905  3.239   1.00 85.59  ? 139 ASP   A O    1 
ATOM   1086 C  CB   . ASP   A 1 139 ? -12.069 -7.886  5.188   1.00 92.64  ? 139 ASP   A CB   1 
ATOM   1087 C  CG   . ASP   A 1 139 ? -13.404 -8.178  5.856   1.00 98.66  ? 139 ASP   A CG   1 
ATOM   1088 O  OD1  . ASP   A 1 139 ? -14.078 -7.224  6.306   1.00 96.98  ? 139 ASP   A OD1  1 
ATOM   1089 O  OD2  . ASP   A 1 139 ? -13.791 -9.378  5.889   1.00 98.68  ? 139 ASP   A OD2  1 
ATOM   1090 N  N    . LEU   A 1 140 ? -13.274 -4.536  4.971   1.00 90.78  ? 140 LEU   A N    1 
ATOM   1091 C  CA   . LEU   A 1 140 ? -13.830 -3.488  4.130   1.00 87.12  ? 140 LEU   A CA   1 
ATOM   1092 C  C    . LEU   A 1 140 ? -12.834 -2.354  3.970   1.00 88.44  ? 140 LEU   A C    1 
ATOM   1093 O  O    . LEU   A 1 140 ? -12.181 -1.932  4.930   1.00 91.38  ? 140 LEU   A O    1 
ATOM   1094 C  CB   . LEU   A 1 140 ? -15.132 -2.888  4.649   1.00 82.64  ? 140 LEU   A CB   1 
ATOM   1095 C  CG   . LEU   A 1 140 ? -16.380 -3.724  4.685   1.00 80.93  ? 140 LEU   A CG   1 
ATOM   1096 C  CD1  . LEU   A 1 140 ? -17.494 -2.890  5.311   1.00 77.48  ? 140 LEU   A CD1  1 
ATOM   1097 C  CD2  . LEU   A 1 140 ? -16.671 -4.161  3.279   1.00 80.31  ? 140 LEU   A CD2  1 
ATOM   1098 N  N    . ILE   A 1 141 ? -12.733 -1.879  2.740   1.00 86.25  ? 141 ILE   A N    1 
ATOM   1099 C  CA   . ILE   A 1 141 ? -12.207 -0.559  2.425   1.00 80.15  ? 141 ILE   A CA   1 
ATOM   1100 C  C    . ILE   A 1 141 ? -13.283 0.482   2.698   1.00 80.75  ? 141 ILE   A C    1 
ATOM   1101 O  O    . ILE   A 1 141 ? -14.367 0.439   2.107   1.00 80.19  ? 141 ILE   A O    1 
ATOM   1102 C  CB   . ILE   A 1 141 ? -11.755 -0.510  0.966   1.00 71.89  ? 141 ILE   A CB   1 
ATOM   1103 C  CG1  . ILE   A 1 141 ? -10.572 -1.469  0.758   1.00 74.52  ? 141 ILE   A CG1  1 
ATOM   1104 C  CG2  . ILE   A 1 141 ? -11.598 0.911   0.523   1.00 74.04  ? 141 ILE   A CG2  1 
ATOM   1105 C  CD1  . ILE   A 1 141 ? -10.217 -1.709  -0.681  1.00 75.47  ? 141 ILE   A CD1  1 
ATOM   1106 N  N    . LEU   A 1 142 ? -12.991 1.415   3.596   1.00 85.10  ? 142 LEU   A N    1 
ATOM   1107 C  CA   . LEU   A 1 142 ? -13.917 2.491   3.922   1.00 90.13  ? 142 LEU   A CA   1 
ATOM   1108 C  C    . LEU   A 1 142 ? -13.495 3.752   3.169   1.00 96.38  ? 142 LEU   A C    1 
ATOM   1109 O  O    . LEU   A 1 142 ? -12.329 4.170   3.231   1.00 95.53  ? 142 LEU   A O    1 
ATOM   1110 C  CB   . LEU   A 1 142 ? -13.955 2.766   5.424   1.00 86.79  ? 142 LEU   A CB   1 
ATOM   1111 C  CG   . LEU   A 1 142 ? -14.886 1.910   6.279   1.00 90.15  ? 142 LEU   A CG   1 
ATOM   1112 C  CD1  . LEU   A 1 142 ? -16.344 2.160   5.992   1.00 92.41  ? 142 LEU   A CD1  1 
ATOM   1113 C  CD2  . LEU   A 1 142 ? -14.542 0.440   6.160   1.00 94.81  ? 142 LEU   A CD2  1 
ATOM   1114 N  N    . GLN   A 1 143 ? -14.437 4.344   2.444   1.00 90.64  ? 143 GLN   A N    1 
ATOM   1115 C  CA   . GLN   A 1 143 ? -14.163 5.549   1.690   1.00 87.40  ? 143 GLN   A CA   1 
ATOM   1116 C  C    . GLN   A 1 143 ? -15.114 6.629   2.142   1.00 89.98  ? 143 GLN   A C    1 
ATOM   1117 O  O    . GLN   A 1 143 ? -16.234 6.343   2.577   1.00 94.44  ? 143 GLN   A O    1 
ATOM   1118 C  CB   . GLN   A 1 143 ? -14.296 5.337   0.189   1.00 87.52  ? 143 GLN   A CB   1 
ATOM   1119 C  CG   . GLN   A 1 143 ? -13.133 4.565   -0.410  1.00 93.29  ? 143 GLN   A CG   1 
ATOM   1120 C  CD   . GLN   A 1 143 ? -13.349 4.224   -1.875  1.00 95.46  ? 143 GLN   A CD   1 
ATOM   1121 O  OE1  . GLN   A 1 143 ? -14.455 4.375   -2.407  1.00 88.47  ? 143 GLN   A OE1  1 
ATOM   1122 N  NE2  . GLN   A 1 143 ? -12.286 3.770   -2.540  1.00 93.48  ? 143 GLN   A NE2  1 
ATOM   1123 N  N    . GLY   A 1 144 ? -14.627 7.863   2.064   1.00 90.74  ? 144 GLY   A N    1 
ATOM   1124 C  CA   . GLY   A 1 144 ? -15.441 9.015   2.405   1.00 94.41  ? 144 GLY   A CA   1 
ATOM   1125 C  C    . GLY   A 1 144 ? -15.853 9.023   3.862   1.00 97.40  ? 144 GLY   A C    1 
ATOM   1126 O  O    . GLY   A 1 144 ? -15.040 8.861   4.781   1.00 100.03 ? 144 GLY   A O    1 
ATOM   1127 N  N    . ASP   A 1 145 ? -17.145 9.221   4.072   1.00 94.59  ? 145 ASP   A N    1 
ATOM   1128 C  CA   . ASP   A 1 145 ? -17.712 9.409   5.394   1.00 100.15 ? 145 ASP   A CA   1 
ATOM   1129 C  C    . ASP   A 1 145 ? -18.078 8.100   6.057   1.00 100.28 ? 145 ASP   A C    1 
ATOM   1130 O  O    . ASP   A 1 145 ? -18.694 8.116   7.127   1.00 105.83 ? 145 ASP   A O    1 
ATOM   1131 C  CB   . ASP   A 1 145 ? -18.981 10.268  5.304   1.00 108.66 ? 145 ASP   A CB   1 
ATOM   1132 C  CG   . ASP   A 1 145 ? -18.706 11.704  4.881   1.00 112.86 ? 145 ASP   A CG   1 
ATOM   1133 O  OD1  . ASP   A 1 145 ? -17.598 12.229  5.150   1.00 119.32 ? 145 ASP   A OD1  1 
ATOM   1134 O  OD2  . ASP   A 1 145 ? -19.623 12.311  4.281   1.00 106.93 ? 145 ASP   A OD2  1 
ATOM   1135 N  N    . ALA   A 1 146 ? -17.760 6.976   5.430   1.00 96.70  ? 146 ALA   A N    1 
ATOM   1136 C  CA   . ALA   A 1 146 ? -18.328 5.711   5.862   1.00 100.20 ? 146 ALA   A CA   1 
ATOM   1137 C  C    . ALA   A 1 146 ? -17.669 5.241   7.163   1.00 104.54 ? 146 ALA   A C    1 
ATOM   1138 O  O    . ALA   A 1 146 ? -16.470 5.448   7.395   1.00 102.29 ? 146 ALA   A O    1 
ATOM   1139 C  CB   . ALA   A 1 146 ? -18.197 4.677   4.744   1.00 92.55  ? 146 ALA   A CB   1 
ATOM   1140 N  N    . THR   A 1 147 ? -18.484 4.642   8.034   1.00 105.52 ? 147 THR   A N    1 
ATOM   1141 C  CA   . THR   A 1 147 ? -18.109 4.314   9.403   1.00 105.48 ? 147 THR   A CA   1 
ATOM   1142 C  C    . THR   A 1 147 ? -18.781 3.007   9.813   1.00 107.25 ? 147 THR   A C    1 
ATOM   1143 O  O    . THR   A 1 147 ? -19.893 2.701   9.371   1.00 103.15 ? 147 THR   A O    1 
ATOM   1144 C  CB   . THR   A 1 147 ? -18.568 5.391   10.388  1.00 107.74 ? 147 THR   A CB   1 
ATOM   1145 O  OG1  . THR   A 1 147 ? -19.999 5.361   10.467  1.00 108.29 ? 147 THR   A OG1  1 
ATOM   1146 C  CG2  . THR   A 1 147 ? -18.150 6.773   9.932   1.00 104.67 ? 147 THR   A CG2  1 
ATOM   1147 N  N    . THR   A 1 148 ? -18.132 2.270   10.711  1.00 108.05 ? 148 THR   A N    1 
ATOM   1148 C  CA   . THR   A 1 148 ? -18.653 1.000   11.195  1.00 107.23 ? 148 THR   A CA   1 
ATOM   1149 C  C    . THR   A 1 148 ? -18.751 1.029   12.717  1.00 108.29 ? 148 THR   A C    1 
ATOM   1150 O  O    . THR   A 1 148 ? -18.220 1.924   13.377  1.00 110.39 ? 148 THR   A O    1 
ATOM   1151 C  CB   . THR   A 1 148 ? -17.755 -0.162  10.748  1.00 108.41 ? 148 THR   A CB   1 
ATOM   1152 O  OG1  . THR   A 1 148 ? -16.457 -0.018  11.331  1.00 115.28 ? 148 THR   A OG1  1 
ATOM   1153 C  CG2  . THR   A 1 148 ? -17.577 -0.152  9.237   1.00 101.39 ? 148 THR   A CG2  1 
ATOM   1154 N  N    . GLY   A 1 149 ? -19.450 0.035   13.274  1.00 109.13 ? 149 GLY   A N    1 
ATOM   1155 C  CA   . GLY   A 1 149 ? -19.411 -0.269  14.696  1.00 117.57 ? 149 GLY   A CA   1 
ATOM   1156 C  C    . GLY   A 1 149 ? -20.593 0.236   15.501  1.00 120.53 ? 149 GLY   A C    1 
ATOM   1157 O  O    . GLY   A 1 149 ? -20.892 -0.329  16.572  1.00 116.77 ? 149 GLY   A O    1 
ATOM   1158 N  N    . THR   A 1 150 ? -21.250 1.297   15.029  1.00 121.98 ? 150 THR   A N    1 
ATOM   1159 C  CA   . THR   A 1 150 ? -22.440 1.857   15.670  1.00 126.65 ? 150 THR   A CA   1 
ATOM   1160 C  C    . THR   A 1 150 ? -23.576 0.860   15.533  1.00 120.93 ? 150 THR   A C    1 
ATOM   1161 O  O    . THR   A 1 150 ? -24.138 0.703   14.446  1.00 120.46 ? 150 THR   A O    1 
ATOM   1162 C  CB   . THR   A 1 150 ? -22.829 3.185   15.027  1.00 130.46 ? 150 THR   A CB   1 
ATOM   1163 O  OG1  . THR   A 1 150 ? -22.713 3.081   13.596  1.00 131.99 ? 150 THR   A OG1  1 
ATOM   1164 C  CG2  . THR   A 1 150 ? -21.948 4.322   15.551  1.00 126.73 ? 150 THR   A CG2  1 
ATOM   1165 N  N    . ASP   A 1 151 ? -23.910 0.172   16.625  1.00 119.71 ? 151 ASP   A N    1 
ATOM   1166 C  CA   . ASP   A 1 151 ? -25.012 -0.779  16.636  1.00 118.51 ? 151 ASP   A CA   1 
ATOM   1167 C  C    . ASP   A 1 151 ? -24.707 -2.006  15.789  1.00 113.18 ? 151 ASP   A C    1 
ATOM   1168 O  O    . ASP   A 1 151 ? -25.619 -2.753  15.433  1.00 112.46 ? 151 ASP   A O    1 
ATOM   1169 C  CB   . ASP   A 1 151 ? -26.304 -0.127  16.115  1.00 121.21 ? 151 ASP   A CB   1 
ATOM   1170 C  CG   . ASP   A 1 151 ? -26.841 0.963   17.020  1.00 128.64 ? 151 ASP   A CG   1 
ATOM   1171 O  OD1  . ASP   A 1 151 ? -26.640 0.879   18.255  1.00 139.86 ? 151 ASP   A OD1  1 
ATOM   1172 O  OD2  . ASP   A 1 151 ? -27.434 1.928   16.469  1.00 122.08 ? 151 ASP   A OD2  1 
ATOM   1173 N  N    . GLY   A 1 152 ? -23.450 -2.209  15.409  1.00 113.04 ? 152 GLY   A N    1 
ATOM   1174 C  CA   . GLY   A 1 152 ? -23.141 -3.254  14.449  1.00 111.66 ? 152 GLY   A CA   1 
ATOM   1175 C  C    . GLY   A 1 152 ? -23.595 -2.969  13.030  1.00 107.62 ? 152 GLY   A C    1 
ATOM   1176 O  O    . GLY   A 1 152 ? -23.787 -3.911  12.247  1.00 103.34 ? 152 GLY   A O    1 
ATOM   1177 N  N    . ASN   A 1 153 ? -23.768 -1.693  12.676  1.00 108.10 ? 153 ASN   A N    1 
ATOM   1178 C  CA   . ASN   A 1 153 ? -24.199 -1.259  11.355  1.00 99.42  ? 153 ASN   A CA   1 
ATOM   1179 C  C    . ASN   A 1 153 ? -23.063 -0.589  10.604  1.00 98.19  ? 153 ASN   A C    1 
ATOM   1180 O  O    . ASN   A 1 153 ? -22.072 -0.140  11.189  1.00 103.12 ? 153 ASN   A O    1 
ATOM   1181 C  CB   . ASN   A 1 153 ? -25.364 -0.277  11.438  1.00 92.29  ? 153 ASN   A CB   1 
ATOM   1182 C  CG   . ASN   A 1 153 ? -26.616 -0.924  11.943  1.00 97.52  ? 153 ASN   A CG   1 
ATOM   1183 O  OD1  . ASN   A 1 153 ? -26.695 -2.145  12.098  1.00 96.55  ? 153 ASN   A OD1  1 
ATOM   1184 N  ND2  . ASN   A 1 153 ? -27.597 -0.107  12.251  1.00 101.30 ? 153 ASN   A ND2  1 
ATOM   1185 N  N    . LEU   A 1 154 ? -23.235 -0.547  9.287   1.00 96.28  ? 154 LEU   A N    1 
ATOM   1186 C  CA   . LEU   A 1 154 ? -22.453 0.287   8.384   1.00 93.31  ? 154 LEU   A CA   1 
ATOM   1187 C  C    . LEU   A 1 154 ? -23.250 1.541   8.061   1.00 98.48  ? 154 LEU   A C    1 
ATOM   1188 O  O    . LEU   A 1 154 ? -24.397 1.449   7.611   1.00 100.31 ? 154 LEU   A O    1 
ATOM   1189 C  CB   . LEU   A 1 154 ? -22.125 -0.442  7.085   1.00 87.04  ? 154 LEU   A CB   1 
ATOM   1190 C  CG   . LEU   A 1 154 ? -21.332 0.443   6.131   1.00 89.39  ? 154 LEU   A CG   1 
ATOM   1191 C  CD1  . LEU   A 1 154 ? -19.999 0.851   6.744   1.00 102.33 ? 154 LEU   A CD1  1 
ATOM   1192 C  CD2  . LEU   A 1 154 ? -21.120 -0.199  4.806   1.00 85.67  ? 154 LEU   A CD2  1 
ATOM   1193 N  N    . GLU   A 1 155 ? -22.647 2.708   8.286   1.00 98.38  ? 155 GLU   A N    1 
ATOM   1194 C  CA   . GLU   A 1 155 ? -23.265 3.989   7.962   1.00 96.32  ? 155 GLU   A CA   1 
ATOM   1195 C  C    . GLU   A 1 155 ? -22.452 4.615   6.838   1.00 103.47 ? 155 GLU   A C    1 
ATOM   1196 O  O    . GLU   A 1 155 ? -21.308 5.029   7.053   1.00 105.85 ? 155 GLU   A O    1 
ATOM   1197 C  CB   . GLU   A 1 155 ? -23.300 4.890   9.186   1.00 103.36 ? 155 GLU   A CB   1 
ATOM   1198 C  CG   . GLU   A 1 155 ? -23.927 4.225   10.385  1.00 111.65 ? 155 GLU   A CG   1 
ATOM   1199 C  CD   . GLU   A 1 155 ? -25.403 4.525   10.506  1.00 116.96 ? 155 GLU   A CD   1 
ATOM   1200 O  OE1  . GLU   A 1 155 ? -25.993 4.990   9.494   1.00 112.97 ? 155 GLU   A OE1  1 
ATOM   1201 O  OE2  . GLU   A 1 155 ? -25.962 4.266   11.606  1.00 120.38 ? 155 GLU   A OE2  1 
ATOM   1202 N  N    . LEU   A 1 156 ? -23.028 4.665   5.635   1.00 100.90 ? 156 LEU   A N    1 
ATOM   1203 C  CA   . LEU   A 1 156 ? -22.277 5.179   4.495   1.00 95.91  ? 156 LEU   A CA   1 
ATOM   1204 C  C    . LEU   A 1 156 ? -22.213 6.699   4.476   1.00 100.62 ? 156 LEU   A C    1 
ATOM   1205 O  O    . LEU   A 1 156 ? -21.239 7.262   3.975   1.00 98.18  ? 156 LEU   A O    1 
ATOM   1206 C  CB   . LEU   A 1 156 ? -22.887 4.663   3.203   1.00 91.08  ? 156 LEU   A CB   1 
ATOM   1207 C  CG   . LEU   A 1 156 ? -22.915 3.156   3.083   1.00 89.82  ? 156 LEU   A CG   1 
ATOM   1208 C  CD1  . LEU   A 1 156 ? -24.030 2.819   2.149   1.00 91.95  ? 156 LEU   A CD1  1 
ATOM   1209 C  CD2  . LEU   A 1 156 ? -21.563 2.641   2.544   1.00 81.23  ? 156 LEU   A CD2  1 
ATOM   1210 N  N    . THR   A 1 157 ? -23.230 7.374   4.998   1.00 104.06 ? 157 THR   A N    1 
ATOM   1211 C  CA   . THR   A 1 157 ? -23.226 8.815   5.164   1.00 103.56 ? 157 THR   A CA   1 
ATOM   1212 C  C    . THR   A 1 157 ? -23.053 9.182   6.627   1.00 111.19 ? 157 THR   A C    1 
ATOM   1213 O  O    . THR   A 1 157 ? -23.338 8.388   7.527   1.00 111.61 ? 157 THR   A O    1 
ATOM   1214 C  CB   . THR   A 1 157 ? -24.515 9.445   4.643   1.00 105.20 ? 157 THR   A CB   1 
ATOM   1215 O  OG1  . THR   A 1 157 ? -25.602 9.075   5.507   1.00 108.30 ? 157 THR   A OG1  1 
ATOM   1216 C  CG2  . THR   A 1 157 ? -24.770 9.038   3.223   1.00 100.14 ? 157 THR   A CG2  1 
ATOM   1217 N  N    . ARG   A 1 158 ? -22.598 10.416  6.843   1.00 119.44 ? 158 ARG   A N    1 
ATOM   1218 C  CA   . ARG   A 1 158 ? -22.332 10.887  8.188   1.00 119.69 ? 158 ARG   A CA   1 
ATOM   1219 C  C    . ARG   A 1 158 ? -23.627 11.155  8.936   1.00 122.04 ? 158 ARG   A C    1 
ATOM   1220 O  O    . ARG   A 1 158 ? -24.573 11.722  8.387   1.00 118.47 ? 158 ARG   A O    1 
ATOM   1221 C  CB   . ARG   A 1 158 ? -21.541 12.179  8.180   1.00 122.31 ? 158 ARG   A CB   1 
ATOM   1222 C  CG   . ARG   A 1 158 ? -21.161 12.444  9.586   1.00 140.64 ? 158 ARG   A CG   1 
ATOM   1223 C  CD   . ARG   A 1 158 ? -20.508 13.739  9.799   1.00 146.83 ? 158 ARG   A CD   1 
ATOM   1224 N  NE   . ARG   A 1 158 ? -19.241 13.924  9.147   1.00 133.79 ? 158 ARG   A NE   1 
ATOM   1225 C  CZ   . ARG   A 1 158 ? -18.653 15.104  9.151   1.00 136.10 ? 158 ARG   A CZ   1 
ATOM   1226 N  NH1  . ARG   A 1 158 ? -17.491 15.264  8.576   1.00 147.51 ? 158 ARG   A NH1  1 
ATOM   1227 N  NH2  . ARG   A 1 158 ? -19.237 16.118  9.776   1.00 141.50 ? 158 ARG   A NH2  1 
ATOM   1228 N  N    . VAL   A 1 159 ? -23.636 10.797  10.220  1.00 128.11 ? 159 VAL   A N    1 
ATOM   1229 C  CA   . VAL   A 1 159 ? -24.770 11.010  11.108  1.00 136.27 ? 159 VAL   A CA   1 
ATOM   1230 C  C    . VAL   A 1 159 ? -24.232 11.577  12.428  1.00 144.42 ? 159 VAL   A C    1 
ATOM   1231 O  O    . VAL   A 1 159 ? -23.051 11.427  12.751  1.00 143.80 ? 159 VAL   A O    1 
ATOM   1232 C  CB   . VAL   A 1 159 ? -25.559 9.689   11.314  1.00 132.29 ? 159 VAL   A CB   1 
ATOM   1233 C  CG1  . VAL   A 1 159 ? -26.710 9.859   12.267  1.00 135.79 ? 159 VAL   A CG1  1 
ATOM   1234 C  CG2  . VAL   A 1 159 ? -26.073 9.145   9.983   1.00 125.93 ? 159 VAL   A CG2  1 
ATOM   1235 N  N    . SER   A 1 160 ? -25.103 12.265  13.184  1.00 141.37 ? 160 SER   A N    1 
ATOM   1236 C  CA   . SER   A 1 160 ? -24.732 12.796  14.496  1.00 142.14 ? 160 SER   A CA   1 
ATOM   1237 C  C    . SER   A 1 160 ? -24.877 11.721  15.585  1.00 151.03 ? 160 SER   A C    1 
ATOM   1238 O  O    . SER   A 1 160 ? -25.362 10.614  15.341  1.00 150.11 ? 160 SER   A O    1 
ATOM   1239 C  CB   . SER   A 1 160 ? -25.578 14.019  14.848  1.00 138.67 ? 160 SER   A CB   1 
ATOM   1240 O  OG   . SER   A 1 160 ? -25.354 15.092  13.953  1.00 142.95 ? 160 SER   A OG   1 
ATOM   1241 N  N    . SER   A 1 161 ? -24.440 12.059  16.810  1.00 158.33 ? 161 SER   A N    1 
ATOM   1242 C  CA   . SER   A 1 161 ? -24.535 11.114  17.931  1.00 156.39 ? 161 SER   A CA   1 
ATOM   1243 C  C    . SER   A 1 161 ? -25.980 10.933  18.386  1.00 150.21 ? 161 SER   A C    1 
ATOM   1244 O  O    . SER   A 1 161 ? -26.378 9.843   18.818  1.00 145.92 ? 161 SER   A O    1 
ATOM   1245 C  CB   . SER   A 1 161 ? -23.662 11.585  19.102  1.00 158.14 ? 161 SER   A CB   1 
ATOM   1246 O  OG   . SER   A 1 161 ? -24.161 12.793  19.666  1.00 165.34 ? 161 SER   A OG   1 
ATOM   1247 N  N    . ASN   A 1 162 ? -26.768 12.003  18.323  1.00 152.35 ? 162 ASN   A N    1 
ATOM   1248 C  CA   . ASN   A 1 162 ? -28.203 11.887  18.534  1.00 153.86 ? 162 ASN   A CA   1 
ATOM   1249 C  C    . ASN   A 1 162 ? -28.864 11.018  17.464  1.00 151.85 ? 162 ASN   A C    1 
ATOM   1250 O  O    . ASN   A 1 162 ? -29.914 10.413  17.718  1.00 152.53 ? 162 ASN   A O    1 
ATOM   1251 C  CB   . ASN   A 1 162 ? -28.809 13.299  18.604  1.00 152.88 ? 162 ASN   A CB   1 
ATOM   1252 C  CG   . ASN   A 1 162 ? -28.293 14.223  17.488  1.00 150.80 ? 162 ASN   A CG   1 
ATOM   1253 O  OD1  . ASN   A 1 162 ? -28.208 13.832  16.330  1.00 150.74 ? 162 ASN   A OD1  1 
ATOM   1254 N  ND2  . ASN   A 1 162 ? -27.951 15.459  17.849  1.00 148.58 ? 162 ASN   A ND2  1 
ATOM   1255 N  N    . GLY   A 1 163 ? -28.252 10.914  16.283  1.00 146.16 ? 163 GLY   A N    1 
ATOM   1256 C  CA   . GLY   A 1 163 ? -28.821 10.187  15.155  1.00 140.55 ? 163 GLY   A CA   1 
ATOM   1257 C  C    . GLY   A 1 163 ? -29.240 11.053  13.971  1.00 148.47 ? 163 GLY   A C    1 
ATOM   1258 O  O    . GLY   A 1 163 ? -29.702 10.500  12.961  1.00 149.08 ? 163 GLY   A O    1 
ATOM   1259 N  N    . SER   A 1 164 ? -29.093 12.382  14.023  1.00 150.53 ? 164 SER   A N    1 
ATOM   1260 C  CA   . SER   A 1 164 ? -29.590 13.245  12.948  1.00 137.73 ? 164 SER   A CA   1 
ATOM   1261 C  C    . SER   A 1 164 ? -28.732 13.076  11.700  1.00 135.50 ? 164 SER   A C    1 
ATOM   1262 O  O    . SER   A 1 164 ? -27.504 13.210  11.775  1.00 136.30 ? 164 SER   A O    1 
ATOM   1263 C  CB   . SER   A 1 164 ? -29.584 14.717  13.377  1.00 140.23 ? 164 SER   A CB   1 
ATOM   1264 O  OG   . SER   A 1 164 ? -30.102 14.906  14.686  1.00 148.03 ? 164 SER   A OG   1 
ATOM   1265 N  N    . PRO   A 1 165 ? -29.329 12.808  10.541  1.00 131.91 ? 165 PRO   A N    1 
ATOM   1266 C  CA   . PRO   A 1 165 ? -28.542 12.749  9.306   1.00 124.59 ? 165 PRO   A CA   1 
ATOM   1267 C  C    . PRO   A 1 165 ? -27.882 14.089  9.043   1.00 121.49 ? 165 PRO   A C    1 
ATOM   1268 O  O    . PRO   A 1 165 ? -28.229 15.101  9.647   1.00 127.63 ? 165 PRO   A O    1 
ATOM   1269 C  CB   . PRO   A 1 165 ? -29.592 12.433  8.242   1.00 123.88 ? 165 PRO   A CB   1 
ATOM   1270 C  CG   . PRO   A 1 165 ? -30.842 13.090  8.787   1.00 127.42 ? 165 PRO   A CG   1 
ATOM   1271 C  CD   . PRO   A 1 165 ? -30.780 12.834  10.275  1.00 130.21 ? 165 PRO   A CD   1 
ATOM   1272 N  N    . GLN   A 1 166 ? -26.909 14.103  8.145   1.00 121.47 ? 166 GLN   A N    1 
ATOM   1273 C  CA   . GLN   A 1 166 ? -26.405 15.386  7.679   1.00 130.40 ? 166 GLN   A CA   1 
ATOM   1274 C  C    . GLN   A 1 166 ? -26.467 15.499  6.167   1.00 120.69 ? 166 GLN   A C    1 
ATOM   1275 O  O    . GLN   A 1 166 ? -26.446 14.503  5.441   1.00 117.58 ? 166 GLN   A O    1 
ATOM   1276 C  CB   . GLN   A 1 166 ? -24.964 15.700  8.127   1.00 132.07 ? 166 GLN   A CB   1 
ATOM   1277 C  CG   . GLN   A 1 166 ? -24.767 15.964  9.612   1.00 131.06 ? 166 GLN   A CG   1 
ATOM   1278 C  CD   . GLN   A 1 166 ? -23.320 16.290  9.909   1.00 139.23 ? 166 GLN   A CD   1 
ATOM   1279 O  OE1  . GLN   A 1 166 ? -22.472 16.252  9.008   1.00 143.46 ? 166 GLN   A OE1  1 
ATOM   1280 N  NE2  . GLN   A 1 166 ? -23.032 16.661  11.154  1.00 142.79 ? 166 GLN   A NE2  1 
ATOM   1281 N  N    . GLY   A 1 167 ? -26.540 16.762  5.719   1.00 116.77 ? 167 GLY   A N    1 
ATOM   1282 C  CA   . GLY   A 1 167 ? -26.455 17.094  4.320   1.00 114.52 ? 167 GLY   A CA   1 
ATOM   1283 C  C    . GLY   A 1 167 ? -25.030 17.084  3.784   1.00 112.11 ? 167 GLY   A C    1 
ATOM   1284 O  O    . GLY   A 1 167 ? -24.050 17.034  4.530   1.00 105.78 ? 167 GLY   A O    1 
ATOM   1285 N  N    . SER   A 1 168 ? -24.962 17.120  2.453   1.00 113.71 ? 168 SER   A N    1 
ATOM   1286 C  CA   . SER   A 1 168 ? -23.732 17.132  1.656   1.00 109.93 ? 168 SER   A CA   1 
ATOM   1287 C  C    . SER   A 1 168 ? -22.705 16.120  2.158   1.00 111.12 ? 168 SER   A C    1 
ATOM   1288 O  O    . SER   A 1 168 ? -21.555 16.447  2.460   1.00 106.49 ? 168 SER   A O    1 
ATOM   1289 C  CB   . SER   A 1 168 ? -23.137 18.526  1.602   1.00 110.99 ? 168 SER   A CB   1 
ATOM   1290 O  OG   . SER   A 1 168 ? -21.772 18.453  1.237   1.00 124.30 ? 168 SER   A OG   1 
ATOM   1291 N  N    . SER   A 1 169 ? -23.123 14.856  2.191   1.00 115.57 ? 169 SER   A N    1 
ATOM   1292 C  CA   . SER   A 1 169 ? -22.316 13.762  2.711   1.00 111.52 ? 169 SER   A CA   1 
ATOM   1293 C  C    . SER   A 1 169 ? -22.129 12.693  1.628   1.00 107.45 ? 169 SER   A C    1 
ATOM   1294 O  O    . SER   A 1 169 ? -23.018 12.477  0.800   1.00 107.05 ? 169 SER   A O    1 
ATOM   1295 C  CB   . SER   A 1 169 ? -22.993 13.201  3.974   1.00 108.82 ? 169 SER   A CB   1 
ATOM   1296 O  OG   . SER   A 1 169 ? -22.405 11.991  4.384   1.00 115.28 ? 169 SER   A OG   1 
ATOM   1297 N  N    . VAL   A 1 170 ? -20.956 12.046  1.602   1.00 103.45 ? 170 VAL   A N    1 
ATOM   1298 C  CA   . VAL   A 1 170 ? -20.637 11.043  0.572   1.00 105.05 ? 170 VAL   A CA   1 
ATOM   1299 C  C    . VAL   A 1 170 ? -19.765 9.919   1.156   1.00 106.34 ? 170 VAL   A C    1 
ATOM   1300 O  O    . VAL   A 1 170 ? -18.665 10.169  1.664   1.00 102.99 ? 170 VAL   A O    1 
ATOM   1301 C  CB   . VAL   A 1 170 ? -19.954 11.680  -0.664  1.00 105.40 ? 170 VAL   A CB   1 
ATOM   1302 C  CG1  . VAL   A 1 170 ? -18.614 12.309  -0.317  1.00 106.96 ? 170 VAL   A CG1  1 
ATOM   1303 C  CG2  . VAL   A 1 170 ? -19.715 10.638  -1.723  1.00 104.75 ? 170 VAL   A CG2  1 
ATOM   1304 N  N    . GLY   A 1 171 ? -20.239 8.662   1.037   1.00 103.00 ? 171 GLY   A N    1 
ATOM   1305 C  CA   . GLY   A 1 171 ? -19.522 7.504   1.572   1.00 93.00  ? 171 GLY   A CA   1 
ATOM   1306 C  C    . GLY   A 1 171 ? -19.569 6.171   0.836   1.00 83.65  ? 171 GLY   A C    1 
ATOM   1307 O  O    . GLY   A 1 171 ? -20.608 5.746   0.332   1.00 85.68  ? 171 GLY   A O    1 
ATOM   1308 N  N    . ARG   A 1 172 ? -18.440 5.478   0.790   1.00 82.30  ? 172 ARG   A N    1 
ATOM   1309 C  CA   . ARG   A 1 172 ? -18.331 4.244   0.034   1.00 79.24  ? 172 ARG   A CA   1 
ATOM   1310 C  C    . ARG   A 1 172 ? -17.627 3.211   0.903   1.00 86.42  ? 172 ARG   A C    1 
ATOM   1311 O  O    . ARG   A 1 172 ? -16.852 3.566   1.798   1.00 88.55  ? 172 ARG   A O    1 
ATOM   1312 C  CB   . ARG   A 1 172 ? -17.554 4.456   -1.274  1.00 77.66  ? 172 ARG   A CB   1 
ATOM   1313 C  CG   . ARG   A 1 172 ? -18.248 5.351   -2.305  1.00 78.12  ? 172 ARG   A CG   1 
ATOM   1314 C  CD   . ARG   A 1 172 ? -17.922 4.984   -3.765  1.00 76.88  ? 172 ARG   A CD   1 
ATOM   1315 N  NE   . ARG   A 1 172 ? -16.529 4.595   -3.999  1.00 80.70  ? 172 ARG   A NE   1 
ATOM   1316 C  CZ   . ARG   A 1 172 ? -15.895 4.674   -5.172  1.00 91.20  ? 172 ARG   A CZ   1 
ATOM   1317 N  NH1  . ARG   A 1 172 ? -16.522 5.143   -6.260  1.00 95.90  ? 172 ARG   A NH1  1 
ATOM   1318 N  NH2  . ARG   A 1 172 ? -14.627 4.266   -5.264  1.00 88.28  ? 172 ARG   A NH2  1 
ATOM   1319 N  N    . ALA   A 1 173 ? -17.918 1.930   0.642   1.00 82.82  ? 173 ALA   A N    1 
ATOM   1320 C  CA   . ALA   A 1 173 ? -17.301 0.807   1.345   1.00 74.02  ? 173 ALA   A CA   1 
ATOM   1321 C  C    . ALA   A 1 173 ? -17.110 -0.319  0.348   1.00 71.16  ? 173 ALA   A C    1 
ATOM   1322 O  O    . ALA   A 1 173 ? -18.075 -0.786  -0.257  1.00 79.91  ? 173 ALA   A O    1 
ATOM   1323 C  CB   . ALA   A 1 173 ? -18.152 0.342   2.531   1.00 74.52  ? 173 ALA   A CB   1 
ATOM   1324 N  N    . LEU   A 1 174 ? -15.881 -0.758  0.171   1.00 69.15  ? 174 LEU   A N    1 
ATOM   1325 C  CA   . LEU   A 1 174 ? -15.556 -1.740  -0.850  1.00 73.71  ? 174 LEU   A CA   1 
ATOM   1326 C  C    . LEU   A 1 174 ? -15.039 -3.019  -0.203  1.00 77.48  ? 174 LEU   A C    1 
ATOM   1327 O  O    . LEU   A 1 174 ? -14.387 -2.986  0.840   1.00 80.77  ? 174 LEU   A O    1 
ATOM   1328 C  CB   . LEU   A 1 174 ? -14.493 -1.191  -1.808  1.00 75.27  ? 174 LEU   A CB   1 
ATOM   1329 C  CG   . LEU   A 1 174 ? -15.016 -0.358  -2.972  1.00 74.47  ? 174 LEU   A CG   1 
ATOM   1330 C  CD1  . LEU   A 1 174 ? -15.326 1.009   -2.450  1.00 75.50  ? 174 LEU   A CD1  1 
ATOM   1331 C  CD2  . LEU   A 1 174 ? -14.031 -0.302  -4.145  1.00 76.62  ? 174 LEU   A CD2  1 
ATOM   1332 N  N    . PHE   A 1 175 ? -15.311 -4.161  -0.813  1.00 81.08  ? 175 PHE   A N    1 
ATOM   1333 C  CA   . PHE   A 1 175 ? -14.688 -5.355  -0.271  1.00 80.83  ? 175 PHE   A CA   1 
ATOM   1334 C  C    . PHE   A 1 175 ? -13.197 -5.263  -0.527  1.00 73.55  ? 175 PHE   A C    1 
ATOM   1335 O  O    . PHE   A 1 175 ? -12.767 -4.799  -1.585  1.00 75.40  ? 175 PHE   A O    1 
ATOM   1336 C  CB   . PHE   A 1 175 ? -15.274 -6.645  -0.866  1.00 77.87  ? 175 PHE   A CB   1 
ATOM   1337 C  CG   . PHE   A 1 175 ? -14.817 -7.891  -0.138  1.00 77.37  ? 175 PHE   A CG   1 
ATOM   1338 C  CD1  . PHE   A 1 175 ? -14.993 -8.016  1.240   1.00 83.84  ? 175 PHE   A CD1  1 
ATOM   1339 C  CD2  . PHE   A 1 175 ? -14.156 -8.903  -0.805  1.00 77.65  ? 175 PHE   A CD2  1 
ATOM   1340 C  CE1  . PHE   A 1 175 ? -14.543 -9.153  1.929   1.00 80.88  ? 175 PHE   A CE1  1 
ATOM   1341 C  CE2  . PHE   A 1 175 ? -13.690 -10.030 -0.127  1.00 76.51  ? 175 PHE   A CE2  1 
ATOM   1342 C  CZ   . PHE   A 1 175 ? -13.884 -10.154 1.240   1.00 77.17  ? 175 PHE   A CZ   1 
ATOM   1343 N  N    . TYR   A 1 176 ? -12.418 -5.664  0.477   1.00 75.48  ? 176 TYR   A N    1 
ATOM   1344 C  CA   . TYR   A 1 176 ? -10.963 -5.625  0.367   1.00 86.92  ? 176 TYR   A CA   1 
ATOM   1345 C  C    . TYR   A 1 176 ? -10.473 -6.499  -0.791  1.00 84.09  ? 176 TYR   A C    1 
ATOM   1346 O  O    . TYR   A 1 176 ? -9.469  -6.179  -1.434  1.00 89.06  ? 176 TYR   A O    1 
ATOM   1347 C  CB   . TYR   A 1 176 ? -10.320 -6.063  1.699   1.00 91.28  ? 176 TYR   A CB   1 
ATOM   1348 C  CG   . TYR   A 1 176 ? -8.868  -5.603  1.971   1.00 95.98  ? 176 TYR   A CG   1 
ATOM   1349 C  CD1  . TYR   A 1 176 ? -7.773  -6.322  1.472   1.00 97.56  ? 176 TYR   A CD1  1 
ATOM   1350 C  CD2  . TYR   A 1 176 ? -8.596  -4.494  2.792   1.00 93.95  ? 176 TYR   A CD2  1 
ATOM   1351 C  CE1  . TYR   A 1 176 ? -6.431  -5.924  1.734   1.00 104.48 ? 176 TYR   A CE1  1 
ATOM   1352 C  CE2  . TYR   A 1 176 ? -7.254  -4.089  3.067   1.00 105.71 ? 176 TYR   A CE2  1 
ATOM   1353 C  CZ   . TYR   A 1 176 ? -6.171  -4.811  2.530   1.00 109.73 ? 176 TYR   A CZ   1 
ATOM   1354 O  OH   . TYR   A 1 176 ? -4.838  -4.455  2.776   1.00 106.07 ? 176 TYR   A OH   1 
ATOM   1355 N  N    . ALA   A 1 177 ? -11.152 -7.551  -1.083  1.00 78.29  ? 177 ALA   A N    1 
ATOM   1356 C  CA   . ALA   A 1 177 ? -10.406 -8.266  -2.106  1.00 79.83  ? 177 ALA   A CA   1 
ATOM   1357 C  C    . ALA   A 1 177 ? -10.896 -7.906  -3.511  1.00 85.09  ? 177 ALA   A C    1 
ATOM   1358 O  O    . ALA   A 1 177 ? -12.031 -7.426  -3.687  1.00 81.07  ? 177 ALA   A O    1 
ATOM   1359 C  CB   . ALA   A 1 177 ? -10.511 -9.778  -1.890  1.00 80.41  ? 177 ALA   A CB   1 
ATOM   1360 N  N    . PRO   A 1 178 ? -10.034 -8.103  -4.520  1.00 90.95  ? 178 PRO   A N    1 
ATOM   1361 C  CA   . PRO   A 1 178 ? -10.482 -7.982  -5.908  1.00 85.56  ? 178 PRO   A CA   1 
ATOM   1362 C  C    . PRO   A 1 178 ? -11.251 -9.211  -6.360  1.00 84.32  ? 178 PRO   A C    1 
ATOM   1363 O  O    . PRO   A 1 178 ? -10.909 -10.360 -6.058  1.00 85.88  ? 178 PRO   A O    1 
ATOM   1364 C  CB   . PRO   A 1 178 ? -9.173  -7.830  -6.686  1.00 79.86  ? 178 PRO   A CB   1 
ATOM   1365 C  CG   . PRO   A 1 178 ? -8.224  -8.571  -5.908  1.00 82.55  ? 178 PRO   A CG   1 
ATOM   1366 C  CD   . PRO   A 1 178 ? -8.573  -8.285  -4.469  1.00 87.91  ? 178 PRO   A CD   1 
ATOM   1367 N  N    . VAL   A 1 179 ? -12.306 -8.942  -7.086  1.00 80.12  ? 179 VAL   A N    1 
ATOM   1368 C  CA   . VAL   A 1 179 ? -13.213 -9.962  -7.550  1.00 78.53  ? 179 VAL   A CA   1 
ATOM   1369 C  C    . VAL   A 1 179 ? -12.827 -10.280 -8.974  1.00 77.01  ? 179 VAL   A C    1 
ATOM   1370 O  O    . VAL   A 1 179 ? -12.547 -9.373  -9.757  1.00 81.54  ? 179 VAL   A O    1 
ATOM   1371 C  CB   . VAL   A 1 179 ? -14.658 -9.464  -7.459  1.00 82.02  ? 179 VAL   A CB   1 
ATOM   1372 C  CG1  . VAL   A 1 179 ? -15.595 -10.565 -7.803  1.00 81.41  ? 179 VAL   A CG1  1 
ATOM   1373 C  CG2  . VAL   A 1 179 ? -14.918 -8.906  -6.055  1.00 80.29  ? 179 VAL   A CG2  1 
ATOM   1374 N  N    . HIS   A 1 180 ? -12.756 -11.556 -9.304  1.00 83.50  ? 180 HIS   A N    1 
ATOM   1375 C  CA   . HIS   A 1 180 ? -12.619 -11.957 -10.701 1.00 84.86  ? 180 HIS   A CA   1 
ATOM   1376 C  C    . HIS   A 1 180 ? -14.043 -12.014 -11.228 1.00 90.01  ? 180 HIS   A C    1 
ATOM   1377 O  O    . HIS   A 1 180 ? -14.809 -12.932 -10.915 1.00 95.17  ? 180 HIS   A O    1 
ATOM   1378 C  CB   . HIS   A 1 180 ? -11.887 -13.284 -10.842 1.00 84.60  ? 180 HIS   A CB   1 
ATOM   1379 C  CG   . HIS   A 1 180 ? -11.354 -13.528 -12.216 1.00 89.75  ? 180 HIS   A CG   1 
ATOM   1380 N  ND1  . HIS   A 1 180 ? -10.455 -14.535 -12.501 1.00 97.09  ? 180 HIS   A ND1  1 
ATOM   1381 C  CD2  . HIS   A 1 180 ? -11.568 -12.878 -13.382 1.00 95.77  ? 180 HIS   A CD2  1 
ATOM   1382 C  CE1  . HIS   A 1 180 ? -10.146 -14.501 -13.787 1.00 99.72  ? 180 HIS   A CE1  1 
ATOM   1383 N  NE2  . HIS   A 1 180 ? -10.812 -13.506 -14.346 1.00 100.85 ? 180 HIS   A NE2  1 
ATOM   1384 N  N    . ILE   A 1 181 ? -14.428 -10.994 -11.976 1.00 88.93  ? 181 ILE   A N    1 
ATOM   1385 C  CA   . ILE   A 1 181 ? -15.831 -10.851 -12.305 1.00 86.09  ? 181 ILE   A CA   1 
ATOM   1386 C  C    . ILE   A 1 181 ? -16.177 -11.570 -13.600 1.00 89.33  ? 181 ILE   A C    1 
ATOM   1387 O  O    . ILE   A 1 181 ? -17.317 -11.987 -13.776 1.00 94.38  ? 181 ILE   A O    1 
ATOM   1388 C  CB   . ILE   A 1 181 ? -16.213 -9.368  -12.367 1.00 86.06  ? 181 ILE   A CB   1 
ATOM   1389 C  CG1  . ILE   A 1 181 ? -17.722 -9.252  -12.427 1.00 92.70  ? 181 ILE   A CG1  1 
ATOM   1390 C  CG2  . ILE   A 1 181 ? -15.597 -8.684  -13.576 1.00 83.73  ? 181 ILE   A CG2  1 
ATOM   1391 C  CD1  . ILE   A 1 181 ? -18.404 -9.748  -11.183 1.00 91.18  ? 181 ILE   A CD1  1 
ATOM   1392 N  N    . TRP   A 1 182 ? -15.216 -11.766 -14.499 1.00 92.77  ? 182 TRP   A N    1 
ATOM   1393 C  CA   . TRP   A 1 182 ? -15.461 -12.523 -15.721 1.00 96.77  ? 182 TRP   A CA   1 
ATOM   1394 C  C    . TRP   A 1 182 ? -14.139 -13.095 -16.227 1.00 101.34 ? 182 TRP   A C    1 
ATOM   1395 O  O    . TRP   A 1 182 ? -13.055 -12.669 -15.828 1.00 100.94 ? 182 TRP   A O    1 
ATOM   1396 C  CB   . TRP   A 1 182 ? -16.165 -11.665 -16.796 1.00 96.95  ? 182 TRP   A CB   1 
ATOM   1397 C  CG   . TRP   A 1 182 ? -15.328 -10.531 -17.405 1.00 103.81 ? 182 TRP   A CG   1 
ATOM   1398 C  CD1  . TRP   A 1 182 ? -15.334 -9.211  -17.032 1.00 99.25  ? 182 TRP   A CD1  1 
ATOM   1399 C  CD2  . TRP   A 1 182 ? -14.407 -10.624 -18.507 1.00 104.02 ? 182 TRP   A CD2  1 
ATOM   1400 N  NE1  . TRP   A 1 182 ? -14.460 -8.491  -17.814 1.00 96.38  ? 182 TRP   A NE1  1 
ATOM   1401 C  CE2  . TRP   A 1 182 ? -13.885 -9.334  -18.727 1.00 100.93 ? 182 TRP   A CE2  1 
ATOM   1402 C  CE3  . TRP   A 1 182 ? -13.973 -11.674 -19.322 1.00 106.67 ? 182 TRP   A CE3  1 
ATOM   1403 C  CZ2  . TRP   A 1 182 ? -12.956 -9.071  -19.719 1.00 106.49 ? 182 TRP   A CZ2  1 
ATOM   1404 C  CZ3  . TRP   A 1 182 ? -13.053 -11.409 -20.305 1.00 110.24 ? 182 TRP   A CZ3  1 
ATOM   1405 C  CH2  . TRP   A 1 182 ? -12.553 -10.119 -20.497 1.00 111.15 ? 182 TRP   A CH2  1 
ATOM   1406 N  N    . GLU   A 1 183 ? -14.236 -14.089 -17.097 1.00 102.03 ? 183 GLU   A N    1 
ATOM   1407 C  CA   . GLU   A 1 183 ? -13.051 -14.705 -17.658 1.00 103.09 ? 183 GLU   A CA   1 
ATOM   1408 C  C    . GLU   A 1 183 ? -13.294 -14.894 -19.137 1.00 106.81 ? 183 GLU   A C    1 
ATOM   1409 O  O    . GLU   A 1 183 ? -14.437 -15.033 -19.576 1.00 102.86 ? 183 GLU   A O    1 
ATOM   1410 C  CB   . GLU   A 1 183 ? -12.733 -16.046 -17.000 1.00 107.59 ? 183 GLU   A CB   1 
ATOM   1411 C  CG   . GLU   A 1 183 ? -11.312 -16.521 -17.214 1.00 116.42 ? 183 GLU   A CG   1 
ATOM   1412 C  CD   . GLU   A 1 183 ? -10.845 -17.407 -16.070 1.00 121.92 ? 183 GLU   A CD   1 
ATOM   1413 O  OE1  . GLU   A 1 183 ? -11.685 -17.720 -15.192 1.00 114.33 ? 183 GLU   A OE1  1 
ATOM   1414 O  OE2  . GLU   A 1 183 ? -9.637  -17.751 -16.017 1.00 132.46 ? 183 GLU   A OE2  1 
ATOM   1415 N  N    . SER   A 1 184 ? -12.211 -14.868 -19.907 1.00 111.66 ? 184 SER   A N    1 
ATOM   1416 C  CA   . SER   A 1 184 ? -12.354 -15.063 -21.341 1.00 115.81 ? 184 SER   A CA   1 
ATOM   1417 C  C    . SER   A 1 184 ? -12.854 -16.467 -21.664 1.00 115.55 ? 184 SER   A C    1 
ATOM   1418 O  O    . SER   A 1 184 ? -13.573 -16.657 -22.652 1.00 116.17 ? 184 SER   A O    1 
ATOM   1419 C  CB   . SER   A 1 184 ? -11.021 -14.767 -22.027 1.00 114.16 ? 184 SER   A CB   1 
ATOM   1420 O  OG   . SER   A 1 184 ? -10.045 -15.711 -21.623 1.00 116.13 ? 184 SER   A OG   1 
ATOM   1421 N  N    . SER   A 1 185 ? -12.542 -17.444 -20.814 1.00 115.41 ? 185 SER   A N    1 
ATOM   1422 C  CA   . SER   A 1 185 ? -12.723 -18.855 -21.135 1.00 119.32 ? 185 SER   A CA   1 
ATOM   1423 C  C    . SER   A 1 185 ? -13.761 -19.553 -20.264 1.00 111.92 ? 185 SER   A C    1 
ATOM   1424 O  O    . SER   A 1 185 ? -13.839 -20.784 -20.271 1.00 116.67 ? 185 SER   A O    1 
ATOM   1425 C  CB   . SER   A 1 185 ? -11.378 -19.577 -21.019 1.00 126.82 ? 185 SER   A CB   1 
ATOM   1426 O  OG   . SER   A 1 185 ? -10.928 -19.591 -19.667 1.00 124.19 ? 185 SER   A OG   1 
ATOM   1427 N  N    . ALA   A 1 186 ? -14.552 -18.817 -19.514 1.00 110.31 ? 186 ALA   A N    1 
ATOM   1428 C  CA   . ALA   A 1 186 ? -15.501 -19.430 -18.604 1.00 111.23 ? 186 ALA   A CA   1 
ATOM   1429 C  C    . ALA   A 1 186 ? -16.894 -19.439 -19.220 1.00 109.35 ? 186 ALA   A C    1 
ATOM   1430 O  O    . ALA   A 1 186 ? -17.338 -18.432 -19.773 1.00 110.62 ? 186 ALA   A O    1 
ATOM   1431 C  CB   . ALA   A 1 186 ? -15.510 -18.683 -17.276 1.00 110.80 ? 186 ALA   A CB   1 
ATOM   1432 N  N    . VAL   A 1 187 ? -17.592 -20.571 -19.097 1.00 108.35 ? 187 VAL   A N    1 
ATOM   1433 C  CA   . VAL   A 1 187 ? -18.841 -20.758 -19.836 1.00 107.69 ? 187 VAL   A CA   1 
ATOM   1434 C  C    . VAL   A 1 187 ? -20.019 -20.003 -19.210 1.00 109.66 ? 187 VAL   A C    1 
ATOM   1435 O  O    . VAL   A 1 187 ? -21.002 -19.699 -19.902 1.00 110.01 ? 187 VAL   A O    1 
ATOM   1436 C  CB   . VAL   A 1 187 ? -19.173 -22.252 -19.973 1.00 113.78 ? 187 VAL   A CB   1 
ATOM   1437 C  CG1  . VAL   A 1 187 ? -18.100 -22.991 -20.779 1.00 123.20 ? 187 VAL   A CG1  1 
ATOM   1438 C  CG2  . VAL   A 1 187 ? -19.342 -22.862 -18.618 1.00 120.57 ? 187 VAL   A CG2  1 
ATOM   1439 N  N    . VAL   A 1 188 ? -19.976 -19.714 -17.908 1.00 104.45 ? 188 VAL   A N    1 
ATOM   1440 C  CA   . VAL   A 1 188 ? -20.969 -18.867 -17.258 1.00 99.53  ? 188 VAL   A CA   1 
ATOM   1441 C  C    . VAL   A 1 188 ? -20.241 -18.099 -16.164 1.00 99.05  ? 188 VAL   A C    1 
ATOM   1442 O  O    . VAL   A 1 188 ? -19.181 -18.505 -15.693 1.00 95.56  ? 188 VAL   A O    1 
ATOM   1443 C  CB   . VAL   A 1 188 ? -22.161 -19.661 -16.676 1.00 91.86  ? 188 VAL   A CB   1 
ATOM   1444 C  CG1  . VAL   A 1 188 ? -21.713 -20.502 -15.537 1.00 99.51  ? 188 VAL   A CG1  1 
ATOM   1445 C  CG2  . VAL   A 1 188 ? -23.292 -18.733 -16.234 1.00 91.44  ? 188 VAL   A CG2  1 
ATOM   1446 N  N    . ALA   A 1 189 ? -20.813 -16.962 -15.771 1.00 95.84  ? 189 ALA   A N    1 
ATOM   1447 C  CA   . ALA   A 1 189 ? -20.129 -16.029 -14.896 1.00 88.25  ? 189 ALA   A CA   1 
ATOM   1448 C  C    . ALA   A 1 189 ? -21.171 -15.312 -14.056 1.00 87.01  ? 189 ALA   A C    1 
ATOM   1449 O  O    . ALA   A 1 189 ? -21.450 -14.141 -14.225 1.00 91.71  ? 189 ALA   A O    1 
ATOM   1450 C  CB   . ALA   A 1 189 ? -19.296 -15.032 -15.697 1.00 90.72  ? 189 ALA   A CB   1 
ATOM   1451 N  N    . SER   A 1 190 ? -21.772 -16.085 -13.159 1.00 84.09  ? 190 SER   A N    1 
ATOM   1452 C  CA   . SER   A 1 190 ? -22.839 -15.561 -12.282 1.00 86.01  ? 190 SER   A CA   1 
ATOM   1453 C  C    . SER   A 1 190 ? -22.218 -14.744 -11.156 1.00 81.05  ? 190 SER   A C    1 
ATOM   1454 O  O    . SER   A 1 190 ? -21.034 -14.926 -10.871 1.00 75.91  ? 190 SER   A O    1 
ATOM   1455 C  CB   . SER   A 1 190 ? -23.674 -16.685 -11.740 1.00 94.25  ? 190 SER   A CB   1 
ATOM   1456 O  OG   . SER   A 1 190 ? -23.274 -17.035 -10.424 1.00 95.45  ? 190 SER   A OG   1 
ATOM   1457 N  N    . PHE   A 1 191 ? -23.034 -13.893 -10.549 1.00 81.84  ? 191 PHE   A N    1 
ATOM   1458 C  CA   . PHE   A 1 191 ? -22.638 -13.058 -9.395  1.00 82.30  ? 191 PHE   A CA   1 
ATOM   1459 C  C    . PHE   A 1 191 ? -23.942 -12.574 -8.778  1.00 80.81  ? 191 PHE   A C    1 
ATOM   1460 O  O    . PHE   A 1 191 ? -24.825 -12.174 -9.530  1.00 76.88  ? 191 PHE   A O    1 
ATOM   1461 C  CB   . PHE   A 1 191 ? -21.666 -11.955 -9.816  1.00 78.72  ? 191 PHE   A CB   1 
ATOM   1462 C  CG   . PHE   A 1 191 ? -22.268 -10.619 -10.167 1.00 87.28  ? 191 PHE   A CG   1 
ATOM   1463 C  CD1  . PHE   A 1 191 ? -22.016 -10.033 -11.393 1.00 92.91  ? 191 PHE   A CD1  1 
ATOM   1464 C  CD2  . PHE   A 1 191 ? -23.041 -9.921  -9.261  1.00 89.88  ? 191 PHE   A CD2  1 
ATOM   1465 C  CE1  . PHE   A 1 191 ? -22.555 -8.801  -11.716 1.00 85.44  ? 191 PHE   A CE1  1 
ATOM   1466 C  CE2  . PHE   A 1 191 ? -23.580 -8.689  -9.585  1.00 90.16  ? 191 PHE   A CE2  1 
ATOM   1467 C  CZ   . PHE   A 1 191 ? -23.335 -8.131  -10.810 1.00 76.27  ? 191 PHE   A CZ   1 
ATOM   1468 N  N    . GLU   A 1 192 ? -24.068 -12.666 -7.462  1.00 79.59  ? 192 GLU   A N    1 
ATOM   1469 C  CA   . GLU   A 1 192 ? -25.329 -12.239 -6.823  1.00 74.80  ? 192 GLU   A CA   1 
ATOM   1470 C  C    . GLU   A 1 192 ? -24.974 -11.423 -5.588  1.00 74.33  ? 192 GLU   A C    1 
ATOM   1471 O  O    . GLU   A 1 192 ? -23.948 -11.711 -4.977  1.00 74.00  ? 192 GLU   A O    1 
ATOM   1472 C  CB   . GLU   A 1 192 ? -26.183 -13.461 -6.496  1.00 84.86  ? 192 GLU   A CB   1 
ATOM   1473 C  CG   . GLU   A 1 192 ? -26.226 -13.802 -5.020  1.00 102.43 ? 192 GLU   A CG   1 
ATOM   1474 C  CD   . GLU   A 1 192 ? -26.854 -15.150 -4.710  1.00 115.82 ? 192 GLU   A CD   1 
ATOM   1475 O  OE1  . GLU   A 1 192 ? -26.952 -15.496 -3.521  1.00 114.87 ? 192 GLU   A OE1  1 
ATOM   1476 O  OE2  . GLU   A 1 192 ? -27.239 -15.849 -5.660  1.00 122.15 ? 192 GLU   A OE2  1 
ATOM   1477 N  N    . ALA   A 1 193 ? -25.801 -10.434 -5.268  1.00 77.72  ? 193 ALA   A N    1 
ATOM   1478 C  CA   . ALA   A 1 193 ? -25.573 -9.575  -4.126  1.00 73.18  ? 193 ALA   A CA   1 
ATOM   1479 C  C    . ALA   A 1 193 ? -26.876 -9.234  -3.429  1.00 74.30  ? 193 ALA   A C    1 
ATOM   1480 O  O    . ALA   A 1 193 ? -27.911 -9.047  -4.070  1.00 74.90  ? 193 ALA   A O    1 
ATOM   1481 C  CB   . ALA   A 1 193 ? -24.881 -8.286  -4.537  1.00 72.12  ? 193 ALA   A CB   1 
ATOM   1482 N  N    . THR   A 1 194 ? -26.796 -9.105  -2.113  1.00 76.65  ? 194 THR   A N    1 
ATOM   1483 C  CA   . THR   A 1 194 ? -27.973 -8.908  -1.289  1.00 77.59  ? 194 THR   A CA   1 
ATOM   1484 C  C    . THR   A 1 194 ? -27.611 -7.934  -0.189  1.00 77.46  ? 194 THR   A C    1 
ATOM   1485 O  O    . THR   A 1 194 ? -26.508 -7.998  0.352   1.00 80.29  ? 194 THR   A O    1 
ATOM   1486 C  CB   . THR   A 1 194 ? -28.436 -10.225 -0.673  1.00 82.20  ? 194 THR   A CB   1 
ATOM   1487 O  OG1  . THR   A 1 194 ? -28.599 -11.211 -1.702  1.00 87.11  ? 194 THR   A OG1  1 
ATOM   1488 C  CG2  . THR   A 1 194 ? -29.758 -10.029 0.056   1.00 88.57  ? 194 THR   A CG2  1 
ATOM   1489 N  N    . PHE   A 1 195 ? -28.516 -7.029  0.147   1.00 77.41  ? 195 PHE   A N    1 
ATOM   1490 C  CA   . PHE   A 1 195 ? -28.182 -6.186  1.286   1.00 76.86  ? 195 PHE   A CA   1 
ATOM   1491 C  C    . PHE   A 1 195 ? -29.429 -5.523  1.825   1.00 75.46  ? 195 PHE   A C    1 
ATOM   1492 O  O    . PHE   A 1 195 ? -30.394 -5.280  1.097   1.00 79.98  ? 195 PHE   A O    1 
ATOM   1493 C  CB   . PHE   A 1 195 ? -27.150 -5.102  0.952   1.00 75.46  ? 195 PHE   A CB   1 
ATOM   1494 C  CG   . PHE   A 1 195 ? -27.666 -4.016  0.042   1.00 81.24  ? 195 PHE   A CG   1 
ATOM   1495 C  CD1  . PHE   A 1 195 ? -28.391 -2.939  0.554   1.00 78.86  ? 195 PHE   A CD1  1 
ATOM   1496 C  CD2  . PHE   A 1 195 ? -27.385 -4.040  -1.319  1.00 79.26  ? 195 PHE   A CD2  1 
ATOM   1497 C  CE1  . PHE   A 1 195 ? -28.857 -1.941  -0.281  1.00 75.11  ? 195 PHE   A CE1  1 
ATOM   1498 C  CE2  . PHE   A 1 195 ? -27.845 -3.037  -2.157  1.00 75.40  ? 195 PHE   A CE2  1 
ATOM   1499 C  CZ   . PHE   A 1 195 ? -28.582 -1.986  -1.634  1.00 73.51  ? 195 PHE   A CZ   1 
ATOM   1500 N  N    . THR   A 1 196 ? -29.380 -5.205  3.101   1.00 69.69  ? 196 THR   A N    1 
ATOM   1501 C  CA   . THR   A 1 196 ? -30.449 -4.456  3.714   1.00 77.05  ? 196 THR   A CA   1 
ATOM   1502 C  C    . THR   A 1 196 ? -29.946 -3.112  4.199   1.00 81.30  ? 196 THR   A C    1 
ATOM   1503 O  O    . THR   A 1 196 ? -28.743 -2.877  4.343   1.00 78.84  ? 196 THR   A O    1 
ATOM   1504 C  CB   . THR   A 1 196 ? -31.105 -5.240  4.826   1.00 78.09  ? 196 THR   A CB   1 
ATOM   1505 O  OG1  . THR   A 1 196 ? -30.113 -5.637  5.767   1.00 83.91  ? 196 THR   A OG1  1 
ATOM   1506 C  CG2  . THR   A 1 196 ? -31.777 -6.415  4.236   1.00 87.02  ? 196 THR   A CG2  1 
ATOM   1507 N  N    . PHE   A 1 197 ? -30.911 -2.222  4.406   1.00 81.32  ? 197 PHE   A N    1 
ATOM   1508 C  CA   . PHE   A 1 197 ? -30.656 -0.802  4.510   1.00 76.63  ? 197 PHE   A CA   1 
ATOM   1509 C  C    . PHE   A 1 197 ? -31.773 -0.193  5.313   1.00 82.39  ? 197 PHE   A C    1 
ATOM   1510 O  O    . PHE   A 1 197 ? -32.893 -0.701  5.320   1.00 89.24  ? 197 PHE   A O    1 
ATOM   1511 C  CB   . PHE   A 1 197 ? -30.605 -0.109  3.151   1.00 75.92  ? 197 PHE   A CB   1 
ATOM   1512 C  CG   . PHE   A 1 197 ? -31.809 -0.361  2.297   1.00 73.87  ? 197 PHE   A CG   1 
ATOM   1513 C  CD1  . PHE   A 1 197 ? -33.039 0.183   2.607   1.00 82.62  ? 197 PHE   A CD1  1 
ATOM   1514 C  CD2  . PHE   A 1 197 ? -31.715 -1.162  1.182   1.00 78.82  ? 197 PHE   A CD2  1 
ATOM   1515 C  CE1  . PHE   A 1 197 ? -34.153 -0.064  1.815   1.00 86.36  ? 197 PHE   A CE1  1 
ATOM   1516 C  CE2  . PHE   A 1 197 ? -32.823 -1.418  0.390   1.00 81.75  ? 197 PHE   A CE2  1 
ATOM   1517 C  CZ   . PHE   A 1 197 ? -34.040 -0.867  0.706   1.00 82.72  ? 197 PHE   A CZ   1 
ATOM   1518 N  N    . LEU   A 1 198 ? -31.465 0.909   5.971   1.00 89.58  ? 198 LEU   A N    1 
ATOM   1519 C  CA   . LEU   A 1 198 ? -32.479 1.686   6.653   1.00 92.84  ? 198 LEU   A CA   1 
ATOM   1520 C  C    . LEU   A 1 198 ? -32.395 3.106   6.151   1.00 95.20  ? 198 LEU   A C    1 
ATOM   1521 O  O    . LEU   A 1 198 ? -31.329 3.721   6.207   1.00 94.81  ? 198 LEU   A O    1 
ATOM   1522 C  CB   . LEU   A 1 198 ? -32.306 1.641   8.166   1.00 93.66  ? 198 LEU   A CB   1 
ATOM   1523 C  CG   . LEU   A 1 198 ? -33.448 2.333   8.907   1.00 100.39 ? 198 LEU   A CG   1 
ATOM   1524 C  CD1  . LEU   A 1 198 ? -33.614 1.705   10.256  1.00 105.39 ? 198 LEU   A CD1  1 
ATOM   1525 C  CD2  . LEU   A 1 198 ? -33.149 3.812   9.111   1.00 107.72 ? 198 LEU   A CD2  1 
ATOM   1526 N  N    . ILE   A 1 199 ? -33.522 3.630   5.689   1.00 102.57 ? 199 ILE   A N    1 
ATOM   1527 C  CA   . ILE   A 1 199 ? -33.604 5.014   5.247   1.00 106.54 ? 199 ILE   A CA   1 
ATOM   1528 C  C    . ILE   A 1 199 ? -34.726 5.738   5.989   1.00 109.98 ? 199 ILE   A C    1 
ATOM   1529 O  O    . ILE   A 1 199 ? -35.885 5.302   5.980   1.00 107.13 ? 199 ILE   A O    1 
ATOM   1530 C  CB   . ILE   A 1 199 ? -33.749 5.100   3.718   1.00 105.01 ? 199 ILE   A CB   1 
ATOM   1531 C  CG1  . ILE   A 1 199 ? -32.431 4.636   3.082   1.00 98.70  ? 199 ILE   A CG1  1 
ATOM   1532 C  CG2  . ILE   A 1 199 ? -34.126 6.491   3.284   1.00 109.38 ? 199 ILE   A CG2  1 
ATOM   1533 C  CD1  . ILE   A 1 199 ? -32.467 4.431   1.595   1.00 92.60  ? 199 ILE   A CD1  1 
ATOM   1534 N  N    . LYS   A 1 200 ? -34.350 6.836   6.652   1.00 112.64 ? 200 LYS   A N    1 
ATOM   1535 C  CA   . LYS   A 1 200 ? -35.187 7.652   7.519   1.00 112.96 ? 200 LYS   A CA   1 
ATOM   1536 C  C    . LYS   A 1 200 ? -34.728 9.094   7.331   1.00 114.97 ? 200 LYS   A C    1 
ATOM   1537 O  O    . LYS   A 1 200 ? -33.522 9.365   7.339   1.00 109.77 ? 200 LYS   A O    1 
ATOM   1538 C  CB   . LYS   A 1 200 ? -35.044 7.197   8.987   1.00 110.17 ? 200 LYS   A CB   1 
ATOM   1539 C  CG   . LYS   A 1 200 ? -35.994 7.815   10.025  1.00 111.49 ? 200 LYS   A CG   1 
ATOM   1540 C  CD   . LYS   A 1 200 ? -35.868 7.088   11.379  1.00 108.43 ? 200 LYS   A CD   1 
ATOM   1541 C  CE   . LYS   A 1 200 ? -36.929 7.516   12.389  1.00 113.70 ? 200 LYS   A CE   1 
ATOM   1542 N  NZ   . LYS   A 1 200 ? -38.286 6.936   12.112  1.00 116.88 ? 200 LYS   A NZ   1 
ATOM   1543 N  N    . SER   A 1 201 ? -35.675 10.003  7.093   1.00 117.42 ? 201 SER   A N    1 
ATOM   1544 C  CA   . SER   A 1 201 ? -35.380 11.423  7.198   1.00 121.12 ? 201 SER   A CA   1 
ATOM   1545 C  C    . SER   A 1 201 ? -36.414 12.103  8.080   1.00 130.20 ? 201 SER   A C    1 
ATOM   1546 O  O    . SER   A 1 201 ? -37.611 11.781  8.015   1.00 128.04 ? 201 SER   A O    1 
ATOM   1547 C  CB   . SER   A 1 201 ? -35.329 12.138  5.840   1.00 115.64 ? 201 SER   A CB   1 
ATOM   1548 O  OG   . SER   A 1 201 ? -34.252 11.675  5.063   1.00 114.14 ? 201 SER   A OG   1 
ATOM   1549 N  N    . PRO   A 1 202 ? -35.974 13.038  8.925   1.00 132.54 ? 202 PRO   A N    1 
ATOM   1550 C  CA   . PRO   A 1 202 ? -36.939 13.903  9.608   1.00 130.53 ? 202 PRO   A CA   1 
ATOM   1551 C  C    . PRO   A 1 202 ? -37.801 14.642  8.617   1.00 134.11 ? 202 PRO   A C    1 
ATOM   1552 O  O    . PRO   A 1 202 ? -38.967 14.942  8.901   1.00 136.36 ? 202 PRO   A O    1 
ATOM   1553 C  CB   . PRO   A 1 202 ? -36.043 14.868  10.392  1.00 136.96 ? 202 PRO   A CB   1 
ATOM   1554 C  CG   . PRO   A 1 202 ? -34.713 14.839  9.667   1.00 130.43 ? 202 PRO   A CG   1 
ATOM   1555 C  CD   . PRO   A 1 202 ? -34.576 13.452  9.156   1.00 126.47 ? 202 PRO   A CD   1 
ATOM   1556 N  N    . ASP   A 1 203 ? -37.252 14.875  7.427   1.00 139.02 ? 203 ASP   A N    1 
ATOM   1557 C  CA   . ASP   A 1 203 ? -37.764 15.819  6.449   1.00 142.67 ? 203 ASP   A CA   1 
ATOM   1558 C  C    . ASP   A 1 203 ? -39.011 15.264  5.753   1.00 138.40 ? 203 ASP   A C    1 
ATOM   1559 O  O    . ASP   A 1 203 ? -39.350 14.082  5.861   1.00 128.45 ? 203 ASP   A O    1 
ATOM   1560 C  CB   . ASP   A 1 203 ? -36.687 16.111  5.389   1.00 145.93 ? 203 ASP   A CB   1 
ATOM   1561 C  CG   . ASP   A 1 203 ? -35.448 16.817  5.958   1.00 148.91 ? 203 ASP   A CG   1 
ATOM   1562 O  OD1  . ASP   A 1 203 ? -35.560 17.539  6.976   1.00 156.08 ? 203 ASP   A OD1  1 
ATOM   1563 O  OD2  . ASP   A 1 203 ? -34.350 16.636  5.369   1.00 137.96 ? 203 ASP   A OD2  1 
ATOM   1564 N  N    . SER   A 1 204 ? -39.704 16.152  5.031   1.00 143.49 ? 204 SER   A N    1 
ATOM   1565 C  CA   . SER   A 1 204 ? -40.658 15.700  4.025   1.00 142.46 ? 204 SER   A CA   1 
ATOM   1566 C  C    . SER   A 1 204 ? -39.936 15.102  2.822   1.00 143.44 ? 204 SER   A C    1 
ATOM   1567 O  O    . SER   A 1 204 ? -40.488 14.243  2.126   1.00 142.28 ? 204 SER   A O    1 
ATOM   1568 C  CB   . SER   A 1 204 ? -41.555 16.860  3.566   1.00 139.44 ? 204 SER   A CB   1 
ATOM   1569 O  OG   . SER   A 1 204 ? -42.386 17.349  4.604   1.00 125.75 ? 204 SER   A OG   1 
ATOM   1570 N  N    . HIS   A 1 205 ? -38.706 15.541  2.562   1.00 141.20 ? 205 HIS   A N    1 
ATOM   1571 C  CA   . HIS   A 1 205 ? -38.031 15.245  1.307   1.00 136.76 ? 205 HIS   A CA   1 
ATOM   1572 C  C    . HIS   A 1 205 ? -36.690 14.613  1.681   1.00 135.10 ? 205 HIS   A C    1 
ATOM   1573 O  O    . HIS   A 1 205 ? -35.881 15.271  2.362   1.00 137.77 ? 205 HIS   A O    1 
ATOM   1574 C  CB   . HIS   A 1 205 ? -37.795 16.527  0.474   1.00 140.28 ? 205 HIS   A CB   1 
ATOM   1575 C  CG   . HIS   A 1 205 ? -39.033 17.346  0.217   1.00 147.19 ? 205 HIS   A CG   1 
ATOM   1576 N  ND1  . HIS   A 1 205 ? -39.390 18.420  1.016   1.00 146.42 ? 205 HIS   A ND1  1 
ATOM   1577 C  CD2  . HIS   A 1 205 ? -40.002 17.244  -0.725  1.00 153.87 ? 205 HIS   A CD2  1 
ATOM   1578 C  CE1  . HIS   A 1 205 ? -40.521 18.942  0.571   1.00 152.60 ? 205 HIS   A CE1  1 
ATOM   1579 N  NE2  . HIS   A 1 205 ? -40.916 18.245  -0.483  1.00 160.08 ? 205 HIS   A NE2  1 
ATOM   1580 N  N    . PRO   A 1 206 ? -36.385 13.345  1.295   1.00 125.73 ? 206 PRO   A N    1 
ATOM   1581 C  CA   . PRO   A 1 206 ? -35.050 12.795  1.584   1.00 118.49 ? 206 PRO   A CA   1 
ATOM   1582 C  C    . PRO   A 1 206 ? -34.162 12.697  0.348   1.00 115.61 ? 206 PRO   A C    1 
ATOM   1583 O  O    . PRO   A 1 206 ? -34.679 12.700  -0.775  1.00 116.93 ? 206 PRO   A O    1 
ATOM   1584 C  CB   . PRO   A 1 206 ? -35.392 11.419  2.155   1.00 115.09 ? 206 PRO   A CB   1 
ATOM   1585 C  CG   . PRO   A 1 206 ? -36.610 10.995  1.339   1.00 115.25 ? 206 PRO   A CG   1 
ATOM   1586 C  CD   . PRO   A 1 206 ? -37.268 12.280  0.787   1.00 123.45 ? 206 PRO   A CD   1 
ATOM   1587 N  N    . ALA   A 1 207 ? -32.839 12.608  0.521   1.00 111.27 ? 207 ALA   A N    1 
ATOM   1588 C  CA   . ALA   A 1 207 ? -31.916 12.611  -0.617  1.00 111.33 ? 207 ALA   A CA   1 
ATOM   1589 C  C    . ALA   A 1 207 ? -30.541 12.149  -0.166  1.00 106.37 ? 207 ALA   A C    1 
ATOM   1590 O  O    . ALA   A 1 207 ? -30.185 12.333  0.997   1.00 106.95 ? 207 ALA   A O    1 
ATOM   1591 C  CB   . ALA   A 1 207 ? -31.805 14.005  -1.237  1.00 114.36 ? 207 ALA   A CB   1 
ATOM   1592 N  N    . ASP   A 1 208 ? -29.758 11.556  -1.080  1.00 107.71 ? 208 ASP   A N    1 
ATOM   1593 C  CA   . ASP   A 1 208 ? -30.134 11.182  -2.461  1.00 113.70 ? 208 ASP   A CA   1 
ATOM   1594 C  C    . ASP   A 1 208 ? -30.397 9.687   -2.643  1.00 111.06 ? 208 ASP   A C    1 
ATOM   1595 O  O    . ASP   A 1 208 ? -31.432 9.312   -3.191  1.00 108.16 ? 208 ASP   A O    1 
ATOM   1596 C  CB   . ASP   A 1 208 ? -29.051 11.590  -3.468  1.00 113.23 ? 208 ASP   A CB   1 
ATOM   1597 C  CG   . ASP   A 1 208 ? -28.675 13.052  -3.379  1.00 116.72 ? 208 ASP   A CG   1 
ATOM   1598 O  OD1  . ASP   A 1 208 ? -27.797 13.412  -2.566  1.00 115.34 ? 208 ASP   A OD1  1 
ATOM   1599 O  OD2  . ASP   A 1 208 ? -29.273 13.847  -4.127  1.00 122.51 ? 208 ASP   A OD2  1 
ATOM   1600 N  N    . GLY   A 1 209 ? -29.456 8.840   -2.232  1.00 110.21 ? 209 GLY   A N    1 
ATOM   1601 C  CA   . GLY   A 1 209 ? -29.709 7.411   -2.246  1.00 107.59 ? 209 GLY   A CA   1 
ATOM   1602 C  C    . GLY   A 1 209 ? -28.478 6.561   -1.953  1.00 103.39 ? 209 GLY   A C    1 
ATOM   1603 O  O    . GLY   A 1 209 ? -27.388 7.066   -1.663  1.00 101.09 ? 209 GLY   A O    1 
ATOM   1604 N  N    . ILE   A 1 210 ? -28.702 5.235   -2.031  1.00 99.68  ? 210 ILE   A N    1 
ATOM   1605 C  CA   . ILE   A 1 210 ? -27.692 4.187   -1.913  1.00 85.84  ? 210 ILE   A CA   1 
ATOM   1606 C  C    . ILE   A 1 210 ? -27.560 3.509   -3.265  1.00 78.54  ? 210 ILE   A C    1 
ATOM   1607 O  O    . ILE   A 1 210 ? -28.508 3.464   -4.056  1.00 77.53  ? 210 ILE   A O    1 
ATOM   1608 C  CB   . ILE   A 1 210 ? -28.059 3.136   -0.840  1.00 80.65  ? 210 ILE   A CB   1 
ATOM   1609 C  CG1  . ILE   A 1 210 ? -28.593 3.808   0.437   1.00 85.99  ? 210 ILE   A CG1  1 
ATOM   1610 C  CG2  . ILE   A 1 210 ? -26.885 2.221   -0.574  1.00 80.24  ? 210 ILE   A CG2  1 
ATOM   1611 C  CD1  . ILE   A 1 210 ? -29.010 2.856   1.544   1.00 78.52  ? 210 ILE   A CD1  1 
ATOM   1612 N  N    . ALA   A 1 211 ? -26.380 2.970   -3.532  1.00 78.62  ? 211 ALA   A N    1 
ATOM   1613 C  CA   . ALA   A 1 211 ? -26.187 2.193   -4.744  1.00 80.09  ? 211 ALA   A CA   1 
ATOM   1614 C  C    . ALA   A 1 211 ? -25.192 1.070   -4.474  1.00 82.87  ? 211 ALA   A C    1 
ATOM   1615 O  O    . ALA   A 1 211 ? -24.181 1.277   -3.799  1.00 85.33  ? 211 ALA   A O    1 
ATOM   1616 C  CB   . ALA   A 1 211 ? -25.706 3.071   -5.908  1.00 73.86  ? 211 ALA   A CB   1 
ATOM   1617 N  N    . PHE   A 1 212 ? -25.512 -0.130  -4.960  1.00 79.38  ? 212 PHE   A N    1 
ATOM   1618 C  CA   . PHE   A 1 212 ? -24.508 -1.168  -5.126  1.00 73.23  ? 212 PHE   A CA   1 
ATOM   1619 C  C    . PHE   A 1 212 ? -23.756 -0.869  -6.396  1.00 72.24  ? 212 PHE   A C    1 
ATOM   1620 O  O    . PHE   A 1 212 ? -24.380 -0.608  -7.425  1.00 77.53  ? 212 PHE   A O    1 
ATOM   1621 C  CB   . PHE   A 1 212 ? -25.139 -2.553  -5.233  1.00 75.77  ? 212 PHE   A CB   1 
ATOM   1622 C  CG   . PHE   A 1 212 ? -24.131 -3.658  -5.449  1.00 81.64  ? 212 PHE   A CG   1 
ATOM   1623 C  CD1  . PHE   A 1 212 ? -23.354 -4.148  -4.398  1.00 79.97  ? 212 PHE   A CD1  1 
ATOM   1624 C  CD2  . PHE   A 1 212 ? -23.886 -4.143  -6.746  1.00 81.20  ? 212 PHE   A CD2  1 
ATOM   1625 C  CE1  . PHE   A 1 212 ? -22.382 -5.155  -4.630  1.00 79.18  ? 212 PHE   A CE1  1 
ATOM   1626 C  CE2  . PHE   A 1 212 ? -22.921 -5.136  -6.997  1.00 74.03  ? 212 PHE   A CE2  1 
ATOM   1627 C  CZ   . PHE   A 1 212 ? -22.169 -5.645  -5.941  1.00 75.13  ? 212 PHE   A CZ   1 
ATOM   1628 N  N    . PHE   A 1 213 ? -22.434 -0.905  -6.345  1.00 67.87  ? 213 PHE   A N    1 
ATOM   1629 C  CA   . PHE   A 1 213 ? -21.681 -0.643  -7.552  1.00 70.85  ? 213 PHE   A CA   1 
ATOM   1630 C  C    . PHE   A 1 213 ? -20.562 -1.649  -7.691  1.00 74.17  ? 213 PHE   A C    1 
ATOM   1631 O  O    . PHE   A 1 213 ? -20.130 -2.291  -6.726  1.00 73.19  ? 213 PHE   A O    1 
ATOM   1632 C  CB   . PHE   A 1 213 ? -21.089 0.771   -7.583  1.00 76.94  ? 213 PHE   A CB   1 
ATOM   1633 C  CG   . PHE   A 1 213 ? -19.914 0.970   -6.649  1.00 81.97  ? 213 PHE   A CG   1 
ATOM   1634 C  CD1  . PHE   A 1 213 ? -18.608 0.601   -7.033  1.00 84.41  ? 213 PHE   A CD1  1 
ATOM   1635 C  CD2  . PHE   A 1 213 ? -20.106 1.501   -5.387  1.00 76.58  ? 213 PHE   A CD2  1 
ATOM   1636 C  CE1  . PHE   A 1 213 ? -17.533 0.764   -6.181  1.00 74.32  ? 213 PHE   A CE1  1 
ATOM   1637 C  CE2  . PHE   A 1 213 ? -19.041 1.654   -4.537  1.00 77.31  ? 213 PHE   A CE2  1 
ATOM   1638 C  CZ   . PHE   A 1 213 ? -17.750 1.287   -4.940  1.00 76.74  ? 213 PHE   A CZ   1 
ATOM   1639 N  N    . ILE   A 1 214 ? -20.072 -1.732  -8.918  1.00 79.32  ? 214 ILE   A N    1 
ATOM   1640 C  CA   . ILE   A 1 214 ? -18.895 -2.517  -9.264  1.00 86.15  ? 214 ILE   A CA   1 
ATOM   1641 C  C    . ILE   A 1 214 ? -17.993 -1.594  -10.042 1.00 83.84  ? 214 ILE   A C    1 
ATOM   1642 O  O    . ILE   A 1 214 ? -18.463 -0.818  -10.876 1.00 86.51  ? 214 ILE   A O    1 
ATOM   1643 C  CB   . ILE   A 1 214 ? -19.226 -3.751  -10.134 1.00 84.21  ? 214 ILE   A CB   1 
ATOM   1644 C  CG1  . ILE   A 1 214 ? -20.100 -4.722  -9.375  1.00 77.49  ? 214 ILE   A CG1  1 
ATOM   1645 C  CG2  . ILE   A 1 214 ? -17.967 -4.472  -10.555 1.00 73.42  ? 214 ILE   A CG2  1 
ATOM   1646 C  CD1  . ILE   A 1 214 ? -21.055 -5.310  -10.250 1.00 68.15  ? 214 ILE   A CD1  1 
ATOM   1647 N  N    . SER   A 1 215 ? -16.691 -1.621  -9.757  1.00 84.11  ? 215 SER   A N    1 
ATOM   1648 C  CA   . SER   A 1 215 ? -15.758 -0.757  -10.518 1.00 90.62  ? 215 SER   A CA   1 
ATOM   1649 C  C    . SER   A 1 215 ? -14.387 -1.423  -10.588 1.00 91.29  ? 215 SER   A C    1 
ATOM   1650 O  O    . SER   A 1 215 ? -14.285 -2.599  -10.222 1.00 91.23  ? 215 SER   A O    1 
ATOM   1651 C  CB   . SER   A 1 215 ? -15.648 0.572   -9.866  1.00 96.76  ? 215 SER   A CB   1 
ATOM   1652 O  OG   . SER   A 1 215 ? -15.151 0.409   -8.551  1.00 98.96  ? 215 SER   A OG   1 
ATOM   1653 N  N    . ASN   A 1 216 ? -13.379 -0.670  -11.028 1.00 93.96  ? 216 ASN   A N    1 
ATOM   1654 C  CA   . ASN   A 1 216 ? -11.990 -1.181  -11.139 1.00 100.59 ? 216 ASN   A CA   1 
ATOM   1655 C  C    . ASN   A 1 216 ? -11.379 -1.284  -9.742  1.00 103.93 ? 216 ASN   A C    1 
ATOM   1656 O  O    . ASN   A 1 216 ? -11.833 -0.578  -8.837  1.00 100.14 ? 216 ASN   A O    1 
ATOM   1657 C  CB   . ASN   A 1 216 ? -11.132 -0.297  -12.038 1.00 103.66 ? 216 ASN   A CB   1 
ATOM   1658 C  CG   . ASN   A 1 216 ? -11.750 1.069   -12.208 1.00 113.17 ? 216 ASN   A CG   1 
ATOM   1659 O  OD1  . ASN   A 1 216 ? -12.932 1.244   -11.931 1.00 109.15 ? 216 ASN   A OD1  1 
ATOM   1660 N  ND2  . ASN   A 1 216 ? -10.963 2.035   -12.647 1.00 119.96 ? 216 ASN   A ND2  1 
ATOM   1661 N  N    . ILE   A 1 217 ? -10.313 -2.071  -9.614  1.00 99.49  ? 217 ILE   A N    1 
ATOM   1662 C  CA   . ILE   A 1 217 ? -9.641  -2.323  -8.308  1.00 91.92  ? 217 ILE   A CA   1 
ATOM   1663 C  C    . ILE   A 1 217 ? -9.124  -1.010  -7.720  1.00 101.10 ? 217 ILE   A C    1 
ATOM   1664 O  O    . ILE   A 1 217 ? -9.269  -0.822  -6.510  1.00 100.25 ? 217 ILE   A O    1 
ATOM   1665 C  CB   . ILE   A 1 217 ? -8.479  -3.303  -8.523  1.00 90.57  ? 217 ILE   A CB   1 
ATOM   1666 C  CG1  . ILE   A 1 217 ? -7.940  -3.210  -9.949  1.00 102.68 ? 217 ILE   A CG1  1 
ATOM   1667 C  CG2  . ILE   A 1 217 ? -8.901  -4.717  -8.183  1.00 97.52  ? 217 ILE   A CG2  1 
ATOM   1668 C  CD1  . ILE   A 1 217 ? -6.983  -4.314  -10.310 1.00 98.51  ? 217 ILE   A CD1  1 
ATOM   1669 N  N    . ASP   A 1 218 ? -8.600  -0.119  -8.564  1.00 113.29 ? 218 ASP   A N    1 
ATOM   1670 C  CA   . ASP   A 1 218 ? -7.974  1.164   -8.144  1.00 112.40 ? 218 ASP   A CA   1 
ATOM   1671 C  C    . ASP   A 1 218 ? -9.016  2.270   -7.939  1.00 107.09 ? 218 ASP   A C    1 
ATOM   1672 O  O    . ASP   A 1 218 ? -8.608  3.391   -7.615  1.00 105.89 ? 218 ASP   A O    1 
ATOM   1673 C  CB   . ASP   A 1 218 ? -6.936  1.616   -9.174  1.00 118.07 ? 218 ASP   A CB   1 
ATOM   1674 C  CG   . ASP   A 1 218 ? -7.392  1.454   -10.616 1.00 119.78 ? 218 ASP   A CG   1 
ATOM   1675 O  OD1  . ASP   A 1 218 ? -8.557  1.774   -10.899 1.00 114.37 ? 218 ASP   A OD1  1 
ATOM   1676 O  OD2  . ASP   A 1 218 ? -6.576  1.015   -11.447 1.00 118.92 ? 218 ASP   A OD2  1 
ATOM   1677 N  N    . SER   A 1 219 ? -10.303 1.972   -8.104  1.00 104.38 ? 219 SER   A N    1 
ATOM   1678 C  CA   . SER   A 1 219 ? -11.344 3.024   -8.002  1.00 104.86 ? 219 SER   A CA   1 
ATOM   1679 C  C    . SER   A 1 219 ? -11.336 3.703   -6.634  1.00 102.86 ? 219 SER   A C    1 
ATOM   1680 O  O    . SER   A 1 219 ? -11.138 3.021   -5.624  1.00 102.49 ? 219 SER   A O    1 
ATOM   1681 C  CB   . SER   A 1 219 ? -12.701 2.476   -8.303  1.00 99.94  ? 219 SER   A CB   1 
ATOM   1682 O  OG   . SER   A 1 219 ? -13.697 3.311   -7.740  1.00 102.22 ? 219 SER   A OG   1 
ATOM   1683 N  N    . SER   A 1 220 ? -11.540 5.020   -6.661  1.00 107.75 ? 220 SER   A N    1 
ATOM   1684 C  CA   . SER   A 1 220 ? -11.636 5.920   -5.482  1.00 107.60 ? 220 SER   A CA   1 
ATOM   1685 C  C    . SER   A 1 220 ? -12.813 6.879   -5.703  1.00 106.04 ? 220 SER   A C    1 
ATOM   1686 O  O    . SER   A 1 220 ? -13.337 6.922   -6.831  1.00 107.64 ? 220 SER   A O    1 
ATOM   1687 C  CB   . SER   A 1 220 ? -10.357 6.670   -5.277  1.00 106.11 ? 220 SER   A CB   1 
ATOM   1688 O  OG   . SER   A 1 220 ? -10.398 7.907   -5.966  1.00 114.80 ? 220 SER   A OG   1 
ATOM   1689 N  N    . ILE   A 1 221 ? -13.207 7.656   -4.694  1.00 97.65  ? 221 ILE   A N    1 
ATOM   1690 C  CA   . ILE   A 1 221 ? -14.385 8.499   -4.922  1.00 97.33  ? 221 ILE   A CA   1 
ATOM   1691 C  C    . ILE   A 1 221 ? -14.049 9.531   -5.990  1.00 105.17 ? 221 ILE   A C    1 
ATOM   1692 O  O    . ILE   A 1 221 ? -12.980 10.164  -5.925  1.00 105.75 ? 221 ILE   A O    1 
ATOM   1693 C  CB   . ILE   A 1 221 ? -14.855 9.170   -3.624  1.00 91.70  ? 221 ILE   A CB   1 
ATOM   1694 C  CG1  . ILE   A 1 221 ? -15.281 8.125   -2.611  1.00 92.54  ? 221 ILE   A CG1  1 
ATOM   1695 C  CG2  . ILE   A 1 221 ? -16.110 9.980   -3.864  1.00 91.07  ? 221 ILE   A CG2  1 
ATOM   1696 C  CD1  . ILE   A 1 221 ? -15.531 8.661   -1.245  1.00 92.40  ? 221 ILE   A CD1  1 
ATOM   1697 N  N    . PRO   A 1 222 ? -14.885 9.688   -7.012  1.00 112.46 ? 222 PRO   A N    1 
ATOM   1698 C  CA   . PRO   A 1 222 ? -14.726 10.824  -7.928  1.00 114.73 ? 222 PRO   A CA   1 
ATOM   1699 C  C    . PRO   A 1 222 ? -15.008 12.144  -7.223  1.00 121.09 ? 222 PRO   A C    1 
ATOM   1700 O  O    . PRO   A 1 222 ? -15.882 12.229  -6.353  1.00 115.97 ? 222 PRO   A O    1 
ATOM   1701 C  CB   . PRO   A 1 222 ? -15.758 10.535  -9.030  1.00 113.66 ? 222 PRO   A CB   1 
ATOM   1702 C  CG   . PRO   A 1 222 ? -16.034 9.043   -8.909  1.00 117.04 ? 222 PRO   A CG   1 
ATOM   1703 C  CD   . PRO   A 1 222 ? -15.975 8.795   -7.438  1.00 114.16 ? 222 PRO   A CD   1 
ATOM   1704 N  N    . SER   A 1 223 ? -14.249 13.175  -7.611  1.00 126.06 ? 223 SER   A N    1 
ATOM   1705 C  CA   . SER   A 1 223 ? -14.323 14.466  -6.940  1.00 123.84 ? 223 SER   A CA   1 
ATOM   1706 C  C    . SER   A 1 223 ? -15.667 15.127  -7.197  1.00 121.63 ? 223 SER   A C    1 
ATOM   1707 O  O    . SER   A 1 223 ? -16.217 15.050  -8.301  1.00 119.10 ? 223 SER   A O    1 
ATOM   1708 C  CB   . SER   A 1 223 ? -13.200 15.389  -7.412  1.00 117.23 ? 223 SER   A CB   1 
ATOM   1709 O  OG   . SER   A 1 223 ? -11.923 14.890  -7.060  1.00 118.29 ? 223 SER   A OG   1 
ATOM   1710 N  N    . GLY   A 1 224 ? -16.174 15.823  -6.183  1.00 120.14 ? 224 GLY   A N    1 
ATOM   1711 C  CA   . GLY   A 1 224 ? -17.395 16.592  -6.367  1.00 124.10 ? 224 GLY   A CA   1 
ATOM   1712 C  C    . GLY   A 1 224 ? -18.582 15.707  -6.665  1.00 121.85 ? 224 GLY   A C    1 
ATOM   1713 O  O    . GLY   A 1 224 ? -19.416 16.037  -7.522  1.00 116.59 ? 224 GLY   A O    1 
ATOM   1714 N  N    . SER   A 1 225 ? -18.640 14.542  -6.018  1.00 123.75 ? 225 SER   A N    1 
ATOM   1715 C  CA   . SER   A 1 225 ? -19.661 13.555  -6.344  1.00 118.19 ? 225 SER   A CA   1 
ATOM   1716 C  C    . SER   A 1 225 ? -20.801 13.439  -5.329  1.00 113.79 ? 225 SER   A C    1 
ATOM   1717 O  O    . SER   A 1 225 ? -21.765 12.704  -5.586  1.00 113.78 ? 225 SER   A O    1 
ATOM   1718 C  CB   . SER   A 1 225 ? -19.021 12.164  -6.485  1.00 113.56 ? 225 SER   A CB   1 
ATOM   1719 O  OG   . SER   A 1 225 ? -18.498 11.612  -5.282  1.00 114.54 ? 225 SER   A OG   1 
ATOM   1720 N  N    . THR   A 1 226 ? -20.740 14.161  -4.220  1.00 113.92 ? 226 THR   A N    1 
ATOM   1721 C  CA   . THR   A 1 226 ? -21.857 14.230  -3.282  1.00 112.10 ? 226 THR   A CA   1 
ATOM   1722 C  C    . THR   A 1 226 ? -23.092 14.692  -4.036  1.00 112.11 ? 226 THR   A C    1 
ATOM   1723 O  O    . THR   A 1 226 ? -22.996 15.360  -5.070  1.00 116.94 ? 226 THR   A O    1 
ATOM   1724 C  CB   . THR   A 1 226 ? -21.523 15.190  -2.121  1.00 114.35 ? 226 THR   A CB   1 
ATOM   1725 O  OG1  . THR   A 1 226 ? -21.709 16.540  -2.549  1.00 126.40 ? 226 THR   A OG1  1 
ATOM   1726 C  CG2  . THR   A 1 226 ? -20.092 15.088  -1.618  1.00 110.83 ? 226 THR   A CG2  1 
ATOM   1727 N  N    . GLY   A 1 227 ? -24.235 14.353  -3.514  1.00 107.90 ? 227 GLY   A N    1 
ATOM   1728 C  CA   . GLY   A 1 227 ? -25.503 14.784  -4.102  1.00 110.06 ? 227 GLY   A CA   1 
ATOM   1729 C  C    . GLY   A 1 227 ? -26.030 13.791  -5.145  1.00 115.93 ? 227 GLY   A C    1 
ATOM   1730 O  O    . GLY   A 1 227 ? -26.268 12.643  -4.826  1.00 118.37 ? 227 GLY   A O    1 
ATOM   1731 N  N    . ARG   A 1 228 ? -26.231 14.264  -6.382  1.00 118.21 ? 228 ARG   A N    1 
ATOM   1732 C  CA   . ARG   A 1 228 ? -26.936 13.475  -7.399  1.00 109.97 ? 228 ARG   A CA   1 
ATOM   1733 C  C    . ARG   A 1 228 ? -26.146 12.250  -7.826  1.00 103.00 ? 228 ARG   A C    1 
ATOM   1734 O  O    . ARG   A 1 228 ? -26.747 11.223  -8.160  1.00 101.36 ? 228 ARG   A O    1 
ATOM   1735 C  CB   . ARG   A 1 228 ? -27.226 14.330  -8.637  1.00 114.37 ? 228 ARG   A CB   1 
ATOM   1736 C  CG   . ARG   A 1 228 ? -28.053 15.542  -8.292  1.00 122.74 ? 228 ARG   A CG   1 
ATOM   1737 C  CD   . ARG   A 1 228 ? -28.489 16.499  -9.412  1.00 130.10 ? 228 ARG   A CD   1 
ATOM   1738 N  NE   . ARG   A 1 228 ? -27.410 17.176  -10.136 1.00 125.53 ? 228 ARG   A NE   1 
ATOM   1739 C  CZ   . ARG   A 1 228 ? -27.637 18.008  -11.143 1.00 123.55 ? 228 ARG   A CZ   1 
ATOM   1740 N  NH1  . ARG   A 1 228 ? -28.887 18.323  -11.451 1.00 126.36 ? 228 ARG   A NH1  1 
ATOM   1741 N  NH2  . ARG   A 1 228 ? -26.632 18.573  -11.791 1.00 130.82 ? 228 ARG   A NH2  1 
ATOM   1742 N  N    . LEU   A 1 229 ? -24.810 12.343  -7.809  1.00 103.14 ? 229 LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 229 ? -23.870 11.337  -8.312  1.00 109.99 ? 229 LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 229 ? -23.538 10.216  -7.318  1.00 108.51 ? 229 LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 229 ? -22.769 9.302   -7.669  1.00 105.70 ? 229 LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 229 ? -22.570 12.025  -8.753  1.00 110.66 ? 229 LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 229 ? -22.685 13.260  -9.640  1.00 110.08 ? 229 LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 229 ? -21.382 14.032  -9.661  1.00 115.02 ? 229 LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 229 ? -23.022 12.790  -11.040 1.00 106.52 ? 229 LEU   A CD2  1 
ATOM   1750 N  N    . LEU   A 1 230 ? -24.058 10.269  -6.091  1.00 104.57 ? 230 LEU   A N    1 
ATOM   1751 C  CA   . LEU   A 1 230 ? -24.090 9.122   -5.195  1.00 92.97  ? 230 LEU   A CA   1 
ATOM   1752 C  C    . LEU   A 1 230 ? -22.701 8.582   -4.905  1.00 91.73  ? 230 LEU   A C    1 
ATOM   1753 O  O    . LEU   A 1 230 ? -22.551 7.424   -4.555  1.00 98.61  ? 230 LEU   A O    1 
ATOM   1754 C  CB   . LEU   A 1 230 ? -24.948 8.018   -5.802  1.00 95.40  ? 230 LEU   A CB   1 
ATOM   1755 C  CG   . LEU   A 1 230 ? -26.418 8.367   -5.996  1.00 99.06  ? 230 LEU   A CG   1 
ATOM   1756 C  CD1  . LEU   A 1 230 ? -27.047 7.224   -6.749  1.00 90.85  ? 230 LEU   A CD1  1 
ATOM   1757 C  CD2  . LEU   A 1 230 ? -27.171 8.706   -4.699  1.00 100.07 ? 230 LEU   A CD2  1 
ATOM   1758 N  N    . GLY   A 1 231 ? -21.668 9.385   -5.085  1.00 94.68  ? 231 GLY   A N    1 
ATOM   1759 C  CA   . GLY   A 1 231 ? -20.313 8.907   -4.910  1.00 95.61  ? 231 GLY   A CA   1 
ATOM   1760 C  C    . GLY   A 1 231 ? -19.818 7.979   -5.994  1.00 98.55  ? 231 GLY   A C    1 
ATOM   1761 O  O    . GLY   A 1 231 ? -19.009 7.088   -5.711  1.00 98.14  ? 231 GLY   A O    1 
ATOM   1762 N  N    . LEU   A 1 232 ? -20.240 8.185   -7.238  1.00 100.54 ? 232 LEU   A N    1 
ATOM   1763 C  CA   . LEU   A 1 232 ? -20.020 7.159   -8.247  1.00 102.60 ? 232 LEU   A CA   1 
ATOM   1764 C  C    . LEU   A 1 232 ? -19.346 7.723   -9.495  1.00 103.77 ? 232 LEU   A C    1 
ATOM   1765 O  O    . LEU   A 1 232 ? -18.342 7.193   -9.987  1.00 98.25  ? 232 LEU   A O    1 
ATOM   1766 C  CB   . LEU   A 1 232 ? -21.367 6.528   -8.598  1.00 99.55  ? 232 LEU   A CB   1 
ATOM   1767 C  CG   . LEU   A 1 232 ? -21.935 5.584   -7.536  1.00 94.43  ? 232 LEU   A CG   1 
ATOM   1768 C  CD1  . LEU   A 1 232 ? -23.430 5.337   -7.763  1.00 94.78  ? 232 LEU   A CD1  1 
ATOM   1769 C  CD2  . LEU   A 1 232 ? -21.154 4.274   -7.475  1.00 85.98  ? 232 LEU   A CD2  1 
ATOM   1770 N  N    . PHE   A 1 233 ? -19.894 8.827   -9.984  1.00 110.69 ? 233 PHE   A N    1 
ATOM   1771 C  CA   . PHE   A 1 233 ? -19.598 9.384   -11.284 1.00 116.23 ? 233 PHE   A CA   1 
ATOM   1772 C  C    . PHE   A 1 233 ? -19.031 10.780  -11.101 1.00 119.49 ? 233 PHE   A C    1 
ATOM   1773 O  O    . PHE   A 1 233 ? -19.598 11.574  -10.334 1.00 117.70 ? 233 PHE   A O    1 
ATOM   1774 C  CB   . PHE   A 1 233 ? -20.876 9.487   -12.113 1.00 117.70 ? 233 PHE   A CB   1 
ATOM   1775 C  CG   . PHE   A 1 233 ? -21.559 8.185   -12.327 1.00 114.36 ? 233 PHE   A CG   1 
ATOM   1776 C  CD1  . PHE   A 1 233 ? -21.136 7.295   -13.307 1.00 110.23 ? 233 PHE   A CD1  1 
ATOM   1777 C  CD2  . PHE   A 1 233 ? -22.610 7.835   -11.495 1.00 105.18 ? 233 PHE   A CD2  1 
ATOM   1778 C  CE1  . PHE   A 1 233 ? -21.779 6.098   -13.477 1.00 103.74 ? 233 PHE   A CE1  1 
ATOM   1779 C  CE2  . PHE   A 1 233 ? -23.250 6.653   -11.653 1.00 105.34 ? 233 PHE   A CE2  1 
ATOM   1780 C  CZ   . PHE   A 1 233 ? -22.839 5.772   -12.642 1.00 105.86 ? 233 PHE   A CZ   1 
ATOM   1781 N  N    . PRO   A 1 234 ? -17.935 11.127  -11.773 1.00 120.13 ? 234 PRO   A N    1 
ATOM   1782 C  CA   . PRO   A 1 234 ? -17.462 12.519  -11.703 1.00 119.45 ? 234 PRO   A CA   1 
ATOM   1783 C  C    . PRO   A 1 234 ? -18.446 13.517  -12.298 1.00 124.25 ? 234 PRO   A C    1 
ATOM   1784 O  O    . PRO   A 1 234 ? -18.711 14.568  -11.695 1.00 120.94 ? 234 PRO   A O    1 
ATOM   1785 C  CB   . PRO   A 1 234 ? -16.141 12.462  -12.481 1.00 119.80 ? 234 PRO   A CB   1 
ATOM   1786 C  CG   . PRO   A 1 234 ? -16.273 11.254  -13.373 1.00 118.63 ? 234 PRO   A CG   1 
ATOM   1787 C  CD   . PRO   A 1 234 ? -17.016 10.267  -12.534 1.00 119.10 ? 234 PRO   A CD   1 
ATOM   1788 N  N    . ASP   A 1 235 ? -18.995 13.215  -13.472 1.00 125.94 ? 235 ASP   A N    1 
ATOM   1789 C  CA   . ASP   A 1 235 ? -19.877 14.121  -14.186 1.00 119.67 ? 235 ASP   A CA   1 
ATOM   1790 C  C    . ASP   A 1 235 ? -21.245 13.490  -14.376 1.00 124.97 ? 235 ASP   A C    1 
ATOM   1791 O  O    . ASP   A 1 235 ? -21.426 12.280  -14.214 1.00 131.02 ? 235 ASP   A O    1 
ATOM   1792 C  CB   . ASP   A 1 235 ? -19.272 14.525  -15.542 1.00 128.25 ? 235 ASP   A CB   1 
ATOM   1793 C  CG   . ASP   A 1 235 ? -19.084 13.351  -16.491 1.00 134.69 ? 235 ASP   A CG   1 
ATOM   1794 O  OD1  . ASP   A 1 235 ? -19.953 12.455  -16.542 1.00 140.58 ? 235 ASP   A OD1  1 
ATOM   1795 O  OD2  . ASP   A 1 235 ? -18.061 13.341  -17.219 1.00 137.82 ? 235 ASP   A OD2  1 
ATOM   1796 N  N    . ALA   A 1 236 ? -22.210 14.327  -14.744 1.00 126.27 ? 236 ALA   A N    1 
ATOM   1797 C  CA   . ALA   A 1 236 ? -23.557 13.865  -15.039 1.00 127.06 ? 236 ALA   A CA   1 
ATOM   1798 C  C    . ALA   A 1 236 ? -23.762 13.538  -16.516 1.00 130.42 ? 236 ALA   A C    1 
ATOM   1799 O  O    . ALA   A 1 236 ? -24.897 13.628  -17.002 1.00 126.48 ? 236 ALA   A O    1 
ATOM   1800 C  CB   . ALA   A 1 236 ? -24.579 14.905  -14.585 1.00 123.53 ? 236 ALA   A CB   1 
ATOM   1801 N  N    . ASN   A 1 237 ? -22.693 13.176  -17.236 1.00 135.03 ? 237 ASN   A N    1 
ATOM   1802 C  CA   . ASN   A 1 237 ? -22.794 12.721  -18.633 1.00 139.13 ? 237 ASN   A CA   1 
ATOM   1803 C  C    . ASN   A 1 237 ? -23.527 11.379  -18.753 1.00 137.55 ? 237 ASN   A C    1 
ATOM   1804 O  O    . ASN   A 1 237 ? -22.981 10.441  -19.348 1.00 137.94 ? 237 ASN   A O    1 
ATOM   1805 C  CB   . ASN   A 1 237 ? -21.405 12.580  -19.302 1.00 140.35 ? 237 ASN   A CB   1 
ATOM   1806 C  CG   . ASN   A 1 237 ? -20.622 13.898  -19.383 1.00 144.57 ? 237 ASN   A CG   1 
ATOM   1807 O  OD1  . ASN   A 1 237 ? -21.166 14.988  -19.170 1.00 147.40 ? 237 ASN   A OD1  1 
ATOM   1808 N  ND2  . ASN   A 1 237 ? -19.329 13.791  -19.703 1.00 142.51 ? 237 ASN   A ND2  1 
ATOM   1809 O  OXT  . ASN   A 1 237 ? -24.662 11.192  -18.290 1.00 132.29 ? 237 ASN   A OXT  1 
ATOM   1810 N  N    . ALA   B 1 1   ? -52.926 -33.536 -17.459 1.00 143.79 ? 1   ALA   B N    1 
ATOM   1811 C  CA   . ALA   B 1 1   ? -52.241 -34.704 -16.913 1.00 148.69 ? 1   ALA   B CA   1 
ATOM   1812 C  C    . ALA   B 1 1   ? -51.274 -34.313 -15.800 1.00 146.00 ? 1   ALA   B C    1 
ATOM   1813 O  O    . ALA   B 1 1   ? -51.706 -33.946 -14.700 1.00 146.14 ? 1   ALA   B O    1 
ATOM   1814 C  CB   . ALA   B 1 1   ? -51.506 -35.447 -18.014 1.00 145.23 ? 1   ALA   B CB   1 
ATOM   1815 N  N    . ASP   B 1 2   ? -49.973 -34.421 -16.094 1.00 142.56 ? 2   ASP   B N    1 
ATOM   1816 C  CA   . ASP   B 1 2   ? -48.893 -33.980 -15.212 1.00 140.98 ? 2   ASP   B CA   1 
ATOM   1817 C  C    . ASP   B 1 2   ? -48.139 -32.835 -15.875 1.00 134.13 ? 2   ASP   B C    1 
ATOM   1818 O  O    . ASP   B 1 2   ? -47.700 -32.965 -17.023 1.00 134.42 ? 2   ASP   B O    1 
ATOM   1819 C  CB   . ASP   B 1 2   ? -47.902 -35.113 -14.901 1.00 139.57 ? 2   ASP   B CB   1 
ATOM   1820 C  CG   . ASP   B 1 2   ? -48.529 -36.277 -14.126 1.00 144.12 ? 2   ASP   B CG   1 
ATOM   1821 O  OD1  . ASP   B 1 2   ? -49.713 -36.186 -13.714 1.00 148.35 ? 2   ASP   B OD1  1 
ATOM   1822 O  OD2  . ASP   B 1 2   ? -47.805 -37.280 -13.903 1.00 137.48 ? 2   ASP   B OD2  1 
ATOM   1823 N  N    . THR   B 1 3   ? -47.967 -31.728 -15.152 1.00 123.48 ? 3   THR   B N    1 
ATOM   1824 C  CA   . THR   B 1 3   ? -47.294 -30.573 -15.734 1.00 118.54 ? 3   THR   B CA   1 
ATOM   1825 C  C    . THR   B 1 3   ? -45.796 -30.804 -15.818 1.00 110.20 ? 3   THR   B C    1 
ATOM   1826 O  O    . THR   B 1 3   ? -45.187 -31.279 -14.856 1.00 113.92 ? 3   THR   B O    1 
ATOM   1827 C  CB   . THR   B 1 3   ? -47.574 -29.327 -14.918 1.00 115.97 ? 3   THR   B CB   1 
ATOM   1828 O  OG1  . THR   B 1 3   ? -48.958 -29.310 -14.556 1.00 123.14 ? 3   THR   B OG1  1 
ATOM   1829 C  CG2  . THR   B 1 3   ? -47.246 -28.112 -15.742 1.00 109.50 ? 3   THR   B CG2  1 
ATOM   1830 N  N    . ILE   B 1 4   ? -45.204 -30.464 -16.965 1.00 100.87 ? 4   ILE   B N    1 
ATOM   1831 C  CA   . ILE   B 1 4   ? -43.790 -30.725 -17.237 1.00 103.87 ? 4   ILE   B CA   1 
ATOM   1832 C  C    . ILE   B 1 4   ? -43.132 -29.475 -17.788 1.00 101.70 ? 4   ILE   B C    1 
ATOM   1833 O  O    . ILE   B 1 4   ? -43.482 -29.005 -18.876 1.00 103.81 ? 4   ILE   B O    1 
ATOM   1834 C  CB   . ILE   B 1 4   ? -43.565 -31.881 -18.226 1.00 105.10 ? 4   ILE   B CB   1 
ATOM   1835 C  CG1  . ILE   B 1 4   ? -44.032 -33.218 -17.660 1.00 108.61 ? 4   ILE   B CG1  1 
ATOM   1836 C  CG2  . ILE   B 1 4   ? -42.096 -31.953 -18.632 1.00 95.61  ? 4   ILE   B CG2  1 
ATOM   1837 C  CD1  . ILE   B 1 4   ? -43.299 -33.664 -16.499 1.00 93.19  ? 4   ILE   B CD1  1 
ATOM   1838 N  N    . VAL   B 1 5   ? -42.144 -28.973 -17.069 1.00 100.21 ? 5   VAL   B N    1 
ATOM   1839 C  CA   . VAL   B 1 5   ? -41.208 -28.001 -17.595 1.00 94.41  ? 5   VAL   B CA   1 
ATOM   1840 C  C    . VAL   B 1 5   ? -39.878 -28.723 -17.708 1.00 91.90  ? 5   VAL   B C    1 
ATOM   1841 O  O    . VAL   B 1 5   ? -39.509 -29.490 -16.809 1.00 89.26  ? 5   VAL   B O    1 
ATOM   1842 C  CB   . VAL   B 1 5   ? -41.097 -26.773 -16.681 1.00 91.66  ? 5   VAL   B CB   1 
ATOM   1843 C  CG1  . VAL   B 1 5   ? -40.349 -25.690 -17.393 1.00 94.61  ? 5   VAL   B CG1  1 
ATOM   1844 C  CG2  . VAL   B 1 5   ? -42.458 -26.295 -16.246 1.00 93.81  ? 5   VAL   B CG2  1 
ATOM   1845 N  N    . ALA   B 1 6   ? -39.168 -28.503 -18.809 1.00 90.54  ? 6   ALA   B N    1 
ATOM   1846 C  CA   . ALA   B 1 6   ? -37.923 -29.229 -19.013 1.00 84.69  ? 6   ALA   B CA   1 
ATOM   1847 C  C    . ALA   B 1 6   ? -37.055 -28.510 -20.031 1.00 87.40  ? 6   ALA   B C    1 
ATOM   1848 O  O    . ALA   B 1 6   ? -37.557 -27.781 -20.891 1.00 88.15  ? 6   ALA   B O    1 
ATOM   1849 C  CB   . ALA   B 1 6   ? -38.181 -30.659 -19.476 1.00 85.38  ? 6   ALA   B CB   1 
ATOM   1850 N  N    . VAL   B 1 7   ? -35.743 -28.713 -19.904 1.00 86.16  ? 7   VAL   B N    1 
ATOM   1851 C  CA   . VAL   B 1 7   ? -34.768 -28.304 -20.909 1.00 82.46  ? 7   VAL   B CA   1 
ATOM   1852 C  C    . VAL   B 1 7   ? -34.351 -29.561 -21.647 1.00 90.11  ? 7   VAL   B C    1 
ATOM   1853 O  O    . VAL   B 1 7   ? -33.856 -30.512 -21.027 1.00 88.06  ? 7   VAL   B O    1 
ATOM   1854 C  CB   . VAL   B 1 7   ? -33.548 -27.606 -20.291 1.00 72.33  ? 7   VAL   B CB   1 
ATOM   1855 C  CG1  . VAL   B 1 7   ? -32.538 -27.340 -21.339 1.00 74.20  ? 7   VAL   B CG1  1 
ATOM   1856 C  CG2  . VAL   B 1 7   ? -33.932 -26.305 -19.695 1.00 75.38  ? 7   VAL   B CG2  1 
ATOM   1857 N  N    . GLU   B 1 8   ? -34.569 -29.564 -22.964 1.00 91.91  ? 8   GLU   B N    1 
ATOM   1858 C  CA   . GLU   B 1 8   ? -34.381 -30.719 -23.824 1.00 87.02  ? 8   GLU   B CA   1 
ATOM   1859 C  C    . GLU   B 1 8   ? -33.094 -30.568 -24.620 1.00 92.05  ? 8   GLU   B C    1 
ATOM   1860 O  O    . GLU   B 1 8   ? -32.675 -29.460 -24.963 1.00 95.30  ? 8   GLU   B O    1 
ATOM   1861 C  CB   . GLU   B 1 8   ? -35.610 -30.918 -24.743 1.00 88.52  ? 8   GLU   B CB   1 
ATOM   1862 C  CG   . GLU   B 1 8   ? -35.810 -29.938 -25.915 1.00 100.47 ? 8   GLU   B CG   1 
ATOM   1863 C  CD   . GLU   B 1 8   ? -36.781 -30.456 -27.025 1.00 112.69 ? 8   GLU   B CD   1 
ATOM   1864 O  OE1  . GLU   B 1 8   ? -37.634 -31.328 -26.740 1.00 117.73 ? 8   GLU   B OE1  1 
ATOM   1865 O  OE2  . GLU   B 1 8   ? -36.688 -29.993 -28.198 1.00 119.39 ? 8   GLU   B OE2  1 
ATOM   1866 N  N    . LEU   B 1 9   ? -32.443 -31.703 -24.863 1.00 102.44 ? 9   LEU   B N    1 
ATOM   1867 C  CA   . LEU   B 1 9   ? -31.256 -31.818 -25.720 1.00 108.59 ? 9   LEU   B CA   1 
ATOM   1868 C  C    . LEU   B 1 9   ? -31.555 -32.829 -26.847 1.00 116.55 ? 9   LEU   B C    1 
ATOM   1869 O  O    . LEU   B 1 9   ? -31.159 -33.993 -26.723 1.00 118.81 ? 9   LEU   B O    1 
ATOM   1870 C  CB   . LEU   B 1 9   ? -29.999 -32.275 -24.881 1.00 99.43  ? 9   LEU   B CB   1 
ATOM   1871 C  CG   . LEU   B 1 9   ? -29.295 -31.396 -23.833 1.00 95.40  ? 9   LEU   B CG   1 
ATOM   1872 C  CD1  . LEU   B 1 9   ? -30.275 -30.990 -22.764 1.00 97.11  ? 9   LEU   B CD1  1 
ATOM   1873 C  CD2  . LEU   B 1 9   ? -28.068 -32.075 -23.198 1.00 80.21  ? 9   LEU   B CD2  1 
ATOM   1874 N  N    . ASP   B 1 10  ? -32.249 -32.408 -27.931 1.00 111.00 ? 10  ASP   B N    1 
ATOM   1875 C  CA   . ASP   B 1 10  ? -32.444 -33.279 -29.096 1.00 107.83 ? 10  ASP   B CA   1 
ATOM   1876 C  C    . ASP   B 1 10  ? -31.143 -33.485 -29.839 1.00 112.50 ? 10  ASP   B C    1 
ATOM   1877 O  O    . ASP   B 1 10  ? -30.641 -32.576 -30.514 1.00 108.54 ? 10  ASP   B O    1 
ATOM   1878 C  CB   . ASP   B 1 10  ? -33.506 -32.776 -30.064 1.00 112.12 ? 10  ASP   B CB   1 
ATOM   1879 C  CG   . ASP   B 1 10  ? -34.883 -33.019 -29.557 1.00 120.35 ? 10  ASP   B CG   1 
ATOM   1880 O  OD1  . ASP   B 1 10  ? -35.057 -34.041 -28.851 1.00 126.19 ? 10  ASP   B OD1  1 
ATOM   1881 O  OD2  . ASP   B 1 10  ? -35.775 -32.220 -29.858 1.00 118.95 ? 10  ASP   B OD2  1 
ATOM   1882 N  N    . THR   B 1 11  ? -30.615 -34.703 -29.709 1.00 118.85 ? 11  THR   B N    1 
ATOM   1883 C  CA   . THR   B 1 11  ? -29.605 -35.203 -30.626 1.00 120.42 ? 11  THR   B CA   1 
ATOM   1884 C  C    . THR   B 1 11  ? -30.228 -35.599 -31.955 1.00 122.76 ? 11  THR   B C    1 
ATOM   1885 O  O    . THR   B 1 11  ? -29.517 -35.653 -32.967 1.00 115.52 ? 11  THR   B O    1 
ATOM   1886 C  CB   . THR   B 1 11  ? -28.872 -36.401 -30.012 1.00 121.49 ? 11  THR   B CB   1 
ATOM   1887 O  OG1  . THR   B 1 11  ? -29.702 -37.567 -30.099 1.00 128.12 ? 11  THR   B OG1  1 
ATOM   1888 C  CG2  . THR   B 1 11  ? -28.545 -36.154 -28.557 1.00 116.69 ? 11  THR   B CG2  1 
ATOM   1889 N  N    . TYR   B 1 12  ? -31.541 -35.871 -31.977 1.00 122.75 ? 12  TYR   B N    1 
ATOM   1890 C  CA   . TYR   B 1 12  ? -32.211 -36.330 -33.191 1.00 123.74 ? 12  TYR   B CA   1 
ATOM   1891 C  C    . TYR   B 1 12  ? -33.302 -35.334 -33.586 1.00 122.49 ? 12  TYR   B C    1 
ATOM   1892 O  O    . TYR   B 1 12  ? -34.254 -35.111 -32.805 1.00 114.80 ? 12  TYR   B O    1 
ATOM   1893 C  CB   . TYR   B 1 12  ? -32.801 -37.740 -33.005 1.00 128.88 ? 12  TYR   B CB   1 
ATOM   1894 C  CG   . TYR   B 1 12  ? -33.445 -38.301 -34.266 1.00 133.46 ? 12  TYR   B CG   1 
ATOM   1895 C  CD1  . TYR   B 1 12  ? -32.650 -38.686 -35.347 1.00 132.46 ? 12  TYR   B CD1  1 
ATOM   1896 C  CD2  . TYR   B 1 12  ? -34.822 -38.442 -34.386 1.00 133.94 ? 12  TYR   B CD2  1 
ATOM   1897 C  CE1  . TYR   B 1 12  ? -33.207 -39.184 -36.512 1.00 136.60 ? 12  TYR   B CE1  1 
ATOM   1898 C  CE2  . TYR   B 1 12  ? -35.392 -38.945 -35.558 1.00 138.00 ? 12  TYR   B CE2  1 
ATOM   1899 C  CZ   . TYR   B 1 12  ? -34.577 -39.313 -36.616 1.00 140.30 ? 12  TYR   B CZ   1 
ATOM   1900 O  OH   . TYR   B 1 12  ? -35.134 -39.808 -37.780 1.00 144.94 ? 12  TYR   B OH   1 
ATOM   1901 N  N    . PRO   B 1 13  ? -33.175 -34.686 -34.762 1.00 127.20 ? 13  PRO   B N    1 
ATOM   1902 C  CA   . PRO   B 1 13  ? -34.267 -33.862 -35.285 1.00 125.32 ? 13  PRO   B CA   1 
ATOM   1903 C  C    . PRO   B 1 13  ? -35.509 -34.696 -35.519 1.00 126.42 ? 13  PRO   B C    1 
ATOM   1904 O  O    . PRO   B 1 13  ? -35.439 -35.889 -35.812 1.00 124.42 ? 13  PRO   B O    1 
ATOM   1905 C  CB   . PRO   B 1 13  ? -33.706 -33.325 -36.611 1.00 117.94 ? 13  PRO   B CB   1 
ATOM   1906 C  CG   . PRO   B 1 13  ? -32.240 -33.379 -36.459 1.00 111.15 ? 13  PRO   B CG   1 
ATOM   1907 C  CD   . PRO   B 1 13  ? -31.996 -34.620 -35.649 1.00 121.47 ? 13  PRO   B CD   1 
ATOM   1908 N  N    . ASN   B 1 14  ? -36.656 -34.035 -35.418 1.00 128.72 ? 14  ASN   B N    1 
ATOM   1909 C  CA   . ASN   B 1 14  ? -37.957 -34.684 -35.459 1.00 131.22 ? 14  ASN   B CA   1 
ATOM   1910 C  C    . ASN   B 1 14  ? -38.908 -33.780 -36.245 1.00 131.88 ? 14  ASN   B C    1 
ATOM   1911 O  O    . ASN   B 1 14  ? -39.936 -33.355 -35.733 1.00 138.74 ? 14  ASN   B O    1 
ATOM   1912 C  CB   . ASN   B 1 14  ? -38.501 -34.885 -34.042 1.00 135.89 ? 14  ASN   B CB   1 
ATOM   1913 C  CG   . ASN   B 1 14  ? -37.717 -35.899 -33.222 1.00 135.95 ? 14  ASN   B CG   1 
ATOM   1914 O  OD1  . ASN   B 1 14  ? -37.391 -36.995 -33.675 1.00 135.34 ? 14  ASN   B OD1  1 
ATOM   1915 N  ND2  . ASN   B 1 14  ? -37.373 -35.502 -32.012 1.00 130.63 ? 14  ASN   B ND2  1 
ATOM   1916 N  N    . THR   B 1 15  ? -38.563 -33.454 -37.504 1.00 131.88 ? 15  THR   B N    1 
ATOM   1917 C  CA   . THR   B 1 15  ? -39.240 -32.372 -38.235 1.00 130.76 ? 15  THR   B CA   1 
ATOM   1918 C  C    . THR   B 1 15  ? -40.748 -32.568 -38.362 1.00 136.80 ? 15  THR   B C    1 
ATOM   1919 O  O    . THR   B 1 15  ? -41.460 -31.595 -38.649 1.00 134.35 ? 15  THR   B O    1 
ATOM   1920 C  CB   . THR   B 1 15  ? -38.633 -32.205 -39.623 1.00 123.69 ? 15  THR   B CB   1 
ATOM   1921 O  OG1  . THR   B 1 15  ? -38.773 -33.428 -40.353 1.00 133.83 ? 15  THR   B OG1  1 
ATOM   1922 C  CG2  . THR   B 1 15  ? -37.183 -31.877 -39.506 1.00 118.17 ? 15  THR   B CG2  1 
ATOM   1923 N  N    . ASP   B 1 16  ? -41.238 -33.792 -38.128 1.00 143.43 ? 16  ASP   B N    1 
ATOM   1924 C  CA   . ASP   B 1 16  ? -42.676 -34.055 -38.092 1.00 145.19 ? 16  ASP   B CA   1 
ATOM   1925 C  C    . ASP   B 1 16  ? -43.385 -33.409 -36.876 1.00 142.58 ? 16  ASP   B C    1 
ATOM   1926 O  O    . ASP   B 1 16  ? -44.539 -32.972 -37.007 1.00 141.30 ? 16  ASP   B O    1 
ATOM   1927 C  CB   . ASP   B 1 16  ? -42.917 -35.591 -38.253 1.00 148.02 ? 16  ASP   B CB   1 
ATOM   1928 C  CG   . ASP   B 1 16  ? -42.167 -36.483 -37.212 1.00 154.19 ? 16  ASP   B CG   1 
ATOM   1929 O  OD1  . ASP   B 1 16  ? -41.363 -35.980 -36.398 1.00 156.94 ? 16  ASP   B OD1  1 
ATOM   1930 O  OD2  . ASP   B 1 16  ? -42.413 -37.718 -37.202 1.00 150.00 ? 16  ASP   B OD2  1 
ATOM   1931 N  N    . ILE   B 1 17  ? -42.722 -33.281 -35.709 1.00 143.24 ? 17  ILE   B N    1 
ATOM   1932 C  CA   . ILE   B 1 17  ? -43.347 -32.597 -34.564 1.00 139.85 ? 17  ILE   B CA   1 
ATOM   1933 C  C    . ILE   B 1 17  ? -42.906 -31.146 -34.416 1.00 134.40 ? 17  ILE   B C    1 
ATOM   1934 O  O    . ILE   B 1 17  ? -43.468 -30.428 -33.575 1.00 132.94 ? 17  ILE   B O    1 
ATOM   1935 C  CB   . ILE   B 1 17  ? -43.079 -33.287 -33.209 1.00 136.63 ? 17  ILE   B CB   1 
ATOM   1936 C  CG1  . ILE   B 1 17  ? -41.604 -33.215 -32.847 1.00 134.35 ? 17  ILE   B CG1  1 
ATOM   1937 C  CG2  . ILE   B 1 17  ? -43.429 -34.713 -33.292 1.00 137.04 ? 17  ILE   B CG2  1 
ATOM   1938 C  CD1  . ILE   B 1 17  ? -41.326 -33.661 -31.424 1.00 134.34 ? 17  ILE   B CD1  1 
ATOM   1939 N  N    . GLY   B 1 18  ? -41.900 -30.698 -35.158 1.00 128.09 ? 18  GLY   B N    1 
ATOM   1940 C  CA   . GLY   B 1 18  ? -41.441 -29.323 -35.101 1.00 120.85 ? 18  GLY   B CA   1 
ATOM   1941 C  C    . GLY   B 1 18  ? -39.953 -29.153 -34.877 1.00 113.95 ? 18  GLY   B C    1 
ATOM   1942 O  O    . GLY   B 1 18  ? -39.403 -28.115 -35.259 1.00 106.24 ? 18  GLY   B O    1 
ATOM   1943 N  N    . ASP   B 1 19  ? -39.285 -30.137 -34.278 1.00 116.97 ? 19  ASP   B N    1 
ATOM   1944 C  CA   . ASP   B 1 19  ? -37.867 -30.029 -33.946 1.00 116.36 ? 19  ASP   B CA   1 
ATOM   1945 C  C    . ASP   B 1 19  ? -37.075 -29.534 -35.158 1.00 113.42 ? 19  ASP   B C    1 
ATOM   1946 O  O    . ASP   B 1 19  ? -37.306 -29.999 -36.272 1.00 120.15 ? 19  ASP   B O    1 
ATOM   1947 C  CB   . ASP   B 1 19  ? -37.318 -31.396 -33.525 1.00 121.01 ? 19  ASP   B CB   1 
ATOM   1948 C  CG   . ASP   B 1 19  ? -37.475 -31.671 -32.030 1.00 129.89 ? 19  ASP   B CG   1 
ATOM   1949 O  OD1  . ASP   B 1 19  ? -37.590 -30.698 -31.242 1.00 134.94 ? 19  ASP   B OD1  1 
ATOM   1950 O  OD2  . ASP   B 1 19  ? -37.436 -32.872 -31.642 1.00 127.25 ? 19  ASP   B OD2  1 
ATOM   1951 N  N    . PRO   B 1 20  ? -36.152 -28.589 -34.992 1.00 114.59 ? 20  PRO   B N    1 
ATOM   1952 C  CA   . PRO   B 1 20  ? -35.320 -28.184 -36.130 1.00 117.74 ? 20  PRO   B CA   1 
ATOM   1953 C  C    . PRO   B 1 20  ? -34.517 -29.355 -36.664 1.00 121.84 ? 20  PRO   B C    1 
ATOM   1954 O  O    . PRO   B 1 20  ? -34.390 -30.398 -36.020 1.00 122.60 ? 20  PRO   B O    1 
ATOM   1955 C  CB   . PRO   B 1 20  ? -34.405 -27.099 -35.545 1.00 113.61 ? 20  PRO   B CB   1 
ATOM   1956 C  CG   . PRO   B 1 20  ? -35.160 -26.579 -34.394 1.00 113.97 ? 20  PRO   B CG   1 
ATOM   1957 C  CD   . PRO   B 1 20  ? -35.858 -27.778 -33.804 1.00 119.10 ? 20  PRO   B CD   1 
ATOM   1958 N  N    . SER   B 1 21  ? -33.980 -29.171 -37.869 1.00 123.03 ? 21  SER   B N    1 
ATOM   1959 C  CA   . SER   B 1 21  ? -33.158 -30.195 -38.517 1.00 125.71 ? 21  SER   B CA   1 
ATOM   1960 C  C    . SER   B 1 21  ? -31.677 -30.020 -38.168 1.00 129.88 ? 21  SER   B C    1 
ATOM   1961 O  O    . SER   B 1 21  ? -30.821 -29.802 -39.036 1.00 129.99 ? 21  SER   B O    1 
ATOM   1962 C  CB   . SER   B 1 21  ? -33.369 -30.174 -40.028 1.00 124.30 ? 21  SER   B CB   1 
ATOM   1963 O  OG   . SER   B 1 21  ? -34.689 -30.534 -40.370 1.00 126.26 ? 21  SER   B OG   1 
ATOM   1964 N  N    . TYR   B 1 22  ? -31.388 -30.125 -36.874 1.00 124.33 ? 22  TYR   B N    1 
ATOM   1965 C  CA   . TYR   B 1 22  ? -30.021 -30.209 -36.375 1.00 119.96 ? 22  TYR   B CA   1 
ATOM   1966 C  C    . TYR   B 1 22  ? -30.078 -30.493 -34.877 1.00 115.66 ? 22  TYR   B C    1 
ATOM   1967 O  O    . TYR   B 1 22  ? -31.091 -30.204 -34.230 1.00 114.71 ? 22  TYR   B O    1 
ATOM   1968 C  CB   . TYR   B 1 22  ? -29.231 -28.918 -36.664 1.00 120.75 ? 22  TYR   B CB   1 
ATOM   1969 C  CG   . TYR   B 1 22  ? -29.985 -27.633 -36.395 1.00 124.66 ? 22  TYR   B CG   1 
ATOM   1970 C  CD1  . TYR   B 1 22  ? -30.783 -27.044 -37.366 1.00 127.31 ? 22  TYR   B CD1  1 
ATOM   1971 C  CD2  . TYR   B 1 22  ? -29.854 -26.980 -35.188 1.00 125.89 ? 22  TYR   B CD2  1 
ATOM   1972 C  CE1  . TYR   B 1 22  ? -31.459 -25.869 -37.120 1.00 126.44 ? 22  TYR   B CE1  1 
ATOM   1973 C  CE2  . TYR   B 1 22  ? -30.519 -25.807 -34.939 1.00 123.34 ? 22  TYR   B CE2  1 
ATOM   1974 C  CZ   . TYR   B 1 22  ? -31.313 -25.254 -35.902 1.00 124.81 ? 22  TYR   B CZ   1 
ATOM   1975 O  OH   . TYR   B 1 22  ? -31.963 -24.075 -35.624 1.00 132.78 ? 22  TYR   B OH   1 
ATOM   1976 N  N    . PRO   B 1 23  ? -29.015 -31.070 -34.314 1.00 113.14 ? 23  PRO   B N    1 
ATOM   1977 C  CA   . PRO   B 1 23  ? -28.976 -31.286 -32.863 1.00 110.66 ? 23  PRO   B CA   1 
ATOM   1978 C  C    . PRO   B 1 23  ? -29.086 -29.965 -32.116 1.00 108.41 ? 23  PRO   B C    1 
ATOM   1979 O  O    . PRO   B 1 23  ? -28.266 -29.057 -32.276 1.00 107.41 ? 23  PRO   B O    1 
ATOM   1980 C  CB   . PRO   B 1 23  ? -27.621 -31.962 -32.641 1.00 113.63 ? 23  PRO   B CB   1 
ATOM   1981 C  CG   . PRO   B 1 23  ? -26.817 -31.651 -33.865 1.00 113.33 ? 23  PRO   B CG   1 
ATOM   1982 C  CD   . PRO   B 1 23  ? -27.787 -31.540 -34.979 1.00 112.05 ? 23  PRO   B CD   1 
ATOM   1983 N  N    . HIS   B 1 24  ? -30.109 -29.868 -31.286 1.00 105.98 ? 24  HIS   B N    1 
ATOM   1984 C  CA   . HIS   B 1 24  ? -30.490 -28.610 -30.679 1.00 105.85 ? 24  HIS   B CA   1 
ATOM   1985 C  C    . HIS   B 1 24  ? -30.696 -28.791 -29.179 1.00 107.81 ? 24  HIS   B C    1 
ATOM   1986 O  O    . HIS   B 1 24  ? -30.787 -29.912 -28.670 1.00 108.53 ? 24  HIS   B O    1 
ATOM   1987 C  CB   . HIS   B 1 24  ? -31.755 -28.061 -31.373 1.00 106.23 ? 24  HIS   B CB   1 
ATOM   1988 C  CG   . HIS   B 1 24  ? -32.968 -28.949 -31.269 1.00 106.99 ? 24  HIS   B CG   1 
ATOM   1989 N  ND1  . HIS   B 1 24  ? -33.340 -29.809 -32.278 1.00 108.13 ? 24  HIS   B ND1  1 
ATOM   1990 C  CD2  . HIS   B 1 24  ? -33.953 -29.022 -30.339 1.00 102.66 ? 24  HIS   B CD2  1 
ATOM   1991 C  CE1  . HIS   B 1 24  ? -34.462 -30.419 -31.945 1.00 107.83 ? 24  HIS   B CE1  1 
ATOM   1992 N  NE2  . HIS   B 1 24  ? -34.856 -29.959 -30.772 1.00 98.85  ? 24  HIS   B NE2  1 
ATOM   1993 N  N    . ILE   B 1 25  ? -30.713 -27.666 -28.469 1.00 102.25 ? 25  ILE   B N    1 
ATOM   1994 C  CA   . ILE   B 1 25  ? -31.145 -27.579 -27.077 1.00 100.04 ? 25  ILE   B CA   1 
ATOM   1995 C  C    . ILE   B 1 25  ? -32.399 -26.718 -27.067 1.00 94.41  ? 25  ILE   B C    1 
ATOM   1996 O  O    . ILE   B 1 25  ? -32.628 -25.940 -27.999 1.00 100.00 ? 25  ILE   B O    1 
ATOM   1997 C  CB   . ILE   B 1 25  ? -30.009 -27.022 -26.172 1.00 102.18 ? 25  ILE   B CB   1 
ATOM   1998 C  CG1  . ILE   B 1 25  ? -29.601 -25.601 -26.564 1.00 98.60  ? 25  ILE   B CG1  1 
ATOM   1999 C  CG2  . ILE   B 1 25  ? -28.761 -27.866 -26.273 1.00 103.92 ? 25  ILE   B CG2  1 
ATOM   2000 C  CD1  . ILE   B 1 25  ? -28.632 -24.947 -25.593 1.00 87.84  ? 25  ILE   B CD1  1 
ATOM   2001 N  N    . GLY   B 1 26  ? -33.239 -26.877 -26.054 1.00 84.53  ? 26  GLY   B N    1 
ATOM   2002 C  CA   . GLY   B 1 26  ? -34.513 -26.182 -26.154 1.00 88.70  ? 26  GLY   B CA   1 
ATOM   2003 C  C    . GLY   B 1 26  ? -35.341 -26.250 -24.891 1.00 91.29  ? 26  GLY   B C    1 
ATOM   2004 O  O    . GLY   B 1 26  ? -35.110 -27.072 -24.003 1.00 96.00  ? 26  GLY   B O    1 
ATOM   2005 N  N    . ILE   B 1 27  ? -36.350 -25.387 -24.844 1.00 87.31  ? 27  ILE   B N    1 
ATOM   2006 C  CA   . ILE   B 1 27  ? -37.122 -25.129 -23.633 1.00 91.59  ? 27  ILE   B CA   1 
ATOM   2007 C  C    . ILE   B 1 27  ? -38.530 -25.672 -23.869 1.00 94.84  ? 27  ILE   B C    1 
ATOM   2008 O  O    . ILE   B 1 27  ? -39.222 -25.206 -24.780 1.00 102.46 ? 27  ILE   B O    1 
ATOM   2009 C  CB   . ILE   B 1 27  ? -37.180 -23.619 -23.330 1.00 97.21  ? 27  ILE   B CB   1 
ATOM   2010 C  CG1  . ILE   B 1 27  ? -35.795 -22.927 -23.220 1.00 88.32  ? 27  ILE   B CG1  1 
ATOM   2011 C  CG2  . ILE   B 1 27  ? -37.975 -23.371 -22.043 1.00 99.14  ? 27  ILE   B CG2  1 
ATOM   2012 C  CD1  . ILE   B 1 27  ? -34.875 -23.392 -22.146 1.00 79.68  ? 27  ILE   B CD1  1 
ATOM   2013 N  N    . ASP   B 1 28  ? -38.985 -26.631 -23.062 1.00 95.95  ? 28  ASP   B N    1 
ATOM   2014 C  CA   . ASP   B 1 28  ? -40.315 -27.218 -23.268 1.00 102.10 ? 28  ASP   B CA   1 
ATOM   2015 C  C    . ASP   B 1 28  ? -41.246 -26.853 -22.126 1.00 102.13 ? 28  ASP   B C    1 
ATOM   2016 O  O    . ASP   B 1 28  ? -41.010 -27.240 -20.974 1.00 99.62  ? 28  ASP   B O    1 
ATOM   2017 C  CB   . ASP   B 1 28  ? -40.289 -28.747 -23.407 1.00 106.36 ? 28  ASP   B CB   1 
ATOM   2018 C  CG   . ASP   B 1 28  ? -39.290 -29.240 -24.442 1.00 108.31 ? 28  ASP   B CG   1 
ATOM   2019 O  OD1  . ASP   B 1 28  ? -39.023 -28.519 -25.436 1.00 105.26 ? 28  ASP   B OD1  1 
ATOM   2020 O  OD2  . ASP   B 1 28  ? -38.833 -30.396 -24.295 1.00 111.51 ? 28  ASP   B OD2  1 
ATOM   2021 N  N    . ILE   B 1 29  ? -42.340 -26.162 -22.439 1.00 100.30 ? 29  ILE   B N    1 
ATOM   2022 C  CA   . ILE   B 1 29  ? -43.301 -25.766 -21.372 1.00 100.80 ? 29  ILE   B CA   1 
ATOM   2023 C  C    . ILE   B 1 29  ? -44.649 -26.428 -21.646 1.00 96.88  ? 29  ILE   B C    1 
ATOM   2024 O  O    . ILE   B 1 29  ? -45.412 -25.874 -22.443 1.00 96.78  ? 29  ILE   B O    1 
ATOM   2025 C  CB   . ILE   B 1 29  ? -43.432 -24.237 -21.303 1.00 107.88 ? 29  ILE   B CB   1 
ATOM   2026 C  CG1  . ILE   B 1 29  ? -42.060 -23.564 -21.289 1.00 102.55 ? 29  ILE   B CG1  1 
ATOM   2027 C  CG2  . ILE   B 1 29  ? -44.265 -23.833 -20.103 1.00 102.81 ? 29  ILE   B CG2  1 
ATOM   2028 C  CD1  . ILE   B 1 29  ? -41.157 -24.059 -20.194 1.00 97.42  ? 29  ILE   B CD1  1 
ATOM   2029 N  N    . LYS   B 1 30  ? -44.856 -27.614 -21.065 1.00 102.94 ? 30  LYS   B N    1 
ATOM   2030 C  CA   . LYS   B 1 30  ? -46.087 -28.454 -21.143 1.00 109.06 ? 30  LYS   B CA   1 
ATOM   2031 C  C    . LYS   B 1 30  ? -46.303 -29.032 -22.545 1.00 111.50 ? 30  LYS   B C    1 
ATOM   2032 O  O    . LYS   B 1 30  ? -47.424 -29.484 -22.802 1.00 111.38 ? 30  LYS   B O    1 
ATOM   2033 C  CB   . LYS   B 1 30  ? -47.353 -27.720 -20.687 1.00 102.78 ? 30  LYS   B CB   1 
ATOM   2034 C  CG   . LYS   B 1 30  ? -47.219 -26.828 -19.463 1.00 103.90 ? 30  LYS   B CG   1 
ATOM   2035 C  CD   . LYS   B 1 30  ? -48.320 -25.792 -19.371 1.00 109.20 ? 30  LYS   B CD   1 
ATOM   2036 C  CE   . LYS   B 1 30  ? -49.309 -26.066 -18.260 1.00 108.20 ? 30  LYS   B CE   1 
ATOM   2037 N  NZ   . LYS   B 1 30  ? -50.174 -24.891 -18.008 1.00 101.79 ? 30  LYS   B NZ   1 
ATOM   2038 N  N    . SER   B 1 31  ? -45.274 -29.070 -23.391 1.00 106.30 ? 31  SER   B N    1 
ATOM   2039 C  CA   . SER   B 1 31  ? -45.433 -29.595 -24.769 1.00 108.08 ? 31  SER   B CA   1 
ATOM   2040 C  C    . SER   B 1 31  ? -44.052 -29.884 -25.342 1.00 106.24 ? 31  SER   B C    1 
ATOM   2041 O  O    . SER   B 1 31  ? -43.207 -28.988 -25.267 1.00 101.82 ? 31  SER   B O    1 
ATOM   2042 C  CB   . SER   B 1 31  ? -46.176 -28.612 -25.635 1.00 111.90 ? 31  SER   B CB   1 
ATOM   2043 O  OG   . SER   B 1 31  ? -45.289 -27.861 -26.456 1.00 111.34 ? 31  SER   B OG   1 
ATOM   2044 N  N    . VAL   B 1 32  ? -43.870 -31.071 -25.914 1.00 110.30 ? 32  VAL   B N    1 
ATOM   2045 C  CA   . VAL   B 1 32  ? -42.556 -31.437 -26.512 1.00 112.47 ? 32  VAL   B CA   1 
ATOM   2046 C  C    . VAL   B 1 32  ? -42.259 -30.356 -27.547 1.00 110.36 ? 32  VAL   B C    1 
ATOM   2047 O  O    . VAL   B 1 32  ? -41.148 -30.331 -28.082 1.00 108.52 ? 32  VAL   B O    1 
ATOM   2048 C  CB   . VAL   B 1 32  ? -42.569 -32.836 -27.143 1.00 114.92 ? 32  VAL   B CB   1 
ATOM   2049 C  CG1  . VAL   B 1 32  ? -43.923 -33.501 -26.984 1.00 129.02 ? 32  VAL   B CG1  1 
ATOM   2050 C  CG2  . VAL   B 1 32  ? -42.159 -32.781 -28.603 1.00 117.26 ? 32  VAL   B CG2  1 
ATOM   2051 N  N    . ARG   B 1 33  ? -43.270 -29.553 -27.872 1.00 114.89 ? 33  ARG   B N    1 
ATOM   2052 C  CA   . ARG   B 1 33  ? -43.042 -28.394 -28.714 1.00 118.83 ? 33  ARG   B CA   1 
ATOM   2053 C  C    . ARG   B 1 33  ? -42.234 -27.346 -27.963 1.00 108.19 ? 33  ARG   B C    1 
ATOM   2054 O  O    . ARG   B 1 33  ? -42.745 -26.648 -27.074 1.00 100.94 ? 33  ARG   B O    1 
ATOM   2055 C  CB   . ARG   B 1 33  ? -44.377 -27.869 -29.219 1.00 126.20 ? 33  ARG   B CB   1 
ATOM   2056 C  CG   . ARG   B 1 33  ? -44.910 -28.889 -30.186 1.00 133.97 ? 33  ARG   B CG   1 
ATOM   2057 C  CD   . ARG   B 1 33  ? -46.195 -28.552 -30.854 1.00 138.61 ? 33  ARG   B CD   1 
ATOM   2058 N  NE   . ARG   B 1 33  ? -46.501 -29.673 -31.725 1.00 146.09 ? 33  ARG   B NE   1 
ATOM   2059 C  CZ   . ARG   B 1 33  ? -46.011 -29.765 -32.961 1.00 146.05 ? 33  ARG   B CZ   1 
ATOM   2060 N  NH1  . ARG   B 1 33  ? -45.188 -28.816 -33.418 1.00 134.34 ? 33  ARG   B NH1  1 
ATOM   2061 N  NH2  . ARG   B 1 33  ? -46.300 -30.814 -33.727 1.00 145.81 ? 33  ARG   B NH2  1 
ATOM   2062 N  N    . SER   B 1 34  ? -40.962 -27.251 -28.345 1.00 107.61 ? 34  SER   B N    1 
ATOM   2063 C  CA   . SER   B 1 34  ? -40.042 -26.313 -27.728 1.00 101.86 ? 34  SER   B CA   1 
ATOM   2064 C  C    . SER   B 1 34  ? -40.484 -24.903 -28.048 1.00 95.91  ? 34  SER   B C    1 
ATOM   2065 O  O    . SER   B 1 34  ? -40.782 -24.597 -29.202 1.00 96.59  ? 34  SER   B O    1 
ATOM   2066 C  CB   . SER   B 1 34  ? -38.625 -26.543 -28.246 1.00 96.65  ? 34  SER   B CB   1 
ATOM   2067 O  OG   . SER   B 1 34  ? -38.160 -27.821 -27.878 1.00 98.13  ? 34  SER   B OG   1 
ATOM   2068 N  N    . LYS   B 1 35  ? -40.544 -24.050 -27.025 1.00 92.53  ? 35  LYS   B N    1 
ATOM   2069 C  CA   . LYS   B 1 35  ? -40.864 -22.649 -27.241 1.00 91.37  ? 35  LYS   B CA   1 
ATOM   2070 C  C    . LYS   B 1 35  ? -39.646 -21.816 -27.675 1.00 97.41  ? 35  LYS   B C    1 
ATOM   2071 O  O    . LYS   B 1 35  ? -39.815 -20.716 -28.222 1.00 100.59 ? 35  LYS   B O    1 
ATOM   2072 C  CB   . LYS   B 1 35  ? -41.494 -22.074 -25.974 1.00 90.65  ? 35  LYS   B CB   1 
ATOM   2073 C  CG   . LYS   B 1 35  ? -42.453 -22.979 -25.206 1.00 89.37  ? 35  LYS   B CG   1 
ATOM   2074 C  CD   . LYS   B 1 35  ? -43.774 -23.204 -25.886 1.00 88.06  ? 35  LYS   B CD   1 
ATOM   2075 C  CE   . LYS   B 1 35  ? -44.610 -24.150 -25.042 1.00 92.42  ? 35  LYS   B CE   1 
ATOM   2076 N  NZ   . LYS   B 1 35  ? -46.079 -24.064 -25.273 1.00 89.53  ? 35  LYS   B NZ   1 
ATOM   2077 N  N    . LYS   B 1 36  ? -38.428 -22.305 -27.461 1.00 92.08  ? 36  LYS   B N    1 
ATOM   2078 C  CA   . LYS   B 1 36  ? -37.256 -21.661 -28.036 1.00 91.27  ? 36  LYS   B CA   1 
ATOM   2079 C  C    . LYS   B 1 36  ? -36.187 -22.730 -28.154 1.00 92.85  ? 36  LYS   B C    1 
ATOM   2080 O  O    . LYS   B 1 36  ? -36.131 -23.637 -27.319 1.00 90.45  ? 36  LYS   B O    1 
ATOM   2081 C  CB   . LYS   B 1 36  ? -36.793 -20.483 -27.169 1.00 98.36  ? 36  LYS   B CB   1 
ATOM   2082 C  CG   . LYS   B 1 36  ? -35.584 -19.699 -27.663 1.00 97.71  ? 36  LYS   B CG   1 
ATOM   2083 C  CD   . LYS   B 1 36  ? -35.948 -18.930 -28.890 1.00 109.41 ? 36  LYS   B CD   1 
ATOM   2084 C  CE   . LYS   B 1 36  ? -37.005 -17.866 -28.575 1.00 115.20 ? 36  LYS   B CE   1 
ATOM   2085 N  NZ   . LYS   B 1 36  ? -36.492 -16.715 -27.751 1.00 121.48 ? 36  LYS   B NZ   1 
ATOM   2086 N  N    . THR   B 1 37  ? -35.393 -22.663 -29.222 1.00 95.20  ? 37  THR   B N    1 
ATOM   2087 C  CA   . THR   B 1 37  ? -34.378 -23.676 -29.488 1.00 95.76  ? 37  THR   B CA   1 
ATOM   2088 C  C    . THR   B 1 37  ? -33.125 -22.987 -29.982 1.00 95.96  ? 37  THR   B C    1 
ATOM   2089 O  O    . THR   B 1 37  ? -33.194 -21.862 -30.490 1.00 95.71  ? 37  THR   B O    1 
ATOM   2090 C  CB   . THR   B 1 37  ? -34.765 -24.677 -30.578 1.00 100.52 ? 37  THR   B CB   1 
ATOM   2091 O  OG1  . THR   B 1 37  ? -34.896 -23.973 -31.821 1.00 105.16 ? 37  THR   B OG1  1 
ATOM   2092 C  CG2  . THR   B 1 37  ? -36.077 -25.395 -30.254 1.00 99.18  ? 37  THR   B CG2  1 
ATOM   2093 N  N    . ALA   B 1 38  ? -31.992 -23.700 -29.881 1.00 97.16  ? 38  ALA   B N    1 
ATOM   2094 C  CA   . ALA   B 1 38  ? -30.708 -23.211 -30.386 1.00 100.90 ? 38  ALA   B CA   1 
ATOM   2095 C  C    . ALA   B 1 38  ? -29.819 -24.352 -30.878 1.00 105.36 ? 38  ALA   B C    1 
ATOM   2096 O  O    . ALA   B 1 38  ? -29.898 -25.485 -30.386 1.00 104.12 ? 38  ALA   B O    1 
ATOM   2097 C  CB   . ALA   B 1 38  ? -29.947 -22.412 -29.334 1.00 97.83  ? 38  ALA   B CB   1 
ATOM   2098 N  N    . LYS   B 1 39  ? -28.957 -24.026 -31.854 1.00 109.03 ? 39  LYS   B N    1 
ATOM   2099 C  CA   . LYS   B 1 39  ? -28.136 -25.027 -32.535 1.00 110.86 ? 39  LYS   B CA   1 
ATOM   2100 C  C    . LYS   B 1 39  ? -27.037 -25.493 -31.606 1.00 108.45 ? 39  LYS   B C    1 
ATOM   2101 O  O    . LYS   B 1 39  ? -26.357 -24.682 -30.976 1.00 100.88 ? 39  LYS   B O    1 
ATOM   2102 C  CB   . LYS   B 1 39  ? -27.497 -24.473 -33.829 1.00 119.45 ? 39  LYS   B CB   1 
ATOM   2103 C  CG   . LYS   B 1 39  ? -26.746 -25.534 -34.715 1.00 117.88 ? 39  LYS   B CG   1 
ATOM   2104 C  CD   . LYS   B 1 39  ? -26.200 -25.010 -36.066 1.00 121.48 ? 39  LYS   B CD   1 
ATOM   2105 C  CE   . LYS   B 1 39  ? -24.663 -24.774 -36.004 1.00 127.91 ? 39  LYS   B CE   1 
ATOM   2106 N  NZ   . LYS   B 1 39  ? -23.896 -24.931 -37.293 1.00 132.81 ? 39  LYS   B NZ   1 
ATOM   2107 N  N    . TRP   B 1 40  ? -26.846 -26.806 -31.552 1.00 111.59 ? 40  TRP   B N    1 
ATOM   2108 C  CA   . TRP   B 1 40  ? -25.874 -27.423 -30.661 1.00 111.99 ? 40  TRP   B CA   1 
ATOM   2109 C  C    . TRP   B 1 40  ? -24.993 -28.325 -31.513 1.00 112.29 ? 40  TRP   B C    1 
ATOM   2110 O  O    . TRP   B 1 40  ? -25.471 -29.335 -32.040 1.00 110.24 ? 40  TRP   B O    1 
ATOM   2111 C  CB   . TRP   B 1 40  ? -26.607 -28.206 -29.564 1.00 111.05 ? 40  TRP   B CB   1 
ATOM   2112 C  CG   . TRP   B 1 40  ? -25.792 -29.137 -28.697 1.00 111.74 ? 40  TRP   B CG   1 
ATOM   2113 C  CD1  . TRP   B 1 40  ? -24.481 -28.998 -28.297 1.00 111.39 ? 40  TRP   B CD1  1 
ATOM   2114 C  CD2  . TRP   B 1 40  ? -26.248 -30.369 -28.142 1.00 104.85 ? 40  TRP   B CD2  1 
ATOM   2115 N  NE1  . TRP   B 1 40  ? -24.109 -30.073 -27.514 1.00 101.07 ? 40  TRP   B NE1  1 
ATOM   2116 C  CE2  . TRP   B 1 40  ? -25.177 -30.925 -27.412 1.00 101.88 ? 40  TRP   B CE2  1 
ATOM   2117 C  CE3  . TRP   B 1 40  ? -27.464 -31.052 -28.185 1.00 97.33  ? 40  TRP   B CE3  1 
ATOM   2118 C  CZ2  . TRP   B 1 40  ? -25.295 -32.122 -26.741 1.00 102.33 ? 40  TRP   B CZ2  1 
ATOM   2119 C  CZ3  . TRP   B 1 40  ? -27.574 -32.229 -27.524 1.00 92.76  ? 40  TRP   B CZ3  1 
ATOM   2120 C  CH2  . TRP   B 1 40  ? -26.502 -32.762 -26.815 1.00 99.82  ? 40  TRP   B CH2  1 
ATOM   2121 N  N    . ASN   B 1 41  ? -23.725 -27.944 -31.693 1.00 114.14 ? 41  ASN   B N    1 
ATOM   2122 C  CA   . ASN   B 1 41  ? -22.784 -28.891 -32.283 1.00 120.97 ? 41  ASN   B CA   1 
ATOM   2123 C  C    . ASN   B 1 41  ? -22.437 -29.969 -31.252 1.00 117.23 ? 41  ASN   B C    1 
ATOM   2124 O  O    . ASN   B 1 41  ? -21.452 -29.842 -30.515 1.00 113.07 ? 41  ASN   B O    1 
ATOM   2125 C  CB   . ASN   B 1 41  ? -21.509 -28.199 -32.801 1.00 128.05 ? 41  ASN   B CB   1 
ATOM   2126 C  CG   . ASN   B 1 41  ? -21.744 -27.359 -34.064 1.00 132.88 ? 41  ASN   B CG   1 
ATOM   2127 O  OD1  . ASN   B 1 41  ? -22.502 -27.741 -34.965 1.00 130.61 ? 41  ASN   B OD1  1 
ATOM   2128 N  ND2  . ASN   B 1 41  ? -21.042 -26.231 -34.152 1.00 137.26 ? 41  ASN   B ND2  1 
ATOM   2129 N  N    . MET   B 1 42  ? -23.262 -31.017 -31.186 1.00 114.98 ? 42  MET   B N    1 
ATOM   2130 C  CA   . MET   B 1 42  ? -23.056 -32.142 -30.277 1.00 109.35 ? 42  MET   B CA   1 
ATOM   2131 C  C    . MET   B 1 42  ? -21.721 -32.837 -30.541 1.00 116.50 ? 42  MET   B C    1 
ATOM   2132 O  O    . MET   B 1 42  ? -21.224 -32.857 -31.668 1.00 128.44 ? 42  MET   B O    1 
ATOM   2133 C  CB   . MET   B 1 42  ? -24.221 -33.118 -30.438 1.00 105.14 ? 42  MET   B CB   1 
ATOM   2134 C  CG   . MET   B 1 42  ? -24.396 -34.100 -29.315 1.00 111.53 ? 42  MET   B CG   1 
ATOM   2135 S  SD   . MET   B 1 42  ? -23.623 -35.671 -29.684 1.00 124.14 ? 42  MET   B SD   1 
ATOM   2136 C  CE   . MET   B 1 42  ? -24.924 -36.378 -30.705 1.00 119.22 ? 42  MET   B CE   1 
ATOM   2137 N  N    . GLN   B 1 43  ? -21.119 -33.404 -29.492 1.00 108.76 ? 43  GLN   B N    1 
ATOM   2138 C  CA   . GLN   B 1 43  ? -19.858 -34.131 -29.627 1.00 109.37 ? 43  GLN   B CA   1 
ATOM   2139 C  C    . GLN   B 1 43  ? -20.079 -35.568 -29.191 1.00 111.79 ? 43  GLN   B C    1 
ATOM   2140 O  O    . GLN   B 1 43  ? -20.452 -35.824 -28.042 1.00 117.82 ? 43  GLN   B O    1 
ATOM   2141 C  CB   . GLN   B 1 43  ? -18.719 -33.494 -28.820 1.00 107.94 ? 43  GLN   B CB   1 
ATOM   2142 C  CG   . GLN   B 1 43  ? -18.217 -32.145 -29.366 1.00 108.71 ? 43  GLN   B CG   1 
ATOM   2143 C  CD   . GLN   B 1 43  ? -16.830 -31.744 -28.845 1.00 119.13 ? 43  GLN   B CD   1 
ATOM   2144 O  OE1  . GLN   B 1 43  ? -15.981 -32.600 -28.577 1.00 127.13 ? 43  GLN   B OE1  1 
ATOM   2145 N  NE2  . GLN   B 1 43  ? -16.597 -30.439 -28.706 1.00 113.59 ? 43  GLN   B NE2  1 
ATOM   2146 N  N    . ASN   B 1 44  ? -19.863 -36.498 -30.106 1.00 110.03 ? 44  ASN   B N    1 
ATOM   2147 C  CA   . ASN   B 1 44  ? -20.027 -37.901 -29.780 1.00 112.59 ? 44  ASN   B CA   1 
ATOM   2148 C  C    . ASN   B 1 44  ? -18.835 -38.352 -28.948 1.00 120.20 ? 44  ASN   B C    1 
ATOM   2149 O  O    . ASN   B 1 44  ? -17.681 -38.030 -29.270 1.00 118.77 ? 44  ASN   B O    1 
ATOM   2150 C  CB   . ASN   B 1 44  ? -20.167 -38.730 -31.058 1.00 112.14 ? 44  ASN   B CB   1 
ATOM   2151 C  CG   . ASN   B 1 44  ? -20.371 -40.226 -30.792 1.00 118.09 ? 44  ASN   B CG   1 
ATOM   2152 O  OD1  . ASN   B 1 44  ? -19.777 -40.809 -29.893 1.00 122.18 ? 44  ASN   B OD1  1 
ATOM   2153 N  ND2  . ASN   B 1 44  ? -21.250 -40.839 -31.565 1.00 119.01 ? 44  ASN   B ND2  1 
ATOM   2154 N  N    . GLY   B 1 45  ? -19.130 -39.071 -27.860 1.00 120.70 ? 45  GLY   B N    1 
ATOM   2155 C  CA   . GLY   B 1 45  ? -18.116 -39.748 -27.067 1.00 118.80 ? 45  GLY   B CA   1 
ATOM   2156 C  C    . GLY   B 1 45  ? -17.289 -38.834 -26.195 1.00 116.23 ? 45  GLY   B C    1 
ATOM   2157 O  O    . GLY   B 1 45  ? -16.176 -39.198 -25.795 1.00 115.81 ? 45  GLY   B O    1 
ATOM   2158 N  N    . LYS   B 1 46  ? -17.797 -37.650 -25.896 1.00 110.44 ? 46  LYS   B N    1 
ATOM   2159 C  CA   . LYS   B 1 46  ? -17.067 -36.686 -25.102 1.00 101.59 ? 46  LYS   B CA   1 
ATOM   2160 C  C    . LYS   B 1 46  ? -17.970 -36.277 -23.955 1.00 99.68  ? 46  LYS   B C    1 
ATOM   2161 O  O    . LYS   B 1 46  ? -19.200 -36.272 -24.094 1.00 99.19  ? 46  LYS   B O    1 
ATOM   2162 C  CB   . LYS   B 1 46  ? -16.670 -35.490 -25.952 1.00 105.10 ? 46  LYS   B CB   1 
ATOM   2163 C  CG   . LYS   B 1 46  ? -15.692 -35.848 -27.057 1.00 112.57 ? 46  LYS   B CG   1 
ATOM   2164 C  CD   . LYS   B 1 46  ? -14.253 -35.482 -26.717 1.00 120.56 ? 46  LYS   B CD   1 
ATOM   2165 C  CE   . LYS   B 1 46  ? -13.298 -35.971 -27.809 1.00 117.27 ? 46  LYS   B CE   1 
ATOM   2166 N  NZ   . LYS   B 1 46  ? -12.660 -37.278 -27.482 1.00 109.58 ? 46  LYS   B NZ   1 
ATOM   2167 N  N    . VAL   B 1 47  ? -17.370 -35.969 -22.816 1.00 92.92  ? 47  VAL   B N    1 
ATOM   2168 C  CA   . VAL   B 1 47  ? -18.163 -35.620 -21.646 1.00 91.57  ? 47  VAL   B CA   1 
ATOM   2169 C  C    . VAL   B 1 47  ? -18.492 -34.134 -21.714 1.00 93.56  ? 47  VAL   B C    1 
ATOM   2170 O  O    . VAL   B 1 47  ? -17.596 -33.299 -21.873 1.00 95.23  ? 47  VAL   B O    1 
ATOM   2171 C  CB   . VAL   B 1 47  ? -17.417 -35.964 -20.348 1.00 89.25  ? 47  VAL   B CB   1 
ATOM   2172 C  CG1  . VAL   B 1 47  ? -18.235 -35.548 -19.161 1.00 88.37  ? 47  VAL   B CG1  1 
ATOM   2173 C  CG2  . VAL   B 1 47  ? -17.109 -37.436 -20.260 1.00 86.49  ? 47  VAL   B CG2  1 
ATOM   2174 N  N    . GLY   B 1 48  ? -19.778 -33.796 -21.591 1.00 89.77  ? 48  GLY   B N    1 
ATOM   2175 C  CA   . GLY   B 1 48  ? -20.209 -32.422 -21.685 1.00 88.26  ? 48  GLY   B CA   1 
ATOM   2176 C  C    . GLY   B 1 48  ? -21.058 -32.025 -20.492 1.00 89.27  ? 48  GLY   B C    1 
ATOM   2177 O  O    . GLY   B 1 48  ? -21.498 -32.863 -19.716 1.00 89.85  ? 48  GLY   B O    1 
ATOM   2178 N  N    . THR   B 1 49  ? -21.293 -30.719 -20.370 1.00 91.12  ? 49  THR   B N    1 
ATOM   2179 C  CA   . THR   B 1 49  ? -21.865 -30.138 -19.162 1.00 88.54  ? 49  THR   B CA   1 
ATOM   2180 C  C    . THR   B 1 49  ? -22.993 -29.193 -19.499 1.00 84.81  ? 49  THR   B C    1 
ATOM   2181 O  O    . THR   B 1 49  ? -22.801 -28.253 -20.271 1.00 91.86  ? 49  THR   B O    1 
ATOM   2182 C  CB   . THR   B 1 49  ? -20.838 -29.344 -18.376 1.00 101.97 ? 49  THR   B CB   1 
ATOM   2183 O  OG1  . THR   B 1 49  ? -19.745 -30.190 -18.003 1.00 122.78 ? 49  THR   B OG1  1 
ATOM   2184 C  CG2  . THR   B 1 49  ? -21.499 -28.779 -17.141 1.00 98.30  ? 49  THR   B CG2  1 
ATOM   2185 N  N    . ALA   B 1 50  ? -24.135 -29.390 -18.861 1.00 83.21  ? 50  ALA   B N    1 
ATOM   2186 C  CA   . ALA   B 1 50  ? -25.298 -28.534 -19.038 1.00 81.07  ? 50  ALA   B CA   1 
ATOM   2187 C  C    . ALA   B 1 50  ? -25.573 -27.751 -17.758 1.00 78.07  ? 50  ALA   B C    1 
ATOM   2188 O  O    . ALA   B 1 50  ? -25.586 -28.321 -16.667 1.00 83.43  ? 50  ALA   B O    1 
ATOM   2189 C  CB   . ALA   B 1 50  ? -26.511 -29.371 -19.427 1.00 73.02  ? 50  ALA   B CB   1 
ATOM   2190 N  N    . HIS   B 1 51  ? -25.785 -26.451 -17.887 1.00 71.52  ? 51  HIS   B N    1 
ATOM   2191 C  CA   . HIS   B 1 51  ? -26.150 -25.593 -16.769 1.00 78.58  ? 51  HIS   B CA   1 
ATOM   2192 C  C    . HIS   B 1 51  ? -27.546 -25.045 -17.019 1.00 76.97  ? 51  HIS   B C    1 
ATOM   2193 O  O    . HIS   B 1 51  ? -27.778 -24.440 -18.059 1.00 83.22  ? 51  HIS   B O    1 
ATOM   2194 C  CB   . HIS   B 1 51  ? -25.170 -24.418 -16.633 1.00 87.84  ? 51  HIS   B CB   1 
ATOM   2195 C  CG   . HIS   B 1 51  ? -23.770 -24.807 -16.254 1.00 91.86  ? 51  HIS   B CG   1 
ATOM   2196 N  ND1  . HIS   B 1 51  ? -23.393 -25.089 -14.958 1.00 93.95  ? 51  HIS   B ND1  1 
ATOM   2197 C  CD2  . HIS   B 1 51  ? -22.666 -24.999 -17.018 1.00 93.44  ? 51  HIS   B CD2  1 
ATOM   2198 C  CE1  . HIS   B 1 51  ? -22.109 -25.406 -14.934 1.00 100.47 ? 51  HIS   B CE1  1 
ATOM   2199 N  NE2  . HIS   B 1 51  ? -21.646 -25.361 -16.171 1.00 98.21  ? 51  HIS   B NE2  1 
ATOM   2200 N  N    . ILE   B 1 52  ? -28.471 -25.246 -16.083 1.00 76.38  ? 52  ILE   B N    1 
ATOM   2201 C  CA   . ILE   B 1 52  ? -29.816 -24.678 -16.157 1.00 73.27  ? 52  ILE   B CA   1 
ATOM   2202 C  C    . ILE   B 1 52  ? -29.962 -23.707 -15.000 1.00 76.72  ? 52  ILE   B C    1 
ATOM   2203 O  O    . ILE   B 1 52  ? -29.526 -24.009 -13.883 1.00 80.31  ? 52  ILE   B O    1 
ATOM   2204 C  CB   . ILE   B 1 52  ? -30.948 -25.723 -16.064 1.00 70.89  ? 52  ILE   B CB   1 
ATOM   2205 C  CG1  . ILE   B 1 52  ? -30.952 -26.715 -17.218 1.00 67.74  ? 52  ILE   B CG1  1 
ATOM   2206 C  CG2  . ILE   B 1 52  ? -32.275 -25.032 -15.928 1.00 72.29  ? 52  ILE   B CG2  1 
ATOM   2207 C  CD1  . ILE   B 1 52  ? -30.140 -27.942 -16.960 1.00 69.43  ? 52  ILE   B CD1  1 
ATOM   2208 N  N    . ILE   B 1 53  ? -30.596 -22.561 -15.251 1.00 75.18  ? 53  ILE   B N    1 
ATOM   2209 C  CA   . ILE   B 1 53  ? -30.658 -21.463 -14.289 1.00 69.74  ? 53  ILE   B CA   1 
ATOM   2210 C  C    . ILE   B 1 53  ? -31.916 -20.639 -14.547 1.00 72.67  ? 53  ILE   B C    1 
ATOM   2211 O  O    . ILE   B 1 53  ? -32.269 -20.370 -15.693 1.00 81.98  ? 53  ILE   B O    1 
ATOM   2212 C  CB   . ILE   B 1 53  ? -29.365 -20.615 -14.357 1.00 70.95  ? 53  ILE   B CB   1 
ATOM   2213 C  CG1  . ILE   B 1 53  ? -29.151 -20.030 -15.735 1.00 79.86  ? 53  ILE   B CG1  1 
ATOM   2214 C  CG2  . ILE   B 1 53  ? -28.096 -21.404 -14.071 1.00 82.12  ? 53  ILE   B CG2  1 
ATOM   2215 C  CD1  . ILE   B 1 53  ? -27.988 -19.038 -15.798 1.00 87.42  ? 53  ILE   B CD1  1 
ATOM   2216 N  N    . TYR   B 1 54  ? -32.603 -20.245 -13.484 1.00 76.41  ? 54  TYR   B N    1 
ATOM   2217 C  CA   . TYR   B 1 54  ? -33.800 -19.413 -13.570 1.00 79.37  ? 54  TYR   B CA   1 
ATOM   2218 C  C    . TYR   B 1 54  ? -34.003 -18.656 -12.264 1.00 85.57  ? 54  TYR   B C    1 
ATOM   2219 O  O    . TYR   B 1 54  ? -33.856 -19.232 -11.187 1.00 85.97  ? 54  TYR   B O    1 
ATOM   2220 C  CB   . TYR   B 1 54  ? -35.030 -20.266 -13.862 1.00 78.16  ? 54  TYR   B CB   1 
ATOM   2221 C  CG   . TYR   B 1 54  ? -36.392 -19.618 -13.638 1.00 87.87  ? 54  TYR   B CG   1 
ATOM   2222 C  CD1  . TYR   B 1 54  ? -36.948 -19.526 -12.363 1.00 80.78  ? 54  TYR   B CD1  1 
ATOM   2223 C  CD2  . TYR   B 1 54  ? -37.122 -19.101 -14.699 1.00 93.80  ? 54  TYR   B CD2  1 
ATOM   2224 C  CE1  . TYR   B 1 54  ? -38.167 -18.927 -12.164 1.00 80.00  ? 54  TYR   B CE1  1 
ATOM   2225 C  CE2  . TYR   B 1 54  ? -38.343 -18.509 -14.503 1.00 90.19  ? 54  TYR   B CE2  1 
ATOM   2226 C  CZ   . TYR   B 1 54  ? -38.858 -18.424 -13.242 1.00 85.01  ? 54  TYR   B CZ   1 
ATOM   2227 O  OH   . TYR   B 1 54  ? -40.073 -17.820 -13.090 1.00 89.23  ? 54  TYR   B OH   1 
ATOM   2228 N  N    . ASN   B 1 55  ? -34.385 -17.378 -12.364 1.00 91.13  ? 55  ASN   B N    1 
ATOM   2229 C  CA   . ASN   B 1 55  ? -34.655 -16.524 -11.208 1.00 91.32  ? 55  ASN   B CA   1 
ATOM   2230 C  C    . ASN   B 1 55  ? -35.972 -15.793 -11.388 1.00 90.40  ? 55  ASN   B C    1 
ATOM   2231 O  O    . ASN   B 1 55  ? -36.309 -15.349 -12.488 1.00 91.53  ? 55  ASN   B O    1 
ATOM   2232 C  CB   . ASN   B 1 55  ? -33.579 -15.482 -11.010 1.00 93.39  ? 55  ASN   B CB   1 
ATOM   2233 C  CG   . ASN   B 1 55  ? -33.219 -14.792 -12.315 1.00 105.78 ? 55  ASN   B CG   1 
ATOM   2234 O  OD1  . ASN   B 1 55  ? -33.869 -15.013 -13.344 1.00 104.21 ? 55  ASN   B OD1  1 
ATOM   2235 N  ND2  . ASN   B 1 55  ? -32.149 -14.003 -12.302 1.00 111.70 ? 55  ASN   B ND2  1 
ATOM   2236 N  N    . SER   B 1 56  ? -36.700 -15.649 -10.289 1.00 91.20  ? 56  SER   B N    1 
ATOM   2237 C  CA   . SER   B 1 56  ? -37.929 -14.878 -10.315 1.00 87.51  ? 56  SER   B CA   1 
ATOM   2238 C  C    . SER   B 1 56  ? -37.738 -13.537 -10.969 1.00 94.43  ? 56  SER   B C    1 
ATOM   2239 O  O    . SER   B 1 56  ? -38.667 -13.011 -11.591 1.00 99.00  ? 56  SER   B O    1 
ATOM   2240 C  CB   . SER   B 1 56  ? -38.435 -14.649 -8.905  1.00 90.37  ? 56  SER   B CB   1 
ATOM   2241 O  OG   . SER   B 1 56  ? -39.587 -13.847 -8.948  1.00 96.23  ? 56  SER   B OG   1 
ATOM   2242 N  N    . VAL   B 1 57  ? -36.553 -12.957 -10.832 1.00 96.65  ? 57  VAL   B N    1 
ATOM   2243 C  CA   . VAL   B 1 57  ? -36.410 -11.544 -11.147 1.00 99.60  ? 57  VAL   B CA   1 
ATOM   2244 C  C    . VAL   B 1 57  ? -36.452 -11.328 -12.661 1.00 101.82 ? 57  VAL   B C    1 
ATOM   2245 O  O    . VAL   B 1 57  ? -37.365 -10.675 -13.179 1.00 101.59 ? 57  VAL   B O    1 
ATOM   2246 C  CB   . VAL   B 1 57  ? -35.139 -10.980 -10.495 1.00 96.64  ? 57  VAL   B CB   1 
ATOM   2247 C  CG1  . VAL   B 1 57  ? -34.948 -9.523  -10.882 1.00 93.31  ? 57  VAL   B CG1  1 
ATOM   2248 C  CG2  . VAL   B 1 57  ? -35.238 -11.127 -8.978  1.00 93.20  ? 57  VAL   B CG2  1 
ATOM   2249 N  N    . ASP   B 1 58  ? -35.488 -11.894 -13.397 1.00 102.32 ? 58  ASP   B N    1 
ATOM   2250 C  CA   . ASP   B 1 58  ? -35.555 -11.817 -14.856 1.00 98.18  ? 58  ASP   B CA   1 
ATOM   2251 C  C    . ASP   B 1 58  ? -36.867 -12.368 -15.379 1.00 107.14 ? 58  ASP   B C    1 
ATOM   2252 O  O    . ASP   B 1 58  ? -37.383 -11.863 -16.384 1.00 116.29 ? 58  ASP   B O    1 
ATOM   2253 C  CB   . ASP   B 1 58  ? -34.414 -12.601 -15.516 1.00 105.86 ? 58  ASP   B CB   1 
ATOM   2254 C  CG   . ASP   B 1 58  ? -33.029 -12.167 -15.054 1.00 113.74 ? 58  ASP   B CG   1 
ATOM   2255 O  OD1  . ASP   B 1 58  ? -32.895 -11.043 -14.535 1.00 120.34 ? 58  ASP   B OD1  1 
ATOM   2256 O  OD2  . ASP   B 1 58  ? -32.067 -12.962 -15.188 1.00 109.98 ? 58  ASP   B OD2  1 
ATOM   2257 N  N    . LYS   B 1 59  ? -37.426 -13.388 -14.692 1.00 107.19 ? 59  LYS   B N    1 
ATOM   2258 C  CA   . LYS   B 1 59  ? -38.379 -14.364 -15.261 1.00 99.21  ? 59  LYS   B CA   1 
ATOM   2259 C  C    . LYS   B 1 59  ? -37.851 -14.978 -16.538 1.00 98.89  ? 59  LYS   B C    1 
ATOM   2260 O  O    . LYS   B 1 59  ? -38.626 -15.407 -17.391 1.00 99.31  ? 59  LYS   B O    1 
ATOM   2261 C  CB   . LYS   B 1 59  ? -39.772 -13.777 -15.481 1.00 91.67  ? 59  LYS   B CB   1 
ATOM   2262 C  CG   . LYS   B 1 59  ? -40.412 -13.415 -14.203 1.00 96.56  ? 59  LYS   B CG   1 
ATOM   2263 C  CD   . LYS   B 1 59  ? -41.771 -12.833 -14.389 1.00 106.41 ? 59  LYS   B CD   1 
ATOM   2264 C  CE   . LYS   B 1 59  ? -42.389 -12.547 -13.011 1.00 116.52 ? 59  LYS   B CE   1 
ATOM   2265 N  NZ   . LYS   B 1 59  ? -41.723 -11.479 -12.211 1.00 103.48 ? 59  LYS   B NZ   1 
ATOM   2266 N  N    . ARG   B 1 60  ? -36.524 -15.103 -16.642 1.00 99.35  ? 60  ARG   B N    1 
ATOM   2267 C  CA   . ARG   B 1 60  ? -35.909 -15.691 -17.864 1.00 98.09  ? 60  ARG   B CA   1 
ATOM   2268 C  C    . ARG   B 1 60  ? -35.284 -17.059 -17.552 1.00 94.46  ? 60  ARG   B C    1 
ATOM   2269 O  O    . ARG   B 1 60  ? -34.335 -17.102 -16.744 1.00 96.30  ? 60  ARG   B O    1 
ATOM   2270 C  CB   . ARG   B 1 60  ? -34.862 -14.734 -18.444 1.00 101.61 ? 60  ARG   B CB   1 
ATOM   2271 C  CG   . ARG   B 1 60  ? -34.685 -14.846 -19.951 1.00 103.93 ? 60  ARG   B CG   1 
ATOM   2272 C  CD   . ARG   B 1 60  ? -33.889 -13.689 -20.525 1.00 112.05 ? 60  ARG   B CD   1 
ATOM   2273 N  NE   . ARG   B 1 60  ? -34.032 -13.579 -21.970 1.00 125.52 ? 60  ARG   B NE   1 
ATOM   2274 C  CZ   . ARG   B 1 60  ? -33.118 -13.972 -22.848 1.00 129.69 ? 60  ARG   B CZ   1 
ATOM   2275 N  NH1  . ARG   B 1 60  ? -31.984 -14.506 -22.428 1.00 123.17 ? 60  ARG   B NH1  1 
ATOM   2276 N  NH2  . ARG   B 1 60  ? -33.340 -13.831 -24.143 1.00 132.90 ? 60  ARG   B NH2  1 
ATOM   2277 N  N    . LEU   B 1 61  ? -35.803 -18.126 -18.173 1.00 88.38  ? 61  LEU   B N    1 
ATOM   2278 C  CA   . LEU   B 1 61  ? -35.264 -19.475 -17.996 1.00 84.87  ? 61  LEU   B CA   1 
ATOM   2279 C  C    . LEU   B 1 61  ? -34.163 -19.774 -19.016 1.00 85.78  ? 61  LEU   B C    1 
ATOM   2280 O  O    . LEU   B 1 61  ? -34.342 -19.549 -20.214 1.00 91.56  ? 61  LEU   B O    1 
ATOM   2281 C  CB   . LEU   B 1 61  ? -36.368 -20.528 -18.086 1.00 83.94  ? 61  LEU   B CB   1 
ATOM   2282 C  CG   . LEU   B 1 61  ? -35.844 -21.963 -17.961 1.00 85.45  ? 61  LEU   B CG   1 
ATOM   2283 C  CD1  . LEU   B 1 61  ? -35.155 -22.192 -16.642 1.00 84.66  ? 61  LEU   B CD1  1 
ATOM   2284 C  CD2  . LEU   B 1 61  ? -36.996 -22.919 -18.067 1.00 83.67  ? 61  LEU   B CD2  1 
ATOM   2285 N  N    . SER   B 1 62  ? -33.035 -20.316 -18.552 1.00 85.87  ? 62  SER   B N    1 
ATOM   2286 C  CA   . SER   B 1 62  ? -31.829 -20.358 -19.377 1.00 85.30  ? 62  SER   B CA   1 
ATOM   2287 C  C    . SER   B 1 62  ? -31.082 -21.685 -19.241 1.00 80.72  ? 62  SER   B C    1 
ATOM   2288 O  O    . SER   B 1 62  ? -31.206 -22.404 -18.244 1.00 76.62  ? 62  SER   B O    1 
ATOM   2289 C  CB   . SER   B 1 62  ? -30.904 -19.193 -19.024 1.00 83.08  ? 62  SER   B CB   1 
ATOM   2290 O  OG   . SER   B 1 62  ? -31.569 -17.970 -19.247 1.00 89.85  ? 62  SER   B OG   1 
ATOM   2291 N  N    . ALA   B 1 63  ? -30.288 -21.999 -20.271 1.00 79.84  ? 63  ALA   B N    1 
ATOM   2292 C  CA   . ALA   B 1 63  ? -29.546 -23.254 -20.328 1.00 76.30  ? 63  ALA   B CA   1 
ATOM   2293 C  C    . ALA   B 1 63  ? -28.344 -23.092 -21.250 1.00 73.45  ? 63  ALA   B C    1 
ATOM   2294 O  O    . ALA   B 1 63  ? -28.408 -22.358 -22.238 1.00 72.62  ? 63  ALA   B O    1 
ATOM   2295 C  CB   . ALA   B 1 63  ? -30.429 -24.415 -20.798 1.00 74.22  ? 63  ALA   B CB   1 
ATOM   2296 N  N    . VAL   B 1 64  ? -27.240 -23.762 -20.895 1.00 74.32  ? 64  VAL   B N    1 
ATOM   2297 C  CA   . VAL   B 1 64  ? -25.991 -23.727 -21.653 1.00 79.45  ? 64  VAL   B CA   1 
ATOM   2298 C  C    . VAL   B 1 64  ? -25.387 -25.109 -21.690 1.00 78.83  ? 64  VAL   B C    1 
ATOM   2299 O  O    . VAL   B 1 64  ? -25.057 -25.671 -20.644 1.00 84.43  ? 64  VAL   B O    1 
ATOM   2300 C  CB   . VAL   B 1 64  ? -24.950 -22.794 -21.032 1.00 84.00  ? 64  VAL   B CB   1 
ATOM   2301 C  CG1  . VAL   B 1 64  ? -23.691 -22.776 -21.906 1.00 90.62  ? 64  VAL   B CG1  1 
ATOM   2302 C  CG2  . VAL   B 1 64  ? -25.522 -21.459 -20.881 1.00 91.80  ? 64  VAL   B CG2  1 
ATOM   2303 N  N    . VAL   B 1 65  ? -25.164 -25.628 -22.874 1.00 76.58  ? 65  VAL   B N    1 
ATOM   2304 C  CA   . VAL   B 1 65  ? -24.530 -26.920 -22.996 1.00 81.04  ? 65  VAL   B CA   1 
ATOM   2305 C  C    . VAL   B 1 65  ? -23.199 -26.694 -23.677 1.00 86.27  ? 65  VAL   B C    1 
ATOM   2306 O  O    . VAL   B 1 65  ? -23.106 -25.894 -24.607 1.00 93.74  ? 65  VAL   B O    1 
ATOM   2307 C  CB   . VAL   B 1 65  ? -25.409 -27.901 -23.777 1.00 84.00  ? 65  VAL   B CB   1 
ATOM   2308 C  CG1  . VAL   B 1 65  ? -24.699 -29.227 -23.901 1.00 91.06  ? 65  VAL   B CG1  1 
ATOM   2309 C  CG2  . VAL   B 1 65  ? -26.739 -28.044 -23.082 1.00 80.55  ? 65  VAL   B CG2  1 
ATOM   2310 N  N    . SER   B 1 66  ? -22.168 -27.386 -23.217 1.00 90.17  ? 66  SER   B N    1 
ATOM   2311 C  CA   . SER   B 1 66  ? -20.823 -26.979 -23.580 1.00 95.99  ? 66  SER   B CA   1 
ATOM   2312 C  C    . SER   B 1 66  ? -19.846 -28.106 -23.300 1.00 96.54  ? 66  SER   B C    1 
ATOM   2313 O  O    . SER   B 1 66  ? -19.967 -28.817 -22.304 1.00 99.95  ? 66  SER   B O    1 
ATOM   2314 C  CB   . SER   B 1 66  ? -20.435 -25.712 -22.810 1.00 105.44 ? 66  SER   B CB   1 
ATOM   2315 O  OG   . SER   B 1 66  ? -20.733 -25.838 -21.418 1.00 107.69 ? 66  SER   B OG   1 
ATOM   2316 N  N    . TYR   B 1 67  ? -18.880 -28.251 -24.183 1.00 98.88  ? 67  TYR   B N    1 
ATOM   2317 C  CA   . TYR   B 1 67  ? -17.823 -29.234 -24.063 1.00 101.95 ? 67  TYR   B CA   1 
ATOM   2318 C  C    . TYR   B 1 67  ? -16.507 -28.527 -23.789 1.00 113.41 ? 67  TYR   B C    1 
ATOM   2319 O  O    . TYR   B 1 67  ? -16.386 -27.324 -24.044 1.00 117.94 ? 67  TYR   B O    1 
ATOM   2320 C  CB   . TYR   B 1 67  ? -17.741 -30.036 -25.361 1.00 103.56 ? 67  TYR   B CB   1 
ATOM   2321 C  CG   . TYR   B 1 67  ? -18.921 -30.932 -25.566 1.00 93.89  ? 67  TYR   B CG   1 
ATOM   2322 C  CD1  . TYR   B 1 67  ? -18.949 -32.189 -24.995 1.00 96.79  ? 67  TYR   B CD1  1 
ATOM   2323 C  CD2  . TYR   B 1 67  ? -20.027 -30.506 -26.283 1.00 96.17  ? 67  TYR   B CD2  1 
ATOM   2324 C  CE1  . TYR   B 1 67  ? -20.026 -33.034 -25.168 1.00 100.69 ? 67  TYR   B CE1  1 
ATOM   2325 C  CE2  . TYR   B 1 67  ? -21.126 -31.337 -26.457 1.00 101.85 ? 67  TYR   B CE2  1 
ATOM   2326 C  CZ   . TYR   B 1 67  ? -21.118 -32.611 -25.894 1.00 103.36 ? 67  TYR   B CZ   1 
ATOM   2327 O  OH   . TYR   B 1 67  ? -22.188 -33.478 -26.038 1.00 99.71  ? 67  TYR   B OH   1 
ATOM   2328 N  N    . PRO   B 1 68  ? -15.501 -29.224 -23.257 1.00 112.14 ? 68  PRO   B N    1 
ATOM   2329 C  CA   . PRO   B 1 68  ? -14.198 -28.581 -23.115 1.00 121.54 ? 68  PRO   B CA   1 
ATOM   2330 C  C    . PRO   B 1 68  ? -13.662 -28.265 -24.496 1.00 125.97 ? 68  PRO   B C    1 
ATOM   2331 O  O    . PRO   B 1 68  ? -13.839 -29.042 -25.441 1.00 129.97 ? 68  PRO   B O    1 
ATOM   2332 C  CB   . PRO   B 1 68  ? -13.347 -29.637 -22.407 1.00 120.07 ? 68  PRO   B CB   1 
ATOM   2333 C  CG   . PRO   B 1 68  ? -14.307 -30.500 -21.746 1.00 121.16 ? 68  PRO   B CG   1 
ATOM   2334 C  CD   . PRO   B 1 68  ? -15.479 -30.575 -22.684 1.00 108.69 ? 68  PRO   B CD   1 
ATOM   2335 N  N    . ASN   B 1 69  ? -13.054 -27.089 -24.622 1.00 124.57 ? 69  ASN   B N    1 
ATOM   2336 C  CA   . ASN   B 1 69  ? -12.361 -26.707 -25.845 1.00 129.41 ? 69  ASN   B CA   1 
ATOM   2337 C  C    . ASN   B 1 69  ? -13.320 -26.562 -27.016 1.00 130.13 ? 69  ASN   B C    1 
ATOM   2338 O  O    . ASN   B 1 69  ? -12.953 -26.843 -28.159 1.00 136.23 ? 69  ASN   B O    1 
ATOM   2339 C  CB   . ASN   B 1 69  ? -11.278 -27.729 -26.210 1.00 133.45 ? 69  ASN   B CB   1 
ATOM   2340 C  CG   . ASN   B 1 69  ? -10.145 -27.755 -25.216 1.00 143.57 ? 69  ASN   B CG   1 
ATOM   2341 O  OD1  . ASN   B 1 69  ? -9.686  -26.712 -24.745 1.00 153.78 ? 69  ASN   B OD1  1 
ATOM   2342 N  ND2  . ASN   B 1 69  ? -9.681  -28.960 -24.884 1.00 141.54 ? 69  ASN   B ND2  1 
ATOM   2343 N  N    . ALA   B 1 70  ? -14.561 -26.168 -26.749 1.00 126.23 ? 70  ALA   B N    1 
ATOM   2344 C  CA   . ALA   B 1 70  ? -15.584 -26.201 -27.780 1.00 125.93 ? 70  ALA   B CA   1 
ATOM   2345 C  C    . ALA   B 1 70  ? -16.607 -25.107 -27.527 1.00 128.71 ? 70  ALA   B C    1 
ATOM   2346 O  O    . ALA   B 1 70  ? -16.826 -24.687 -26.388 1.00 128.59 ? 70  ALA   B O    1 
ATOM   2347 C  CB   . ALA   B 1 70  ? -16.279 -27.563 -27.832 1.00 117.46 ? 70  ALA   B CB   1 
ATOM   2348 N  N    . ASP   B 1 71  ? -17.250 -24.665 -28.607 1.00 130.96 ? 71  ASP   B N    1 
ATOM   2349 C  CA   . ASP   B 1 71  ? -18.278 -23.638 -28.494 1.00 128.21 ? 71  ASP   B CA   1 
ATOM   2350 C  C    . ASP   B 1 71  ? -19.459 -24.144 -27.681 1.00 117.37 ? 71  ASP   B C    1 
ATOM   2351 O  O    . ASP   B 1 71  ? -19.713 -25.349 -27.577 1.00 118.90 ? 71  ASP   B O    1 
ATOM   2352 C  CB   . ASP   B 1 71  ? -18.774 -23.188 -29.870 1.00 138.37 ? 71  ASP   B CB   1 
ATOM   2353 C  CG   . ASP   B 1 71  ? -17.717 -22.439 -30.668 1.00 150.65 ? 71  ASP   B CG   1 
ATOM   2354 O  OD1  . ASP   B 1 71  ? -16.821 -21.817 -30.047 1.00 155.62 ? 71  ASP   B OD1  1 
ATOM   2355 O  OD2  . ASP   B 1 71  ? -17.800 -22.472 -31.920 1.00 152.85 ? 71  ASP   B OD2  1 
ATOM   2356 N  N    . SER   B 1 72  ? -20.196 -23.207 -27.113 1.00 105.11 ? 72  SER   B N    1 
ATOM   2357 C  CA   . SER   B 1 72  ? -21.263 -23.542 -26.192 1.00 103.30 ? 72  SER   B CA   1 
ATOM   2358 C  C    . SER   B 1 72  ? -22.587 -22.994 -26.709 1.00 99.95  ? 72  SER   B C    1 
ATOM   2359 O  O    . SER   B 1 72  ? -22.717 -21.796 -26.965 1.00 101.80 ? 72  SER   B O    1 
ATOM   2360 C  CB   . SER   B 1 72  ? -20.925 -23.028 -24.793 1.00 99.66  ? 72  SER   B CB   1 
ATOM   2361 O  OG   . SER   B 1 72  ? -20.881 -21.620 -24.742 1.00 103.85 ? 72  SER   B OG   1 
ATOM   2362 N  N    . ALA   B 1 73  ? -23.555 -23.883 -26.886 1.00 96.53  ? 73  ALA   B N    1 
ATOM   2363 C  CA   . ALA   B 1 73  ? -24.894 -23.492 -27.287 1.00 91.30  ? 73  ALA   B CA   1 
ATOM   2364 C  C    . ALA   B 1 73  ? -25.702 -23.028 -26.086 1.00 88.52  ? 73  ALA   B C    1 
ATOM   2365 O  O    . ALA   B 1 73  ? -25.621 -23.616 -25.005 1.00 91.36  ? 73  ALA   B O    1 
ATOM   2366 C  CB   . ALA   B 1 73  ? -25.593 -24.673 -27.942 1.00 102.66 ? 73  ALA   B CB   1 
ATOM   2367 N  N    . THR   B 1 74  ? -26.493 -21.974 -26.276 1.00 89.46  ? 74  THR   B N    1 
ATOM   2368 C  CA   . THR   B 1 74  ? -27.265 -21.383 -25.186 1.00 92.38  ? 74  THR   B CA   1 
ATOM   2369 C  C    . THR   B 1 74  ? -28.691 -21.105 -25.635 1.00 87.38  ? 74  THR   B C    1 
ATOM   2370 O  O    . THR   B 1 74  ? -28.931 -20.777 -26.796 1.00 95.87  ? 74  THR   B O    1 
ATOM   2371 C  CB   . THR   B 1 74  ? -26.641 -20.062 -24.684 1.00 92.44  ? 74  THR   B CB   1 
ATOM   2372 O  OG1  . THR   B 1 74  ? -26.986 -18.998 -25.581 1.00 98.21  ? 74  THR   B OG1  1 
ATOM   2373 C  CG2  . THR   B 1 74  ? -25.129 -20.169 -24.620 1.00 92.44  ? 74  THR   B CG2  1 
ATOM   2374 N  N    . VAL   B 1 75  ? -29.629 -21.193 -24.699 1.00 79.08  ? 75  VAL   B N    1 
ATOM   2375 C  CA   . VAL   B 1 75  ? -31.040 -20.964 -24.986 1.00 85.35  ? 75  VAL   B CA   1 
ATOM   2376 C  C    . VAL   B 1 75  ? -31.662 -20.195 -23.826 1.00 92.50  ? 75  VAL   B C    1 
ATOM   2377 O  O    . VAL   B 1 75  ? -31.275 -20.379 -22.668 1.00 92.14  ? 75  VAL   B O    1 
ATOM   2378 C  CB   . VAL   B 1 75  ? -31.800 -22.286 -25.237 1.00 86.05  ? 75  VAL   B CB   1 
ATOM   2379 C  CG1  . VAL   B 1 75  ? -31.800 -23.169 -24.019 1.00 89.38  ? 75  VAL   B CG1  1 
ATOM   2380 C  CG2  . VAL   B 1 75  ? -33.225 -22.006 -25.592 1.00 91.23  ? 75  VAL   B CG2  1 
ATOM   2381 N  N    . SER   B 1 76  ? -32.630 -19.331 -24.136 1.00 96.15  ? 76  SER   B N    1 
ATOM   2382 C  CA   . SER   B 1 76  ? -33.267 -18.494 -23.130 1.00 89.76  ? 76  SER   B CA   1 
ATOM   2383 C  C    . SER   B 1 76  ? -34.669 -18.142 -23.592 1.00 92.53  ? 76  SER   B C    1 
ATOM   2384 O  O    . SER   B 1 76  ? -34.871 -17.815 -24.766 1.00 98.49  ? 76  SER   B O    1 
ATOM   2385 C  CB   . SER   B 1 76  ? -32.462 -17.218 -22.903 1.00 96.56  ? 76  SER   B CB   1 
ATOM   2386 O  OG   . SER   B 1 76  ? -31.210 -17.479 -22.300 1.00 98.14  ? 76  SER   B OG   1 
ATOM   2387 N  N    . TYR   B 1 77  ? -35.618 -18.175 -22.661 1.00 87.65  ? 77  TYR   B N    1 
ATOM   2388 C  CA   . TYR   B 1 77  ? -37.027 -17.949 -22.956 1.00 98.84  ? 77  TYR   B CA   1 
ATOM   2389 C  C    . TYR   B 1 77  ? -37.723 -17.343 -21.743 1.00 101.17 ? 77  TYR   B C    1 
ATOM   2390 O  O    . TYR   B 1 77  ? -37.700 -17.941 -20.664 1.00 100.69 ? 77  TYR   B O    1 
ATOM   2391 C  CB   . TYR   B 1 77  ? -37.702 -19.266 -23.347 1.00 94.18  ? 77  TYR   B CB   1 
ATOM   2392 C  CG   . TYR   B 1 77  ? -39.191 -19.170 -23.580 1.00 99.21  ? 77  TYR   B CG   1 
ATOM   2393 C  CD1  . TYR   B 1 77  ? -39.720 -18.337 -24.568 1.00 95.92  ? 77  TYR   B CD1  1 
ATOM   2394 C  CD2  . TYR   B 1 77  ? -40.081 -19.908 -22.782 1.00 102.70 ? 77  TYR   B CD2  1 
ATOM   2395 C  CE1  . TYR   B 1 77  ? -41.110 -18.257 -24.769 1.00 104.85 ? 77  TYR   B CE1  1 
ATOM   2396 C  CE2  . TYR   B 1 77  ? -41.468 -19.841 -22.971 1.00 103.66 ? 77  TYR   B CE2  1 
ATOM   2397 C  CZ   . TYR   B 1 77  ? -41.983 -19.016 -23.964 1.00 109.42 ? 77  TYR   B CZ   1 
ATOM   2398 O  OH   . TYR   B 1 77  ? -43.361 -18.961 -24.137 1.00 109.49 ? 77  TYR   B OH   1 
ATOM   2399 N  N    . ASP   B 1 78  ? -38.341 -16.167 -21.910 1.00 100.98 ? 78  ASP   B N    1 
ATOM   2400 C  CA   . ASP   B 1 78  ? -39.089 -15.545 -20.813 1.00 101.69 ? 78  ASP   B CA   1 
ATOM   2401 C  C    . ASP   B 1 78  ? -40.301 -16.390 -20.438 1.00 98.96  ? 78  ASP   B C    1 
ATOM   2402 O  O    . ASP   B 1 78  ? -41.224 -16.520 -21.242 1.00 104.05 ? 78  ASP   B O    1 
ATOM   2403 C  CB   . ASP   B 1 78  ? -39.570 -14.135 -21.169 1.00 114.11 ? 78  ASP   B CB   1 
ATOM   2404 C  CG   . ASP   B 1 78  ? -38.449 -13.146 -21.488 1.00 134.29 ? 78  ASP   B CG   1 
ATOM   2405 O  OD1  . ASP   B 1 78  ? -37.292 -13.343 -21.097 1.00 130.53 ? 78  ASP   B OD1  1 
ATOM   2406 O  OD2  . ASP   B 1 78  ? -38.745 -12.116 -22.131 1.00 152.12 ? 78  ASP   B OD2  1 
ATOM   2407 N  N    . VAL   B 1 79  ? -40.327 -16.931 -19.217 1.00 94.84  ? 79  VAL   B N    1 
ATOM   2408 C  CA   . VAL   B 1 79  ? -41.499 -17.645 -18.705 1.00 92.96  ? 79  VAL   B CA   1 
ATOM   2409 C  C    . VAL   B 1 79  ? -41.665 -17.365 -17.217 1.00 95.90  ? 79  VAL   B C    1 
ATOM   2410 O  O    . VAL   B 1 79  ? -40.696 -17.128 -16.492 1.00 99.55  ? 79  VAL   B O    1 
ATOM   2411 C  CB   . VAL   B 1 79  ? -41.437 -19.170 -18.974 1.00 91.85  ? 79  VAL   B CB   1 
ATOM   2412 C  CG1  . VAL   B 1 79  ? -40.349 -19.830 -18.177 1.00 94.73  ? 79  VAL   B CG1  1 
ATOM   2413 C  CG2  . VAL   B 1 79  ? -42.773 -19.819 -18.617 1.00 97.90  ? 79  VAL   B CG2  1 
ATOM   2414 N  N    . ASP   B 1 80  ? -42.912 -17.371 -16.764 1.00 97.75  ? 80  ASP   B N    1 
ATOM   2415 C  CA   . ASP   B 1 80  ? -43.237 -17.180 -15.356 1.00 104.18 ? 80  ASP   B CA   1 
ATOM   2416 C  C    . ASP   B 1 80  ? -43.760 -18.499 -14.809 1.00 103.43 ? 80  ASP   B C    1 
ATOM   2417 O  O    . ASP   B 1 80  ? -44.922 -18.847 -15.033 1.00 105.93 ? 80  ASP   B O    1 
ATOM   2418 C  CB   . ASP   B 1 80  ? -44.267 -16.067 -15.171 1.00 114.49 ? 80  ASP   B CB   1 
ATOM   2419 C  CG   . ASP   B 1 80  ? -44.544 -15.769 -13.706 1.00 118.51 ? 80  ASP   B CG   1 
ATOM   2420 O  OD1  . ASP   B 1 80  ? -44.475 -16.717 -12.888 1.00 115.66 ? 80  ASP   B OD1  1 
ATOM   2421 O  OD2  . ASP   B 1 80  ? -44.844 -14.593 -13.378 1.00 121.26 ? 80  ASP   B OD2  1 
ATOM   2422 N  N    . LEU   B 1 81  ? -42.923 -19.190 -14.036 1.00 101.07 ? 81  LEU   B N    1 
ATOM   2423 C  CA   . LEU   B 1 81  ? -43.153 -20.584 -13.694 1.00 95.96  ? 81  LEU   B CA   1 
ATOM   2424 C  C    . LEU   B 1 81  ? -44.119 -20.775 -12.537 1.00 99.46  ? 81  LEU   B C    1 
ATOM   2425 O  O    . LEU   B 1 81  ? -44.455 -21.923 -12.240 1.00 106.25 ? 81  LEU   B O    1 
ATOM   2426 C  CB   . LEU   B 1 81  ? -41.825 -21.284 -13.366 1.00 92.20  ? 81  LEU   B CB   1 
ATOM   2427 C  CG   . LEU   B 1 81  ? -40.755 -21.421 -14.468 1.00 91.09  ? 81  LEU   B CG   1 
ATOM   2428 C  CD1  . LEU   B 1 81  ? -39.453 -22.047 -13.967 1.00 85.61  ? 81  LEU   B CD1  1 
ATOM   2429 C  CD2  . LEU   B 1 81  ? -41.277 -22.202 -15.655 1.00 97.88  ? 81  LEU   B CD2  1 
ATOM   2430 N  N    . ASP   B 1 82  ? -44.594 -19.725 -11.865 1.00 102.17 ? 82  ASP   B N    1 
ATOM   2431 C  CA   . ASP   B 1 82  ? -45.605 -20.023 -10.847 1.00 111.95 ? 82  ASP   B CA   1 
ATOM   2432 C  C    . ASP   B 1 82  ? -46.979 -20.160 -11.488 1.00 114.84 ? 82  ASP   B C    1 
ATOM   2433 O  O    . ASP   B 1 82  ? -47.833 -20.895 -10.974 1.00 111.61 ? 82  ASP   B O    1 
ATOM   2434 C  CB   . ASP   B 1 82  ? -45.618 -18.985 -9.706  1.00 114.75 ? 82  ASP   B CB   1 
ATOM   2435 C  CG   . ASP   B 1 82  ? -46.080 -17.591 -10.131 1.00 124.04 ? 82  ASP   B CG   1 
ATOM   2436 O  OD1  . ASP   B 1 82  ? -46.419 -17.372 -11.316 1.00 127.75 ? 82  ASP   B OD1  1 
ATOM   2437 O  OD2  . ASP   B 1 82  ? -46.078 -16.695 -9.250  1.00 124.84 ? 82  ASP   B OD2  1 
ATOM   2438 N  N    . ASN   B 1 83  ? -47.197 -19.463 -12.611 1.00 117.35 ? 83  ASN   B N    1 
ATOM   2439 C  CA   . ASN   B 1 83  ? -48.397 -19.673 -13.413 1.00 113.78 ? 83  ASN   B CA   1 
ATOM   2440 C  C    . ASN   B 1 83  ? -48.446 -21.099 -13.942 1.00 114.81 ? 83  ASN   B C    1 
ATOM   2441 O  O    . ASN   B 1 83  ? -49.492 -21.752 -13.891 1.00 127.37 ? 83  ASN   B O    1 
ATOM   2442 C  CB   . ASN   B 1 83  ? -48.442 -18.678 -14.576 1.00 114.71 ? 83  ASN   B CB   1 
ATOM   2443 C  CG   . ASN   B 1 83  ? -48.824 -17.267 -14.139 1.00 120.17 ? 83  ASN   B CG   1 
ATOM   2444 O  OD1  . ASN   B 1 83  ? -49.356 -17.058 -13.042 1.00 123.44 ? 83  ASN   B OD1  1 
ATOM   2445 N  ND2  . ASN   B 1 83  ? -48.579 -16.294 -15.015 1.00 115.34 ? 83  ASN   B ND2  1 
ATOM   2446 N  N    . VAL   B 1 84  ? -47.302 -21.608 -14.409 1.00 109.11 ? 84  VAL   B N    1 
ATOM   2447 C  CA   . VAL   B 1 84  ? -47.229 -22.904 -15.094 1.00 102.55 ? 84  VAL   B CA   1 
ATOM   2448 C  C    . VAL   B 1 84  ? -47.303 -24.080 -14.112 1.00 102.02 ? 84  VAL   B C    1 
ATOM   2449 O  O    . VAL   B 1 84  ? -48.149 -24.972 -14.251 1.00 97.73  ? 84  VAL   B O    1 
ATOM   2450 C  CB   . VAL   B 1 84  ? -45.945 -22.961 -15.933 1.00 101.58 ? 84  VAL   B CB   1 
ATOM   2451 C  CG1  . VAL   B 1 84  ? -45.750 -24.335 -16.520 1.00 98.84  ? 84  VAL   B CG1  1 
ATOM   2452 C  CG2  . VAL   B 1 84  ? -45.997 -21.868 -17.013 1.00 108.12 ? 84  VAL   B CG2  1 
ATOM   2453 N  N    . LEU   B 1 85  ? -46.390 -24.114 -13.107 1.00 102.78 ? 85  LEU   B N    1 
ATOM   2454 C  CA   . LEU   B 1 85  ? -46.050 -25.236 -12.235 1.00 95.52  ? 85  LEU   B CA   1 
ATOM   2455 C  C    . LEU   B 1 85  ? -46.839 -25.207 -10.936 1.00 99.57  ? 85  LEU   B C    1 
ATOM   2456 O  O    . LEU   B 1 85  ? -47.336 -24.156 -10.533 1.00 106.78 ? 85  LEU   B O    1 
ATOM   2457 C  CB   . LEU   B 1 85  ? -44.564 -25.191 -11.918 1.00 96.41  ? 85  LEU   B CB   1 
ATOM   2458 C  CG   . LEU   B 1 85  ? -43.681 -25.851 -12.973 1.00 101.12 ? 85  LEU   B CG   1 
ATOM   2459 C  CD1  . LEU   B 1 85  ? -42.224 -25.807 -12.572 1.00 93.33  ? 85  LEU   B CD1  1 
ATOM   2460 C  CD2  . LEU   B 1 85  ? -44.125 -27.303 -13.194 1.00 104.07 ? 85  LEU   B CD2  1 
ATOM   2461 N  N    . PRO   B 1 86  ? -46.966 -26.342 -10.243 1.00 102.03 ? 86  PRO   B N    1 
ATOM   2462 C  CA   . PRO   B 1 86  ? -47.584 -26.337 -8.913  1.00 100.02 ? 86  PRO   B CA   1 
ATOM   2463 C  C    . PRO   B 1 86  ? -46.624 -25.753 -7.895  1.00 99.01  ? 86  PRO   B C    1 
ATOM   2464 O  O    . PRO   B 1 86  ? -45.428 -25.613 -8.140  1.00 100.65 ? 86  PRO   B O    1 
ATOM   2465 C  CB   . PRO   B 1 86  ? -47.843 -27.820 -8.623  1.00 99.53  ? 86  PRO   B CB   1 
ATOM   2466 C  CG   . PRO   B 1 86  ? -46.733 -28.493 -9.292  1.00 96.04  ? 86  PRO   B CG   1 
ATOM   2467 C  CD   . PRO   B 1 86  ? -46.531 -27.702 -10.604 1.00 104.88 ? 86  PRO   B CD   1 
ATOM   2468 N  N    . GLU   B 1 87  ? -47.166 -25.431 -6.725  1.00 101.82 ? 87  GLU   B N    1 
ATOM   2469 C  CA   . GLU   B 1 87  ? -46.322 -24.838 -5.700  1.00 102.80 ? 87  GLU   B CA   1 
ATOM   2470 C  C    . GLU   B 1 87  ? -45.239 -25.835 -5.248  1.00 96.85  ? 87  GLU   B C    1 
ATOM   2471 O  O    . GLU   B 1 87  ? -44.086 -25.443 -5.046  1.00 90.52  ? 87  GLU   B O    1 
ATOM   2472 C  CB   . GLU   B 1 87  ? -47.232 -24.315 -4.570  1.00 106.80 ? 87  GLU   B CB   1 
ATOM   2473 C  CG   . GLU   B 1 87  ? -46.578 -23.527 -3.430  1.00 112.44 ? 87  GLU   B CG   1 
ATOM   2474 C  CD   . GLU   B 1 87  ? -47.595 -22.975 -2.411  1.00 126.14 ? 87  GLU   B CD   1 
ATOM   2475 O  OE1  . GLU   B 1 87  ? -48.805 -23.246 -2.565  1.00 134.50 ? 87  GLU   B OE1  1 
ATOM   2476 O  OE2  . GLU   B 1 87  ? -47.194 -22.228 -1.478  1.00 133.88 ? 87  GLU   B OE2  1 
ATOM   2477 N  N    . TRP   B 1 88  ? -45.547 -27.130 -5.183  1.00 92.56  ? 88  TRP   B N    1 
ATOM   2478 C  CA   . TRP   B 1 88  ? -44.559 -28.154 -4.861  1.00 86.66  ? 88  TRP   B CA   1 
ATOM   2479 C  C    . TRP   B 1 88  ? -44.330 -29.041 -6.078  1.00 88.09  ? 88  TRP   B C    1 
ATOM   2480 O  O    . TRP   B 1 88  ? -45.286 -29.479 -6.730  1.00 91.43  ? 88  TRP   B O    1 
ATOM   2481 C  CB   . TRP   B 1 88  ? -45.012 -29.011 -3.687  1.00 83.35  ? 88  TRP   B CB   1 
ATOM   2482 C  CG   . TRP   B 1 88  ? -44.880 -28.378 -2.349  1.00 84.69  ? 88  TRP   B CG   1 
ATOM   2483 C  CD1  . TRP   B 1 88  ? -45.836 -27.662 -1.693  1.00 88.41  ? 88  TRP   B CD1  1 
ATOM   2484 C  CD2  . TRP   B 1 88  ? -43.761 -28.461 -1.454  1.00 90.67  ? 88  TRP   B CD2  1 
ATOM   2485 N  NE1  . TRP   B 1 88  ? -45.381 -27.263 -0.459  1.00 89.15  ? 88  TRP   B NE1  1 
ATOM   2486 C  CE2  . TRP   B 1 88  ? -44.112 -27.746 -0.281  1.00 92.29  ? 88  TRP   B CE2  1 
ATOM   2487 C  CE3  . TRP   B 1 88  ? -42.492 -29.058 -1.530  1.00 88.56  ? 88  TRP   B CE3  1 
ATOM   2488 C  CZ2  . TRP   B 1 88  ? -43.240 -27.606 0.804   1.00 96.26  ? 88  TRP   B CZ2  1 
ATOM   2489 C  CZ3  . TRP   B 1 88  ? -41.631 -28.925 -0.451  1.00 88.94  ? 88  TRP   B CZ3  1 
ATOM   2490 C  CH2  . TRP   B 1 88  ? -42.010 -28.201 0.704   1.00 94.75  ? 88  TRP   B CH2  1 
ATOM   2491 N  N    . VAL   B 1 89  ? -43.064 -29.316 -6.377  1.00 89.28  ? 89  VAL   B N    1 
ATOM   2492 C  CA   . VAL   B 1 89  ? -42.713 -30.109 -7.547  1.00 87.76  ? 89  VAL   B CA   1 
ATOM   2493 C  C    . VAL   B 1 89  ? -41.742 -31.189 -7.136  1.00 83.91  ? 89  VAL   B C    1 
ATOM   2494 O  O    . VAL   B 1 89  ? -41.539 -31.442 -5.946  1.00 86.25  ? 89  VAL   B O    1 
ATOM   2495 C  CB   . VAL   B 1 89  ? -42.071 -29.274 -8.668  1.00 84.12  ? 89  VAL   B CB   1 
ATOM   2496 C  CG1  . VAL   B 1 89  ? -43.003 -28.186 -9.121  1.00 92.54  ? 89  VAL   B CG1  1 
ATOM   2497 C  CG2  . VAL   B 1 89  ? -40.747 -28.734 -8.252  1.00 84.05  ? 89  VAL   B CG2  1 
ATOM   2498 N  N    . ARG   B 1 90  ? -41.145 -31.823 -8.134  1.00 80.91  ? 90  ARG   B N    1 
ATOM   2499 C  CA   . ARG   B 1 90  ? -40.057 -32.760 -7.952  1.00 85.13  ? 90  ARG   B CA   1 
ATOM   2500 C  C    . ARG   B 1 90  ? -39.264 -32.739 -9.257  1.00 88.00  ? 90  ARG   B C    1 
ATOM   2501 O  O    . ARG   B 1 90  ? -39.843 -32.603 -10.339 1.00 84.53  ? 90  ARG   B O    1 
ATOM   2502 C  CB   . ARG   B 1 90  ? -40.580 -34.140 -7.536  1.00 78.07  ? 90  ARG   B CB   1 
ATOM   2503 C  CG   . ARG   B 1 90  ? -39.472 -35.117 -7.301  1.00 85.21  ? 90  ARG   B CG   1 
ATOM   2504 C  CD   . ARG   B 1 90  ? -39.850 -36.542 -6.766  1.00 93.85  ? 90  ARG   B CD   1 
ATOM   2505 N  NE   . ARG   B 1 90  ? -40.352 -36.690 -5.385  1.00 95.71  ? 90  ARG   B NE   1 
ATOM   2506 C  CZ   . ARG   B 1 90  ? -41.569 -37.084 -5.013  1.00 97.87  ? 90  ARG   B CZ   1 
ATOM   2507 N  NH1  . ARG   B 1 90  ? -42.498 -37.375 -5.920  1.00 108.91 ? 90  ARG   B NH1  1 
ATOM   2508 N  NH2  . ARG   B 1 90  ? -41.852 -37.200 -3.714  1.00 89.17  ? 90  ARG   B NH2  1 
ATOM   2509 N  N    . VAL   B 1 91  ? -37.935 -32.742 -9.138  1.00 88.72  ? 91  VAL   B N    1 
ATOM   2510 C  CA   . VAL   B 1 91  ? -37.057 -32.435 -10.261 1.00 82.85  ? 91  VAL   B CA   1 
ATOM   2511 C  C    . VAL   B 1 91  ? -36.328 -33.716 -10.609 1.00 83.40  ? 91  VAL   B C    1 
ATOM   2512 O  O    . VAL   B 1 91  ? -36.269 -34.661 -9.812  1.00 83.06  ? 91  VAL   B O    1 
ATOM   2513 C  CB   . VAL   B 1 91  ? -36.042 -31.309 -9.950  1.00 78.27  ? 91  VAL   B CB   1 
ATOM   2514 C  CG1  . VAL   B 1 91  ? -36.739 -30.018 -9.591  1.00 77.01  ? 91  VAL   B CG1  1 
ATOM   2515 C  CG2  . VAL   B 1 91  ? -35.108 -31.731 -8.860  1.00 76.50  ? 91  VAL   B CG2  1 
ATOM   2516 N  N    . GLY   B 1 92  ? -35.750 -33.748 -11.801 1.00 79.20  ? 92  GLY   B N    1 
ATOM   2517 C  CA   . GLY   B 1 92  ? -34.956 -34.913 -12.136 1.00 80.64  ? 92  GLY   B CA   1 
ATOM   2518 C  C    . GLY   B 1 92  ? -34.389 -34.842 -13.535 1.00 81.99  ? 92  GLY   B C    1 
ATOM   2519 O  O    . GLY   B 1 92  ? -34.570 -33.860 -14.267 1.00 82.44  ? 92  GLY   B O    1 
ATOM   2520 N  N    . LEU   B 1 93  ? -33.680 -35.908 -13.890 1.00 77.66  ? 93  LEU   B N    1 
ATOM   2521 C  CA   . LEU   B 1 93  ? -33.193 -36.096 -15.244 1.00 83.64  ? 93  LEU   B CA   1 
ATOM   2522 C  C    . LEU   B 1 93  ? -33.955 -37.216 -15.944 1.00 91.40  ? 93  LEU   B C    1 
ATOM   2523 O  O    . LEU   B 1 93  ? -34.228 -38.269 -15.351 1.00 88.57  ? 93  LEU   B O    1 
ATOM   2524 C  CB   . LEU   B 1 93  ? -31.702 -36.411 -15.268 1.00 78.73  ? 93  LEU   B CB   1 
ATOM   2525 C  CG   . LEU   B 1 93  ? -30.846 -35.251 -14.800 1.00 74.92  ? 93  LEU   B CG   1 
ATOM   2526 C  CD1  . LEU   B 1 93  ? -29.362 -35.605 -14.755 1.00 70.27  ? 93  LEU   B CD1  1 
ATOM   2527 C  CD2  . LEU   B 1 93  ? -31.120 -34.089 -15.692 1.00 79.07  ? 93  LEU   B CD2  1 
ATOM   2528 N  N    . SER   B 1 94  ? -34.265 -36.987 -17.225 1.00 91.01  ? 94  SER   B N    1 
ATOM   2529 C  CA   . SER   B 1 94  ? -34.922 -37.961 -18.079 1.00 89.51  ? 94  SER   B CA   1 
ATOM   2530 C  C    . SER   B 1 94  ? -34.128 -38.120 -19.363 1.00 93.83  ? 94  SER   B C    1 
ATOM   2531 O  O    . SER   B 1 94  ? -33.421 -37.197 -19.774 1.00 97.96  ? 94  SER   B O    1 
ATOM   2532 C  CB   . SER   B 1 94  ? -36.323 -37.530 -18.436 1.00 94.62  ? 94  SER   B CB   1 
ATOM   2533 O  OG   . SER   B 1 94  ? -36.924 -38.505 -19.270 1.00 100.17 ? 94  SER   B OG   1 
ATOM   2534 N  N    . ALA   B 1 95  ? -34.259 -39.288 -19.999 1.00 96.37  ? 95  ALA   B N    1 
ATOM   2535 C  CA   . ALA   B 1 95  ? -33.625 -39.551 -21.291 1.00 97.12  ? 95  ALA   B CA   1 
ATOM   2536 C  C    . ALA   B 1 95  ? -34.189 -40.836 -21.899 1.00 101.85 ? 95  ALA   B C    1 
ATOM   2537 O  O    . ALA   B 1 95  ? -34.729 -41.697 -21.195 1.00 102.06 ? 95  ALA   B O    1 
ATOM   2538 C  CB   . ALA   B 1 95  ? -32.101 -39.637 -21.165 1.00 95.55  ? 95  ALA   B CB   1 
ATOM   2539 N  N    . SER   B 1 96  ? -34.038 -40.956 -23.223 1.00 108.37 ? 96  SER   B N    1 
ATOM   2540 C  CA   . SER   B 1 96  ? -34.612 -42.075 -23.961 1.00 109.96 ? 96  SER   B CA   1 
ATOM   2541 C  C    . SER   B 1 96  ? -34.034 -42.172 -25.370 1.00 114.11 ? 96  SER   B C    1 
ATOM   2542 O  O    . SER   B 1 96  ? -33.351 -41.268 -25.862 1.00 110.47 ? 96  SER   B O    1 
ATOM   2543 C  CB   . SER   B 1 96  ? -36.124 -41.946 -24.073 1.00 115.58 ? 96  SER   B CB   1 
ATOM   2544 O  OG   . SER   B 1 96  ? -36.450 -40.846 -24.893 1.00 119.73 ? 96  SER   B OG   1 
ATOM   2545 N  N    . THR   B 1 97  ? -34.389 -43.281 -26.032 1.00 124.65 ? 97  THR   B N    1 
ATOM   2546 C  CA   . THR   B 1 97  ? -33.958 -43.629 -27.385 1.00 126.99 ? 97  THR   B CA   1 
ATOM   2547 C  C    . THR   B 1 97  ? -35.159 -44.091 -28.232 1.00 125.64 ? 97  THR   B C    1 
ATOM   2548 O  O    . THR   B 1 97  ? -36.279 -44.268 -27.730 1.00 124.58 ? 97  THR   B O    1 
ATOM   2549 C  CB   . THR   B 1 97  ? -32.832 -44.689 -27.341 1.00 122.28 ? 97  THR   B CB   1 
ATOM   2550 O  OG1  . THR   B 1 97  ? -33.283 -45.872 -26.668 1.00 123.25 ? 97  THR   B OG1  1 
ATOM   2551 C  CG2  . THR   B 1 97  ? -31.592 -44.155 -26.637 1.00 118.92 ? 97  THR   B CG2  1 
ATOM   2552 N  N    . GLY   B 1 98  ? -34.914 -44.260 -29.551 1.00 127.52 ? 98  GLY   B N    1 
ATOM   2553 C  CA   . GLY   B 1 98  ? -35.893 -44.695 -30.537 1.00 137.66 ? 98  GLY   B CA   1 
ATOM   2554 C  C    . GLY   B 1 98  ? -35.346 -45.819 -31.418 1.00 135.06 ? 98  GLY   B C    1 
ATOM   2555 O  O    . GLY   B 1 98  ? -34.698 -46.733 -30.942 1.00 131.50 ? 98  GLY   B O    1 
ATOM   2556 N  N    . LEU   B 1 99  ? -35.651 -45.771 -32.727 1.00 140.35 ? 99  LEU   B N    1 
ATOM   2557 C  CA   . LEU   B 1 99  ? -34.832 -46.519 -33.689 1.00 141.07 ? 99  LEU   B CA   1 
ATOM   2558 C  C    . LEU   B 1 99  ? -33.366 -46.279 -33.452 1.00 138.69 ? 99  LEU   B C    1 
ATOM   2559 O  O    . LEU   B 1 99  ? -32.586 -47.213 -33.231 1.00 143.37 ? 99  LEU   B O    1 
ATOM   2560 C  CB   . LEU   B 1 99  ? -35.150 -46.195 -35.166 1.00 146.74 ? 99  LEU   B CB   1 
ATOM   2561 C  CG   . LEU   B 1 99  ? -36.088 -47.027 -36.048 1.00 148.71 ? 99  LEU   B CG   1 
ATOM   2562 C  CD1  . LEU   B 1 99  ? -35.332 -48.292 -36.255 1.00 145.68 ? 99  LEU   B CD1  1 
ATOM   2563 C  CD2  . LEU   B 1 99  ? -37.386 -47.379 -35.390 1.00 149.91 ? 99  LEU   B CD2  1 
ATOM   2564 N  N    . TYR   B 1 100 ? -32.954 -45.035 -33.500 1.00 137.78 ? 100 TYR   B N    1 
ATOM   2565 C  CA   . TYR   B 1 100 ? -31.530 -44.948 -33.290 1.00 142.79 ? 100 TYR   B CA   1 
ATOM   2566 C  C    . TYR   B 1 100 ? -31.302 -44.877 -31.785 1.00 139.88 ? 100 TYR   B C    1 
ATOM   2567 O  O    . TYR   B 1 100 ? -32.232 -44.690 -30.996 1.00 136.15 ? 100 TYR   B O    1 
ATOM   2568 C  CB   . TYR   B 1 100 ? -30.928 -43.772 -34.055 1.00 143.04 ? 100 TYR   B CB   1 
ATOM   2569 C  CG   . TYR   B 1 100 ? -31.152 -43.838 -35.565 1.00 142.52 ? 100 TYR   B CG   1 
ATOM   2570 C  CD1  . TYR   B 1 100 ? -31.703 -44.964 -36.175 1.00 140.30 ? 100 TYR   B CD1  1 
ATOM   2571 C  CD2  . TYR   B 1 100 ? -30.758 -42.782 -36.383 1.00 139.59 ? 100 TYR   B CD2  1 
ATOM   2572 C  CE1  . TYR   B 1 100 ? -31.901 -45.007 -37.545 1.00 143.90 ? 100 TYR   B CE1  1 
ATOM   2573 C  CE2  . TYR   B 1 100 ? -30.937 -42.827 -37.751 1.00 133.66 ? 100 TYR   B CE2  1 
ATOM   2574 C  CZ   . TYR   B 1 100 ? -31.507 -43.940 -38.327 1.00 138.18 ? 100 TYR   B CZ   1 
ATOM   2575 O  OH   . TYR   B 1 100 ? -31.694 -44.018 -39.690 1.00 142.81 ? 100 TYR   B OH   1 
ATOM   2576 N  N    . LYS   B 1 101 ? -30.056 -45.078 -31.392 1.00 136.33 ? 101 LYS   B N    1 
ATOM   2577 C  CA   . LYS   B 1 101 ? -29.728 -45.413 -30.023 1.00 129.52 ? 101 LYS   B CA   1 
ATOM   2578 C  C    . LYS   B 1 101 ? -28.461 -44.663 -29.626 1.00 131.11 ? 101 LYS   B C    1 
ATOM   2579 O  O    . LYS   B 1 101 ? -27.703 -44.176 -30.477 1.00 130.67 ? 101 LYS   B O    1 
ATOM   2580 C  CB   . LYS   B 1 101 ? -29.640 -46.957 -29.883 1.00 129.64 ? 101 LYS   B CB   1 
ATOM   2581 C  CG   . LYS   B 1 101 ? -28.589 -47.615 -30.803 1.00 137.12 ? 101 LYS   B CG   1 
ATOM   2582 C  CD   . LYS   B 1 101 ? -28.590 -49.151 -30.750 1.00 135.00 ? 101 LYS   B CD   1 
ATOM   2583 C  CE   . LYS   B 1 101 ? -27.535 -49.739 -31.713 1.00 137.76 ? 101 LYS   B CE   1 
ATOM   2584 N  NZ   . LYS   B 1 101 ? -27.850 -49.514 -33.169 1.00 135.80 ? 101 LYS   B NZ   1 
ATOM   2585 N  N    . GLU   B 1 102 ? -28.279 -44.527 -28.308 1.00 128.98 ? 102 GLU   B N    1 
ATOM   2586 C  CA   . GLU   B 1 102 ? -27.149 -43.818 -27.723 1.00 121.63 ? 102 GLU   B CA   1 
ATOM   2587 C  C    . GLU   B 1 102 ? -27.037 -44.171 -26.247 1.00 113.10 ? 102 GLU   B C    1 
ATOM   2588 O  O    . GLU   B 1 102 ? -28.010 -44.568 -25.599 1.00 108.16 ? 102 GLU   B O    1 
ATOM   2589 C  CB   . GLU   B 1 102 ? -27.292 -42.302 -27.878 1.00 126.39 ? 102 GLU   B CB   1 
ATOM   2590 C  CG   . GLU   B 1 102 ? -28.472 -41.720 -27.086 1.00 126.50 ? 102 GLU   B CG   1 
ATOM   2591 C  CD   . GLU   B 1 102 ? -28.638 -40.204 -27.246 1.00 122.59 ? 102 GLU   B CD   1 
ATOM   2592 O  OE1  . GLU   B 1 102 ? -27.871 -39.581 -28.006 1.00 122.16 ? 102 GLU   B OE1  1 
ATOM   2593 O  OE2  . GLU   B 1 102 ? -29.538 -39.630 -26.591 1.00 120.37 ? 102 GLU   B OE2  1 
ATOM   2594 N  N    . THR   B 1 103 ? -25.830 -43.999 -25.725 1.00 116.49 ? 103 THR   B N    1 
ATOM   2595 C  CA   . THR   B 1 103 ? -25.609 -44.076 -24.290 1.00 113.45 ? 103 THR   B CA   1 
ATOM   2596 C  C    . THR   B 1 103 ? -25.947 -42.741 -23.650 1.00 110.44 ? 103 THR   B C    1 
ATOM   2597 O  O    . THR   B 1 103 ? -25.543 -41.680 -24.141 1.00 111.97 ? 103 THR   B O    1 
ATOM   2598 C  CB   . THR   B 1 103 ? -24.157 -44.432 -23.977 1.00 113.20 ? 103 THR   B CB   1 
ATOM   2599 O  OG1  . THR   B 1 103 ? -23.289 -43.414 -24.501 1.00 112.34 ? 103 THR   B OG1  1 
ATOM   2600 C  CG2  . THR   B 1 103 ? -23.800 -45.772 -24.573 1.00 118.65 ? 103 THR   B CG2  1 
ATOM   2601 N  N    . ASN   B 1 104 ? -26.686 -42.793 -22.547 1.00 103.31 ? 104 ASN   B N    1 
ATOM   2602 C  CA   . ASN   B 1 104 ? -27.138 -41.586 -21.869 1.00 95.99  ? 104 ASN   B CA   1 
ATOM   2603 C  C    . ASN   B 1 104 ? -26.629 -41.627 -20.437 1.00 89.87  ? 104 ASN   B C    1 
ATOM   2604 O  O    . ASN   B 1 104 ? -27.400 -41.703 -19.484 1.00 89.34  ? 104 ASN   B O    1 
ATOM   2605 C  CB   . ASN   B 1 104 ? -28.660 -41.454 -21.936 1.00 102.22 ? 104 ASN   B CB   1 
ATOM   2606 C  CG   . ASN   B 1 104 ? -29.141 -40.926 -23.292 1.00 105.05 ? 104 ASN   B CG   1 
ATOM   2607 O  OD1  . ASN   B 1 104 ? -30.331 -40.971 -23.621 1.00 98.96  ? 104 ASN   B OD1  1 
ATOM   2608 N  ND2  . ASN   B 1 104 ? -28.201 -40.424 -24.087 1.00 110.88 ? 104 ASN   B ND2  1 
ATOM   2609 N  N    . THR   B 1 105 ? -25.314 -41.564 -20.290 1.00 91.27  ? 105 THR   B N    1 
ATOM   2610 C  CA   . THR   B 1 105 ? -24.696 -41.736 -18.989 1.00 90.42  ? 105 THR   B CA   1 
ATOM   2611 C  C    . THR   B 1 105 ? -24.587 -40.386 -18.307 1.00 87.78  ? 105 THR   B C    1 
ATOM   2612 O  O    . THR   B 1 105 ? -24.066 -39.433 -18.879 1.00 93.05  ? 105 THR   B O    1 
ATOM   2613 C  CB   . THR   B 1 105 ? -23.315 -42.367 -19.106 1.00 91.49  ? 105 THR   B CB   1 
ATOM   2614 O  OG1  . THR   B 1 105 ? -23.423 -43.625 -19.780 1.00 98.03  ? 105 THR   B OG1  1 
ATOM   2615 C  CG2  . THR   B 1 105 ? -22.773 -42.634 -17.711 1.00 92.82  ? 105 THR   B CG2  1 
ATOM   2616 N  N    . ILE   B 1 106 ? -25.079 -40.306 -17.090 1.00 90.40  ? 106 ILE   B N    1 
ATOM   2617 C  CA   . ILE   B 1 106 ? -25.014 -39.087 -16.302 1.00 89.26  ? 106 ILE   B CA   1 
ATOM   2618 C  C    . ILE   B 1 106 ? -23.848 -39.251 -15.332 1.00 91.39  ? 106 ILE   B C    1 
ATOM   2619 O  O    . ILE   B 1 106 ? -23.873 -40.110 -14.441 1.00 94.25  ? 106 ILE   B O    1 
ATOM   2620 C  CB   . ILE   B 1 106 ? -26.340 -38.827 -15.575 1.00 87.40  ? 106 ILE   B CB   1 
ATOM   2621 C  CG1  . ILE   B 1 106 ? -27.441 -38.596 -16.600 1.00 82.48  ? 106 ILE   B CG1  1 
ATOM   2622 C  CG2  . ILE   B 1 106 ? -26.212 -37.665 -14.632 1.00 83.65  ? 106 ILE   B CG2  1 
ATOM   2623 C  CD1  . ILE   B 1 106 ? -27.117 -37.451 -17.521 1.00 92.93  ? 106 ILE   B CD1  1 
ATOM   2624 N  N    . LEU   B 1 107 ? -22.804 -38.448 -15.513 1.00 87.54  ? 107 LEU   B N    1 
ATOM   2625 C  CA   . LEU   B 1 107 ? -21.620 -38.610 -14.682 1.00 83.83  ? 107 LEU   B CA   1 
ATOM   2626 C  C    . LEU   B 1 107 ? -21.747 -37.908 -13.338 1.00 83.31  ? 107 LEU   B C    1 
ATOM   2627 O  O    . LEU   B 1 107 ? -21.089 -38.317 -12.376 1.00 84.40  ? 107 LEU   B O    1 
ATOM   2628 C  CB   . LEU   B 1 107 ? -20.404 -38.095 -15.433 1.00 79.74  ? 107 LEU   B CB   1 
ATOM   2629 C  CG   . LEU   B 1 107 ? -20.171 -38.813 -16.738 1.00 79.26  ? 107 LEU   B CG   1 
ATOM   2630 C  CD1  . LEU   B 1 107 ? -18.752 -38.647 -17.103 1.00 87.47  ? 107 LEU   B CD1  1 
ATOM   2631 C  CD2  . LEU   B 1 107 ? -20.405 -40.256 -16.461 1.00 89.19  ? 107 LEU   B CD2  1 
ATOM   2632 N  N    . SER   B 1 108 ? -22.586 -36.873 -13.257 1.00 79.71  ? 108 SER   B N    1 
ATOM   2633 C  CA   . SER   B 1 108 ? -22.733 -36.013 -12.089 1.00 75.72  ? 108 SER   B CA   1 
ATOM   2634 C  C    . SER   B 1 108 ? -23.942 -35.095 -12.271 1.00 72.33  ? 108 SER   B C    1 
ATOM   2635 O  O    . SER   B 1 108 ? -24.266 -34.698 -13.394 1.00 76.25  ? 108 SER   B O    1 
ATOM   2636 C  CB   . SER   B 1 108 ? -21.454 -35.197 -11.856 1.00 85.35  ? 108 SER   B CB   1 
ATOM   2637 O  OG   . SER   B 1 108 ? -21.387 -34.024 -12.659 1.00 85.11  ? 108 SER   B OG   1 
ATOM   2638 N  N    . TRP   B 1 109 ? -24.603 -34.762 -11.160 1.00 63.77  ? 109 TRP   B N    1 
ATOM   2639 C  CA   . TRP   B 1 109 ? -25.790 -33.919 -11.200 1.00 63.14  ? 109 TRP   B CA   1 
ATOM   2640 C  C    . TRP   B 1 109 ? -25.955 -33.179 -9.877  1.00 70.37  ? 109 TRP   B C    1 
ATOM   2641 O  O    . TRP   B 1 109 ? -25.959 -33.810 -8.820  1.00 75.16  ? 109 TRP   B O    1 
ATOM   2642 C  CB   . TRP   B 1 109 ? -27.029 -34.765 -11.492 1.00 66.79  ? 109 TRP   B CB   1 
ATOM   2643 C  CG   . TRP   B 1 109 ? -28.318 -34.024 -11.408 1.00 69.41  ? 109 TRP   B CG   1 
ATOM   2644 C  CD1  . TRP   B 1 109 ? -28.543 -32.736 -11.771 1.00 73.91  ? 109 TRP   B CD1  1 
ATOM   2645 C  CD2  . TRP   B 1 109 ? -29.563 -34.527 -10.947 1.00 69.66  ? 109 TRP   B CD2  1 
ATOM   2646 N  NE1  . TRP   B 1 109 ? -29.850 -32.397 -11.553 1.00 70.83  ? 109 TRP   B NE1  1 
ATOM   2647 C  CE2  . TRP   B 1 109 ? -30.501 -33.483 -11.048 1.00 71.48  ? 109 TRP   B CE2  1 
ATOM   2648 C  CE3  . TRP   B 1 109 ? -29.980 -35.761 -10.461 1.00 74.62  ? 109 TRP   B CE3  1 
ATOM   2649 C  CZ2  . TRP   B 1 109 ? -31.831 -33.632 -10.682 1.00 77.70  ? 109 TRP   B CZ2  1 
ATOM   2650 C  CZ3  . TRP   B 1 109 ? -31.301 -35.910 -10.091 1.00 81.91  ? 109 TRP   B CZ3  1 
ATOM   2651 C  CH2  . TRP   B 1 109 ? -32.213 -34.849 -10.200 1.00 81.10  ? 109 TRP   B CH2  1 
ATOM   2652 N  N    . SER   B 1 110 ? -26.097 -31.852 -9.933  1.00 67.49  ? 110 SER   B N    1 
ATOM   2653 C  CA   . SER   B 1 110 ? -26.349 -31.024 -8.764  1.00 67.25  ? 110 SER   B CA   1 
ATOM   2654 C  C    . SER   B 1 110 ? -27.507 -30.084 -9.054  1.00 70.84  ? 110 SER   B C    1 
ATOM   2655 O  O    . SER   B 1 110 ? -27.936 -29.936 -10.197 1.00 74.69  ? 110 SER   B O    1 
ATOM   2656 C  CB   . SER   B 1 110 ? -25.121 -30.207 -8.393  1.00 76.77  ? 110 SER   B CB   1 
ATOM   2657 O  OG   . SER   B 1 110 ? -24.862 -29.261 -9.407  1.00 86.25  ? 110 SER   B OG   1 
ATOM   2658 N  N    . PHE   B 1 111 ? -27.983 -29.404 -8.016  1.00 70.98  ? 111 PHE   B N    1 
ATOM   2659 C  CA   . PHE   B 1 111 ? -29.164 -28.541 -8.094  1.00 78.35  ? 111 PHE   B CA   1 
ATOM   2660 C  C    . PHE   B 1 111 ? -29.365 -27.835 -6.751  1.00 79.57  ? 111 PHE   B C    1 
ATOM   2661 O  O    . PHE   B 1 111 ? -28.977 -28.348 -5.700  1.00 75.34  ? 111 PHE   B O    1 
ATOM   2662 C  CB   . PHE   B 1 111 ? -30.407 -29.355 -8.535  1.00 72.96  ? 111 PHE   B CB   1 
ATOM   2663 C  CG   . PHE   B 1 111 ? -31.761 -28.711 -8.256  1.00 76.15  ? 111 PHE   B CG   1 
ATOM   2664 C  CD1  . PHE   B 1 111 ? -32.366 -28.878 -7.012  1.00 73.71  ? 111 PHE   B CD1  1 
ATOM   2665 C  CD2  . PHE   B 1 111 ? -32.441 -27.989 -9.212  1.00 79.78  ? 111 PHE   B CD2  1 
ATOM   2666 C  CE1  . PHE   B 1 111 ? -33.594 -28.307 -6.717  1.00 74.18  ? 111 PHE   B CE1  1 
ATOM   2667 C  CE2  . PHE   B 1 111 ? -33.691 -27.426 -8.918  1.00 79.98  ? 111 PHE   B CE2  1 
ATOM   2668 C  CZ   . PHE   B 1 111 ? -34.259 -27.588 -7.668  1.00 74.33  ? 111 PHE   B CZ   1 
ATOM   2669 N  N    . THR   B 1 112 ? -29.953 -26.638 -6.827  1.00 83.26  ? 112 THR   B N    1 
ATOM   2670 C  CA   . THR   B 1 112 ? -30.063 -25.658 -5.747  1.00 79.16  ? 112 THR   B CA   1 
ATOM   2671 C  C    . THR   B 1 112 ? -31.332 -24.871 -6.029  1.00 80.28  ? 112 THR   B C    1 
ATOM   2672 O  O    . THR   B 1 112 ? -31.501 -24.398 -7.157  1.00 80.39  ? 112 THR   B O    1 
ATOM   2673 C  CB   . THR   B 1 112 ? -28.849 -24.700 -5.735  1.00 89.02  ? 112 THR   B CB   1 
ATOM   2674 O  OG1  . THR   B 1 112 ? -27.612 -25.427 -5.670  1.00 95.91  ? 112 THR   B OG1  1 
ATOM   2675 C  CG2  . THR   B 1 112 ? -28.928 -23.675 -4.601  1.00 88.21  ? 112 THR   B CG2  1 
ATOM   2676 N  N    . SER   B 1 113 ? -32.222 -24.736 -5.044  1.00 79.07  ? 113 SER   B N    1 
ATOM   2677 C  CA   . SER   B 1 113 ? -33.364 -23.834 -5.161  1.00 81.52  ? 113 SER   B CA   1 
ATOM   2678 C  C    . SER   B 1 113 ? -33.488 -23.055 -3.871  1.00 85.00  ? 113 SER   B C    1 
ATOM   2679 O  O    . SER   B 1 113 ? -33.475 -23.648 -2.792  1.00 89.52  ? 113 SER   B O    1 
ATOM   2680 C  CB   . SER   B 1 113 ? -34.687 -24.538 -5.359  1.00 83.79  ? 113 SER   B CB   1 
ATOM   2681 O  OG   . SER   B 1 113 ? -35.021 -25.217 -4.163  1.00 89.52  ? 113 SER   B OG   1 
ATOM   2682 N  N    . LYS   B 1 114 ? -33.668 -21.744 -3.988  1.00 84.90  ? 114 LYS   B N    1 
ATOM   2683 C  CA   . LYS   B 1 114 ? -33.747 -20.845 -2.850  1.00 84.39  ? 114 LYS   B CA   1 
ATOM   2684 C  C    . LYS   B 1 114 ? -35.079 -20.092 -2.933  1.00 88.66  ? 114 LYS   B C    1 
ATOM   2685 O  O    . LYS   B 1 114 ? -35.576 -19.826 -4.031  1.00 87.41  ? 114 LYS   B O    1 
ATOM   2686 C  CB   . LYS   B 1 114 ? -32.528 -19.877 -2.866  1.00 89.61  ? 114 LYS   B CB   1 
ATOM   2687 C  CG   . LYS   B 1 114 ? -31.098 -20.491 -2.658  1.00 84.05  ? 114 LYS   B CG   1 
ATOM   2688 C  CD   . LYS   B 1 114 ? -30.018 -19.362 -2.726  1.00 103.04 ? 114 LYS   B CD   1 
ATOM   2689 C  CE   . LYS   B 1 114 ? -28.553 -19.797 -2.579  1.00 96.29  ? 114 LYS   B CE   1 
ATOM   2690 N  NZ   . LYS   B 1 114 ? -27.640 -18.595 -2.664  1.00 103.92 ? 114 LYS   B NZ   1 
ATOM   2691 N  N    . LEU   B 1 115 ? -35.677 -19.773 -1.771  1.00 94.54  ? 115 LEU   B N    1 
ATOM   2692 C  CA   . LEU   B 1 115 ? -36.864 -18.901 -1.674  1.00 91.32  ? 115 LEU   B CA   1 
ATOM   2693 C  C    . LEU   B 1 115 ? -36.598 -17.736 -0.730  1.00 103.64 ? 115 LEU   B C    1 
ATOM   2694 O  O    . LEU   B 1 115 ? -37.014 -17.766 0.429   1.00 108.85 ? 115 LEU   B O    1 
ATOM   2695 C  CB   . LEU   B 1 115 ? -38.073 -19.624 -1.192  1.00 84.23  ? 115 LEU   B CB   1 
ATOM   2696 C  CG   . LEU   B 1 115 ? -38.699 -20.699 -2.005  1.00 82.73  ? 115 LEU   B CG   1 
ATOM   2697 C  CD1  . LEU   B 1 115 ? -39.798 -21.244 -1.147  1.00 89.56  ? 115 LEU   B CD1  1 
ATOM   2698 C  CD2  . LEU   B 1 115 ? -39.196 -20.058 -3.248  1.00 87.12  ? 115 LEU   B CD2  1 
ATOM   2699 N  N    . LYS   B 1 116 ? -35.946 -16.694 -1.214  1.00 108.92 ? 116 LYS   B N    1 
ATOM   2700 C  CA   . LYS   B 1 116 ? -35.661 -15.577 -0.340  1.00 118.89 ? 116 LYS   B CA   1 
ATOM   2701 C  C    . LYS   B 1 116 ? -36.963 -14.808 -0.173  1.00 120.00 ? 116 LYS   B C    1 
ATOM   2702 O  O    . LYS   B 1 116 ? -37.690 -14.612 -1.144  1.00 119.32 ? 116 LYS   B O    1 
ATOM   2703 C  CB   . LYS   B 1 116 ? -34.538 -14.719 -0.925  1.00 119.44 ? 116 LYS   B CB   1 
ATOM   2704 C  CG   . LYS   B 1 116 ? -33.186 -15.471 -1.138  1.00 128.35 ? 116 LYS   B CG   1 
ATOM   2705 C  CD   . LYS   B 1 116 ? -32.135 -14.521 -1.731  1.00 128.71 ? 116 LYS   B CD   1 
ATOM   2706 C  CE   . LYS   B 1 116 ? -30.785 -15.171 -1.985  1.00 123.42 ? 116 LYS   B CE   1 
ATOM   2707 N  NZ   . LYS   B 1 116 ? -30.946 -16.149 -3.062  1.00 130.64 ? 116 LYS   B NZ   1 
ATOM   2708 N  N    . SER   B 1 117 ? -37.309 -14.452 1.058   1.00 138.28 ? 117 SER   B N    1 
ATOM   2709 C  CA   . SER   B 1 117 ? -38.614 -13.857 1.323   1.00 148.11 ? 117 SER   B CA   1 
ATOM   2710 C  C    . SER   B 1 117 ? -38.507 -12.340 1.472   1.00 160.65 ? 117 SER   B C    1 
ATOM   2711 O  O    . SER   B 1 117 ? -37.415 -11.753 1.456   1.00 153.03 ? 117 SER   B O    1 
ATOM   2712 C  CB   . SER   B 1 117 ? -39.257 -14.479 2.572   1.00 158.16 ? 117 SER   B CB   1 
ATOM   2713 O  OG   . SER   B 1 117 ? -40.517 -13.889 2.853   1.00 155.71 ? 117 SER   B OG   1 
ATOM   2714 N  N    . ASN   B 1 118 ? -39.686 -11.711 1.631   1.00 166.99 ? 118 ASN   B N    1 
ATOM   2715 C  CA   . ASN   B 1 118 ? -39.791 -10.250 1.655   1.00 172.30 ? 118 ASN   B CA   1 
ATOM   2716 C  C    . ASN   B 1 118 ? -38.964 -9.637  2.786   1.00 180.45 ? 118 ASN   B C    1 
ATOM   2717 O  O    . ASN   B 1 118 ? -38.489 -8.498  2.669   1.00 212.55 ? 118 ASN   B O    1 
ATOM   2718 C  CB   . ASN   B 1 118 ? -41.279 -9.831  1.710   1.00 163.26 ? 118 ASN   B CB   1 
ATOM   2719 C  CG   . ASN   B 1 118 ? -42.033 -10.351 2.953   1.00 163.68 ? 118 ASN   B CG   1 
ATOM   2720 O  OD1  . ASN   B 1 118 ? -41.445 -10.927 3.873   1.00 173.50 ? 118 ASN   B OD1  1 
ATOM   2721 N  ND2  . ASN   B 1 118 ? -43.355 -10.156 2.960   1.00 147.55 ? 118 ASN   B ND2  1 
ATOM   2722 N  N    . SER   B 1 119 ? -38.762 -10.384 3.868   1.00 188.46 ? 119 SER   B N    1 
ATOM   2723 C  CA   . SER   B 1 119 ? -37.735 -10.091 4.859   1.00 194.33 ? 119 SER   B CA   1 
ATOM   2724 C  C    . SER   B 1 119 ? -36.506 -10.958 4.572   1.00 198.93 ? 119 SER   B C    1 
ATOM   2725 O  O    . SER   B 1 119 ? -36.621 -12.185 4.486   1.00 198.56 ? 119 SER   B O    1 
ATOM   2726 C  CB   . SER   B 1 119 ? -38.298 -10.310 6.266   1.00 193.39 ? 119 SER   B CB   1 
ATOM   2727 O  OG   . SER   B 1 119 ? -38.658 -11.660 6.490   1.00 204.58 ? 119 SER   B OG   1 
ATOM   2728 N  N    . THR   B 1 120 ? -35.337 -10.321 4.413   1.00 206.04 ? 120 THR   B N    1 
ATOM   2729 C  CA   . THR   B 1 120 ? -34.142 -11.015 3.931   1.00 205.87 ? 120 THR   B CA   1 
ATOM   2730 C  C    . THR   B 1 120 ? -33.621 -12.012 4.953   1.00 204.74 ? 120 THR   B C    1 
ATOM   2731 O  O    . THR   B 1 120 ? -33.844 -11.881 6.165   1.00 209.24 ? 120 THR   B O    1 
ATOM   2732 C  CB   . THR   B 1 120 ? -32.996 -10.054 3.641   1.00 200.61 ? 120 THR   B CB   1 
ATOM   2733 O  OG1  . THR   B 1 120 ? -31.929 -10.781 3.009   1.00 190.82 ? 120 THR   B OG1  1 
ATOM   2734 C  CG2  . THR   B 1 120 ? -32.452 -9.530  4.961   1.00 200.15 ? 120 THR   B CG2  1 
ATOM   2735 N  N    . HIS   B 1 121 ? -32.860 -12.985 4.444   1.00 202.71 ? 121 HIS   B N    1 
ATOM   2736 C  CA   . HIS   B 1 121 ? -32.334 -14.070 5.262   1.00 196.63 ? 121 HIS   B CA   1 
ATOM   2737 C  C    . HIS   B 1 121 ? -33.424 -14.602 6.189   1.00 211.73 ? 121 HIS   B C    1 
ATOM   2738 O  O    . HIS   B 1 121 ? -33.211 -14.845 7.377   1.00 202.11 ? 121 HIS   B O    1 
ATOM   2739 C  CB   . HIS   B 1 121 ? -31.082 -13.605 5.997   1.00 191.69 ? 121 HIS   B CB   1 
ATOM   2740 C  CG   . HIS   B 1 121 ? -30.061 -13.044 5.064   1.00 179.66 ? 121 HIS   B CG   1 
ATOM   2741 N  ND1  . HIS   B 1 121 ? -29.913 -13.522 3.778   1.00 171.77 ? 121 HIS   B ND1  1 
ATOM   2742 C  CD2  . HIS   B 1 121 ? -29.205 -12.004 5.183   1.00 167.89 ? 121 HIS   B CD2  1 
ATOM   2743 C  CE1  . HIS   B 1 121 ? -28.972 -12.835 3.163   1.00 153.16 ? 121 HIS   B CE1  1 
ATOM   2744 N  NE2  . HIS   B 1 121 ? -28.526 -11.908 3.993   1.00 152.52 ? 121 HIS   B NE2  1 
ATOM   2745 N  N    . GLU   B 1 122 ? -34.638 -14.685 5.633   1.00 205.77 ? 122 GLU   B N    1 
ATOM   2746 C  CA   . GLU   B 1 122 ? -35.716 -15.540 6.110   1.00 177.69 ? 122 GLU   B CA   1 
ATOM   2747 C  C    . GLU   B 1 122 ? -36.027 -16.546 4.993   1.00 160.51 ? 122 GLU   B C    1 
ATOM   2748 O  O    . GLU   B 1 122 ? -37.175 -16.957 4.779   1.00 148.68 ? 122 GLU   B O    1 
ATOM   2749 C  CB   . GLU   B 1 122 ? -36.943 -14.707 6.480   1.00 187.57 ? 122 GLU   B CB   1 
ATOM   2750 C  CG   . GLU   B 1 122 ? -36.676 -13.558 7.508   1.00 198.16 ? 122 GLU   B CG   1 
ATOM   2751 C  CD   . GLU   B 1 122 ? -36.196 -13.931 8.910   1.00 197.35 ? 122 GLU   B CD   1 
ATOM   2752 O  OE1  . GLU   B 1 122 ? -36.530 -15.030 9.412   1.00 183.38 ? 122 GLU   B OE1  1 
ATOM   2753 O  OE2  . GLU   B 1 122 ? -35.483 -13.087 9.510   1.00 195.16 ? 122 GLU   B OE2  1 
ATOM   2754 N  N    . THR   B 1 123 ? -34.969 -16.913 4.266   1.00 150.52 ? 123 THR   B N    1 
ATOM   2755 C  CA   . THR   B 1 123 ? -34.968 -17.713 3.050   1.00 131.45 ? 123 THR   B CA   1 
ATOM   2756 C  C    . THR   B 1 123 ? -35.376 -19.175 3.356   1.00 115.10 ? 123 THR   B C    1 
ATOM   2757 O  O    . THR   B 1 123 ? -35.509 -19.562 4.507   1.00 114.58 ? 123 THR   B O    1 
ATOM   2758 C  CB   . THR   B 1 123 ? -33.568 -17.592 2.419   1.00 133.33 ? 123 THR   B CB   1 
ATOM   2759 O  OG1  . THR   B 1 123 ? -32.587 -18.123 3.311   1.00 132.89 ? 123 THR   B OG1  1 
ATOM   2760 C  CG2  . THR   B 1 123 ? -33.184 -16.122 2.238   1.00 141.23 ? 123 THR   B CG2  1 
ATOM   2761 N  N    . ASN   B 1 124 ? -35.608 -19.990 2.307   1.00 108.12 ? 124 ASN   B N    1 
ATOM   2762 C  CA   . ASN   B 1 124 ? -35.773 -21.452 2.426   1.00 93.99  ? 124 ASN   B CA   1 
ATOM   2763 C  C    . ASN   B 1 124 ? -34.987 -22.129 1.316   1.00 87.95  ? 124 ASN   B C    1 
ATOM   2764 O  O    . ASN   B 1 124 ? -35.003 -21.640 0.186   1.00 90.49  ? 124 ASN   B O    1 
ATOM   2765 C  CB   . ASN   B 1 124 ? -37.209 -21.930 2.264   1.00 88.92  ? 124 ASN   B CB   1 
ATOM   2766 C  CG   . ASN   B 1 124 ? -38.039 -21.650 3.450   1.00 100.21 ? 124 ASN   B CG   1 
ATOM   2767 O  OD1  . ASN   B 1 124 ? -37.974 -20.552 4.015   1.00 107.84 ? 124 ASN   B OD1  1 
ATOM   2768 N  ND2  . ASN   B 1 124 ? -38.822 -22.642 3.872   1.00 101.67 ? 124 ASN   B ND2  1 
ATOM   2769 N  N    . ALA   B 1 125 ? -34.336 -23.264 1.591   1.00 81.09  ? 125 ALA   B N    1 
ATOM   2770 C  CA   . ALA   B 1 125 ? -33.408 -23.735 0.560   1.00 77.03  ? 125 ALA   B CA   1 
ATOM   2771 C  C    . ALA   B 1 125 ? -33.049 -25.208 0.678   1.00 68.37  ? 125 ALA   B C    1 
ATOM   2772 O  O    . ALA   B 1 125 ? -33.049 -25.789 1.768   1.00 65.53  ? 125 ALA   B O    1 
ATOM   2773 C  CB   . ALA   B 1 125 ? -32.116 -22.926 0.572   1.00 84.46  ? 125 ALA   B CB   1 
ATOM   2774 N  N    . LEU   B 1 126 ? -32.659 -25.762 -0.485  1.00 66.15  ? 126 LEU   B N    1 
ATOM   2775 C  CA   . LEU   B 1 126 ? -32.291 -27.152 -0.744  1.00 62.58  ? 126 LEU   B CA   1 
ATOM   2776 C  C    . LEU   B 1 126 ? -31.245 -27.235 -1.835  1.00 63.27  ? 126 LEU   B C    1 
ATOM   2777 O  O    . LEU   B 1 126 ? -31.494 -26.744 -2.935  1.00 70.10  ? 126 LEU   B O    1 
ATOM   2778 C  CB   . LEU   B 1 126 ? -33.510 -27.937 -1.183  1.00 69.93  ? 126 LEU   B CB   1 
ATOM   2779 C  CG   . LEU   B 1 126 ? -33.361 -29.412 -1.478  1.00 67.82  ? 126 LEU   B CG   1 
ATOM   2780 C  CD1  . LEU   B 1 126 ? -34.677 -30.059 -1.185  1.00 83.01  ? 126 LEU   B CD1  1 
ATOM   2781 C  CD2  . LEU   B 1 126 ? -33.093 -29.562 -2.950  1.00 69.53  ? 126 LEU   B CD2  1 
ATOM   2782 N  N    . HIS   B 1 127 ? -30.118 -27.903 -1.553  1.00 63.04  ? 127 HIS   B N    1 
ATOM   2783 C  CA   . HIS   B 1 127 ? -29.059 -28.124 -2.536  1.00 67.16  ? 127 HIS   B CA   1 
ATOM   2784 C  C    . HIS   B 1 127 ? -28.637 -29.593 -2.506  1.00 68.33  ? 127 HIS   B C    1 
ATOM   2785 O  O    . HIS   B 1 127 ? -28.598 -30.212 -1.439  1.00 64.72  ? 127 HIS   B O    1 
ATOM   2786 C  CB   . HIS   B 1 127 ? -27.866 -27.220 -2.266  1.00 65.09  ? 127 HIS   B CB   1 
ATOM   2787 C  CG   . HIS   B 1 127 ? -26.584 -27.724 -2.846  1.00 74.35  ? 127 HIS   B CG   1 
ATOM   2788 N  ND1  . HIS   B 1 127 ? -26.314 -27.674 -4.197  1.00 75.96  ? 127 HIS   B ND1  1 
ATOM   2789 C  CD2  . HIS   B 1 127 ? -25.506 -28.311 -2.270  1.00 72.34  ? 127 HIS   B CD2  1 
ATOM   2790 C  CE1  . HIS   B 1 127 ? -25.124 -28.201 -4.429  1.00 70.25  ? 127 HIS   B CE1  1 
ATOM   2791 N  NE2  . HIS   B 1 127 ? -24.614 -28.598 -3.276  1.00 71.08  ? 127 HIS   B NE2  1 
ATOM   2792 N  N    . PHE   B 1 128 ? -28.338 -30.179 -3.667  1.00 69.65  ? 128 PHE   B N    1 
ATOM   2793 C  CA   . PHE   B 1 128 ? -28.026 -31.594 -3.566  1.00 65.97  ? 128 PHE   B CA   1 
ATOM   2794 C  C    . PHE   B 1 128 ? -27.080 -31.877 -4.732  1.00 72.78  ? 128 PHE   B C    1 
ATOM   2795 O  O    . PHE   B 1 128 ? -27.303 -31.372 -5.849  1.00 67.51  ? 128 PHE   B O    1 
ATOM   2796 C  CB   . PHE   B 1 128 ? -29.358 -32.413 -3.599  1.00 75.29  ? 128 PHE   B CB   1 
ATOM   2797 C  CG   . PHE   B 1 128 ? -29.946 -32.658 -4.990  1.00 78.55  ? 128 PHE   B CG   1 
ATOM   2798 C  CD1  . PHE   B 1 128 ? -30.281 -31.646 -5.802  1.00 83.61  ? 128 PHE   B CD1  1 
ATOM   2799 C  CD2  . PHE   B 1 128 ? -30.382 -33.932 -5.357  1.00 83.67  ? 128 PHE   B CD2  1 
ATOM   2800 C  CE1  . PHE   B 1 128 ? -30.823 -31.884 -7.045  1.00 81.83  ? 128 PHE   B CE1  1 
ATOM   2801 C  CE2  . PHE   B 1 128 ? -31.001 -34.151 -6.600  1.00 88.21  ? 128 PHE   B CE2  1 
ATOM   2802 C  CZ   . PHE   B 1 128 ? -31.207 -33.116 -7.439  1.00 82.49  ? 128 PHE   B CZ   1 
ATOM   2803 N  N    . MET   B 1 129 ? -25.976 -32.595 -4.456  1.00 73.49  ? 129 MET   B N    1 
ATOM   2804 C  CA   . MET   B 1 129 ? -24.937 -32.830 -5.462  1.00 74.63  ? 129 MET   B CA   1 
ATOM   2805 C  C    . MET   B 1 129 ? -24.460 -34.278 -5.453  1.00 76.70  ? 129 MET   B C    1 
ATOM   2806 O  O    . MET   B 1 129 ? -24.206 -34.844 -4.383  1.00 81.52  ? 129 MET   B O    1 
ATOM   2807 C  CB   . MET   B 1 129 ? -23.757 -31.876 -5.239  1.00 77.16  ? 129 MET   B CB   1 
ATOM   2808 C  CG   . MET   B 1 129 ? -22.424 -32.297 -5.838  1.00 87.64  ? 129 MET   B CG   1 
ATOM   2809 S  SD   . MET   B 1 129 ? -21.130 -31.023 -5.696  1.00 104.81 ? 129 MET   B SD   1 
ATOM   2810 C  CE   . MET   B 1 129 ? -21.856 -29.629 -6.586  1.00 108.51 ? 129 MET   B CE   1 
ATOM   2811 N  N    . PHE   B 1 130 ? -24.357 -34.862 -6.658  1.00 74.47  ? 130 PHE   B N    1 
ATOM   2812 C  CA   . PHE   B 1 130 ? -23.851 -36.216 -6.905  1.00 79.97  ? 130 PHE   B CA   1 
ATOM   2813 C  C    . PHE   B 1 130 ? -22.685 -36.077 -7.867  1.00 86.67  ? 130 PHE   B C    1 
ATOM   2814 O  O    . PHE   B 1 130 ? -22.872 -35.579 -8.977  1.00 85.38  ? 130 PHE   B O    1 
ATOM   2815 C  CB   . PHE   B 1 130 ? -24.922 -37.125 -7.531  1.00 77.86  ? 130 PHE   B CB   1 
ATOM   2816 C  CG   . PHE   B 1 130 ? -26.185 -37.231 -6.726  1.00 82.98  ? 130 PHE   B CG   1 
ATOM   2817 C  CD1  . PHE   B 1 130 ? -26.234 -38.011 -5.600  1.00 88.21  ? 130 PHE   B CD1  1 
ATOM   2818 C  CD2  . PHE   B 1 130 ? -27.300 -36.480 -7.053  1.00 83.73  ? 130 PHE   B CD2  1 
ATOM   2819 C  CE1  . PHE   B 1 130 ? -27.382 -38.077 -4.846  1.00 89.19  ? 130 PHE   B CE1  1 
ATOM   2820 C  CE2  . PHE   B 1 130 ? -28.437 -36.540 -6.293  1.00 80.42  ? 130 PHE   B CE2  1 
ATOM   2821 C  CZ   . PHE   B 1 130 ? -28.482 -37.344 -5.198  1.00 80.85  ? 130 PHE   B CZ   1 
ATOM   2822 N  N    . ASN   B 1 131 ? -21.483 -36.478 -7.445  1.00 92.39  ? 131 ASN   B N    1 
ATOM   2823 C  CA   . ASN   B 1 131 ? -20.349 -36.597 -8.353  1.00 94.21  ? 131 ASN   B CA   1 
ATOM   2824 C  C    . ASN   B 1 131 ? -20.025 -38.038 -8.685  1.00 100.32 ? 131 ASN   B C    1 
ATOM   2825 O  O    . ASN   B 1 131 ? -19.267 -38.287 -9.631  1.00 107.20 ? 131 ASN   B O    1 
ATOM   2826 C  CB   . ASN   B 1 131 ? -19.101 -35.926 -7.771  1.00 107.31 ? 131 ASN   B CB   1 
ATOM   2827 C  CG   . ASN   B 1 131 ? -19.087 -34.430 -7.993  1.00 121.42 ? 131 ASN   B CG   1 
ATOM   2828 O  OD1  . ASN   B 1 131 ? -19.685 -33.673 -7.226  1.00 112.65 ? 131 ASN   B OD1  1 
ATOM   2829 N  ND2  . ASN   B 1 131 ? -18.367 -33.988 -9.028  1.00 132.71 ? 131 ASN   B ND2  1 
ATOM   2830 N  N    . GLN   B 1 132 ? -20.603 -38.976 -7.940  1.00 97.36  ? 132 GLN   B N    1 
ATOM   2831 C  CA   . GLN   B 1 132 ? -20.622 -40.388 -8.271  1.00 102.67 ? 132 GLN   B CA   1 
ATOM   2832 C  C    . GLN   B 1 132 ? -21.925 -40.970 -7.744  1.00 100.97 ? 132 GLN   B C    1 
ATOM   2833 O  O    . GLN   B 1 132 ? -22.478 -40.481 -6.754  1.00 100.60 ? 132 GLN   B O    1 
ATOM   2834 C  CB   . GLN   B 1 132 ? -19.400 -41.070 -7.674  1.00 110.83 ? 132 GLN   B CB   1 
ATOM   2835 C  CG   . GLN   B 1 132 ? -19.396 -40.937 -6.170  1.00 121.79 ? 132 GLN   B CG   1 
ATOM   2836 C  CD   . GLN   B 1 132 ? -18.166 -41.523 -5.496  1.00 139.23 ? 132 GLN   B CD   1 
ATOM   2837 O  OE1  . GLN   B 1 132 ? -17.321 -42.155 -6.135  1.00 145.95 ? 132 GLN   B OE1  1 
ATOM   2838 N  NE2  . GLN   B 1 132 ? -18.040 -41.270 -4.195  1.00 143.68 ? 132 GLN   B NE2  1 
ATOM   2839 N  N    . PHE   B 1 133 ? -22.437 -41.987 -8.430  1.00 98.75  ? 133 PHE   B N    1 
ATOM   2840 C  CA   . PHE   B 1 133 ? -23.675 -42.638 -8.030  1.00 97.70  ? 133 PHE   B CA   1 
ATOM   2841 C  C    . PHE   B 1 133 ? -23.390 -44.050 -7.553  1.00 112.11 ? 133 PHE   B C    1 
ATOM   2842 O  O    . PHE   B 1 133 ? -22.812 -44.851 -8.299  1.00 115.58 ? 133 PHE   B O    1 
ATOM   2843 C  CB   . PHE   B 1 133 ? -24.659 -42.689 -9.177  1.00 91.99  ? 133 PHE   B CB   1 
ATOM   2844 C  CG   . PHE   B 1 133 ? -25.063 -41.358 -9.656  1.00 93.47  ? 133 PHE   B CG   1 
ATOM   2845 C  CD1  . PHE   B 1 133 ? -24.296 -40.681 -10.587 1.00 93.76  ? 133 PHE   B CD1  1 
ATOM   2846 C  CD2  . PHE   B 1 133 ? -26.208 -40.756 -9.166  1.00 95.30  ? 133 PHE   B CD2  1 
ATOM   2847 C  CE1  . PHE   B 1 133 ? -24.683 -39.433 -11.048 1.00 88.32  ? 133 PHE   B CE1  1 
ATOM   2848 C  CE2  . PHE   B 1 133 ? -26.596 -39.501 -9.610  1.00 92.09  ? 133 PHE   B CE2  1 
ATOM   2849 C  CZ   . PHE   B 1 133 ? -25.831 -38.840 -10.555 1.00 85.46  ? 133 PHE   B CZ   1 
ATOM   2850 N  N    . SER   B 1 134 ? -23.817 -44.358 -6.325  1.00 116.18 ? 134 SER   B N    1 
ATOM   2851 C  CA   . SER   B 1 134 ? -23.548 -45.656 -5.729  1.00 115.06 ? 134 SER   B CA   1 
ATOM   2852 C  C    . SER   B 1 134 ? -24.524 -46.705 -6.249  1.00 116.52 ? 134 SER   B C    1 
ATOM   2853 O  O    . SER   B 1 134 ? -25.529 -46.407 -6.903  1.00 113.37 ? 134 SER   B O    1 
ATOM   2854 C  CB   . SER   B 1 134 ? -23.639 -45.606 -4.203  1.00 115.45 ? 134 SER   B CB   1 
ATOM   2855 O  OG   . SER   B 1 134 ? -24.970 -45.356 -3.786  1.00 113.77 ? 134 SER   B OG   1 
ATOM   2856 N  N    . LYS   B 1 135 ? -24.225 -47.950 -5.874  1.00 119.59 ? 135 LYS   B N    1 
ATOM   2857 C  CA   . LYS   B 1 135 ? -24.875 -49.131 -6.432  1.00 118.11 ? 135 LYS   B CA   1 
ATOM   2858 C  C    . LYS   B 1 135 ? -26.357 -49.085 -6.109  1.00 119.59 ? 135 LYS   B C    1 
ATOM   2859 O  O    . LYS   B 1 135 ? -27.198 -49.581 -6.868  1.00 117.69 ? 135 LYS   B O    1 
ATOM   2860 C  CB   . LYS   B 1 135 ? -24.265 -50.365 -5.782  1.00 119.86 ? 135 LYS   B CB   1 
ATOM   2861 C  CG   . LYS   B 1 135 ? -22.884 -50.790 -6.254  1.00 130.85 ? 135 LYS   B CG   1 
ATOM   2862 C  CD   . LYS   B 1 135 ? -21.957 -49.707 -5.646  1.00 124.03 ? 135 LYS   B CD   1 
ATOM   2863 C  CE   . LYS   B 1 135 ? -21.970 -49.755 -4.108  1.00 111.37 ? 135 LYS   B CE   1 
ATOM   2864 N  NZ   . LYS   B 1 135 ? -21.105 -48.729 -3.460  1.00 101.78 ? 135 LYS   B NZ   1 
ATOM   2865 N  N    . ASP   B 1 136 ? -26.672 -48.502 -4.946  1.00 124.05 ? 136 ASP   B N    1 
ATOM   2866 C  CA   . ASP   B 1 136 ? -28.016 -48.279 -4.417  1.00 120.97 ? 136 ASP   B CA   1 
ATOM   2867 C  C    . ASP   B 1 136 ? -28.099 -46.825 -3.972  1.00 117.98 ? 136 ASP   B C    1 
ATOM   2868 O  O    . ASP   B 1 136 ? -27.477 -46.442 -2.971  1.00 112.52 ? 136 ASP   B O    1 
ATOM   2869 C  CB   . ASP   B 1 136 ? -28.310 -49.209 -3.237  1.00 126.89 ? 136 ASP   B CB   1 
ATOM   2870 C  CG   . ASP   B 1 136 ? -29.727 -49.017 -2.660  1.00 131.25 ? 136 ASP   B CG   1 
ATOM   2871 O  OD1  . ASP   B 1 136 ? -30.573 -48.326 -3.292  1.00 124.13 ? 136 ASP   B OD1  1 
ATOM   2872 O  OD2  . ASP   B 1 136 ? -29.979 -49.554 -1.546  1.00 133.92 ? 136 ASP   B OD2  1 
ATOM   2873 N  N    . GLN   B 1 137 ? -28.875 -46.023 -4.695  1.00 116.92 ? 137 GLN   B N    1 
ATOM   2874 C  CA   . GLN   B 1 137 ? -29.089 -44.627 -4.340  1.00 108.80 ? 137 GLN   B CA   1 
ATOM   2875 C  C    . GLN   B 1 137 ? -30.462 -44.535 -3.691  1.00 102.16 ? 137 GLN   B C    1 
ATOM   2876 O  O    . GLN   B 1 137 ? -31.470 -44.412 -4.396  1.00 98.52  ? 137 GLN   B O    1 
ATOM   2877 C  CB   . GLN   B 1 137 ? -28.996 -43.720 -5.560  1.00 103.63 ? 137 GLN   B CB   1 
ATOM   2878 C  CG   . GLN   B 1 137 ? -28.411 -42.382 -5.177  1.00 98.66  ? 137 GLN   B CG   1 
ATOM   2879 C  CD   . GLN   B 1 137 ? -26.918 -42.507 -4.958  1.00 101.32 ? 137 GLN   B CD   1 
ATOM   2880 O  OE1  . GLN   B 1 137 ? -26.302 -43.469 -5.427  1.00 104.44 ? 137 GLN   B OE1  1 
ATOM   2881 N  NE2  . GLN   B 1 137 ? -26.337 -41.581 -4.196  1.00 98.32  ? 137 GLN   B NE2  1 
ATOM   2882 N  N    . LYS   B 1 138 ? -30.488 -44.596 -2.350  1.00 98.34  ? 138 LYS   B N    1 
ATOM   2883 C  CA   . LYS   B 1 138 ? -31.746 -44.499 -1.610  1.00 95.91  ? 138 LYS   B CA   1 
ATOM   2884 C  C    . LYS   B 1 138 ? -32.526 -43.229 -1.942  1.00 95.34  ? 138 LYS   B C    1 
ATOM   2885 O  O    . LYS   B 1 138 ? -33.762 -43.244 -1.926  1.00 98.14  ? 138 LYS   B O    1 
ATOM   2886 C  CB   . LYS   B 1 138 ? -31.502 -44.563 -0.098  1.00 93.32  ? 138 LYS   B CB   1 
ATOM   2887 C  CG   . LYS   B 1 138 ? -30.828 -45.807 0.448   1.00 90.60  ? 138 LYS   B CG   1 
ATOM   2888 C  CD   . LYS   B 1 138 ? -31.814 -46.908 0.721   1.00 92.39  ? 138 LYS   B CD   1 
ATOM   2889 C  CE   . LYS   B 1 138 ? -31.194 -47.989 1.595   1.00 97.49  ? 138 LYS   B CE   1 
ATOM   2890 N  NZ   . LYS   B 1 138 ? -31.011 -49.277 0.859   1.00 100.32 ? 138 LYS   B NZ   1 
ATOM   2891 N  N    . ASP   B 1 139 ? -31.844 -42.130 -2.250  1.00 97.95  ? 139 ASP   B N    1 
ATOM   2892 C  CA   . ASP   B 1 139 ? -32.515 -40.844 -2.439  1.00 96.73  ? 139 ASP   B CA   1 
ATOM   2893 C  C    . ASP   B 1 139 ? -32.839 -40.494 -3.902  1.00 93.04  ? 139 ASP   B C    1 
ATOM   2894 O  O    . ASP   B 1 139 ? -33.470 -39.458 -4.152  1.00 85.21  ? 139 ASP   B O    1 
ATOM   2895 C  CB   . ASP   B 1 139 ? -31.684 -39.755 -1.740  1.00 95.82  ? 139 ASP   B CB   1 
ATOM   2896 C  CG   . ASP   B 1 139 ? -30.267 -39.648 -2.283  1.00 97.31  ? 139 ASP   B CG   1 
ATOM   2897 O  OD1  . ASP   B 1 139 ? -29.896 -40.441 -3.183  1.00 94.54  ? 139 ASP   B OD1  1 
ATOM   2898 O  OD2  . ASP   B 1 139 ? -29.508 -38.799 -1.752  1.00 101.71 ? 139 ASP   B OD2  1 
ATOM   2899 N  N    . LEU   B 1 140 ? -32.502 -41.347 -4.871  1.00 93.66  ? 140 LEU   B N    1 
ATOM   2900 C  CA   . LEU   B 1 140 ? -33.018 -41.195 -6.228  1.00 91.07  ? 140 LEU   B CA   1 
ATOM   2901 C  C    . LEU   B 1 140 ? -34.184 -42.151 -6.456  1.00 92.16  ? 140 LEU   B C    1 
ATOM   2902 O  O    . LEU   B 1 140 ? -34.043 -43.369 -6.275  1.00 94.65  ? 140 LEU   B O    1 
ATOM   2903 C  CB   . LEU   B 1 140 ? -31.946 -41.430 -7.293  1.00 85.86  ? 140 LEU   B CB   1 
ATOM   2904 C  CG   . LEU   B 1 140 ? -30.814 -40.432 -7.388  1.00 81.26  ? 140 LEU   B CG   1 
ATOM   2905 C  CD1  . LEU   B 1 140 ? -29.825 -40.905 -8.417  1.00 78.77  ? 140 LEU   B CD1  1 
ATOM   2906 C  CD2  . LEU   B 1 140 ? -31.413 -39.116 -7.763  1.00 84.87  ? 140 LEU   B CD2  1 
ATOM   2907 N  N    . ILE   B 1 141 ? -35.328 -41.589 -6.845  1.00 87.93  ? 141 ILE   B N    1 
ATOM   2908 C  CA   . ILE   B 1 141 ? -36.418 -42.337 -7.468  1.00 86.30  ? 141 ILE   B CA   1 
ATOM   2909 C  C    . ILE   B 1 141 ? -36.047 -42.663 -8.911  1.00 91.38  ? 141 ILE   B C    1 
ATOM   2910 O  O    . ILE   B 1 141 ? -35.879 -41.762 -9.742  1.00 91.92  ? 141 ILE   B O    1 
ATOM   2911 C  CB   . ILE   B 1 141 ? -37.735 -41.548 -7.397  1.00 84.75  ? 141 ILE   B CB   1 
ATOM   2912 C  CG1  . ILE   B 1 141 ? -38.219 -41.401 -5.944  1.00 82.43  ? 141 ILE   B CG1  1 
ATOM   2913 C  CG2  . ILE   B 1 141 ? -38.771 -42.086 -8.385  1.00 82.91  ? 141 ILE   B CG2  1 
ATOM   2914 C  CD1  . ILE   B 1 141 ? -39.368 -40.424 -5.794  1.00 82.65  ? 141 ILE   B CD1  1 
ATOM   2915 N  N    . LEU   B 1 142 ? -35.916 -43.956 -9.210  1.00 95.27  ? 142 LEU   B N    1 
ATOM   2916 C  CA   . LEU   B 1 142 ? -35.531 -44.437 -10.533 1.00 94.70  ? 142 LEU   B CA   1 
ATOM   2917 C  C    . LEU   B 1 142 ? -36.749 -44.976 -11.268 1.00 87.83  ? 142 LEU   B C    1 
ATOM   2918 O  O    . LEU   B 1 142 ? -37.491 -45.805 -10.731 1.00 84.08  ? 142 LEU   B O    1 
ATOM   2919 C  CB   . LEU   B 1 142 ? -34.453 -45.511 -10.417 1.00 95.62  ? 142 LEU   B CB   1 
ATOM   2920 C  CG   . LEU   B 1 142 ? -33.223 -45.016 -9.673  1.00 87.99  ? 142 LEU   B CG   1 
ATOM   2921 C  CD1  . LEU   B 1 142 ? -32.515 -46.129 -8.896  1.00 90.14  ? 142 LEU   B CD1  1 
ATOM   2922 C  CD2  . LEU   B 1 142 ? -32.322 -44.389 -10.707 1.00 82.95  ? 142 LEU   B CD2  1 
ATOM   2923 N  N    . GLN   B 1 143 ? -36.956 -44.497 -12.484 1.00 86.76  ? 143 GLN   B N    1 
ATOM   2924 C  CA   . GLN   B 1 143 ? -38.158 -44.825 -13.230 1.00 95.75  ? 143 GLN   B CA   1 
ATOM   2925 C  C    . GLN   B 1 143 ? -37.806 -45.378 -14.596 1.00 101.17 ? 143 GLN   B C    1 
ATOM   2926 O  O    . GLN   B 1 143 ? -36.868 -44.902 -15.240 1.00 104.92 ? 143 GLN   B O    1 
ATOM   2927 C  CB   . GLN   B 1 143 ? -39.071 -43.619 -13.405 1.00 93.99  ? 143 GLN   B CB   1 
ATOM   2928 C  CG   . GLN   B 1 143 ? -40.068 -43.438 -12.298 1.00 92.69  ? 143 GLN   B CG   1 
ATOM   2929 C  CD   . GLN   B 1 143 ? -40.638 -42.054 -12.287 1.00 96.01  ? 143 GLN   B CD   1 
ATOM   2930 O  OE1  . GLN   B 1 143 ? -40.247 -41.201 -13.089 1.00 92.21  ? 143 GLN   B OE1  1 
ATOM   2931 N  NE2  . GLN   B 1 143 ? -41.594 -41.821 -11.398 1.00 101.34 ? 143 GLN   B NE2  1 
ATOM   2932 N  N    . GLY   B 1 144 ? -38.581 -46.358 -15.050 1.00 98.78  ? 144 GLY   B N    1 
ATOM   2933 C  CA   . GLY   B 1 144 ? -38.220 -46.997 -16.297 1.00 102.91 ? 144 GLY   B CA   1 
ATOM   2934 C  C    . GLY   B 1 144 ? -36.850 -47.644 -16.194 1.00 99.30  ? 144 GLY   B C    1 
ATOM   2935 O  O    . GLY   B 1 144 ? -36.502 -48.265 -15.184 1.00 99.08  ? 144 GLY   B O    1 
ATOM   2936 N  N    . ASP   B 1 145 ? -36.044 -47.470 -17.238 1.00 98.56  ? 145 ASP   B N    1 
ATOM   2937 C  CA   . ASP   B 1 145 ? -34.854 -48.285 -17.461 1.00 106.75 ? 145 ASP   B CA   1 
ATOM   2938 C  C    . ASP   B 1 145 ? -33.631 -47.788 -16.699 1.00 104.06 ? 145 ASP   B C    1 
ATOM   2939 O  O    . ASP   B 1 145 ? -32.498 -48.178 -17.025 1.00 101.32 ? 145 ASP   B O    1 
ATOM   2940 C  CB   . ASP   B 1 145 ? -34.522 -48.337 -18.958 1.00 113.62 ? 145 ASP   B CB   1 
ATOM   2941 C  CG   . ASP   B 1 145 ? -35.579 -49.087 -19.780 1.00 120.10 ? 145 ASP   B CG   1 
ATOM   2942 O  OD1  . ASP   B 1 145 ? -36.258 -49.993 -19.238 1.00 124.81 ? 145 ASP   B OD1  1 
ATOM   2943 O  OD2  . ASP   B 1 145 ? -35.696 -48.798 -20.995 1.00 120.35 ? 145 ASP   B OD2  1 
ATOM   2944 N  N    . ALA   B 1 146 ? -33.832 -46.935 -15.706 1.00 101.27 ? 146 ALA   B N    1 
ATOM   2945 C  CA   . ALA   B 1 146 ? -32.721 -46.250 -15.074 1.00 102.57 ? 146 ALA   B CA   1 
ATOM   2946 C  C    . ALA   B 1 146 ? -31.973 -47.192 -14.133 1.00 104.41 ? 146 ALA   B C    1 
ATOM   2947 O  O    . ALA   B 1 146 ? -32.584 -47.932 -13.354 1.00 103.47 ? 146 ALA   B O    1 
ATOM   2948 C  CB   . ALA   B 1 146 ? -33.244 -45.023 -14.328 1.00 99.25  ? 146 ALA   B CB   1 
ATOM   2949 N  N    . THR   B 1 147 ? -30.639 -47.166 -14.218 1.00 104.13 ? 147 THR   B N    1 
ATOM   2950 C  CA   . THR   B 1 147 ? -29.771 -48.032 -13.424 1.00 111.89 ? 147 THR   B CA   1 
ATOM   2951 C  C    . THR   B 1 147 ? -28.533 -47.269 -12.948 1.00 113.91 ? 147 THR   B C    1 
ATOM   2952 O  O    . THR   B 1 147 ? -27.969 -46.454 -13.691 1.00 107.49 ? 147 THR   B O    1 
ATOM   2953 C  CB   . THR   B 1 147 ? -29.339 -49.275 -14.230 1.00 113.23 ? 147 THR   B CB   1 
ATOM   2954 O  OG1  . THR   B 1 147 ? -28.582 -48.867 -15.374 1.00 117.60 ? 147 THR   B OG1  1 
ATOM   2955 C  CG2  . THR   B 1 147 ? -30.536 -50.073 -14.715 1.00 112.31 ? 147 THR   B CG2  1 
ATOM   2956 N  N    . THR   B 1 148 ? -28.108 -47.540 -11.707 1.00 115.67 ? 148 THR   B N    1 
ATOM   2957 C  CA   . THR   B 1 148 ? -26.908 -46.932 -11.135 1.00 113.64 ? 148 THR   B CA   1 
ATOM   2958 C  C    . THR   B 1 148 ? -25.950 -48.036 -10.713 1.00 116.17 ? 148 THR   B C    1 
ATOM   2959 O  O    . THR   B 1 148 ? -26.317 -49.210 -10.652 1.00 116.15 ? 148 THR   B O    1 
ATOM   2960 C  CB   . THR   B 1 148 ? -27.215 -46.033 -9.918  1.00 110.74 ? 148 THR   B CB   1 
ATOM   2961 O  OG1  . THR   B 1 148 ? -27.436 -46.836 -8.755  1.00 114.29 ? 148 THR   B OG1  1 
ATOM   2962 C  CG2  . THR   B 1 148 ? -28.457 -45.214 -10.147 1.00 104.17 ? 148 THR   B CG2  1 
ATOM   2963 N  N    . GLY   B 1 149 ? -24.711 -47.645 -10.399 1.00 116.03 ? 149 GLY   B N    1 
ATOM   2964 C  CA   . GLY   B 1 149 ? -23.680 -48.563 -9.965  1.00 117.12 ? 149 GLY   B CA   1 
ATOM   2965 C  C    . GLY   B 1 149 ? -22.623 -48.879 -11.009 1.00 126.50 ? 149 GLY   B C    1 
ATOM   2966 O  O    . GLY   B 1 149 ? -21.496 -49.246 -10.634 1.00 129.22 ? 149 GLY   B O    1 
ATOM   2967 N  N    . THR   B 1 150 ? -22.956 -48.745 -12.302 1.00 130.57 ? 150 THR   B N    1 
ATOM   2968 C  CA   . THR   B 1 150 ? -22.057 -49.045 -13.429 1.00 135.63 ? 150 THR   B CA   1 
ATOM   2969 C  C    . THR   B 1 150 ? -20.971 -47.993 -13.515 1.00 131.77 ? 150 THR   B C    1 
ATOM   2970 O  O    . THR   B 1 150 ? -21.155 -46.948 -14.151 1.00 128.68 ? 150 THR   B O    1 
ATOM   2971 C  CB   . THR   B 1 150 ? -22.807 -49.093 -14.758 1.00 138.54 ? 150 THR   B CB   1 
ATOM   2972 O  OG1  . THR   B 1 150 ? -23.770 -50.154 -14.739 1.00 153.01 ? 150 THR   B OG1  1 
ATOM   2973 C  CG2  . THR   B 1 150 ? -21.822 -49.279 -15.952 1.00 128.45 ? 150 THR   B CG2  1 
ATOM   2974 N  N    . ASP   B 1 151 ? -19.829 -48.277 -12.889 1.00 132.78 ? 151 ASP   B N    1 
ATOM   2975 C  CA   . ASP   B 1 151 ? -18.686 -47.385 -12.948 1.00 131.29 ? 151 ASP   B CA   1 
ATOM   2976 C  C    . ASP   B 1 151 ? -18.995 -46.085 -12.199 1.00 125.43 ? 151 ASP   B C    1 
ATOM   2977 O  O    . ASP   B 1 151 ? -18.515 -45.006 -12.553 1.00 121.91 ? 151 ASP   B O    1 
ATOM   2978 C  CB   . ASP   B 1 151 ? -18.300 -47.160 -14.426 1.00 138.24 ? 151 ASP   B CB   1 
ATOM   2979 C  CG   . ASP   B 1 151 ? -17.041 -46.332 -14.619 1.00 154.44 ? 151 ASP   B CG   1 
ATOM   2980 O  OD1  . ASP   B 1 151 ? -16.277 -46.133 -13.642 1.00 159.42 ? 151 ASP   B OD1  1 
ATOM   2981 O  OD2  . ASP   B 1 151 ? -16.821 -45.884 -15.775 1.00 154.75 ? 151 ASP   B OD2  1 
ATOM   2982 N  N    . GLY   B 1 152 ? -19.825 -46.179 -11.162 1.00 123.08 ? 152 GLY   B N    1 
ATOM   2983 C  CA   . GLY   B 1 152 ? -20.200 -45.000 -10.401 1.00 117.16 ? 152 GLY   B CA   1 
ATOM   2984 C  C    . GLY   B 1 152 ? -21.030 -44.009 -11.180 1.00 107.79 ? 152 GLY   B C    1 
ATOM   2985 O  O    . GLY   B 1 152 ? -20.990 -42.807 -10.894 1.00 105.90 ? 152 GLY   B O    1 
ATOM   2986 N  N    . ASN   B 1 153 ? -21.787 -44.482 -12.159 1.00 106.67 ? 153 ASN   B N    1 
ATOM   2987 C  CA   . ASN   B 1 153 ? -22.506 -43.613 -13.069 1.00 104.86 ? 153 ASN   B CA   1 
ATOM   2988 C  C    . ASN   B 1 153 ? -23.980 -43.970 -13.109 1.00 102.49 ? 153 ASN   B C    1 
ATOM   2989 O  O    . ASN   B 1 153 ? -24.398 -45.100 -12.828 1.00 104.62 ? 153 ASN   B O    1 
ATOM   2990 C  CB   . ASN   B 1 153 ? -21.943 -43.661 -14.495 1.00 102.43 ? 153 ASN   B CB   1 
ATOM   2991 C  CG   . ASN   B 1 153 ? -20.559 -43.072 -14.592 1.00 109.34 ? 153 ASN   B CG   1 
ATOM   2992 O  OD1  . ASN   B 1 153 ? -20.133 -42.292 -13.734 1.00 105.53 ? 153 ASN   B OD1  1 
ATOM   2993 N  ND2  . ASN   B 1 153 ? -19.844 -43.438 -15.640 1.00 110.37 ? 153 ASN   B ND2  1 
ATOM   2994 N  N    . LEU   B 1 154 ? -24.750 -42.954 -13.473 1.00 92.98  ? 154 LEU   B N    1 
ATOM   2995 C  CA   . LEU   B 1 154 ? -26.177 -43.072 -13.689 1.00 91.21  ? 154 LEU   B CA   1 
ATOM   2996 C  C    . LEU   B 1 154 ? -26.401 -43.295 -15.167 1.00 91.36  ? 154 LEU   B C    1 
ATOM   2997 O  O    . LEU   B 1 154 ? -25.992 -42.472 -15.983 1.00 92.85  ? 154 LEU   B O    1 
ATOM   2998 C  CB   . LEU   B 1 154 ? -26.897 -41.809 -13.227 1.00 90.16  ? 154 LEU   B CB   1 
ATOM   2999 C  CG   . LEU   B 1 154 ? -28.425 -41.733 -13.335 1.00 89.42  ? 154 LEU   B CG   1 
ATOM   3000 C  CD1  . LEU   B 1 154 ? -29.131 -42.736 -12.465 1.00 91.91  ? 154 LEU   B CD1  1 
ATOM   3001 C  CD2  . LEU   B 1 154 ? -28.886 -40.360 -12.957 1.00 90.93  ? 154 LEU   B CD2  1 
ATOM   3002 N  N    . GLU   B 1 155 ? -27.012 -44.411 -15.514 1.00 94.95  ? 155 GLU   B N    1 
ATOM   3003 C  CA   . GLU   B 1 155 ? -27.380 -44.684 -16.894 1.00 97.66  ? 155 GLU   B CA   1 
ATOM   3004 C  C    . GLU   B 1 155 ? -28.894 -44.571 -16.971 1.00 100.00 ? 155 GLU   B C    1 
ATOM   3005 O  O    . GLU   B 1 155 ? -29.620 -45.418 -16.442 1.00 102.93 ? 155 GLU   B O    1 
ATOM   3006 C  CB   . GLU   B 1 155 ? -26.864 -46.048 -17.354 1.00 106.22 ? 155 GLU   B CB   1 
ATOM   3007 C  CG   . GLU   B 1 155 ? -25.360 -46.276 -17.079 1.00 111.86 ? 155 GLU   B CG   1 
ATOM   3008 C  CD   . GLU   B 1 155 ? -24.466 -45.983 -18.291 1.00 111.61 ? 155 GLU   B CD   1 
ATOM   3009 O  OE1  . GLU   B 1 155 ? -24.977 -45.381 -19.274 1.00 104.69 ? 155 GLU   B OE1  1 
ATOM   3010 O  OE2  . GLU   B 1 155 ? -23.252 -46.336 -18.238 1.00 114.30 ? 155 GLU   B OE2  1 
ATOM   3011 N  N    . LEU   B 1 156 ? -29.361 -43.484 -17.573 1.00 101.29 ? 156 LEU   B N    1 
ATOM   3012 C  CA   . LEU   B 1 156 ? -30.791 -43.299 -17.766 1.00 101.80 ? 156 LEU   B CA   1 
ATOM   3013 C  C    . LEU   B 1 156 ? -31.316 -44.257 -18.822 1.00 108.51 ? 156 LEU   B C    1 
ATOM   3014 O  O    . LEU   B 1 156 ? -32.399 -44.822 -18.667 1.00 111.41 ? 156 LEU   B O    1 
ATOM   3015 C  CB   . LEU   B 1 156 ? -31.081 -41.845 -18.158 1.00 102.17 ? 156 LEU   B CB   1 
ATOM   3016 C  CG   . LEU   B 1 156 ? -30.916 -40.688 -17.158 1.00 97.48  ? 156 LEU   B CG   1 
ATOM   3017 C  CD1  . LEU   B 1 156 ? -31.751 -39.495 -17.548 1.00 88.91  ? 156 LEU   B CD1  1 
ATOM   3018 C  CD2  . LEU   B 1 156 ? -31.326 -41.131 -15.753 1.00 94.94  ? 156 LEU   B CD2  1 
ATOM   3019 N  N    . THR   B 1 157 ? -30.569 -44.461 -19.899 1.00 111.42 ? 157 THR   B N    1 
ATOM   3020 C  CA   . THR   B 1 157 ? -30.974 -45.432 -20.902 1.00 114.69 ? 157 THR   B CA   1 
ATOM   3021 C  C    . THR   B 1 157 ? -30.272 -46.773 -20.698 1.00 124.26 ? 157 THR   B C    1 
ATOM   3022 O  O    . THR   B 1 157 ? -29.174 -46.866 -20.141 1.00 126.09 ? 157 THR   B O    1 
ATOM   3023 C  CB   . THR   B 1 157 ? -30.726 -44.911 -22.323 1.00 110.42 ? 157 THR   B CB   1 
ATOM   3024 O  OG1  . THR   B 1 157 ? -29.316 -44.894 -22.633 1.00 106.73 ? 157 THR   B OG1  1 
ATOM   3025 C  CG2  . THR   B 1 157 ? -31.349 -43.556 -22.476 1.00 105.39 ? 157 THR   B CG2  1 
ATOM   3026 N  N    . ARG   B 1 158 ? -30.942 -47.817 -21.173 1.00 126.28 ? 158 ARG   B N    1 
ATOM   3027 C  CA   . ARG   B 1 158 ? -30.449 -49.188 -21.130 1.00 125.56 ? 158 ARG   B CA   1 
ATOM   3028 C  C    . ARG   B 1 158 ? -29.277 -49.443 -22.086 1.00 121.68 ? 158 ARG   B C    1 
ATOM   3029 O  O    . ARG   B 1 158 ? -29.208 -48.904 -23.195 1.00 125.03 ? 158 ARG   B O    1 
ATOM   3030 C  CB   . ARG   B 1 158 ? -31.661 -50.091 -21.380 1.00 129.94 ? 158 ARG   B CB   1 
ATOM   3031 C  CG   . ARG   B 1 158 ? -31.587 -51.592 -21.481 1.00 137.18 ? 158 ARG   B CG   1 
ATOM   3032 C  CD   . ARG   B 1 158 ? -33.081 -52.076 -21.497 1.00 135.68 ? 158 ARG   B CD   1 
ATOM   3033 N  NE   . ARG   B 1 158 ? -33.231 -53.502 -21.745 1.00 151.71 ? 158 ARG   B NE   1 
ATOM   3034 C  CZ   . ARG   B 1 158 ? -33.090 -54.505 -20.898 1.00 159.59 ? 158 ARG   B CZ   1 
ATOM   3035 N  NH1  . ARG   B 1 158 ? -32.635 -54.320 -19.675 1.00 158.20 ? 158 ARG   B NH1  1 
ATOM   3036 N  NH2  . ARG   B 1 158 ? -33.356 -55.722 -21.315 1.00 163.40 ? 158 ARG   B NH2  1 
ATOM   3037 N  N    . VAL   B 1 159 ? -28.345 -50.273 -21.620 1.00 124.62 ? 159 VAL   B N    1 
ATOM   3038 C  CA   . VAL   B 1 159 ? -27.060 -50.534 -22.253 1.00 127.21 ? 159 VAL   B CA   1 
ATOM   3039 C  C    . VAL   B 1 159 ? -26.715 -51.995 -21.976 1.00 131.47 ? 159 VAL   B C    1 
ATOM   3040 O  O    . VAL   B 1 159 ? -26.938 -52.500 -20.867 1.00 128.71 ? 159 VAL   B O    1 
ATOM   3041 C  CB   . VAL   B 1 159 ? -25.976 -49.579 -21.704 1.00 125.71 ? 159 VAL   B CB   1 
ATOM   3042 C  CG1  . VAL   B 1 159 ? -24.606 -50.041 -22.167 1.00 130.01 ? 159 VAL   B CG1  1 
ATOM   3043 C  CG2  . VAL   B 1 159 ? -26.259 -48.136 -22.125 1.00 124.53 ? 159 VAL   B CG2  1 
ATOM   3044 N  N    . SER   B 1 160 ? -26.233 -52.689 -23.006 1.00 134.04 ? 160 SER   B N    1 
ATOM   3045 C  CA   . SER   B 1 160 ? -25.828 -54.079 -22.857 1.00 140.08 ? 160 SER   B CA   1 
ATOM   3046 C  C    . SER   B 1 160 ? -24.466 -54.165 -22.150 1.00 144.44 ? 160 SER   B C    1 
ATOM   3047 O  O    . SER   B 1 160 ? -23.654 -53.212 -22.118 1.00 143.00 ? 160 SER   B O    1 
ATOM   3048 C  CB   . SER   B 1 160 ? -25.734 -54.773 -24.228 1.00 143.17 ? 160 SER   B CB   1 
ATOM   3049 O  OG   . SER   B 1 160 ? -24.665 -54.276 -25.043 1.00 144.69 ? 160 SER   B OG   1 
ATOM   3050 N  N    . SER   B 1 161 ? -24.217 -55.329 -21.557 1.00 145.70 ? 161 SER   B N    1 
ATOM   3051 C  CA   . SER   B 1 161 ? -23.079 -55.429 -20.634 1.00 148.08 ? 161 SER   B CA   1 
ATOM   3052 C  C    . SER   B 1 161 ? -21.757 -55.111 -21.317 1.00 154.33 ? 161 SER   B C    1 
ATOM   3053 O  O    . SER   B 1 161 ? -20.855 -54.582 -20.668 1.00 153.58 ? 161 SER   B O    1 
ATOM   3054 C  CB   . SER   B 1 161 ? -23.041 -56.827 -20.014 1.00 146.86 ? 161 SER   B CB   1 
ATOM   3055 O  OG   . SER   B 1 161 ? -22.758 -57.823 -20.978 1.00 154.14 ? 161 SER   B OG   1 
ATOM   3056 N  N    . ASN   B 1 162 ? -21.612 -55.454 -22.618 1.00 157.03 ? 162 ASN   B N    1 
ATOM   3057 C  CA   . ASN   B 1 162 ? -20.373 -55.150 -23.348 1.00 153.82 ? 162 ASN   B CA   1 
ATOM   3058 C  C    . ASN   B 1 162 ? -20.130 -53.641 -23.485 1.00 150.60 ? 162 ASN   B C    1 
ATOM   3059 O  O    . ASN   B 1 162 ? -18.988 -53.205 -23.692 1.00 147.81 ? 162 ASN   B O    1 
ATOM   3060 C  CB   . ASN   B 1 162 ? -20.386 -55.835 -24.735 1.00 149.16 ? 162 ASN   B CB   1 
ATOM   3061 C  CG   . ASN   B 1 162 ? -21.671 -55.554 -25.543 1.00 147.34 ? 162 ASN   B CG   1 
ATOM   3062 O  OD1  . ASN   B 1 162 ? -22.429 -54.632 -25.241 1.00 150.33 ? 162 ASN   B OD1  1 
ATOM   3063 N  ND2  . ASN   B 1 162 ? -21.888 -56.333 -26.593 1.00 145.50 ? 162 ASN   B ND2  1 
ATOM   3064 N  N    . GLY   B 1 163 ? -21.174 -52.829 -23.350 1.00 146.79 ? 163 GLY   B N    1 
ATOM   3065 C  CA   . GLY   B 1 163 ? -21.055 -51.385 -23.452 1.00 142.73 ? 163 GLY   B CA   1 
ATOM   3066 C  C    . GLY   B 1 163 ? -21.798 -50.752 -24.613 1.00 143.60 ? 163 GLY   B C    1 
ATOM   3067 O  O    . GLY   B 1 163 ? -21.879 -49.516 -24.662 1.00 143.97 ? 163 GLY   B O    1 
ATOM   3068 N  N    . SER   B 1 164 ? -22.337 -51.522 -25.561 1.00 142.57 ? 164 SER   B N    1 
ATOM   3069 C  CA   . SER   B 1 164 ? -23.126 -50.938 -26.637 1.00 137.27 ? 164 SER   B CA   1 
ATOM   3070 C  C    . SER   B 1 164 ? -24.513 -50.537 -26.129 1.00 135.31 ? 164 SER   B C    1 
ATOM   3071 O  O    . SER   B 1 164 ? -25.083 -51.194 -25.252 1.00 134.00 ? 164 SER   B O    1 
ATOM   3072 C  CB   . SER   B 1 164 ? -23.271 -51.914 -27.807 1.00 138.57 ? 164 SER   B CB   1 
ATOM   3073 O  OG   . SER   B 1 164 ? -22.122 -51.926 -28.638 1.00 137.12 ? 164 SER   B OG   1 
ATOM   3074 N  N    . PRO   B 1 165 ? -25.078 -49.464 -26.667 1.00 128.11 ? 165 PRO   B N    1 
ATOM   3075 C  CA   . PRO   B 1 165 ? -26.424 -49.057 -26.265 1.00 120.27 ? 165 PRO   B CA   1 
ATOM   3076 C  C    . PRO   B 1 165 ? -27.493 -49.932 -26.904 1.00 123.49 ? 165 PRO   B C    1 
ATOM   3077 O  O    . PRO   B 1 165 ? -27.245 -50.722 -27.813 1.00 126.07 ? 165 PRO   B O    1 
ATOM   3078 C  CB   . PRO   B 1 165 ? -26.505 -47.620 -26.770 1.00 122.41 ? 165 PRO   B CB   1 
ATOM   3079 C  CG   . PRO   B 1 165 ? -25.641 -47.622 -27.971 1.00 124.69 ? 165 PRO   B CG   1 
ATOM   3080 C  CD   . PRO   B 1 165 ? -24.492 -48.532 -27.646 1.00 126.47 ? 165 PRO   B CD   1 
ATOM   3081 N  N    . GLN   B 1 166 ? -28.710 -49.768 -26.402 1.00 124.83 ? 166 GLN   B N    1 
ATOM   3082 C  CA   . GLN   B 1 166 ? -29.871 -50.504 -26.877 1.00 123.71 ? 166 GLN   B CA   1 
ATOM   3083 C  C    . GLN   B 1 166 ? -30.947 -49.498 -27.257 1.00 118.02 ? 166 GLN   B C    1 
ATOM   3084 O  O    . GLN   B 1 166 ? -30.925 -48.350 -26.812 1.00 119.41 ? 166 GLN   B O    1 
ATOM   3085 C  CB   . GLN   B 1 166 ? -30.394 -51.475 -25.803 1.00 120.82 ? 166 GLN   B CB   1 
ATOM   3086 C  CG   . GLN   B 1 166 ? -29.516 -52.710 -25.599 1.00 122.64 ? 166 GLN   B CG   1 
ATOM   3087 C  CD   . GLN   B 1 166 ? -30.159 -53.718 -24.673 1.00 122.43 ? 166 GLN   B CD   1 
ATOM   3088 O  OE1  . GLN   B 1 166 ? -30.991 -53.356 -23.854 1.00 126.13 ? 166 GLN   B OE1  1 
ATOM   3089 N  NE2  . GLN   B 1 166 ? -29.769 -54.985 -24.790 1.00 117.63 ? 166 GLN   B NE2  1 
ATOM   3090 N  N    . GLY   B 1 167 ? -31.887 -49.925 -28.076 1.00 122.15 ? 167 GLY   B N    1 
ATOM   3091 C  CA   . GLY   B 1 167 ? -32.882 -49.008 -28.592 1.00 128.80 ? 167 GLY   B CA   1 
ATOM   3092 C  C    . GLY   B 1 167 ? -34.224 -49.053 -27.855 1.00 125.37 ? 167 GLY   B C    1 
ATOM   3093 O  O    . GLY   B 1 167 ? -34.511 -49.976 -27.093 1.00 128.17 ? 167 GLY   B O    1 
ATOM   3094 N  N    . SER   B 1 168 ? -35.028 -48.017 -28.106 1.00 118.63 ? 168 SER   B N    1 
ATOM   3095 C  CA   . SER   B 1 168 ? -36.390 -47.888 -27.590 1.00 120.95 ? 168 SER   B CA   1 
ATOM   3096 C  C    . SER   B 1 168 ? -36.452 -48.096 -26.078 1.00 121.85 ? 168 SER   B C    1 
ATOM   3097 O  O    . SER   B 1 168 ? -37.226 -48.906 -25.560 1.00 121.53 ? 168 SER   B O    1 
ATOM   3098 C  CB   . SER   B 1 168 ? -37.331 -48.829 -28.327 1.00 123.00 ? 168 SER   B CB   1 
ATOM   3099 O  OG   . SER   B 1 168 ? -37.629 -48.280 -29.599 1.00 125.62 ? 168 SER   B OG   1 
ATOM   3100 N  N    . SER   B 1 169 ? -35.634 -47.314 -25.375 1.00 123.04 ? 169 SER   B N    1 
ATOM   3101 C  CA   . SER   B 1 169 ? -35.513 -47.317 -23.924 1.00 122.51 ? 169 SER   B CA   1 
ATOM   3102 C  C    . SER   B 1 169 ? -35.930 -45.944 -23.407 1.00 117.46 ? 169 SER   B C    1 
ATOM   3103 O  O    . SER   B 1 169 ? -35.664 -44.940 -24.064 1.00 115.59 ? 169 SER   B O    1 
ATOM   3104 C  CB   . SER   B 1 169 ? -34.053 -47.642 -23.522 1.00 117.02 ? 169 SER   B CB   1 
ATOM   3105 O  OG   . SER   B 1 169 ? -33.837 -47.633 -22.123 1.00 114.77 ? 169 SER   B OG   1 
ATOM   3106 N  N    . VAL   B 1 170 ? -36.640 -45.895 -22.271 1.00 117.02 ? 170 VAL   B N    1 
ATOM   3107 C  CA   . VAL   B 1 170 ? -36.796 -44.668 -21.486 1.00 108.24 ? 170 VAL   B CA   1 
ATOM   3108 C  C    . VAL   B 1 170 ? -36.412 -44.970 -20.048 1.00 111.81 ? 170 VAL   B C    1 
ATOM   3109 O  O    . VAL   B 1 170 ? -36.897 -45.939 -19.451 1.00 110.95 ? 170 VAL   B O    1 
ATOM   3110 C  CB   . VAL   B 1 170 ? -38.218 -44.063 -21.518 1.00 107.84 ? 170 VAL   B CB   1 
ATOM   3111 C  CG1  . VAL   B 1 170 ? -38.639 -43.804 -22.904 1.00 118.56 ? 170 VAL   B CG1  1 
ATOM   3112 C  CG2  . VAL   B 1 170 ? -39.256 -44.909 -20.776 1.00 108.11 ? 170 VAL   B CG2  1 
ATOM   3113 N  N    . GLY   B 1 171 ? -35.543 -44.151 -19.491 1.00 109.73 ? 171 GLY   B N    1 
ATOM   3114 C  CA   . GLY   B 1 171 ? -35.247 -44.240 -18.078 1.00 103.67 ? 171 GLY   B CA   1 
ATOM   3115 C  C    . GLY   B 1 171 ? -35.301 -42.861 -17.487 1.00 95.51  ? 171 GLY   B C    1 
ATOM   3116 O  O    . GLY   B 1 171 ? -35.000 -41.869 -18.149 1.00 92.93  ? 171 GLY   B O    1 
ATOM   3117 N  N    . ARG   B 1 172 ? -35.697 -42.794 -16.231 1.00 98.94  ? 172 ARG   B N    1 
ATOM   3118 C  CA   . ARG   B 1 172 ? -35.927 -41.450 -15.762 1.00 92.24  ? 172 ARG   B CA   1 
ATOM   3119 C  C    . ARG   B 1 172 ? -35.533 -41.472 -14.281 1.00 90.52  ? 172 ARG   B C    1 
ATOM   3120 O  O    . ARG   B 1 172 ? -35.702 -42.501 -13.615 1.00 90.73  ? 172 ARG   B O    1 
ATOM   3121 C  CB   . ARG   B 1 172 ? -37.395 -41.076 -16.057 1.00 86.00  ? 172 ARG   B CB   1 
ATOM   3122 C  CG   . ARG   B 1 172 ? -37.506 -39.632 -16.037 1.00 90.40  ? 172 ARG   B CG   1 
ATOM   3123 C  CD   . ARG   B 1 172 ? -38.794 -38.889 -16.333 1.00 90.70  ? 172 ARG   B CD   1 
ATOM   3124 N  NE   . ARG   B 1 172 ? -39.834 -38.969 -15.325 1.00 98.32  ? 172 ARG   B NE   1 
ATOM   3125 C  CZ   . ARG   B 1 172 ? -41.045 -39.434 -15.520 1.00 104.79 ? 172 ARG   B CZ   1 
ATOM   3126 N  NH1  . ARG   B 1 172 ? -41.401 -39.814 -16.736 1.00 116.45 ? 172 ARG   B NH1  1 
ATOM   3127 N  NH2  . ARG   B 1 172 ? -41.904 -39.443 -14.513 1.00 104.09 ? 172 ARG   B NH2  1 
ATOM   3128 N  N    . ALA   B 1 173 ? -34.916 -40.396 -13.785 1.00 82.92  ? 173 ALA   B N    1 
ATOM   3129 C  CA   . ALA   B 1 173 ? -34.351 -40.381 -12.434 1.00 82.01  ? 173 ALA   B CA   1 
ATOM   3130 C  C    . ALA   B 1 173 ? -34.743 -39.107 -11.701 1.00 85.01  ? 173 ALA   B C    1 
ATOM   3131 O  O    . ALA   B 1 173 ? -34.585 -38.010 -12.241 1.00 90.03  ? 173 ALA   B O    1 
ATOM   3132 C  CB   . ALA   B 1 173 ? -32.831 -40.489 -12.470 1.00 84.56  ? 173 ALA   B CB   1 
ATOM   3133 N  N    . LEU   B 1 174 ? -35.204 -39.246 -10.456 1.00 82.38  ? 174 LEU   B N    1 
ATOM   3134 C  CA   . LEU   B 1 174 ? -35.857 -38.161 -9.726  1.00 82.36  ? 174 LEU   B CA   1 
ATOM   3135 C  C    . LEU   B 1 174 ? -35.331 -38.054 -8.300  1.00 84.44  ? 174 LEU   B C    1 
ATOM   3136 O  O    . LEU   B 1 174 ? -35.014 -39.056 -7.652  1.00 83.97  ? 174 LEU   B O    1 
ATOM   3137 C  CB   . LEU   B 1 174 ? -37.359 -38.380 -9.637  1.00 85.15  ? 174 LEU   B CB   1 
ATOM   3138 C  CG   . LEU   B 1 174 ? -38.240 -37.862 -10.749 1.00 81.27  ? 174 LEU   B CG   1 
ATOM   3139 C  CD1  . LEU   B 1 174 ? -38.121 -38.805 -11.898 1.00 85.50  ? 174 LEU   B CD1  1 
ATOM   3140 C  CD2  . LEU   B 1 174 ? -39.660 -37.820 -10.245 1.00 84.55  ? 174 LEU   B CD2  1 
ATOM   3141 N  N    . PHE   B 1 175 ? -35.290 -36.833 -7.789  1.00 82.84  ? 175 PHE   B N    1 
ATOM   3142 C  CA   . PHE   B 1 175 ? -34.942 -36.667 -6.392  1.00 82.92  ? 175 PHE   B CA   1 
ATOM   3143 C  C    . PHE   B 1 175 ? -36.073 -37.044 -5.449  1.00 85.65  ? 175 PHE   B C    1 
ATOM   3144 O  O    . PHE   B 1 175 ? -37.181 -36.515 -5.549  1.00 87.88  ? 175 PHE   B O    1 
ATOM   3145 C  CB   . PHE   B 1 175 ? -34.485 -35.249 -6.108  1.00 86.03  ? 175 PHE   B CB   1 
ATOM   3146 C  CG   . PHE   B 1 175 ? -33.733 -35.150 -4.822  1.00 88.22  ? 175 PHE   B CG   1 
ATOM   3147 C  CD1  . PHE   B 1 175 ? -32.825 -36.128 -4.476  1.00 89.61  ? 175 PHE   B CD1  1 
ATOM   3148 C  CD2  . PHE   B 1 175 ? -33.958 -34.110 -3.935  1.00 85.01  ? 175 PHE   B CD2  1 
ATOM   3149 C  CE1  . PHE   B 1 175 ? -32.145 -36.067 -3.267  1.00 86.32  ? 175 PHE   B CE1  1 
ATOM   3150 C  CE2  . PHE   B 1 175 ? -33.284 -34.048 -2.741  1.00 78.67  ? 175 PHE   B CE2  1 
ATOM   3151 C  CZ   . PHE   B 1 175 ? -32.376 -35.029 -2.408  1.00 78.24  ? 175 PHE   B CZ   1 
ATOM   3152 N  N    . TYR   B 1 176 ? -35.738 -37.904 -4.480  1.00 85.09  ? 176 TYR   B N    1 
ATOM   3153 C  CA   . TYR   B 1 176 ? -36.689 -38.403 -3.488  1.00 87.73  ? 176 TYR   B CA   1 
ATOM   3154 C  C    . TYR   B 1 176 ? -37.567 -37.310 -2.888  1.00 86.85  ? 176 TYR   B C    1 
ATOM   3155 O  O    . TYR   B 1 176 ? -38.781 -37.499 -2.726  1.00 87.61  ? 176 TYR   B O    1 
ATOM   3156 C  CB   . TYR   B 1 176 ? -35.927 -39.122 -2.382  1.00 87.83  ? 176 TYR   B CB   1 
ATOM   3157 C  CG   . TYR   B 1 176 ? -36.739 -40.196 -1.721  1.00 95.53  ? 176 TYR   B CG   1 
ATOM   3158 C  CD1  . TYR   B 1 176 ? -36.738 -41.491 -2.224  1.00 102.09 ? 176 TYR   B CD1  1 
ATOM   3159 C  CD2  . TYR   B 1 176 ? -37.495 -39.925 -0.580  1.00 97.12  ? 176 TYR   B CD2  1 
ATOM   3160 C  CE1  . TYR   B 1 176 ? -37.479 -42.493 -1.626  1.00 111.66 ? 176 TYR   B CE1  1 
ATOM   3161 C  CE2  . TYR   B 1 176 ? -38.237 -40.919 0.041   1.00 103.66 ? 176 TYR   B CE2  1 
ATOM   3162 C  CZ   . TYR   B 1 176 ? -38.227 -42.205 -0.491  1.00 115.00 ? 176 TYR   B CZ   1 
ATOM   3163 O  OH   . TYR   B 1 176 ? -38.961 -43.213 0.103   1.00 127.36 ? 176 TYR   B OH   1 
ATOM   3164 N  N    . ALA   B 1 177 ? -36.966 -36.166 -2.528  1.00 82.48  ? 177 ALA   B N    1 
ATOM   3165 C  CA   . ALA   B 1 177 ? -37.666 -35.116 -1.793  1.00 83.41  ? 177 ALA   B CA   1 
ATOM   3166 C  C    . ALA   B 1 177 ? -38.354 -34.137 -2.747  1.00 88.72  ? 177 ALA   B C    1 
ATOM   3167 O  O    . ALA   B 1 177 ? -37.791 -33.778 -3.795  1.00 85.92  ? 177 ALA   B O    1 
ATOM   3168 C  CB   . ALA   B 1 177 ? -36.710 -34.356 -0.882  1.00 75.06  ? 177 ALA   B CB   1 
ATOM   3169 N  N    . PRO   B 1 178 ? -39.581 -33.727 -2.413  1.00 88.06  ? 178 PRO   B N    1 
ATOM   3170 C  CA   . PRO   B 1 178 ? -40.248 -32.702 -3.209  1.00 85.91  ? 178 PRO   B CA   1 
ATOM   3171 C  C    . PRO   B 1 178 ? -39.638 -31.338 -2.941  1.00 90.74  ? 178 PRO   B C    1 
ATOM   3172 O  O    . PRO   B 1 178 ? -39.250 -30.998 -1.819  1.00 94.32  ? 178 PRO   B O    1 
ATOM   3173 C  CB   . PRO   B 1 178 ? -41.699 -32.769 -2.727  1.00 81.43  ? 178 PRO   B CB   1 
ATOM   3174 C  CG   . PRO   B 1 178 ? -41.581 -33.244 -1.351  1.00 79.58  ? 178 PRO   B CG   1 
ATOM   3175 C  CD   . PRO   B 1 178 ? -40.474 -34.245 -1.365  1.00 86.54  ? 178 PRO   B CD   1 
ATOM   3176 N  N    . VAL   B 1 179 ? -39.554 -30.553 -3.995  1.00 86.97  ? 179 VAL   B N    1 
ATOM   3177 C  CA   . VAL   B 1 179 ? -38.928 -29.249 -3.943  1.00 82.67  ? 179 VAL   B CA   1 
ATOM   3178 C  C    . VAL   B 1 179 ? -40.019 -28.209 -3.883  1.00 81.99  ? 179 VAL   B C    1 
ATOM   3179 O  O    . VAL   B 1 179 ? -40.877 -28.165 -4.761  1.00 90.26  ? 179 VAL   B O    1 
ATOM   3180 C  CB   . VAL   B 1 179 ? -38.033 -29.033 -5.161  1.00 81.14  ? 179 VAL   B CB   1 
ATOM   3181 C  CG1  . VAL   B 1 179 ? -37.368 -27.708 -5.070  1.00 80.61  ? 179 VAL   B CG1  1 
ATOM   3182 C  CG2  . VAL   B 1 179 ? -37.022 -30.152 -5.219  1.00 84.18  ? 179 VAL   B CG2  1 
ATOM   3183 N  N    . HIS   B 1 180 ? -39.996 -27.377 -2.856  1.00 85.85  ? 180 HIS   B N    1 
ATOM   3184 C  CA   . HIS   B 1 180 ? -40.869 -26.210 -2.812  1.00 86.75  ? 180 HIS   B CA   1 
ATOM   3185 C  C    . HIS   B 1 180 ? -40.359 -25.192 -3.821  1.00 88.06  ? 180 HIS   B C    1 
ATOM   3186 O  O    . HIS   B 1 180 ? -39.461 -24.410 -3.512  1.00 89.40  ? 180 HIS   B O    1 
ATOM   3187 C  CB   . HIS   B 1 180 ? -40.887 -25.623 -1.405  1.00 85.78  ? 180 HIS   B CB   1 
ATOM   3188 C  CG   . HIS   B 1 180 ? -42.017 -24.688 -1.150  1.00 84.76  ? 180 HIS   B CG   1 
ATOM   3189 N  ND1  . HIS   B 1 180 ? -42.347 -24.266 0.120   1.00 90.38  ? 180 HIS   B ND1  1 
ATOM   3190 C  CD2  . HIS   B 1 180 ? -42.920 -24.125 -1.983  1.00 90.02  ? 180 HIS   B CD2  1 
ATOM   3191 C  CE1  . HIS   B 1 180 ? -43.395 -23.467 0.054   1.00 99.61  ? 180 HIS   B CE1  1 
ATOM   3192 N  NE2  . HIS   B 1 180 ? -43.764 -23.365 -1.210  1.00 96.63  ? 180 HIS   B NE2  1 
ATOM   3193 N  N    . ILE   B 1 181 ? -40.888 -25.206 -5.039  1.00 88.48  ? 181 ILE   B N    1 
ATOM   3194 C  CA   . ILE   B 1 181 ? -40.230 -24.451 -6.093  1.00 89.36  ? 181 ILE   B CA   1 
ATOM   3195 C  C    . ILE   B 1 181 ? -40.615 -22.968 -6.081  1.00 97.26  ? 181 ILE   B C    1 
ATOM   3196 O  O    . ILE   B 1 181 ? -39.789 -22.119 -6.429  1.00 107.12 ? 181 ILE   B O    1 
ATOM   3197 C  CB   . ILE   B 1 181 ? -40.502 -25.111 -7.452  1.00 89.79  ? 181 ILE   B CB   1 
ATOM   3198 C  CG1  . ILE   B 1 181 ? -39.478 -24.641 -8.494  1.00 99.37  ? 181 ILE   B CG1  1 
ATOM   3199 C  CG2  . ILE   B 1 181 ? -41.914 -24.841 -7.916  1.00 89.85  ? 181 ILE   B CG2  1 
ATOM   3200 C  CD1  . ILE   B 1 181 ? -38.061 -25.168 -8.306  1.00 91.35  ? 181 ILE   B CD1  1 
ATOM   3201 N  N    . TRP   B 1 182 ? -41.836 -22.612 -5.682  1.00 96.04  ? 182 TRP   B N    1 
ATOM   3202 C  CA   . TRP   B 1 182 ? -42.229 -21.208 -5.595  1.00 95.69  ? 182 TRP   B CA   1 
ATOM   3203 C  C    . TRP   B 1 182 ? -43.250 -21.034 -4.481  1.00 101.32 ? 182 TRP   B C    1 
ATOM   3204 O  O    . TRP   B 1 182 ? -43.811 -22.004 -3.976  1.00 107.40 ? 182 TRP   B O    1 
ATOM   3205 C  CB   . TRP   B 1 182 ? -42.762 -20.686 -6.936  1.00 99.72  ? 182 TRP   B CB   1 
ATOM   3206 C  CG   . TRP   B 1 182 ? -44.083 -21.266 -7.377  1.00 109.38 ? 182 TRP   B CG   1 
ATOM   3207 C  CD1  . TRP   B 1 182 ? -44.258 -22.229 -8.326  1.00 111.04 ? 182 TRP   B CD1  1 
ATOM   3208 C  CD2  . TRP   B 1 182 ? -45.411 -20.907 -6.928  1.00 115.79 ? 182 TRP   B CD2  1 
ATOM   3209 N  NE1  . TRP   B 1 182 ? -45.597 -22.509 -8.484  1.00 113.67 ? 182 TRP   B NE1  1 
ATOM   3210 C  CE2  . TRP   B 1 182 ? -46.324 -21.714 -7.637  1.00 113.03 ? 182 TRP   B CE2  1 
ATOM   3211 C  CE3  . TRP   B 1 182 ? -45.912 -19.995 -5.996  1.00 120.31 ? 182 TRP   B CE3  1 
ATOM   3212 C  CZ2  . TRP   B 1 182 ? -47.698 -21.639 -7.438  1.00 110.20 ? 182 TRP   B CZ2  1 
ATOM   3213 C  CZ3  . TRP   B 1 182 ? -47.285 -19.932 -5.799  1.00 119.48 ? 182 TRP   B CZ3  1 
ATOM   3214 C  CH2  . TRP   B 1 182 ? -48.154 -20.746 -6.518  1.00 111.65 ? 182 TRP   B CH2  1 
ATOM   3215 N  N    . GLU   B 1 183 ? -43.474 -19.787 -4.079  1.00 105.03 ? 183 GLU   B N    1 
ATOM   3216 C  CA   . GLU   B 1 183 ? -44.351 -19.522 -2.951  1.00 110.94 ? 183 GLU   B CA   1 
ATOM   3217 C  C    . GLU   B 1 183 ? -45.094 -18.225 -3.200  1.00 120.28 ? 183 GLU   B C    1 
ATOM   3218 O  O    . GLU   B 1 183 ? -44.604 -17.335 -3.904  1.00 112.91 ? 183 GLU   B O    1 
ATOM   3219 C  CB   . GLU   B 1 183 ? -43.580 -19.417 -1.641  1.00 116.49 ? 183 GLU   B CB   1 
ATOM   3220 C  CG   . GLU   B 1 183 ? -44.441 -19.625 -0.415  1.00 131.21 ? 183 GLU   B CG   1 
ATOM   3221 C  CD   . GLU   B 1 183 ? -43.625 -19.576 0.871   1.00 139.85 ? 183 GLU   B CD   1 
ATOM   3222 O  OE1  . GLU   B 1 183 ? -42.377 -19.413 0.780   1.00 123.74 ? 183 GLU   B OE1  1 
ATOM   3223 O  OE2  . GLU   B 1 183 ? -44.231 -19.764 1.960   1.00 150.63 ? 183 GLU   B OE2  1 
ATOM   3224 N  N    . SER   B 1 184 ? -46.277 -18.120 -2.580  1.00 128.61 ? 184 SER   B N    1 
ATOM   3225 C  CA   . SER   B 1 184 ? -47.175 -16.998 -2.850  1.00 131.21 ? 184 SER   B CA   1 
ATOM   3226 C  C    . SER   B 1 184 ? -46.546 -15.658 -2.476  1.00 126.07 ? 184 SER   B C    1 
ATOM   3227 O  O    . SER   B 1 184 ? -46.884 -14.631 -3.075  1.00 126.77 ? 184 SER   B O    1 
ATOM   3228 C  CB   . SER   B 1 184 ? -48.502 -17.204 -2.110  1.00 130.84 ? 184 SER   B CB   1 
ATOM   3229 O  OG   . SER   B 1 184 ? -49.169 -18.362 -2.601  1.00 127.89 ? 184 SER   B OG   1 
ATOM   3230 N  N    . SER   B 1 185 ? -45.599 -15.651 -1.527  1.00 126.38 ? 185 SER   B N    1 
ATOM   3231 C  CA   . SER   B 1 185 ? -45.013 -14.416 -0.987  1.00 131.84 ? 185 SER   B CA   1 
ATOM   3232 C  C    . SER   B 1 185 ? -43.493 -14.558 -0.810  1.00 132.84 ? 185 SER   B C    1 
ATOM   3233 O  O    . SER   B 1 185 ? -42.998 -14.671 0.315   1.00 131.91 ? 185 SER   B O    1 
ATOM   3234 C  CB   . SER   B 1 185 ? -45.684 -14.076 0.313   1.00 130.74 ? 185 SER   B CB   1 
ATOM   3235 O  OG   . SER   B 1 185 ? -45.302 -15.043 1.266   1.00 126.45 ? 185 SER   B OG   1 
ATOM   3236 N  N    . ALA   B 1 186 ? -42.755 -14.507 -1.924  1.00 133.95 ? 186 ALA   B N    1 
ATOM   3237 C  CA   . ALA   B 1 186 ? -41.292 -14.534 -1.925  1.00 129.72 ? 186 ALA   B CA   1 
ATOM   3238 C  C    . ALA   B 1 186 ? -40.770 -13.536 -2.951  1.00 124.49 ? 186 ALA   B C    1 
ATOM   3239 O  O    . ALA   B 1 186 ? -41.176 -13.593 -4.115  1.00 129.06 ? 186 ALA   B O    1 
ATOM   3240 C  CB   . ALA   B 1 186 ? -40.770 -15.940 -2.244  1.00 114.33 ? 186 ALA   B CB   1 
ATOM   3241 N  N    . VAL   B 1 187 ? -39.869 -12.633 -2.538  1.00 123.83 ? 187 VAL   B N    1 
ATOM   3242 C  CA   . VAL   B 1 187 ? -39.439 -11.564 -3.446  1.00 118.71 ? 187 VAL   B CA   1 
ATOM   3243 C  C    . VAL   B 1 187 ? -38.512 -12.085 -4.546  1.00 115.83 ? 187 VAL   B C    1 
ATOM   3244 O  O    . VAL   B 1 187 ? -38.505 -11.553 -5.663  1.00 116.74 ? 187 VAL   B O    1 
ATOM   3245 C  CB   . VAL   B 1 187 ? -38.799 -10.387 -2.678  1.00 121.19 ? 187 VAL   B CB   1 
ATOM   3246 C  CG1  . VAL   B 1 187 ? -39.818 -9.750  -1.785  1.00 133.72 ? 187 VAL   B CG1  1 
ATOM   3247 C  CG2  . VAL   B 1 187 ? -37.595 -10.833 -1.856  1.00 124.22 ? 187 VAL   B CG2  1 
ATOM   3248 N  N    . VAL   B 1 188 ? -37.723 -13.113 -4.279  1.00 110.15 ? 188 VAL   B N    1 
ATOM   3249 C  CA   . VAL   B 1 188 ? -36.948 -13.751 -5.332  1.00 99.78  ? 188 VAL   B CA   1 
ATOM   3250 C  C    . VAL   B 1 188 ? -37.043 -15.255 -5.110  1.00 101.79 ? 188 VAL   B C    1 
ATOM   3251 O  O    . VAL   B 1 188 ? -36.990 -15.733 -3.974  1.00 107.05 ? 188 VAL   B O    1 
ATOM   3252 C  CB   . VAL   B 1 188 ? -35.490 -13.220 -5.381  1.00 95.36  ? 188 VAL   B CB   1 
ATOM   3253 C  CG1  . VAL   B 1 188 ? -34.729 -13.567 -4.144  1.00 104.62 ? 188 VAL   B CG1  1 
ATOM   3254 C  CG2  . VAL   B 1 188 ? -34.740 -13.746 -6.609  1.00 99.04  ? 188 VAL   B CG2  1 
ATOM   3255 N  N    . ALA   B 1 189 ? -37.290 -15.992 -6.181  1.00 89.98  ? 189 ALA   B N    1 
ATOM   3256 C  CA   . ALA   B 1 189 ? -37.251 -17.445 -6.180  1.00 86.34  ? 189 ALA   B CA   1 
ATOM   3257 C  C    . ALA   B 1 189 ? -36.351 -17.852 -7.329  1.00 86.76  ? 189 ALA   B C    1 
ATOM   3258 O  O    . ALA   B 1 189 ? -36.374 -17.222 -8.383  1.00 87.97  ? 189 ALA   B O    1 
ATOM   3259 C  CB   . ALA   B 1 189 ? -38.643 -18.063 -6.352  1.00 84.38  ? 189 ALA   B CB   1 
ATOM   3260 N  N    . SER   B 1 190 ? -35.553 -18.890 -7.144  1.00 88.27  ? 190 SER   B N    1 
ATOM   3261 C  CA   . SER   B 1 190 ? -34.489 -19.145 -8.108  1.00 87.33  ? 190 SER   B CA   1 
ATOM   3262 C  C    . SER   B 1 190 ? -34.166 -20.627 -8.032  1.00 80.00  ? 190 SER   B C    1 
ATOM   3263 O  O    . SER   B 1 190 ? -34.634 -21.306 -7.116  1.00 78.96  ? 190 SER   B O    1 
ATOM   3264 C  CB   . SER   B 1 190 ? -33.292 -18.233 -7.814  1.00 94.47  ? 190 SER   B CB   1 
ATOM   3265 O  OG   . SER   B 1 190 ? -32.472 -18.775 -6.796  1.00 94.59  ? 190 SER   B OG   1 
ATOM   3266 N  N    . PHE   B 1 191 ? -33.399 -21.147 -9.004  1.00 80.81  ? 191 PHE   B N    1 
ATOM   3267 C  CA   . PHE   B 1 191 ? -33.090 -22.573 -8.904  1.00 82.24  ? 191 PHE   B CA   1 
ATOM   3268 C  C    . PHE   B 1 191 ? -32.066 -22.846 -10.005 1.00 78.56  ? 191 PHE   B C    1 
ATOM   3269 O  O    . PHE   B 1 191 ? -32.204 -22.313 -11.108 1.00 82.69  ? 191 PHE   B O    1 
ATOM   3270 C  CB   . PHE   B 1 191 ? -34.411 -23.381 -9.073  1.00 84.19  ? 191 PHE   B CB   1 
ATOM   3271 C  CG   . PHE   B 1 191 ? -34.798 -23.639 -10.479 1.00 81.44  ? 191 PHE   B CG   1 
ATOM   3272 C  CD1  . PHE   B 1 191 ? -35.272 -22.654 -11.276 1.00 88.36  ? 191 PHE   B CD1  1 
ATOM   3273 C  CD2  . PHE   B 1 191 ? -35.030 -24.935 -10.869 1.00 88.37  ? 191 PHE   B CD2  1 
ATOM   3274 C  CE1  . PHE   B 1 191 ? -35.665 -22.900 -12.560 1.00 88.98  ? 191 PHE   B CE1  1 
ATOM   3275 C  CE2  . PHE   B 1 191 ? -35.483 -25.212 -12.141 1.00 91.79  ? 191 PHE   B CE2  1 
ATOM   3276 C  CZ   . PHE   B 1 191 ? -35.811 -24.187 -12.999 1.00 89.53  ? 191 PHE   B CZ   1 
ATOM   3277 N  N    . GLU   B 1 192 ? -30.977 -23.540 -9.689  1.00 77.93  ? 192 GLU   B N    1 
ATOM   3278 C  CA   . GLU   B 1 192 ? -29.960 -23.821 -10.699 1.00 82.19  ? 192 GLU   B CA   1 
ATOM   3279 C  C    . GLU   B 1 192 ? -29.699 -25.318 -10.706 1.00 82.95  ? 192 GLU   B C    1 
ATOM   3280 O  O    . GLU   B 1 192 ? -29.702 -25.963 -9.660  1.00 85.06  ? 192 GLU   B O    1 
ATOM   3281 C  CB   . GLU   B 1 192 ? -28.607 -23.058 -10.490 1.00 86.41  ? 192 GLU   B CB   1 
ATOM   3282 C  CG   . GLU   B 1 192 ? -27.683 -23.480 -9.287  1.00 108.32 ? 192 GLU   B CG   1 
ATOM   3283 C  CD   . GLU   B 1 192 ? -26.375 -22.645 -9.158  1.00 120.31 ? 192 GLU   B CD   1 
ATOM   3284 O  OE1  . GLU   B 1 192 ? -26.217 -21.685 -9.946  1.00 119.82 ? 192 GLU   B OE1  1 
ATOM   3285 O  OE2  . GLU   B 1 192 ? -25.504 -22.976 -8.297  1.00 124.01 ? 192 GLU   B OE2  1 
ATOM   3286 N  N    . ALA   B 1 193 ? -29.477 -25.876 -11.887 1.00 75.87  ? 193 ALA   B N    1 
ATOM   3287 C  CA   . ALA   B 1 193 ? -29.211 -27.300 -11.977 1.00 74.25  ? 193 ALA   B CA   1 
ATOM   3288 C  C    . ALA   B 1 193 ? -28.085 -27.501 -12.967 1.00 73.59  ? 193 ALA   B C    1 
ATOM   3289 O  O    . ALA   B 1 193 ? -28.052 -26.866 -14.015 1.00 76.84  ? 193 ALA   B O    1 
ATOM   3290 C  CB   . ALA   B 1 193 ? -30.453 -28.078 -12.390 1.00 78.11  ? 193 ALA   B CB   1 
ATOM   3291 N  N    . THR   B 1 194 ? -27.140 -28.334 -12.599 1.00 71.97  ? 194 THR   B N    1 
ATOM   3292 C  CA   . THR   B 1 194 ? -25.946 -28.528 -13.382 1.00 71.98  ? 194 THR   B CA   1 
ATOM   3293 C  C    . THR   B 1 194 ? -25.823 -30.032 -13.465 1.00 74.41  ? 194 THR   B C    1 
ATOM   3294 O  O    . THR   B 1 194 ? -26.196 -30.712 -12.510 1.00 75.26  ? 194 THR   B O    1 
ATOM   3295 C  CB   . THR   B 1 194 ? -24.733 -27.908 -12.684 1.00 81.53  ? 194 THR   B CB   1 
ATOM   3296 O  OG1  . THR   B 1 194 ? -24.929 -26.494 -12.509 1.00 85.51  ? 194 THR   B OG1  1 
ATOM   3297 C  CG2  . THR   B 1 194 ? -23.491 -28.137 -13.511 1.00 83.02  ? 194 THR   B CG2  1 
ATOM   3298 N  N    . PHE   B 1 195 ? -25.362 -30.560 -14.597 1.00 74.85  ? 195 PHE   B N    1 
ATOM   3299 C  CA   . PHE   B 1 195 ? -25.191 -32.005 -14.714 1.00 71.56  ? 195 PHE   B CA   1 
ATOM   3300 C  C    . PHE   B 1 195 ? -24.308 -32.278 -15.910 1.00 75.79  ? 195 PHE   B C    1 
ATOM   3301 O  O    . PHE   B 1 195 ? -24.402 -31.580 -16.920 1.00 80.58  ? 195 PHE   B O    1 
ATOM   3302 C  CB   . PHE   B 1 195 ? -26.540 -32.737 -14.842 1.00 72.81  ? 195 PHE   B CB   1 
ATOM   3303 C  CG   . PHE   B 1 195 ? -27.243 -32.512 -16.156 1.00 80.06  ? 195 PHE   B CG   1 
ATOM   3304 C  CD1  . PHE   B 1 195 ? -26.903 -33.246 -17.286 1.00 82.22  ? 195 PHE   B CD1  1 
ATOM   3305 C  CD2  . PHE   B 1 195 ? -28.321 -31.634 -16.234 1.00 77.88  ? 195 PHE   B CD2  1 
ATOM   3306 C  CE1  . PHE   B 1 195 ? -27.569 -33.044 -18.479 1.00 80.15  ? 195 PHE   B CE1  1 
ATOM   3307 C  CE2  . PHE   B 1 195 ? -28.983 -31.416 -17.428 1.00 72.45  ? 195 PHE   B CE2  1 
ATOM   3308 C  CZ   . PHE   B 1 195 ? -28.612 -32.124 -18.550 1.00 75.36  ? 195 PHE   B CZ   1 
ATOM   3309 N  N    . THR   B 1 196 ? -23.439 -33.275 -15.786 1.00 79.27  ? 196 THR   B N    1 
ATOM   3310 C  CA   . THR   B 1 196 ? -22.518 -33.634 -16.855 1.00 83.40  ? 196 THR   B CA   1 
ATOM   3311 C  C    . THR   B 1 196 ? -22.816 -35.045 -17.311 1.00 86.49  ? 196 THR   B C    1 
ATOM   3312 O  O    . THR   B 1 196 ? -23.124 -35.925 -16.503 1.00 87.61  ? 196 THR   B O    1 
ATOM   3313 C  CB   . THR   B 1 196 ? -21.056 -33.567 -16.450 1.00 81.77  ? 196 THR   B CB   1 
ATOM   3314 O  OG1  . THR   B 1 196 ? -20.766 -34.623 -15.535 1.00 84.01  ? 196 THR   B OG1  1 
ATOM   3315 C  CG2  . THR   B 1 196 ? -20.765 -32.248 -15.784 1.00 98.97  ? 196 THR   B CG2  1 
ATOM   3316 N  N    . PHE   B 1 197 ? -22.688 -35.250 -18.608 1.00 90.59  ? 197 PHE   B N    1 
ATOM   3317 C  CA   . PHE   B 1 197 ? -23.230 -36.415 -19.273 1.00 89.90  ? 197 PHE   B CA   1 
ATOM   3318 C  C    . PHE   B 1 197 ? -22.217 -36.882 -20.292 1.00 89.18  ? 197 PHE   B C    1 
ATOM   3319 O  O    . PHE   B 1 197 ? -21.308 -36.143 -20.673 1.00 91.80  ? 197 PHE   B O    1 
ATOM   3320 C  CB   . PHE   B 1 197 ? -24.567 -36.093 -19.948 1.00 83.11  ? 197 PHE   B CB   1 
ATOM   3321 C  CG   . PHE   B 1 197 ? -24.483 -34.949 -20.899 1.00 84.91  ? 197 PHE   B CG   1 
ATOM   3322 C  CD1  . PHE   B 1 197 ? -24.022 -35.129 -22.176 1.00 90.38  ? 197 PHE   B CD1  1 
ATOM   3323 C  CD2  . PHE   B 1 197 ? -24.855 -33.677 -20.510 1.00 88.75  ? 197 PHE   B CD2  1 
ATOM   3324 C  CE1  . PHE   B 1 197 ? -23.926 -34.062 -23.059 1.00 92.64  ? 197 PHE   B CE1  1 
ATOM   3325 C  CE2  . PHE   B 1 197 ? -24.762 -32.601 -21.396 1.00 89.68  ? 197 PHE   B CE2  1 
ATOM   3326 C  CZ   . PHE   B 1 197 ? -24.305 -32.801 -22.668 1.00 87.13  ? 197 PHE   B CZ   1 
ATOM   3327 N  N    . LEU   B 1 198 ? -22.377 -38.123 -20.733 1.00 98.17  ? 198 LEU   B N    1 
ATOM   3328 C  CA   . LEU   B 1 198 ? -21.559 -38.656 -21.812 1.00 98.38  ? 198 LEU   B CA   1 
ATOM   3329 C  C    . LEU   B 1 198 ? -22.466 -39.352 -22.804 1.00 101.04 ? 198 LEU   B C    1 
ATOM   3330 O  O    . LEU   B 1 198 ? -23.094 -40.363 -22.474 1.00 97.28  ? 198 LEU   B O    1 
ATOM   3331 C  CB   . LEU   B 1 198 ? -20.480 -39.609 -21.307 1.00 91.96  ? 198 LEU   B CB   1 
ATOM   3332 C  CG   . LEU   B 1 198 ? -19.522 -40.012 -22.423 1.00 92.12  ? 198 LEU   B CG   1 
ATOM   3333 C  CD1  . LEU   B 1 198 ? -18.181 -40.327 -21.837 1.00 96.16  ? 198 LEU   B CD1  1 
ATOM   3334 C  CD2  . LEU   B 1 198 ? -20.020 -41.230 -23.168 1.00 106.41 ? 198 LEU   B CD2  1 
ATOM   3335 N  N    . ILE   B 1 199 ? -22.497 -38.820 -24.022 1.00 110.42 ? 199 ILE   B N    1 
ATOM   3336 C  CA   . ILE   B 1 199 ? -23.264 -39.372 -25.123 1.00 111.67 ? 199 ILE   B CA   1 
ATOM   3337 C  C    . ILE   B 1 199 ? -22.278 -39.897 -26.150 1.00 117.43 ? 199 ILE   B C    1 
ATOM   3338 O  O    . ILE   B 1 199 ? -21.513 -39.119 -26.743 1.00 110.95 ? 199 ILE   B O    1 
ATOM   3339 C  CB   . ILE   B 1 199 ? -24.198 -38.334 -25.743 1.00 106.27 ? 199 ILE   B CB   1 
ATOM   3340 C  CG1  . ILE   B 1 199 ? -25.352 -38.084 -24.794 1.00 99.60  ? 199 ILE   B CG1  1 
ATOM   3341 C  CG2  . ILE   B 1 199 ? -24.756 -38.867 -27.021 1.00 114.07 ? 199 ILE   B CG2  1 
ATOM   3342 C  CD1  . ILE   B 1 199 ? -26.369 -37.186 -25.349 1.00 99.39  ? 199 ILE   B CD1  1 
ATOM   3343 N  N    . LYS   B 1 200 ? -22.283 -41.221 -26.328 1.00 121.29 ? 200 LYS   B N    1 
ATOM   3344 C  CA   . LYS   B 1 200 ? -21.488 -41.939 -27.316 1.00 124.90 ? 200 LYS   B CA   1 
ATOM   3345 C  C    . LYS   B 1 200 ? -22.446 -42.873 -28.045 1.00 127.25 ? 200 LYS   B C    1 
ATOM   3346 O  O    . LYS   B 1 200 ? -23.307 -43.496 -27.410 1.00 121.30 ? 200 LYS   B O    1 
ATOM   3347 C  CB   . LYS   B 1 200 ? -20.330 -42.719 -26.648 1.00 123.19 ? 200 LYS   B CB   1 
ATOM   3348 C  CG   . LYS   B 1 200 ? -19.427 -43.547 -27.577 1.00 127.69 ? 200 LYS   B CG   1 
ATOM   3349 C  CD   . LYS   B 1 200 ? -18.108 -43.905 -26.878 1.00 134.36 ? 200 LYS   B CD   1 
ATOM   3350 C  CE   . LYS   B 1 200 ? -16.978 -44.186 -27.868 1.00 134.97 ? 200 LYS   B CE   1 
ATOM   3351 N  NZ   . LYS   B 1 200 ? -15.708 -43.491 -27.494 1.00 133.75 ? 200 LYS   B NZ   1 
ATOM   3352 N  N    . SER   B 1 201 ? -22.333 -42.939 -29.375 1.00 131.52 ? 201 SER   B N    1 
ATOM   3353 C  CA   . SER   B 1 201 ? -23.205 -43.821 -30.136 1.00 135.78 ? 201 SER   B CA   1 
ATOM   3354 C  C    . SER   B 1 201 ? -22.390 -44.607 -31.154 1.00 139.91 ? 201 SER   B C    1 
ATOM   3355 O  O    . SER   B 1 201 ? -21.496 -44.044 -31.800 1.00 139.36 ? 201 SER   B O    1 
ATOM   3356 C  CB   . SER   B 1 201 ? -24.314 -43.026 -30.848 1.00 133.51 ? 201 SER   B CB   1 
ATOM   3357 O  OG   . SER   B 1 201 ? -24.885 -43.766 -31.913 1.00 140.48 ? 201 SER   B OG   1 
ATOM   3358 N  N    . PRO   B 1 202 ? -22.642 -45.914 -31.295 1.00 138.68 ? 202 PRO   B N    1 
ATOM   3359 C  CA   . PRO   B 1 202 ? -21.940 -46.665 -32.345 1.00 140.66 ? 202 PRO   B CA   1 
ATOM   3360 C  C    . PRO   B 1 202 ? -22.370 -46.224 -33.730 1.00 144.58 ? 202 PRO   B C    1 
ATOM   3361 O  O    . PRO   B 1 202 ? -21.536 -46.119 -34.642 1.00 138.51 ? 202 PRO   B O    1 
ATOM   3362 C  CB   . PRO   B 1 202 ? -22.332 -48.121 -32.053 1.00 138.86 ? 202 PRO   B CB   1 
ATOM   3363 C  CG   . PRO   B 1 202 ? -23.581 -48.034 -31.263 1.00 133.39 ? 202 PRO   B CG   1 
ATOM   3364 C  CD   . PRO   B 1 202 ? -23.510 -46.776 -30.480 1.00 131.06 ? 202 PRO   B CD   1 
ATOM   3365 N  N    . ASP   B 1 203 ? -23.663 -45.937 -33.887 1.00 147.41 ? 203 ASP   B N    1 
ATOM   3366 C  CA   . ASP   B 1 203 ? -24.233 -45.476 -35.147 1.00 151.29 ? 203 ASP   B CA   1 
ATOM   3367 C  C    . ASP   B 1 203 ? -23.862 -44.018 -35.411 1.00 147.58 ? 203 ASP   B C    1 
ATOM   3368 O  O    . ASP   B 1 203 ? -23.711 -43.213 -34.490 1.00 143.76 ? 203 ASP   B O    1 
ATOM   3369 C  CB   . ASP   B 1 203 ? -25.759 -45.613 -35.109 1.00 152.08 ? 203 ASP   B CB   1 
ATOM   3370 C  CG   . ASP   B 1 203 ? -26.250 -46.937 -35.681 1.00 161.30 ? 203 ASP   B CG   1 
ATOM   3371 O  OD1  . ASP   B 1 203 ? -25.544 -47.539 -36.527 1.00 163.92 ? 203 ASP   B OD1  1 
ATOM   3372 O  OD2  . ASP   B 1 203 ? -27.345 -47.381 -35.263 1.00 160.42 ? 203 ASP   B OD2  1 
ATOM   3373 N  N    . SER   B 1 204 ? -23.733 -43.670 -36.692 1.00 149.65 ? 204 SER   B N    1 
ATOM   3374 C  CA   . SER   B 1 204 ? -23.427 -42.286 -37.029 1.00 148.77 ? 204 SER   B CA   1 
ATOM   3375 C  C    . SER   B 1 204 ? -24.526 -41.352 -36.539 1.00 151.67 ? 204 SER   B C    1 
ATOM   3376 O  O    . SER   B 1 204 ? -24.242 -40.239 -36.084 1.00 157.12 ? 204 SER   B O    1 
ATOM   3377 C  CB   . SER   B 1 204 ? -23.224 -42.129 -38.536 1.00 154.18 ? 204 SER   B CB   1 
ATOM   3378 O  OG   . SER   B 1 204 ? -24.457 -42.165 -39.232 1.00 155.38 ? 204 SER   B OG   1 
ATOM   3379 N  N    . HIS   B 1 205 ? -25.787 -41.788 -36.612 1.00 151.18 ? 205 HIS   B N    1 
ATOM   3380 C  CA   . HIS   B 1 205 ? -26.894 -40.974 -36.118 1.00 152.83 ? 205 HIS   B CA   1 
ATOM   3381 C  C    . HIS   B 1 205 ? -27.373 -41.486 -34.770 1.00 148.59 ? 205 HIS   B C    1 
ATOM   3382 O  O    . HIS   B 1 205 ? -27.776 -42.659 -34.664 1.00 146.10 ? 205 HIS   B O    1 
ATOM   3383 C  CB   . HIS   B 1 205 ? -28.049 -40.958 -37.108 1.00 154.16 ? 205 HIS   B CB   1 
ATOM   3384 C  CG   . HIS   B 1 205 ? -27.653 -40.551 -38.488 1.00 161.25 ? 205 HIS   B CG   1 
ATOM   3385 N  ND1  . HIS   B 1 205 ? -27.527 -41.452 -39.523 1.00 164.12 ? 205 HIS   B ND1  1 
ATOM   3386 C  CD2  . HIS   B 1 205 ? -27.364 -39.335 -39.009 1.00 164.93 ? 205 HIS   B CD2  1 
ATOM   3387 C  CE1  . HIS   B 1 205 ? -27.172 -40.810 -40.622 1.00 167.20 ? 205 HIS   B CE1  1 
ATOM   3388 N  NE2  . HIS   B 1 205 ? -27.067 -39.525 -40.337 1.00 172.04 ? 205 HIS   B NE2  1 
ATOM   3389 N  N    . PRO   B 1 206 ? -27.346 -40.652 -33.725 1.00 140.35 ? 206 PRO   B N    1 
ATOM   3390 C  CA   . PRO   B 1 206 ? -27.857 -41.077 -32.421 1.00 127.44 ? 206 PRO   B CA   1 
ATOM   3391 C  C    . PRO   B 1 206 ? -29.189 -40.432 -32.088 1.00 122.27 ? 206 PRO   B C    1 
ATOM   3392 O  O    . PRO   B 1 206 ? -29.636 -39.527 -32.800 1.00 121.81 ? 206 PRO   B O    1 
ATOM   3393 C  CB   . PRO   B 1 206 ? -26.737 -40.631 -31.481 1.00 127.53 ? 206 PRO   B CB   1 
ATOM   3394 C  CG   . PRO   B 1 206 ? -26.041 -39.428 -32.242 1.00 126.23 ? 206 PRO   B CG   1 
ATOM   3395 C  CD   . PRO   B 1 206 ? -26.680 -39.342 -33.611 1.00 132.44 ? 206 PRO   B CD   1 
ATOM   3396 N  N    . ALA   B 1 207 ? -29.835 -40.890 -31.017 1.00 121.21 ? 207 ALA   B N    1 
ATOM   3397 C  CA   . ALA   B 1 207 ? -31.205 -40.485 -30.720 1.00 123.32 ? 207 ALA   B CA   1 
ATOM   3398 C  C    . ALA   B 1 207 ? -31.595 -41.004 -29.345 1.00 121.90 ? 207 ALA   B C    1 
ATOM   3399 O  O    . ALA   B 1 207 ? -31.125 -42.068 -28.932 1.00 120.89 ? 207 ALA   B O    1 
ATOM   3400 C  CB   . ALA   B 1 207 ? -32.179 -41.021 -31.777 1.00 125.56 ? 207 ALA   B CB   1 
ATOM   3401 N  N    . ASP   B 1 208 ? -32.452 -40.257 -28.628 1.00 124.34 ? 208 ASP   B N    1 
ATOM   3402 C  CA   . ASP   B 1 208 ? -32.975 -38.912 -28.979 1.00 124.06 ? 208 ASP   B CA   1 
ATOM   3403 C  C    . ASP   B 1 208 ? -32.390 -37.756 -28.161 1.00 118.55 ? 208 ASP   B C    1 
ATOM   3404 O  O    . ASP   B 1 208 ? -32.160 -36.681 -28.707 1.00 112.69 ? 208 ASP   B O    1 
ATOM   3405 C  CB   . ASP   B 1 208 ? -34.494 -38.893 -28.823 1.00 124.44 ? 208 ASP   B CB   1 
ATOM   3406 C  CG   . ASP   B 1 208 ? -35.196 -39.648 -29.917 1.00 132.20 ? 208 ASP   B CG   1 
ATOM   3407 O  OD1  . ASP   B 1 208 ? -34.735 -39.595 -31.068 1.00 139.36 ? 208 ASP   B OD1  1 
ATOM   3408 O  OD2  . ASP   B 1 208 ? -36.121 -40.408 -29.608 1.00 130.17 ? 208 ASP   B OD2  1 
ATOM   3409 N  N    . GLY   B 1 209 ? -32.190 -37.958 -26.860 1.00 116.83 ? 209 GLY   B N    1 
ATOM   3410 C  CA   . GLY   B 1 209 ? -31.458 -36.978 -26.072 1.00 111.27 ? 209 GLY   B CA   1 
ATOM   3411 C  C    . GLY   B 1 209 ? -31.689 -37.136 -24.572 1.00 104.93 ? 209 GLY   B C    1 
ATOM   3412 O  O    . GLY   B 1 209 ? -32.229 -38.138 -24.109 1.00 101.79 ? 209 GLY   B O    1 
ATOM   3413 N  N    . ILE   B 1 210 ? -31.229 -36.121 -23.836 1.00 101.75 ? 210 ILE   B N    1 
ATOM   3414 C  CA   . ILE   B 1 210 ? -31.389 -36.022 -22.393 1.00 95.34  ? 210 ILE   B CA   1 
ATOM   3415 C  C    . ILE   B 1 210 ? -32.149 -34.746 -22.102 1.00 92.00  ? 210 ILE   B C    1 
ATOM   3416 O  O    . ILE   B 1 210 ? -32.031 -33.756 -22.829 1.00 91.66  ? 210 ILE   B O    1 
ATOM   3417 C  CB   . ILE   B 1 210 ? -30.042 -36.008 -21.635 1.00 90.62  ? 210 ILE   B CB   1 
ATOM   3418 C  CG1  . ILE   B 1 210 ? -29.093 -37.051 -22.195 1.00 90.79  ? 210 ILE   B CG1  1 
ATOM   3419 C  CG2  . ILE   B 1 210 ? -30.239 -36.218 -20.156 1.00 86.81  ? 210 ILE   B CG2  1 
ATOM   3420 C  CD1  . ILE   B 1 210 ? -27.683 -36.757 -21.864 1.00 93.17  ? 210 ILE   B CD1  1 
ATOM   3421 N  N    . ALA   B 1 211 ? -32.921 -34.770 -21.021 1.00 92.63  ? 211 ALA   B N    1 
ATOM   3422 C  CA   . ALA   B 1 211 ? -33.645 -33.587 -20.583 1.00 91.70  ? 211 ALA   B CA   1 
ATOM   3423 C  C    . ALA   B 1 211 ? -33.674 -33.534 -19.065 1.00 90.28  ? 211 ALA   B C    1 
ATOM   3424 O  O    . ALA   B 1 211 ? -33.926 -34.548 -18.403 1.00 90.40  ? 211 ALA   B O    1 
ATOM   3425 C  CB   . ALA   B 1 211 ? -35.072 -33.568 -21.138 1.00 87.69  ? 211 ALA   B CB   1 
ATOM   3426 N  N    . PHE   B 1 212 ? -33.400 -32.354 -18.520 1.00 83.90  ? 212 PHE   B N    1 
ATOM   3427 C  CA   . PHE   B 1 212 ? -33.636 -32.121 -17.110 1.00 81.22  ? 212 PHE   B CA   1 
ATOM   3428 C  C    . PHE   B 1 212 ? -35.030 -31.551 -17.034 1.00 80.99  ? 212 PHE   B C    1 
ATOM   3429 O  O    . PHE   B 1 212 ? -35.420 -30.767 -17.902 1.00 82.48  ? 212 PHE   B O    1 
ATOM   3430 C  CB   . PHE   B 1 212 ? -32.607 -31.162 -16.516 1.00 82.58  ? 212 PHE   B CB   1 
ATOM   3431 C  CG   . PHE   B 1 212 ? -33.033 -30.543 -15.217 1.00 84.14  ? 212 PHE   B CG   1 
ATOM   3432 C  CD1  . PHE   B 1 212 ? -32.798 -31.214 -14.013 1.00 81.26  ? 212 PHE   B CD1  1 
ATOM   3433 C  CD2  . PHE   B 1 212 ? -33.619 -29.277 -15.178 1.00 79.13  ? 212 PHE   B CD2  1 
ATOM   3434 C  CE1  . PHE   B 1 212 ? -33.186 -30.654 -12.782 1.00 78.87  ? 212 PHE   B CE1  1 
ATOM   3435 C  CE2  . PHE   B 1 212 ? -34.005 -28.708 -13.955 1.00 74.47  ? 212 PHE   B CE2  1 
ATOM   3436 C  CZ   . PHE   B 1 212 ? -33.785 -29.401 -12.755 1.00 73.43  ? 212 PHE   B CZ   1 
ATOM   3437 N  N    . PHE   B 1 213 ? -35.802 -31.995 -16.046 1.00 77.61  ? 213 PHE   B N    1 
ATOM   3438 C  CA   . PHE   B 1 213 ? -37.221 -31.674 -16.040 1.00 83.35  ? 213 PHE   B CA   1 
ATOM   3439 C  C    . PHE   B 1 213 ? -37.729 -31.472 -14.622 1.00 87.38  ? 213 PHE   B C    1 
ATOM   3440 O  O    . PHE   B 1 213 ? -37.137 -31.923 -13.629 1.00 83.69  ? 213 PHE   B O    1 
ATOM   3441 C  CB   . PHE   B 1 213 ? -38.080 -32.770 -16.682 1.00 88.24  ? 213 PHE   B CB   1 
ATOM   3442 C  CG   . PHE   B 1 213 ? -38.186 -34.012 -15.839 1.00 91.18  ? 213 PHE   B CG   1 
ATOM   3443 C  CD1  . PHE   B 1 213 ? -37.141 -34.932 -15.802 1.00 87.46  ? 213 PHE   B CD1  1 
ATOM   3444 C  CD2  . PHE   B 1 213 ? -39.333 -34.259 -15.081 1.00 90.64  ? 213 PHE   B CD2  1 
ATOM   3445 C  CE1  . PHE   B 1 213 ? -37.222 -36.048 -15.018 1.00 81.42  ? 213 PHE   B CE1  1 
ATOM   3446 C  CE2  . PHE   B 1 213 ? -39.425 -35.386 -14.300 1.00 88.72  ? 213 PHE   B CE2  1 
ATOM   3447 C  CZ   . PHE   B 1 213 ? -38.368 -36.273 -14.265 1.00 85.58  ? 213 PHE   B CZ   1 
ATOM   3448 N  N    . ILE   B 1 214 ? -38.888 -30.832 -14.573 1.00 89.28  ? 214 ILE   B N    1 
ATOM   3449 C  CA   . ILE   B 1 214 ? -39.563 -30.470 -13.345 1.00 88.29  ? 214 ILE   B CA   1 
ATOM   3450 C  C    . ILE   B 1 214 ? -41.012 -30.804 -13.540 1.00 92.41  ? 214 ILE   B C    1 
ATOM   3451 O  O    . ILE   B 1 214 ? -41.584 -30.509 -14.593 1.00 98.13  ? 214 ILE   B O    1 
ATOM   3452 C  CB   . ILE   B 1 214 ? -39.444 -28.979 -13.050 1.00 89.69  ? 214 ILE   B CB   1 
ATOM   3453 C  CG1  . ILE   B 1 214 ? -37.995 -28.617 -12.878 1.00 83.59  ? 214 ILE   B CG1  1 
ATOM   3454 C  CG2  . ILE   B 1 214 ? -40.237 -28.646 -11.798 1.00 92.71  ? 214 ILE   B CG2  1 
ATOM   3455 C  CD1  . ILE   B 1 214 ? -37.899 -27.340 -12.331 1.00 81.35  ? 214 ILE   B CD1  1 
ATOM   3456 N  N    . SER   B 1 215 ? -41.614 -31.389 -12.527 1.00 92.98  ? 215 SER   B N    1 
ATOM   3457 C  CA   . SER   B 1 215 ? -42.995 -31.797 -12.670 1.00 100.91 ? 215 SER   B CA   1 
ATOM   3458 C  C    . SER   B 1 215 ? -43.611 -31.818 -11.301 1.00 99.83  ? 215 SER   B C    1 
ATOM   3459 O  O    . SER   B 1 215 ? -42.913 -31.766 -10.287 1.00 103.48 ? 215 SER   B O    1 
ATOM   3460 C  CB   . SER   B 1 215 ? -43.117 -33.170 -13.322 1.00 105.09 ? 215 SER   B CB   1 
ATOM   3461 O  OG   . SER   B 1 215 ? -42.906 -34.213 -12.394 1.00 105.54 ? 215 SER   B OG   1 
ATOM   3462 N  N    . ASN   B 1 216 ? -44.932 -31.918 -11.294 1.00 102.78 ? 216 ASN   B N    1 
ATOM   3463 C  CA   . ASN   B 1 216 ? -45.661 -32.209 -10.077 1.00 109.28 ? 216 ASN   B CA   1 
ATOM   3464 C  C    . ASN   B 1 216 ? -45.134 -33.484 -9.399  1.00 104.49 ? 216 ASN   B C    1 
ATOM   3465 O  O    . ASN   B 1 216 ? -44.405 -34.302 -9.975  1.00 102.11 ? 216 ASN   B O    1 
ATOM   3466 C  CB   . ASN   B 1 216 ? -47.157 -32.266 -10.384 1.00 116.24 ? 216 ASN   B CB   1 
ATOM   3467 C  CG   . ASN   B 1 216 ? -47.490 -33.275 -11.457 1.00 120.20 ? 216 ASN   B CG   1 
ATOM   3468 O  OD1  . ASN   B 1 216 ? -46.622 -33.995 -11.948 1.00 123.23 ? 216 ASN   B OD1  1 
ATOM   3469 N  ND2  . ASN   B 1 216 ? -48.750 -33.294 -11.866 1.00 124.34 ? 216 ASN   B ND2  1 
ATOM   3470 N  N    . ILE   B 1 217 ? -45.533 -33.618 -8.137  1.00 103.95 ? 217 ILE   B N    1 
ATOM   3471 C  CA   . ILE   B 1 217 ? -44.872 -34.468 -7.155  1.00 104.69 ? 217 ILE   B CA   1 
ATOM   3472 C  C    . ILE   B 1 217 ? -44.977 -35.931 -7.577  1.00 113.73 ? 217 ILE   B C    1 
ATOM   3473 O  O    . ILE   B 1 217 ? -44.010 -36.700 -7.508  1.00 113.16 ? 217 ILE   B O    1 
ATOM   3474 C  CB   . ILE   B 1 217 ? -45.548 -34.231 -5.786  1.00 107.66 ? 217 ILE   B CB   1 
ATOM   3475 C  CG1  . ILE   B 1 217 ? -45.643 -32.748 -5.425  1.00 101.88 ? 217 ILE   B CG1  1 
ATOM   3476 C  CG2  . ILE   B 1 217 ? -44.758 -34.833 -4.697  1.00 95.74  ? 217 ILE   B CG2  1 
ATOM   3477 C  CD1  . ILE   B 1 217 ? -46.980 -32.058 -5.912  1.00 97.68  ? 217 ILE   B CD1  1 
ATOM   3478 N  N    . ASP   B 1 218 ? -46.158 -36.302 -8.053  1.00 126.57 ? 218 ASP   B N    1 
ATOM   3479 C  CA   . ASP   B 1 218 ? -46.632 -37.651 -8.323  1.00 125.38 ? 218 ASP   B CA   1 
ATOM   3480 C  C    . ASP   B 1 218 ? -46.385 -38.122 -9.773  1.00 125.67 ? 218 ASP   B C    1 
ATOM   3481 O  O    . ASP   B 1 218 ? -47.072 -39.039 -10.240 1.00 130.08 ? 218 ASP   B O    1 
ATOM   3482 C  CB   . ASP   B 1 218 ? -48.118 -37.703 -7.908  1.00 128.00 ? 218 ASP   B CB   1 
ATOM   3483 C  CG   . ASP   B 1 218 ? -49.004 -36.624 -8.628  1.00 136.46 ? 218 ASP   B CG   1 
ATOM   3484 O  OD1  . ASP   B 1 218 ? -48.489 -35.825 -9.446  1.00 131.98 ? 218 ASP   B OD1  1 
ATOM   3485 O  OD2  . ASP   B 1 218 ? -50.217 -36.524 -8.313  1.00 138.43 ? 218 ASP   B OD2  1 
ATOM   3486 N  N    . SER   B 1 219 ? -45.372 -37.574 -10.461 1.00 122.04 ? 219 SER   B N    1 
ATOM   3487 C  CA   . SER   B 1 219 ? -45.161 -37.865 -11.880 1.00 120.74 ? 219 SER   B CA   1 
ATOM   3488 C  C    . SER   B 1 219 ? -44.574 -39.254 -12.082 1.00 119.48 ? 219 SER   B C    1 
ATOM   3489 O  O    . SER   B 1 219 ? -43.604 -39.631 -11.412 1.00 112.58 ? 219 SER   B O    1 
ATOM   3490 C  CB   . SER   B 1 219 ? -44.225 -36.831 -12.508 1.00 119.24 ? 219 SER   B CB   1 
ATOM   3491 O  OG   . SER   B 1 219 ? -43.954 -37.104 -13.879 1.00 113.01 ? 219 SER   B OG   1 
ATOM   3492 N  N    . SER   B 1 220 ? -45.160 -40.008 -13.018 1.00 119.70 ? 220 SER   B N    1 
ATOM   3493 C  CA   . SER   B 1 220 ? -44.610 -41.275 -13.491 1.00 116.95 ? 220 SER   B CA   1 
ATOM   3494 C  C    . SER   B 1 220 ? -44.483 -41.206 -15.012 1.00 119.63 ? 220 SER   B C    1 
ATOM   3495 O  O    . SER   B 1 220 ? -44.987 -40.269 -15.643 1.00 121.21 ? 220 SER   B O    1 
ATOM   3496 C  CB   . SER   B 1 220 ? -45.481 -42.468 -13.078 1.00 114.59 ? 220 SER   B CB   1 
ATOM   3497 O  OG   . SER   B 1 220 ? -46.832 -42.247 -13.443 1.00 121.52 ? 220 SER   B OG   1 
ATOM   3498 N  N    . ILE   B 1 221 ? -43.832 -42.214 -15.610 1.00 119.43 ? 221 ILE   B N    1 
ATOM   3499 C  CA   . ILE   B 1 221 ? -43.406 -42.126 -17.014 1.00 116.88 ? 221 ILE   B CA   1 
ATOM   3500 C  C    . ILE   B 1 221 ? -44.681 -42.184 -17.860 1.00 118.87 ? 221 ILE   B C    1 
ATOM   3501 O  O    . ILE   B 1 221 ? -45.568 -42.998 -17.553 1.00 115.12 ? 221 ILE   B O    1 
ATOM   3502 C  CB   . ILE   B 1 221 ? -42.463 -43.269 -17.442 1.00 115.22 ? 221 ILE   B CB   1 
ATOM   3503 C  CG1  . ILE   B 1 221 ? -41.263 -43.464 -16.526 1.00 107.25 ? 221 ILE   B CG1  1 
ATOM   3504 C  CG2  . ILE   B 1 221 ? -41.778 -42.874 -18.735 1.00 107.46 ? 221 ILE   B CG2  1 
ATOM   3505 C  CD1  . ILE   B 1 221 ? -41.539 -44.476 -15.407 1.00 103.00 ? 221 ILE   B CD1  1 
ATOM   3506 N  N    . PRO   B 1 222 ? -44.838 -41.385 -18.923 1.00 121.83 ? 222 PRO   B N    1 
ATOM   3507 C  CA   . PRO   B 1 222 ? -46.038 -41.533 -19.761 1.00 128.41 ? 222 PRO   B CA   1 
ATOM   3508 C  C    . PRO   B 1 222 ? -45.996 -42.812 -20.596 1.00 136.48 ? 222 PRO   B C    1 
ATOM   3509 O  O    . PRO   B 1 222 ? -44.924 -43.287 -20.987 1.00 134.87 ? 222 PRO   B O    1 
ATOM   3510 C  CB   . PRO   B 1 222 ? -46.007 -40.286 -20.657 1.00 126.35 ? 222 PRO   B CB   1 
ATOM   3511 C  CG   . PRO   B 1 222 ? -44.982 -39.369 -20.036 1.00 119.67 ? 222 PRO   B CG   1 
ATOM   3512 C  CD   . PRO   B 1 222 ? -43.998 -40.263 -19.386 1.00 117.01 ? 222 PRO   B CD   1 
ATOM   3513 N  N    . SER   B 1 223 ? -47.185 -43.372 -20.873 1.00 140.56 ? 223 SER   B N    1 
ATOM   3514 C  CA   . SER   B 1 223 ? -47.274 -44.572 -21.708 1.00 135.17 ? 223 SER   B CA   1 
ATOM   3515 C  C    . SER   B 1 223 ? -46.907 -44.234 -23.147 1.00 127.77 ? 223 SER   B C    1 
ATOM   3516 O  O    . SER   B 1 223 ? -47.359 -43.224 -23.695 1.00 128.04 ? 223 SER   B O    1 
ATOM   3517 C  CB   . SER   B 1 223 ? -48.679 -45.189 -21.653 1.00 134.60 ? 223 SER   B CB   1 
ATOM   3518 O  OG   . SER   B 1 223 ? -48.877 -45.954 -20.472 1.00 134.24 ? 223 SER   B OG   1 
ATOM   3519 N  N    . GLY   B 1 224 ? -46.069 -45.070 -23.753 1.00 127.28 ? 224 GLY   B N    1 
ATOM   3520 C  CA   . GLY   B 1 224 ? -45.645 -44.821 -25.121 1.00 130.12 ? 224 GLY   B CA   1 
ATOM   3521 C  C    . GLY   B 1 224 ? -44.873 -43.536 -25.313 1.00 127.69 ? 224 GLY   B C    1 
ATOM   3522 O  O    . GLY   B 1 224 ? -44.953 -42.922 -26.381 1.00 122.62 ? 224 GLY   B O    1 
ATOM   3523 N  N    . SER   B 1 225 ? -44.125 -43.107 -24.303 1.00 132.52 ? 225 SER   B N    1 
ATOM   3524 C  CA   . SER   B 1 225 ? -43.289 -41.926 -24.418 1.00 123.09 ? 225 SER   B CA   1 
ATOM   3525 C  C    . SER   B 1 225 ? -41.895 -42.239 -24.953 1.00 119.71 ? 225 SER   B C    1 
ATOM   3526 O  O    . SER   B 1 225 ? -41.116 -41.309 -25.150 1.00 119.41 ? 225 SER   B O    1 
ATOM   3527 C  CB   . SER   B 1 225 ? -43.183 -41.235 -23.057 1.00 119.68 ? 225 SER   B CB   1 
ATOM   3528 O  OG   . SER   B 1 225 ? -42.940 -42.194 -22.043 1.00 119.90 ? 225 SER   B OG   1 
ATOM   3529 N  N    . THR   B 1 226 ? -41.565 -43.511 -25.194 1.00 121.38 ? 226 THR   B N    1 
ATOM   3530 C  CA   . THR   B 1 226 ? -40.254 -43.885 -25.726 1.00 119.31 ? 226 THR   B CA   1 
ATOM   3531 C  C    . THR   B 1 226 ? -39.978 -43.171 -27.042 1.00 120.80 ? 226 THR   B C    1 
ATOM   3532 O  O    . THR   B 1 226 ? -40.892 -42.874 -27.811 1.00 127.12 ? 226 THR   B O    1 
ATOM   3533 C  CB   . THR   B 1 226 ? -40.183 -45.395 -25.941 1.00 121.07 ? 226 THR   B CB   1 
ATOM   3534 O  OG1  . THR   B 1 226 ? -41.148 -45.773 -26.929 1.00 131.58 ? 226 THR   B OG1  1 
ATOM   3535 C  CG2  . THR   B 1 226 ? -40.512 -46.131 -24.666 1.00 119.54 ? 226 THR   B CG2  1 
ATOM   3536 N  N    . GLY   B 1 227 ? -38.712 -42.889 -27.314 1.00 110.12 ? 227 GLY   B N    1 
ATOM   3537 C  CA   . GLY   B 1 227 ? -38.453 -42.139 -28.531 1.00 122.70 ? 227 GLY   B CA   1 
ATOM   3538 C  C    . GLY   B 1 227 ? -38.547 -40.626 -28.386 1.00 125.41 ? 227 GLY   B C    1 
ATOM   3539 O  O    . GLY   B 1 227 ? -38.268 -40.116 -27.304 1.00 121.88 ? 227 GLY   B O    1 
ATOM   3540 N  N    . ARG   B 1 228 ? -38.947 -39.900 -29.451 1.00 131.63 ? 228 ARG   B N    1 
ATOM   3541 C  CA   . ARG   B 1 228 ? -38.832 -38.434 -29.552 1.00 125.40 ? 228 ARG   B CA   1 
ATOM   3542 C  C    . ARG   B 1 228 ? -39.499 -37.679 -28.407 1.00 122.33 ? 228 ARG   B C    1 
ATOM   3543 O  O    . ARG   B 1 228 ? -39.244 -36.478 -28.258 1.00 120.01 ? 228 ARG   B O    1 
ATOM   3544 C  CB   . ARG   B 1 228 ? -39.452 -37.960 -30.871 1.00 129.89 ? 228 ARG   B CB   1 
ATOM   3545 C  CG   . ARG   B 1 228 ? -40.962 -38.198 -30.917 1.00 133.51 ? 228 ARG   B CG   1 
ATOM   3546 C  CD   . ARG   B 1 228 ? -41.603 -37.861 -32.259 1.00 142.47 ? 228 ARG   B CD   1 
ATOM   3547 N  NE   . ARG   B 1 228 ? -43.051 -38.090 -32.229 1.00 143.76 ? 228 ARG   B NE   1 
ATOM   3548 C  CZ   . ARG   B 1 228 ? -43.866 -37.924 -33.269 1.00 140.82 ? 228 ARG   B CZ   1 
ATOM   3549 N  NH1  . ARG   B 1 228 ? -43.373 -37.595 -34.464 1.00 135.33 ? 228 ARG   B NH1  1 
ATOM   3550 N  NH2  . ARG   B 1 228 ? -45.170 -38.132 -33.118 1.00 138.27 ? 228 ARG   B NH2  1 
ATOM   3551 N  N    . LEU   B 1 229 ? -40.352 -38.344 -27.615 1.00 121.90 ? 229 LEU   B N    1 
ATOM   3552 C  CA   . LEU   B 1 229 ? -41.027 -37.737 -26.466 1.00 121.39 ? 229 LEU   B CA   1 
ATOM   3553 C  C    . LEU   B 1 229 ? -40.186 -37.735 -25.187 1.00 116.60 ? 229 LEU   B C    1 
ATOM   3554 O  O    . LEU   B 1 229 ? -40.577 -37.100 -24.199 1.00 117.61 ? 229 LEU   B O    1 
ATOM   3555 C  CB   . LEU   B 1 229 ? -42.346 -38.464 -26.204 1.00 120.73 ? 229 LEU   B CB   1 
ATOM   3556 C  CG   . LEU   B 1 229 ? -43.330 -38.422 -27.365 1.00 125.97 ? 229 LEU   B CG   1 
ATOM   3557 C  CD1  . LEU   B 1 229 ? -44.585 -39.209 -27.025 1.00 129.70 ? 229 LEU   B CD1  1 
ATOM   3558 C  CD2  . LEU   B 1 229 ? -43.669 -36.974 -27.664 1.00 124.98 ? 229 LEU   B CD2  1 
ATOM   3559 N  N    . LEU   B 1 230 ? -39.080 -38.468 -25.165 1.00 109.37 ? 230 LEU   B N    1 
ATOM   3560 C  CA   . LEU   B 1 230 ? -38.055 -38.377 -24.135 1.00 101.03 ? 230 LEU   B CA   1 
ATOM   3561 C  C    . LEU   B 1 230 ? -38.551 -38.741 -22.736 1.00 103.13 ? 230 LEU   B C    1 
ATOM   3562 O  O    . LEU   B 1 230 ? -37.922 -38.373 -21.749 1.00 105.35 ? 230 LEU   B O    1 
ATOM   3563 C  CB   . LEU   B 1 230 ? -37.424 -36.984 -24.127 1.00 99.91  ? 230 LEU   B CB   1 
ATOM   3564 C  CG   . LEU   B 1 230 ? -36.659 -36.611 -25.400 1.00 106.67 ? 230 LEU   B CG   1 
ATOM   3565 C  CD1  . LEU   B 1 230 ? -36.751 -35.134 -25.670 1.00 110.20 ? 230 LEU   B CD1  1 
ATOM   3566 C  CD2  . LEU   B 1 230 ? -35.197 -37.026 -25.349 1.00 110.55 ? 230 LEU   B CD2  1 
ATOM   3567 N  N    . GLY   B 1 231 ? -39.639 -39.489 -22.597 1.00 106.49 ? 231 GLY   B N    1 
ATOM   3568 C  CA   . GLY   B 1 231 ? -40.058 -39.863 -21.256 1.00 107.12 ? 231 GLY   B CA   1 
ATOM   3569 C  C    . GLY   B 1 231 ? -40.568 -38.707 -20.436 1.00 103.13 ? 231 GLY   B C    1 
ATOM   3570 O  O    . GLY   B 1 231 ? -40.487 -38.727 -19.204 1.00 97.80  ? 231 GLY   B O    1 
ATOM   3571 N  N    . LEU   B 1 232 ? -41.070 -37.693 -21.096 1.00 104.84 ? 232 LEU   B N    1 
ATOM   3572 C  CA   . LEU   B 1 232 ? -41.564 -36.488 -20.465 1.00 107.73 ? 232 LEU   B CA   1 
ATOM   3573 C  C    . LEU   B 1 232 ? -42.987 -36.192 -20.867 1.00 111.90 ? 232 LEU   B C    1 
ATOM   3574 O  O    . LEU   B 1 232 ? -43.793 -35.797 -20.031 1.00 116.34 ? 232 LEU   B O    1 
ATOM   3575 C  CB   . LEU   B 1 232 ? -40.682 -35.302 -20.849 1.00 104.90 ? 232 LEU   B CB   1 
ATOM   3576 C  CG   . LEU   B 1 232 ? -39.250 -35.383 -20.347 1.00 97.69  ? 232 LEU   B CG   1 
ATOM   3577 C  CD1  . LEU   B 1 232 ? -38.434 -34.249 -20.899 1.00 97.58  ? 232 LEU   B CD1  1 
ATOM   3578 C  CD2  . LEU   B 1 232 ? -39.262 -35.326 -18.859 1.00 94.79  ? 232 LEU   B CD2  1 
ATOM   3579 N  N    . PHE   B 1 233 ? -43.316 -36.410 -22.129 1.00 112.61 ? 233 PHE   B N    1 
ATOM   3580 C  CA   . PHE   B 1 233 ? -44.604 -36.050 -22.654 1.00 121.12 ? 233 PHE   B CA   1 
ATOM   3581 C  C    . PHE   B 1 233 ? -45.317 -37.269 -23.242 1.00 130.43 ? 233 PHE   B C    1 
ATOM   3582 O  O    . PHE   B 1 233 ? -44.667 -38.137 -23.841 1.00 127.05 ? 233 PHE   B O    1 
ATOM   3583 C  CB   . PHE   B 1 233 ? -44.414 -34.966 -23.721 1.00 125.53 ? 233 PHE   B CB   1 
ATOM   3584 C  CG   . PHE   B 1 233 ? -43.695 -33.740 -23.216 1.00 118.94 ? 233 PHE   B CG   1 
ATOM   3585 C  CD1  . PHE   B 1 233 ? -44.315 -32.870 -22.321 1.00 113.89 ? 233 PHE   B CD1  1 
ATOM   3586 C  CD2  . PHE   B 1 233 ? -42.392 -33.469 -23.619 1.00 116.86 ? 233 PHE   B CD2  1 
ATOM   3587 C  CE1  . PHE   B 1 233 ? -43.659 -31.735 -21.855 1.00 112.11 ? 233 PHE   B CE1  1 
ATOM   3588 C  CE2  . PHE   B 1 233 ? -41.720 -32.332 -23.151 1.00 116.32 ? 233 PHE   B CE2  1 
ATOM   3589 C  CZ   . PHE   B 1 233 ? -42.355 -31.465 -22.264 1.00 114.05 ? 233 PHE   B CZ   1 
ATOM   3590 N  N    . PRO   B 1 234 ? -46.644 -37.383 -23.057 1.00 134.92 ? 234 PRO   B N    1 
ATOM   3591 C  CA   . PRO   B 1 234 ? -47.370 -38.531 -23.634 1.00 136.16 ? 234 PRO   B CA   1 
ATOM   3592 C  C    . PRO   B 1 234 ? -47.599 -38.419 -25.134 1.00 136.55 ? 234 PRO   B C    1 
ATOM   3593 O  O    . PRO   B 1 234 ? -47.644 -39.452 -25.815 1.00 134.15 ? 234 PRO   B O    1 
ATOM   3594 C  CB   . PRO   B 1 234 ? -48.704 -38.525 -22.871 1.00 128.49 ? 234 PRO   B CB   1 
ATOM   3595 C  CG   . PRO   B 1 234 ? -48.868 -37.101 -22.448 1.00 126.85 ? 234 PRO   B CG   1 
ATOM   3596 C  CD   . PRO   B 1 234 ? -47.488 -36.623 -22.117 1.00 126.87 ? 234 PRO   B CD   1 
ATOM   3597 N  N    . ASP   B 1 235 ? -47.752 -37.205 -25.666 1.00 139.32 ? 235 ASP   B N    1 
ATOM   3598 C  CA   . ASP   B 1 235 ? -48.091 -36.993 -27.068 1.00 141.69 ? 235 ASP   B CA   1 
ATOM   3599 C  C    . ASP   B 1 235 ? -47.434 -35.721 -27.591 1.00 141.89 ? 235 ASP   B C    1 
ATOM   3600 O  O    . ASP   B 1 235 ? -47.329 -34.724 -26.870 1.00 146.58 ? 235 ASP   B O    1 
ATOM   3601 C  CB   . ASP   B 1 235 ? -49.620 -36.915 -27.267 1.00 151.24 ? 235 ASP   B CB   1 
ATOM   3602 C  CG   . ASP   B 1 235 ? -50.259 -35.712 -26.559 1.00 157.80 ? 235 ASP   B CG   1 
ATOM   3603 O  OD1  . ASP   B 1 235 ? -49.751 -35.303 -25.492 1.00 160.98 ? 235 ASP   B OD1  1 
ATOM   3604 O  OD2  . ASP   B 1 235 ? -51.291 -35.196 -27.050 1.00 162.80 ? 235 ASP   B OD2  1 
ATOM   3605 N  N    . ALA   B 1 236 ? -46.999 -35.765 -28.856 1.00 146.18 ? 236 ALA   B N    1 
ATOM   3606 C  CA   . ALA   B 1 236 ? -46.474 -34.587 -29.545 1.00 145.98 ? 236 ALA   B CA   1 
ATOM   3607 C  C    . ALA   B 1 236 ? -47.526 -33.512 -29.759 1.00 153.63 ? 236 ALA   B C    1 
ATOM   3608 O  O    . ALA   B 1 236 ? -47.170 -32.375 -30.107 1.00 146.11 ? 236 ALA   B O    1 
ATOM   3609 C  CB   . ALA   B 1 236 ? -45.896 -34.979 -30.902 1.00 141.30 ? 236 ALA   B CB   1 
ATOM   3610 N  N    . ASN   B 1 237 ? -48.799 -33.856 -29.564 1.00 161.70 ? 237 ASN   B N    1 
ATOM   3611 C  CA   . ASN   B 1 237 ? -49.935 -33.013 -29.897 1.00 158.77 ? 237 ASN   B CA   1 
ATOM   3612 C  C    . ASN   B 1 237 ? -49.994 -31.876 -28.874 1.00 152.25 ? 237 ASN   B C    1 
ATOM   3613 O  O    . ASN   B 1 237 ? -50.876 -31.873 -28.020 1.00 150.91 ? 237 ASN   B O    1 
ATOM   3614 C  CB   . ASN   B 1 237 ? -51.258 -33.827 -29.901 1.00 159.13 ? 237 ASN   B CB   1 
ATOM   3615 C  CG   . ASN   B 1 237 ? -51.265 -34.988 -30.929 1.00 157.52 ? 237 ASN   B CG   1 
ATOM   3616 O  OD1  . ASN   B 1 237 ? -51.366 -36.169 -30.565 1.00 150.65 ? 237 ASN   B OD1  1 
ATOM   3617 N  ND2  . ASN   B 1 237 ? -51.107 -34.649 -32.204 1.00 160.11 ? 237 ASN   B ND2  1 
ATOM   3618 O  OXT  . ASN   B 1 237 ? -49.158 -30.961 -28.848 1.00 147.35 ? 237 ASN   B OXT  1 
HETATM 3619 C  C1   . A1EAW C 2 .   ? -25.894 23.704  0.947   1.00 151.25 ? 301 A1EAW A C1   1 
HETATM 3620 C  C5   . A1EAW C 2 .   ? -26.475 24.025  -1.360  1.00 148.62 ? 301 A1EAW A C5   1 
HETATM 3621 C  C6   . A1EAW C 2 .   ? -27.154 24.875  2.633   1.00 146.63 ? 301 A1EAW A C6   1 
HETATM 3622 C  C3   . A1EAW C 2 .   ? -27.693 25.159  0.301   1.00 154.08 ? 301 A1EAW A C3   1 
HETATM 3623 C  C2   . A1EAW C 2 .   ? -26.914 24.579  1.296   1.00 152.00 ? 301 A1EAW A C2   1 
HETATM 3624 N  N    . A1EAW C 2 .   ? -27.462 24.874  -0.999  1.00 152.34 ? 301 A1EAW A N    1 
HETATM 3625 C  C    . A1EAW C 2 .   ? -25.674 23.425  -0.395  1.00 149.44 ? 301 A1EAW A C    1 
HETATM 3626 O  O    . A1EAW C 2 .   ? -25.106 23.772  -3.257  1.00 143.97 ? 301 A1EAW A O    1 
HETATM 3627 C  C10  . A1EAW C 2 .   ? -29.980 27.210  2.317   1.00 159.24 ? 301 A1EAW A C10  1 
HETATM 3628 C  C11  . A1EAW C 2 .   ? -30.752 27.783  1.312   1.00 160.24 ? 301 A1EAW A C11  1 
HETATM 3629 C  C12  . A1EAW C 2 .   ? -30.500 27.478  -0.021  1.00 160.17 ? 301 A1EAW A C12  1 
HETATM 3630 C  C13  . A1EAW C 2 .   ? -31.360 28.119  -1.095  1.00 159.89 ? 301 A1EAW A C13  1 
HETATM 3631 C  C15  . A1EAW C 2 .   ? -26.241 23.727  -2.812  1.00 147.59 ? 301 A1EAW A C15  1 
HETATM 3632 C  C7   . A1EAW C 2 .   ? -28.176 25.752  2.978   1.00 149.08 ? 301 A1EAW A C7   1 
HETATM 3633 C  C8   . A1EAW C 2 .   ? -28.956 26.331  1.983   1.00 155.38 ? 301 A1EAW A C8   1 
HETATM 3634 C  C9   . A1EAW C 2 .   ? -28.714 26.036  0.648   1.00 155.26 ? 301 A1EAW A C9   1 
HETATM 3635 N  N1   . A1EAW C 2 .   ? -29.489 26.613  -0.318  1.00 158.80 ? 301 A1EAW A N1   1 
HETATM 3636 O  O7   . A1EAW C 2 .   ? -32.305 27.498  -1.554  1.00 153.09 ? 301 A1EAW A O7   1 
HETATM 3637 C  C33  . A1EAW C 2 .   ? -29.158 21.638  -5.704  1.00 141.18 ? 301 A1EAW A C33  1 
HETATM 3638 C  C20  . A1EAW C 2 .   ? -30.269 22.570  -5.236  1.00 141.12 ? 301 A1EAW A C20  1 
HETATM 3639 C  C18  . A1EAW C 2 .   ? -28.673 24.302  -5.415  1.00 153.49 ? 301 A1EAW A C18  1 
HETATM 3640 C  C17  . A1EAW C 2 .   ? -27.315 23.759  -4.988  1.00 153.96 ? 301 A1EAW A C17  1 
HETATM 3641 N  N2   . A1EAW C 2 .   ? -27.284 23.419  -3.579  1.00 151.38 ? 301 A1EAW A N2   1 
HETATM 3642 O  O1   . A1EAW C 2 .   ? -29.696 23.717  -4.612  1.00 146.58 ? 301 A1EAW A O1   1 
HETATM 3643 O  O1M2 . A1EAW C 2 .   ? -29.380 20.331  -5.178  1.00 136.93 ? 301 A1EAW A O1M2 1 
HETATM 3644 C  C1M2 . A1EAW C 2 .   ? -28.241 19.845  -4.470  1.00 137.69 ? 301 A1EAW A C1M2 1 
HETATM 3645 C  C2M2 . A1EAW C 2 .   ? -27.511 18.820  -5.326  1.00 128.54 ? 301 A1EAW A C2M2 1 
HETATM 3646 C  C3M2 . A1EAW C 2 .   ? -28.420 17.634  -5.618  1.00 124.51 ? 301 A1EAW A C3M2 1 
HETATM 3647 C  C4M2 . A1EAW C 2 .   ? -29.081 17.120  -4.345  1.00 126.30 ? 301 A1EAW A C4M2 1 
HETATM 3648 C  C5M2 . A1EAW C 2 .   ? -29.666 18.250  -3.505  1.00 131.69 ? 301 A1EAW A C5M2 1 
HETATM 3649 C  C6M2 . A1EAW C 2 .   ? -30.200 17.722  -2.179  1.00 144.12 ? 301 A1EAW A C6M2 1 
HETATM 3650 O  O2M2 . A1EAW C 2 .   ? -26.338 18.369  -4.641  1.00 123.60 ? 301 A1EAW A O2M2 1 
HETATM 3651 O  O3M2 . A1EAW C 2 .   ? -27.653 16.582  -6.215  1.00 137.23 ? 301 A1EAW A O3M2 1 
HETATM 3652 O  O4M2 . A1EAW C 2 .   ? -30.137 16.229  -4.706  1.00 124.95 ? 301 A1EAW A O4M2 1 
HETATM 3653 O  O5M2 . A1EAW C 2 .   ? -28.663 19.229  -3.257  1.00 141.00 ? 301 A1EAW A O5M2 1 
HETATM 3654 O  O6M2 . A1EAW C 2 .   ? -31.078 16.618  -2.426  1.00 145.61 ? 301 A1EAW A O6M2 1 
HETATM 3655 C  C21  . A1EAW C 2 .   ? -31.335 26.078  -4.301  1.00 166.28 ? 301 A1EAW A C21  1 
HETATM 3656 C  C22  . A1EAW C 2 .   ? -30.029 26.849  -4.454  1.00 163.46 ? 301 A1EAW A C22  1 
HETATM 3657 C  C19  . A1EAW C 2 .   ? -30.073 29.105  -3.755  1.00 166.07 ? 301 A1EAW A C19  1 
HETATM 3658 C  C16  . A1EAW C 2 .   ? -31.172 29.728  -2.902  1.00 162.04 ? 301 A1EAW A C16  1 
HETATM 3659 N  N3   . A1EAW C 2 .   ? -31.059 29.347  -1.508  1.00 162.11 ? 301 A1EAW A N3   1 
HETATM 3660 O  O8   . A1EAW C 2 .   ? -29.877 27.749  -3.358  1.00 177.16 ? 301 A1EAW A O8   1 
HETATM 3661 O  O1M  . A1EAW C 2 .   ? -32.413 26.865  -4.805  1.00 167.55 ? 301 A1EAW A O1M  1 
HETATM 3662 C  C1M  . A1EAW C 2 .   ? -32.867 26.392  -6.071  1.00 158.15 ? 301 A1EAW A C1M  1 
HETATM 3663 C  C2M  . A1EAW C 2 .   ? -31.810 26.681  -7.130  1.00 156.23 ? 301 A1EAW A C2M  1 
HETATM 3664 C  C3M  . A1EAW C 2 .   ? -31.612 28.181  -7.311  1.00 151.97 ? 301 A1EAW A C3M  1 
HETATM 3665 C  C4M  . A1EAW C 2 .   ? -32.950 28.886  -7.495  1.00 148.73 ? 301 A1EAW A C4M  1 
HETATM 3666 C  C5M  . A1EAW C 2 .   ? -33.935 28.473  -6.408  1.00 145.95 ? 301 A1EAW A C5M  1 
HETATM 3667 C  C6M  . A1EAW C 2 .   ? -35.294 29.127  -6.625  1.00 150.17 ? 301 A1EAW A C6M  1 
HETATM 3668 O  O2M  . A1EAW C 2 .   ? -32.209 26.099  -8.376  1.00 150.29 ? 301 A1EAW A O2M  1 
HETATM 3669 O  O3M  . A1EAW C 2 .   ? -30.782 28.421  -8.453  1.00 169.43 ? 301 A1EAW A O3M  1 
HETATM 3670 O  O4M  . A1EAW C 2 .   ? -32.754 30.304  -7.450  1.00 149.54 ? 301 A1EAW A O4M  1 
HETATM 3671 O  O5M  . A1EAW C 2 .   ? -34.082 27.054  -6.417  1.00 157.61 ? 301 A1EAW A O5M  1 
HETATM 3672 O  O6M  . A1EAW C 2 .   ? -35.729 28.888  -7.968  1.00 156.86 ? 301 A1EAW A O6M  1 
HETATM 3673 CA CA   . CA    D 3 .   ? -31.089 11.435  -7.746  1.00 95.70  ? 302 CA    A CA   1 
HETATM 3674 MN MN   . MN    E 4 .   ? -31.515 8.056   -10.924 1.00 94.46  ? 303 MN    A MN   1 
HETATM 3675 CA CA   . CA    F 3 .   ? -35.950 -35.407 -30.610 1.00 117.85 ? 301 CA    B CA   1 
HETATM 3676 MN MN   . MN    G 4 .   ? -37.977 -31.946 -29.325 1.00 123.43 ? 302 MN    B MN   1 
# 
